P02765 (FETUA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-2-HS-glycoprotein

Alternative name(s):
Alpha-2-Z-globulin
Ba-alpha-2-glycoprotein
Fetuin-A

Cleaved into the following 2 chains:

1. Alpha-2-HS-glycoprotein chain A
2. Alpha-2-HS-glycoprotein chain B

Gene names

Name:	AHSG
Synonyms:	FETUA
ORF Names:	PRO2743

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.27
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 process	Mineral balance
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute-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 ossification Inferred from electronic annotation. Source: Compara pinocytosis Non-traceable author statement PubMed 12773197. Source: UniProtKB positive regulation of phagocytosis Inferred from direct assay PubMed 12725640. 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_component	extracellular space Non-traceable author statement PubMed 11922920. Source: UniProtKB
Molecular_function	cysteine-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
ABL1	P00519	1	EBI-1223374,EBI-375543
Hsd17b7	O88736	1	EBI-1223374,EBI-2552537	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Ref.8 Ref.9
	Chain	19 – 300	282	Alpha-2-HS-glycoprotein chain A Ref.8		PRO_0000008887
	Propeptide	301 – 340	40	Connecting peptide		PRO_0000008888
	Chain	341 – 367	27	Alpha-2-HS-glycoprotein chain B		PRO_0000008889
Regions
	Domain	27 – 133	107	Cystatin fetuin-A-type 1
	Domain	144 – 255	112	Cystatin fetuin-A-type 2
Amino acid modifications
	Modified residue	138	1	Phosphoserine Ref.16 Ref.21 Ref.22 Ref.23
	Modified residue	325	1	Phosphoserine By similarity
	Modified residue	328	1	Phosphoserine By similarity
	Modified residue	330	1	Phosphoserine Ref.16
	Glycosylation	156	1	N-linked (GlcNAc...) (complex) Ref.18 Ref.19 Ref.20 Ref.24 Ref.25 Ref.27		CAR_000064
	Glycosylation	176	1	N-linked (GlcNAc...) (complex) Ref.17 Ref.19 Ref.20 Ref.25 Ref.27		CAR_000065
	Glycosylation	256	1	O-linked (GalNAc...)		CAR_000066
	Glycosylation	270	1	O-linked (GalNAc...)		CAR_000067
	Glycosylation	346	1	O-linked (GalNAc...) Ref.27		CAR_000068
	Disulfide bond	32 ↔ 358		Interchain (between A and B chains) Ref.14 Ref.15
	Disulfide bond	89 ↔ 100		Ref.14 Ref.15
	Disulfide bond	114 ↔ 132		Ref.14 Ref.15
	Disulfide bond	146 ↔ 149		Ref.14 Ref.15
	Disulfide bond	208 ↔ 219		Ref.14 Ref.15
	Disulfide bond	230 ↔ 247		Ref.14 Ref.15
Natural variations
	Natural variant	142	1	V → L. Corresponds to variant rs7633550 [ dbSNP | Ensembl ].		VAR_055802
	Natural variant	248	1	T → M in allele AHSG*2. Ref.10 Corresponds to variant rs4917 [ dbSNP | Ensembl ].		VAR_002388
	Natural variant	256	1	T → S in allele AHSG*2. Ref.4 Ref.10 Corresponds to variant rs4918 [ dbSNP | Ensembl ].		VAR_002389
	Natural variant	276	1	D → N in allele AHSG*5. Ref.3		VAR_012474
	Natural variant	317	1	R → C in allele AHSG*3. Ref.3 Corresponds to variant rs35457250 [ dbSNP | Ensembl ].		VAR_012475
Experimental info
	Sequence conflict	16	1	C → W in BAA22652. Ref.2
	Sequence conflict	54	1	W → K AA sequence Ref.8
	Sequence conflict	125	1	F → S in BAA22651. Ref.10
	Sequence conflict	150 – 182	33	PLLAP…SNFQL → MVGWQEGANHKNGAGRSQKQ EMAEKMVPEVASG in AAF69649. Ref.12
	Sequence conflict	204	1	S → C in BAA22652. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P02765 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 1AAF0C8D6B7E2789	FASTA	367	39,325
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[25]	"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, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[26]	"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].
[27]	"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, 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.
IPI	IPI00953689.
PIR	WOHU. A29081.
RefSeq	NP_001613.2. NM_001622.2.
UniGene	Hs.324746.
3D structure databases
ProteinModelPortal	P02765.
ModBase	Search...
Protein-protein interaction databases
IntAct	P02765. 9 interactions.
MINT	MINT-5004009.
STRING	9606.ENSP00000393887.
Protein family/group databases
MEROPS	I25.020.
PTM databases
GlycoSuiteDB	P02765.
PhosphoSite	P02765.
Polymorphism databases
DMDM	112910.
2D gel databases
DOSAC-COBS-2DPAGE	P02765.
SWISS-2DPAGE	P02765.
Proteomic databases
PaxDb	P02765.
PRIDE	P02765.
Protocols and materials databases
DNASU	197.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000411641; ENSP00000393887; ENSG00000145192.
GeneID	197.
KEGG	hsa:197.
Organism-specific databases
CTD	197.
GeneCards	GC03P186330.
H-InvDB	HIX0024338.
HGNC	HGNC:349. AHSG.
HPA	CAB026209. HPA001524. HPA001525.
MIM	138680. gene.
neXtProt	NX_P02765.
PharmGKB	PA24642.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG44208.
HOVERGEN	HBG051607.
InParanoid	P02765.
OrthoDB	EOG4QC164.
Enzyme and pathway databases
Pathway_Interaction_DB	bmppathway. BMP receptor signaling.
Gene expression databases
ArrayExpress	P02765.
Bgee	P02765.
CleanEx	HS_AHSG.
Genevestigator	P02765.
GermOnline	ENSG00000145192. Homo sapiens.
Family and domain databases
InterPro	IPR025760. Cystatin_Fetuin_A. IPR000010. Prot_inh_cystat. IPR001363. Prot_inh_fetuin_CS. [Graphical view]
Pfam	PF00031. Cystatin. 1 hit. [Graphical view]
SMART	SM00043. CY. 2 hits. [Graphical view]
PROSITE	PS51529. CYSTATIN_FETUIN_A. 2 hits. PS01254. FETUIN_1. 1 hit. PS01255. FETUIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AHSG. human.
GenomeRNAi	197.
NextBio	790.
PMAP-CutDB	P02765.
SOURCE	Search...

Entry information

Entry name

FETUA_HUMAN

Accession

Primary (citable) accession number: P02765
Secondary accession number(s): A8K9N6 , B2R7G1, O14961, O14962, Q9P152

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	April 3, 2013
This is version 153 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.