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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.12
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.11
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 Phosphoprotein
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 immune response Traceable author statement. Source: ProtInc peptide antigen stabilization Inferred from sequence or structural similarity. Source: UniProtKB protein complex assembly Traceable author statement. Source: ProtInc retrograde vesicle-mediated transport, Golgi to ER Non-traceable author statement. Source: UniProtKB
Cellular component	Golgi membrane Inferred from direct assay. Source: UniProtKB MHC class I peptide loading complex Non-traceable author statement. Source: UniProtKB integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome microsome Non-traceable author statement. Source: UniProtKB
Molecular function	MHC class I protein binding Traceable author statement. Source: UniProtKB TAP1 binding Inferred from physical interaction. Source: UniProtKB TAP2 binding Inferred from physical interaction. Source: UniProtKB peptide antigen binding Traceable author statement. Source: UniProtKB peptide antigen-transporting ATPase activity Traceable author statement. Source: ProtInc unfolded protein binding Traceable author statement. 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 3 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.

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

Modified residue

3

1

Phosphoserine Ref.13

Modified residue

5

1

Phosphoserine Ref.13

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

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.8 Ref.9
Corresponds to variant rs2071888 [ dbSNP | Ensembl ].

VAR_010253

Experimental info

Sequence conflict

274

1

H → Y in AAH80574. Ref.10

Sequence conflict

412

1

D → N in AAD32924. Ref.7

Secondary structure

1

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448

Helix Strand Turn

Details...

Beta strand

66 – 69

4

Helix

75 – 81

7

Beta strand

90 – 96

7

Helix

104 – 106

3

Beta strand

112 – 114

3

Helix

117 – 119

3

Beta strand

123 – 129

7

Beta strand

134 – 141

8

Beta strand

153 – 164

12

Beta strand

169 – 171

3

Beta strand

176 – 178

3

Beta strand

181 – 184

4

Beta strand

205 – 208

4

Beta strand

216 – 219

4

Beta strand

256 – 258

3

Helix

263 – 265

3

Beta strand

269 – 272

4

Beta strand

282 – 284

3

Beta strand

287 – 290

4

Beta strand

293 – 300

8

Beta strand

313 – 321

9

Beta strand

327 – 333

7

Beta strand

360 – 362

3

Helix

373 – 375

3

Beta strand

379 – 385

7

Beta strand

395 – 399

5

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

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: 9238042] [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: 9271576] [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: 9521053] [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: 9545376] [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: 9802609] [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: 10088603] [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: 14668790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: B-cell.
[8]	"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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-260.
[9]	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.
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Prostate.
[11]	"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: 10382748] [Abstract] Cited for: MUTAGENESIS, DOMAIN CHARACTERIZATION.
[12]	"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: 10636848] [Abstract] Cited for: FUNCTION.
[13]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-5, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 19159218] [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: 21269460] [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: 19119025] [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.
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.

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.

SMR

O15533. Positions 21-401.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15533. 5 interactions.

MINT

MINT-4053688.

STRING

O15533.

PTM databases

PhosphoSite

O15533.

Proteomic databases

PRIDE

O15533.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374572; ENSP00000363700; ENSG00000112493.
ENST00000383198; ENSP00000372685; ENSG00000206281.
ENST00000417059; ENSP00000402087; ENSG00000236490.

GeneID

6892.

KEGG

hsa:6892.

UCSC

uc003oea.1. human.
uc003rqh.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.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG005156.

OrthoDB

EOG469QV7.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

Genevestigator

O15533.

GermOnline

ENSG00000112493. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

KO

K08058.

PANTHER

PTHR23411. Tapasin. 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

NextBio

26935.

SOURCE

Search...

Entry information

Entry name

TPSN_HUMAN

Accession

Primary (citable) accession number: O15533
Secondary accession number(s): A2AB91 , A2ABC0, B0V003, B0V0A6, 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:	January 25, 2012
This is version 120 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.