ARID4A

Protein-coding gene in humans
ARID4A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2LCC, 2MAM, 2YRV

Identifiers
AliasesARID4A, RBBP-1, RBBP1, RBP-1, RBP1, AT-rich interaction domain 4A
External IDsOMIM: 180201 MGI: 2444354 HomoloGene: 11303 GeneCards: ARID4A
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for ARID4A
Genomic location for ARID4A
Band14q23.1Start58,298,504 bp[1]
End58,373,887 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for ARID4A
Genomic location for ARID4A
Band12|12 C2Start71,015,990 bp[2]
End71,098,592 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • sural nerve

  • monocyte

  • bone marrow cells

  • ganglionic eminence

  • thymus

  • corpus callosum

  • superficial temporal artery

  • secondary oocyte

  • lactiferous duct
Top expressed in
  • hand

  • secondary oocyte

  • blood

  • aortic valve

  • ascending aorta

  • cumulus cell

  • supraoptic nucleus

  • bone marrow

  • pineal gland

  • spleen
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • DNA binding
  • histone deacetylase activity
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • transcription repressor complex
  • nucleus
  • nucleoplasm
  • cytosol
  • plasma membrane
Biological process
  • histone H3-K9 trimethylation
  • establishment of Sertoli cell barrier
  • regulation of transcription, DNA-templated
  • regulation of gene expression by genetic imprinting
  • transcription by RNA polymerase II
  • positive regulation of transcription by RNA polymerase II
  • erythrocyte development
  • regulation of transcription by RNA polymerase II
  • spermatogenesis
  • histone H4-K20 trimethylation
  • histone H3-K4 trimethylation
  • transcription, DNA-templated
  • negative regulation of transcription, DNA-templated
  • histone deacetylation
  • chromatin organization
  • cell differentiation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5926

238247

Ensembl

ENSG00000032219

ENSMUSG00000048118

UniProt

P29374

F8VPQ2

RefSeq (mRNA)

NM_002892
NM_023000
NM_023001

NM_001081195

RefSeq (protein)

NP_002883
NP_075376
NP_075377

NP_001074664

Location (UCSC)Chr 14: 58.3 – 58.37 MbChr 12: 71.02 – 71.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

AT rich interactive domain 4A (RBP1-like), also known as ARID4A, is a protein which in humans is encoded by the ARID4A gene.[5][6][7]

Function

The protein encoded by this gene is a ubiquitously expressed nuclear protein. It binds directly, with several other proteins, to retinoblastoma protein (pRB) which regulates cell proliferation. pRB represses transcription by recruiting the encoded protein. This protein, in turn, serves as a bridging molecule to recruit HDACs and, in addition, provides a second HDAC-independent repression function. The encoded protein possesses transcriptional repression activity. Multiple alternatively spliced transcripts have been observed for this gene, although not all transcript variants have been fully described.[5]

Interactions

ARID4A has been shown to interact with Retinoblastoma protein.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000032219 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000048118 - 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. ^ a b "Entrez Gene: ARID4A AT rich interactive domain 4A (RBP1-like)".
  6. ^ Defeo-Jones D, Huang PS, Jones RE, Haskell KM, Vuocolo GA, Hanobik MG, Huber HE, Oliff A (Jul 1991). "Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product". Nature. 352 (6332): 251–4. Bibcode:1991Natur.352..251D. doi:10.1038/352251a0. PMID 1857421. S2CID 4357523.
  7. ^ Otterson GA, Kratzke RA, Lin AY, Johnston PG, Kaye FJ (Apr 1993). "Alternative splicing of the RBP1 gene clusters in an internal exon that encodes potential phosphorylation sites". Oncogene. 8 (4): 949–57. PMID 8455946.
  8. ^ Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE (Oct 1999). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Molecular and Cellular Biology. 19 (10): 6632–41. doi:10.1128/mcb.19.10.6632. PMC 84642. PMID 10490602.

Further reading

  • Defeo-Jones D, Huang PS, Jones RE, Haskell KM, Vuocolo GA, Hanobik MG, Huber HE, Oliff A (Jul 1991). "Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product". Nature. 352 (6332): 251–4. Bibcode:1991Natur.352..251D. doi:10.1038/352251a0. PMID 1857421. S2CID 4357523.
  • Fattaey AR, Helin K, Dembski MS, Dyson N, Harlow E, Vuocolo GA, Hanobik MG, Haskell KM, Oliff A, Defeo-Jones D (Nov 1993). "Characterization of the retinoblastoma binding proteins RBP1 and RBP2". Oncogene. 8 (11): 3149–56. PMID 8414517.
  • Otterson GA, Kratzke RA, Lin AY, Johnston PG, Kaye FJ (Apr 1993). "Alternative splicing of the RBP1 gene clusters in an internal exon that encodes potential phosphorylation sites". Oncogene. 8 (4): 949–57. PMID 8455946.
  • Margottin F, Bour SP, Durand H, Selig L, Benichou S, Richard V, Thomas D, Strebel K, Benarous R (Mar 1998). "A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif". Molecular Cell. 1 (4): 565–74. doi:10.1016/S1097-2765(00)80056-8. PMID 9660940.
  • Lai A, Marcellus RC, Corbeil HB, Branton PE (Mar 1999). "RBP1 induces growth arrest by repression of E2F-dependent transcription". Oncogene. 18 (12): 2091–100. doi:10.1038/sj.onc.1202520. PMID 10321733.
  • Cao J, Gao T, Giuliano AE, Irie RF (Feb 1999). "Recognition of an epitope of a breast cancer antigen by human antibody". Breast Cancer Research and Treatment. 53 (3): 279–90. doi:10.1023/A:1006115922401. PMID 10369074. S2CID 34896754.
  • Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE (Oct 1999). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Molecular and Cellular Biology. 19 (10): 6632–41. doi:10.1128/mcb.19.10.6632. PMC 84642. PMID 10490602.
  • Lai A, Kennedy BK, Barbie DA, Bertos NR, Yang XJ, Theberge MC, Tsai SC, Seto E, Zhang Y, Kuzmichev A, Lane WS, Reinberg D, Harlow E, Branton PE (Apr 2001). "RBP1 recruits the mSIN3-histone deacetylase complex to the pocket of retinoblastoma tumor suppressor family proteins found in limited discrete regions of the nucleus at growth arrest". Molecular and Cellular Biology. 21 (8): 2918–32. doi:10.1128/MCB.21.8.2918-2932.2001. PMC 86920. PMID 11283269.
  • Fleischer TC, Yun UJ, Ayer DE (May 2003). "Identification and characterization of three new components of the mSin3A corepressor complex". Molecular and Cellular Biology. 23 (10): 3456–67. doi:10.1128/MCB.23.10.3456-3467.2003. PMC 164750. PMID 12724404.
  • Meehan WJ, Samant RS, Hopper JE, Carrozza MJ, Shevde LA, Workman JL, Eckert KA, Verderame MF, Welch DR (Jan 2004). "Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription". The Journal of Biological Chemistry. 279 (2): 1562–9. doi:10.1074/jbc.M307969200. PMID 14581478.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Monroe DG, Secreto FJ, Hawse JR, Subramaniam M, Khosla S, Spelsberg TC (Sep 2006). "Estrogen receptor isoform-specific regulation of the retinoblastoma-binding protein 1 (RBBP1) gene: roles of AF1 and enhancer elements". The Journal of Biological Chemistry. 281 (39): 28596–604. doi:10.1074/jbc.M605226200. PMID 16873370.

External links

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

  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies