CNTRB_HUMAN - dbPTM
CNTRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNTRB_HUMAN
UniProt AC Q8N137
Protein Name Centrobin
Gene Name CNTROB
Organism Homo sapiens (Human).
Sequence Length 903
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Centriole-associated, asymmetrically localizes to the daughter centriole.
Protein Description Required for centriole duplication. Inhibition of centriole duplication leading to defects in cytokinesis..
Protein Sequence MATSADSPSSPLGAEDLLSDSSEPPGLNQVSSEVTSQLYASLRLSRQAEATARAQLYLPSTSPPHEGLDGFAQELSRSLSVGLEKNLKKKDGSKHIFEMESVRGQLQTMLQTSRDTAYRDPLIPGAGSERREEDSFDSDSTATLLNTRPLQDLSPSSSAQALEELFPRYTSLRPGPPLNPPDFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQAHWDEANQLLSTTLPPPNPPAPPAGPSSPGPQEPEKEERRVWTMPPMAVALKPVLQQSREARDELPGAPPVLCSSSSDLSLLLGPSFQSQHSFQPLEPKPDLTSSTAGAFSALGAFHPDHRAERPFPEEDPGPDGEGLLKQGLPPAQLEGLKNFLHQLLETVPQNNENPSVDLLPPKSGPLTVPSWEEAPQVPRIPPPVHKTKVPLAMASSLFRVPEPPSSHSQGSGPSSGSPERGGDGLTFPRQLMEVSQLLRLYQARGWGALPAEDLLLYLKRLEHSGTDGRGDNVPRRNTDSRLGEIPRKEIPSQAVPRRLATAPKTEKPPARKKSGHPAPSSMRSRGGVWR
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
7Phosphorylation-MATSADSPSSPLGA
-CCCCCCCCCCCCCH
26.8028348404
9PhosphorylationATSADSPSSPLGAED
CCCCCCCCCCCCHHH
48.8428348404
10PhosphorylationTSADSPSSPLGAEDL
CCCCCCCCCCCHHHH
27.7728348404
19PhosphorylationLGAEDLLSDSSEPPG
CCHHHHCCCCCCCCC
42.6223401153
21PhosphorylationAEDLLSDSSEPPGLN
HHHHCCCCCCCCCHH
32.9728348404
22PhosphorylationEDLLSDSSEPPGLNQ
HHHCCCCCCCCCHHH
60.1428348404
31PhosphorylationPPGLNQVSSEVTSQL
CCCHHHCCHHHHHHH
15.8323401153
32PhosphorylationPGLNQVSSEVTSQLY
CCHHHCCHHHHHHHH
36.9123401153
35PhosphorylationNQVSSEVTSQLYASL
HHCCHHHHHHHHHHH
13.50-
36PhosphorylationQVSSEVTSQLYASLR
HCCHHHHHHHHHHHH
24.30-
41PhosphorylationVTSQLYASLRLSRQA
HHHHHHHHHHHHHHH
10.6423909892
45PhosphorylationLYASLRLSRQAEATA
HHHHHHHHHHHHHHH
18.8623909892
51PhosphorylationLSRQAEATARAQLYL
HHHHHHHHHHEEEEC
14.2626074081
57PhosphorylationATARAQLYLPSTSPP
HHHHEEEECCCCCCC
12.4125850435
60PhosphorylationRAQLYLPSTSPPHEG
HEEEECCCCCCCCCC
38.6324972180
61PhosphorylationAQLYLPSTSPPHEGL
EEEECCCCCCCCCCH
43.2330183078
62PhosphorylationQLYLPSTSPPHEGLD
EEECCCCCCCCCCHH
40.5523401153
76PhosphorylationDGFAQELSRSLSVGL
HHHHHHHHHHHHHHH
21.0422617229
78PhosphorylationFAQELSRSLSVGLEK
HHHHHHHHHHHHHHH
22.9426657352
80PhosphorylationQELSRSLSVGLEKNL
HHHHHHHHHHHHHHC
18.5223401153
88 (in isoform 2)Ubiquitination-68.14-
94UbiquitinationLKKKDGSKHIFEMES
CCCCCCCCEEEEHHH
46.37-
108PhosphorylationSVRGQLQTMLQTSRD
HHHHHHHHHHHHCCC
28.5730242111
112PhosphorylationQLQTMLQTSRDTAYR
HHHHHHHHCCCCCCC
23.0530242111
113PhosphorylationLQTMLQTSRDTAYRD
HHHHHHHCCCCCCCC
18.3930242111
128PhosphorylationPLIPGAGSERREEDS
CCCCCCCCCCCCCCC
27.6528985074
135PhosphorylationSERREEDSFDSDSTA
CCCCCCCCCCCCCHH
33.9427732954
138PhosphorylationREEDSFDSDSTATLL
CCCCCCCCCCHHHHC
31.3027732954
140PhosphorylationEDSFDSDSTATLLNT
CCCCCCCCHHHHCCC
24.7227732954
141PhosphorylationDSFDSDSTATLLNTR
CCCCCCCHHHHCCCC
28.7527732954
143PhosphorylationFDSDSTATLLNTRPL
CCCCCHHHHCCCCCH
31.6927732954
147PhosphorylationSTATLLNTRPLQDLS
CHHHHCCCCCHHHCC
33.3626657352
154PhosphorylationTRPLQDLSPSSSAQA
CCCHHHCCCCCHHHH
30.9027732954
156PhosphorylationPLQDLSPSSSAQALE
CHHHCCCCCHHHHHH
33.2827732954
157PhosphorylationLQDLSPSSSAQALEE
HHHCCCCCHHHHHHH
32.8327732954
158PhosphorylationQDLSPSSSAQALEEL
HHCCCCCHHHHHHHH
28.8327732954
169PhosphorylationLEELFPRYTSLRPGP
HHHHCHHCCCCCCCC
10.8327642862
170PhosphorylationEELFPRYTSLRPGPP
HHHCHHCCCCCCCCC
23.6727251275
171PhosphorylationELFPRYTSLRPGPPL
HHCHHCCCCCCCCCC
17.2827251275
227MethylationVAVAADRKKDTMIEQ
HHHHHHHCHHHHHHH
56.39115972531
227 (in isoform 2)Ubiquitination-56.39-
228MethylationAVAADRKKDTMIEQL
HHHHHHCHHHHHHHH
60.36115972539
230PhosphorylationAADRKKDTMIEQLDK
HHHHCHHHHHHHHHH
29.0020068231
237UbiquitinationTMIEQLDKTLARVVE
HHHHHHHHHHHHHHC
54.7729967540
258MethylationAERTEVLRGLQEEHQ
HHHHHHHHHHHHHHH
49.29115482163
308PhosphorylationLQQRERETLEEERQA
HHHHHHHHHHHHHHH
45.7722210691
322UbiquitinationALTLRLEAEQQRCCV
HHHHHHHHHHHHHEE
25.2121963094
380UbiquitinationYQALQEESQAQLERE
HHHHHHHHHHHHHHH
30.0221963094
424UbiquitinationGELDTARRERDALQL
CCHHHHHHHHHHHHH
40.6221963094
460PhosphorylationVQLEQRVTERLAQAQ
HHHHHHHHHHHHHHH
19.9924719451
469PhosphorylationRLAQAQESSLRQAAS
HHHHHHHHHHHHHHH
23.6924719451
473UbiquitinationAQESSLRQAASLREH
HHHHHHHHHHHHHHH
46.7222505724
504UbiquitinationASQLAQFKVEMAERE
HHHHHHHHHHHHHHH
25.7929967540
521PhosphorylationQQQVAEDYELRLARE
HHHHHHHHHHHHHHH
14.3627642862
521UbiquitinationQQQVAEDYELRLARE
HHHHHHHHHHHHHHH
14.3621963094
531UbiquitinationRLAREQARVCELQSG
HHHHHHHHHHHCCCC
33.0622505724
544UbiquitinationSGNQQLEEQRVELVE
CCCHHHHHHHHHHHH
52.8921963094
569PhosphorylationDEANQLLSTTLPPPN
HHHHHHHHCCCCCCC
28.1226074081
570PhosphorylationEANQLLSTTLPPPNP
HHHHHHHCCCCCCCC
32.1126074081
571PhosphorylationANQLLSTTLPPPNPP
HHHHHHCCCCCCCCC
33.6126074081
575UbiquitinationLSTTLPPPNPPAPPA
HHCCCCCCCCCCCCC
65.1122505724
585PhosphorylationPAPPAGPSSPGPQEP
CCCCCCCCCCCCCCC
48.5226074081
586PhosphorylationAPPAGPSSPGPQEPE
CCCCCCCCCCCCCCC
36.6926074081
602PhosphorylationEERRVWTMPPMAVAL
HHCCCCCCCHHHHHH
1.7432142685
602UbiquitinationEERRVWTMPPMAVAL
HHCCCCCCCHHHHHH
1.7421963094
610UbiquitinationPPMAVALKPVLQQSR
CHHHHHHHHHHHHHH
24.2821963094
610 (in isoform 2)Ubiquitination-24.28-
646UbiquitinationLLLGPSFQSQHSFQP
HHHCCCCCCCCCCCC
46.6621963094
672UbiquitinationAGAFSALGAFHPDHR
HHHHHHHCCCCCCCC
26.3922505724
698UbiquitinationPDGEGLLKQGLPPAQ
CCCCCHHHCCCCHHH
47.572190698
698 (in isoform 1)Ubiquitination-47.5721906983
698 (in isoform 2)Ubiquitination-47.5721906983
698 (in isoform 3)Ubiquitination-47.5721906983
698 (in isoform 5)Ubiquitination-47.5721906983
699PhosphorylationDGEGLLKQGLPPAQL
CCCCHHHCCCCHHHH
59.6432142685
743PhosphorylationSGPLTVPSWEEAPQV
CCCCCCCCHHHCCCC
42.6626471730
743UbiquitinationSGPLTVPSWEEAPQV
CCCCCCCCHHHCCCC
42.6621963094
761UbiquitinationPPPVHKTKVPLAMAS
CCCCCCCCCCHHHHH
46.8122505724
761 (in isoform 2)Ubiquitination-46.81-
769PhosphorylationVPLAMASSLFRVPEP
CCHHHHHHHCCCCCC
23.2224719451
778PhosphorylationFRVPEPPSSHSQGSG
CCCCCCCCCCCCCCC
51.9330108239
779PhosphorylationRVPEPPSSHSQGSGP
CCCCCCCCCCCCCCC
32.6923663014
781PhosphorylationPEPPSSHSQGSGPSS
CCCCCCCCCCCCCCC
37.8817525332
784PhosphorylationPSSHSQGSGPSSGSP
CCCCCCCCCCCCCCC
39.6323663014
787PhosphorylationHSQGSGPSSGSPERG
CCCCCCCCCCCCCCC
51.3529255136
788PhosphorylationSQGSGPSSGSPERGG
CCCCCCCCCCCCCCC
46.5629255136
790PhosphorylationGSGPSSGSPERGGDG
CCCCCCCCCCCCCCC
26.0729255136
799PhosphorylationERGGDGLTFPRQLME
CCCCCCCCHHHHHHH
36.8027174698
808PhosphorylationPRQLMEVSQLLRLYQ
HHHHHHHHHHHHHHH
11.2124043423
814PhosphorylationVSQLLRLYQARGWGA
HHHHHHHHHHCCCCC
8.16-
832UbiquitinationEDLLLYLKRLEHSGT
HHHHHHHHHHHHCCC
41.1821963094
832 (in isoform 2)Ubiquitination-41.18-
837PhosphorylationYLKRLEHSGTDGRGD
HHHHHHHCCCCCCCC
33.73-
853PhosphorylationVPRRNTDSRLGEIPR
CCCCCCCCCCCCCCH
27.6320860994
861UbiquitinationRLGEIPRKEIPSQAV
CCCCCCHHHCCCCCC
55.4229967540
862UbiquitinationLGEIPRKEIPSQAVP
CCCCCHHHCCCCCCC
62.5029967540
865PhosphorylationIPRKEIPSQAVPRRL
CCHHHCCCCCCCHHH
36.1126074081
883UbiquitinationPKTEKPPARKKSGHP
CCCCCCCCCCCCCCC
44.4429967540
883 (in isoform 2)Ubiquitination-44.44-
887PhosphorylationKPPARKKSGHPAPSS
CCCCCCCCCCCCCCH
45.4224719451
909PhosphorylationWR-------------
CC-------------
24719451

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
35TPhosphorylationKinaseNEK2P51955
PSP
36SPhosphorylationKinaseNEK2P51955
PSP
41SPhosphorylationKinaseNEK2P51955
PSP
45SPhosphorylationKinaseNEK2P51955
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNTRB_HUMAN !!

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 CNTRB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PUR8_HUMANADSLphysical
26638075
ALMS1_HUMANALMS1physical
26638075
AURKA_HUMANAURKAphysical
26638075
BAF_HUMANBANF1physical
26638075
BSN_HUMANBSNphysical
26638075
BTF3_HUMANBTF3physical
26638075
CNO11_HUMANCNOT11physical
26638075
CC85C_HUMANCCDC85Cphysical
26638075
CE120_HUMANCEP120physical
26638075
CEP85_HUMANCEP85physical
26638075
KCRB_HUMANCKBphysical
26638075
CNOT1_HUMANCNOT1physical
26638075
CNO10_HUMANCNOT10physical
26638075
CNOT3_HUMANCNOT3physical
26638075
CNOT7_HUMANCNOT7physical
26638075
CYLD_HUMANCYLDphysical
26638075
DDX54_HUMANDDX54physical
26638075
DESP_HUMANDSPphysical
26638075
ECH1_HUMANECH1physical
26638075
EPIPL_HUMANEPPK1physical
26638075
EXOC4_HUMANEXOC4physical
26638075
FA83H_HUMANFAM83Hphysical
26638075
FERM2_HUMANFERMT2physical
26638075
GGYF1_HUMANGIGYF1physical
26638075
AINX_HUMANINAphysical
26638075
KANK2_HUMANKANK2physical
26638075
SKT_HUMANKIAA1217physical
26638075
CIP2A_HUMANKIAA1524physical
26638075
K1671_HUMANKIAA1671physical
26638075
KIF14_HUMANKIF14physical
26638075
LIMD1_HUMANLIMD1physical
26638075
LRC49_HUMANLRRC49physical
26638075
LUZP1_HUMANLUZP1physical
26638075
M21D2_HUMANMB21D2physical
26638075
MPP9_HUMANMPHOSPH9physical
26638075
MTPN_HUMANMTPNphysical
26638075
NCK5L_HUMANNCKAP5Lphysical
26638075
SPN90_HUMANNCKIPSDphysical
26638075
NEDD1_HUMANNEDD1physical
26638075
NDK7_HUMANNME7physical
26638075
NSA2_HUMANNSA2physical
26638075
NUP88_HUMANNUP88physical
26638075
OFD1_HUMANOFD1physical
26638075
PALLD_HUMANPALLDphysical
26638075
PDD2L_HUMANPDCD2Lphysical
26638075
PHIP_HUMANPHIPphysical
26638075
PLK1_HUMANPLK1physical
26638075
ANM3_HUMANPRMT3physical
26638075
RAB18_HUMANRAB18physical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
RAB35_HUMANRAB35physical
26638075
CNOT9_HUMANRQCD1physical
26638075
SCYL2_HUMANSCYL2physical
26638075
SMAP2_HUMANSMAP2physical
26638075
SMG9_HUMANSMG9physical
26638075
SNP47_HUMANSNAP47physical
26638075
SPAT2_HUMANSPATA2physical
26638075
SSRP1_HUMANSSRP1physical
26638075
STXB4_HUMANSTXBP4physical
26638075
SP16H_HUMANSUPT16Hphysical
26638075
TAB1_HUMANTAB1physical
26638075
TAB2_HUMANTAB2physical
26638075
TBK1_HUMANTBK1physical
26638075
TCHP_HUMANTCHPphysical
26638075
TNR6A_HUMANTNRC6Aphysical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
TNR6C_HUMANTNRC6Cphysical
26638075
ASPP2_HUMANTP53BP2physical
26638075
TPGS1_HUMANTPGS1physical
26638075
TRI37_HUMANTRIM37physical
26638075
TRI62_HUMANTRIM62physical
26638075
TRIP6_HUMANTRIP6physical
26638075
TTF2_HUMANTTF2physical
26638075
TTK_HUMANTTKphysical
26638075
ZN326_HUMANZNF326physical
26638075
NH2L1_HUMANNHP2L1physical
26638075
COPD_HUMANARCN1physical
26496610
CALU_HUMANCALUphysical
26496610
CDK2_HUMANCDK2physical
26496610
IF4G1_HUMANEIF4G1physical
26496610
FACD2_HUMANFANCD2physical
26496610
GOGA3_HUMANGOLGA3physical
26496610
CYR61_HUMANCYR61physical
26496610
M3K4_HUMANMAP3K4physical
26496610
NDUA8_HUMANNDUFA8physical
26496610
RL10_HUMANRPL10physical
26496610
ZYX_HUMANZYXphysical
26496610
ATPK_HUMANATP5J2physical
26496610
RM33_HUMANMRPL33physical
26496610
PDC6I_HUMANPDCD6IPphysical
26496610
HMGX4_HUMANHMGXB4physical
26496610
DNJC8_HUMANDNAJC8physical
26496610
SETX_HUMANSETXphysical
26496610
BRD1_HUMANBRD1physical
26496610
MOCOS_HUMANMOCOSphysical
26496610
WAP53_HUMANWRAP53physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
NBEL1_HUMANNBEAL1physical
26496610
CDC73_HUMANCDC73physical
26496610
RT4I1_HUMANRTN4IP1physical
26496610
PIGS_HUMANPIGSphysical
26496610
EME1_HUMANEME1physical
26496610
ZN800_HUMANZNF800physical
26496610
CENPX_HUMANSTRA13physical
26496610
MSL1_HUMANMSL1physical
26496610
MED11_HUMANMED11physical
26496610

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, AND MASSSPECTROMETRY.

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