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Protein FULL name: retinoblastoma-binding protein 8 isoform a [Homo sapiens].
RBBP8 (Homo sapiens) is product of expression of
RBBP8
gene.
FUNCTION: May modulate the functions ascribed to BRCA1 in
transcriptional regulation, DNA repair, and/or cell cycle
checkpoint control.
SUBUNIT: Interacts with CTBP, with the C-terminal (BRCT) domains
of BRCA1, and with the retinoblastoma protein.
INTERACTION:
P38398:BRCA1; NbExp=5; IntAct=EBI-1263531, EBI-349905;
Q6UWZ7:FAM175A; NbExp=1; IntAct=EBI-1263531, EBI-1263451;
SUBCELLULAR LOCATION: Nucleus. Note=Predominantly nuclear.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
Hyperphosphorylation upon ionizing radiation results in
dissociation from BRCA1.
PTM: Ubiquitinated; mediated by SIAH1 and leading to its
subsequent proteasomal degradation (Probable).
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
[LINK]
Links to other databases:
Protein sequence:
MNISGSSCGSPNSADTSSDFKDLWTKLKECHDREVQGLQVKVTKLKQERI
LDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMR
KKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQA
AELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCA
NEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSS
FNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTR
NTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSL
LQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSLGSEVNKIIIQ
SSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKT
EEESEHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAI
QRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSP
GEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVL
DDIKSAGSHEPIKIQTRSDHGGCELASVLQLNPCRTGKIKSLQNNQDVSF
ENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVL
LKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADE
EEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVR
KKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPEN
FWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
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RBBP8 (Homo sapiens) is able to recognize following damages:
RBBP8 (Homo sapiens) belongs to following protein families:
References:
Title
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Authors
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Journal
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Interaction between a cellular protein that binds to the C-terminal region of adenovirus E1A (CtBP) and a novel cellular protein is disrupted by E1A through a conserved PLDLS motif.
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Schaeper U, Subramanian T, Lim L, Boyd JM, Chinnadurai G
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J Biol Chem
April 10, 1998
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Molecular cloning and characterization of a novel retinoblastoma-binding protein.
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Fusco C, Reymond A, Zervos AS
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Genomics
Aug. 1, 1998
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Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor.
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Yu X, Baer R
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J Biol Chem
June 16, 2000
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Functional link of BRCA1 and ataxia telangiectasia gene product in DNA damage response.
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Li S, Ting NS, Zheng L, Chen PL, Ziv Y, Shiloh Y, Lee EY, Lee WH
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Nature
July 13, 2000
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SIAH-1 interacts with CtIP and promotes its degradation by the proteasome pathway.
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Germani A, Prabel A, Mourah S, Podgorniak MP, Di Carlo A, Ehrlich R, Gisselbrecht S, Varin-Blank N, Calvo F, Bruzzoni-Giovanelli H
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Oncogene
Dec. 4, 2003
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Large-scale characterization of HeLa cell nuclear phosphoproteins.
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Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP
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Proc Natl Acad Sci U S A
Aug. 17, 2004
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ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
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Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ
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Science
May 25, 2007
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Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
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Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK
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Sci Signal
Jan. 1, 2009
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Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
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Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S
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Anal Chem
June 1, 2009
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Last modification of this entry: Oct. 11, 2010.
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