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Antigen peptide transporter 2 (APT2) (ATP-binding cassette sub-family B member 3) (Peptide supply factor 2) (Peptide transporter PSF2) (PSF-2) (Peptide transporter TAP2) (Peptide transporter involved in antigen processing 2) (Really interesting new gene 11 protein)

 TAP2_HUMAN              Reviewed;         686 AA.
Q03519; B0V2J8; O95410; Q53FI6; Q5HY71; Q96PT8; Q9UQ83;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-OCT-2017, entry version 193.
RecName: Full=Antigen peptide transporter 2;
Short=APT2;
AltName: Full=ATP-binding cassette sub-family B member 3;
AltName: Full=Peptide supply factor 2;
AltName: Full=Peptide transporter PSF2;
Short=PSF-2;
AltName: Full=Peptide transporter TAP2;
AltName: Full=Peptide transporter involved in antigen processing 2;
AltName: Full=Really interesting new gene 11 protein;
Name=TAP2; Synonyms=ABCB3, PSF2, RING11, Y1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE TAP2*01:01) (ISOFORM 1), AND
POLYMORPHISM.
PubMed=1453454; DOI=10.1016/0022-2836(92)90832-5;
Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P.,
Trowsdale J.;
"DNA sequence analysis of 66 kb of the human MHC class II region
encoding a cluster of genes for antigen processing.";
J. Mol. Biol. 228:433-441(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE TAP2*01:01/TAP2*02:01) (ISOFORM 1),
AND POLYMORPHISM.
PubMed=1741401; DOI=10.1073/pnas.89.4.1463;
Powis S.H., Mockridge I., Kelly A., Kerr L.-A., Glynne R.J.,
Gileadi U., Beck S., Trowsdale J.;
"Polymorphism in a second ABC transporter gene located within the
class II region of the human major histocompatibility complex.";
Proc. Natl. Acad. Sci. U.S.A. 89:1463-1467(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE TAP2*02:01) (ISOFORM 1), AND
POLYMORPHISM.
PubMed=1946428; DOI=10.1073/pnas.88.22.10094;
Bahram S., Arnold D., Bresnahan M., Strominger J.L., Spies T.;
"Two putative subunits of a peptide pump encoded in the human major
histocompatibility complex class II region.";
Proc. Natl. Acad. Sci. U.S.A. 88:10094-10098(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE TAP2*01:02) (ISOFORM 1), AND
POLYMORPHISM.
PubMed=8428770; DOI=10.1007/BF00216802;
Powis S.H., Tonks S., Mockridge I., Kelly A.P., Bodmer J.G.,
Trowsdale J.;
"Alleles and haplotypes of the MHC-encoded ABC transporters TAP1 and
TAP2.";
Immunogenetics 37:373-380(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE TAP2*BKY2) (ISOFORM 1), VARIANT
TAP2*BKY2 VAL-577, AND POLYMORPHISM.
TISSUE=Blood;
PubMed=9324024; DOI=10.1002/art.1780400919;
Kumagai S., Kanagawa S., Morinobu A., Takada M., Nakamura K.,
Sugai S., Maruya E., Saji H.;
"Association of a new allele of the TAP2 gene, TAP2*Bky2 (Val577),
with susceptibility to Sjogren's syndrome.";
Arthritis Rheum. 40:1685-1692(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ILE-379.
TISSUE=Spleen;
PubMed=9916708;
Yan G., Shi L., Faustman D.;
"Novel splicing of the human MHC-encoded peptide transporter confers
unique properties.";
J. Immunol. 162:852-859(1999).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE TAP2*01:01) (ISOFORM 1), AND
POLYMORPHISM.
PubMed=8568858; DOI=10.1006/jmbi.1996.0001;
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.;
"Evolutionary dynamics of non-coding sequences within the class II
region of the human MHC.";
J. Mol. Biol. 255:1-13(1996).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE TAP2*BKY2) (ISOFORM 1).
TISSUE=Liver, and Synovium;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES TAP2*03A AND
TAP2*BKY2).
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 65-686 (ALLELE TAP2*01:03) (ISOFORM 1).
TISSUE=Blood;
PubMed=7792761; DOI=10.1111/j.1399-0039.1995.tb02431.x;
Cano P., Baxter-Lowe L.A.;
"Novel human TAP2*103 allele shows further polymorphism in the ATP-
binding domain.";
Tissue Antigens 45:139-142(1995).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-686 (ISOFORM 1), AND VARIANTS
THR-374 AND ILE-467.
PubMed=9672156; DOI=10.1111/j.1399-0039.1998.tb02992.x;
Tang J., Allen S., Karita E., Musonda R., Kaslow R.A.;
"New TAP2 polymorphisms in Africans.";
Tissue Antigens 51:556-562(1998).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 517-645 (ALLELE TAP2*01:01/TAP2*01:02)
(ISOFORM 1).
Singal D.P., Ye M., D'Souza M.;
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 517-645 (ALLELE TAP2*01:01/TAP2*01:02)
(ISOFORM 1).
PubMed=8162639;
Singal D.P., Ye M., Qiu X., D'Souza M.;
"Polymorphisms in the TAP2 gene and their association with rheumatoid
arthritis.";
Clin. Exp. Rheumatol. 12:29-33(1994).
[15]
INTERACTION WITH HERPES SIMPLEX VIRUS ICP47.
PubMed=7760936; DOI=10.1038/375415a0;
Frueh K., Ahn K., Djaballah H., Sempe P., van Endert P.M., Tampe R.,
Peterson P.A., Yang Y.;
"A viral inhibitor of peptide transporters for antigen presentation.";
Nature 375:415-418(1995).
[16]
PEPTIDE-BINDING SITE.
PubMed=8955196;
Nijenhuis M., Hammerling G.J.;
"Multiple regions of the transporter associated with antigen
processing (TAP) contribute to its peptide binding site.";
J. Immunol. 157:5467-5477(1996).
[17]
INHIBITION BY ICP47.
PubMed=8670825;
Ahn K., Meyer T.H., Uebel S., Sempe P., Djaballah H., Yang Y.,
Peterson P.A., Frueh K., Tampe R.;
"Molecular mechanism and species specificity of TAP inhibition by
herpes simplex virus ICP47.";
EMBO J. 15:3247-3255(1996).
[18]
INHIBITION BY US6 GLYCOPROTEIN.
PubMed=9175839; DOI=10.1016/S1074-7613(00)80349-0;
Ahn K., Gruhler A., Galocha B., Jones T.R., Wiertz E.J.H.J.,
Ploegh H.L., Peterson P.A., Yang Y., Frueh K.;
"The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide
translocation by TAP.";
Immunity 6:613-621(1997).
[19]
INHIBITION BY US6 GLYCOPROTEIN.
PubMed=11157746; DOI=10.1093/emboj/20.3.387;
Hewitt E.W., Gupta S.S., Lehner P.J.;
"The human cytomegalovirus gene product US6 inhibits ATP binding by
TAP.";
EMBO J. 20:387-396(2001).
[20]
INHIBITION BY E3-19K GLYCOPROTEIN.
PubMed=10227971;
Bennett E.M., Bennink J.R., Yewdell J.W., Brodsky F.M.;
"Adenovirus E19 has two mechanisms for affecting class I MHC
expression.";
J. Immunol. 162:5049-5052(1999).
[21]
INTERACTION WITH EBV BNLF2A.
PubMed=19201886; DOI=10.4049/jimmunol.0803218;
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.;
"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.";
J. Immunol. 182:2313-2324(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
VARIANTS ILE-379 AND ALA-665.
PubMed=1570316; DOI=10.1073/pnas.89.9.3932;
Colonna M., Bresnahan M., Bahram S., Strominger J.L., Spies T.;
"Allelic variants of the human putative peptide transporter involved
in antigen processing.";
Proc. Natl. Acad. Sci. U.S.A. 89:3932-3936(1992).
[24]
INVOLVEMENT IN BLS1.
PubMed=7517574; DOI=10.1126/science.7517574;
de la Salle H., Hanau D., Fricker D., Urlacher A., Kelly A.,
Salamero J., Powis S.H., Donato L., Bausinger H., Laforet M.,
Jeras M., Spehner D., Bieber T., Falkenrodt A., Cazenave J.-P.,
Trowsdale J., Tongio M.-M.;
"Homozygous human TAP peptide transporter mutation in HLA class I
deficiency.";
Science 265:237-241(1994).
[25]
VARIANTS THR-374; ILE-379; ILE-467; SER-513 THR-565; CYS-651; ALA-665
AND GLN-GLU-GLY-GLN-ASP-LEU-TYR-SER-ARG-LEU-VAL-GLN-GLN-ARG-LEU-MET-
ASP-686 INS, AND POLYMORPHISM.
PubMed=11294565; DOI=10.1038/sj.gene.6363731;
Tang J., Freedman D.O., Allen S., Karita E., Musonda R., Braga C.,
Jamieson B.D., Louie L., Kaslow R.A.;
"Genotyping TAP2 variants in North American Caucasians, Brazilians,
and Africans.";
Genes Immun. 2:32-40(2001).
-!- 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.
-!- SUBUNIT: Heterodimer of TAP1 and TAP2. Interacts with Epstein-Barr
virus BLNF2a. Interacts with herpes simplex virus ICP47
(PubMed:7760936). {ECO:0000269|PubMed:19201886,
ECO:0000269|PubMed:7760936}.
-!- INTERACTION:
P0C739:BNLF2a (xeno); NbExp=6; IntAct=EBI-780781, EBI-9346744;
Q77CE4:gN (xeno); NbExp=2; IntAct=EBI-780781, EBI-11303846;
Q03518:TAP1; NbExp=17; IntAct=EBI-780781, EBI-747259;
O15533:TAPBP; NbExp=8; IntAct=EBI-780781, EBI-874801;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein. Note=The transmembrane segments seem to form a
pore in the membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q03519-1; Sequence=Displayed;
Name=2;
IsoId=Q03519-2; Sequence=VSP_038904;
-!- INDUCTION: By IFNG/IFN-gamma.
-!- DOMAIN: The peptide-binding site is shared between the cytoplasmic
loops of TAP1 and TAP2.
-!- POLYMORPHISM: 4 common alleles are officially recognized:
TAP2*01:01 (TAP2A or PSF2A or RING11A), TAP2*01:02 (TAP2E),
TAP2*01:03 (TAP2F), and TAP2*02:01 (TAP2B or PSF2B or RING11B).
Other relatively common alleles have been identified: TAP2*01D,
TAP2*01E, TAP2*01F, TAP2*01G, TAP2*01H, TAP2*02B, TAP2*02C
(TAP2*02:02), TAP2*02D, TAP2*02E, TAP2*02F, TAP2*03A and TAP2*04A.
The sequence shown is that of TAP2*01:01.
{ECO:0000269|PubMed:11294565, ECO:0000269|PubMed:1453454,
ECO:0000269|PubMed:1741401, ECO:0000269|PubMed:1946428,
ECO:0000269|PubMed:8428770, ECO:0000269|PubMed:8568858}.
-!- POLYMORPHISM: The allele TAP2*Bky2 is commonly found only in the
Japanese population. It may be associated with susceptibility to
Sjoegren syndrome, an autoimmune disorder characterized by
abnormal dryness of the conjunctiva, cornea and mouth due to
exocrine glands dysfunction. {ECO:0000269|PubMed:9324024}.
-!- 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.
{ECO:0000269|PubMed:7517574}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. MHC peptide exporter (TC 3.A.1.209) subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=TAP2base; Note=TAP2 mutation db;
URL="http://structure.bmc.lu.se/idbase/TAP2base/";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q03519";
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EMBL; X66401; CAA47027.1; -; Genomic_DNA.
EMBL; M84748; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M74447; AAA59841.1; -; mRNA.
EMBL; Z22935; CAA80522.1; -; mRNA.
EMBL; Z22936; CAA80523.1; -; mRNA.
EMBL; AB073779; BAB71769.1; -; mRNA.
EMBL; AF105151; AAD12059.1; -; mRNA.
EMBL; X87344; CAA60788.1; -; Genomic_DNA.
EMBL; AK222823; BAD96543.1; -; mRNA.
EMBL; AK223300; BAD97020.1; -; mRNA.
EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR788227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX682530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR762476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR753889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CT009502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002751; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U07844; AAA79901.1; -; mRNA.
EMBL; AH007554; AAD23381.1; -; Genomic_DNA.
EMBL; L09191; AAA58648.1; -; mRNA.
EMBL; L10287; AAA58649.1; -; mRNA.
CCDS; CCDS4755.1; -. [Q03519-2]
CCDS; CCDS78129.1; -. [Q03519-1]
PIR; B41538; B41538.
RefSeq; NP_000535.3; NM_000544.3.
RefSeq; NP_001276972.1; NM_001290043.1. [Q03519-1]
RefSeq; NP_061313.2; NM_018833.2. [Q03519-2]
UniGene; Hs.502; -.
PDB; 5U1D; EM; 3.97 A; B=1-686.
PDBsum; 5U1D; -.
ProteinModelPortal; Q03519; -.
SMR; Q03519; -.
BioGrid; 112754; 35.
DIP; DIP-322N; -.
IntAct; Q03519; 23.
MINT; MINT-2838244; -.
STRING; 9606.ENSP00000364034; -.
TCDB; 3.A.1.209.1; the atp-binding cassette (abc) superfamily.
iPTMnet; Q03519; -.
PhosphoSitePlus; Q03519; -.
BioMuta; TAP2; -.
DMDM; 549044; -.
EPD; Q03519; -.
PaxDb; Q03519; -.
PeptideAtlas; Q03519; -.
PRIDE; Q03519; -.
TopDownProteomics; Q03519-2; -. [Q03519-2]
DNASU; 6891; -.
Ensembl; ENST00000374897; ENSP00000364032; ENSG00000204267. [Q03519-1]
Ensembl; ENST00000374899; ENSP00000364034; ENSG00000204267. [Q03519-2]
Ensembl; ENST00000383118; ENSP00000372599; ENSG00000206235. [Q03519-1]
Ensembl; ENST00000383119; ENSP00000372600; ENSG00000206235. [Q03519-2]
Ensembl; ENST00000383239; ENSP00000372726; ENSG00000206299. [Q03519-1]
Ensembl; ENST00000383240; ENSP00000372727; ENSG00000206299. [Q03519-2]
Ensembl; ENST00000414145; ENSP00000401377; ENSG00000228582. [Q03519-2]
Ensembl; ENST00000419142; ENSP00000390013; ENSG00000237599.
Ensembl; ENST00000426977; ENSP00000387553; ENSG00000232326. [Q03519-2]
Ensembl; ENST00000439425; ENSP00000396156; ENSG00000225967. [Q03519-2]
Ensembl; ENST00000443713; ENSP00000394101; ENSG00000228582. [Q03519-1]
Ensembl; ENST00000451907; ENSP00000392172; ENSG00000223481. [Q03519-2]
GeneID; 6891; -.
KEGG; hsa:6891; -.
UCSC; uc063yci.1; human. [Q03519-1]
CTD; 6891; -.
DisGeNET; 6891; -.
EuPathDB; HostDB:ENSG00000204267.13; -.
GeneCards; TAP2; -.
H-InvDB; HIX0005757; -.
H-InvDB; HIX0166631; -.
H-InvDB; HIX0166883; -.
H-InvDB; HIX0167147; -.
HGNC; HGNC:44; TAP2.
HPA; HPA001312; -.
MalaCards; TAP2; -.
MIM; 170261; gene.
MIM; 604571; phenotype.
neXtProt; NX_Q03519; -.
OpenTargets; ENSG00000204267; -.
Orphanet; 34592; Immunodeficiency by defective expression of HLA class 1.
PharmGKB; PA35022; -.
eggNOG; KOG0058; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00550000074497; -.
HOVERGEN; HBG008358; -.
InParanoid; Q03519; -.
KO; K05654; -.
PhylomeDB; Q03519; -.
TreeFam; TF105197; -.
BRENDA; 3.6.3.43; 2681.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
GeneWiki; TAP2; -.
GenomeRNAi; 6891; -.
PRO; PR:Q03519; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204267; -.
CleanEx; HS_TAP2; -.
ExpressionAtlas; Q03519; baseline and differential.
Genevisible; Q03519; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0042825; C:TAP complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0023029; F:MHC class Ib protein binding; IPI:UniProtKB.
GO; GO:0015433; F:peptide antigen-transporting ATPase activity; IMP:UniProtKB.
GO; GO:0046978; F:TAP1 binding; IPI:UniProtKB.
GO; GO:0046980; F:tapasin binding; ISS:UniProtKB.
GO; GO:0005215; F:transporter activity; IDA:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IDA:UniProtKB.
GO; GO:0002489; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent; IMP:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0046967; P:cytosol to ER transport; IMP:UniProtKB.
GO; GO:0046968; P:peptide antigen transport; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:1990668; P:vesicle fusion with endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.20.1560.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR013305; ABC_Tap-like.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005293; Tap2/ABCB3.
Pfam; PF00664; ABC_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
PRINTS; PR01897; TAP2PROTEIN.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF90123; SSF90123; 1.
TIGRFAMs; TIGR00958; 3a01208; 1.
PROSITE; PS50929; ABC_TM1F; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
Complete proteome; Endoplasmic reticulum; Host-virus interaction;
Immunity; Membrane; Nucleotide-binding; Peptide transport;
Polymorphism; Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 686 Antigen peptide transporter 2.
/FTId=PRO_0000093329.
TOPO_DOM 1 6 Lumenal. {ECO:0000255}.
TRANSMEM 7 27 Helical; Name=1. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 28 56 Cytoplasmic. {ECO:0000255}.
TRANSMEM 57 77 Helical; Name=2. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 78 98 Lumenal. {ECO:0000255}.
TRANSMEM 99 119 Helical; Name=3. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 120 148 Cytoplasmic. {ECO:0000255}.
TRANSMEM 149 169 Helical; Name=4. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 170 187 Lumenal. {ECO:0000255}.
TRANSMEM 188 208 Helical; Name=5. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 209 266 Cytoplasmic. {ECO:0000255}.
TRANSMEM 267 287 Helical; Name=6. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 288 293 Lumenal. {ECO:0000255}.
TRANSMEM 294 314 Helical; Name=7. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 315 374 Cytoplasmic. {ECO:0000255}.
TRANSMEM 375 395 Helical; Name=8. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 396 408 Lumenal. {ECO:0000255}.
TRANSMEM 409 429 Helical; Name=9. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 430 686 Cytoplasmic. {ECO:0000255}.
DOMAIN 152 435 ABC transmembrane type-1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 468 686 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 503 510 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 301 389 Involved in peptide-binding site.
REGION 414 433 Involved in peptide-binding site.
VAR_SEQ 645 686 LQDWNSRGDRTVLVIAHRLQTVQRAHQILVLQEGKLQKLAQ
L -> KTLWKFMIF (in isoform 2).
{ECO:0000303|PubMed:9916708}.
/FTId=VSP_038904.
VARIANT 56 56 R -> K (in dbSNP:rs17220192).
/FTId=VAR_036873.
VARIANT 374 374 A -> T (in allele TAP2*01F, allele
TAP2*01G, allele TAP2*01H, allele
TAP2*02B and allele TAP2*02D;
dbSNP:rs111303994).
{ECO:0000269|PubMed:11294565,
ECO:0000269|PubMed:9672156}.
/FTId=VAR_014997.
VARIANT 379 379 V -> I (in allele TAP2*01D, allele
TAP2*01E, allele TAP2*01G, allele
TAP2*02C and allele TAP2*02F;
dbSNP:rs1800454).
{ECO:0000269|PubMed:11294565,
ECO:0000269|PubMed:1570316,
ECO:0000269|PubMed:9916708}.
/FTId=VAR_000094.
VARIANT 467 467 V -> I (in allele TAP2*01F and allele
TAP2*02D; dbSNP:rs150253319).
{ECO:0000269|PubMed:11294565,
ECO:0000269|PubMed:9672156}.
/FTId=VAR_014998.
VARIANT 513 513 A -> S (rare polymorphism).
/FTId=VAR_014999.
VARIANT 565 565 A -> T (in allele TAP2*01:02, allele
TAP2*01D, allele TAP2*02E and allele
TAP2*02F; dbSNP:rs2228396).
{ECO:0000269|PubMed:11294565}.
/FTId=VAR_000095.
VARIANT 577 577 M -> V (in allele TAP2*BKY2;
dbSNP:rs2228391).
{ECO:0000269|PubMed:9324024}.
/FTId=VAR_015000.
VARIANT 651 651 R -> C (in allele TAP2*01:03 and allele
TAP2*01G; dbSNP:rs4148876).
{ECO:0000269|PubMed:11294565}.
/FTId=VAR_000096.
VARIANT 665 665 T -> A (in allele TAP2*02:01, allele
TAP2*02B, allele TAP2*02C, allele
TAP2*02D, allele TAP2*02E, allele
TAP2*02F, allele TAP2*04A and allele
TAP2*Bky2; dbSNP:rs241447).
{ECO:0000269|PubMed:11294565,
ECO:0000269|PubMed:1570316}.
/FTId=VAR_000097.
VARIANT 686 686 L -> LQEGQDLYSRLVQQRLMD (in allele
TAP2*02:01, allele TAP2*02B, allele
TAP2*02C, allele TAP2*02D, allele
TAP2*02E, allele TAP2*02F, allele
TAP2*03A and allele TAP2*BKY2).
/FTId=VAR_000098.
CONFLICT 345 345 F -> I (in Ref. 8; BAD97020).
{ECO:0000305}.
CONFLICT 520 520 Y -> N (in Ref. 8; BAD97020).
{ECO:0000305}.
CONFLICT 655 655 T -> A (in Ref. 8; BAD97020).
{ECO:0000305}.
SEQUENCE 686 AA; 75664 MW; E7E4A7F6A2A3B48B CRC64;
MRLPDLRPWT SLLLVDAALL WLLQGPLGTL LPQGLPGLWL EGTLRLGGLW GLLKLRGLLG
FVGTLLLPLC LATPLTVSLR ALVAGASRAP PARVASAPWS WLLVGYGAAG LSWSLWAVLS
PPGAQEKEQD QVNNKVLMWR LLKLSRPDLP LLVAAFFFLV LAVLGETLIP HYSGRVIDIL
GGDFDPHAFA SAIFFMCLFS FGSSLSAGCR GGCFTYTMSR INLRIREQLF SSLLRQDLGF
FQETKTGELN SRLSSDTTLM SNWLPLNANV LLRSLVKVVG LYGFMLSISP RLTLLSLLHM
PFTIAAEKVY NTRHQEVLRE IQDAVARAGQ VVREAVGGLQ TVRSFGAEEH EVCRYKEALE
QCRQLYWRRD LERALYLLVR RVLHLGVQML MLSCGLQQMQ DGELTQGSLL SFMIYQESVG
SYVQTLVYIY GDMLSNVGAA EKVFSYMDRQ PNLPSPGTLA PTTLQGVVKF QDVSFAYPNR
PDRPVLKGLT FTLRPGEVTA LVGPNGSGKS TVAALLQNLY QPTGGQVLLD EKPISQYEHC
YLHSQVVSVG QEPVLFSGSV RNNIAYGLQS CEDDKVMAAA QAAHADDFIQ EMEHGIYTDV
GEKGSQLAAG QKQRLAIARA LVRDPRVLIL DEATSALDVQ CEQALQDWNS RGDRTVLVIA
HRLQTVQRAH QILVLQEGKL QKLAQL


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