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P25311 (ZA2G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc-alpha-2-glycoprotein

Short name=Zn-alpha-2-GP
Short name=Zn-alpha-2-glycoprotein
Gene names
Name:AZGP1
Synonyms:ZAG, ZNGP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.

Subunit structure

Interacts with PIP.

Subcellular location

Secreted.

Tissue specificity

Blood plasma, seminal plasma, urine, saliva, sweat, epithelial cells of various human glands, liver.

Post-translational modification

N-glycosylated. N-glycan at Asn-128: Hex5HexNAc4. Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the MHC class I family.

Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.

Sequence caution

The sequence AAA61311.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA03123.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA14417.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA42438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis

Non-traceable author statement PubMed 10462714. Source: GOC

antigen processing and presentation

Inferred from Biological aspect of Ancestor. Source: RefGenome

antigen processing and presentation of peptide antigen via MHC class I

Inferred from electronic annotation. Source: InterPro

cell adhesion

Inferred from direct assay PubMed 9813179. Source: UniProtKB

detection of chemical stimulus involved in sensory perception of bitter taste

Inferred from direct assay PubMed 24248522. Source: UniProt

immune response

Inferred from electronic annotation. Source: InterPro

negative regulation of cell proliferation

Non-traceable author statement PubMed 10462714. Source: UniProtKB

positive regulation of T cell mediated cytotoxicity

Inferred from electronic annotation. Source: InterPro

protein transmembrane transport

Non-traceable author statement PubMed 6896906. Source: GOC

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

   Cellular_componentMHC class I protein complex

Inferred from electronic annotation. Source: InterPro

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065PubMed 24248522. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionantigen binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

glycoprotein binding

Inferred from physical interaction Ref.23. Source: UniProt

peptide antigen binding

Inferred from electronic annotation. Source: InterPro

protein transmembrane transporter activity

Non-traceable author statement PubMed 6896906. Source: UniProtKB

ribonuclease activity

Non-traceable author statement PubMed 10462714. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.9 Ref.10
Chain21 – 298278Zinc-alpha-2-glycoprotein
PRO_0000019012

Regions

Domain207 – 29286Ig-like C1-type

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid
Glycosylation1091N-linked (GlcNAc...) (complex) Ref.16 Ref.17 Ref.18 Ref.19 Ref.21
Glycosylation1121N-linked (GlcNAc...) Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
Glycosylation1281N-linked (GlcNAc...) (complex) Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Glycosylation2591N-linked (GlcNAc...) Ref.21 Ref.22 Ref.23
Disulfide bond123 ↔ 186 Ref.21 Ref.22 Ref.23
Disulfide bond225 ↔ 280 Ref.21 Ref.22 Ref.23

Experimental info

Sequence conflict21V → S in CAA42438. Ref.1
Sequence conflict51V → L in CAA42438. Ref.1
Sequence conflict331I → V in AAH05306. Ref.7
Sequence conflict851Q → E AA sequence Ref.9
Sequence conflict96 – 972Missing AA sequence Ref.9
Sequence conflict2441E → Q AA sequence Ref.9

Secondary structure

.................................................. 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25311 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: 006A153A8E32A0B1

FASTA29834,259
        10         20         30         40         50         60 
MVRMVPVLLS LLLLLGPAVP QENQDGRYSL TYIYTGLSKH VEDVPAFQAL GSLNDLQFFR 

        70         80         90        100        110        120 
YNSKDRKSQP MGLWRQVEGM EDWKQDSQLQ KAREDIFMET LKDIVEYYND SNGSHVLQGR 

       130        140        150        160        170        180 
FGCEIENNRS SGAFWKYYYD GKDYIEFNKE IPAWVPFDPA AQITKQKWEA EPVYVQRAKA 

       190        200        210        220        230        240 
YLEEECPATL RKYLKYSKNI LDRQDPPSVV VTSHQAPGEK KKLKCLAYDF YPGKIDVHWT 

       250        260        270        280        290 
RAGEVQEPEL RGDVLHNGNG TYQSWVVVAV PPQDTAPYSC HVQHSSLAQP LVVPWEAS 

« Hide

References

« Hide 'large scale' references
[1]"Human Zn-alpha 2-glycoprotein cDNA cloning and expression analysis in benign and malignant breast tissues."
Freije J.P., Fueyo A., Uria J., Lopez-Otin C.
FEBS Lett. 290:247-249(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[2]"Molecular cloning and chromosomal assignment of the gene for human Zn-alpha 2-glycoprotein."
Ueyama H., Deng H.X., Ohkubo I.
Biochemistry 32:12968-12976(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human Zn-alpha 2-glycoprotein: complete genomic sequence, identification of a related pseudogene and relationship to class I major histocompatibility complex genes."
Freije J.P., Fueyo A., Uria J.A., Velasco G., Sanchez L.M., Lopez-Boado Y.S., Lopez-Otin C.
Genomics 18:575-587(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leukocyte.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [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: Colon and Prostate.
[8]"Cloning and nucleotide sequence of a human Zn-alpha 2-glycoprotein cDNA and chromosomal assignment of its gene."
Ueyama H., Niwa M., Tada T., Sasaki M., Ohkubo I.
Biochem. Biophys. Res. Commun. 177:696-703(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-298.
Tissue: Liver and Prostate.
[9]"Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens."
Araki T., Gejyo F., Takagaki K., Haupt H., Schwick H.G., Buergi W., Marti T., Schaller J., Rickli E., Brossmer R., Atkinson P.H., Putnam F.W., Schmid K.
Proc. Natl. Acad. Sci. U.S.A. 85:679-683(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-298, PYROGLUTAMATE FORMATION AT GLN-21.
Tissue: Plasma.
[10]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-35.
[11]"Biochemical characterization and crystallization of human Zn-alpha2-glycoprotein, a soluble class I major histocompatibility complex homolog."
Sanchez L.M., Lopez-Otin C., Bjorkman P.J.
Proc. Natl. Acad. Sci. U.S.A. 94:4626-4630(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, CRYSTALLIZATION.
[12]"Hydrophobic ligand binding by Zn-alpha 2-glycoprotein, a soluble fat-depleting factor related to major histocompatibility complex proteins."
Kennedy M.W., Heikema A.P., Cooper A., Bjorkman P.J., Sanchez L.M.
J. Biol. Chem. 276:35008-35013(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IN VITRO BINDING OF FATTY ACID.
[13]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128.
Tissue: Bile.
[14]"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-112 AND ASN-128.
Tissue: Plasma.
[15]"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-112.
Tissue: Plasma.
[16]"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-109; ASN-112 AND ASN-128.
Tissue: Saliva.
[17]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128.
Tissue: Milk.
[18]"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-109; ASN-112 AND ASN-128.
Tissue: Liver.
[19]"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-109 AND ASN-128.
[20]"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-128, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules."
Sanchez L.M., Chirino A.J., Bjorkman P.J.
Science 283:1914-1919(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-109; ASN-128 AND ASN-259.
[22]"Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein."
Delker S.L., West A.P. Jr., McDermott L., Kennedy M.W., Bjorkman P.J.
J. Struct. Biol. 148:205-213(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 21-298, DISULFIDE BONDS, GLYCOSYLATION AT ASN-128 AND ASN-259.
[23]"Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma."
Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P., Singh T.P.
J. Mol. Biol. 384:663-672(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 32-149 IN COMPLEX WITH PIP, DISULFIDE BONDS, GLYCOSYLATION AT ASN-259.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59766 mRNA. Translation: CAA42438.1. Different initiation.
D14034 Genomic DNA. Translation: BAA03123.1. Different initiation.
X69953 Genomic DNA. Translation: CAA49574.1.
AC004522 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23862.1.
CH471091 Genomic DNA. Translation: EAW76621.1.
CH471091 Genomic DNA. Translation: EAW76622.1.
BC005306 mRNA. Translation: AAH05306.1.
BC033830 mRNA. Translation: AAH33830.1.
D90427 mRNA. Translation: BAA14417.1. Different initiation.
M76707 mRNA. Translation: AAA61311.1. Different initiation.
PIRA54175.
RefSeqNP_001176.1. NM_001185.3.
UniGeneHs.546239.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T7VX-ray1.95A21-298[»]
1T7WX-ray2.70A21-298[»]
1T7XX-ray3.10A21-298[»]
1T7YX-ray2.80A21-298[»]
1T7ZX-ray3.00A21-298[»]
1T80X-ray2.10A21-298[»]
1ZAGX-ray2.80A/B/C/D25-298[»]
3ES6X-ray3.23A22-298[»]
ProteinModelPortalP25311.
SMRP25311. Positions 25-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107040. 8 interactions.
IntActP25311. 9 interactions.
STRING9606.ENSP00000292401.

PTM databases

PhosphoSiteP25311.

Polymorphism databases

DMDM292495049.

2D gel databases

REPRODUCTION-2DPAGEIPI00166729.
SWISS-2DPAGEP25311.

Proteomic databases

PaxDbP25311.
PRIDEP25311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292401; ENSP00000292401; ENSG00000160862.
GeneID563.
KEGGhsa:563.
UCSCuc003ush.3. human.

Organism-specific databases

CTD563.
GeneCardsGC07M099564.
HGNCHGNC:910. AZGP1.
HPACAB016087.
HPA012582.
MIM194460. gene.
neXtProtNX_P25311.
PharmGKBPA25203.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG25830.
HOGENOMHOG000296917.
HOVERGENHBG016709.
InParanoidP25311.
OMANILDRQD.
OrthoDBEOG7JT6WQ.
PhylomeDBP25311.
TreeFamTF336617.

Gene expression databases

ArrayExpressP25311.
BgeeP25311.
CleanExHS_AZGP1.
GenevestigatorP25311.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR027648. MHC_I_a.
IPR001039. MHC_I_a_a1/a2.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
[Graphical view]
PRINTSPR01638. MHCCLASSI.
SMARTSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMSSF54452. SSF54452. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAZGP1. human.
EvolutionaryTraceP25311.
GeneWikiAZGP1.
GenomeRNAi563.
NextBio2301.
PROP25311.
SOURCESearch...

Entry information

Entry nameZA2G_HUMAN
AccessionPrimary (citable) accession number: P25311
Secondary accession number(s): D6W5T8 expand/collapse secondary AC list , O60386, Q5XKQ4, Q8N4N0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 23, 2010
Last modified: April 16, 2014
This is version 149 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM