Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O15533 (TPSN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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, calreticulin, 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-terminal 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 componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processamide transport

Traceable author statement Ref.1. Source: GOC

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

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

immune response

Traceable author statement Ref.2. Source: ProtInc

peptide antigen stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

peptide transport

Traceable author statement Ref.1. Source: GOC

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_componentGolgi membrane

Inferred from direct assay PubMed 11884415. Source: UniProtKB

MHC class I peptide loading complex

Non-traceable author statement PubMed 12788224. Source: UniProtKB

endoplasmic reticulum

Traceable author statement Ref.1Ref.2. Source: ProtInc

endoplasmic reticulum membrane

Inferred from direct assay PubMed 11884415. Source: UniProtKB

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionMHC class I protein binding

Traceable author statement PubMed 12788224. Source: UniProtKB

TAP1 binding

Inferred from physical interaction PubMed 12047747. Source: UniProtKB

TAP2 binding

Inferred from physical interaction PubMed 12047747. Source: UniProtKB

peptide antigen binding

Traceable author statement PubMed 12788224. Source: UniProtKB

peptide antigen-transporting ATPase activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 12213826PubMed 17055437PubMed 19201886. Source: IntAct

unfolded protein binding

Traceable author statement PubMed 12788224. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BNLF2aP0C7395EBI-874801,EBI-9346744From a different organism.
TAP1Q0351812EBI-874801,EBI-747259
TAP2Q035198EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 448428Tapasin
PRO_0000014990

Regions

Topological domain21 – 414394Lumenal Potential
Transmembrane415 – 43521Helical; Potential
Topological domain436 – 44813Cytoplasmic Potential
Domain292 – 399108Ig-like C1-type

Sites

Site4281May be involved in interaction with TAP

Amino acid modifications

Glycosylation2531N-linked (GlcNAc...) Ref.14 Ref.16
Disulfide bond27 ↔ 91 Ref.16
Disulfide bond115Interchain (with C-57 in PDIA3) Ref.16
Disulfide bond315 ↔ 382 Ref.16

Natural variations

Alternative sequence70 – 15687Missing in isoform 4.
VSP_044455
Alternative sequence405 – 44844LSGPS…KKKAE → KSWELCGI in isoform 2.
VSP_002577
Alternative sequence446 – 4483KAE → VQCSTSLYLSLVTLSPHPIS KPMEGGCWCGRQNLGLEFTL IWVKTWHYILTVGLFEHAT in isoform 3.
VSP_017055
Natural variant2601R → T in allele TAPBP*02. Ref.5 Ref.9 Ref.10
Corresponds to variant rs2071888 [ dbSNP | Ensembl ].
VAR_010253

Experimental info

Sequence conflict2741H → Y in AAH80574. Ref.11
Sequence conflict2961L → P in ACD68200. Ref.8
Sequence conflict4121D → N in AAD32924. Ref.7

Secondary structure

............................................................ 448
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7340549519B288AD

FASTA44847,626
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E50E3F41AD7E7EA8
Show »

FASTA41243,885
Isoform 3 [UniParc].

Checksum: BEF063064284DE16
Show »

FASTA50453,943
Isoform 4 (tpsnDeltaEx3) [UniParc].

Checksum: E049AA2C6F0B4DED
Show »

FASTA36138,365

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
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.
CCDSCCDS34426.1. [O15533-1]
CCDS34427.2. [O15533-4]
CCDS34428.2. [O15533-3]
RefSeqNP_003181.3. NM_003190.4.
NP_757345.2. NM_172208.2.
NP_757346.2. NM_172209.2.
UniGeneHs.370937.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3F8UX-ray2.60B/D1-401[»]
ProteinModelPortalO15533.
SMRO15533. Positions 21-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112755. 12 interactions.
IntActO15533. 7 interactions.
MINTMINT-4053688.

PTM databases

PhosphoSiteO15533.

Proteomic databases

MaxQBO15533.
PaxDbO15533.
PRIDEO15533.

Protocols and materials databases

DNASU6892.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374572; ENSP00000363700; ENSG00000112493. [O15533-1]
ENST00000383066; ENSP00000372543; ENSG00000206208.
ENST00000383197; ENSP00000372684; ENSG00000206281. [O15533-3]
ENST00000383198; ENSP00000372685; ENSG00000206281. [O15533-1]
ENST00000395114; ENSP00000378546; ENSG00000112493. [O15533-3]
ENST00000417059; ENSP00000402087; ENSG00000236490. [O15533-1]
ENST00000434618; ENSP00000395701; ENSG00000231925.
ENST00000456807; ENSP00000407195; ENSG00000236490. [O15533-3]
GeneID6892.
KEGGhsa:6892.
UCSCuc003odx.2. human. [O15533-1]
uc003odz.3. human. [O15533-3]
uc010jut.2. human. [O15533-4]
uc011drc.2. human. [O15533-2]

Organism-specific databases

CTD6892.
GeneCardsGC06M033267.
GC06Mj33189.
GC06Mk33245.
GC06Mm33437.
GC06Mn33196.
H-InvDBHIX0058157.
HIX0166135.
HIX0166410.
HGNCHGNC:11566. TAPBP.
HPAHPA007066.
MIM601962. gene.
neXtProtNX_O15533.
Orphanet34592. Immunodeficiency by defective expression of HLA class 1.
PharmGKBPA36331.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41000.
HOVERGENHBG005156.
KOK08058.
OMAYLATVHL.
PhylomeDBO15533.
TreeFamTF334274.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO15533.
BgeeO15533.
GenevestigatorO15533.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003597. Ig_C1-set.
IPR008056. Tapasin.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
[Graphical view]
PRINTSPR01669. TAPASIN.
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTAPBP. human.
EvolutionaryTraceO15533.
GeneWikiTapasin.
GenomeRNAi6892.
NextBio26935.
PROO15533.
SOURCESearch...

Entry information

Entry nameTPSN_HUMAN
AccessionPrimary (citable) accession number: O15533
Secondary accession number(s): A2AB91 expand/collapse secondary AC list , 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: July 9, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM