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AX2R_HUMAN
ID   AX2R_HUMAN              Reviewed;         193 AA.
AC   Q3ZCQ2; Q8NHX5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Annexin-2 receptor;
DE   AltName: Full=Annexin II receptor;
DE            Short=AXIIR;
GN   Name=ANXA2R; Synonyms=AX2R, C5orf39;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Bone marrow;
RX   PubMed=16895901; DOI=10.1074/jbc.m607072200;
RA   Lu G., Maeda H., Reddy S.V., Kurihara N., Leach R., Anderson J.L.,
RA   Roodman G.D.;
RT   "Cloning and characterization of the annexin II receptor on human marrow
RT   stromal cells.";
RL   J. Biol. Chem. 281:30542-30550(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-119.
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=10359570; DOI=10.1172/jci6374;
RA   Menaa C., Devlin R.D., Reddy S.V., Gazitt Y., Choi S.J., Roodman G.D.;
RT   "Annexin II increases osteoclast formation by stimulating the proliferation
RT   of osteoclast precursors in human marrow cultures.";
RL   J. Clin. Invest. 103:1605-1613(1999).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: May act as a receptor for annexin II on marrow stromal cells
CC       to induce osteoclast formation.
CC   -!- INTERACTION:
CC       Q3ZCQ2; A5YKK6: CNOT1; NbExp=3; IntAct=EBI-21258284, EBI-1222758;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in lymphocytes.
CC       Expressed in both resting CD4(+) and CD8(+) T-cells.
CC       {ECO:0000269|PubMed:16895901}.
CC   -!- CAUTION: PubMed:16895901 reports that it is a type I membrane protein.
CC       However, no clear transmembrane region is detected by prediction
CC       methods, suggesting that its localization at the plasma membrane is
CC       unsure. {ECO:0000305}.
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DR   EMBL; AY032883; AAK52335.1; -; mRNA.
DR   EMBL; AC025171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC067873; AAH67873.1; -; mRNA.
DR   CCDS; CCDS34153.1; -.
DR   RefSeq; NP_001014301.1; NM_001014279.2.
DR   AlphaFoldDB; Q3ZCQ2; -.
DR   BioGRID; 133074; 8.
DR   IntAct; Q3ZCQ2; 6.
DR   STRING; 9606.ENSP00000315915; -.
DR   GlyGen; Q3ZCQ2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3ZCQ2; -.
DR   PhosphoSitePlus; Q3ZCQ2; -.
DR   BioMuta; ANXA2R; -.
DR   MassIVE; Q3ZCQ2; -.
DR   PaxDb; Q3ZCQ2; -.
DR   PeptideAtlas; Q3ZCQ2; -.
DR   PRIDE; Q3ZCQ2; -.
DR   ProteomicsDB; 61907; -.
DR   Antibodypedia; 23232; 89 antibodies from 21 providers.
DR   DNASU; 389289; -.
DR   Ensembl; ENST00000314890.3; ENSP00000315915.3; ENSG00000177721.5.
DR   Ensembl; ENST00000616064.2; ENSP00000479862.1; ENSG00000177721.5.
DR   GeneID; 389289; -.
DR   KEGG; hsa:389289; -.
DR   MANE-Select; ENST00000616064.2; ENSP00000479862.1; NM_001014279.3; NP_001014301.1.
DR   UCSC; uc003jnf.4; human.
DR   CTD; 389289; -.
DR   DisGeNET; 389289; -.
DR   GeneCards; ANXA2R; -.
DR   HGNC; HGNC:33463; ANXA2R.
DR   HPA; ENSG00000177721; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 611296; gene.
DR   neXtProt; NX_Q3ZCQ2; -.
DR   OpenTargets; ENSG00000177721; -.
DR   PharmGKB; PA162380171; -.
DR   VEuPathDB; HostDB:ENSG00000177721; -.
DR   eggNOG; ENOG502TEGY; Eukaryota.
DR   GeneTree; ENSGT00390000009290; -.
DR   HOGENOM; CLU_1408354_0_0_1; -.
DR   InParanoid; Q3ZCQ2; -.
DR   OMA; YWQNGLF; -.
DR   OrthoDB; 1501144at2759; -.
DR   PhylomeDB; Q3ZCQ2; -.
DR   TreeFam; TF342039; -.
DR   PathwayCommons; Q3ZCQ2; -.
DR   SignaLink; Q3ZCQ2; -.
DR   BioGRID-ORCS; 389289; 14 hits in 1083 CRISPR screens.
DR   GenomeRNAi; 389289; -.
DR   Pharos; Q3ZCQ2; Tbio.
DR   PRO; PR:Q3ZCQ2; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q3ZCQ2; protein.
DR   Bgee; ENSG00000177721; Expressed in granulocyte and 105 other tissues.
DR   Genevisible; Q3ZCQ2; HS.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   InterPro; IPR031449; ANXA2R.
DR   PANTHER; PTHR38820; PTHR38820; 1.
DR   Pfam; PF15721; ANXA2R; 1.
PE   1: Evidence at protein level;
KW   Receptor; Reference proteome.
FT   CHAIN           1..193
FT                   /note="Annexin-2 receptor"
FT                   /id="PRO_0000295727"
FT   REGION          78..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         119
FT                   /note="Q -> R (in dbSNP:rs1054428)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033348"
FT   VARIANT         186
FT                   /note="R -> W (in dbSNP:rs10971)"
FT                   /id="VAR_033349"
SQ   SEQUENCE   193 AA;  21682 MW;  6BBC734AB14CE32F CRC64;
     MEQHFLGCVK RAWDSAEVAP EPQPPPIVSS EDRGPWPLPL YPVLGEYSLD SCDLGLLSSP
     CWRLPGVYWQ NGLSPGVQST LEPSTAKPTE FSWPGTQKQQ EAPVEEVGQA EEPDRLRLQQ
     LPWSSPLHPW DRQQDTEVCD SGCLLERRHP PALQPWRHLP GFSDCLEWIL RVGFAAFSVL
     WACCSRICGA KQP
 
 
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