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Q03518 (TAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Antigen peptide transporter 1

Short name=APT1
Alternative name(s):
ATP-binding cassette sub-family B member 2
Peptide supply factor 1
Peptide transporter PSF1
Short name=PSF-1
Peptide transporter TAP1
Peptide transporter involved in antigen processing 1
Really interesting new gene 4 protein
Gene names
Name:TAP1
Synonyms:ABCB2, PSF1, RING4, Y3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length808 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-10 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.

Subunit structure

Heterodimer of TAP1 and TAP2. Interacts with Epstein-Barr virus BNLF2a. Interacts with PSMB5 and PSMB8. Ref.18 Ref.19

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Note: The transmembrane segments seem to form a pore in the membrane.

Induction

By IFNG/IFN-gamma. Ref.13

Domain

The peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2.

Polymorphism

There are five common alleles; TAP1*01:01 (PSF1A), TAP1*02:01 (PSF1B), TAP1*03:01 (PSF1C), TAP1*01:04 and TAP1*x. The sequence of TAP1*01:01 is shown here.

Involvement in disease

Bare lymphocyte syndrome 1 (BLS1) [MIM:604571]: A HLA class I deficiency. Contrary to bare lymphocyte syndromes type 2 and type 3, which are characterized by early-onset severe combined immunodeficiency, class I antigen deficiencies are not accompanied by particular pathologic manifestations during the first years of life. Systemic infections have not been described. Chronic bacterial infections, often beginning in the first decade of life, are restricted to the respiratory tract.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Sequence similarities

Belongs to the ABC transporter superfamily. ABCB family. MHC peptide exporter (TC 3.A.1.209) subfamily. [View classification]

Contains 1 ABC transmembrane type-1 domain.

Contains 1 ABC transporter domain.

Caution

It is uncertain whether Met-1 or Met-61 is the initiator.

Sequence caution

The sequence CAA47025.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA60785.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAdaptive immunity
Host-virus interaction
Immunity
Peptide transport
Protein transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I

Inferred from mutant phenotype PubMed 11133832. Source: UniProtKB

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

cytosol to ER transport

Inferred from mutant phenotype PubMed 7538543. Source: UniProtKB

defense response

Inferred from electronic annotation. Source: Ensembl

intracellular transport of viral protein in host cell

Inferred from mutant phenotype PubMed 7538543. Source: UniProtKB

oligopeptide transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

peptide transport

Inferred from mutant phenotype PubMed 11133832PubMed 17418234. Source: UniProtKB

positive regulation of T cell mediated cytotoxicity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentTAP complex

Inferred from direct assay PubMed 11133832PubMed 15518576. Source: UniProtKB

cytosol

Non-traceable author statement PubMed 11133832. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of endoplasmic reticulum membrane

Inferred from direct assay PubMed 11133832PubMed 15577206PubMed 7673167. Source: UniProtKB

integral component of membrane

Inferred from direct assay Ref.12. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionADP binding

Inferred from direct assay Ref.21. Source: UniProtKB

ATP binding

Inferred from direct assay PubMed 11133832PubMed 7673167. Source: UniProtKB

MHC class I protein binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

TAP1 binding

Inferred from sequence or structural similarity. Source: UniProtKB

TAP2 binding

Inferred from physical interaction PubMed 11133832PubMed 1538751PubMed 15518576. Source: UniProtKB

oligopeptide-transporting ATPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

peptide antigen binding

Non-traceable author statement PubMed 11133832. Source: UniProtKB

peptide transporter activity

Inferred from mutant phenotype PubMed 17418234. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

tapasin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 808808Antigen peptide transporter 1
PRO_0000093326

Regions

Topological domain61 – 7515Cytoplasmic Potential
Transmembrane76 – 9621Helical; Name=1; Potential
Topological domain97 – 11317Lumenal Potential
Transmembrane114 – 13623Helical; Name=2; Potential
Topological domain137 – 15216Cytoplasmic Potential
Transmembrane153 – 17321Helical; Name=3; Potential
Topological domain174 – 19320Lumenal Potential
Transmembrane194 – 21421Helical; Name=4; Potential
Topological domain215 – 24632Cytoplasmic Potential
Transmembrane247 – 26721Helical; Name=5; Potential
Topological domain268 – 28720Lumenal Potential
Transmembrane288 – 30821Helical; Name=6; Potential
Topological domain309 – 35850Cytoplasmic Potential
Transmembrane359 – 37921Helical; Name=7; Potential
Topological domain380 – 3889Lumenal Potential
Transmembrane389 – 40921Helical; Name=8; Potential
Topological domain410 – 47869Cytoplasmic Potential
Transmembrane479 – 49921Helical; Name=9; Potential
Topological domain500 – 5034Lumenal Potential
Transmembrane504 – 52421Helical; Name=10; Potential
Topological domain525 – 808284Cytoplasmic Potential
Domain247 – 530284ABC transmembrane type-1
Domain563 – 802240ABC transporter
Nucleotide binding598 – 6058ATP Potential
Region435 – 48046Involved in peptide-binding site
Region513 – 54735Involved in peptide-binding site

Natural variations

Natural variant671P → S. Ref.25
VAR_016801
Natural variant771G → R. Ref.25
Corresponds to variant rs57640466 [ dbSNP | Ensembl ].
VAR_016802
Natural variant1701L → V.
Corresponds to variant rs2228108 [ dbSNP | Ensembl ].
VAR_048137
Natural variant3041V → L.
Corresponds to variant rs36229525 [ dbSNP | Ensembl ].
VAR_060987
Natural variant3461S → F.
Corresponds to variant rs2228111 [ dbSNP | Ensembl ].
VAR_048138
Natural variant3931I → V in allele TAP1*02:01, allele TAP1*03:01, allele TAP1*04:01 and allele TAP1*x. Ref.7 Ref.22 Ref.24 Ref.25
Corresponds to variant rs1057141 [ dbSNP | Ensembl ].
VAR_000092
Natural variant4301A → V in allele TAP1*x. Ref.24 Ref.25
Corresponds to variant rs2127679 [ dbSNP | Ensembl ].
VAR_013151
Natural variant4791G → C. Ref.25
Corresponds to variant rs2228110 [ dbSNP | Ensembl ].
VAR_016803
Natural variant5181V → L in allele TAP1*04:01. Ref.7 Ref.24 Ref.25
Corresponds to variant rs41550019 [ dbSNP | Ensembl ].
VAR_013152
Natural variant5781V → I in allele TAP1*x. Ref.24
Corresponds to variant rs41561219 [ dbSNP | Ensembl ].
VAR_013153
Natural variant6971D → G in allele TAP1*02:01, allele TAP1*04:01 and allele TAP1*x. Ref.7 Ref.9 Ref.22 Ref.24 Ref.25
Corresponds to variant rs1135216 [ dbSNP | Ensembl ].
VAR_000093
Natural variant7081R → Q in allele TAP1*04:01. Ref.7 Ref.9 Ref.24 Ref.25
Corresponds to variant rs1057149 [ dbSNP | Ensembl ].
VAR_013154
Natural variant7191R → Q in a lung cancer cell line deficient in MHC class I presentation. Ref.23
Corresponds to variant rs121917702 [ dbSNP | Ensembl ].
VAR_013173
Natural variant7681Q → R.
Corresponds to variant rs1057149 [ dbSNP | Ensembl ].
VAR_047514

Secondary structure

................................................ 808
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03518 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 9CA5FF96FADD6A1B

FASTA80887,218
        10         20         30         40         50         60 
MAELLASAGS ACSWDFPRAP PSFPPPAASR GGLGGTRSFR PHRGAESPRP GRDRDGVRVP 

        70         80         90        100        110        120 
MASSRCPAPR GCRCLPGASL AWLGTVLLLL ADWVLLRTAL PRIFSLLVPT ALPLLRVWAV 

       130        140        150        160        170        180 
GLSRWAVLWL GACGVLRATV GSKSENAGAQ GWLAALKPLA AALGLALPGL ALFRELISWG 

       190        200        210        220        230        240 
APGSADSTRL LHWGSHPTAF VVSYAAALPA AALWHKLGSL WVPGGQGGSG NPVRRLLGCL 

       250        260        270        280        290        300 
GSETRRLSLF LVLVVLSSLG EMAIPFFTGR LTDWILQDGS ADTFTRNLTL MSILTIASAV 

       310        320        330        340        350        360 
LEFVGDGIYN NTMGHVHSHL QGEVFGAVLR QETEFFQQNQ TGNIMSRVTE DTSTLSDSLS 

       370        380        390        400        410        420 
ENLSLFLWYL VRGLCLLGIM LWGSVSLTMV TLITLPLLFL LPKKVGKWYQ LLEVQVRESL 

       430        440        450        460        470        480 
AKSSQVAIEA LSAMPTVRSF ANEEGEAQKF REKLQEIKTL NQKEAVAYAV NSWTTSISGM 

       490        500        510        520        530        540 
LLKVGILYIG GQLVTSGAVS SGNLVTFVLY QMQFTQAVEV LLSIYPRVQK AVGSSEKIFE 

       550        560        570        580        590        600 
YLDRTPRCPP SGLLTPLHLE GLVQFQDVSF AYPNRPDVLV LQGLTFTLRP GEVTALVGPN 

       610        620        630        640        650        660 
GSGKSTVAAL LQNLYQPTGG QLLLDGKPLP QYEHRYLHRQ VAAVGQEPQV FGRSLQENIA 

       670        680        690        700        710        720 
YGLTQKPTME EITAAAVKSG AHSFISGLPQ GYDTEVDEAG SQLSGGQRQA VALARALIRK 

       730        740        750        760        770        780 
PCVLILDDAT SALDANSQLQ VEQLLYESPE RYSRSVLLIT QHLSLVEQAD HILFLEGGAI 

       790        800 
REGGTHQQLM EKKGCYWAMV QAPADAPE 

« Hide

References

« Hide 'large scale' references
[1]"Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters."
Trowsdale J., Hanson I., Mockridge I., Beck S., Townsend A., Kelly A.
Nature 348:741-744(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing."
Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., Trowsdale J.
J. Mol. Biol. 228:433-441(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Evolutionary dynamics of non-coding sequences within the class II region of the human MHC."
Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L., Trowsdale J.
J. Mol. Biol. 255:1-13(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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].
[5]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].
[6]"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].
Tissue: Uterus.
[7]"TAP1 alleles in insulin-dependent diabetes mellitus: a newly defined centromeric boundary of disease susceptibility."
Jackson D.G., Capra J.D.
Proc. Natl. Acad. Sci. U.S.A. 90:11079-11083(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-808, VARIANTS VAL-393; LEU-518; GLY-697 AND GLN-708.
Tissue: Blood.
[8]"A gene in the human major histocompatibility complex class II region controlling the class I antigen presentation pathway."
Spies T., Bresnahan M., Bahram S., Arnold D., Blanck G., Mellins E., Pious D., Demars R.
Nature 348:744-747(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 183-612.
[9]"New allelic polymorphisms in TAP genes."
Szafer F., Oksenberg J.R., Steinman L.
Immunogenetics 39:374-374(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 691-723, VARIANTS GLY-697 AND GLN-708.
[10]"Two putative subunits of a peptide pump encoded in the human major histocompatibility complex class II region."
Bahram S., Arnold D., Bresnahan M., Strominger J.L., Spies T.
Proc. Natl. Acad. Sci. U.S.A. 88:10094-10098(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47."
Ahn K., Meyer T.H., Uebel S., Sempe P., Djaballah H., Yang Y., Peterson P.A., Frueh K., Tampe R.
EMBO J. 15:3247-3255(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY ICP47.
[12]"Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site."
Nijenhuis M., Hammerling G.J.
J. Immunol. 157:5467-5477(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PEPTIDE-BINDING SITE.
[13]"Downregulation of TAP1 in B lymphocytes by cellular and Epstein-Barr virus-encoded interleukin-10."
Zeidler R., Eissner G., Meissner P., Uebel S., Tampe R., Lazis S., Hammerschmidt W.
Blood 90:2390-2397(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DOWN-REGULATION BY VIRAL IL-10.
[14]"The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide translocation by TAP."
Ahn K., Gruhler A., Galocha B., Jones T.R., Wiertz E.J.H.J., Ploegh H.L., Peterson P.A., Yang Y., Frueh K.
Immunity 6:613-621(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY US6 GLYCOPROTEIN.
[15]"Splice acceptor site mutation of the transporter associated with antigen processing-1 gene in human bare lymphocyte syndrome."
Furukawa H., Murata S., Yabe T., Shimbara N., Keicho N., Kashiwase K., Watanabe K., Ishikawa Y., Akaza T., Tadokoro K., Tohma S., Inoue T., Tokunaga K., Yamamoto K., Tanaka K., Juji T.
J. Clin. Invest. 103:755-758(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BLS1.
[16]"Adenovirus E19 has two mechanisms for affecting class I MHC expression."
Bennett E.M., Bennink J.R., Yewdell J.W., Brodsky F.M.
J. Immunol. 162:5049-5052(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY E3-19K GLYCOPROTEIN.
[17]"The human cytomegalovirus gene product US6 inhibits ATP binding by TAP."
Hewitt E.W., Gupta S.S., Lehner P.J.
EMBO J. 20:387-396(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY US6 GLYCOPROTEIN.
[18]"Cytoplasmic domains of the transporter associated with antigen processing and P-glycoprotein interact with subunits of the proteasome."
Begley G.S., Horvath A.R., Taylor J.C., Higgins C.F.
Mol. Immunol. 42:137-141(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMB5 AND PSMB8.
[19]"Specific targeting of the EBV lytic phase protein BNLF2a to the transporter associated with antigen processing results in impairment of HLA class I-restricted antigen presentation."
Horst D., van Leeuwen D., Croft N.P., Garstka M.A., Hislop A.D., Kremmer E., Rickinson A.B., Wiertz E.J.H.J., Ressing M.E.
J. Immunol. 182:2313-2324(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBV BNLF2A.
[20]"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].
[21]"Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing."
Gaudet R., Wiley D.C.
EMBO J. 20:4964-4972(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 549-808.
[22]"Allelic variants of the human putative peptide transporter involved in antigen processing."
Colonna M., Bresnahan M., Bahram S., Strominger J.L., Spies T.
Proc. Natl. Acad. Sci. U.S.A. 89:3932-3936(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-393 AND GLY-697.
[23]"A functionally defective allele of TAP1 results in loss of MHC class I antigen presentation in a human lung cancer."
Chen H.L., Gabrilovich D., Tampe R., Girgis K.R., Nadaf S., Carbone D.P.
Nat. Genet. 13:210-213(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-719.
[24]"TAP1 polymorphisms in several human ethnic groups: characteristics, evolution, and genotyping strategies."
Tang J., Freedman D.O., Allen S., Karita E., Musonda R., Braga C., Margolick J., Kaslow R.A.
Hum. Immunol. 62:256-268(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-393; VAL-430; LEU-518; ILE-578; GLY-697 AND GLN-708.
[25]"Novel TAP1 polymorphisms in indigenous Zimbabweans: their potential implications on TAP function and in human diseases."
Lajoie J., Zijenah L.S., Faucher M.C., Ward B.J., Roger M.
Hum. Immunol. 64:823-829(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-67; ARG-77; VAL-393; VAL-430; CYS-479; LEU-518; GLY-697 AND GLN-708.
+Additional computationally mapped references.

Web resources

TAP1base

TAP1 mutation db

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57522 mRNA. Translation: CAA40741.1.
X66401 Genomic DNA. Translation: CAA47025.1. Different initiation.
X87344 Genomic DNA. Translation: CAA60785.1. Different initiation.
AL669918 Genomic DNA. Translation: CAI18140.1.
AL671681 Genomic DNA. Translation: CAI17714.1.
AL935043 Genomic DNA. Translation: CAI18626.1.
BX927138 Genomic DNA. Translation: CAQ08449.1.
CR762476 Genomic DNA. Translation: CAQ08495.1.
CR933844 Genomic DNA. Translation: CAQ08906.1.
CR753889 Genomic DNA. Translation: CAQ10287.1.
CH471081 Genomic DNA. Translation: EAX03647.1.
BC014081 mRNA. Translation: AAH14081.1.
L21204 mRNA. Translation: AAC12902.1.
L21205 mRNA. Translation: AAC12903.1.
L21206 mRNA. Translation: AAC12904.1.
L21207 mRNA. Translation: AAC12905.1.
L21208 mRNA. Translation: AAC12906.1.
X57521 mRNA. Translation: CAA40740.1.
S70274 mRNA. Translation: AAD14056.1.
PIRA41538. S13427.
RefSeqNP_000584.2. NM_000593.5.
UniGeneHs.352018.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JJ7X-ray2.40A549-808[»]
ProteinModelPortalQ03518.
SMRQ03518. Positions 234-802.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112753. 24 interactions.
DIPDIP-35626N.
IntActQ03518. 17 interactions.
MINTMINT-1477433.
STRING9606.ENSP00000346206.

Protein family/group databases

TCDB3.A.1.209.1. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteQ03518.

Polymorphism databases

DMDM215273957.

Proteomic databases

PaxDbQ03518.
PRIDEQ03518.

Protocols and materials databases

DNASU6890.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354258; ENSP00000346206; ENSG00000168394.
ENST00000383235; ENSP00000372722; ENSG00000206297.
ENST00000414467; ENSP00000405356; ENSG00000226173.
ENST00000418205; ENSP00000401149; ENSG00000227816.
ENST00000424897; ENSP00000413080; ENSG00000230705.
ENST00000439781; ENSP00000415660; ENSG00000224212.
ENST00000440894; ENSP00000402316; ENSG00000232367.
GeneID6890.
KEGGhsa:6890.
UCSCuc003ocg.3. human.

Organism-specific databases

CTD6890.
GeneCardsGC06M032812.
GC06Mi32796.
GC06Mj32735.
GC06Mk32790.
GC06Ml32966.
GC06Mm32846.
GC06Mn32741.
HGNCHGNC:43. TAP1.
HPACAB009516.
MIM170260. gene.
604571. phenotype.
neXtProtNX_Q03518.
Orphanet34592. Immunodeficiency by defective expression of HLA class 1.
PharmGKBPA35021.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1132.
HOVERGENHBG008358.
InParanoidQ03518.
KOK05653.
OMACLGSEIR.
PhylomeDBQ03518.
TreeFamTF105197.

Enzyme and pathway databases

BRENDA3.6.3.43. 2681.
ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ03518.
BgeeQ03518.
CleanExHS_TAP1.
GenevestigatorQ03518.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR013305. ABC_B2.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR005293. Ag_transporter2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
PRINTSPR01896. TAP1PROTEIN.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsTIGR00958. 3a01208. 1 hit.
PROSITEPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ03518.
GeneWikiTAP1.
GenomeRNAi6890.
NextBio26925.
PROQ03518.
SOURCESearch...

Entry information

Entry nameTAP1_HUMAN
AccessionPrimary (citable) accession number: Q03518
Secondary accession number(s): Q16149, Q96CP4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 154 of the entry and version 2 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