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 27-MAR-2024, entry version 213. 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=13; 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. [O15533-1] DR RefSeq; NP_757345.2; NM_172208.2. [O15533-3] DR RefSeq; NP_757346.2; NM_172209.2. [O15533-4] DR PDB; 3F8U; X-ray; 2.60 A; B/D=1-401. DR PDB; 6ENY; EM; 5.80 A; C=21-448. DR PDB; 7QNG; X-ray; 2.70 A; A=1-401. DR PDB; 7QPD; EM; 3.73 A; T=21-448. DR PDB; 7TUE; X-ray; 3.10 A; D=21-401. DR PDB; 7TUF; X-ray; 2.80 A; C/D=21-401. DR PDB; 7TUG; X-ray; 3.90 A; D=21-401. DR PDBsum; 3F8U; -. DR PDBsum; 6ENY; -. DR PDBsum; 7QNG; -. DR PDBsum; 7QPD; -. DR PDBsum; 7TUE; -. DR PDBsum; 7TUF; -. DR PDBsum; 7TUG; -. DR AlphaFoldDB; O15533; -. DR EMDB; EMD-14119; -. DR EMDB; EMD-3906; -. DR SMR; O15533; -. DR BioGRID; 112755; 108. DR ComplexPortal; CPX-2375; Tapasin-ERp57 complex. DR IntAct; O15533; 17. DR MINT; O15533; -. DR STRING; 9606.ENSP00000404833; -. DR TCDB; 8.A.196.1.1; the tapasin (tapasin) family. DR TCDB; 9.A.75.1.2; the mhc ii receptor (mhc2r) family. DR GlyConnect; 1784; 2 N-Linked glycans (1 site). DR GlyCosmos; O15533; 1 site, 1 glycan. DR GlyGen; O15533; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; O15533; -. DR PhosphoSitePlus; O15533; -. DR SwissPalm; O15533; -. DR BioMuta; TAPBP; -. DR EPD; O15533; -. DR jPOST; O15533; -. DR MassIVE; O15533; -. DR MaxQB; O15533; -. DR PaxDb; 9606-ENSP00000404833; -. DR PeptideAtlas; O15533; -. DR ProteomicsDB; 20346; -. DR ProteomicsDB; 48740; -. [O15533-1] DR ProteomicsDB; 48741; -. [O15533-2] DR ProteomicsDB; 48742; -. [O15533-3] DR Pumba; O15533; -. DR TopDownProteomics; O15533-3; -. [O15533-3] DR Antibodypedia; 45647; 221 antibodies from 30 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; ENSG00000231925.14. [O15533-3] DR Ensembl; ENST00000434618.7; ENSP00000395701.2; ENSG00000231925.14. [O15533-1] DR Ensembl; ENST00000456807.6; ENSP00000407195.2; ENSG00000236490.9. DR Ensembl; ENST00000489157.6; ENSP00000419659.1; ENSG00000231925.14. [O15533-4] DR Ensembl; ENST00000551943.3; ENSP00000447665.1; ENSG00000206208.11. [O15533-4] DR Ensembl; ENST00000699659.1; ENSP00000514507.1; ENSG00000231925.14. [O15533-3] 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 AGR; HGNC:11566; -. 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 OMA; YMPPTLE; -. DR OrthoDB; 4240386at2759; -. 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 1155 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 96 other cell types or tissues. DR ExpressionAtlas; O15533; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IC:UniProt. 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:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. 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:0042288; F:MHC class I protein binding; TAS:UniProtKB. DR GO; GO:0023024; F:MHC class I protein complex binding; IBA:GO_Central. DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt. DR GO; GO:0042605; F:peptide antigen binding; TAS:UniProtKB. DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProt. 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: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:UniProt. 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: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; Immunoglobulins; 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 PANTHER; PTHR23411; TAPASIN; 1. DR PANTHER; PTHR23411:SF22; TAPASIN; 1. DR Pfam; PF07654; C1-set; 1. DR PRINTS; PR01669; TAPASIN. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; O15533; HS. 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 58..60 FT /evidence="ECO:0007829|PDB:7TUF" FT TURN 62..64 FT /evidence="ECO:0007829|PDB:7TUF" 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 HELIX 188..191 FT /evidence="ECO:0007829|PDB:7TUF" 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 246..248 FT /evidence="ECO:0007829|PDB:7TUF" 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 302..304 FT /evidence="ECO:0007829|PDB:7TUF" FT TURN 306..308 FT /evidence="ECO:0007829|PDB:7TUF" 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 //