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HLA class I histocompatibility antigen, A-23 alpha chain (HLA class I histocompatibility antigen, A-9 alpha chain) (MHC class I antigen A*23)

 1A23_HUMAN              Reviewed;         365 AA.
P30447; Q9TQF1; Q9TQF8; Q9TQG5; Q9TQM6;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
10-OCT-2018, entry version 148.
RecName: Full=HLA class I histocompatibility antigen, A-23 alpha chain;
AltName: Full=HLA class I histocompatibility antigen, A-9 alpha chain;
AltName: Full=MHC class I antigen A*23;
Flags: Precursor;
Name=HLA-A; Synonyms=HLAA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE (ALLELE A*23:01).
PubMed=1729171; DOI=10.1007/BF00216625;
Little A.-M., Madrigal J.A., Parham P.;
"Molecular definition of an elusive third HLA-A9 molecule: HLA-A9.3.";
Immunogenetics 35:41-45(1992).
[2]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*23:02 AND A*23:03).
PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x;
Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R.,
Ng J., Hartzman R.J., Hurley C.K.;
"Seventeen more novel HLA-A locus alleles.";
Tissue Antigens 55:369-373(2000).
[3]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*23:04 AND A*23:05).
PubMed=11169246; DOI=10.1034/j.1399-0039.2000.560610.x;
Steiner N.K., Edson S.M., Mitton W., Ng J., Hartzman R.J.,
Hurley C.K.;
"Seven novel HLA-A alleles carry previously observed polymorphisms.";
Tissue Antigens 56:551-552(2000).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-352; SER-356
AND SER-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Involved in the presentation of foreign antigens to the
immune system.
-!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
microglobulin). {ECO:0000250|UniProtKB:P01892}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- PTM: Polyubiquitinated in a post ER compartment by interaction
with human herpesvirus 8 MIR1 protein. This targets the protein
for rapid degradation via the ubiquitin system (By similarity).
{ECO:0000250}.
-!- POLYMORPHISM: The following alleles of A-23 are known: A*23:01,
A*23:02, A*23:03, A*23:04 and A*23:05. The sequence shown is that
of A*23:01.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M64742; AAA03662.1; -; mRNA.
EMBL; AH007754; AAD33736.1; -; Genomic_DNA.
EMBL; AH007619; AAD28171.1; -; Genomic_DNA.
EMBL; AH007540; AAD22272.1; -; Genomic_DNA.
EMBL; AH007726; AAD31878.1; -; Genomic_DNA.
UniGene; Hs.181244; -.
UniGene; Hs.713441; -.
ProteinModelPortal; P30447; -.
SMR; P30447; -.
IntAct; P30447; 3.
GlyConnect; 1315; -.
iPTMnet; P30447; -.
SwissPalm; P30447; -.
DMDM; 231359; -.
EPD; P30447; -.
MaxQB; P30447; -.
PeptideAtlas; P30447; -.
PRIDE; P30447; -.
Ensembl; ENST00000454091; ENSP00000410645; ENSG00000223980.
DisGeNET; 3105; -.
GeneCards; HLA-A; -.
HGNC; HGNC:4931; HLA-A.
MalaCards; HLA-A; -.
MIM; 142800; gene.
neXtProt; NX_P30447; -.
HOVERGEN; HBG016709; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
ChiTaRS; HLA-A; human.
Proteomes; UP000005640; Chromosome 6.
CleanEx; HS_HLA-A; -.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0042612; C:MHC class I protein complex; ISS:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0030881; F:beta-2-microglobulin binding; ISS:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR001039; MHC_I_a_a1/a2.
InterPro; IPR010579; MHC_I_a_C.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
Pfam; PF06623; MHC_I_C; 1.
PRINTS; PR01638; MHCCLASSI.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane;
MHC I; Phosphoprotein; Polymorphism; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 24
CHAIN 25 365 HLA class I histocompatibility antigen,
A-23 alpha chain.
/FTId=PRO_0000018817.
TOPO_DOM 25 308 Extracellular. {ECO:0000255}.
TRANSMEM 309 332 Helical. {ECO:0000255}.
TOPO_DOM 333 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 209 295 Ig-like C1-type.
REGION 25 114 Alpha-1.
REGION 115 206 Alpha-2.
REGION 207 298 Alpha-3.
REGION 299 308 Connecting peptide.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 344 344 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 125 188 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 227 283 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 31 31 Y -> C (in allele A*23:05).
/FTId=VAR_016606.
VARIANT 151 151 K -> N (in allele A*23:03).
/FTId=VAR_016607.
VARIANT 180 180 L -> W (in allele A*23:02).
/FTId=VAR_016608.
VARIANT 190 191 DG -> EW (in allele A*23:04).
/FTId=VAR_016609.
VARIANT 205 205 R -> H (in dbSNP:rs17185861).
/FTId=VAR_056262.
SEQUENCE 365 AA; 40733 MW; C372DE503BF393D0 CRC64;
MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF
DSDAASQRME PRAPWIEQEG PEYWDEETGK VKAHSQTDRE NLRIALRYYN QSEAGSHTLQ
MMFGCDVGSD GRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQITQRK WEAARVAEQL
RAYLEGTCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
SSQPTVHIVG IIAGLVLLGA VITGAVVAAV MWRRNSSDRK GGSYSQAASS DSAQGSDVSL
TACKV


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