TAP1

Protein-coding gene in the species Homo sapiens
TAP1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1JJ7

Identifiers
AliasesTAP1, ABC17, ABCB2, APT1, D6S114E, PSF-1, PSF1, RING4, TAP1*0102N, TAP1N, transporter 1, ATP-binding cassette, sub-family B (MDR/TAP), transporter 1, ATP binding cassette subfamily B member
External IDsOMIM: 170260 MGI: 98483 HomoloGene: 495 GeneCards: TAP1
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for TAP1
Genomic location for TAP1
Band6p21.32Start32,845,209 bp[1]
End32,853,816 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for TAP1
Genomic location for TAP1
Band17 B1|17 17.98 cMStart34,406,527 bp[2]
End34,416,199 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • appendix

  • lymph node

  • blood

  • spleen

  • monocyte

  • duodenum

  • skin of abdomen

  • upper lobe of left lung

  • rectum

  • right lung
Top expressed in
  • thymus

  • spleen

  • mucous cell of stomach

  • intestinal villus

  • jejunum

  • duodenum

  • subcutaneous adipose tissue

  • blood

  • bone marrow

  • submandibular gland
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • MHC protein binding
  • nucleotide binding
  • protein homodimerization activity
  • ABC-type peptide transporter activity
  • TAP2 binding
  • MHC class Ib protein binding
  • ATPase activity
  • protein binding
  • MHC class I protein binding
  • TAP1 binding
  • ATP binding
  • peptide antigen binding
  • ADP binding
  • ATPase-coupled transmembrane transporter activity
  • ABC-type peptide antigen transporter activity
  • peptide transmembrane transporter activity
Cellular component
  • integral component of membrane
  • endoplasmic reticulum membrane
  • membrane
  • TAP complex
  • integral component of endoplasmic reticulum membrane
  • mitochondrion
  • endoplasmic reticulum
  • microtubule organizing center
  • phagocytic vesicle membrane
  • endoplasmic reticulum-Golgi intermediate compartment membrane
  • MHC class I peptide loading complex
Biological process
  • defense response
  • adaptive immune response
  • immune system process
  • antigen processing and presentation of peptide antigen via MHC class I
  • antigen processing and presentation of endogenous peptide antigen via MHC class I
  • protein transport
  • peptide transport
  • viral process
  • cytosol to endoplasmic reticulum transport
  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent
  • vesicle fusion with endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane
  • transmembrane transport
  • transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6890

21354

Ensembl
ENSG00000226173
ENSG00000168394
ENSG00000224212
ENSG00000230705
ENSG00000206297

ENSG00000227816
ENSG00000224748
ENSG00000232367

ENSMUSG00000037321

UniProt

Q03518

P21958

RefSeq (mRNA)

NM_001292022
NM_000593

NM_001161730
NM_013683

RefSeq (protein)

NP_000584
NP_001278951

NP_001155202
NP_038711

Location (UCSC)Chr 6: 32.85 – 32.85 MbChr 17: 34.41 – 34.42 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transporter associated with antigen processing 1 (TAP1) is a protein that in humans is encoded by the TAP1 gene. A member of the ATP-binding cassette transporter family, it is also known as ABCB2.[5][6]

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.[7]

See also

Interactions

TAP1 has been shown to interact with:

References

  1. ^ a b c ENSG00000168394, ENSG00000224212, ENSG00000230705, ENSG00000206297, ENSG00000227816, ENSG00000224748, ENSG00000232367 GRCh38: Ensembl release 89: ENSG00000226173, ENSG00000168394, ENSG00000224212, ENSG00000230705, ENSG00000206297, ENSG00000227816, ENSG00000224748, ENSG00000232367 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037321 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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): 161–173. doi:10.1111/j.1399-0039.1992.tb01932.x. PMID 1529427.
  6. ^ 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): 10094–10098. Bibcode:1991PNAS...8810094B. doi:10.1073/pnas.88.22.10094. PMC 52874. PMID 1946428.
  7. ^ "Entrez Gene: TAP1 transporter 1, ATP-binding cassette, sub-family B (MDR/TAP)".
  8. ^ a b 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): 18266–18271. doi:10.1074/jbc.M201388200. PMID 11884415.
  9. ^ 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): 41786–41794. doi:10.1074/jbc.M207128200. PMID 12213826.

Further reading

  • Townsend A, Trowsdale J (1993). "The transporters associated with antigen presentation". Semin. Cell Biol. 4 (1): 53–61. doi:10.1006/scel.1993.1007. PMID 8453065.
  • Schölz C, Tampé R (2006). "The intracellular antigen transport machinery TAP in adaptive immunity and virus escape mechanisms". J. Bioenerg. Biomembr. 37 (6): 509–515. doi:10.1007/s10863-005-9500-1. PMID 16691491. S2CID 28129678.
  • Beck S, Kelly A, Radley E, Khurshid F, Alderton RP, Trowsdale J (1992). "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 (2): 433–441. doi:10.1016/0022-2836(92)90832-5. PMID 1453454.
  • Colonna M, Bresnahan M, Bahram S, Strominger JL, Spies T (1992). "Allelic variants of the human putative peptide transporter involved in antigen processing". Proc. Natl. Acad. Sci. U.S.A. 89 (9): 3932–3936. Bibcode:1992PNAS...89.3932C. doi:10.1073/pnas.89.9.3932. PMC 525605. PMID 1570316.
  • Trowsdale J, Hanson I, Mockridge I, Beck S, Townsend A, Kelly A (1991). "Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters". Nature. 348 (6303): 741–744. doi:10.1038/348741a0. PMID 2259383. S2CID 4279033.
  • Spies T, Bresnahan M, Bahram S, Arnold D, Blanck G, Mellins E, Pious D, DeMars R (1991). "A gene in the human major histocompatibility complex class II region controlling the class I antigen presentation pathway". Nature. 348 (6303): 744–747. doi:10.1038/348744a0. PMID 2259384. S2CID 31875999.
  • Cerundolo V, Alexander J, Anderson K, Lamb C, Cresswell P, McMichael A, Gotch F, Townsend A (1990). "Presentation of viral antigen controlled by a gene in the major histocompatibility complex". Nature. 345 (6274): 449–452. Bibcode:1990Natur.345..449C. doi:10.1038/345449a0. PMID 2342577. S2CID 20178053.
  • Szafer F, Oksenberg JR, Steinman L (1994). "New allelic polymorphisms in TAP genes". Immunogenetics. 39 (5): 374. doi:10.1007/BF00189240. PMID 8168860. S2CID 23485390.
  • Jackson DG, Capra JD (1994). "TAP1 alleles in insulin-dependent diabetes mellitus: a newly defined centromeric boundary of disease susceptibility". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 11079–11083. doi:10.1073/pnas.90.23.11079. PMC 47925. PMID 8248212.
  • Glynne R, Kerr LA, Mockridge I, Beck S, Kelly A, Trowsdale J (1993). "The major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processing". Eur. J. Immunol. 23 (4): 860–866. doi:10.1002/eji.1830230414. PMID 8458375. S2CID 44733094.
  • 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 (1996). "Evolutionary dynamics of non-coding sequences within the class II region of the human MHC". J. Mol. Biol. 255 (1): 1–13. doi:10.1006/jmbi.1996.0001. PMID 8568858.
  • Chen HL, Gabrilovich D, Tampé R, Girgis KR, Nadaf S, Carbone DP (1996). "A functionally defective allele of TAP1 results in loss of MHC class I antigen presentation in a human lung cancer". Nat. Genet. 13 (2): 210–213. doi:10.1038/ng0696-210. PMID 8640228. S2CID 20367760.
  • Ahn K, Meyer TH, Uebel S, Sempé P, Djaballah H, Yang Y, Peterson PA, Früh K, Tampé R (1996). "Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47". EMBO J. 15 (13): 3247–3255. doi:10.1002/j.1460-2075.1996.tb00689.x. PMC 451885. PMID 8670825.
  • Lewis JW, Neisig A, Neefjes J, Elliott T (1997). "Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP". Curr. Biol. 6 (7): 873–883. doi:10.1016/S0960-9822(02)00611-5. PMID 8805302.
  • Nijenhuis M, Hämmerling GJ (1997). "Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site". J. Immunol. 157 (12): 5467–5477. doi:10.4049/jimmunol.157.12.5467. PMID 8955196.
  • Gobin SJ, Wilson L, Keijsers V, Van den Elsen PJ (1997). "Antigen processing and presentation by human trophoblast-derived cell lines". J. Immunol. 158 (8): 3587–3592. doi:10.4049/jimmunol.158.8.3587. PMID 9103419.
  • Ahn K, Gruhler A, Galocha B, Jones TR, Wiertz EJ, Ploegh HL, Peterson PA, Yang Y, Früh K (1997). "The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide translocation by TAP". Immunity. 6 (5): 613–621. doi:10.1016/S1074-7613(00)80349-0. PMID 9175839.

External links

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  • 1jj7: Crystal Structure of the C-terminal ATPase domain of human TAP1
    1jj7: Crystal Structure of the C-terminal ATPase domain of human TAP1

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