FETUA_HUMAN - dbPTM
FETUA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FETUA_HUMAN
UniProt AC P02765
Protein Name Alpha-2-HS-glycoprotein
Gene Name AHSG
Organism Homo sapiens (Human).
Sequence Length 367
Subcellular Localization Secreted.
Protein Description Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions..
Protein Sequence MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCTVFQTQPVTSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
59O-linked_GlycosylationLPWGYKHTLNQIDEV
CCCCCCCCCCCCCEE		24.21OGP
59PhosphorylationLPWGYKHTLNQIDEV
CCCCCCCCCCCCCEE		24.2124144214
74PhosphorylationKVWPQQPSGELFEIE
EECCCCCCCCEEEEE		40.3327130503
124AcetylationQLLKLDGKFSVVYAK
EEEEECCEEEEEEEE		33.8527178108
126PhosphorylationLKLDGKFSVVYAKCD
EEECCEEEEEEEECC		17.7329759185
129PhosphorylationDGKFSVVYAKCDSSP
CCEEEEEEEECCCCC		9.7429759185
131UbiquitinationKFSVVYAKCDSSPDS
EEEEEEEECCCCCCC		22.38-
134PhosphorylationVVYAKCDSSPDSAED
EEEEECCCCCCCHHH		53.9224043423
135PhosphorylationVYAKCDSSPDSAEDV
EEEECCCCCCCHHHH		21.3423911959
137PhosphorylationAKCDSSPDSAEDVRK
EECCCCCCCHHHHHH		63.5332645325
138PhosphorylationKCDSSPDSAEDVRKV
ECCCCCCCHHHHHHH		36.6219664994
144AcetylationDSAEDVRKVCQDCPL
CCHHHHHHHHHCCCC		47.40129503
156N-linked_GlycosylationCPLLAPLNDTRVVHA
CCCEEECCCCHHHHH		47.7722171320
156N-linked_GlycosylationCPLLAPLNDTRVVHA
CCCEEECCCCHHHHH		47.7722171320
176N-linked_GlycosylationAAFNAQNNGSNFQLE
HHHHHCCCCCCCCCE		43.0922171320
176N-linked_GlycosylationAAFNAQNNGSNFQLE
HHHHHCCCCCCCCCE		43.0922171320
196O-linked_GlycosylationQLVPLPPSTYVEFTV
EEECCCCCCEEEEEE		30.36OGP
197O-linked_GlycosylationLVPLPPSTYVEFTVS
EECCCCCCEEEEEEE		37.04OGP
202O-linked_GlycosylationPSTYVEFTVSGTDCV
CCCEEEEEEECCCHH		10.56OGP
224UbiquitinationAKCNLLAEKQYGFCK
HHCCHHHHHHHCCCE		40.4333845483
225AcetylationKCNLLAEKQYGFCKA
HCCHHHHHHHCCCEE		43.1226051181
225UbiquitinationKCNLLAEKQYGFCKA
HCCHHHHHHHCCCEE		43.1233845483
227PhosphorylationNLLAEKQYGFCKATL
CHHHHHHHCCCEEHH		24.20-
231MethylationEKQYGFCKATLSEKL
HHHHCCCEEHHHHHH		41.99-
256O-linked_GlycosylationVFQTQPVTSQPQPEG
EEECCCCCCCCCCCC		28.476833285
270O-linked_GlycosylationGANEAVPTPVVDPDA
CCCCCCCCCCCCCCC		23.326833285
270O-linked_GlycosylationGANEAVPTPVVDPDA
CCCCCCCCCCCCCCC		23.323944104
280O-linked_GlycosylationVDPDAPPSPPLGAPG
CCCCCCCCCCCCCCC		37.78OGP
293O-linked_GlycosylationPGLPPAGSPPDSHVL
CCCCCCCCCCCCEEE		35.05OGP
319PhosphorylationAHYDLRHTFMGVVSL
EECCHHHHEEEEEEC		14.6428060719
319O-linked_GlycosylationAHYDLRHTFMGVVSL
EECCHHHHEEEEEEC		14.64OGP
325PhosphorylationHTFMGVVSLGSPSGE
HHEEEEEECCCCCCC		25.3026657352
325O-linked_GlycosylationHTFMGVVSLGSPSGE
HHEEEEEECCCCCCC		25.30OGP
328O-linked_GlycosylationMGVVSLGSPSGEVSH
EEEEECCCCCCCCCC		22.61OGP
328PhosphorylationMGVVSLGSPSGEVSH
EEEEECCCCCCCCCC		22.6121082442
330O-linked_GlycosylationVVSLGSPSGEVSHPR
EEECCCCCCCCCCCC		49.65OGP
330PhosphorylationVVSLGSPSGEVSHPR
EEECCCCCCCCCCCC		49.6523911959
334O-linked_GlycosylationGSPSGEVSHPRKTRT
CCCCCCCCCCCCCCE		24.38OGP
334PhosphorylationGSPSGEVSHPRKTRT
CCCCCCCCCCCCCCE		24.3821082442
339PhosphorylationEVSHPRKTRTVVQPS
CCCCCCCCCEEECCC		32.6224505115
339O-linked_GlycosylationEVSHPRKTRTVVQPS
CCCCCCCCCEEECCC		32.62UniProtKB CARBOHYD
341PhosphorylationSHPRKTRTVVQPSVG
CCCCCCCEEECCCCC		30.2024505115
341O-linked_GlycosylationSHPRKTRTVVQPSVG
CCCCCCCEEECCCCC		30.20OGP
346O-linked_GlycosylationTRTVVQPSVGAAAGP
CCEEECCCCCHHCCC		18.9822171320
346PhosphorylationTRTVVQPSVGAAAGP
CCEEECCCCCHHCCC		18.9824505115
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
135SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
138SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
319TPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
325SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
328SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
330SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFBXO2Q9UK22
PMID:12140560
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FETUA_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FETUA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPP5_HUMANPPP5Cphysical
22939629
POTEF_HUMANPOTEFphysical
26186194
POTEF_HUMANPOTEFphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FETUA_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT ASN-156; ASN-176 AND SER-346, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156 AND ASN-176, STRUCTUREOF CARBOHYDRATES, AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156, AND MASSSPECTROMETRY.
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156 AND ASN-176, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156 AND ASN-176, AND MASSSPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-176.
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT ASN-156; ASN-176 AND SER-346, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-138, ANDMASS SPECTROMETRY.
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-330 ANDSER-334, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.
"Phosphorylation of human plasma alpha2-Heremans-Schmid glycoprotein(human fetuin) in vivo.";
Haglund A.C., Ek B., Ek P.;
Biochem. J. 357:437-445(2001).
Cited for: PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-138 AND SER-330.

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