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{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''Transporter associated with Antigen Processing 1''' is a [[protein]] that in humans is encoded by the ''TAP1'' [[gene]].<ref name="pmid1529427">{{cite journal | vauthors = Bodmer JG, Marsh SG, Albert ED, Bodmer WF, Dupont B, Erlich HA, Mach B, Mayr WR, Parham P, Sasazuki T | title = Nomenclature for factors of the HLA system, 1991. WHO Nomenclature Committee for factors of the HLA system | journal = Tissue Antigens | volume = 39 | issue = 4 | pages = 161–73 | date = Oct 1992 | pmid = 1529427 | pmc =  | doi = 10.1111/j.1399-0039.1992.tb01932.x }}</ref><ref name="pmid1946428">{{cite journal | vauthors = Bahram S, Arnold D, Bresnahan M, Strominger JL, Spies T | title = Two putative subunits of a peptide pump encoded in the human major histocompatibility complex class II region | journal = Proc Natl Acad Sci U S A | volume = 88 | issue = 22 | pages = 10094–8 | date = Dec 1991 | pmid = 1946428 | pmc = 52874 | doi = 10.1073/pnas.88.22.10094 }}</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
{{GNF_Protein_box
| image = PBB_Protein_TAP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jj7.
| Name = Transporter 1, ATP-binding cassette, sub-family B (MDR/TAP)
| HGNCid = 43
| Symbol = TAP1
| AltSymbols =; APT1; ABC17; ABCB2; D6S114E; FLJ26666; FLJ41500; PSF1; RING4; TAP1*0102N; TAP1N
| OMIM = 170260
| ECnumber = 
| Homologene = 495
| MGIid = 98483
| GeneAtlas_image1 = PBB_GE_TAP1_202307_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015198 |text = oligopeptide transporter activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042626 |text = ATPase activity, coupled to transmembrane movement of substances}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
  | Process = {{GNF_GO|id=GO:0006857 |text = oligopeptide transport}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6890
    | Hs_Ensembl = ENSG00000168394
    | Hs_RefseqProtein = NP_000584
    | Hs_RefseqmRNA = NM_000593
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 32920804
    | Hs_GenLoc_end = 32929729
    | Hs_Uniprot = Q03518
    | Mm_EntrezGene = 21354
    | Mm_Ensembl = ENSMUSG00000037321
    | Mm_RefseqmRNA = NM_013683
    | Mm_RefseqProtein = NP_038711
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 33798022
    | Mm_GenLoc_end = 33807437
    | Mm_Uniprot = Q3U543
  }}
}}
{{CMG}}
__NOTOC__


== Function ==


==Overview==
The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MDR/TAP subfamily. Members of the MDR/TAP subfamily are involved in multidrug resistance. The protein encoded by this gene is involved in the pumping of degraded cytosolic peptides across the endoplasmic reticulum into the membrane-bound compartment where class I molecules assemble. Mutations in this gene may be associated with ankylosing spondylitis, insulin-dependent diabetes mellitus, and celiac disease.<ref>{{cite web | title = Entrez Gene: TAP1 transporter 1, ATP-binding cassette, sub-family B (MDR/TAP)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6890| accessdate = }}</ref>
'''Transporter 1, ATP-binding cassette, sub-family B (MDR/TAP)''', also known as '''TAP1''', is a human [[gene]].
 
{{PBB_Summary
== See also ==
| section_title =
| summary_text = The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MDR/TAP subfamily. Members of the MDR/TAP subfamily are involved in multidrug resistance. The protein encoded by this gene is involved in the pumping of degraded cytosolic peptides across the endoplasmic reticulum into the membrane-bound compartment where class I molecules assemble. Mutations in this gene may be associated with ankylosing spondylitis, insulin-dependent diabetes mellitus, and celiac disease.<ref>{{cite web | title = Entrez Gene: TAP1 transporter 1, ATP-binding cassette, sub-family B (MDR/TAP)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6890| accessdate = }}</ref>
}}
==See also==
* [[ATP-binding cassette transporter]]
* [[ATP-binding cassette transporter]]


==References==
== Interactions ==
 
TAP1 has been shown to [[Protein-protein interaction|interact]] with:
* [[HLA-A]],<ref name = pmid11884415/> and
* [[Tapasin]].<ref name = pmid11884415>{{cite journal | vauthors = Paulsson KM, Kleijmeer MJ, Griffith J, Jevon M, Chen S, Anderson PO, Sjogren HO, Li S, Wang P | title = Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum | journal = J. Biol. Chem. | volume = 277 | issue = 21 | pages = 18266–71 | date = May 2002 | pmid = 11884415 | doi = 10.1074/jbc.M201388200 }}</ref><ref name = pmid12213826>{{cite journal | vauthors = Raghuraman G, Lapinski PE, Raghavan M | title = Tapasin interacts with the membrane-spanning domains of both TAP subunits and enhances the structural stability of TAP1 x TAP2 Complexes | journal = J. Biol. Chem. | volume = 277 | issue = 44 | pages = 41786–94 | date = Nov 2002 | pmid = 12213826 | doi = 10.1074/jbc.M207128200 }}</ref>
 
== References ==
{{reflist}}
{{reflist}}
{{Clear}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Townsend A, Trowsdale J | title = The transporters associated with antigen presentation | journal = Semin. Cell Biol. | volume = 4 | issue = 1 | pages = 53–61 | year = 1993 | pmid = 8453065 | doi = 10.1006/scel.1993.1007 }}
| citations =
* {{cite journal | vauthors = Schölz C, Tampé R | title = The intracellular antigen transport machinery TAP in adaptive immunity and virus escape mechanisms | journal = J. Bioenerg. Biomembr. | volume = 37 | issue = 6 | pages = 509–15 | year = 2006 | pmid = 16691491 | doi = 10.1007/s10863-005-9500-1 }}
*{{cite journal | author=Townsend A, Trowsdale J |title=The transporters associated with antigen presentation. |journal=Semin. Cell Biol. |volume=4 |issue= 1 |pages= 53-61 |year= 1993 |pmid= 8453065 |doi= }}
* {{cite journal | vauthors = Beck S, Kelly A, Radley E, Khurshid F, Alderton RP, Trowsdale J | title = DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing | journal = J. Mol. Biol. | volume = 228 | issue = 2 | pages = 433–41 | year = 1992 | pmid = 1453454 | doi = 10.1016/0022-2836(92)90832-5 }}
*{{cite journal | author=Schölz C, Tampé R |title=The intracellular antigen transport machinery TAP in adaptive immunity and virus escape mechanisms. |journal=J. Bioenerg. Biomembr. |volume=37 |issue= 6 |pages= 509-15 |year= 2006 |pmid= 16691491 |doi= 10.1007/s10863-005-9500-1 }}
* {{cite journal | vauthors = Colonna M, Bresnahan M, Bahram S, Strominger JL, Spies T | title = Allelic variants of the human putative peptide transporter involved in antigen processing | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 89 | issue = 9 | pages = 3932–6 | year = 1992 | pmid = 1570316 | pmc = 525605 | doi = 10.1073/pnas.89.9.3932 }}
*{{cite journal | author=Beck S, Kelly A, Radley E, ''et al.'' |title=DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing. |journal=J. Mol. Biol. |volume=228 |issue= 2 |pages= 433-41 |year= 1992 |pmid= 1453454 |doi= }}
* {{cite journal | vauthors = Trowsdale J, Hanson I, Mockridge I, Beck S, Townsend A, Kelly A | title = Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters | journal = Nature | volume = 348 | issue = 6303 | pages = 741–4 | year = 1991 | pmid = 2259383 | doi = 10.1038/348741a0 }}
*{{cite journal  | author=Bodmer JG, Marsh SG, Albert ED, ''et al.'' |title=Nomenclature for factors of the HLA system, 1991. WHO Nomenclature Committee for factors of the HLA system. |journal=Tissue Antigens |volume=39 |issue= 4 |pages= 161-73 |year= 1992 |pmid= 1529427 |doi=  }}
* {{cite journal | vauthors = Spies T, Bresnahan M, Bahram S, Arnold D, Blanck G, Mellins E, Pious D, DeMars R | title = A gene in the human major histocompatibility complex class II region controlling the class I antigen presentation pathway | journal = Nature | volume = 348 | issue = 6303 | pages = 744–7 | year = 1991 | pmid = 2259384 | doi = 10.1038/348744a0 }}
*{{cite journal | author=Colonna M, Bresnahan M, Bahram S, ''et al.'' |title=Allelic variants of the human putative peptide transporter involved in antigen processing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 9 |pages= 3932-6 |year= 1992 |pmid= 1570316 |doi= }}
* {{cite journal | vauthors = Cerundolo V, Alexander J, Anderson K, Lamb C, Cresswell P, McMichael A, Gotch F, Townsend A | title = Presentation of viral antigen controlled by a gene in the major histocompatibility complex | journal = Nature | volume = 345 | issue = 6274 | pages = 449–52 | year = 1990 | pmid = 2342577 | doi = 10.1038/345449a0 }}
*{{cite journal  | author=Bahram S, Arnold D, Bresnahan M, ''et al.'' |title=Two putative subunits of a peptide pump encoded in the human major histocompatibility complex class II region. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 22 |pages= 10094-8 |year= 1991 |pmid= 1946428 |doi=  }}
* {{cite journal | vauthors = Szafer F, Oksenberg JR, Steinman L | title = New allelic polymorphisms in TAP genes | journal = Immunogenetics | volume = 39 | issue = 5 | pages = 374 | year = 1994 | pmid = 8168860 | doi = 10.1007/BF00189240 }}
*{{cite journal | author=Trowsdale J, Hanson I, Mockridge I, ''et al.'' |title=Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters. |journal=Nature |volume=348 |issue= 6303 |pages= 741-4 |year= 1991 |pmid= 2259383 |doi= 10.1038/348741a0 }}
* {{cite journal | vauthors = Jackson DG, Capra JD | title = TAP1 alleles in insulin-dependent diabetes mellitus: a newly defined centromeric boundary of disease susceptibility | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 90 | issue = 23 | pages = 11079–83 | year = 1994 | pmid = 8248212 | pmc = 47925 | doi = 10.1073/pnas.90.23.11079 }}
*{{cite journal | author=Spies T, Bresnahan M, Bahram S, ''et al.'' |title=A gene in the human major histocompatibility complex class II region controlling the class I antigen presentation pathway. |journal=Nature |volume=348 |issue= 6303 |pages= 744-7 |year= 1991 |pmid= 2259384 |doi= 10.1038/348744a0 }}
* {{cite journal | vauthors = Glynne R, Kerr LA, Mockridge I, Beck S, Kelly A, Trowsdale J | title = The major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processing | journal = Eur. J. Immunol. | volume = 23 | issue = 4 | pages = 860–6 | year = 1993 | pmid = 8458375 | doi = 10.1002/eji.1830230414 }}
*{{cite journal | author=Cerundolo V, Alexander J, Anderson K, ''et al.'' |title=Presentation of viral antigen controlled by a gene in the major histocompatibility complex. |journal=Nature |volume=345 |issue= 6274 |pages= 449-52 |year= 1990 |pmid= 2342577 |doi= 10.1038/345449a0 }}
* {{cite journal | vauthors = Beck S, Abdulla S, Alderton RP, Glynne RJ, Gut IG, Hosking LK, Jackson A, Kelly A, Newell WR, Sanseau P, Radley E, Thorpe KL, Trowsdale J | title = Evolutionary dynamics of non-coding sequences within the class II region of the human MHC | journal = J. Mol. Biol. | volume = 255 | issue = 1 | pages = 1–13 | year = 1996 | pmid = 8568858 | doi = 10.1006/jmbi.1996.0001 }}
*{{cite journal | author=Szafer F, Oksenberg JR, Steinman L |title=New allelic polymorphisms in TAP genes. |journal=Immunogenetics |volume=39 |issue= 5 |pages= 374 |year= 1994 |pmid= 8168860 |doi= }}
* {{cite journal | vauthors = Chen HL, Gabrilovich D, Tampé R, Girgis KR, Nadaf S, Carbone DP | title = A functionally defective allele of TAP1 results in loss of MHC class I antigen presentation in a human lung cancer | journal = Nat. Genet. | volume = 13 | issue = 2 | pages = 210–3 | year = 1996 | pmid = 8640228 | doi = 10.1038/ng0696-210 }}
*{{cite journal | author=Jackson DG, Capra JD |title=TAP1 alleles in insulin-dependent diabetes mellitus: a newly defined centromeric boundary of disease susceptibility. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 23 |pages= 11079-83 |year= 1994 |pmid= 8248212 |doi= }}
* {{cite journal | vauthors = Ahn K, Meyer TH, Uebel S, Sempé P, Djaballah H, Yang Y, Peterson PA, Früh K, Tampé R | title = Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47 | journal = EMBO J. | volume = 15 | issue = 13 | pages = 3247–55 | year = 1996 | pmid = 8670825 | pmc = 451885 | doi =  }}
*{{cite journal | author=Glynne R, Kerr LA, Mockridge I, ''et al.'' |title=The major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processing. |journal=Eur. J. Immunol. |volume=23 |issue= 4 |pages= 860-6 |year= 1993 |pmid= 8458375 |doi= }}
* {{cite journal | vauthors = Lewis JW, Neisig A, Neefjes J, Elliott T | title = Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP | journal = Curr. Biol. | volume = 6 | issue = 7 | pages = 873–83 | year = 1997 | pmid = 8805302 | doi = 10.1016/S0960-9822(02)00611-5 }}
*{{cite journal | author=Beck S, Abdulla S, Alderton RP, ''et al.'' |title=Evolutionary dynamics of non-coding sequences within the class II region of the human MHC. |journal=J. Mol. Biol. |volume=255 |issue= 1 |pages= 1-13 |year= 1996 |pmid= 8568858 |doi= 10.1006/jmbi.1996.0001 }}
* {{cite journal | vauthors = Nijenhuis M, Hämmerling GJ | title = Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site | journal = J. Immunol. | volume = 157 | issue = 12 | pages = 5467–77 | year = 1997 | pmid = 8955196 | doi =  }}
*{{cite journal | author=Chen HL, Gabrilovich D, Tampé R, ''et al.'' |title=A functionally defective allele of TAP1 results in loss of MHC class I antigen presentation in a human lung cancer. |journal=Nat. Genet. |volume=13 |issue= 2 |pages= 210-3 |year= 1996 |pmid= 8640228 |doi= 10.1038/ng0696-210 }}
* {{cite journal | vauthors = Gobin SJ, Wilson L, Keijsers V, Van den Elsen PJ | title = Antigen processing and presentation by human trophoblast-derived cell lines | journal = J. Immunol. | volume = 158 | issue = 8 | pages = 3587–92 | year = 1997 | pmid = 9103419 | doi =  }}
*{{cite journal | author=Ahn K, Meyer TH, Uebel S, ''et al.'' |title=Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47. |journal=EMBO J. |volume=15 |issue= 13 |pages= 3247-55 |year= 1996 |pmid= 8670825 |doi=  }}
* {{cite journal | vauthors = Ahn K, Gruhler A, Galocha B, Jones TR, Wiertz EJ, Ploegh HL, Peterson PA, Yang Y, Früh K | title = The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide translocation by TAP | journal = Immunity | volume = 6 | issue = 5 | pages = 613–21 | year = 1997 | pmid = 9175839 | doi = 10.1016/S1074-7613(00)80349-0 }}
*{{cite journal | author=Lewis JW, Neisig A, Neefjes J, Elliott T |title=Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP. |journal=Curr. Biol. |volume=6 |issue= 7 |pages= 873-83 |year= 1997 |pmid= 8805302 |doi= }}
*{{cite journal | author=Nijenhuis M, Hämmerling GJ |title=Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site. |journal=J. Immunol. |volume=157 |issue= 12 |pages= 5467-77 |year= 1997 |pmid= 8955196 |doi=  }}
*{{cite journal | author=Gobin SJ, Wilson L, Keijsers V, Van den Elsen PJ |title=Antigen processing and presentation by human trophoblast-derived cell lines. |journal=J. Immunol. |volume=158 |issue= 8 |pages= 3587-92 |year= 1997 |pmid= 9103419 |doi=  }}
*{{cite journal | author=Ahn K, Gruhler A, Galocha B, ''et al.'' |title=The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide translocation by TAP. |journal=Immunity |volume=6 |issue= 5 |pages= 613-21 |year= 1997 |pmid= 9175839 |doi= }}
}}
{{refend}}
{{refend}}


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* {{MeshName|TAP1+protein,+human}}
* {{MeshName|TAP1+protein,+human}}


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Latest revision as of 00:22, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Transporter associated with Antigen Processing 1 is a protein that in humans is encoded by the TAP1 gene.[1][2]

Function

The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MDR/TAP subfamily. Members of the MDR/TAP subfamily are involved in multidrug resistance. The protein encoded by this gene is involved in the pumping of degraded cytosolic peptides across the endoplasmic reticulum into the membrane-bound compartment where class I molecules assemble. Mutations in this gene may be associated with ankylosing spondylitis, insulin-dependent diabetes mellitus, and celiac disease.[3]

See also

Interactions

TAP1 has been shown to interact with:

References

  1. ↑ Bodmer JG, Marsh SG, Albert ED, Bodmer WF, Dupont B, Erlich HA, Mach B, Mayr WR, Parham P, Sasazuki T (Oct 1992). "Nomenclature for factors of the HLA system, 1991. WHO Nomenclature Committee for factors of the HLA system". Tissue Antigens. 39 (4): 161–73. doi:10.1111/j.1399-0039.1992.tb01932.x. PMID 1529427.
  2. ↑ Bahram S, Arnold D, Bresnahan M, Strominger JL, Spies T (Dec 1991). "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 (22): 10094–8. doi:10.1073/pnas.88.22.10094. PMC 52874. PMID 1946428.
  3. ↑ "Entrez Gene: TAP1 transporter 1, ATP-binding cassette, sub-family B (MDR/TAP)".
  4. ↑ 4.0 4.1 Paulsson KM, Kleijmeer MJ, Griffith J, Jevon M, Chen S, Anderson PO, Sjogren HO, Li S, Wang P (May 2002). "Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum". J. Biol. Chem. 277 (21): 18266–71. doi:10.1074/jbc.M201388200. PMID 11884415.
  5. ↑ Raghuraman G, Lapinski PE, Raghavan M (Nov 2002). "Tapasin interacts with the membrane-spanning domains of both TAP subunits and enhances the structural stability of TAP1 x TAP2 Complexes". J. Biol. Chem. 277 (44): 41786–94. doi:10.1074/jbc.M207128200. PMID 12213826.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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