TPSN_HUMAN
ID TPSN_HUMAN Reviewed; 448 AA.
AC O15533; A2AB91; A2ABC0; B0V003; B0V0A6; B2ZUA4; E9PGM2; O15210; O15272;
AC Q5STJ8; Q5STK6; Q5STQ5; Q5STQ6; Q66K65; Q96KK7; Q9HAN8; Q9UEE0; Q9UEE4;
AC Q9UIZ6; Q9Y6K2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Tapasin {ECO:0000303|PubMed:12582157};
DE Short=TPN;
DE Short=TPSN;
DE AltName: Full=NGS-17;
DE AltName: Full=TAP-associated protein;
DE AltName: Full=TAP-binding protein;
DE Flags: Precursor;
GN Name=TAPBP {ECO:0000312|HGNC:HGNC:11566}; Synonyms=NGS17, TAPA;
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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT ARG-260.
RC TISSUE=Lymphoblast;
RX PubMed=9238042; DOI=10.1073/pnas.94.16.8708;
RA Li S., Sjoegren H.-O., Hellman U., Pettersson R.F., Wang P.;
RT "Cloning and functional characterization of a subunit of the transporter
RT associated with antigen processing.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8708-8713(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-260.
RC TISSUE=B-cell;
RX PubMed=9271576; DOI=10.1126/science.277.5330.1306;
RA Ortmann B., Copeman J., Lehner P.J., Sadasivan B., Herberg J.A.,
RA Grandea A.G., Riddell S.R., Tampe R., Spies T., Trowsdale J., Cresswell P.;
RT "A critical role for tapasin in the assembly and function of multimeric MHC
RT class I-TAP complexes.";
RL Science 277:1306-1309(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-260.
RX PubMed=9521053;
RX DOI=10.1002/(sici)1521-4141(199802)28:02<459::aid-immu459>3.0.co;2-z;
RA Herberg J.A., Sgouros J., Jones T., Copeman J., Humphray S.J., Sheer D.,
RA Cresswell P., Beck S., Trowsdale J.;
RT "Genomic analysis of the Tapasin gene, located close to the TAP loci in the
RT MHC.";
RL Eur. J. Immunol. 28:459-467(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9545376; DOI=10.1006/jmbi.1998.1637;
RA Herberg J.A., Beck S., Trowsdale J.;
RT "TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense
RT cluster at the centromeric end of the MHC.";
RL J. Mol. Biol. 277:839-857(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), POLYMORPHISM, AND
RP VARIANT ARG-260.
RC TISSUE=Lymphocyte;
RX PubMed=9802609; DOI=10.1111/j.1399-0039.1998.tb03044.x;
RA Furukawa H., Kashiwase K., Yabe T., Ishikawa Y., Akaza T., Tadokoro K.,
RA Tohma S., Inoue T., Tokunaga K., Yamamoto K., Juji T.;
RT "Polymorphism of TAPASIN and its linkage disequilibria with HLA class II
RT genes in the Japanese population.";
RL Tissue Antigens 52:279-281(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-260.
RC TISSUE=Neutrophil;
RX PubMed=10088603; DOI=10.1002/jlb.65.2.205;
RA El Ouakfaoui S., Heitz D., Paquin R., Beaulieu A.D.;
RT "Granulocyte-macrophage colony-stimulating factor modulates tapasin
RT expression in human neutrophils.";
RL J. Leukoc. Biol. 65:205-210(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ARG-260.
RC TISSUE=B-cell;
RX PubMed=14668790; DOI=10.1038/sj.gene.6364043;
RA Gao B., Williams A., Sewell A., Elliott T.;
RT "Generation of a functional, soluble tapasin protein from an alternatively
RT spliced mRNA.";
RL Genes Immun. 5:101-108(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING, AND VARIANT
RP ARG-260.
RC TISSUE=Melanoma;
RX PubMed=20600451; DOI=10.1016/j.humimm.2010.05.019;
RA Belicha-Villanueva A., Golding M., McEvoy S., Sarvaiya N., Cresswell P.,
RA Gollnick S.O., Bangia N.;
RT "Identification of an alternate splice form of tapasin in human melanoma.";
RL Hum. Immunol. 71:1018-1026(2010).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-260.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-260.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ARG-260.
RC TISSUE=Prostate;
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 [12]
RP MUTAGENESIS, AND DOMAIN CHARACTERIZATION.
RX PubMed=10382748;
RX DOI=10.1002/(sici)1521-4141(199906)29:06<1858::aid-immu1858>3.0.co;2-c;
RA Bangia N., Lehner P.J., Hughes E.A., Surman M., Cresswell P.;
RT "The N-terminal region of tapasin is required to stabilize the MHC class I
RT loading complex.";
RL Eur. J. Immunol. 29:1858-1870(1999).
RN [13]
RP FUNCTION.
RX PubMed=10636848; DOI=10.1074/jbc.275.3.1581;
RA Li S., Paulsson K.M., Chen S., Sjoegren H.-O., Wang P.;
RT "Tapasin is required for efficient peptide binding to transporter
RT associated with antigen processing.";
RL J. Biol. Chem. 275:1581-1586(2000).
RN [14]
RP FUNCTION.
RX PubMed=12582157; DOI=10.1074/jbc.m212882200;
RA Park B., Ahn K.;
RT "An essential function of tapasin in quality control of HLA-G molecules.";
RL J. Biol. Chem. 278:14337-14345(2003).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP FUNCTION, INTERACTION WITH HLA-A*02-B2M, AND MUTAGENESIS OF CYS-115 AND
RP ASN-253.
RX PubMed=21263072; DOI=10.4049/jimmunol.1002959;
RA Rizvi S.M., Del Cid N., Lybarger L., Raghavan M.;
RT "Distinct functions for the glycans of tapasin and heavy chains in the
RT assembly of MHC class I molecules.";
RL J. Immunol. 186:2309-2320(2011).
RN [18]
RP INTERACTION WITH TAP1-TAP2.
RX PubMed=22638925; DOI=10.1007/s00018-012-1005-6;
RA Hulpke S., Tomioka M., Kremmer E., Ueda K., Abele R., Tampe R.;
RT "Direct evidence that the N-terminal extensions of the TAP complex act as
RT autonomous interaction scaffolds for the assembly of the MHC I peptide-
RT loading complex.";
RL Cell. Mol. Life Sci. 69:3317-3327(2012).
RN [19]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-20, AND
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).
RN [20]
RP FUNCTION, SUBUNIT, INTERACTION WITH TAP1-TAP2, SITE, AND MUTAGENESIS OF
RP LYS-428.
RX PubMed=26611325; DOI=10.1038/srep17341;
RA Blees A., Reichel K., Trowitzsch S., Fisette O., Bock C., Abele R.,
RA Hummer G., Schaefer L.V., Tampe R.;
RT "Assembly of the MHC I peptide-loading complex determined by a conserved
RT ionic lock-switch.";
RL Sci. Rep. 5:17341-17341(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-401 IN COMPLEX WITH PDIA3,
RP SUBUNIT, INTERACTION WITH PDIA3, GLYCOSYLATION AT ASN-253, AND DISULFIDE
RP BONDS.
RX PubMed=19119025; DOI=10.1016/j.immuni.2008.10.018;
RA Dong G., Wearsch P.A., Peaper D.R., Cresswell P., Reinisch K.M.;
RT "Insights into MHC class I peptide loading from the structure of the
RT tapasin-ERp57 thiol oxidoreductase heterodimer.";
RL Immunity 30:21-32(2009).
RN [22]
RP INVOLVEMENT IN BLS1.
RX PubMed=12149238; DOI=10.1182/blood-2001-12-0252;
RA Yabe T., Kawamura S., Sato M., Kashiwase K., Tanaka H., Ishikawa Y.,
RA Asao Y., Oyama J., Tsuruta K., Tokunaga K., Tadokoro K., Juji T.;
RT "A subject with a novel type I bare lymphocyte syndrome has tapasin
RT deficiency due to deletion of 4 exons by Alu-mediated recombination.";
RL Blood 100:1496-1498(2002).
CC -!- FUNCTION: Involved in the association of MHC class I with transporter
CC associated with antigen processing (TAP) and in the assembly of MHC
CC class I with peptide (peptide loading). {ECO:0000269|PubMed:10636848,
CC ECO:0000269|PubMed:12582157, ECO:0000269|PubMed:21263072,
CC ECO:0000269|PubMed:26611325}.
CC -!- SUBUNIT: Heterodimer with PDIA3; disulfide-linked. Obligatory mediator
CC for the interaction between newly assembled MHC class I molecules,
CC calreticulin, PDIA3 and TAP. Up to 4 MHC class I/tapasin complexes bind
CC to 1 TAP (PubMed:19119025, PubMed:21263072, PubMed:26611325). Interacts
CC with HLA-G-B2M complex; this interaction is required for loading of
CC high affinity peptides. {ECO:0000269|PubMed:12582157,
CC ECO:0000269|PubMed:19119025, ECO:0000269|PubMed:21263072}.
CC -!- INTERACTION:
CC O15533; P01892: HLA-A; NbExp=10; IntAct=EBI-874801, EBI-2839473;
CC O15533; Q03518: TAP1; NbExp=14; IntAct=EBI-874801, EBI-747259;
CC O15533; Q03519: TAP2; NbExp=8; IntAct=EBI-874801, EBI-780781;
CC O15533; P0C739: BNLF2a; Xeno; NbExp=6; IntAct=EBI-874801, EBI-9346744;
CC O15533; Q77CE4: gN; Xeno; NbExp=2; IntAct=EBI-874801, EBI-11303846;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O15533-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15533-2; Sequence=VSP_002577;
CC Name=3;
CC IsoId=O15533-3; Sequence=VSP_017055;
CC Name=4; Synonyms=tpsnDeltaEx3;
CC IsoId=O15533-4; Sequence=VSP_044455;
CC -!- TISSUE SPECIFICITY: Neutrophils, mostly in fully differentiated cells.
CC -!- DOMAIN: The N-terminus is required for efficient association with MHC
CC class I molecule and for a stable interaction between MHC I and
CC calreticulin. Binding to TAP is mediated by the C-terminal region.
CC {ECO:0000269|PubMed:10382748}.
CC -!- POLYMORPHISM: The 2 alleles of TAPBP; TAPBP*01 (Tapasin*01) (shown
CC here) and TAPBP*02 (Tapasin*02); are in linkage disequilibria with the
CC HLA-DRB1 locus in a Japanese population. {ECO:0000269|PubMed:9802609}.
CC -!- DISEASE: Bare lymphocyte syndrome 1 (BLS1) [MIM:604571]: A HLA class I
CC deficiency. Contrary to bare lymphocyte syndromes type 2 and type 3,
CC which are characterized by early-onset severe combined
CC immunodeficiency, class I antigen deficiencies are not accompanied by
CC particular pathologic manifestations during the first years of life.
CC Systemic infections have not been described. Chronic bacterial
CC infections, often beginning in the first decade of life, are restricted
CC to the respiratory tract. {ECO:0000269|PubMed:12149238}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to a partial intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD32924.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=TAPBPbase; Note=TAPBP mutation db;
CC URL="http://structure.bmc.lu.se/idbase/TAPBPbase/";
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DR EMBL; Y13582; CAA73909.1; -; mRNA.
DR EMBL; AF009510; AAC20076.1; -; mRNA.
DR EMBL; AB010639; BAA28757.1; -; mRNA.
DR EMBL; AB012622; BAA28758.1; -; Genomic_DNA.
DR EMBL; AB012920; BAA28759.1; -; Genomic_DNA.
DR EMBL; AF029750; AAB82949.1; -; mRNA.
DR EMBL; AF067286; AAD32924.2; ALT_SEQ; mRNA.
DR EMBL; AF314222; AAG33061.1; -; mRNA.
DR EMBL; EU693375; ACD68200.1; -; mRNA.
DR EMBL; AL662820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z97183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z97184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03717.1; -; Genomic_DNA.
DR EMBL; BC080574; AAH80574.1; -; mRNA.
DR CCDS; CCDS34426.1; -. [O15533-1]
DR CCDS; CCDS34427.2; -. [O15533-4]
DR CCDS; CCDS34428.2; -. [O15533-3]
DR RefSeq; NP_003181.3; NM_003190.4.
DR RefSeq; NP_757345.2; NM_172208.2.
DR RefSeq; NP_757346.2; NM_172209.2.
DR PDB; 3F8U; X-ray; 2.60 A; B/D=1-401.
DR PDB; 6ENY; EM; 5.80 A; C=21-448.
DR PDBsum; 3F8U; -.
DR PDBsum; 6ENY; -.
DR AlphaFoldDB; O15533; -.
DR BioGRID; 112755; 102.
DR ComplexPortal; CPX-2375; Tapasin-ERp57 complex.
DR IntAct; O15533; 17.
DR MINT; O15533; -.
DR STRING; 9606.ENSP00000404833; -.
DR TCDB; 9.A.75.1.2; the mhc ii receptor (mhc2r) family.
DR GlyConnect; 1784; 2 N-Linked glycans (1 site).
DR GlyGen; O15533; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; O15533; -.
DR PhosphoSitePlus; O15533; -.
DR BioMuta; TAPBP; -.
DR EPD; O15533; -.
DR jPOST; O15533; -.
DR MassIVE; O15533; -.
DR MaxQB; O15533; -.
DR PaxDb; O15533; -.
DR PeptideAtlas; O15533; -.
DR PRIDE; O15533; -.
DR ProteomicsDB; 20346; -.
DR ProteomicsDB; 48740; -. [O15533-1]
DR ProteomicsDB; 48741; -. [O15533-2]
DR ProteomicsDB; 48742; -. [O15533-3]
DR TopDownProteomics; O15533-3; -. [O15533-3]
DR Antibodypedia; 45647; 205 antibodies from 29 providers.
DR CPTC; O15533; 2 antibodies.
DR DNASU; 6892; -.
DR Ensembl; ENST00000374572.7; ENSP00000363700.3; ENSG00000112493.12.
DR Ensembl; ENST00000383065.8; ENSP00000372542.4; ENSG00000206208.11. [O15533-3]
DR Ensembl; ENST00000383066.8; ENSP00000372543.4; ENSG00000206208.11. [O15533-1]
DR Ensembl; ENST00000383197.8; ENSP00000372684.4; ENSG00000206281.11.
DR Ensembl; ENST00000383198.6; ENSP00000372685.2; ENSG00000206281.11.
DR Ensembl; ENST00000395114.7; ENSP00000378546.3; ENSG00000112493.12.
DR Ensembl; ENST00000417059.5; ENSP00000402087.1; ENSG00000236490.9.
DR Ensembl; ENST00000426633.6; ENSP00000404833.2; ENSG00000231925.13. [O15533-3]
DR Ensembl; ENST00000434618.7; ENSP00000395701.2; ENSG00000231925.13. [O15533-1]
DR Ensembl; ENST00000456807.6; ENSP00000407195.2; ENSG00000236490.9.
DR Ensembl; ENST00000489157.5; ENSP00000419659.1; ENSG00000231925.13. [O15533-4]
DR Ensembl; ENST00000551943.3; ENSP00000447665.1; ENSG00000206208.11. [O15533-4]
DR GeneID; 6892; -.
DR KEGG; hsa:6892; -.
DR MANE-Select; ENST00000434618.7; ENSP00000395701.2; NM_003190.5; NP_003181.3.
DR UCSC; uc003odx.3; human. [O15533-1]
DR CTD; 6892; -.
DR DisGeNET; 6892; -.
DR GeneCards; TAPBP; -.
DR HGNC; HGNC:11566; TAPBP.
DR HPA; ENSG00000231925; Low tissue specificity.
DR MalaCards; TAPBP; -.
DR MIM; 601962; gene.
DR MIM; 604571; phenotype.
DR neXtProt; NX_O15533; -.
DR OpenTargets; ENSG00000231925; -.
DR Orphanet; 34592; Immunodeficiency by defective expression of MHC class I.
DR PharmGKB; PA36331; -.
DR VEuPathDB; HostDB:ENSG00000231925; -.
DR eggNOG; ENOG502QR0A; Eukaryota.
DR GeneTree; ENSGT00940000159200; -.
DR InParanoid; O15533; -.
DR OrthoDB; 865957at2759; -.
DR PhylomeDB; O15533; -.
DR TreeFam; TF334274; -.
DR PathwayCommons; O15533; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR SignaLink; O15533; -.
DR BioGRID-ORCS; 6892; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; TAPBP; human.
DR EvolutionaryTrace; O15533; -.
DR GeneWiki; Tapasin; -.
DR GenomeRNAi; 6892; -.
DR Pharos; O15533; Tbio.
DR PRO; PR:O15533; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O15533; protein.
DR Bgee; ENSG00000231925; Expressed in bone marrow cell and 94 other tissues.
DR ExpressionAtlas; O15533; baseline and differential.
DR Genevisible; O15533; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0042824; C:MHC class I peptide loading complex; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0061779; C:Tapasin-ERp57 complex; IPI:ComplexPortal.
DR GO; GO:0015433; F:ABC-type peptide antigen transporter activity; TAS:ProtInc.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0042288; F:MHC class I protein binding; TAS:UniProtKB.
DR GO; GO:0042605; F:peptide antigen binding; TAS:UniProtKB.
DR GO; GO:0062061; F:TAP complex binding; IDA:UniProtKB.
DR GO; GO:0046978; F:TAP1 binding; IDA:UniProtKB.
DR GO; GO:0046979; F:TAP2 binding; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0002397; P:MHC class I protein complex assembly; IBA:GO_Central.
DR GO; GO:0002398; P:MHC class Ib protein complex assembly; IMP:UniProtKB.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; IDA:ComplexPortal.
DR GO; GO:0050823; P:peptide antigen stabilization; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:AgBase.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0061635; P:regulation of protein complex stability; IDA:AgBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR008056; Tapasin.
DR Pfam; PF07654; C1-set; 1.
DR PRINTS; PR01669; TAPASIN.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 21..448
FT /note="Tapasin"
FT /id="PRO_0000014990"
FT TOPO_DOM 21..414
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 292..399
FT /note="Ig-like C1-type"
FT SITE 428
FT /note="Inter-subunit salt bridge with TAP1-TAP2. Essential
FT peptide loading complex assembly"
FT /evidence="ECO:0000269|PubMed:26611325"
FT SITE 428
FT /note="May be involved in interaction with TAP"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19119025,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 27..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:19119025"
FT DISULFID 115
FT /note="Interchain (with C-57 in PDIA3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:19119025"
FT DISULFID 315..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:19119025"
FT VAR_SEQ 70..156
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:20600451"
FT /id="VSP_044455"
FT VAR_SEQ 405..448
FT /note="LSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKKKAE -> KSWE
FT LCGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14668790"
FT /id="VSP_002577"
FT VAR_SEQ 446..448
FT /note="KAE -> VQCSTSLYLSLVTLSPHPISKPMEGGCWCGRQNLGLEFTLIWVKT
FT WHYILTVGLFEHAT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017055"
FT VARIANT 260
FT /note="T -> R (in allele TAPBP*01; dbSNP:rs2071888)"
FT /evidence="ECO:0000269|PubMed:10088603,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:14668790,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:20600451,
FT ECO:0000269|PubMed:9238042, ECO:0000269|PubMed:9271576,
FT ECO:0000269|PubMed:9521053, ECO:0000269|PubMed:9802609,
FT ECO:0000269|Ref.10"
FT /id="VAR_010253"
FT MUTAGEN 115
FT /note="C->A: Abolishes the recruitment of PDIA3, CALR and
FT B2M to the peptide-loading complex."
FT /evidence="ECO:0000269|PubMed:21263072"
FT MUTAGEN 253
FT /note="N->Q: Reduces the recruitment of PDIA3 to TAP1-TAP2
FT transporter."
FT /evidence="ECO:0000269|PubMed:21263072"
FT MUTAGEN 428
FT /note="K->D: Restores interaction with TAP1-TAP2; when
FT associated with TAP1 K-92 or TAP2 K-16."
FT /evidence="ECO:0000269|PubMed:26611325"
FT CONFLICT 274
FT /note="H -> Y (in Ref. 11; AAH80574)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="L -> P (in Ref. 8; ACD68200)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="D -> N (in Ref. 7; AAD32924)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3F8U"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3F8U"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3F8U"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:3F8U"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 278..290
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 313..323
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 327..337
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:3F8U"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:3F8U"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:3F8U"
SQ SEQUENCE 448 AA; 47571 MW; 9F7BF490BA148B08 CRC64;
MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDASGKGLAK RPGALLLRQG PGEPPPRPDL
DPELYLSVHD PAGALQAAFR RYPRGAPAPH CEMSRFVPLP ASAKWASGLT PAQNCPRALD
GAWLMVSISS PVLSLSSLLR PQPEPQQEPV LITMATVVLT VLTHTPAPRV RLGQDALLDL
SFAYMPPTSE AASSLAPGPP PFGLEWRRQH LGKGHLLLAA TPGLNGQMPA AQEGAVAFAA
WDDDEPWGPW TGNGTFWLPT VQPFQEGTYL ATIHLPYLQG QVTLELAVYK PPKVSLMPAT
LARAAPGEAP PELLCLVSHF YPSGGLEVEW ELRGGPGGRS QKAEGQRWLS ALRHHSDGSV
SLSGHLQPPP VTTEQHGARY ACRIHHPSLP ASGRSAEVTL EVAGLSGPSL EDSVGLFLSA
FLLLGLFKAL GWAAVYLSTC KDSKKKAE
