Reviewed,
UniProtKB/Swiss-Prot P02765 (FETUA_HUMAN)
Last modified
September 2, 2008.
Version 108.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Alpha-2-HS-glycoprotein Alternative name(s): Ba-alpha-2-glycoprotein Alpha-2-Z-globulin Fetuin-A Cleaved into the following 2 chains: 1- Recommended name: Alpha-2-HS-glycoprotein chain A 2- Recommended name: Alpha-2-HS-glycoprotein chain B | ||||||
| Gene names |
| ||||||
| Organism | Homo sapiens (Human) | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 | |
| Tissue specificity | Synthesized in liver and selectively concentrated in bone matrix. Secrete din plasma. It is also found in dentin in much higher quantities than other plasma proteins. |
| 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 domains. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||||
Molecule processing | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | ||||||||
| Chain | 19 – 300 | 282 | Alpha-2-HS-glycoprotein chain A | |||||||
| Propeptide | 301 – 340 | 40 | Connecting peptide | |||||||
| Chain | 341 – 367 | 27 | Alpha-2-HS-glycoprotein chain B | |||||||
Regions | ||||||||||
| Domain | 27 – 144 | 118 | Cystatin 1 | |||||||
| Domain | 145 – 260 | 116 | Cystatin 2 | |||||||
Amino acid modifications | ||||||||||
| Modified residue | 138 | 1 | Phosphoserine | |||||||
| Modified residue | 325 | 1 | Phosphoserine By similarity | |||||||
| Modified residue | 328 | 1 | Phosphoserine By similarity | |||||||
| Modified residue | 330 | 1 | Phosphoserine | |||||||
| Glycosylation | 156 | 1 | N-linked (GlcNAc...) | |||||||
| Glycosylation | 176 | 1 | N-linked (GlcNAc...) | |||||||
| Glycosylation | 256 | 1 | O-linked (GalNAc...) | |||||||
| Glycosylation | 270 | 1 | O-linked (GalNAc...) | |||||||
| Glycosylation | 346 | 1 | O-linked (GalNAc...) | |||||||
| Disulfide bond | 32 ↔ 358 | Interchain (between A and B chains) | ||||||||
| Disulfide bond | 89 ↔ 100 | |||||||||
| Disulfide bond | 114 ↔ 132 | |||||||||
| Disulfide bond | 146 ↔ 149 | |||||||||
| Disulfide bond | 208 ↔ 219 | |||||||||
| Disulfide bond | 230 ↔ 247 | |||||||||
Natural variations | ||||||||||
| Natural variant | 248 | 1 | T → M in allele AHSG*2. dbSNP rs4917. | |||||||
| Natural variant | 256 | 1 | T → S in allele AHSG*2. dbSNP rs4918. | |||||||
| Natural variant | 276 | 1 | D → N in allele AHSG*5. | |||||||
| Natural variant | 317 | 1 | R → C in allele AHSG*3. | |||||||
Experimental info | ||||||||||
| Sequence conflict | 16 | 1 | C → W in BAA22652. Ref.2 | |||||||
| Sequence conflict | 54 | 1 | W → K AA sequence Ref.5 | |||||||
| Sequence conflict | 125 | 1 | F → S in BAA22651. Ref.7 | |||||||
| Sequence conflict | 150 – 182 | 33 | PLLAP…SNFQL → MVGWQEGANHKNGAGRSQKQ EMAEKMVPEVASG in AAF69649. Ref.9 | |||||||
| Sequence conflict | 204 | 1 | S → C in BAA22652. Ref.2 | |||||||
Sequences
| ||||||||||||||||||
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: 3474608] [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: 9322749] [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: 11415520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS AHSG*5 ASN-276 AND AHSG*3 CYS-317. |
| [4] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver. |
| [5] | "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: 3944104] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-300. |
| [6] | "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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-28. Tissue: Platelet. |
| [7] | "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: 9003486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-367, VARIANTS ALLELE AHSG*2 MET-248 AND SER-256. Tissue: Liver. |
| [8] | Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 107-120, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell. |
| [9] | "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. |
| [10] | "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 F.G. J. Biol. Chem. 258:4966-4971(1983) [PubMed: 6833285] [Abstract] Cited for: PROTEIN SEQUENCE OF 341-367. |
| [11] | "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: 2645941] [Abstract] Cited for: DISULFIDE BONDS. |
| [12] | "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: 2760061] [Abstract] Cited for: DISULFIDE BONDS. |
| [13] | "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: 11439093] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-138 AND SER-330. Tissue: Plasma. |
| [14] | "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: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-176. |
| [15] | "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: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156, MASS SPECTROMETRY. Tissue: Plasma. |
| [16] | "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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156 AND ASN-176, MASS SPECTROMETRY. Tissue: Plasma. |
| [17] | "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: 16740002] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156 AND ASN-176, MASS SPECTROMETRY. Tissue: Saliva. |
| [18] | "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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, MASS SPECTROMETRY. Tissue: Platelet. |
| [19] | "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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M16961 mRNA. Translation: AAA51683.1. D67013 Genomic DNA. Translation: BAA22652.1. AB038689 Genomic DNA. Translation: BAA92189.1. BC048198 mRNA. Translation: AAH48198.1. BC052590 mRNA. Translation: AAH52590.1. D67012 mRNA. Translation: BAA22651.1. AF119895 mRNA. Translation: AAF69649.1. | |
| PIR | WOHU. A29081. |
| RefSeq | NP_001613.2. |
| UniGene | Hs.324746 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P02765. |
Protein family/group databases | |
| MEROPS | I25.020. I25.021. |
PTM databases | |
| GlycoSuiteDB | P02765. |
| PhosphoSite | P02765. |
2-D gel databases | |
| SWISS-2DPAGE | P02765. |
| DOSAC-COBS-2DPAGE | P02765. |
| Siena-2DPAGE | P02765. |
Genome annotation databases | |
| Ensembl | ENSG00000145192. Homo sapiens. [Contig view] |
| GeneID | 197. |
| KEGG | hsa:197. |
Organism-specific databases | |
| H-InvDB | HIX0024338. |
| HGNC | HGNC:349. AHSG. |
| HPA | HPA001524. HPA001525. |
| MIM | 138680. gene. |
| PharmGKB | PA24642. |
| GenAtlas | Search... |
| GeneCards | Search... |
Phylogenomic databases | |
| HOGENOM | P02765. |
| HOVERGEN | P02765. |
Gene expression databases | |
| ArrayExpress | P02765. |
| CleanEx | HS_AHSG. |
| GermOnline | ENSG00000145192. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR000010. Prot_inh_cystat. IPR001363. Prot_inh_fetuin_CS. [Graphical view] |
| Pfam | PF00031. Cystatin. 2 hits. [Graphical view] |
| SMART | SM00043. CY. 2 hits. [Graphical view] |
| PROSITE | PS01254. FETUIN_1. 1 hit. PS01255. FETUIN_2. 1 hit. [Graphical view] |
| ProDom | P02765. [Graphical view] [Entries sharing at least one domain] |
| BLOCKS | Search... |
Other Resources | |
| SOURCE | Search... |
| ProtoNet | Search... |
Entry information
| Entry name | FETUA_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P02765 Secondary accession number(s): O14961, O14962, Q9P152 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


