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Protein

Alpha-2-HS-glycoprotein

Gene

AHSG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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: UniProtKB
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

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

BgeeiP02765.
CleanExiHS_AHSG.
ExpressionAtlasiP02765. baseline and differential.
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. 19 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.
GeneTreeiENSGT00530000063413.
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

        10         20         30         40         50
MKSLVLLLCL AQLWGCHSAP HGPGLIYRQP NCDDPETEEA ALVAIDYINQ
60 70 80 90 100
NLPWGYKHTL NQIDEVKVWP QQPSGELFEI EIDTLETTCH VLDPTPVARC
110 120 130 140 150
SVRQLKEHAV EGDCDFQLLK LDGKFSVVYA KCDSSPDSAE DVRKVCQDCP
160 170 180 190 200
LLAPLNDTRV VHAAKAALAA FNAQNNGSNF QLEEISRAQL VPLPPSTYVE
210 220 230 240 250
FTVSGTDCVA KEATEAAKCN LLAEKQYGFC KATLSEKLGG AEVAVTCTVF
260 270 280 290 300
QTQPVTSQPQ PEGANEAVPT PVVDPDAPPS PPLGAPGLPP AGSPPDSHVL
310 320 330 340 350
LAAPPGHQLH RAHYDLRHTF MGVVSLGSPS GEVSHPRKTR TVVQPSVGAA
360
AGPVVPPCPG RIRHFKV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP02765.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106700. 19 interactions.
IntActiP02765. 9 interactions.
MINTiMINT-5004009.
STRINGi9606.ENSP00000393887.

Protein family/group databases

MEROPSiI25.020.

PTM databases

PhosphoSiteiP02765.
UniCarbKBiP02765.

Polymorphism databases

DMDMi112910.

2D gel databases

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

Proteomic databases

MaxQBiP02765.
PaxDbiP02765.
PRIDEiP02765.

Protocols and materials databases

DNASUi197.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi197.
GeneCardsiGC03P186330.
H-InvDBHIX0024338.
HGNCiHGNC:349. AHSG.
HPAiCAB026209.
HPA001524.
HPA001525.
MIMi138680. gene.
neXtProtiNX_P02765.
PharmGKBiPA24642.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44208.
GeneTreeiENSGT00530000063413.
HOVERGENiHBG051607.
InParanoidiP02765.
OrthoDBiEOG71K63R.
PhylomeDBiP02765.
TreeFamiTF333729.

Miscellaneous databases

ChiTaRSiAHSG. human.
GeneWikiiAlpha-2-HS-glycoprotein.
GenomeRNAii197.
NextBioi790.
PMAP-CutDBP02765.
PROiP02765.
SOURCEiSearch...

Gene expression databases

BgeeiP02765.
CleanExiHS_AHSG.
ExpressionAtlasiP02765. baseline and differential.
GenevestigatoriP02765.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.