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P02765

- FETUA_HUMAN

UniProt

P02765 - FETUA_HUMAN

Protein

Alpha-2-HS-glycoprotein

Gene

AHSG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. cysteine-type endopeptidase inhibitor activity Source: InterPro
    2. kinase inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. acute-phase response Source: UniProtKB
    2. negative regulation of bone mineralization Source: UniProtKB
    3. negative regulation of insulin receptor signaling pathway Source: UniProtKB
    4. negative regulation of phosphorylation Source: GOC
    5. ossification Source: Ensembl
    6. pinocytosis Source: UniProtKB
    7. positive regulation of phagocytosis Source: UniProtKB
    8. regulation of bone mineralization Source: UniProtKB
    9. regulation of inflammatory response Source: UniProtKB
    10. skeletal system development Source: UniProtKB

    Keywords - Biological processi

    Mineral balance

    Protein family/group databases

    MEROPSiI25.020.

    Names & Taxonomyi

    Protein namesi
    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:
    Gene namesi
    Name:AHSG
    Synonyms:FETUA
    ORF Names:PRO2743
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:349. AHSG.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24642.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 300282Alpha-2-HS-glycoprotein chain A1 PublicationPRO_0000008887Add
    BLAST
    Propeptidei301 – 34040Connecting peptide1 PublicationPRO_0000008888Add
    BLAST
    Chaini341 – 36727Alpha-2-HS-glycoprotein chain BPRO_0000008889Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 358Interchain (between A and B chains)
    Disulfide bondi89 ↔ 1001 PublicationPROSITE-ProRule annotation
    Disulfide bondi114 ↔ 1321 PublicationPROSITE-ProRule annotation
    Modified residuei138 – 1381Phosphoserine4 Publications
    Disulfide bondi146 ↔ 1491 PublicationPROSITE-ProRule annotation
    Glycosylationi156 – 1561N-linked (GlcNAc...) (complex)7 PublicationsCAR_000064
    Glycosylationi176 – 1761N-linked (GlcNAc...) (complex)5 PublicationsCAR_000065
    Disulfide bondi208 ↔ 2191 PublicationPROSITE-ProRule annotation
    Disulfide bondi230 ↔ 2471 PublicationPROSITE-ProRule annotation
    Glycosylationi256 – 2561O-linked (GalNAc...)CAR_000066
    Glycosylationi270 – 2701O-linked (GalNAc...)CAR_000067
    Modified residuei325 – 3251PhosphoserineBy similarity
    Modified residuei328 – 3281PhosphoserineBy similarity
    Modified residuei330 – 3301Phosphoserine1 Publication
    Glycosylationi346 – 3461O-linked (GalNAc...)1 PublicationCAR_000068

    Post-translational modificationi

    Phosphorylation sites are present in the extracellular medium.4 Publications
    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).8 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP02765.
    PaxDbiP02765.
    PRIDEiP02765.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP02765.
    UniCarbKBiP02765.

    Miscellaneous databases

    PMAP-CutDBP02765.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiP02765.
    BgeeiP02765.
    CleanExiHS_AHSG.
    GenevestigatoriP02765.

    Organism-specific databases

    HPAiCAB026209.
    HPA001524.
    HPA001525.

    Interactioni

    Subunit structurei

    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.

    Protein-protein interaction databases

    BioGridi106700. 16 interactions.
    IntActiP02765. 9 interactions.
    MINTiMINT-5004009.
    STRINGi9606.ENSP00000393887.

    Structurei

    3D structure databases

    ProteinModelPortaliP02765.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 133107Cystatin fetuin-A-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 255112Cystatin fetuin-A-type 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the fetuin family.PROSITE-ProRule annotation
    Contains 2 cystatin fetuin-A-type domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG44208.
    HOVERGENiHBG051607.
    InParanoidiP02765.
    OrthoDBiEOG71K63R.
    PhylomeDBiP02765.
    TreeFamiTF333729.

    Family and domain databases

    InterProiIPR025760. Cystatin_Fetuin_A.
    IPR000010. Prot_inh_cystat.
    IPR001363. Prot_inh_fetuin_CS.
    [Graphical view]
    PfamiPF00031. Cystatin. 1 hit.
    [Graphical view]
    SMARTiSM00043. CY. 2 hits.
    [Graphical view]
    PROSITEiPS51529. CYSTATIN_FETUIN_A. 2 hits.
    PS01254. FETUIN_1. 1 hit.
    PS01255. FETUIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02765-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSLVLLLCL AQLWGCHSAP HGPGLIYRQP NCDDPETEEA ALVAIDYINQ    50
    NLPWGYKHTL NQIDEVKVWP QQPSGELFEI EIDTLETTCH VLDPTPVARC 100
    SVRQLKEHAV EGDCDFQLLK LDGKFSVVYA KCDSSPDSAE DVRKVCQDCP 150
    LLAPLNDTRV VHAAKAALAA FNAQNNGSNF QLEEISRAQL VPLPPSTYVE 200
    FTVSGTDCVA KEATEAAKCN LLAEKQYGFC KATLSEKLGG AEVAVTCTVF 250
    QTQPVTSQPQ PEGANEAVPT PVVDPDAPPS PPLGAPGLPP AGSPPDSHVL 300
    LAAPPGHQLH RAHYDLRHTF MGVVSLGSPS GEVSHPRKTR TVVQPSVGAA 350
    AGPVVPPCPG RIRHFKV 367
    Length:367
    Mass (Da):39,325
    Last modified:April 1, 1988 - v1
    Checksum:i1AAF0C8D6B7E2789
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161C → W in BAA22652. (PubMed:9322749)Curated
    Sequence conflicti54 – 541W → K AA sequence (PubMed:3944104)Curated
    Sequence conflicti125 – 1251F → S in BAA22651. (PubMed:9003486)Curated
    Sequence conflicti150 – 18233PLLAP…SNFQL → MVGWQEGANHKNGAGRSQKQ EMAEKMVPEVASG in AAF69649. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti204 – 2041S → C in BAA22652. (PubMed:9322749)Curated

    Polymorphismi

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti142 – 1421V → L.
    Corresponds to variant rs7633550 [ dbSNP | Ensembl ].
    VAR_055802
    Natural varianti248 – 2481T → M in allele AHSG*2. 1 Publication
    Corresponds to variant rs4917 [ dbSNP | Ensembl ].
    VAR_002388
    Natural varianti256 – 2561T → S in allele AHSG*2. 2 Publications
    Corresponds to variant rs4918 [ dbSNP | Ensembl ].
    VAR_002389
    Natural varianti276 – 2761D → N in allele AHSG*5. 1 Publication
    Corresponds to variant rs70961709 [ dbSNP | Ensembl ].
    VAR_012474
    Natural varianti317 – 3171R → C in allele AHSG*3. 1 Publication
    Corresponds to variant rs35457250 [ dbSNP | Ensembl ].
    VAR_012475

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3278.1.
    PIRiA29081. WOHU.
    RefSeqiNP_001613.2. NM_001622.2.
    UniGeneiHs.324746.

    Genome annotation databases

    EnsembliENST00000411641; ENSP00000393887; ENSG00000145192.
    GeneIDi197.
    KEGGihsa:197.

    Polymorphism databases

    DMDMi112910.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3278.1.
    PIRi A29081. WOHU.
    RefSeqi NP_001613.2. NM_001622.2.
    UniGenei Hs.324746.

    3D structure databases

    ProteinModelPortali P02765.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106700. 16 interactions.
    IntActi P02765. 9 interactions.
    MINTi MINT-5004009.
    STRINGi 9606.ENSP00000393887.

    Protein family/group databases

    MEROPSi I25.020.

    PTM databases

    PhosphoSitei P02765.
    UniCarbKBi P02765.

    Polymorphism databases

    DMDMi 112910.

    2D gel databases

    DOSAC-COBS-2DPAGE P02765.
    SWISS-2DPAGE P02765.

    Proteomic databases

    MaxQBi P02765.
    PaxDbi P02765.
    PRIDEi P02765.

    Protocols and materials databases

    DNASUi 197.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000411641 ; ENSP00000393887 ; ENSG00000145192 .
    GeneIDi 197.
    KEGGi hsa:197.

    Organism-specific databases

    CTDi 197.
    GeneCardsi GC03P186330.
    H-InvDB HIX0024338.
    HGNCi HGNC:349. AHSG.
    HPAi CAB026209.
    HPA001524.
    HPA001525.
    MIMi 138680. gene.
    neXtProti NX_P02765.
    PharmGKBi PA24642.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44208.
    HOVERGENi HBG051607.
    InParanoidi P02765.
    OrthoDBi EOG71K63R.
    PhylomeDBi P02765.
    TreeFami TF333729.

    Miscellaneous databases

    ChiTaRSi AHSG. human.
    GeneWikii Alpha-2-HS-glycoprotein.
    GenomeRNAii 197.
    NextBioi 790.
    PMAP-CutDB P02765.
    PROi P02765.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02765.
    Bgeei P02765.
    CleanExi HS_AHSG.
    Genevestigatori P02765.

    Family and domain databases

    InterProi IPR025760. Cystatin_Fetuin_A.
    IPR000010. Prot_inh_cystat.
    IPR001363. Prot_inh_fetuin_CS.
    [Graphical view ]
    Pfami PF00031. Cystatin. 1 hit.
    [Graphical view ]
    SMARTi SM00043. CY. 2 hits.
    [Graphical view ]
    PROSITEi PS51529. CYSTATIN_FETUIN_A. 2 hits.
    PS01254. FETUIN_1. 1 hit.
    PS01255. FETUIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    22. 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. 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. 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.

    Entry informationi

    Entry nameiFETUA_HUMAN
    AccessioniPrimary (citable) accession number: P02765
    Secondary accession number(s): A8K9N6
    , B2R7G1, O14961, O14962, Q9P152
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 166 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3