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Antigen peptide transporter 1 (APT1) (ATP-binding cassette sub-family B member 2) (Peptide supply factor 1) (Peptide transporter PSF1) (PSF-1) (Peptide transporter TAP1) (Peptide transporter involved in antigen processing 1) (Really interesting new gene 4 protein)

 TAP1_HUMAN              Reviewed;         808 AA.
Q03518; Q16149; Q96CP4;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
25-OCT-2017, entry version 191.
RecName: Full=Antigen peptide transporter 1;
Short=APT1;
AltName: Full=ATP-binding cassette sub-family B member 2;
AltName: Full=Peptide supply factor 1;
AltName: Full=Peptide transporter PSF1;
Short=PSF-1;
AltName: Full=Peptide transporter TAP1;
AltName: Full=Peptide transporter involved in antigen processing 1;
AltName: Full=Really interesting new gene 4 protein;
Name=TAP1; Synonyms=ABCB2, PSF1, RING4, Y3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2259383; DOI=10.1038/348741a0;
Trowsdale J., Hanson I., Mockridge I., Beck S., Townsend A., Kelly A.;
"Sequences encoded in the class II region of the MHC related to the
'ABC' superfamily of transporters.";
Nature 348:741-744(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 61-808, VARIANTS VAL-393; LEU-518;
GLY-697 AND GLN-708, AND POLYMORPHISM.
TISSUE=Blood;
PubMed=8248212; DOI=10.1073/pnas.90.23.11079;
Jackson D.G., Capra J.D.;
"TAP1 alleles in insulin-dependent diabetes mellitus: a newly defined
centromeric boundary of disease susceptibility.";
Proc. Natl. Acad. Sci. U.S.A. 90:11079-11083(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 183-612.
PubMed=2259384; DOI=10.1038/348744a0;
Spies T., Bresnahan M., Bahram S., Arnold D., Blanck G., Mellins E.,
Pious D., Demars R.;
"A gene in the human major histocompatibility complex class II region
controlling the class I antigen presentation pathway.";
Nature 348:744-747(1990).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 691-723, VARIANTS GLY-697 AND GLN-708,
AND POLYMORPHISM.
PubMed=8168860; DOI=10.1007/BF00189240;
Szafer F., Oksenberg J.R., Steinman L.;
"New allelic polymorphisms in TAP genes.";
Immunogenetics 39:374-374(1994).
[10]
TISSUE SPECIFICITY.
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).
[11]
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).
[12]
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).
[13]
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).
[14]
DOWN-REGULATION BY VIRAL IL-10.
PubMed=9310490;
Zeidler R., Eissner G., Meissner P., Uebel S., Tampe R., Lazis S.,
Hammerschmidt W.;
"Downregulation of TAP1 in B lymphocytes by cellular and Epstein-Barr
virus-encoded interleukin-10.";
Blood 90:2390-2397(1997).
[15]
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).
[16]
INVOLVEMENT IN BLS1.
PubMed=10074494; DOI=10.1172/JCI5335;
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.;
"Splice acceptor site mutation of the transporter associated with
antigen processing-1 gene in human bare lymphocyte syndrome.";
J. Clin. Invest. 103:755-758(1999).
[17]
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).
[18]
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).
[19]
INTERACTION WITH PSMB5 AND PSMB8.
PubMed=15488952; DOI=10.1016/j.molimm.2004.07.005;
Begley G.S., Horvath A.R., Taylor J.C., Higgins C.F.;
"Cytoplasmic domains of the transporter associated with antigen
processing and P-glycoprotein interact with subunits of the
proteasome.";
Mol. Immunol. 42:137-141(2005).
[20]
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).
[21]
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).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[23]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 549-808.
PubMed=11532960; DOI=10.1093/emboj/20.17.4964;
Gaudet R., Wiley D.C.;
"Structure of the ABC ATPase domain of human TAP1, the transporter
associated with antigen processing.";
EMBO J. 20:4964-4972(2001).
[24]
VARIANTS VAL-393 AND GLY-697, AND POLYMORPHISM.
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).
[25]
VARIANT GLN-719.
PubMed=8640228; DOI=10.1038/ng0696-210;
Chen H.L., Gabrilovich D., Tampe R., Girgis K.R., Nadaf S.,
Carbone D.P.;
"A functionally defective allele of TAP1 results in loss of MHC class
I antigen presentation in a human lung cancer.";
Nat. Genet. 13:210-213(1996).
[26]
VARIANTS VAL-393; VAL-430; LEU-518; ILE-578; GLY-697 AND GLN-708, AND
POLYMORPHISM.
PubMed=11250043; DOI=10.1016/S0198-8859(00)00259-7;
Tang J., Freedman D.O., Allen S., Karita E., Musonda R., Braga C.,
Margolick J., Kaslow R.A.;
"TAP1 polymorphisms in several human ethnic groups: characteristics,
evolution, and genotyping strategies.";
Hum. Immunol. 62:256-268(2001).
[27]
VARIANTS SER-67; ARG-77; VAL-393; VAL-430; CYS-479; LEU-518; GLY-697
AND GLN-708, AND POLYMORPHISM.
PubMed=12878362; DOI=10.1016/S0198-8859(03)00110-1;
Lajoie J., Zijenah L.S., Faucher M.C., Ward B.J., Roger M.;
"Novel TAP1 polymorphisms in indigenous Zimbabweans: their potential
implications on TAP function and in human diseases.";
Hum. Immunol. 64:823-829(2003).
-!- 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: Heterodimer of TAP1 and TAP2. Interacts with Epstein-Barr
virus BNLF2a. Interacts with herpes simplex virus ICP47
(PubMed:7760936). Interacts with PSMB5 and PSMB8.
{ECO:0000269|PubMed:15488952, ECO:0000269|PubMed:19201886,
ECO:0000269|PubMed:7760936}.
-!- INTERACTION:
P0C739:BNLF2a (xeno); NbExp=9; IntAct=EBI-747259, EBI-9346744;
P27797:CALR; NbExp=2; IntAct=EBI-747259, EBI-1049597;
Q77CE4:gN (xeno); NbExp=6; IntAct=EBI-747259, EBI-11303846;
P07237:P4HB; NbExp=4; IntAct=EBI-747259, EBI-395883;
P30101:PDIA3; NbExp=4; IntAct=EBI-747259, EBI-979862;
Q03519:TAP2; NbExp=17; IntAct=EBI-747259, EBI-780781;
O15533:TAPBP; NbExp=14; IntAct=EBI-747259, EBI-874801;
Q13769:THOC5; NbExp=4; IntAct=EBI-747259, EBI-5280316;
-!- 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.
-!- 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.
{ECO:0000269|PubMed:11250043, ECO:0000269|PubMed:12878362,
ECO:0000269|PubMed:1570316, ECO:0000269|PubMed:8168860,
ECO:0000269|PubMed:8248212}.
-!- 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:10074494}. 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}.
-!- CAUTION: It is uncertain whether Met-1 or Met-61 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA47025.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA60785.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=TAP1base; Note=TAP1 mutation db;
URL="http://structure.bmc.lu.se/idbase/TAP1base/";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q03518";
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EMBL; X57522; CAA40741.1; -; mRNA.
EMBL; X66401; CAA47025.1; ALT_INIT; Genomic_DNA.
EMBL; X87344; CAA60785.1; ALT_INIT; Genomic_DNA.
EMBL; AL669918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL671681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL935043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX927138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR762476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR933844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR753889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03647.1; -; Genomic_DNA.
EMBL; BC014081; AAH14081.1; -; mRNA.
EMBL; L21204; AAC12902.1; -; mRNA.
EMBL; L21205; AAC12903.1; -; mRNA.
EMBL; L21206; AAC12904.1; -; mRNA.
EMBL; L21207; AAC12905.1; -; mRNA.
EMBL; L21208; AAC12906.1; -; mRNA.
EMBL; X57521; CAA40740.1; -; mRNA.
EMBL; S70274; AAD14056.1; -; mRNA.
CCDS; CCDS4758.1; -.
PIR; S13427; A41538.
RefSeq; NP_000584.2; NM_000593.5.
RefSeq; NP_001278951.1; NM_001292022.1.
UniGene; Hs.352018; -.
UniGene; Hs.731555; -.
PDB; 1JJ7; X-ray; 2.40 A; A=549-808.
PDB; 5U1D; EM; 3.97 A; A=61-808.
PDBsum; 1JJ7; -.
PDBsum; 5U1D; -.
ProteinModelPortal; Q03518; -.
SMR; Q03518; -.
BioGrid; 112753; 41.
DIP; DIP-35626N; -.
IntAct; Q03518; 42.
MINT; MINT-1477433; -.
STRING; 9606.ENSP00000346206; -.
DrugBank; DB01259; Lapatinib.
TCDB; 3.A.1.209.1; the atp-binding cassette (abc) superfamily.
iPTMnet; Q03518; -.
PhosphoSitePlus; Q03518; -.
SwissPalm; Q03518; -.
BioMuta; TAP1; -.
DMDM; 215273957; -.
EPD; Q03518; -.
MaxQB; Q03518; -.
PaxDb; Q03518; -.
PeptideAtlas; Q03518; -.
PRIDE; Q03518; -.
DNASU; 6890; -.
Ensembl; ENST00000354258; ENSP00000346206; ENSG00000168394.
Ensembl; ENST00000383235; ENSP00000372722; ENSG00000206297.
Ensembl; ENST00000414467; ENSP00000405356; ENSG00000226173.
Ensembl; ENST00000418205; ENSP00000401149; ENSG00000227816.
Ensembl; ENST00000424897; ENSP00000413080; ENSG00000230705.
Ensembl; ENST00000439781; ENSP00000415660; ENSG00000224212.
Ensembl; ENST00000440894; ENSP00000402316; ENSG00000232367.
GeneID; 6890; -.
KEGG; hsa:6890; -.
UCSC; uc003ocg.4; human.
CTD; 6890; -.
DisGeNET; 6890; -.
EuPathDB; HostDB:ENSG00000168394.10; -.
GeneCards; TAP1; -.
HGNC; HGNC:43; TAP1.
HPA; CAB009516; -.
HPA; HPA072354; -.
MalaCards; TAP1; -.
MIM; 170260; gene.
MIM; 604571; phenotype.
neXtProt; NX_Q03518; -.
OpenTargets; ENSG00000168394; -.
Orphanet; 34592; Immunodeficiency by defective expression of HLA class 1.
PharmGKB; PA35021; -.
eggNOG; KOG0058; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00550000074497; -.
HOVERGEN; HBG008358; -.
InParanoid; Q03518; -.
KO; K05653; -.
OMA; QNQTGAI; -.
OrthoDB; EOG09370VL2; -.
PhylomeDB; Q03518; -.
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.
ChiTaRS; TAP1; human.
EvolutionaryTrace; Q03518; -.
GeneWiki; TAP1; -.
GenomeRNAi; 6890; -.
PRO; PR:Q03518; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000168394; -.
CleanEx; HS_TAP1; -.
ExpressionAtlas; Q03518; baseline and differential.
Genevisible; Q03518; 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:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0042825; C:TAP complex; IDA:UniProtKB.
GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0042288; F:MHC class I protein binding; IEA:Ensembl.
GO; GO:0023029; F:MHC class Ib protein binding; IPI:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; NAS:UniProtKB.
GO; GO:0015197; F:peptide transporter activity; IMP:UniProtKB.
GO; GO:0015440; F:peptide-transporting ATPase activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0046978; F:TAP1 binding; ISS:UniProtKB.
GO; GO:0046979; F:TAP2 binding; IPI:UniProtKB.
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; 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:0006952; P:defense response; IEA:Ensembl.
GO; GO:0015833; P:peptide transport; IMP: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; IPR013306; Tap1/ABCB2.
PANTHER; PTHR24221:SF249; PTHR24221:SF249; 1.
Pfam; PF00664; ABC_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
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; 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 1 808 Antigen peptide transporter 1.
/FTId=PRO_0000093326.
TOPO_DOM 61 75 Cytoplasmic. {ECO:0000255}.
TRANSMEM 76 96 Helical; Name=1. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 97 113 Lumenal. {ECO:0000255}.
TRANSMEM 114 136 Helical; Name=2. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 137 152 Cytoplasmic. {ECO:0000255}.
TRANSMEM 153 173 Helical; Name=3. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 174 193 Lumenal. {ECO:0000255}.
TRANSMEM 194 214 Helical; Name=4. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 215 246 Cytoplasmic. {ECO:0000255}.
TRANSMEM 247 267 Helical; Name=5. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 268 287 Lumenal. {ECO:0000255}.
TRANSMEM 288 308 Helical; Name=6. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 309 358 Cytoplasmic. {ECO:0000255}.
TRANSMEM 359 379 Helical; Name=7. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 380 388 Lumenal. {ECO:0000255}.
TRANSMEM 389 409 Helical; Name=8. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 410 478 Cytoplasmic. {ECO:0000255}.
TRANSMEM 479 499 Helical; Name=9. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 500 503 Lumenal. {ECO:0000255}.
TRANSMEM 504 524 Helical; Name=10. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 525 808 Cytoplasmic. {ECO:0000255}.
DOMAIN 247 530 ABC transmembrane type-1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 563 802 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 598 605 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 435 480 Involved in peptide-binding site.
REGION 513 547 Involved in peptide-binding site.
VARIANT 67 67 P -> S (in dbSNP:rs375389015).
{ECO:0000269|PubMed:12878362}.
/FTId=VAR_016801.
VARIANT 77 77 G -> R (in dbSNP:rs57640466).
{ECO:0000269|PubMed:12878362}.
/FTId=VAR_016802.
VARIANT 170 170 L -> V (in dbSNP:rs2228108).
/FTId=VAR_048137.
VARIANT 304 304 V -> L (in dbSNP:rs36229525).
/FTId=VAR_060987.
VARIANT 346 346 S -> F (in dbSNP:rs2228111).
/FTId=VAR_048138.
VARIANT 393 393 I -> V (in allele TAP1*02:01, allele
TAP1*03:01, allele TAP1*04:01 and allele
TAP1*x; dbSNP:rs1057141).
{ECO:0000269|PubMed:11250043,
ECO:0000269|PubMed:12878362,
ECO:0000269|PubMed:1570316,
ECO:0000269|PubMed:8248212}.
/FTId=VAR_000092.
VARIANT 430 430 A -> V (in allele TAP1*x;
dbSNP:rs2127679).
{ECO:0000269|PubMed:11250043,
ECO:0000269|PubMed:12878362}.
/FTId=VAR_013151.
VARIANT 479 479 G -> C (in dbSNP:rs2228110).
{ECO:0000269|PubMed:12878362}.
/FTId=VAR_016803.
VARIANT 518 518 V -> L (in allele TAP1*04:01;
dbSNP:rs41550019).
{ECO:0000269|PubMed:11250043,
ECO:0000269|PubMed:12878362,
ECO:0000269|PubMed:8248212}.
/FTId=VAR_013152.
VARIANT 578 578 V -> I (in allele TAP1*x;
dbSNP:rs41561219).
{ECO:0000269|PubMed:11250043}.
/FTId=VAR_013153.
VARIANT 697 697 D -> G (in allele TAP1*02:01, allele
TAP1*04:01 and allele TAP1*x;
dbSNP:rs1135216).
{ECO:0000269|PubMed:11250043,
ECO:0000269|PubMed:12878362,
ECO:0000269|PubMed:1570316,
ECO:0000269|PubMed:8168860,
ECO:0000269|PubMed:8248212}.
/FTId=VAR_000093.
VARIANT 708 708 R -> Q (in allele TAP1*04:01;
dbSNP:rs1057149).
{ECO:0000269|PubMed:11250043,
ECO:0000269|PubMed:12878362,
ECO:0000269|PubMed:8168860,
ECO:0000269|PubMed:8248212}.
/FTId=VAR_013154.
VARIANT 719 719 R -> Q (in a lung cancer cell line
deficient in MHC class I presentation;
dbSNP:rs121917702).
{ECO:0000269|PubMed:8640228}.
/FTId=VAR_013173.
VARIANT 768 768 Q -> R (in dbSNP:rs1057149).
/FTId=VAR_047514.
STRAND 563 570 {ECO:0000244|PDB:1JJ7}.
STRAND 580 588 {ECO:0000244|PDB:1JJ7}.
STRAND 593 597 {ECO:0000244|PDB:1JJ7}.
HELIX 604 611 {ECO:0000244|PDB:1JJ7}.
STRAND 618 624 {ECO:0000244|PDB:1JJ7}.
HELIX 629 631 {ECO:0000244|PDB:1JJ7}.
HELIX 634 640 {ECO:0000244|PDB:1JJ7}.
STRAND 641 644 {ECO:0000244|PDB:1JJ7}.
STRAND 652 654 {ECO:0000244|PDB:1JJ7}.
HELIX 655 660 {ECO:0000244|PDB:1JJ7}.
HELIX 669 678 {ECO:0000244|PDB:1JJ7}.
HELIX 682 686 {ECO:0000244|PDB:1JJ7}.
HELIX 691 693 {ECO:0000244|PDB:1JJ7}.
STRAND 701 703 {ECO:0000244|PDB:1JJ7}.
HELIX 705 717 {ECO:0000244|PDB:1JJ7}.
STRAND 722 728 {ECO:0000244|PDB:1JJ7}.
TURN 729 732 {ECO:0000244|PDB:1JJ7}.
HELIX 735 746 {ECO:0000244|PDB:1JJ7}.
HELIX 749 753 {ECO:0000244|PDB:1JJ7}.
STRAND 755 759 {ECO:0000244|PDB:1JJ7}.
HELIX 763 767 {ECO:0000244|PDB:1JJ7}.
STRAND 770 776 {ECO:0000244|PDB:1JJ7}.
STRAND 779 784 {ECO:0000244|PDB:1JJ7}.
HELIX 786 792 {ECO:0000244|PDB:1JJ7}.
HELIX 795 800 {ECO:0000244|PDB:1JJ7}.
SEQUENCE 808 AA; 87218 MW; 9CA5FF96FADD6A1B CRC64;
MAELLASAGS ACSWDFPRAP PSFPPPAASR GGLGGTRSFR PHRGAESPRP GRDRDGVRVP
MASSRCPAPR GCRCLPGASL AWLGTVLLLL ADWVLLRTAL PRIFSLLVPT ALPLLRVWAV
GLSRWAVLWL GACGVLRATV GSKSENAGAQ GWLAALKPLA AALGLALPGL ALFRELISWG
APGSADSTRL LHWGSHPTAF VVSYAAALPA AALWHKLGSL WVPGGQGGSG NPVRRLLGCL
GSETRRLSLF LVLVVLSSLG EMAIPFFTGR LTDWILQDGS ADTFTRNLTL MSILTIASAV
LEFVGDGIYN NTMGHVHSHL QGEVFGAVLR QETEFFQQNQ TGNIMSRVTE DTSTLSDSLS
ENLSLFLWYL VRGLCLLGIM LWGSVSLTMV TLITLPLLFL LPKKVGKWYQ LLEVQVRESL
AKSSQVAIEA LSAMPTVRSF ANEEGEAQKF REKLQEIKTL NQKEAVAYAV NSWTTSISGM
LLKVGILYIG GQLVTSGAVS SGNLVTFVLY QMQFTQAVEV LLSIYPRVQK AVGSSEKIFE
YLDRTPRCPP SGLLTPLHLE GLVQFQDVSF AYPNRPDVLV LQGLTFTLRP GEVTALVGPN
GSGKSTVAAL LQNLYQPTGG QLLLDGKPLP QYEHRYLHRQ VAAVGQEPQV FGRSLQENIA
YGLTQKPTME EITAAAVKSG AHSFISGLPQ GYDTEVDEAG SQLSGGQRQA VALARALIRK
PCVLILDDAT SALDANSQLQ VEQLLYESPE RYSRSVLLIT QHLSLVEQAD HILFLEGGAI
REGGTHQQLM EKKGCYWAMV QAPADAPE


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