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Protein Ontology report - glycoprotein
PR:000037069 - http://purl.obolibrary.org/obo/PR_000037069
 
  Protein Forms  Complex  Annotations      
Ontology Information Show OBO stanza
  PRO ID
PR:000037069   
  PRO nameglycoprotein 
  Synonyms
PRO-Short-label: EXACT:Prot/GlycoRes+
Other: EXACT:glycated protein | glycosylated protein
  Definition"A protein that includes at least one glycosylated residue." [PRO:DAN] 
  PRO Categorymodification 
  ParentPR:000000001 protein
  Terms by PRO Category
Organism-Independent Organism-Specific
         Category          Number of Terms          Category          Number of Terms
         Modification68                                                  Organism-Modification 40                                        
  Term Hierarchy
  Visualization
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Protein Forms Switch to Compact View   

Category  

PRO ID

Name

Short Name

Definition

Ann. Has Annotation?

comp. In Complex?
modification



PR:000037069

glycoprotein

Prot/GlycoRes+


"A protein that includes at least one glycosylated residue." [PRO:DAN]


modification



PR:000000279

follistatin isoform 1, signal peptide removed glycosylated form

FST/iso:1/SigPep-/GlycoRes+


"A follistatin isoform 1, signal peptide removed form that includes at least one glycosylated residue." [PRO:CNA, PRO:DAN]


modification



PR:000000434

follistatin isoform 1 cleaved and N-glycosylated 2

FST/iso:1/ClvNGlyco:2


"A follistatin isoform 1, signal peptide removed glycosylated form that has had the C-terminal residues up to, but not including, the acidic region removed, and has been N-glycosylated at residues equivalent to Asn-124 and Asn-288 of the amino acid sequence represented by UniProtKB:P10669-1. Example: UniProtKB:P10669-1, 30-332, Asn-124/Asn-288, MOD:00160." [PMID:8340384, PRO:CNA, PRO:DAN]


organism-modification



PR:000036413

follistatin isoform 1 cleaved and N-glycosylated 2 (pig)

pig-FST/iso:1/ClvNGlyco:2


"A follistatin isoform 1 cleaved and N-glycosylated 2 in pig. UniProtKB:P10669-1, 30-332, Asn-124/Asn-288, MOD:00160." [PMID:8340384, PRO:CNA]

Yes

organism-modification



PR:000036414

follistatin isoform 1 cleaved and N-glycosylated 2 (human)

hFST/iso:1/ClvNGlyco:2


"A follistatin isoform 1 cleaved and N-glycosylated 2 in human. UniProtKB:P19883-1, 30-332, Asn-124/Asn-288, MOD:00160." [PMID:16150905, PRO:CNA, PRO:DAN]

Yes

organism-modification



PR:000036412

follistatin isoform 1, signal peptide removed glycosylated form (human)

hFST/iso:1/SigPep-/GlycoRes+


"A follistatin isoform 1, signal peptide removed glycosylated form in human. UniProtKB:P19883-1, 30-344, MOD:00693." [PMID:16150905, PRO:CNA]

Yes

organism-modification



PR:000036414

follistatin isoform 1 cleaved and N-glycosylated 2 (human)

hFST/iso:1/ClvNGlyco:2


"A follistatin isoform 1 cleaved and N-glycosylated 2 in human. UniProtKB:P19883-1, 30-332, Asn-124/Asn-288, MOD:00160." [PMID:16150905, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000280

follistatin isoform 2, signal peptide removed glycosylated form

FST/iso:2/SigPep-/GlycoRes+


"A follistatin isoform 2, signal peptide removed form that includes at least one glycosylated residue." [PRO:CNA, PRO:DAN]


organism-modification



PR:000036415

follistatin isoform 2, signal peptide removed N-glycosylated 1 (human)

hFST/iso:2/SigPep-/NGlyco:1


"A follistatin isoform 2, signal peptide removed glycosylated form that is in human and has been N-glycosylated at residues equivalent to Asn-124 and Asn-288 of the amino acid sequence represented by UniProtKB:P19883-2. UniProtKB:P19883-2, 30-317, Asn-124/Asn-288, MOD:00160." [PMID:15454184, PMID:16150905, PMID:1906804, PRO:CNA, PRO:DAN]

Yes

organism-modification



PR:000036416

follistatin isoform 2, signal peptide removed N-glycosylated 1 (pig)

pig-FST/iso:2/SigPep-/NGlyco:1


"A follistatin isoform 2, signal peptide removed glycosylated form that is in pig and has been N-glycosylated at residues equivalent to Asn-124 and Asn-288 of the amino acid sequence represented by UniProtKB:P10669-2. UniProtKB:P10669-2, 30-317, Asn-124/Asn-288, MOD:00160." [PMID:8340384, PRO:CNA, PRO:DAN]


modification



PR:000000414

activin receptor type-2A isoform 1 glycosylated and phosphorylated form

ACVR2A/iso:1/GlycoPhos+


"An activin receptor type-2A isoform 1 that includes at least one glycosylated residue and at least one phosphorylated residue." [PRO:CNA]


modification



PR:000000528

activin receptor type-2A isoform 1 glycosylated and phosphorylated 1

ACVR2A/iso:1/GlycoPhos:1


"An activin receptor type-2A isoform 1 glycosylated and phosphorylated form in which the phosphorylation occurs at Ser/Thr residues. This constitutes the active receptor subunit." [PMID:8395525]


organism-modification



PR:000036440

activin receptor type-2A isoform 1 glycosylated and phosphorylated 1 (mouse)

mACVR2A/iso:1/GlycoPhos:1


"An activin receptor type-2A isoform 1 glycosylated and phosphorylated 1 in mouse." [PMID:10452853, PMID:11459935, PMID:12414726, PMID:16991118, PMID:7885474, PMID:8395525, PMID:8612709, PRO:CNA]

Yes

organism-modification



PR:000036441

activin receptor type-2A isoform 1 glycosylated and phosphorylated 1 (human)

hACVR2A/iso:1/GlycoPhos:1


"An activin receptor type-2A isoform 1 glycosylated and phosphorylated 1 in human." [PMID:12665502, PMID:1314589, PMID:8622651, PRO:CNA]

Yes

modification



PR:000000415

activin receptor type-2B isoform ActR-IIB2 glycosylated and phosphorylated form

ACVR2B/iso:ActR-IIB2/GlycoPhos+


"An activin receptor type-2B isoform ActR-IIB2 that includes at least one glycosylated residue and at least one phosphorylated residue." [PRO:CNA]


modification



PR:000000529

activin receptor type-2B isoform ActR-IIB2 N-glycosylated and phosphorylated 1

ACVR2B/iso:ActR-IIB2/NGlycoPhos:1


"An activin receptor type-2B isoform ActR-IIB2 glycosylated and phosphorylated form in which the phosphorylation occurs at Ser/Thr residues within the GS-motif, and constitutes an active activin receptor subunit." [PRO:CNA]


organism-modification



PR:000036442

activin receptor type-2B isoform ActR-IIB2 N-glycosylated and phosphorylated 1 (mouse)

mACVR2B/iso:ActR-IIB2/NGlycoPhos:1


"An activin receptor type-2B isoform ActR-IIB2 N-glycosylated and phosphorylated 1 in mouse." [PMID:10452853, PMID:11459935, PMID:12414726, PMID:1326537, PMID:16991118, PMID:8721982, PRO:CNA]

Yes

organism-modification



PR:000036443

activin receptor type-2B isoform ActR-IIB2 N-glycosylated and phosphorylated 1 (human)

hACVR2B/iso:ActR-IIB2/NGlycoPhos:1


"An activin receptor type-2B isoform ActR-IIB2 N-glycosylated and phosphorylated 1 in human." [PMID:11279102, PMID:24337809, PMID:8161782, PMID:8622651, PMID:9872992, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000419

Muellerian-inhibiting factor isoform 1 cleaved and glycosylated form

AMH/iso:1/ClvGlyco+


"A Muellerian-inhibiting factor isoform 1 cleaved 1 that includes at least one glycosylated residue." [PRO:CNA, PRO:DAN]


modification



PR:000000534

Muellerian-inhibiting factor isoform 1 cleaved and glycosylated 2

AMH/iso:1/ClvGlyco:2


"A Muellerian-inhibiting factor isoform 1 cleaved and glycosylated form that has been cleaved at the RxxR dibasic cleavage site rendering the propeptide and the mature protein non-covalently bound." [PMID:14673134]


organism-modification



PR:000036444

Muellerian-inhibiting factor isoform 1 cleaved and N-glycosylated 2 (human)

hAMH/iso:1/ClvNGlyco:2


"A Muellerian-inhibiting factor isoform 1 cleaved and glycosylated 2 in human, in which the cleaved parts remain joined by disulfide bonds. The position(s) of glycosylation sites have not been experimentally determined. UniProtKB:P03971-1, 26-450, 451-560, MOD:00160." [PMID:12834017, PMID:14673134, PMID:14750901, PMID:3754790, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000421

c-myc protein isoform 1 glycosylated form

MYC/iso:1/GlycoRes+


"A c-myc protein isoform 1 that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000000536

c-myc protein isoform 1 O-glycosylated 1

MYC/iso:1/OGlyco:1


"A c-myc protein isoform 1 glycosylated form that has been O-glycosylated at the Thr residue within the L[LY]PTLTPPLS sequence of the Myc box I within the amino-terminal regulatory domain. Example: UniProtKB:P01106-1, Thr-58, MOD:00806." [PMID:11904304, PMID:7642555]


organism-modification



PR:000026051

c-myc protein isoform 1 O-glycosylated 1 (human)

hMYC/iso:1/OGlyco:1


"A c-myc protein isoform 1 O-glycosylated 1 in human. UniProtKB:P01106-1, Thr-58, MOD:00806." [PMID:11904304, PMID:7642555]

Yes

modification



PR:000000429

decorin isoform A cleaved and glycosylated form

DCN/iso:A/ClvGlyco+


"A decorin isoform A, signal peptide removed form that has had the propeptide removed and that includes at least one glycosylated residue." [PRO:CNA, PRO:DAN]


modification



PR:000000545

decorin isoform A cleaved and glycosylated 1

DCN/iso:A/ClvGlyco:1


"A decorin isoform A cleaved and glycosylated form that has been modified with O-linked glycosaminoglycan at the most N-terminal SG site and additional N-linked glycosylated Asn residues. Example: UniProtKB:P07585-1, 31-359, Ser-34, MOD:00814|Asn-211/Asn-262/Asn-303, MOD:00160." [PMID:16258169, PRO:CNA, PRO:DAN]


organism-modification



PR:000036457

decorin isoform A cleaved and glycosylated 1 (human)

hDCN/iso:A/ClvGlyco:1


"A decorin isoform A cleaved and glycosylated 1 in human. UniProtKB:P07585-1, 31-359, Ser-34, MOD:00814|Asn-211/Asn-262/Asn-303, MOD:00160." [PMID:16258169, PMID:17651433, PMID:9988678, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000432

tumor necrosis factor ligand superfamily member 6 isoform FasL glycosylated form

FASLG/iso:FasL/GlycoRes+


"A tumor necrosis factor ligand superfamily member 6 isoform FasL that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000000546

tumor necrosis factor ligand superfamily member 6 isoform FasL N-glycosylated 1

FASLG/iso:FasL/NGlyco:1


"A tumor necrosis factor ligand superfamily member 6 isoform FasL glycosylated form that has been N-glycosylated at the Asn residues within the N-glycosylation sites located in the C-terminal extracellular region. Example: UniProtKB:P48023-1, Asn-184/Asn-250/Asn-260, MOD:00160." [PMID:9405425]


organism-modification



PR:000036458

tumor necrosis factor ligand superfamily member 6 isoform FasL N-glycosylated 1 (human)

hFASLG/iso:FasL/NGlyco:1


"A tumor necrosis factor ligand superfamily member 6 isoform FasL N-glycosylated 1 in human. UniProtKB:P48023-1, Asn-184/Asn-250/Asn-260, MOD:00160." [PMID:9405425, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000446

interferon gamma isoform 1, signal peptide removed glycosylated form

IFNG/iso:1/SigPep-/GlycoRes+


"An interferon gamma isoform 1, signal peptide removed form that includes at least one glycosylated residue." [PMID:3109913, PRO:CNA]


modification



PR:000000447

interferon gamma isoform 1 cleaved and N-glycosylated 2

IFNG/iso:1/ClvNGlyco:2


"An interferon gamma isoform 1, signal peptide removed glycosylated form that is a mature protein with N-linked glycosylation and partial proteolytic degradation of the C-terminus. Example: UniProtKB:P01579-1, 24-161, Asn-48/Asn-120, MOD:00160." [PRO:CNA, PRO:DAN]


organism-modification



PR:000036420

interferon gamma isoform 1 cleaved and N-glycosylated 2 (human)

hIFNG/iso:1/ClvNGlyco:2


"An interferon gamma isoform 1 cleaved and N-glycosylated 2 in human. UniProtKB:P01579-1, 24-161, Asn-48/Asn-120, MOD:00160." [PMID:1902591, PMID:6427223, PRO:CNA]

Yes

organism-modification



PR:000036407

interferon gamma isoform 1, signal peptide removed glycosylated form (mouse)

mIFNG/iso:1/SigPep-/GlycoRes+


"An interferon gamma isoform 1, signal peptide removed glycosylated form in mouse. UniProtKB:P01580-1, 23-155, MOD:00693." [PMID:11027433, PMID:11057672, PMID:11728336, PMID:12882831, PMID:12925700, PMID:15240714, PMID:15240719, PRO:CNA]

Yes

organism-modification



PR:000036419

interferon gamma isoform 1, signal peptide removed N-glycosylated 1 (human)

hIFNG/iso:1/SigPep-/NGlyco:1


"An interferon gamma isoform 1, signal peptide removed glycosylated form in human in which N-linked glycosylation occurs at Asn-48 and Asn-120. UniProtKB:P01579-1, 24-157, Asn-48/Asn-120, MOD:00160." [PMID:10986460, PMID:3109913, PMID:6427223, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000485

thrombospondin-1 isoform 1 cleaved and glycosylated form

THBS1/iso:1/ClvGlyco+


"A thrombospondin-1 isoform 1, signal peptide removed form that has been processed by proteolytic cleavage and includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000000590

thrombospondin-1 isoform 1 cleaved 2 glycosylated form

THBS1/iso:1/Clv:2/GlycoRes+


"A thrombospondin-1 isoform 1 cleaved and glycosylated form that has been proteolytically processed by ADAMTS1 to render a C-terminal domain product." [PMID:17082774]


organism-modification



PR:000036489

thrombospondin-1 isoform 1 cleaved 2 glycosylated 1 (human)

hTHBS1/iso:1/Clv:2/Glyco:1


"A thrombospondin-1 isoform 1 cleaved 2 glycosylated form in human and that has been post-translationally modified at four Trp residues, one Ser residue, and two Thr residues. UniProtKB:P07996-1, 312-1170, Trp-385/Trp-438/Trp-441/Trp-498, MOD:00222|Ser-394, MOD:00812|Thr-450/Thr-507, MOD:00813." [PMID:11067851, PRO:CNA]


organism-modification



PR:000036490

thrombospondin-1 isoform 1 cleaved 2 glycosylated form (mouse)

mTHBS1/iso:1/Clv:2/GlycoRes+


"A thrombospondin-1 isoform 1 cleaved 2 glycosylated form in mouse. UniProtKB:P35441-1, 312-1170, MOD:00693." [PMID:17082774, PRO:CNA]

Yes

modification



PR:000000492

transcription factor Sp1 isoform 1 glycosylated form

SP1/iso:1/GlycoRes+


"A transcription factor Sp1 isoform 1 that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000000598

transcription factor Sp1 isoform 1 O-glycosylated 1

SP1/iso:1/OGlyco:1


"A transcription factor Sp1 isoform 1 glycosylated form that has terminal O-linked N-acetylglucosamines. Example: UniProtKB:P08047-1, Ser-491, MOD:00805." [PMID:11371615, PRO:CNA, PRO:DAN]


organism-modification



PR:000036498

transcription factor Sp1 isoform 1 O-glycosylated 1 (human)

hSP1/iso:1/OGlyco:1


"A transcription factor Sp1 isoform 1 O-glycosylated 1 in human. UniProtKB:P08047-1, Ser-491, MOD:00805." [PMID:11371615, PMID:9343410, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000505

bone morphogenetic protein 7 isoform 1, mature glycosylated form

BMP7/iso:1/ClvGlyco+


"A bone morphogenetic protein 7 isoform 1, mature form that includes at least one glycosylated residue." [PRO:CNA, PRO:DAN]


modification



PR:000000613

bone morphogenetic protein 7 isoform 1, mature N-glycosylated 1

BMP7/iso:1/mature/NGlyco:1


"A bone morphogenetic protein 7 isoform 1, mature glycosylated form that is N-glycosylated at the N{P}[ST]{P} motif. This form is a disulfide linked homodimer. Example: UniProtKB:P18075-1, 293-431, Asn-372, MOD:00160." [PMID:15929982, PRO:CNA, PRO:DAN]


organism-modification



PR:000036517

bone morphogenetic protein 7 isoform 1, mature N-glycosylated 1 (human)

hBMP7/iso:1/mature/NGlyco:1


"A bone morphogenetic protein 7 isoform 1, mature N-glycosylated 1 in human. UniProtKB:P18075-1, 293-431, Asn-372, MOD:00160." [PMID:15047707, PMID:15929982, PMID:8570652, PMID:9872992, PRO:CNA, PRO:DAN]

Yes

organism-modification



PR:000036518

bone morphogenetic protein 7 isoform 1, mature N-glycosylated 1 (mouse)

mBMP7/iso:1/mature/NGlyco:1


"A bone morphogenetic protein 7 isoform 1, mature N-glycosylated 1 in mouse. UniProtKB:P23359-1, 292-430, Asn-371, MOD:00160." [PMID:14623234, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000614

bone morphogenetic protein 7 isoform 1, mature N-glycosylated 2

BMP7/iso:1/mature/NGlyco:2


"A bone morphogenetic protein 7 isoform 1, mature glycosylated form that has the propeptide still bound to the mature protein. This form is N-glycosylated at the most C-terminal N{P}[ST]{P} motif and is a homodimer. Example: UniProtKB:P18075-1, 20-292, 293-431, Asn-372, MOD:00160." [PMID:15929982]


organism-modification



PR:000036519

bone morphogenetic protein 7 isoform 1, mature N-glycosylated 2 (human)

hBMP7/iso:1/mature/NGlyco:2


"A bone morphogenetic protein 7 isoform 1, mature N-glycosylated 2 in human, in which the cleaved parts remain joined by disulfide bonds. UniProtKB:P18075-1, 20-292, 293-431, Asn-372, MOD:00160." [PMID:15929982, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000935

potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 isoform 1 glycosylated form

HCN1/iso:1/GlycoRes+


"A potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 isoform 1 that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000000984

potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 isoform 1 N-glycosylated 1

HCN1/iso:1/NGlyco:1


"A potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 isoform 1 glycosylated form with N-glycosylation at the N-linked glycosylation consensus sequence (Nx[ST]) in the extracellular domain between S5 and S6 transmembrane segments. Example: UniProtKB:O88704-1, Asn-327, MOD:00160." [PMID:17988239]


organism-modification



PR:000036573

potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 isoform 1 N-glycosylated 1 (mouse)

mHCN1/iso:1/NGlyco:1


"A potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 isoform 1 N-glycosylated 1 in mouse. UniProtKB:O88704-1, Asn-327, MOD:00160." [PMID:12928435, PRO:CNA, PRO:DAN]

Yes

modification



PR:000000936

potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 isoform 1 glycosylated form

HCN2/iso:1/GlycoRes+


"A potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 isoform 1 that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000000985

potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 isoform 1 N-glycosylated 1

HCN2/iso:1/NGlyco:1


"A potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 isoform 1 glycosylated form with N-glycosylation at the N-linked glycosylation consensus sequence (Nx[ST]) in the extracellular domain between S5 and S6 transmembrane segments. Example: UniProtKB:O88703-1, Asn-380, MOD:00160." [PMID:12928435]


organism-modification



PR:000036574

potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 isoform 1 N-glycosylated 1 (mouse)

mHCN2/iso:1/NGlyco:1


"A potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 isoform 1 N-glycosylated 1 in mouse. UniProtKB:O88703-1, Asn-380, MOD:00160." [PMID:12928435, PRO:CNA]

Yes

modification



PR:000000989

voltage-gated potassium channel KCNH2 isoform A glycosylated form

KCNH2/iso:A/GlycoRes+


"A voltage-gated potassium channel KCNH2 isoform A that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000000998

voltage-gated potassium channel KCNH2 isoform A N-glycosylated 1

KCNH2/iso:A/NGlyco:1


"A voltage-gated potassium channel KCNH2 isoform A glycosylated form that has been glycosylated at the Asn residue within the Nx[T/S] motif located approximately 26 amino acids downstream of the S5 transmembrane domain. Example: UniProtKB:Q12809-1, Asn-598, MOD:00160." [PMID:12063277]


organism-modification



PR:000036581

voltage-gated potassium channel KCNH2 isoform A N-glycosylated 1 (human)

hKCNH2/iso:A/NGlyco:1


"A voltage-gated potassium channel KCNH2 isoform A N-glycosylated 1 in human. UniProtKB:Q12809-1, Asn-598, MOD:00160." [PMID:12063277, PRO:CNA]

Yes

organism-modification



PR:000036582

voltage-gated potassium channel KCNH2 isoform A N-glycosylated 1 (mouse)

mKCNH2/iso:A/NGlyco:1


"A voltage-gated potassium channel KCNH2 isoform A N-glycosylated 1 in mouse. UniProtKB:O35219-1, Asn-600, MOD:00160." [PMID:14668215, PRO:CNA]

Yes

modification



PR:000001048

cftr isoform 1 glycosylated form

CFTR/iso:1/GlycoRes+


"A cftr isoform 1 that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000001049

cftr isoform 1 N-glycosylated 1

CFTR/iso:1/NGlyco:1


"A cftr isoform 1 glycosylated form in which the glycosylation is at two Asn residues within the N{P}[ST]{P} motif, located in the fourth extracellular loop. Example: UniProtKB:P13569-1, Asn-894/Asn-900, MOD:00160." [PMID:7518437]


organism-modification



PR:000036593

cftr isoform 1 N-glycosylated 1 (human)

hCFTR/iso:1/NGlyco:1


"A cftr isoform 1 N-glycosylated 1 in human. UniProtKB:P13569-1, Asn-894/Asn-900, MOD:00160." [PMID:7518437, PRO:CNA]


modification



PR:000001723

transient receptor potential cation channel TRPM8 isoform 1 glycosylated form

TRPM8/iso:1/GlycoRes+


"A transient receptor potential cation channel TRPM8 isoform 1 that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000001724

transient receptor potential cation channel TRPM8 isoform 1 N-glycosylated 1

TRPM8/iso:1/NGlyco:1


"A transient receptor potential cation channel TRPM8 isoform 1 glycosylated form that has been N-glycosylated on the Asn consensus N-glycosylation site within the pore loop region. Example: UniProtKB:Q8R4D5-1, Asn-934, MOD:00160." [PMID:17015441]


organism-modification



PR:000036607

transient receptor potential cation channel TRPM8 isoform 1 N-glycosylated 1 (mouse)

mTRPM8/iso:1/NGlyco:1


"A transient receptor potential cation channel TRPM8 isoform 1 N-glycosylated 1 in mouse. UniProtKB:Q8R4D5-1, Asn-934, MOD:00160." [PMID:17015441, PRO:HJD]


modification



PR:000001737

inhibin alpha chain isoform 1 glycosylated form

INHA/iso:1/GlycoRes+


"An inhibin alpha chain isoform 1 that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000001732

inhibin alpha chain isoform 1 cleaved and glycosylated form

INHA/iso:1/ClvGlyco+


"An inhibin alpha chain isoform 1, signal peptide removed form that has been processed by proteolytic cleavage and includes at least one glycosylated residue." [PRO:CNA, PRO:DAN]


modification



PR:000001733

inhibin alpha chain isoform 1 cleaved and N-glycosylated 2

INHA/iso:1/ClvNGlyco:2


"An inhibin alpha chain isoform 1 cleaved and glycosylated form that has had release of the propeptide and has been glycosylated at Asn residues within the two consensus glycosylation sites. Glycosylation favors formation of the inhibin A complex. Example: UniProtKB:P05111-1, 233-366, Asn-268/Asn-302, MOD:00160." [PMID:17456790, PMID:8885240]


organism-modification



PR:000036608

inhibin alpha chain isoform 1 cleaved and N-glycosylated 2 (human)

hINHA/iso:1/ClvNGlyco:2


"An inhibin alpha chain isoform 1 cleaved and N-glycosylated 2 in human. UniProtKB:P05111-1, 233-366, Asn-268/Asn-302, MOD:00160." [PMID:17456790, PMID:8885240, PRO:CNA]

Yes

modification



PR:000001736

inhibin alpha chain isoform 1 cleaved and N-glycosylated 1

INHA/iso:1/ClvNGlyco:1


"An inhibin alpha chain isoform 1 cleaved and glycosylated form that has had release of the propeptide and has been N-glycosylated at an Asn residue within the first (or unique) consensus glycosylation site. Glycosylation favors formation of the inhibin A complex." [PMID:17456790]


modification



PR:000001738

inhibin alpha chain isoform 1 N-glycosylated 1

INHA/iso:1/NGlyco:1


"An inhibin alpha chain isoform 1 glycosylated form that is N-glycosylated at the Asn residue within the conserved N-glycosylation consensus site within the alphan N-terminal region, and in the first (or unique) consensus N-glycosylation site in the alpha C-terminal region. This is a glycosylated precursor for the mature inhibin alpha. Example: UniProtKB:P05111-1, Asn-146/Asn-268, MOD:00160." [PMID:17456790]


organism-modification



PR:000036610

inhibin alpha chain isoform 1 N-glycosylated 1 (human)

hINHA/iso:1/NGlyco:1


"An inhibin alpha chain isoform 1 N-glycosylated 1 in human. UniProtKB:P05111-1, Asn-146/Asn-268, MOD:00160." [PMID:17456790, PRO:CNA]


modification



PR:000001739

inhibin alpha chain isoform 1 N-glycosylated 2

INHA/iso:1/NGlyco:2


"An inhibin alpha chain isoform 1 glycosylated form that is N-glycosylated at the Asn residue located in the conserved N-glycosylation consensus site within the alphan N-terminal region, and at the Asn residues within the two consensus N-glycosylation sites within the alpha C-terminal region. This is a glycosylated precursor for the mature inhibin alpha. Example: UniProtKB:P05111-1, Asn-146/Asn-268/Asn-302, MOD:00160." [PMID:17456790]


organism-modification



PR:000036611

inhibin alpha chain isoform 1 N-glycosylated 2 (human)

hINHA/iso:1/NGlyco:2


"An inhibin alpha chain isoform 1 N-glycosylated 2 in human. UniProtKB:P05111-1, Asn-146/Asn-268/Asn-302, MOD:00160." [PMID:17456790, PRO:CNA]


modification



PR:000001792

prominin-1 isoform 6 glycosylated form

PROM1/iso:6/GlycoRes+


"A prominin-1 isoform 6 that includes at least one glycosylated residue." [PRO:HJD]


modification



PR:000001793

prominin-1 isoform 3 glycosylated form

PROM1/iso:3/GlycoRes+


"A prominin-1 isoform 3 that includes at least one glycosylated residue." [PRO:HJD]


modification



PR:000003018

prostate-specific antigen isoform 1 cleaved and glycosylated form

KLK3/iso:1/ClvGlyco+


"A prostate-specific antigen isoform 1, signal peptide removed form that has had the propeptide removed and that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000003019

prostate-specific antigen isoform 1 cleaved and N-glycosylated 1

KLK3/iso:1/ClvNGlyco:1


"A prostate-specific antigen isoform 1 cleaved and glycosylated form that contains an N-glycosylated Asn residue within the glycosylation consensus sequence near its N terminus. Example: UniProtKB:P07288-1, 25-261, Asn-69, MOD:00160." [PMID:2422647, PMID:3691515, PRO:CNA, PRO:DAN]


modification



PR:000003081

neuropilin-1 isoform 1, signal peptide removed glycosylated form

NRP1/iso:1/SigPep-/GlycoRes+


"A neuropilin-1 isoform 1, signal peptide removed form that has been post-translationally modified to include a glycosylated residue." [PRO:CNA]


modification



PR:000003082

neuropilin-1 isoform 1, signal peptide removed O-glycosylated 1

NRP1/iso:1/SigPep-/OGlyco:1


"A neuropilin-1 isoform 1, signal peptide removed glycosylated form that has a heparan sulfate moiety on a Ser residue located in the region between the F5/8 type C domain (Pfam:PF00754) and the MAM domain (Pfam:PF00629). Example: UniProtKB:O14786-1, 22-923, Ser-612, MOD:00215." [PMID:16763549, PRO:JAN]


organism-modification



PR:000036631

neuropilin-1 isoform 1, signal peptide removed O-glycosylated 1 (human)

hNRP1/iso:1/ClvOGlyco:1


"A neuropilin-1 isoform 1, signal peptide removed O-glycosylated 1 in human. UniProtKB:O14786-1, 22-923, Ser-612, MOD:00215." [PMID:16763549, PRO:JAN]

Yes

modification



PR:000003083

neuropilin-1 isoform 1, signal peptide removed O-glycosylated 2

NRP1/iso:1/SigPep-/OGlyco:2


"A neuropilin-1 isoform 1, signal peptide removed glycosylated form that has a chondroitin sulfate moiety on a Ser residue located in the region between the F5/8 type C domain (Pfam:PF00754) and the MAM domain (Pfam:PF00629). Example: UniProtKB:O14786-1, 22-923, Ser-612, MOD:00213." [PMID:16763549, PRO:JAN]


organism-modification



PR:000036632

neuropilin-1 isoform 1, signal peptide removed O-glycosylated 2 (human)

hNRP1/iso:1/ClvOGlyco:2


"A neuropilin-1 isoform 1, signal peptide removed O-glycosylated 2 in human. UniProtKB:O14786-1, 22-923, Ser-612, MOD:00213." [PMID:16763549, PRO:JAN]

Yes

modification



PR:000003227

HIV envelope glycoprotein gp160 glycosylated form

env/Clv:gp160/GlycoRes+


"An HIV envelope glycoprotein gp160 that includes at least one glycosylated residue." [PRO:CNA, PRO:DAN]


modification



PR:000003229

HIV envelope glycoprotein gp120 glycosylated form

env/Clv:gp120/GlycoRes+


"An HIV envelope glycoprotein gp160 glycosylated form that is the N-terminal product of proteolytic processing by host furin or furin-like proteases." [PRO:CNA, PRO:DAN]


modification



PR:000036935

HIV envelope glycoprotein gp120 N-glycosylated 1

env/Clv:gp120/NGlyco:1


"An HIV envelope glycoprotein gp120 glycosylated form that is glycosylated on residues equivalent to Asn-200, Asn-233, Asn-244, Asn-265, Asn-298, Asn-304, Asn-334, Asn-341, Asn-388, Asn-394, and Asn-400 of the amino acid sequence represented by UniProtKB:P03378. Example: UniProtKB:P03378, 32-509, Asn-200/Asn-233/Asn-244/Asn-265/Asn-298/Asn-304/Asn-334/Asn-341/Asn-388/Asn-394/Asn-400, MOD:00160." [PRO:DAN]


organism-modification



PR:000036640

envelope glycoprotein gp120 glycosylated 1 (Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2))

env/Clv:gp120/NGlyco:1 (HV1A2)


"An HIV envelope glycoprotein gp120 N-glycosylated 1 in Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2). UniProtKB:P03378, 32-509, Asn-200/Asn-233/Asn-244/Asn-265/Asn-298/Asn-304/Asn-334/Asn-341/Asn-388/Asn-394/Asn-400, MOD:00160." [PMID:12438611, PMID:15043214, PRO:CNA]


organism-modification



PR:000044791

envelope glycoprotein gp120 N-glycosylated 1 (Human immunodeficiency virus type 1 group M subtype B (isolate JRCSF))

HIV1(JRCSF)-env/Clv:gp120/NGlyco:1


"An HIV envelope glycoprotein gp120 N-glycosylated 1 in Human immunodeficiency virus type 1 group M subtype B (isolate JRCSF). UniProtKB:P20871, 31-503, Asn-195/Asn-228/Asn-239/Asn-260/Asn-293/Asn-299/Asn-329/Asn-336/Asn-382/Asn-388/Asn-392, MOD:00160." [PMID:12438611, PRO:DAN]

Yes

modification



PR:000003230

HIV envelope glycoprotein gp41 glycosylated form

env/Clv:gp41/GlycoRes+


"An HIV envelope glycoprotein gp160 glycosylated form that is the C-terminal product of proteolytic processing by host furin or furin-like proteases. This cleaved form includes part of the extracellular domain, the transmembrane and the cytosolic domains." [PRO:CNA, PRO:DAN]


modification



PR:000003255

antithrombin-III isoform 1, signal peptide removed glycosylated form

SERPINC1/iso:1/SigPep-/GlycoRes+


"An antithrombin-III isoform 1, signal peptide removed form that includes at least one glycosylated residue." [PRO:CNA]


modification



PR:000003256

antithrombin-III isoform 1, signal peptide removed glycosylated 1

SERPINC1/iso:1/SigPep-/Glyco:1


"An antithrombin-III isoform 1, signal peptide removed glycosylated form that has been N-glycosylated in the Asn residue within the four glycosylation patterns N{P}[ST]{P}." [PMID:17330941, UniProtKB:P01008]


modification



PR:000003298

lymphocyte antigen 96 isoform 1, signal peptide removed glycosylated form

LY96/iso:1/SigPep-/GlycoRes+


"A lymphocyte antigen 96 isoform 1, signal peptide removed form that includes at least one glycosylated residue." [PRO:CNA]


Yes
modification



PR:000003299

lymphocyte antigen 96 isoform 1, signal peptide removed N-glycosylated 1

LY96/iso:1/SigPep-/NGlyco:1


"A lymphocyte antigen 96 isoform 1, signal peptide removed glycosylated form that has been N-glycosylated at positions equivalent to Asn-26 and Asn-114 of the amino acid sequence represented by UniProtKB:Q9Y6Y9-1. Example: UniProtKB:Q9Y6Y9-1, 19-160, Asn-26/Asn-114, MOD:00160." [PMID:11593030, PMID:17569869, PRO:CNA, PRO:DAN, TLR:AMM]


Yes
organism-modification



PR:000025786

lymphocyte antigen 96 isoform 1, signal peptide removed N-glycosylated 1 (human)

hLY96/iso:1/SigPep-/NGlyco:1


"A lymphocyte antigen 96 isoform 1, signal peptide removed N-glycosylated 1 in human. UniProtKB:Q9Y6Y9-1, 19-160, Asn-26/Asn-114, MOD:00160." [PMID:11593030, PMID:11706042, PMID:17569869, TLR:AMM]

Yes

Yes
organism-modification



PR:000027171

lymphocyte antigen 96 isoform 1, signal peptide removed N-glycosylated 1 (mouse)

mLY96/iso:1/SigPep-/NGlyco:1


"A lymphocyte antigen 96 isoform 1, signal peptide removed glycosylated form in mouse that has been N-glycosylated on Asn residues at positions 26, 114, and 150 of the amino acid sequence represented by UniProtKB:Q9JHF9-1. UniProtKB:Q9JHF9-1, 19-160, Asn-26/Asn-114/Asn-150, MOD:00160." [PMID:17803912, PRO:CNA]

Yes

Yes
modification



PR:000021989

leucoagglutinating phytohemagglutinin isoform 1, signal peptide removed glycosylated form

DLEC2/iso:1/SigPep-/GlycoRes+


"A leucoagglutinating phytohemagglutinin isoform 1, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


modification



PR:000021957

leucoagglutinating phytohemagglutinin isoform 1, signal peptide removed N-glycosylated 1

DLEC2/iso:1/SigPep-/NGlyco:1


"A leucoagglutinating phytohemagglutinin isoform 1, signal peptide removed glycosylated form that has been N-glycosylated on residues equivalent to UniProtKB:P05087-1 Asn-32 and Asn-80. Example: UniProtKB:P05087-1, 21-272, Asn-32/Asn-80, MOD:00160." [UniProtKB:P05087]


modification



PR:000025408

T-cell surface glycoprotein CD8 alpha chain isoform 1, signal peptide removed glycosylated form

CD8A/iso:1/SigPep-/GlycoRes+


"A T-cell surface glycoprotein CD8 alpha chain isoform 1, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


Yes
modification



PR:000025409

T-cell surface glycoprotein CD8 beta chain isoform 1, signal peptide removed glycosylated form

CD8B/iso:1/SigPep-/GlycoRes+


"A T-cell surface glycoprotein CD8 beta chain isoform 1, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


Yes
modification



PR:000025813

receptor-type tyrosine-protein phosphatase C isoform CD45RABC, signal peptide removed glycosylated form

PTPRC/iso:CD45R/SigPep-/GlycoRes+


"A receptor-type tyrosine-protein phosphatase C isoform CD45RABC, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


modification



PR:000025814

receptor-type tyrosine-protein phosphatase C isoform CD45RA, signal peptide removed glycosylated form

PTPRC/iso:CD45RA/SigPep-/GlycoRes+


"A receptor-type tyrosine-protein phosphatase C isoform CD45RA, signal peptide removed form that includes at least one glycosylated residue." [PMID:1351092, PRO:CNA]


modification



PR:000025815

receptor-type tyrosine-protein phosphatase C isoform CD45RB, signal peptide removed glycosylated form

PTPRC/iso:CD45RB/SigPep-/GlycoRes+


"A receptor-type tyrosine-protein phosphatase C isoform CD45RB, signal peptide removed form that includes at least one glycosylated residue." [PMID:1351092, PRO:CNA]


modification



PR:000025816

receptor-type tyrosine-protein phosphatase C isoform CD45RO, signal peptide removed glycosylated form

PTPRC/iso:CD45RO/SigPep-/GlycoRes+


"A receptor-type tyrosine-protein phosphatase C isoform CD45RO, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


modification



PR:000025817

receptor-type tyrosine-protein phosphatase C isoform CD45RC, signal peptide removed glycosylated form

PTPRC/iso:CD45RC/SigPep-/GlycoRes+


"A receptor-type tyrosine-protein phosphatase C isoform CD45RC, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


modification



PR:000025818

receptor-type tyrosine-protein phosphatase C isoform CD45RAB, signal peptide removed glycosylated form

PTPRC/iso:CD45RAB/SigPep-/GlycoRes+


"A receptor-type tyrosine-protein phosphatase C isoform CD45RAB, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


modification



PR:000025819

receptor-type tyrosine-protein phosphatase C isoform CD45RAC, signal peptide removed glycosylated form

PTPRC/iso:CD45RAC/SigPep-/GlycoRes+


"A receptor-type tyrosine-protein phosphatase C isoform CD45RAC, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


modification



PR:000025820

receptor-type tyrosine-protein phosphatase C isoform CD45RBC, signal peptide removed glycosylated form

PTPRC/iso:CD45RBC/SigPep-/GlycoRes+


"A receptor-type tyrosine-protein phosphatase C isoform CD45RBC, signal peptide removed form that includes at least one glycosylated residue." [PRO:DAN]


organism-modification



PR:000037264

cochlin, signal peptide removed glycosylated form (mouse)

mCOCH/SigPep-/GlycoRes+


"A cochlin, signal peptide removed form (mouse) that includes at least one glycosylated residue. UniProtKB:Q62507, 26-552, MOD:00693." [PMID:23684986, PRO:KRC]


organism-modification



PR:000037262

cochlin p18 (mouse)

mCOCH/Clv:p18


"A cochlin, signal peptide removed form (mouse) that results from cleavage downstream of the LCCL domain (Pfam:PF03815), and includes at least one glycosylated residue. UniProtKB:Q62507, 26-134, MOD:00693." [PMID:23684986, PRO:KRC]

Yes

organism-modification



PR:000044792

interleukin-1 receptor-like 1 isoform B, signal peptide removed glycosylated form (mouse)

mIL1RL1/iso:B/SigPep-/GlycoRes+


"An interleukin-1 receptor-like 1 isoform B, signal peptide removed form (mouse) that has been post-translationally modified by N-glycosylation and sialylation. UniProtKB:P14719-2, 27-337, MOD:00693." [PMID:1532358, PRO:KRC]


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Prot/GlycoRes+ forms found in complexes   

Prot/GlycoRes+ Component
Complexes
PR:000003298 LY96/iso:1/SigPep-/GlycoRes+ PR:000036078 TIRAP:PIP2:activated TLR4 complex
PR:000003299 LY96/iso:1/SigPep-/NGlyco:1 PR:000025495 lipopolysaccharide receptor complex 1
PR:000025496 lipopolysaccharide receptor complex 2
PR:000025497 lipopolysaccharide receptor complex 3
PR:000025498 lipopolysaccharide receptor complex 4
PR:000025408 CD8A/iso:1/SigPep-/GlycoRes+ PR:000025402 T cell receptor co-receptor CD8
PR:000025409 CD8B/iso:1/SigPep-/GlycoRes+ PR:000025402 T cell receptor co-receptor CD8
PR:000025786 hLY96/iso:1/SigPep-/NGlyco:1 PR:000025773 lipopolysaccharide receptor complex 3 (human)
PR:000027183 IRAK4:MYD88:TIRAP:activated TLR4 complex (human)
PR:000027192 pIRAK4:MYD88:TIRAP:activated TLR4 complex (human)
PR:000027208 ticam1:ticam2:activated TLR4 complex (human)
PR:000027218 pTIRAP:PIP2:activated TLR4 complex (human)
PR:000027495 pIRAK1:pIRAK4:MYD88:TIRAP:activated TLR4 (human)
PR:000028678 ticam2:activated TLR4 complex (human)
PR:000028680 traf6:ticam1:ticam2:activated TLR4 complex (human)
PR:000035715 pUbtraf6:ticam1:ticam2:activated TLR4 complex (human)
PR:000035734 free K63-linked pUb:TAK1complex:pUbtraf6:ticam1:ticam2:activated TLR4 complex (human)
PR:000035738 free K63-linked pUb:activated TAK1 complex:pUbtraf6:ticam1:ticam2:activated TLR4 complex (human)
PR:000036004 LY96:TLR4 complex (human)
PR:000036022 traf3:ticam1:ticam2:activated TLR4 complex (human)
PR:000036024 rip1:ticam1:ticam2:activated TLR4 complex (human)
PR:000036027 sarm:ticam1:ticam2:activated TLR4 complex (human)
PR:000036030 IRF3:p-tbk1:K63-poly-Ub-TRAF3:ticam1:ticam2:activated TLR4 complex (human)
PR:000036034 IRF7:p-tbk1:K63-poly-Ub-TRAF3:ticam1:ticam2:activated TLR4 complex (human)
PR:000036036 IRF3:p-IKKE:K63-poly-Ub-TRAF3:ticam1:ticam2:activated TLR4 complex (human)
PR:000036038 IRF7:p-IKKE:K63-poly-Ub-TRAF3:ticam1:ticam2:activated TLR4 complex (human)
PR:000036041 K63-poly-Ub-TRAF3:ticam1:ticam2:activated TLR4 complex (human)
PR:000036049 K63-pUb-rip1:ticam1:ticam2:activated TLR4 complex (human)
PR:000036053 IKK complex:K63-pUb-rip1:ticam1:ticam2:activated TLR4 complex (human)
PR:000036056 rip3:ticam1:ticam2:activated TLR4 complex (human)
PR:000036058 rip1:rip3:ticam1:ticam2:activated TLR4 complex (human)
PR:000036060 pro-caspase-8:fadd:rip1:ticam1:ticam2:activated TLR4 complex (human)
PR:000036123 p-tbk1:K63-poly-Ub-TRAF3:ticam1:ticam2:activated TLR4 complex complex (human)
PR:000036124 p-IKKE:K63-poly-Ub-TRAF3:ticam1:ticam2:activated TLR4 complex complex (human)
PR:000036135 TIRAP:PIP2:activated TLR4 complex (human)
PR:000037446 MYD88:TIRAP:PIP2:BTK:activated TLR4 complex (human)
PR:000037447 TIRAP:PIP2:BTK:activated TLR4 complex (human)
PR:000037448 pTIRAP:PIP2:BTK:activated TLR4 complex (human)
PR:000037479 lipopolysaccharide receptor complex 4 (human)
PR:000044684 activated TLR4 complex (human)
PR:000027171 mLY96/iso:1/SigPep-/NGlyco:1 PR:000027174 MYD88s:TIRAP:activated TLR4 receptor (mouse)
PR:000027175 MYD88l:TIRAP:activated TLR4 receptor (mouse)
PR:000027187 IRAK4:MYD88:TIRAP:activated TLR4 complex (mouse)
PR:000027196 TIRAP:PIP2:activated TLR4 (mouse)
PR:000027204 ticam2:activated TLR4 complex (mouse)
PR:000027207 ticam1:ticam2:activated TLR4 complex (mouse)
PR:000027217 pTIRAP:PIP2:activated TLR4 complex (mouse)
PR:000027220 IRAK1:IRAK4:MYD88:TIRAP:activated TLR4 (mouse)
PR:000027221 pIRAK1:IRAK4:MYD88:TIRAP:activated TLR4 (mouse)
PR:000027267 IRAK3:IRAK1:IRAK4:MYD88:TIRAP:activated TLR4 (mouse)
PR:000028683 traf3:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000035710 traf6:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000036005 LY96:TLR4 complex (mouse)
PR:000036077 activated TLR4 complex (mouse)
PR:000036090 tbk1:tank:ikke:traf3:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000036093 tbk1:K63-poly-Ub-tank:Ikke:traf3:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000036095 K63-poly-Ub-tank:traf3:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000036097 tbk1:K63-poly-Ub-tank:traf3:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000036099 ikke:K63-poly-Ub-tank:traf3:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000036101 rip1:traf6:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000036105 pel1:rip1:traf6:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000036109 pel1:K63-poly-Ub-rip1:traf6:ticam1:ticam2:activated TLR4 complex (mouse)
PR:000037476 lipopolysaccharide receptor complex 3 (mouse)
PR:000037477 TIRAP:PIP2:BTK:activated TLR4 complex (mouse)
PR:000037478 pTIRAP:PIP2:BTK:activated TLR4 complex (mouse)
PR:000037481 MYD88:TIRAP:PIP2:BTK:activated TLR4 complex (mouse)
PR:000037794 MD2:GB4:TLR4 complex (mouse)
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Functional Annotation (PRO-centric view) Switch to GO Centric View   
PRO Term GO Annotation Evidence
PR:000025786 hLY96/iso:1/SigPep-/NGlyco:1
UniProtKB:Q9Y6Y9-1, 19-160, Asn-26/Asn-114, MOD:00160
enablesGO:0001530 lipopolysaccharide binding PMID:17569869
GO:1990458 lipooligosaccharide binding PMID:19783674
located_inGO:0005615 extracellular space PMID:19783674
GO:0005615 extracellular space PMID:19783674
GO:0005886 plasma membrane Reactome:REACT_7660
PR:000026051 hMYC/iso:1/OGlyco:1
UniProtKB:P01106-1, Thr-58, MOD:00806
acts_upstream_of_or_withinGO:0006357 regulation of transcription by RNA polymerase II PMID:11904304
enablesGO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific PMID:11904304
PR:000027171 mLY96/iso:1/SigPep-/NGlyco:1
UniProtKB:Q9JHF9-1, 19-160, Asn-26/Asn-114/Asn-150, MOD:00160
enablesNOT GO:1990458 lipooligosaccharide binding PMID:19783674
located_inGO:0005615 extracellular space PMID:19783674
PR:000036407 mIFNG/iso:1/SigPep-/GlycoRes+
UniProtKB:P01580-1, 23-155, MOD:00693
acts_upstream_of_or_withinGO:0050776 regulation of immune response PMID:12882831
enablesGO:0005125 cytokine activity PMID:11027433; PMID:12925700; PMID:15240719
located_inGO:0005615 extracellular space PMID:11057672; PMID:11728336; PMID:15240714
PR:000036412 hFST/iso:1/SigPep-/GlycoRes+
UniProtKB:P19883-1, 30-344, MOD:00693
located_inGO:0005615 extracellular space PMID:16150905
PR:000036413 pig-FST/iso:1/ClvNGlyco:2
UniProtKB:P10669-1, 30-332, Asn-124/Asn-288, MOD:00160
acts_upstream_of_or_withinGO:0032926 negative regulation of activin receptor signaling pathway PMID:8340384
PR:000036414 hFST/iso:1/ClvNGlyco:2
UniProtKB:P19883-1, 30-332, Asn-124/Asn-288, MOD:00160
located_inGO:0005615 extracellular space PMID:16150905
PR:000036415 hFST/iso:2/SigPep-/NGlyco:1
UniProtKB:P19883-2, 30-317, Asn-124/Asn-288, MOD:00160
acts_upstream_of_or_withinGO:0032926 negative regulation of activin receptor signaling pathway PMID:1906804
located_inGO:0005615 extracellular space PMID:16150905
PR:000036419 hIFNG/iso:1/SigPep-/NGlyco:1
UniProtKB:P01579-1, 24-157, Asn-48/Asn-120, MOD:00160
enablesGO:0005133 type II interferon receptor binding PMID:10986460
GO:0042803 protein homodimerization activity PMID:3109913
located_inGO:0005615 extracellular space PMID:6427223
PR:000036420 hIFNG/iso:1/ClvNGlyco:2
UniProtKB:P01579-1, 24-161, Asn-48/Asn-120, MOD:00160
enablesGO:0042803 protein homodimerization activity PMID:1902591
PR:000036440 mACVR2A/iso:1/GlycoPhos:1 acts_upstream_of_or_withinGO:0008584 male gonad development PMID:7885474
GO:0009952 anterior/posterior pattern specification PMID:10452853; PMID:16991118
enablesGO:0004675 transmembrane receptor protein serine/threonine kinase activity PMID:8395525
GO:0016362 activin receptor activity, type II PMID:8395525
GO:0019838 growth factor binding PMID:11459935; PMID:12414726
GO:0042803 protein homodimerization activity PMID:8612709
located_inGO:0048179 activin receptor complex PMID:8395525
PR:000036441 hACVR2A/iso:1/GlycoPhos:1 acts_upstream_of_or_withinGO:0007178 cell surface receptor protein serine/threonine kinase signaling pathway PMID:1314589
enablesGO:0016362 activin receptor activity, type II PMID:12665502
located_inGO:0005886 plasma membrane PMID:1314589
GO:0048179 activin receptor complex PMID:8622651
PR:000036442 mACVR2B/iso:ActR-IIB2/NGlycoPhos:1 acts_upstream_of_or_withinGO:0007178 cell surface receptor protein serine/threonine kinase signaling pathway PMID:8721982
GO:0009952 anterior/posterior pattern specification PMID:10452853; PMID:16991118
GO:0032925 regulation of activin receptor signaling pathway PMID:8721982
enablesGO:0004675 transmembrane receptor protein serine/threonine kinase activity PMID:1326537
GO:0019838 growth factor binding PMID:11459935; PMID:12414726
NOT GO:0050431 transforming growth factor beta binding PMID:1326537
PR:000036443 hACVR2B/iso:ActR-IIB2/NGlycoPhos:1 enablesGO:0004675 transmembrane receptor protein serine/threonine kinase activity PMID:8622651
GO:0005515 protein binding PMID:11279102; PMID:9872992
GO:0016362 activin receptor activity, type II PMID:8622651
located_inGO:0005886 plasma membrane PMID:8161782
GO:0048179 activin receptor complex PMID:8622651
PR:000036444 hAMH/iso:1/ClvNGlyco:2
UniProtKB:P03971-1, 26-450, 451-560, MOD:00160
acts_upstream_of_or_withinGO:0001880 Mullerian duct regression PMID:14750901; PMID:3754790
GO:0007267 cell-cell signaling PMID:3754790
GO:0007548 sex differentiation PMID:12834017
enablesGO:0005102 signaling receptor binding PMID:14750901
GO:0005179 hormone activity PMID:14750901
GO:0046983 protein dimerization activity PMID:14673134
located_inGO:0005576 extracellular region PMID:14750901; PMID:3754790
PR:000036457 hDCN/iso:A/ClvGlyco:1
UniProtKB:P07585-1, 31-359, Ser-34, MOD:00814|Asn-211/Asn-262/Asn-303, MOD:00160
acts_upstream_of_or_withinGO:0030199 collagen fibril organization PMID:17651433
enablesGO:0005154 epidermal growth factor receptor binding PMID:9988678
located_inGO:0031012 extracellular matrix PMID:17651433; PMID:9988678
PR:000036458 hFASLG/iso:FasL/NGlyco:1
UniProtKB:P48023-1, Asn-184/Asn-250/Asn-260, MOD:00160
acts_upstream_of_or_withinGO:0097190 apoptotic signaling pathway PMID:9405425
enablesGO:0005102 signaling receptor binding PMID:9405425
PR:000036490 mTHBS1/iso:1/Clv:2/GlycoRes+
UniProtKB:P35441-1, 312-1170, MOD:00693
acts_upstream_of_or_withinGO:0016525 negative regulation of angiogenesis PMID:17082774
GO:0060055 angiogenesis involved in wound healing PMID:17082774
PR:000036498 hSP1/iso:1/OGlyco:1
UniProtKB:P08047-1, Ser-491, MOD:00805
enablesGO:0003677 DNA binding PMID:11371615
increased GO:0003700 DNA-binding transcription factor activity relative to PR:000036497 hSP1/iso:1/Clv:1 PMID:11371615
located_inGO:0005634 nucleus PMID:11371615
PR:000036517 hBMP7/iso:1/mature/NGlyco:1
UniProtKB:P18075-1, 293-431, Asn-372, MOD:00160
enablesGO:0005102 signaling receptor binding PMID:9872992
GO:0042803 protein homodimerization activity PMID:15929982; PMID:8570652
located_inGO:0005615 extracellular space PMID:15047707; PMID:15929982
PR:000036518 mBMP7/iso:1/mature/NGlyco:1
UniProtKB:P23359-1, 292-430, Asn-371, MOD:00160
acts_upstream_of_or_withinGO:0030509 BMP signaling pathway PMID:14623234
PR:000036519 hBMP7/iso:1/mature/NGlyco:2
UniProtKB:P18075-1, 20-292, 293-431, Asn-372, MOD:00160
enablesNOT GO:0005102 signaling receptor binding PMID:15929982
located_inGO:0005615 extracellular space PMID:15929982
PR:000036573 mHCN1/iso:1/NGlyco:1
UniProtKB:O88704-1, Asn-327, MOD:00160
located_inGO:0009986 cell surface PMID:12928435
PR:000036574 mHCN2/iso:1/NGlyco:1
UniProtKB:O88703-1, Asn-380, MOD:00160
located_inGO:0009986 cell surface PMID:12928435
PR:000036581 hKCNH2/iso:A/NGlyco:1
UniProtKB:Q12809-1, Asn-598, MOD:00160
located_inGO:0008076 voltage-gated potassium channel complex PMID:12063277
GO:0009986 cell surface PMID:12063277
PR:000036582 mKCNH2/iso:A/NGlyco:1
UniProtKB:O35219-1, Asn-600, MOD:00160
located_inGO:0005886 plasma membrane MGI_ref:3040012; PMID:14668215
PR:000036608 hINHA/iso:1/ClvNGlyco:2
UniProtKB:P05111-1, 233-366, Asn-268/Asn-302, MOD:00160
located_inGO:0005615 extracellular space PMID:17456790; PMID:8885240
GO:0043512 inhibin A complex PMID:17456790; PMID:8885240
PR:000036631 hNRP1/iso:1/ClvOGlyco:1
UniProtKB:O14786-1, 22-923, Ser-612, MOD:00215
acts_upstream_of_or_withinGO:0030947 regulation of vascular endothelial growth factor receptor signaling pathway PMID:16763549
enablesincreased GO:0005515 protein binding with PR:P15692-4 PMID:16763549
GO:0043184 vascular endothelial growth factor receptor 2 binding PMID:16763549
PR:000036632 hNRP1/iso:1/ClvOGlyco:2
UniProtKB:O14786-1, 22-923, Ser-612, MOD:00213
acts_upstream_of_or_withinGO:0030947 regulation of vascular endothelial growth factor receptor signaling pathway PMID:16763549
enablesincreased GO:0005515 protein binding with PR:P15692-4 PMID:16763549
decreased GO:0043184 vascular endothelial growth factor receptor 2 binding relative to PR:000036635 hNRP1/iso:1/SigPep- PMID:16763549
PR:000037262 mCOCH/Clv:p18
UniProtKB:Q62507, 26-134, MOD:00693
located_inGO:0005576 extracellular region MGI_ref:5525040; PMID:23684986
PR:000044791 HIV1(JRCSF)-env/Clv:gp120/NGlyco:1
UniProtKB:P20871, 31-503, Asn-195/Asn-228/Asn-239/Asn-260/Asn-293/Asn-299/Asn-329/Asn-336/Asn-382/Asn-388/Asn-392, MOD:00160
enablesGO:0005515 protein binding with PR:Q9NNX6 C-type lectin domain family 4 member L (human) PMID:12438611