Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
CtIP (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CtIP a transcription factor containing C2H2 zinc fingers. May modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. Interacts with CTBP, with the C-terminal (BRCT) domains of BRCA1, and with the retinoblastoma protein. Abundantly expressed in brain and the immune system and associated with immune system malignancies. Ionizing radiation induces its hyperphosphorylation and dissociation from BRCA1 in an ATM-dependent manner. Note: This description may include information from UniProtKB.
Protein type: Transcription, coactivator/corepressor; EC 3.1.-.-
Cellular Component: transcriptional repressor complex; nucleolus; nucleus
Molecular Function: protein binding; single-stranded DNA specific endodeoxyribonuclease activity; damaged DNA binding
Biological Process: regulation of transcription from RNA polymerase II promoter; mitosis; meiosis; blastocyst hatching; negative regulation of transcription from RNA polymerase II promoter; DNA repair; G2/M transition DNA damage checkpoint; DNA catabolic process, endonucleolytic; cell cycle checkpoint; double-strand break repair via homologous recombination; G1/S transition of mitotic cell cycle
Reference #:  Q99708 (UniProtKB)
Alt. Names/Synonyms: CtBP-interacting protein; CTIP; RBBP-8; RBBP8; retinoblastoma binding protein 8; Retinoblastoma-binding protein 8; retinoblastoma-interacting myosin-like; Retinoblastoma-interacting protein and myosin-like; RIM
Gene Symbols: RBBP8
Molecular weight: 101,942 Da
Basal Isoelectric point: 5.92  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CtIP

Protein Structure Not Found.


STRING  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho.ELM  |  NetworKIN  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  InnateDB


Sites Implicated In
cell cycle regulation: S327‑p, T847‑p
chromatin organization, altered: T847‑p
molecular association, regulation: S327‑p, S664‑p, S745‑p, T859‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S10-p ISGSSCGsPNSADTs
0 1 S17-p sPNSADTssDFKDLW
0 1 S18-p PNSADTssDFKDLWT
1 0 S231-p VADTYDQsQsPMAKA
0 5 S233-p DTYDQsQsPMAKAHG
2 0 S276-p SETQGPMsPLGDELY
0 2 K314 RFSDSTSKtPPQEEL
2 4 T315-p FSDSTSKtPPQEELP
0 1 T323-p PPQEELPtRVssPVF
0 2 S326-p EELPtRVssPVFGAT
3 9 S327-p ELPtRVssPVFGATS
0 1 S345-p SGLDLNTsLsPsLLQ
1 2 S347-p LDLNTsLsPsLLQPG
0 1 S349-p LNTsLsPsLLQPGKK
0 3 T361-p GKKKHLKtLPFSNTC
0 2 S379-p LEKTRSKsEDSALFT
0 1 T422-p SLGEQNRtEyGKDsN
0 1 Y424-p GEQNRtEyGKDsNTD
0 1 S428-p RtEyGKDsNTDkHLE
1 0 K432-ac GKDsNTDkHLEPLKS
0 1 T450-p RTSKRKKtEEESEHE
1 0 K513-ac SQGSETSkNkFRQVT
1 0 K515-ac GSETSkNkFRQVTLy
0 6 Y522-p kFRQVTLyEALkTIP
1 0 K526-ac VTLyEALkTIPKGFS
0 2 S555-p DSPGEPCsQECIILQ
0 2 I586 EENAVFKIPLRPREs
0 2 P590 VFKIPLRPREsLETE
0 7 S593-p IPLRPREsLETENVL
0 1 T596 RPREsLETENVLDDI
1 0 K604-ac ENVLDDIkSAGSHEP
2 0 S664-p IDPGADLsQYKMDVT
0 1 S679-p VIDTKDGsQSKLGGE
0 5 S723-p EERKMNDsLEDMFDR
2 2 S745-p SCLADSFsQAADEEE
2 1 T847-p FRYIPPNtPENFWEV
2 0 T859-p WEVGFPStQTCMERG
0 1 C875 IKEDLDPCPRPKRRQ
  CtIP iso3  
S10 ISGSSCGSPNSADTS
S17 SPNSADTSSDFKDLW
S18 PNSADTSSDFKDLWT
S231 VADTYDQSQSPMAKA
S233 DTYDQSQSPMAKAHG
S276 SETQGPMSPLGDELY
K314 RFSDSTSKTPPQEEL
T315 FSDSTSKTPPQEELP
T323 PPQEELPTRVSSPVF
S326 EELPTRVSSPVFGAT
S327 ELPTRVSSPVFGATS
S345 SGLDLNTSLSPSLLQ
S347 LDLNTSLSPSLLQPG
S349 LNTSLSPSLLQPGKK
T361 GKKKHLKTLPFSNTC
S379 LEKTRSKSEDSALFT
T422 SLGEQNRTEYGKDSN
Y424 GEQNRTEYGKDSNTD
S428 RTEYGKDSNTDKHLE
K432 GKDSNTDKHLEPLKS
T450 RTSKRKKTEEESEHE
K513 SQGSETSKNKFRQVT
K515 GSETSKNKFRQVTLY
Y522 KFRQVTLYEALKTIP
K526 VTLYEALKTIPKGFS
S555 DSPGEPCSQECIILQ
I586 EENAVFKIPLRPRES
P590 VFKIPLRPRESLETE
S593 IPLRPRESLETENVL
T596 RPRESLETENVLDDI
K604 ENVLDDIKSAGSHEP
S664 IDPGADLSQYKMDVT
S679 VIDTKDGSQSKLGGE
S723 EERKMNDSLEDMFDR
S745 SCLADSFSQAADEEE
- gap
- gap
- gap
  mouse

 
S10 ISGSGCGSPNSADAS
S17 SPNSADASNDFKELW
N18 PNSADASNDFKELWT
N231 VADTCDQNHsPLSKI
S233-p DTCDQNHsPLSKICE
S276 SEPQGPMSPLGSELY
K314-ac RFSDSASktPPQEFT
T315-p FSDSASktPPQEFTT
T322 tPPQEFTTRASsPVF
S325 QEFTTRASsPVFGAT
S326-p EFTTRASsPVFGATS
S344 AHLGLNTSFSPSLLD
S346 LGLNTSFSPSLLDIG
S348 LNTSFSPSLLDIGKK
T360 GKKNLLKTAPFSNIA
S378-p SEKVRSKsEDNALFT
A421 SVDEQCSADHMNTTV
H423 DEQCSADHMNTTVAD
T427 SADHMNTTVADKYLV
K431 MNTTVADKYLVPLKS
T449 KASKRKRTEEESEHA
K512 NHGNETSKNKLKQAT
K514 GNETSKNKLKQATIY
Y521 KLKQATIYEALKPIP
K525 ATIYEALKPIPKGSS
C553 KDSWETYCLQPRSLQ
T584-p EENPVFKtPPCsQEs
S588-p VFKtPPCsQEsLEtE
S591-p tPPCsQEsLEtENLF
T594-p CsQEsLEtENLFGDV
K602 ENLFGDVKGTGSLVP
S662 VDPGADLSQYKMDVT
S677 VIDTKDSSHSRLGGE
S720-p GDIKMNDsLEDMFDR
S742 SCLADSFSQVPDEEE
T843 FRYIPPNTPENFWEV
T855 WEVGFPSTQTCLERG
S871-p IKEDLDLsPRPKRRQ
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.