O15533 (TPSN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tapasin
Short name=TPN
Short name=TPSN

Alternative name(s):
NGS-17
TAP-associated protein
TAP-binding protein

Gene names

Name:	TAPBP
Synonyms:	NGS17, TAPA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	448 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading). Ref.13
Subunit structure	Heterodimer with PDIA3; disulfide-linked. Interacts with TAP1 and is thus a subunit of the TAP complex, also known as the peptide loading complex (PLC). Interaction with TAP1 is TAP2-independent and is required for efficient peptide-TAP interaction. Obligatory mediator for the interaction between newly assembled MHC class I molecules, clareticulin, PDIA3 and TAP. Up to 4 MHC class I/tapasin complexes bind to 1 TAP. Ref.16
Subcellular location	Endoplasmic reticulum membrane; Single-pass type I membrane protein Probable.
Tissue specificity	Neutrophils, mostly in fully differentiated cells.
Domain	The N-terminus is required for efficient association with MHC class I molecule and for a stable interaction between MHC I and calreticulin. Binding to TAP is mediated by the C-terminus region. Ref.12
Polymorphism	The 2 alleles of TAPBP; TAPBP*01 (Tapasin*01) (shown here) and TAPBP*02 (Tapasin*02); are in linkage disequilibria with the HLA-DRB1 locus in a Japanese population.
Sequence similarities	Contains 1 Ig-like C1-type (immunoglobulin-like) domain.
Sequence caution	The sequence AAD32924.2 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I Inferred from electronic annotation. Source: InterPro antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome defense response Inferred from electronic annotation. Source: Compara immune response Traceable author statement Ref.2. Source: ProtInc peptide antigen stabilization Inferred from sequence or structural similarity. Source: UniProtKB protein complex assembly Traceable author statement Ref.2. Source: ProtInc retrograde vesicle-mediated transport, Golgi to ER Non-traceable author statement PubMed 11884415. Source: UniProtKB
Cellular_component	Golgi membrane Inferred from direct assay PubMed 11884415. Source: UniProtKB MHC class I peptide loading complex Non-traceable author statement PubMed 12788224. Source: UniProtKB integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome
Molecular_function	MHC class I protein binding Traceable author statement PubMed 12788224. Source: UniProtKB TAP1 binding Traceable author statement PubMed 12788224. Source: UniProtKB TAP2 binding Traceable author statement PubMed 12788224. Source: UniProtKB peptide antigen binding Traceable author statement PubMed 12788224. Source: UniProtKB peptide antigen-transporting ATPase activity Traceable author statement Ref.1. Source: ProtInc unfolded protein binding Traceable author statement PubMed 12788224. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TAP1	Q03518	7	EBI-874801,EBI-747259
TAP2	Q03519	3	EBI-874801,EBI-780781

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15533-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O15533-2)

The sequence of this isoform differs from the canonical sequence as follows:
     405-448: LSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKKKAE → KSWELCGI

Note: Due to a partial intron retention.

Isoform 3 (identifier: O15533-3)

The sequence of this isoform differs from the canonical sequence as follows:
     446-448: KAE → VQCSTSLYLSLVTLSPHPISKPMEGGCWCGRQNLGLEFTLIWVKTWHYILTVGLFEHAT

Note: No experimental confirmation available.

Isoform 4 (identifier: O15533-4)

Also known as: tpsnDeltaEx3;

The sequence of this isoform differs from the canonical sequence as follows:
     70-156: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Chain

21 – 448

428

Tapasin

PRO_0000014990

Regions

Topological domain

21 – 414

394

Lumenal Potential

Transmembrane

415 – 435

21

Helical; Potential

Topological domain

436 – 448

13

Cytoplasmic Potential

Domain

292 – 399

108

Ig-like C1-type

Sites

Site

428

1

May be involved in interaction with TAP

Amino acid modifications

Glycosylation

253

1

N-linked (GlcNAc...) Ref.14 Ref.16

Disulfide bond

27 ↔ 91

Ref.16

Disulfide bond

115

Interchain (with C-57 in PDIA3) Ref.16

Disulfide bond

315 ↔ 382

Ref.16

Natural variations

Alternative sequence

70 – 156

87

Missing in isoform 4.

VSP_044455

Alternative sequence

405 – 448

44

LSGPS…KKKAE → KSWELCGI in isoform 2.

VSP_002577

Alternative sequence

446 – 448

3

KAE → VQCSTSLYLSLVTLSPHPIS KPMEGGCWCGRQNLGLEFTL IWVKTWHYILTVGLFEHAT in isoform 3.

VSP_017055

Natural variant

260

1

R → T in allele TAPBP*02. Ref.5 Ref.9 Ref.10
Corresponds to variant rs2071888 [ dbSNP | Ensembl ].

VAR_010253

Experimental info

Sequence conflict

274

1

H → Y in AAH80574. Ref.11

Sequence conflict

296

1

L → P in ACD68200. Ref.8

Sequence conflict

412

1

D → N in AAD32924. Ref.7

Secondary structure

1

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448

Helix Strand Turn

Details...

Beta strand

23 – 29

7

Beta strand

41 – 46

6

Beta strand

65 – 69

5

Helix

74 – 81

8

Beta strand

90 – 96

7

Helix

104 – 109

6

Beta strand

112 – 116

5

Helix

117 – 119

3

Beta strand

123 – 129

7

Beta strand

134 – 141

8

Beta strand

148 – 150

3

Beta strand

153 – 164

12

Beta strand

169 – 171

3

Beta strand

176 – 178

3

Beta strand

181 – 184

4

Beta strand

203 – 210

8

Beta strand

213 – 220

8

Beta strand

236 – 242

7

Beta strand

250 – 258

9

Helix

263 – 265

3

Beta strand

267 – 275

9

Beta strand

278 – 290

13

Beta strand

293 – 300

8

Beta strand

313 – 323

11

Beta strand

327 – 337

11

Beta strand

345 – 349

5

Beta strand

360 – 367

8

Helix

373 – 375

3

Beta strand

379 – 385

7

Beta strand

394 – 399

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 7340549519B288AD	FASTA	448	47,626
	10 20 30 40 50 60 MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDASGKGLAK RPGALLLRQG PGEPPPRPDL 70 80 90 100 110 120 DPELYLSVHD PAGALQAAFR RYPRGAPAPH CEMSRFVPLP ASAKWASGLT PAQNCPRALD 130 140 150 160 170 180 GAWLMVSISS PVLSLSSLLR PQPEPQQEPV LITMATVVLT VLTHTPAPRV RLGQDALLDL 190 200 210 220 230 240 SFAYMPPTSE AASSLAPGPP PFGLEWRRQH LGKGHLLLAA TPGLNGQMPA AQEGAVAFAA 250 260 270 280 290 300 WDDDEPWGPW TGNGTFWLPR VQPFQEGTYL ATIHLPYLQG QVTLELAVYK PPKVSLMPAT 310 320 330 340 350 360 LARAAPGEAP PELLCLVSHF YPSGGLEVEW ELRGGPGGRS QKAEGQRWLS ALRHHSDGSV 370 380 390 400 410 420 SLSGHLQPPP VTTEQHGARY ACRIHHPSLP ASGRSAEVTL EVAGLSGPSL EDSVGLFLSA 430 440 FLLLGLFKAL GWAAVYLSTC KDSKKKAE
	Isoform 2 [UniParc]. Checksum: E50E3F41AD7E7EA8	FASTA	412	43,885
	10 20 30 40 50 60 MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDASGKGLAK RPGALLLRQG PGEPPPRPDL 70 80 90 100 110 120 DPELYLSVHD PAGALQAAFR RYPRGAPAPH CEMSRFVPLP ASAKWASGLT PAQNCPRALD 130 140 150 160 170 180 GAWLMVSISS PVLSLSSLLR PQPEPQQEPV LITMATVVLT VLTHTPAPRV RLGQDALLDL 190 200 210 220 230 240 SFAYMPPTSE AASSLAPGPP PFGLEWRRQH LGKGHLLLAA TPGLNGQMPA AQEGAVAFAA 250 260 270 280 290 300 WDDDEPWGPW TGNGTFWLPR VQPFQEGTYL ATIHLPYLQG QVTLELAVYK PPKVSLMPAT 310 320 330 340 350 360 LARAAPGEAP PELLCLVSHF YPSGGLEVEW ELRGGPGGRS QKAEGQRWLS ALRHHSDGSV 370 380 390 400 410 SLSGHLQPPP VTTEQHGARY ACRIHHPSLP ASGRSAEVTL EVAGKSWELC GI
	Isoform 3 [UniParc]. Checksum: BEF063064284DE16	FASTA	504	53,943
	10 20 30 40 50 60 MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDASGKGLAK RPGALLLRQG PGEPPPRPDL 70 80 90 100 110 120 DPELYLSVHD PAGALQAAFR RYPRGAPAPH CEMSRFVPLP ASAKWASGLT PAQNCPRALD 130 140 150 160 170 180 GAWLMVSISS PVLSLSSLLR PQPEPQQEPV LITMATVVLT VLTHTPAPRV RLGQDALLDL 190 200 210 220 230 240 SFAYMPPTSE AASSLAPGPP PFGLEWRRQH LGKGHLLLAA TPGLNGQMPA AQEGAVAFAA 250 260 270 280 290 300 WDDDEPWGPW TGNGTFWLPR VQPFQEGTYL ATIHLPYLQG QVTLELAVYK PPKVSLMPAT 310 320 330 340 350 360 LARAAPGEAP PELLCLVSHF YPSGGLEVEW ELRGGPGGRS QKAEGQRWLS ALRHHSDGSV 370 380 390 400 410 420 SLSGHLQPPP VTTEQHGARY ACRIHHPSLP ASGRSAEVTL EVAGLSGPSL EDSVGLFLSA 430 440 450 460 470 480 FLLLGLFKAL GWAAVYLSTC KDSKKVQCST SLYLSLVTLS PHPISKPMEG GCWCGRQNLG 490 500 LEFTLIWVKT WHYILTVGLF EHAT
	Isoform 4 (tpsnDeltaEx3) [UniParc]. Checksum: E049AA2C6F0B4DED	FASTA	361	38,365
	10 20 30 40 50 60 MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDASGKGLAK RPGALLLRQG PGEPPPRPDL 70 80 90 100 110 120 DPELYLSVHV VLTVLTHTPA PRVRLGQDAL LDLSFAYMPP TSEAASSLAP GPPPFGLEWR 130 140 150 160 170 180 RQHLGKGHLL LAATPGLNGQ MPAAQEGAVA FAAWDDDEPW GPWTGNGTFW LPRVQPFQEG 190 200 210 220 230 240 TYLATIHLPY LQGQVTLELA VYKPPKVSLM PATLARAAPG EAPPELLCLV SHFYPSGGLE 250 260 270 280 290 300 VEWELRGGPG GRSQKAEGQR WLSALRHHSD GSVSLSGHLQ PPPVTTEQHG ARYACRIHHP 310 320 330 340 350 360 SLPASGRSAE VTLEVAGLSG PSLEDSVGLF LSAFLLLGLF KALGWAAVYL STCKDSKKKA E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional characterization of a subunit of the transporter associated with antigen processing." Li S., Sjoegren H.-O., Hellman U., Pettersson R.F., Wang P. Proc. Natl. Acad. Sci. U.S.A. 94:8708-8713(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Lymphoblast.
[2]	"A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes." 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. Science 277:1306-1309(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: B-cell.
[3]	"Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC." Herberg J.A., Sgouros J., Jones T., Copeman J., Humphray S.J., Sheer D., Cresswell P., Beck S., Trowsdale J. Eur. J. Immunol. 28:459-467(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC." Herberg J.A., Beck S., Trowsdale J. J. Mol. Biol. 277:839-857(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Polymorphism of TAPASIN and its linkage disequilibria with HLA class II genes in the Japanese population." Furukawa H., Kashiwase K., Yabe T., Ishikawa Y., Akaza T., Tadokoro K., Tohma S., Inoue T., Tokunaga K., Yamamoto K., Juji T. Tissue Antigens 52:279-281(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT THR-260. Tissue: Lymphocyte.
[6]	"Granulocyte-macrophage colony-stimulating factor modulates tapasin expression in human neutrophils." El Ouakfaoui S., Heitz D., Paquin R., Beaulieu A.D. J. Leukoc. Biol. 65:205-210(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Neutrophil.
[7]	"Generation of a functional, soluble tapasin protein from an alternatively spliced mRNA." Gao B., Williams A., Sewell A., Elliott T. Genes Immun. 5:101-108(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: B-cell.
[8]	"Identification of an alternate splice form of tapasin in human melanoma." Belicha-Villanueva A., Golding M., McEvoy S., Sarvaiya N., Cresswell P., Gollnick S.O., Bangia N. Hum. Immunol. 71:1018-1026(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING. Tissue: Melanoma.
[9]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-260.
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-260.
[11]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Prostate.
[12]	"The N-terminal region of tapasin is required to stabilize the MHC class I loading complex." Bangia N., Lehner P.J., Hughes E.A., Surman M., Cresswell P. Eur. J. Immunol. 29:1858-1870(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS, DOMAIN CHARACTERIZATION.
[13]	"Tapasin is required for efficient peptide binding to transporter associated with antigen processing." Li S., Paulsson K.M., Chen S., Sjoegren H.-O., Wang P. J. Biol. Chem. 275:1581-1586(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253, MASS SPECTROMETRY. Tissue: Liver.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer." Dong G., Wearsch P.A., Peaper D.R., Cresswell P., Reinisch K.M. Immunity 30:21-32(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-401 IN COMPLEX WITH PDIA3, SUBUNIT, INTERACTION WITH PDIA3, GLYCOSYLATION AT ASN-253, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

TAPBPbase

TAPBP mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y13582 mRNA. Translation: CAA73909.1.
AF009510 mRNA. Translation: AAC20076.1.
AB010639 mRNA. Translation: BAA28757.1.
AB012622 Genomic DNA. Translation: BAA28758.1.
AB012920 Genomic DNA. Translation: BAA28759.1.
AF029750 mRNA. Translation: AAB82949.1.
AF067286 mRNA. Translation: AAD32924.2. Sequence problems.
AF314222 mRNA. Translation: AAG33061.1.
EU693375 mRNA. Translation: ACD68200.1.
BX248088 Genomic DNA. Translation: CAI41784.1.
AL662827 Genomic DNA. Translation: CAM24888.1.
AL662820 Genomic DNA. Translation: CAM25472.1.
BX248088 Genomic DNA. Translation: CAM25703.1.
CR759817 Genomic DNA. Translation: CAQ08029.1.
CR759817 Genomic DNA. Translation: CAQ08031.1.
CR759786 Genomic DNA. Translation: CAQ08259.1.
CR759786 Genomic DNA. Translation: CAQ08261.1.
Z97183 Genomic DNA. No translation available.
Z97184 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03717.1.
BC080574 mRNA. Translation: AAH80574.1.

IPI

IPI00007327.
IPI00217384.
IPI00645962.
IPI00942301.

RefSeq

NP_003181.3. NM_003190.4.
NP_757345.2. NM_172208.2.
NP_757346.2. NM_172209.2.

UniGene

Hs.370937.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3F8U	X-ray	2.60	B/D	1-401	[»]

ProteinModelPortal

O15533.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15533. 5 interactions.

MINT

MINT-4053688.

PTM databases

PhosphoSite

O15533.

Proteomic databases

PaxDb

O15533.

PRIDE

O15533.

Protocols and materials databases

DNASU

6892.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374572; ENSP00000363700; ENSG00000112493.
ENST00000383065; ENSP00000372542; ENSG00000206208.
ENST00000383066; ENSP00000372543; ENSG00000206208.
ENST00000383197; ENSP00000372684; ENSG00000206281.
ENST00000383198; ENSP00000372685; ENSG00000206281.
ENST00000395114; ENSP00000378546; ENSG00000112493.
ENST00000417059; ENSP00000402087; ENSG00000236490.
ENST00000426633; ENSP00000404833; ENSG00000231925.
ENST00000434618; ENSP00000395701; ENSG00000231925.
ENST00000456807; ENSP00000407195; ENSG00000236490.

GeneID

6892.

KEGG

hsa:6892.

UCSC

uc003odx.2. human.
uc003odz.3. human.
uc010jut.2. human.
uc011drc.2. human.

Organism-specific databases

CTD

6892.

GeneCards

GC06M033267.

H-InvDB

HIX0058157.
HIX0166135.
HIX0166410.

HGNC

HGNC:11566. TAPBP.

HPA

HPA007066.

MIM

601962. gene.

neXtProt

NX_O15533.

Orphanet

34592. Immunodeficiency by defective expression of HLA class 1.

PharmGKB

PA36331.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41000.

HOVERGEN

HBG005156.

KO

K08058.

OrthoDB

EOG469QV7.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

O15533.

Bgee

O15533.

Genevestigator

O15533.

GermOnline

ENSG00000112493. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003597. Ig_C1-set.
IPR008056. Tapasin.
[Graphical view]

PANTHER

PTHR23411. PTHR23411. 1 hit.

Pfam

PF07654. C1-set. 1 hit.
[Graphical view]

PRINTS

PR01669. TAPASIN.

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TAPBP. human.

EvolutionaryTrace

O15533.

GenomeRNAi

6892.

NextBio

26935.

SOURCE

Search...

Entry information

Entry name

TPSN_HUMAN

Accession

Primary (citable) accession number: O15533
Secondary accession number(s): A2AB91 , A2ABC0, B0V003, B0V0A6, B2ZUA4, E9PGM2, O15210, O15272, Q5STJ8, Q5STK6, Q5STQ5, Q5STQ6, Q66K65, Q96KK7, Q9HAN8, Q9UEE0, Q9UEE4, Q9UIZ6, Q9Y6K2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 1, 1998
Last modified:	May 29, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.