Full text data of TAPBP
TAPBP
(NGS17, TAPA)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Tapasin; TPN; TPSN (NGS-17; TAP-associated protein; TAP-binding protein; Flags: Precursor)
Tapasin; TPN; TPSN (NGS-17; TAP-associated protein; TAP-binding protein; Flags: Precursor)
UniProt
O15533
ID TPSN_HUMAN Reviewed; 448 AA.
AC O15533; A2AB91; A2ABC0; B0V003; B0V0A6; B2ZUA4; E9PGM2; O15210;
read moreAC O15272; Q5STJ8; Q5STK6; Q5STQ5; Q5STQ6; Q66K65; Q96KK7; Q9HAN8;
AC Q9UEE0; Q9UEE4; Q9UIZ6; Q9Y6K2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 140.
DE RecName: Full=Tapasin;
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; Synonyms=NGS17, TAPA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
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
RT transporter associated with antigen processing.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8708-8713(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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.,
RA Cresswell P.;
RT "A critical role for tapasin in the assembly and function of
RT multimeric MHC class I-TAP complexes.";
RL Science 277:1306-1309(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9521053;
RX DOI=10.1002/(SICI)1521-4141(199802)28:02<459::AID-IMMU459>3.3.CO;2-Q;
RA Herberg J.A., Sgouros J., Jones T., Copeman J., Humphray S.J.,
RA Sheer D., Cresswell P., Beck S., Trowsdale J.;
RT "Genomic analysis of the Tapasin gene, located close to the TAP loci
RT in the 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
RT dense 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), AND VARIANT
RP THR-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.,
RA Tadokoro K., Tohma S., Inoue T., Tokunaga K., Yamamoto K., Juji T.;
RT "Polymorphism of TAPASIN and its linkage disequilibria with HLA class
RT II genes in the Japanese population.";
RL Tissue Antigens 52:279-281(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Neutrophil;
RX PubMed=10088603;
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).
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
RT alternatively spliced mRNA.";
RL Genes Immun. 5:101-108(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING.
RC TISSUE=Melanoma;
RX PubMed=20600451; DOI=10.1016/j.humimm.2010.05.019;
RA Belicha-Villanueva A., Golding M., McEvoy S., Sarvaiya N.,
RA Cresswell P., Gollnick S.O., Bangia N.;
RT "Identification of an alternate splice form of tapasin in human
RT melanoma.";
RL Hum. Immunol. 71:1018-1026(2010).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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 THR-260.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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
RT project: 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
RT class I 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-401 IN COMPLEX WITH PDIA3,
RP SUBUNIT, INTERACTION WITH PDIA3, GLYCOSYLATION AT ASN-253, AND
RP DISULFIDE 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).
CC -!- FUNCTION: Involved in the association of MHC class I with
CC transporter associated with antigen processing (TAP) and in the
CC assembly of MHC class I with peptide (peptide loading).
CC -!- SUBUNIT: Heterodimer with PDIA3; disulfide-linked. Interacts with
CC TAP1 and is thus a subunit of the TAP complex, also known as the
CC peptide loading complex (PLC). Interaction with TAP1 is TAP2-
CC independent and is required for efficient peptide-TAP interaction.
CC Obligatory mediator for the interaction between newly assembled
CC MHC class I molecules, calreticulin, PDIA3 and TAP. Up to 4 MHC
CC class I/tapasin complexes bind to 1 TAP.
CC -!- INTERACTION:
CC Q03518:TAP1; NbExp=7; IntAct=EBI-874801, EBI-747259;
CC Q03519:TAP2; NbExp=3; IntAct=EBI-874801, EBI-780781;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein (Probable).
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 Note=Due to a partial intron retention;
CC Name=3;
CC IsoId=O15533-3; Sequence=VSP_017055;
CC Note=No experimental confirmation available;
CC Name=4; Synonyms=tpsnDeltaEx3;
CC IsoId=O15533-4; Sequence=VSP_044455;
CC -!- TISSUE SPECIFICITY: Neutrophils, mostly in fully differentiated
CC cells.
CC -!- DOMAIN: The N-terminus is required for efficient association with
CC MHC class I molecule and for a stable interaction between MHC I
CC and calreticulin. Binding to TAP is mediated by the C-terminus
CC region.
CC -!- POLYMORPHISM: The 2 alleles of TAPBP; TAPBP*01 (Tapasin*01) (shown
CC here) and TAPBP*02 (Tapasin*02); are in linkage disequilibria with
CC the HLA-DRB1 locus in a Japanese population.
CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like)
CC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD32924.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC -!- WEB RESOURCE: Name=TAPBPbase; Note=TAPBP mutation db;
CC URL="http://bioinf.uta.fi/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; BX248088; CAI41784.1; -; Genomic_DNA.
DR EMBL; AL662827; CAM24888.1; -; Genomic_DNA.
DR EMBL; AL662820; CAM25472.1; -; Genomic_DNA.
DR EMBL; BX248088; CAM25703.1; -; Genomic_DNA.
DR EMBL; CR759817; CAQ08029.1; -; Genomic_DNA.
DR EMBL; CR759817; CAQ08031.1; -; Genomic_DNA.
DR EMBL; CR759786; CAQ08259.1; -; Genomic_DNA.
DR EMBL; CR759786; CAQ08261.1; -; 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 RefSeq; NP_003181.3; NM_003190.4.
DR RefSeq; NP_757345.2; NM_172208.2.
DR RefSeq; NP_757346.2; NM_172209.2.
DR UniGene; Hs.370937; -.
DR PDB; 3F8U; X-ray; 2.60 A; B/D=1-401.
DR PDBsum; 3F8U; -.
DR ProteinModelPortal; O15533; -.
DR SMR; O15533; 21-401.
DR IntAct; O15533; 6.
DR MINT; MINT-4053688; -.
DR PhosphoSite; O15533; -.
DR PaxDb; O15533; -.
DR PRIDE; O15533; -.
DR DNASU; 6892; -.
DR Ensembl; ENST00000374572; ENSP00000363700; ENSG00000112493.
DR Ensembl; ENST00000383066; ENSP00000372543; ENSG00000206208.
DR Ensembl; ENST00000383197; ENSP00000372684; ENSG00000206281.
DR Ensembl; ENST00000383198; ENSP00000372685; ENSG00000206281.
DR Ensembl; ENST00000395114; ENSP00000378546; ENSG00000112493.
DR Ensembl; ENST00000417059; ENSP00000402087; ENSG00000236490.
DR Ensembl; ENST00000434618; ENSP00000395701; ENSG00000231925.
DR Ensembl; ENST00000456807; ENSP00000407195; ENSG00000236490.
DR GeneID; 6892; -.
DR KEGG; hsa:6892; -.
DR UCSC; uc003odx.2; human.
DR CTD; 6892; -.
DR GeneCards; GC06M033267; -.
DR GeneCards; GC06Mj33189; -.
DR GeneCards; GC06Mk33245; -.
DR GeneCards; GC06Mm33437; -.
DR GeneCards; GC06Mn33196; -.
DR H-InvDB; HIX0058157; -.
DR H-InvDB; HIX0166135; -.
DR H-InvDB; HIX0166410; -.
DR HGNC; HGNC:11566; TAPBP.
DR HPA; HPA007066; -.
DR MIM; 601962; gene.
DR neXtProt; NX_O15533; -.
DR Orphanet; 34592; Immunodeficiency by defective expression of HLA class 1.
DR PharmGKB; PA36331; -.
DR eggNOG; NOG41000; -.
DR HOVERGEN; HBG005156; -.
DR KO; K08058; -.
DR OMA; YLATVHL; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; TAPBP; human.
DR EvolutionaryTrace; O15533; -.
DR GeneWiki; Tapasin; -.
DR GenomeRNAi; 6892; -.
DR NextBio; 26935; -.
DR PRO; PR:O15533; -.
DR ArrayExpress; O15533; -.
DR Bgee; O15533; -.
DR Genevestigator; O15533; -.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0042824; C:MHC class I peptide loading complex; NAS:UniProtKB.
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:0015433; F:peptide antigen-transporting ATPase activity; TAS:ProtInc.
DR GO; GO:0046978; F:TAP1 binding; TAS:UniProtKB.
DR GO; GO:0046979; F:TAP2 binding; TAS: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:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006952; P:defense response; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0050823; P:peptide antigen stabilization; ISS:UniProtKB.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR008056; Tapasin.
DR PANTHER; PTHR23411:SF0; PTHR23411:SF0; 1.
DR Pfam; PF07654; C1-set; 1.
DR PRINTS; PR01669; TAPASIN.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 20
FT CHAIN 21 448 Tapasin.
FT /FTId=PRO_0000014990.
FT TOPO_DOM 21 414 Lumenal (Potential).
FT TRANSMEM 415 435 Helical; (Potential).
FT TOPO_DOM 436 448 Cytoplasmic (Potential).
FT DOMAIN 292 399 Ig-like C1-type.
FT SITE 428 428 May be involved in interaction with TAP.
FT CARBOHYD 253 253 N-linked (GlcNAc...).
FT DISULFID 27 91
FT DISULFID 115 115 Interchain (with C-57 in PDIA3).
FT DISULFID 315 382
FT VAR_SEQ 70 156 Missing (in isoform 4).
FT /FTId=VSP_044455.
FT VAR_SEQ 405 448 LSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKK
FT KAE -> KSWELCGI (in isoform 2).
FT /FTId=VSP_002577.
FT VAR_SEQ 446 448 KAE -> VQCSTSLYLSLVTLSPHPISKPMEGGCWCGRQNL
FT GLEFTLIWVKTWHYILTVGLFEHAT (in isoform 3).
FT /FTId=VSP_017055.
FT VARIANT 260 260 R -> T (in allele TAPBP*02;
FT dbSNP:rs2071888).
FT /FTId=VAR_010253.
FT CONFLICT 274 274 H -> Y (in Ref. 11; AAH80574).
FT CONFLICT 296 296 L -> P (in Ref. 8; ACD68200).
FT CONFLICT 412 412 D -> N (in Ref. 7; AAD32924).
FT STRAND 23 29
FT STRAND 41 46
FT STRAND 65 69
FT HELIX 74 81
FT STRAND 90 96
FT HELIX 104 109
FT STRAND 112 116
FT HELIX 117 119
FT STRAND 123 129
FT STRAND 134 141
FT STRAND 148 150
FT STRAND 153 164
FT STRAND 169 171
FT STRAND 176 178
FT STRAND 181 184
FT STRAND 203 210
FT STRAND 213 220
FT STRAND 236 242
FT STRAND 250 258
FT HELIX 263 265
FT STRAND 267 275
FT STRAND 278 290
FT STRAND 293 300
FT STRAND 313 323
FT STRAND 327 337
FT STRAND 345 349
FT STRAND 360 367
FT HELIX 373 375
FT STRAND 379 385
FT STRAND 394 399
SQ SEQUENCE 448 AA; 47626 MW; 7340549519B288AD 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 TGNGTFWLPR VQPFQEGTYL ATIHLPYLQG QVTLELAVYK PPKVSLMPAT
LARAAPGEAP PELLCLVSHF YPSGGLEVEW ELRGGPGGRS QKAEGQRWLS ALRHHSDGSV
SLSGHLQPPP VTTEQHGARY ACRIHHPSLP ASGRSAEVTL EVAGLSGPSL EDSVGLFLSA
FLLLGLFKAL GWAAVYLSTC KDSKKKAE
//
ID TPSN_HUMAN Reviewed; 448 AA.
AC O15533; A2AB91; A2ABC0; B0V003; B0V0A6; B2ZUA4; E9PGM2; O15210;
read moreAC O15272; Q5STJ8; Q5STK6; Q5STQ5; Q5STQ6; Q66K65; Q96KK7; Q9HAN8;
AC Q9UEE0; Q9UEE4; Q9UIZ6; Q9Y6K2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 140.
DE RecName: Full=Tapasin;
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; Synonyms=NGS17, TAPA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
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
RT transporter associated with antigen processing.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8708-8713(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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.,
RA Cresswell P.;
RT "A critical role for tapasin in the assembly and function of
RT multimeric MHC class I-TAP complexes.";
RL Science 277:1306-1309(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9521053;
RX DOI=10.1002/(SICI)1521-4141(199802)28:02<459::AID-IMMU459>3.3.CO;2-Q;
RA Herberg J.A., Sgouros J., Jones T., Copeman J., Humphray S.J.,
RA Sheer D., Cresswell P., Beck S., Trowsdale J.;
RT "Genomic analysis of the Tapasin gene, located close to the TAP loci
RT in the 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
RT dense 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), AND VARIANT
RP THR-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.,
RA Tadokoro K., Tohma S., Inoue T., Tokunaga K., Yamamoto K., Juji T.;
RT "Polymorphism of TAPASIN and its linkage disequilibria with HLA class
RT II genes in the Japanese population.";
RL Tissue Antigens 52:279-281(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Neutrophil;
RX PubMed=10088603;
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).
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
RT alternatively spliced mRNA.";
RL Genes Immun. 5:101-108(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING.
RC TISSUE=Melanoma;
RX PubMed=20600451; DOI=10.1016/j.humimm.2010.05.019;
RA Belicha-Villanueva A., Golding M., McEvoy S., Sarvaiya N.,
RA Cresswell P., Gollnick S.O., Bangia N.;
RT "Identification of an alternate splice form of tapasin in human
RT melanoma.";
RL Hum. Immunol. 71:1018-1026(2010).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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 THR-260.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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
RT project: 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
RT class I 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-401 IN COMPLEX WITH PDIA3,
RP SUBUNIT, INTERACTION WITH PDIA3, GLYCOSYLATION AT ASN-253, AND
RP DISULFIDE 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).
CC -!- FUNCTION: Involved in the association of MHC class I with
CC transporter associated with antigen processing (TAP) and in the
CC assembly of MHC class I with peptide (peptide loading).
CC -!- SUBUNIT: Heterodimer with PDIA3; disulfide-linked. Interacts with
CC TAP1 and is thus a subunit of the TAP complex, also known as the
CC peptide loading complex (PLC). Interaction with TAP1 is TAP2-
CC independent and is required for efficient peptide-TAP interaction.
CC Obligatory mediator for the interaction between newly assembled
CC MHC class I molecules, calreticulin, PDIA3 and TAP. Up to 4 MHC
CC class I/tapasin complexes bind to 1 TAP.
CC -!- INTERACTION:
CC Q03518:TAP1; NbExp=7; IntAct=EBI-874801, EBI-747259;
CC Q03519:TAP2; NbExp=3; IntAct=EBI-874801, EBI-780781;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein (Probable).
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 Note=Due to a partial intron retention;
CC Name=3;
CC IsoId=O15533-3; Sequence=VSP_017055;
CC Note=No experimental confirmation available;
CC Name=4; Synonyms=tpsnDeltaEx3;
CC IsoId=O15533-4; Sequence=VSP_044455;
CC -!- TISSUE SPECIFICITY: Neutrophils, mostly in fully differentiated
CC cells.
CC -!- DOMAIN: The N-terminus is required for efficient association with
CC MHC class I molecule and for a stable interaction between MHC I
CC and calreticulin. Binding to TAP is mediated by the C-terminus
CC region.
CC -!- POLYMORPHISM: The 2 alleles of TAPBP; TAPBP*01 (Tapasin*01) (shown
CC here) and TAPBP*02 (Tapasin*02); are in linkage disequilibria with
CC the HLA-DRB1 locus in a Japanese population.
CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like)
CC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD32924.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC -!- WEB RESOURCE: Name=TAPBPbase; Note=TAPBP mutation db;
CC URL="http://bioinf.uta.fi/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; BX248088; CAI41784.1; -; Genomic_DNA.
DR EMBL; AL662827; CAM24888.1; -; Genomic_DNA.
DR EMBL; AL662820; CAM25472.1; -; Genomic_DNA.
DR EMBL; BX248088; CAM25703.1; -; Genomic_DNA.
DR EMBL; CR759817; CAQ08029.1; -; Genomic_DNA.
DR EMBL; CR759817; CAQ08031.1; -; Genomic_DNA.
DR EMBL; CR759786; CAQ08259.1; -; Genomic_DNA.
DR EMBL; CR759786; CAQ08261.1; -; 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 RefSeq; NP_003181.3; NM_003190.4.
DR RefSeq; NP_757345.2; NM_172208.2.
DR RefSeq; NP_757346.2; NM_172209.2.
DR UniGene; Hs.370937; -.
DR PDB; 3F8U; X-ray; 2.60 A; B/D=1-401.
DR PDBsum; 3F8U; -.
DR ProteinModelPortal; O15533; -.
DR SMR; O15533; 21-401.
DR IntAct; O15533; 6.
DR MINT; MINT-4053688; -.
DR PhosphoSite; O15533; -.
DR PaxDb; O15533; -.
DR PRIDE; O15533; -.
DR DNASU; 6892; -.
DR Ensembl; ENST00000374572; ENSP00000363700; ENSG00000112493.
DR Ensembl; ENST00000383066; ENSP00000372543; ENSG00000206208.
DR Ensembl; ENST00000383197; ENSP00000372684; ENSG00000206281.
DR Ensembl; ENST00000383198; ENSP00000372685; ENSG00000206281.
DR Ensembl; ENST00000395114; ENSP00000378546; ENSG00000112493.
DR Ensembl; ENST00000417059; ENSP00000402087; ENSG00000236490.
DR Ensembl; ENST00000434618; ENSP00000395701; ENSG00000231925.
DR Ensembl; ENST00000456807; ENSP00000407195; ENSG00000236490.
DR GeneID; 6892; -.
DR KEGG; hsa:6892; -.
DR UCSC; uc003odx.2; human.
DR CTD; 6892; -.
DR GeneCards; GC06M033267; -.
DR GeneCards; GC06Mj33189; -.
DR GeneCards; GC06Mk33245; -.
DR GeneCards; GC06Mm33437; -.
DR GeneCards; GC06Mn33196; -.
DR H-InvDB; HIX0058157; -.
DR H-InvDB; HIX0166135; -.
DR H-InvDB; HIX0166410; -.
DR HGNC; HGNC:11566; TAPBP.
DR HPA; HPA007066; -.
DR MIM; 601962; gene.
DR neXtProt; NX_O15533; -.
DR Orphanet; 34592; Immunodeficiency by defective expression of HLA class 1.
DR PharmGKB; PA36331; -.
DR eggNOG; NOG41000; -.
DR HOVERGEN; HBG005156; -.
DR KO; K08058; -.
DR OMA; YLATVHL; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; TAPBP; human.
DR EvolutionaryTrace; O15533; -.
DR GeneWiki; Tapasin; -.
DR GenomeRNAi; 6892; -.
DR NextBio; 26935; -.
DR PRO; PR:O15533; -.
DR ArrayExpress; O15533; -.
DR Bgee; O15533; -.
DR Genevestigator; O15533; -.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0042824; C:MHC class I peptide loading complex; NAS:UniProtKB.
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:0015433; F:peptide antigen-transporting ATPase activity; TAS:ProtInc.
DR GO; GO:0046978; F:TAP1 binding; TAS:UniProtKB.
DR GO; GO:0046979; F:TAP2 binding; TAS: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:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006952; P:defense response; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0050823; P:peptide antigen stabilization; ISS:UniProtKB.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR008056; Tapasin.
DR PANTHER; PTHR23411:SF0; PTHR23411:SF0; 1.
DR Pfam; PF07654; C1-set; 1.
DR PRINTS; PR01669; TAPASIN.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 20
FT CHAIN 21 448 Tapasin.
FT /FTId=PRO_0000014990.
FT TOPO_DOM 21 414 Lumenal (Potential).
FT TRANSMEM 415 435 Helical; (Potential).
FT TOPO_DOM 436 448 Cytoplasmic (Potential).
FT DOMAIN 292 399 Ig-like C1-type.
FT SITE 428 428 May be involved in interaction with TAP.
FT CARBOHYD 253 253 N-linked (GlcNAc...).
FT DISULFID 27 91
FT DISULFID 115 115 Interchain (with C-57 in PDIA3).
FT DISULFID 315 382
FT VAR_SEQ 70 156 Missing (in isoform 4).
FT /FTId=VSP_044455.
FT VAR_SEQ 405 448 LSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKK
FT KAE -> KSWELCGI (in isoform 2).
FT /FTId=VSP_002577.
FT VAR_SEQ 446 448 KAE -> VQCSTSLYLSLVTLSPHPISKPMEGGCWCGRQNL
FT GLEFTLIWVKTWHYILTVGLFEHAT (in isoform 3).
FT /FTId=VSP_017055.
FT VARIANT 260 260 R -> T (in allele TAPBP*02;
FT dbSNP:rs2071888).
FT /FTId=VAR_010253.
FT CONFLICT 274 274 H -> Y (in Ref. 11; AAH80574).
FT CONFLICT 296 296 L -> P (in Ref. 8; ACD68200).
FT CONFLICT 412 412 D -> N (in Ref. 7; AAD32924).
FT STRAND 23 29
FT STRAND 41 46
FT STRAND 65 69
FT HELIX 74 81
FT STRAND 90 96
FT HELIX 104 109
FT STRAND 112 116
FT HELIX 117 119
FT STRAND 123 129
FT STRAND 134 141
FT STRAND 148 150
FT STRAND 153 164
FT STRAND 169 171
FT STRAND 176 178
FT STRAND 181 184
FT STRAND 203 210
FT STRAND 213 220
FT STRAND 236 242
FT STRAND 250 258
FT HELIX 263 265
FT STRAND 267 275
FT STRAND 278 290
FT STRAND 293 300
FT STRAND 313 323
FT STRAND 327 337
FT STRAND 345 349
FT STRAND 360 367
FT HELIX 373 375
FT STRAND 379 385
FT STRAND 394 399
SQ SEQUENCE 448 AA; 47626 MW; 7340549519B288AD 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 TGNGTFWLPR VQPFQEGTYL ATIHLPYLQG QVTLELAVYK PPKVSLMPAT
LARAAPGEAP PELLCLVSHF YPSGGLEVEW ELRGGPGGRS QKAEGQRWLS ALRHHSDGSV
SLSGHLQPPP VTTEQHGARY ACRIHHPSLP ASGRSAEVTL EVAGLSGPSL EDSVGLFLSA
FLLLGLFKAL GWAAVYLSTC KDSKKKAE
//
MIM
601962
*RECORD*
*FIELD* NO
601962
*FIELD* TI
*601962 TAP-BINDING PROTEIN; TAPBP
;;TAPASIN; TPSN; TPN
*FIELD* TX
CLONING
Newly assembled major histocompatibility complex (MHC) class I molecules
read more(see 142800), together with the endoplasmic reticulum (ER) chaperone
calreticulin (109091), interact with the transporter associated with
antigen processing (TAP1; 170260) through a molecule called tapasin
(Sadasivan et al., 1996). By molecular cloning of tapasin, Ortmann et
al. (1997) found it to be a type I transmembrane glycoprotein encoded by
an MHC-linked gene. The mature protein has 428 amino acids with a single
N-linked glycosylation site at position 233. It is a member of the
immunoglobulin superfamily with a probable cytoplasmic ER retention
signal. Up to 4 MHC class I/tapasin complexes were found to bind to each
TAP molecule in Daudi and L001 cells. Expression of tapasin in a
negative mutant human cell line restored class I/TAP association and
normal class I cell surface expression. Tapasin expression also
corrected the defective recognition of virus-infected cells of the same
line by class I-restricted cytotoxic T cells, thus establishing a
critical functional role for tapasin in MHC class I-restricted antigen
processing. Herberg et al. (1998) identified an EST encoding the mouse
tapasin homolog.
GENE FUNCTION
Mayer and Klein (2001) proposed that tapasin is in reality an MHC class
I molecule with a different function from that currently executed by
conventional class I molecules. They based this proposal on the amino
acid sequence similarity between tapasin and conventional class I
molecules, on similarity of predicted tertiary structure and domain
organization of the molecules, on similarity of exon/intron organization
of the encoding genes, and on the mapping of the class IA and tapasin
genes into the same chromosomal region in all jawed vertebrates that had
been tested to that time (Michalova et al., 2000).
Yabe et al. (2002) stated that HLA class I expression depends on the
formation of a peptide-loading complex composed of class I heavy chain;
beta-2-microglobulin (B2M; 109700); TAP; and tapasin, which links TAP to
the heavy chain.
Using purified proteins, Rizvi and Raghavan (2006) demonstrated direct
binding of TPN to peptide-deficient MHC class I molecules at physiologic
temperatures. TPN also bound mouse M10.5, a pheromone
receptor-associated protein with a class I-like fold. Class I-TPN
complexes containing B2M assembled more rapidly with peptides than
complexes lacking B2M. Peptide loading of class I inhibited class I-TPN
binding, whereas peptide depletion enhanced binding.
GENE STRUCTURE
Herberg et al. (1998) determined that the coding sequence of the tapasin
gene contains 8 exons, spanning approximately 12 kb. Teng et al. (2002)
noted the presence of a C-terminal KKxx ER retention motif in the TAPBP
gene. The promoter region of TAPBP contains gamma-interferon (IFNG;
147570) induction elements, but no TATA or CAATT boxes.
MAPPING
Ortmann et al. (1997) mapped the tapasin gene to 6p21.3 by analysis of
somatic cell hybrids containing chromosome 6 fragments and fluorescence
in situ hybridization. Herberg et al. (1998) localized the tapasin gene
to a position between the HSET (603763) and HKE1.5 genes and within 500
kb of the TAP1 and TAP2 (170261) genes. By inclusion within mapped
clones, they determined that mouse tapasin maps to chromosome 17 in a
region showing homology of synteny with human chromosome 6p21.3.
MOLECULAR GENETICS
Mutations in the TAP2 gene (e.g., 170261.0004) result in an HLA class I
deficiency called type I bare lymphocyte syndrome (604571). Yabe et al.
(2002) described a 54-year-old woman with type I bare lymphocyte
syndrome who did not exhibit apparent TAP abnormalities but who had a
tapasin defect. The gene encoding tapasin had a 7.4-kb deletion between
introns 3 and 7 caused by an Alu repeat-mediated unequal homologous
recombination (601962.0001). No tapasin polypeptide was detected in the
subject's cells. The cell surface class I expression level in
tapasin-deficient cells was markedly reduced but the reduction was not
as profound as in TAP-deficient cells. Thus, tapasin deficiency is
another cause of type I BLS.
*FIELD* AV
.0001
BARE LYMPHOCYTE SYNDROME, TYPE I
TAPBP, 7.4-KB DEL
In a patient with tapasin deficiency and type I bare lymphocyte syndrome
(604571), Yabe et al. (2002) identified an Alu-mediated 7.4-kb deletion,
encompassing exons 4 through 7, in the TAPBP gene. The patient was a
54-year-old woman who suffered from chronic glomerulonephritis for 10
years. She had been receiving hemodialysis for 5 years. Because kidney
transplantation was being considered, she was subjected to serologic HLA
typing. Her class II antigens could be typed, but class I typing was not
possible. She had a history of herpes zoster and polyps of the stomach
and colon, but no respiratory and skin infections typical of
TAP-deficient subjects. The reason for this difference was not known.
*FIELD* RF
1. Herberg, J. A.; Sgouros, J.; Jones, T.; Copeman, J.; Humphray,
S. J.; Sheer, D.; Cresswell, P.; Beck, S.; Trowsdale, J.: Genomic
analysis of the Tapasin gene, located close to the TAP loci in the
MHC. Europ. J. Immun. 28: 459-467, 1998.
2. Mayer, W. E.; Klein, J.: Is tapasin a modified Mhc class I molecule? Immunogenetics 53:
719-723, 2001.
3. Michalova, V.; Murray, B. W.; Sultmann, H.; Klein, J.: A contig
map of the Mhc class I genomic region in the zebrafish reveals ancient
synteny. J. Immun. 164: 5296-5305, 2000.
4. Ortmann, B.; Copeman, J.; Lehner, P. J.; Sadasivan, B.; Herberg,
J. A.; Grandea, A. G.; Riddell, S. R.; Tampe, R.; Spies, T.; Trowsdale,
J.; Cresswell, P.: A critical role for tapasin in the assembly and
function of multimeric MHC class I-TAP complexes. Science 277: 1306-1309,
1997.
5. Rizvi, S. M.; Raghavan, M.: Direct peptide-regulatable interactions
between MHC class I molecules and tapasin. Proc. Nat. Acad. Sci. 103:
18220-18225, 2006.
6. Sadasivan, B.; Lehner, P. J.; Ortmann, B.; Spies, T.; Cresswell,
P.: Roles for calreticulin and a novel glycoprotein, tapasin, in
the interaction of MHC class I molecules with TAP. Immunity 5: 103-114,
1996.
7. Teng, M. S.; Stephens, R.; Du Pasquier, L.; Freeman, T.; Lindquist,
J. A.; Trowsdale, J.: A human TAPBP (TAPASIN)-related gene, TAPBP-R. Europ.
J. Immun. 32: 1059-1068, 2002.
8. Yabe, T.; Kawamura, S.; Sato, M.; Kashiwase, K.; Tanaka, H.; Ishikawa,
Y.; Asao, Y.; Oyama, J.; Tsuruta, K.; Tokunaga, K.; Tadokoro, K.;
Juji, T.: A subject with a novel type I bare lymphocyte syndrome
has tapasin deficiency due to deletion of 4 exons by Alu-mediated
recombination. Blood 100: 1496-1498, 2002.
*FIELD* CN
Paul J. Converse - updated: 1/26/2007
Victor A. McKusick - updated: 10/21/2002
Paul J. Converse - updated: 6/28/2002
Victor A. McKusick - updated: 5/13/2002
Rebekah S. Rasooly - updated: 3/5/1999
*FIELD* CD
Victor A. McKusick: 8/28/1997
*FIELD* ED
joanna: 02/02/2009
mgross: 1/26/2007
carol: 10/24/2002
tkritzer: 10/21/2002
mgross: 6/28/2002
alopez: 5/21/2002
terry: 5/13/2002
alopez: 4/22/1999
mgross: 3/8/1999
mgross: 3/5/1999
psherman: 6/24/1998
mark: 12/20/1997
mark: 9/17/1997
mark: 8/28/1997
*RECORD*
*FIELD* NO
601962
*FIELD* TI
*601962 TAP-BINDING PROTEIN; TAPBP
;;TAPASIN; TPSN; TPN
*FIELD* TX
CLONING
Newly assembled major histocompatibility complex (MHC) class I molecules
read more(see 142800), together with the endoplasmic reticulum (ER) chaperone
calreticulin (109091), interact with the transporter associated with
antigen processing (TAP1; 170260) through a molecule called tapasin
(Sadasivan et al., 1996). By molecular cloning of tapasin, Ortmann et
al. (1997) found it to be a type I transmembrane glycoprotein encoded by
an MHC-linked gene. The mature protein has 428 amino acids with a single
N-linked glycosylation site at position 233. It is a member of the
immunoglobulin superfamily with a probable cytoplasmic ER retention
signal. Up to 4 MHC class I/tapasin complexes were found to bind to each
TAP molecule in Daudi and L001 cells. Expression of tapasin in a
negative mutant human cell line restored class I/TAP association and
normal class I cell surface expression. Tapasin expression also
corrected the defective recognition of virus-infected cells of the same
line by class I-restricted cytotoxic T cells, thus establishing a
critical functional role for tapasin in MHC class I-restricted antigen
processing. Herberg et al. (1998) identified an EST encoding the mouse
tapasin homolog.
GENE FUNCTION
Mayer and Klein (2001) proposed that tapasin is in reality an MHC class
I molecule with a different function from that currently executed by
conventional class I molecules. They based this proposal on the amino
acid sequence similarity between tapasin and conventional class I
molecules, on similarity of predicted tertiary structure and domain
organization of the molecules, on similarity of exon/intron organization
of the encoding genes, and on the mapping of the class IA and tapasin
genes into the same chromosomal region in all jawed vertebrates that had
been tested to that time (Michalova et al., 2000).
Yabe et al. (2002) stated that HLA class I expression depends on the
formation of a peptide-loading complex composed of class I heavy chain;
beta-2-microglobulin (B2M; 109700); TAP; and tapasin, which links TAP to
the heavy chain.
Using purified proteins, Rizvi and Raghavan (2006) demonstrated direct
binding of TPN to peptide-deficient MHC class I molecules at physiologic
temperatures. TPN also bound mouse M10.5, a pheromone
receptor-associated protein with a class I-like fold. Class I-TPN
complexes containing B2M assembled more rapidly with peptides than
complexes lacking B2M. Peptide loading of class I inhibited class I-TPN
binding, whereas peptide depletion enhanced binding.
GENE STRUCTURE
Herberg et al. (1998) determined that the coding sequence of the tapasin
gene contains 8 exons, spanning approximately 12 kb. Teng et al. (2002)
noted the presence of a C-terminal KKxx ER retention motif in the TAPBP
gene. The promoter region of TAPBP contains gamma-interferon (IFNG;
147570) induction elements, but no TATA or CAATT boxes.
MAPPING
Ortmann et al. (1997) mapped the tapasin gene to 6p21.3 by analysis of
somatic cell hybrids containing chromosome 6 fragments and fluorescence
in situ hybridization. Herberg et al. (1998) localized the tapasin gene
to a position between the HSET (603763) and HKE1.5 genes and within 500
kb of the TAP1 and TAP2 (170261) genes. By inclusion within mapped
clones, they determined that mouse tapasin maps to chromosome 17 in a
region showing homology of synteny with human chromosome 6p21.3.
MOLECULAR GENETICS
Mutations in the TAP2 gene (e.g., 170261.0004) result in an HLA class I
deficiency called type I bare lymphocyte syndrome (604571). Yabe et al.
(2002) described a 54-year-old woman with type I bare lymphocyte
syndrome who did not exhibit apparent TAP abnormalities but who had a
tapasin defect. The gene encoding tapasin had a 7.4-kb deletion between
introns 3 and 7 caused by an Alu repeat-mediated unequal homologous
recombination (601962.0001). No tapasin polypeptide was detected in the
subject's cells. The cell surface class I expression level in
tapasin-deficient cells was markedly reduced but the reduction was not
as profound as in TAP-deficient cells. Thus, tapasin deficiency is
another cause of type I BLS.
*FIELD* AV
.0001
BARE LYMPHOCYTE SYNDROME, TYPE I
TAPBP, 7.4-KB DEL
In a patient with tapasin deficiency and type I bare lymphocyte syndrome
(604571), Yabe et al. (2002) identified an Alu-mediated 7.4-kb deletion,
encompassing exons 4 through 7, in the TAPBP gene. The patient was a
54-year-old woman who suffered from chronic glomerulonephritis for 10
years. She had been receiving hemodialysis for 5 years. Because kidney
transplantation was being considered, she was subjected to serologic HLA
typing. Her class II antigens could be typed, but class I typing was not
possible. She had a history of herpes zoster and polyps of the stomach
and colon, but no respiratory and skin infections typical of
TAP-deficient subjects. The reason for this difference was not known.
*FIELD* RF
1. Herberg, J. A.; Sgouros, J.; Jones, T.; Copeman, J.; Humphray,
S. J.; Sheer, D.; Cresswell, P.; Beck, S.; Trowsdale, J.: Genomic
analysis of the Tapasin gene, located close to the TAP loci in the
MHC. Europ. J. Immun. 28: 459-467, 1998.
2. Mayer, W. E.; Klein, J.: Is tapasin a modified Mhc class I molecule? Immunogenetics 53:
719-723, 2001.
3. Michalova, V.; Murray, B. W.; Sultmann, H.; Klein, J.: A contig
map of the Mhc class I genomic region in the zebrafish reveals ancient
synteny. J. Immun. 164: 5296-5305, 2000.
4. Ortmann, B.; Copeman, J.; Lehner, P. J.; Sadasivan, B.; Herberg,
J. A.; Grandea, A. G.; Riddell, S. R.; Tampe, R.; Spies, T.; Trowsdale,
J.; Cresswell, P.: A critical role for tapasin in the assembly and
function of multimeric MHC class I-TAP complexes. Science 277: 1306-1309,
1997.
5. Rizvi, S. M.; Raghavan, M.: Direct peptide-regulatable interactions
between MHC class I molecules and tapasin. Proc. Nat. Acad. Sci. 103:
18220-18225, 2006.
6. Sadasivan, B.; Lehner, P. J.; Ortmann, B.; Spies, T.; Cresswell,
P.: Roles for calreticulin and a novel glycoprotein, tapasin, in
the interaction of MHC class I molecules with TAP. Immunity 5: 103-114,
1996.
7. Teng, M. S.; Stephens, R.; Du Pasquier, L.; Freeman, T.; Lindquist,
J. A.; Trowsdale, J.: A human TAPBP (TAPASIN)-related gene, TAPBP-R. Europ.
J. Immun. 32: 1059-1068, 2002.
8. Yabe, T.; Kawamura, S.; Sato, M.; Kashiwase, K.; Tanaka, H.; Ishikawa,
Y.; Asao, Y.; Oyama, J.; Tsuruta, K.; Tokunaga, K.; Tadokoro, K.;
Juji, T.: A subject with a novel type I bare lymphocyte syndrome
has tapasin deficiency due to deletion of 4 exons by Alu-mediated
recombination. Blood 100: 1496-1498, 2002.
*FIELD* CN
Paul J. Converse - updated: 1/26/2007
Victor A. McKusick - updated: 10/21/2002
Paul J. Converse - updated: 6/28/2002
Victor A. McKusick - updated: 5/13/2002
Rebekah S. Rasooly - updated: 3/5/1999
*FIELD* CD
Victor A. McKusick: 8/28/1997
*FIELD* ED
joanna: 02/02/2009
mgross: 1/26/2007
carol: 10/24/2002
tkritzer: 10/21/2002
mgross: 6/28/2002
alopez: 5/21/2002
terry: 5/13/2002
alopez: 4/22/1999
mgross: 3/8/1999
mgross: 3/5/1999
psherman: 6/24/1998
mark: 12/20/1997
mark: 9/17/1997
mark: 8/28/1997