CTIP_HUMAN - dbPTM
CTIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTIP_HUMAN
UniProt AC Q99708
Protein Name DNA endonuclease RBBP8
Gene Name RBBP8
Organism Homo sapiens (Human).
Sequence Length 897
Subcellular Localization Nucleus . Chromosome . Associates with sites of DNA damage in S/G2 phase (PubMed:10764811, PubMed:25349192). Ubiquitinated RBBP8 binds to chromatin following DNA damage (PubMed:16818604).
Protein Description Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage. [PubMed: 10764811]
Protein Sequence MNISGSSCGSPNSADTSSDFKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSLGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEEESEHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNPCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MNISGSSCGSP
----CCCCCCCCCCC
26074081
6Phosphorylation--MNISGSSCGSPNS
--CCCCCCCCCCCCC
26074081
7Phosphorylation-MNISGSSCGSPNSA
-CCCCCCCCCCCCCC
23401153
10PhosphorylationISGSSCGSPNSADTS
CCCCCCCCCCCCCCC
25159151
13PhosphorylationSSCGSPNSADTSSDF
CCCCCCCCCCCCHHH
28985074
16PhosphorylationGSPNSADTSSDFKDL
CCCCCCCCCHHHHHH
26074081
17PhosphorylationSPNSADTSSDFKDLW
CCCCCCCCHHHHHHH
26074081
18PhosphorylationPNSADTSSDFKDLWT
CCCCCCCHHHHHHHH
26074081
25PhosphorylationSDFKDLWTKLKECHD
HHHHHHHHHHHHHHH
26074081
62SumoylationRLEEFFTKNQQLREQ
HHHHHHHHHHHHHHH
28112733
62UbiquitinationRLEEFFTKNQQLREQ
HHHHHHHHHHHHHHH
-
115SumoylationNIRQQNLKLITELMN
HHHHHHHHHHHHHHH
-
115SumoylationNIRQQNLKLITELMN
HHHHHHHHHHHHHHH
28112733
126PhosphorylationELMNERNTLQEENKK
HHHHHHHHHHHHHHH
-
163PhosphorylationEEDVIPDSPITAFSF
CCCCCCCCCCEEEEE
30266825
166PhosphorylationVIPDSPITAFSFSGV
CCCCCCCEEEEECCH
30266825
169PhosphorylationDSPITAFSFSGVNRL
CCCCEEEEECCHHHH
30266825
171PhosphorylationPITAFSFSGVNRLRR
CCEEEEECCHHHHHC
27251275
193SumoylationYIEQTHTKLEHSVCA
HEHHHCCHHHHHHHH
28112733
227PhosphorylationNEILVADTYDQSQSP
CCEEEEECCCCCCCC
30576142
228PhosphorylationEILVADTYDQSQSPM
CEEEEECCCCCCCCC
30576142
231PhosphorylationVADTYDQSQSPMAKA
EEECCCCCCCCCHHH
30576142
233PhosphorylationDTYDQSQSPMAKAHG
ECCCCCCCCCHHHCC
23401153
241PhosphorylationPMAKAHGTSSYTPDK
CCHHHCCCCCCCCCC
22115753
242PhosphorylationMAKAHGTSSYTPDKS
CHHHCCCCCCCCCCH
29396449
243PhosphorylationAKAHGTSSYTPDKSS
HHHCCCCCCCCCCHH
25159151
244PhosphorylationKAHGTSSYTPDKSSF
HHCCCCCCCCCCHHC
27251275
245PhosphorylationAHGTSSYTPDKSSFN
HCCCCCCCCCCHHCC
25159151
249PhosphorylationSSYTPDKSSFNLATV
CCCCCCCHHCCHHHH
25332170
269PhosphorylationGLGVQEESETQGPMS
CCCCCCCCCCCCCCC
27251275
271PhosphorylationGVQEESETQGPMSPL
CCCCCCCCCCCCCCC
27251275
276PhosphorylationSETQGPMSPLGDELY
CCCCCCCCCCHHHHH
26074081
302PhosphorylationFEESTRNTEDSLRFS
CCHHCCCCHHHCCCC
20873877
305PhosphorylationSTRNTEDSLRFSDST
HCCCCHHHCCCCCCC
20873877
309PhosphorylationTEDSLRFSDSTSKTP
CHHHCCCCCCCCCCC
29255136
311PhosphorylationDSLRFSDSTSKTPPQ
HHCCCCCCCCCCCCH
29255136
312PhosphorylationSLRFSDSTSKTPPQE
HCCCCCCCCCCCCHH
29255136
313PhosphorylationLRFSDSTSKTPPQEE
CCCCCCCCCCCCHHH
29255136
314UbiquitinationRFSDSTSKTPPQEEL
CCCCCCCCCCCHHHC
-
315PhosphorylationFSDSTSKTPPQEELP
CCCCCCCCCCHHHCC
23401153
323PhosphorylationPPQEELPTRVSSPVF
CCHHHCCCCCCCCCC
23401153
326PhosphorylationEELPTRVSSPVFGAT
HHCCCCCCCCCCCCC
23927012
327PhosphorylationELPTRVSSPVFGATS
HCCCCCCCCCCCCCC
25159151
333PhosphorylationSSPVFGATSSIKSGL
CCCCCCCCCCCCCCC
23927012
334PhosphorylationSPVFGATSSIKSGLD
CCCCCCCCCCCCCCC
23927012
335PhosphorylationPVFGATSSIKSGLDL
CCCCCCCCCCCCCCC
23927012
338PhosphorylationGATSSIKSGLDLNTS
CCCCCCCCCCCCCCC
22199227
344PhosphorylationKSGLDLNTSLSPSLL
CCCCCCCCCCCHHHC
30266825
345PhosphorylationSGLDLNTSLSPSLLQ
CCCCCCCCCCHHHCC
30266825
347PhosphorylationLDLNTSLSPSLLQPG
CCCCCCCCHHHCCCC
30266825
349PhosphorylationLNTSLSPSLLQPGKK
CCCCCCHHHCCCCCC
30266825
360SumoylationPGKKKHLKTLPFSNT
CCCCCCCCCCCCCHH
28112733
360UbiquitinationPGKKKHLKTLPFSNT
CCCCCCCCCCCCCHH
-
361PhosphorylationGKKKHLKTLPFSNTC
CCCCCCCCCCCCHHH
-
375PhosphorylationCISRLEKTRSKSEDS
HHHHHHHHCCCCCCC
29632367
377PhosphorylationSRLEKTRSKSEDSAL
HHHHHHCCCCCCCHH
29632367
378SumoylationRLEKTRSKSEDSALF
HHHHHCCCCCCCHHH
-
378SumoylationRLEKTRSKSEDSALF
HHHHHCCCCCCCHHH
28112733
378UbiquitinationRLEKTRSKSEDSALF
HHHHHCCCCCCCHHH
-
379PhosphorylationLEKTRSKSEDSALFT
HHHHCCCCCCCHHHC
25159151
382PhosphorylationTRSKSEDSALFTHHS
HCCCCCCCHHHCHHC
29632367
386PhosphorylationSEDSALFTHHSLGSE
CCCCHHHCHHCCCHH
29632367
389PhosphorylationSALFTHHSLGSEVNK
CHHHCHHCCCHHHHE
29632367
392PhosphorylationFTHHSLGSEVNKIII
HCHHCCCHHHHEEEE
29978859
396SumoylationSLGSEVNKIIIQSSN
CCCHHHHEEEEECCC
28112733
404SumoylationIIIQSSNKQILINKN
EEEECCCCEEEECCC
28112733
410SumoylationNKQILINKNISESLG
CCEEEECCCHHHHHC
28112733
410UbiquitinationNKQILINKNISESLG
CCEEEECCCHHHHHC
-
422PhosphorylationSLGEQNRTEYGKDSN
HHCCCCCHHHCCCCC
-
424PhosphorylationGEQNRTEYGKDSNTD
CCCCCHHHCCCCCCH
-
428PhosphorylationRTEYGKDSNTDKHLE
CHHHCCCCCCHHHHH
-
432AcetylationGKDSNTDKHLEPLKS
CCCCCCHHHHHHHHH
20829486
438SumoylationDKHLEPLKSLGGRTS
HHHHHHHHHCCCCCC
-
438SumoylationDKHLEPLKSLGGRTS
HHHHHHHHHCCCCCC
28112733
438UbiquitinationDKHLEPLKSLGGRTS
HHHHHHHHHCCCCCC
-
439PhosphorylationKHLEPLKSLGGRTSK
HHHHHHHHCCCCCCC
24719451
449SumoylationGRTSKRKKTEEESEH
CCCCCCCCCHHHHCC
-
449SumoylationGRTSKRKKTEEESEH
CCCCCCCCCHHHHCC
28112733
450PhosphorylationRTSKRKKTEEESEHE
CCCCCCCCHHHHCCC
27251275
454PhosphorylationRKKTEEESEHEVSCP
CCCCHHHHCCCCCCC
27251275
467UbiquitinationCPQASFDKENAFPFP
CCCCCCCCCCCCCCC
27561354
513AcetylationSQGSETSKNKFRQVT
HCCCCCCHHHHHHHH
67251203
515AcetylationGSETSKNKFRQVTLY
CCCCCHHHHHHHHHH
67251201
522PhosphorylationKFRQVTLYEALKTIP
HHHHHHHHHHHHHCC
-
526AcetylationVTLYEALKTIPKGFS
HHHHHHHHHCCCCCC
20829486
526SumoylationVTLYEALKTIPKGFS
HHHHHHHHHCCCCCC
28112733
526UbiquitinationVTLYEALKTIPKGFS
HHHHHHHHHCCCCCC
20829486
527O-linked_GlycosylationTLYEALKTIPKGFSS
HHHHHHHHCCCCCCC
31492838
530SumoylationEALKTIPKGFSSSRK
HHHHHCCCCCCCCCC
28112733
530UbiquitinationEALKTIPKGFSSSRK
HHHHHCCCCCCCCCC
-
533PhosphorylationKTIPKGFSSSRKASD
HHCCCCCCCCCCCCC
23882029
534PhosphorylationTIPKGFSSSRKASDG
HCCCCCCCCCCCCCC
23882029
535PhosphorylationIPKGFSSSRKASDGN
CCCCCCCCCCCCCCC
23882029
539PhosphorylationFSSSRKASDGNCTLP
CCCCCCCCCCCCCCC
24247654
544PhosphorylationKASDGNCTLPKDSPG
CCCCCCCCCCCCCCC
23882029
549PhosphorylationNCTLPKDSPGEPCSQ
CCCCCCCCCCCCCCC
25159151
555PhosphorylationDSPGEPCSQECIILQ
CCCCCCCCCEEEEEE
30576142
568PhosphorylationLQPLNKCSPDNKPSL
EEECHHCCCCCCCCC
20873877
572SumoylationNKCSPDNKPSLQIKE
HHCCCCCCCCCEEEC
28112733
574PhosphorylationCSPDNKPSLQIKEEN
CCCCCCCCCEEECCC
26074081
578SumoylationNKPSLQIKEENAVFK
CCCCCEEECCCEEEE
-
578SumoylationNKPSLQIKEENAVFK
CCCCCEEECCCEEEE
28112733
585UbiquitinationKEENAVFKIPLRPRE
ECCCEEEEEECCCHH
-
593PhosphorylationIPLRPRESLETENVL
EECCCHHHCCCCCHH
28355574
596PhosphorylationRPRESLETENVLDDI
CCHHHCCCCCHHHHH
27251275
604SumoylationENVLDDIKSAGSHEP
CCHHHHHHHCCCCCC
-
604AcetylationENVLDDIKSAGSHEP
CCHHHHHHHCCCCCC
20829486
604SumoylationENVLDDIKSAGSHEP
CCHHHHHHHCCCCCC
20829486
604UbiquitinationENVLDDIKSAGSHEP
CCHHHHHHHCCCCCC
20829486
604 (in isoform 2)Ubiquitination--
613SumoylationAGSHEPIKIQTRSDH
CCCCCCEEEEECCCC
28112733
613UbiquitinationAGSHEPIKIQTRSDH
CCCCCCEEEEECCCC
-
638SumoylationLNPCRTGKIKSLQNN
CCCCCCCCCCCCCCC
28112733
640SumoylationPCRTGKIKSLQNNQD
CCCCCCCCCCCCCCC
28112733
640UbiquitinationPCRTGKIKSLQNNQD
CCCCCCCCCCCCCCC
-
649PhosphorylationLQNNQDVSFENIQWS
CCCCCCCCEEEEEEE
27251275
664PhosphorylationIDPGADLSQYKMDVT
ECCCCCHHHCEEEEE
11689934
676SumoylationDVTVIDTKDGSQSKL
EEEEEECCCCCCCCC
28112733
679PhosphorylationVIDTKDGSQSKLGGE
EEECCCCCCCCCCCE
17525332
693PhosphorylationETVDMDCTLVSETVL
EECCCCCEEEEHHHH
-
714PhosphorylationEQKGEKSSNEERKMN
HHHCCCCCHHHHHHH
28787133
719SumoylationKSSNEERKMNDSLED
CCCHHHHHHHHHHHH
28112733
723PhosphorylationEERKMNDSLEDMFDR
HHHHHHHHHHHHHHC
25159151
731PhosphorylationLEDMFDRTTHEEYES
HHHHHHCCHHHHHHH
-
743PhosphorylationYESCLADSFSQAADE
HHHHHHHHHHHHCCH
30576142
745PhosphorylationSCLADSFSQAADEEE
HHHHHHHHHHCCHHH
11689934
755PhosphorylationADEEEELSTATKKLH
CCHHHHHHHHHHHHH
30576142
756PhosphorylationDEEEELSTATKKLHT
CHHHHHHHHHHHHHH
30576142
760UbiquitinationELSTATKKLHTHGDK
HHHHHHHHHHHCCCC
-
774SumoylationKQDKVKQKAFVEPYF
CCHHHHHHHHCCCCC
-
774SumoylationKQDKVKQKAFVEPYF
CCHHHHHHHHCCCCC
-
782SumoylationAFVEPYFKGDERETS
HHCCCCCCCCCCCHH
28112733
782UbiquitinationAFVEPYFKGDERETS
HHCCCCCCCCCCCHH
-
788PhosphorylationFKGDERETSLQNFPH
CCCCCCCHHHHCCCC
20873877
789PhosphorylationKGDERETSLQNFPHI
CCCCCCHHHHCCCCE
20873877
836PhosphorylationEKKLASCSRHRFRYI
HHHHHHCCCCCCCCC
23532336
847PhosphorylationFRYIPPNTPENFWEV
CCCCCCCCCCCCCCC
26502057
859PhosphorylationWEVGFPSTQTCMERG
CCCCCCCHHHHHHCC
-
869SumoylationCMERGYIKEDLDPCP
HHHCCCCCCCCCCCC
-
869SumoylationCMERGYIKEDLDPCP
HHHCCCCCCCCCCCC
28112733
884PhosphorylationRPKRRQPYNAIFSPK
CCCCCCCCCCCCCCC
30576142
889PhosphorylationQPYNAIFSPKGKEQK
CCCCCCCCCCCCCCC
28985074

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
126TPhosphorylationKinasePKMP14618
PSP
315TPhosphorylationKinaseCDK2P24941
Uniprot
327SPhosphorylationKinaseAURAO14965
PSP
327SPhosphorylationKinaseCDK1P06493
PSP
593SPhosphorylationKinaseAURAO14965
PSP
664SPhosphorylationKinaseATMQ13315
Uniprot
693TPhosphorylationKinasePLK1P53350
PSP
723SPhosphorylationKinasePLK1P53350
PSP
731TPhosphorylationKinasePLK1P53350
PSP
745SPhosphorylationKinaseATMQ13315
Uniprot
847TPhosphorylationKinaseCDK1P06493
Uniprot
847TPhosphorylationKinaseCDK2P24941
PSP
859TPhosphorylationKinaseATRQ13535
PSP
-KUbiquitinationE3 ubiquitin ligaseBRCA1P38398
PMID:16818604
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:14654780
-KUbiquitinationE3 ubiquitin ligaseRNF138Q8WVD3
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseKLHL15Q96M94
PMID:27561354

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

27561354
276SPhosphorylation

23623683
315TPhosphorylation

23186163
315TPhosphorylation

23186163
327SPhosphorylation

15485915
847TPhosphorylation

19202191

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CTIP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBL1_HUMANRBL1physical
9721205
LMO4_HUMANLMO4physical
11751867
HID1_HUMANHID1physical
16189514
FXR2_HUMANFXR2physical
16189514
NTAQ1_HUMANWDYHV1physical
16189514
RBL1_HUMANRBL1physical
16189514
BRCA1_HUMANBRCA1physical
10910365
CTIP_HUMANRBBP8physical
15084581
IKZF1_HUMANIKZF1physical
11959865
RBL2_HUMANRBL2physical
10449734
SIAH1_HUMANSIAH1physical
14654780
BRCA1_HUMANBRCA1physical
10764811
CTBP1_HUMANCTBP1physical
9535825
RB_HUMANRB1physical
9721205
RBL2_HUMANRBL2physical
9721205
RB_HUMANRB1physical
16581787
BARD1_HUMANBARD1physical
16391231
BARD1_HUMANBARD1physical
20351172
BRCA1_HUMANBRCA1physical
20351172
ZN350_HUMANZNF350physical
16843262
BRCA1_HUMANBRCA1physical
16843262
ATM_HUMANATMphysical
10910365
BRCA1_HUMANBRCA1physical
11689934
NBN_HUMANNBNphysical
18171670
PCNA_HUMANPCNAphysical
19342888
RGS17_HUMANRGS17physical
21988832
TMM54_HUMANTMEM54physical
21988832
LMO4_HUMANLMO4physical
25416956
FZR1_HUMANFZR1physical
25349192
MRE11_HUMANMRE11Aphysical
25349192
FACD2_HUMANFANCD2physical
24556218
BRCA1_HUMANBRCA1physical
25310973
UBP4_HUMANUSP4physical
26455393
EXD2_HUMANEXD2physical
26807646
EXO1_HUMANEXO1physical
26807646
MRE11_HUMANMRE11Aphysical
26807646
CTBP1_HUMANCTBP1physical
26807646
CTBP2_HUMANCTBP2physical
26807646
BRCA1_HUMANBRCA1physical
26387952
LMO4_HUMANLMO4physical
26387952
NBN_HUMANNBNphysical
26387952
BRX1_HUMANBRIX1physical
26387952
DEF1_HUMANDEFA1physical
26387952
UBP4_HUMANUSP4physical
26387952
SIAH1_HUMANSIAH1physical
26387952
MRE11_HUMANMRE11Aphysical
26387952
XRCC1_HUMANXRCC1physical
26387952
FACD2_HUMANFANCD2physical
24794434
FACD2_HUMANFANCD2genetic
24794434
UBC_HUMANUBCphysical
24794434
FACD2_HUMANFANCD2physical
24794430
FACD2_HUMANFANCD2genetic
24794430
KLH15_HUMANKLHL15physical
27561354
CUL3_HUMANCUL3physical
27561354
MRE11_HUMANMRE11Aphysical
27561354
NBN_HUMANNBNphysical
27561354

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTIP_HUMAN

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Related Literatures of Post-Translational Modification

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