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P02765 (FETUA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-2-HS-glycoprotein
Alternative name(s):
Alpha-2-Z-globulin
Ba-alpha-2-glycoprotein
Fetuin-A
Gene names
Name:AHSG
Synonyms:FETUA
ORF Names:PRO2743
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions.

Subunit structure

Alpha-2-HS glycoprotein derives from this precursor, when the connecting peptide is cleaved off. The two chains A and B are held together by a single disulfide bond.

Subcellular location

Secreted.

Tissue specificity

Synthesized in liver and selectively concentrated in bone matrix. Secreted in plasma. It is also found in dentin in much higher quantities than other plasma proteins.

Post-translational modification

Phosphorylation sites are present in the extracellular medium.

O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor). Ref.17 Ref.25 Ref.28

Polymorphism

There are two common alleles, AHSG*1 and AHSG*2. AHSG*1 has Thr-248/Thr-256; AHSG*2 has Met-248/Ser-256.

Sequence similarities

Belongs to the fetuin family.

Contains 2 cystatin fetuin-A-type domains.

Ontologies

Keywords
   Biological processMineral balance
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from direct assay PubMed 12153747. Source: UniProtKB

negative regulation of bone mineralization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of insulin receptor signaling pathway

Non-traceable author statement PubMed 12153747. Source: UniProtKB

negative regulation of phosphorylation

Non-traceable author statement PubMed 12203945. Source: GOC

ossification

Inferred from electronic annotation. Source: Ensembl

pinocytosis

Non-traceable author statement PubMed 12773197. Source: UniProtKB

positive regulation of phagocytosis

Inferred from direct assay PubMed 12725640. Source: UniProtKB

regulation of bone mineralization

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of inflammatory response

Inferred from mutant phenotype PubMed 12642050. Source: UniProtKB

skeletal system development

Non-traceable author statement PubMed 12153747. Source: UniProtKB

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Non-traceable author statement PubMed 11922920. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_functioncysteine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: InterPro

kinase inhibitor activity

Non-traceable author statement PubMed 12203945. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABL1P005191EBI-1223374,EBI-375543
Hsd17b7O887361EBI-1223374,EBI-2552537From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.8 Ref.9
Chain19 – 300282Alpha-2-HS-glycoprotein chain A Ref.8
PRO_0000008887
Propeptide301 – 34040Connecting peptide
PRO_0000008888
Chain341 – 36727Alpha-2-HS-glycoprotein chain B
PRO_0000008889

Regions

Domain27 – 133107Cystatin fetuin-A-type 1
Domain144 – 255112Cystatin fetuin-A-type 2

Amino acid modifications

Modified residue1381Phosphoserine Ref.16 Ref.21 Ref.22 Ref.23
Modified residue3251Phosphoserine By similarity
Modified residue3281Phosphoserine By similarity
Modified residue3301Phosphoserine Ref.16
Glycosylation1561N-linked (GlcNAc...) (complex) Ref.18 Ref.19 Ref.20 Ref.24 Ref.25 Ref.26 Ref.28
CAR_000064
Glycosylation1761N-linked (GlcNAc...) (complex) Ref.17 Ref.19 Ref.20 Ref.26 Ref.28
CAR_000065
Glycosylation2561O-linked (GalNAc...)
CAR_000066
Glycosylation2701O-linked (GalNAc...)
CAR_000067
Glycosylation3461O-linked (GalNAc...) Ref.28
CAR_000068
Disulfide bond32 ↔ 358Interchain (between A and B chains) Ref.14 Ref.15
Disulfide bond89 ↔ 100 Ref.14 Ref.15
Disulfide bond114 ↔ 132 Ref.14 Ref.15
Disulfide bond146 ↔ 149 Ref.14 Ref.15
Disulfide bond208 ↔ 219 Ref.14 Ref.15
Disulfide bond230 ↔ 247 Ref.14 Ref.15

Natural variations

Natural variant1421V → L.
Corresponds to variant rs7633550 [ dbSNP | Ensembl ].
VAR_055802
Natural variant2481T → M in allele AHSG*2. Ref.10
Corresponds to variant rs4917 [ dbSNP | Ensembl ].
VAR_002388
Natural variant2561T → S in allele AHSG*2. Ref.4 Ref.10
Corresponds to variant rs4918 [ dbSNP | Ensembl ].
VAR_002389
Natural variant2761D → N in allele AHSG*5. Ref.3
Corresponds to variant rs70961709 [ dbSNP | Ensembl ].
VAR_012474
Natural variant3171R → C in allele AHSG*3. Ref.3
Corresponds to variant rs35457250 [ dbSNP | Ensembl ].
VAR_012475

Experimental info

Sequence conflict161C → W in BAA22652. Ref.2
Sequence conflict541W → K AA sequence Ref.8
Sequence conflict1251F → S in BAA22651. Ref.10
Sequence conflict150 – 18233PLLAP…SNFQL → MVGWQEGANHKNGAGRSQKQ EMAEKMVPEVASG in AAF69649. Ref.12
Sequence conflict2041S → C in BAA22652. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P02765 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 1AAF0C8D6B7E2789

FASTA36739,325
        10         20         30         40         50         60 
MKSLVLLLCL AQLWGCHSAP HGPGLIYRQP NCDDPETEEA ALVAIDYINQ NLPWGYKHTL 

        70         80         90        100        110        120 
NQIDEVKVWP QQPSGELFEI EIDTLETTCH VLDPTPVARC SVRQLKEHAV EGDCDFQLLK 

       130        140        150        160        170        180 
LDGKFSVVYA KCDSSPDSAE DVRKVCQDCP LLAPLNDTRV VHAAKAALAA FNAQNNGSNF 

       190        200        210        220        230        240 
QLEEISRAQL VPLPPSTYVE FTVSGTDCVA KEATEAAKCN LLAEKQYGFC KATLSEKLGG 

       250        260        270        280        290        300 
AEVAVTCTVF QTQPVTSQPQ PEGANEAVPT PVVDPDAPPS PPLGAPGLPP AGSPPDSHVL 

       310        320        330        340        350        360 
LAAPPGHQLH RAHYDLRHTF MGVVSLGSPS GEVSHPRKTR TVVQPSVGAA AGPVVPPCPG 


RIRHFKV 

« Hide

References

« Hide 'large scale' references
[1]"Human alpha 2-HS-glycoprotein: the A and B chains with a connecting sequence are encoded by a single mRNA transcript."
Lee C.-C., Bowman B.H., Yang F.
Proc. Natl. Acad. Sci. U.S.A. 84:4403-4407(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure of the gene encoding human alpha 2-HS glycoprotein (AHSG)."
Osawa M., Umetsu K., Sato M., Ohki T., Yukawa N., Suzuki T., Takeichi S.
Gene 196:121-125(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Haplotype analysis of the human alpha2-HS glycoprotein (fetuin) gene."
Osawa M., Yuasa I., Kitano T., Henke J., Kaneko M., Udono T., Saitou N., Umetsu K.
Ann. Hum. Genet. 65:27-34(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS AHSG*5 ASN-276 AND AHSG*3 CYS-317.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-256.
Tissue: Liver and Mammary gland.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[8]"The complete amino acid sequence of the A-chain of human plasma alpha 2HS-glycoprotein."
Yoshioka Y., Gejyo F., Marti T., Rickli E.E., Burgi W., Offner G.D., Troxler R.F., Schmid K.
J. Biol. Chem. 261:1665-1676(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-300.
[9]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-28.
Tissue: Platelet.
[10]"Molecular evidence for human alpha 2-HS glycoprotein (AHSG) polymorphism."
Osawa M., Umetsu K., Ohki T., Nagasawa T., Suzuki T., Takeichi S.
Hum. Genet. 99:18-21(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-367, VARIANTS ALLELE AHSG*2 MET-248 AND SER-256.
Tissue: Liver.
[11]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 107-120, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[12]"Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-367.
Tissue: Fetal liver.
[13]"Characterization of the B-chain of human plasma alpha 2HS-glycoprotein. The complete amino acid sequence and primary structure of its heteroglycan."
Gejyo F., Chang J.-L., Burgi W., Schmid K., Offner G.D., Troxler R.F., van Halbeek H., Dorland L., Gerwig G.J., Vliegenthart J.F.G.
J. Biol. Chem. 258:4966-4971(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 341-367.
[14]"The position of the disulfide bonds in human plasma alpha 2 HS-glycoprotein and the repeating double disulfide bonds in the domain structure."
Araki T., Yoshioka Y., Schmid K.
Biochim. Biophys. Acta 994:195-199(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[15]"The arrangement of disulfide loops in human alpha 2-HS glycoprotein. Similarity to the disulfide bridge structures of cystatins and kininogens."
Kellerman J., Haupt H., Auerswald E.-A., Mueller-Esterl W.
J. Biol. Chem. 264:14121-14128(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[16]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-138 AND SER-330.
Tissue: Plasma.
[17]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-176.
[18]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156.
Tissue: Plasma.
[19]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156 AND ASN-176.
Tissue: Plasma.
[20]"Identification of N-linked glycoproteins in human saliva by glycoprotein 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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156 AND ASN-176.
Tissue: Saliva.
[21]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[22]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[24]"Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156.
Tissue: Liver.
[25]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-156.
[26]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156 AND ASN-176, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Human urinary glycoproteomics; attachment site specific analysis of N-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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-156; ASN-176 AND SER-346, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16961 mRNA. Translation: AAA51683.1.
D67013 Genomic DNA. Translation: BAA22652.1.
AB038689 Genomic DNA. Translation: BAA92189.1.
AK292751 mRNA. Translation: BAF85440.1.
AK312969 mRNA. Translation: BAG35808.1.
AC068631 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78189.1.
BC048198 mRNA. Translation: AAH48198.1.
BC052590 mRNA. Translation: AAH52590.1.
D67012 mRNA. Translation: BAA22651.1.
AF119895 mRNA. Translation: AAF69649.1.
PIRWOHU. A29081.
RefSeqNP_001613.2. NM_001622.2.
UniGeneHs.324746.

3D structure databases

ProteinModelPortalP02765.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106700. 13 interactions.
IntActP02765. 9 interactions.
MINTMINT-5004009.
STRING9606.ENSP00000393887.

Protein family/group databases

MEROPSI25.020.

PTM databases

PhosphoSiteP02765.
UniCarbKBP02765.

Polymorphism databases

DMDM112910.

2D gel databases

DOSAC-COBS-2DPAGEP02765.
SWISS-2DPAGEP02765.

Proteomic databases

PaxDbP02765.
PRIDEP02765.

Protocols and materials databases

DNASU197.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000411641; ENSP00000393887; ENSG00000145192.
GeneID197.
KEGGhsa:197.

Organism-specific databases

CTD197.
GeneCardsGC03P186330.
H-InvDBHIX0024338.
HGNCHGNC:349. AHSG.
HPACAB026209.
HPA001524.
HPA001525.
MIM138680. gene.
neXtProtNX_P02765.
PharmGKBPA24642.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44208.
HOVERGENHBG051607.
InParanoidP02765.
OrthoDBEOG71K63R.
PhylomeDBP02765.
TreeFamTF333729.

Gene expression databases

ArrayExpressP02765.
BgeeP02765.
CleanExHS_AHSG.
GenevestigatorP02765.

Family and domain databases

InterProIPR025760. Cystatin_Fetuin_A.
IPR000010. Prot_inh_cystat.
IPR001363. Prot_inh_fetuin_CS.
[Graphical view]
PfamPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTSM00043. CY. 2 hits.
[Graphical view]
PROSITEPS51529. CYSTATIN_FETUIN_A. 2 hits.
PS01254. FETUIN_1. 1 hit.
PS01255. FETUIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAHSG. human.
GeneWikiAlpha-2-HS-glycoprotein.
GenomeRNAi197.
NextBio790.
PMAP-CutDBP02765.
PROP02765.
SOURCESearch...

Entry information

Entry nameFETUA_HUMAN
AccessionPrimary (citable) accession number: P02765
Secondary accession number(s): A8K9N6 expand/collapse secondary AC list , B2R7G1, O14961, O14962, Q9P152
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM