CENPJ_HUMAN - dbPTM
CENPJ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPJ_HUMAN
UniProt AC Q9HC77
Protein Name Centromere protein J
Gene Name CENPJ
Organism Homo sapiens (Human).
Sequence Length 1338
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Localized within the center of microtubule asters (PubMed:11003675). During centriole biogenesis, it
Protein Description Plays an important role in cell division and centrosome function by participating in centriole duplication. [PubMed: 17681131]
Protein Sequence MFLMPTSSELNSGQNFLTQWMTNPSRAGVILNRGFPILEADKEKRAAVDISTSFPIKGTHFSDSFSFINEEDSLLEEQKLESNNPYKPQSDKSETHTAFPCIKKGPQVAACHSAPGHQEENKNDFIPDLASEFKEGAYKDPLFKKLEQLKEVQQKKQEQLKRQQLEQLQRLMEEQEKLLTMVSGQCTLPGLSLLPDDQSQKHRSPGNTTTGERATCCFPSYVYPDPTQEETYPSNILSHEQSNFCRTAHGDFVLTSKRASPNLFSEAQYQEAPVEKNNLKEENRNHPTGESILCWEKVTEQIQEANDKNLQKHDDSSEVANIEERPIKAAIGERKQTFEDYLEEQIQLEEQELKQKQLKEAEGPLPIKAKPKQPFLKRGEGLARFTNAKSKFQKGKESKLVTNQSTSEDQPLFKMDRQQLQRKTALKNKELCADNPILKKDSKARTKSGSVTLSQKPKMLKCSNRKSLSPSGLKIQTGKKCDGQFRDQIKFENKVTSNNKENVTECPKPCDTGCTGWNKTQGKDRLPLSTGPASRLAAKSPIRETMKESESSLDVSLQKKLETWEREKEKENLELDEFLFLEQAADEISFSSNSSFVLKILERDQQICKGHRMSSTPVKAVPQKTNPADPISHCNRSEDLDHTAREKESECEVAPKQLHSLSSADELREQPCKIRKAVQKSTSENQTEWNARDDEGVPNSDSSTDSEEQLDVTIKPSTEDRERGISSREDSPQVCDDKGPFKDTRTQEDKRRDVDLDLSDKDYSSDESIMESIKHKVSEPSRSSSLSLSKMDFDDERTWTDLEENLCNHDVVLGNESTYGTPQTCYPNNEIGILDKTIKRKIAPVKRGEDLSKSRRSRSPPTSELMMKFFPSLKPKPKSDSHLGNELKLNISQDQPPGDNARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEKYTTAARTFPDKKEREEIQTLKQQIADLREDLKRKETKWSSTHSRLRSQIQMLVRENTDLREEIKVMERFRLDAWKRAEAIESSLEVEKKDKLANTSVRFQNSQISSGTQVEKYKKNYLPMQGNPPRRSKSAPPRDLGNLDKGQAASPREPLEPLNFPDPEYKEEEEDQDIQGEISHPDGKVEKVYKNGCRVILFPNGTRKEVSADGKTITVTFFNGDVKQVMPDQRVIYYYAAAQTTHTTYPEGLEVLHFSSGQIEKHYPDGRKEITFPDQTVKNLFPDGQEESIFPDGTIVRVQRDGNKLIEFNNGQRELHTAQFKRREYPDGTVKTVYANGHQETKYRSGRIRVKDKEGNVLMDTEL
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
53PhosphorylationAAVDISTSFPIKGTH
CCCEECCCCCCCCCC
23.41-
103UbiquitinationHTAFPCIKKGPQVAA
CCCCCHHCCCCCEEE
59.40-
113PhosphorylationPQVAACHSAPGHQEE
CCEEECCCCCCCCCC
35.72-
131PhosphorylationDFIPDLASEFKEGAY
CCCHHHHHHHHCCCC
51.3624532841
134UbiquitinationPDLASEFKEGAYKDP
HHHHHHHHCCCCCCH
51.71-
150UbiquitinationFKKLEQLKEVQQKKQ
HHHHHHHHHHHHHHH
56.38-
150UbiquitinationFKKLEQLKEVQQKKQ
HHHHHHHHHHHHHHH
56.38-
201UbiquitinationLPDDQSQKHRSPGNT
CCCCCCCCCCCCCCC
46.35-
255PhosphorylationAHGDFVLTSKRASPN
CCCCEEEECCCCCCC
27.2226074081
256PhosphorylationHGDFVLTSKRASPNL
CCCEEEECCCCCCCC
18.9126074081
257UbiquitinationGDFVLTSKRASPNLF
CCEEEECCCCCCCCC
46.91-
260PhosphorylationVLTSKRASPNLFSEA
EEECCCCCCCCCCHH
20.5323401153
265PhosphorylationRASPNLFSEAQYQEA
CCCCCCCCHHHHHCC
34.8829255136
269PhosphorylationNLFSEAQYQEAPVEK
CCCCHHHHHCCCCHH
18.5028796482
297UbiquitinationESILCWEKVTEQIQE
CCCHHHHHHHHHHHH
29.92-
308UbiquitinationQIQEANDKNLQKHDD
HHHHHHHHHHHHCCC
60.40-
316PhosphorylationNLQKHDDSSEVANIE
HHHHCCCCHHCCCHH
34.1625849741
317PhosphorylationLQKHDDSSEVANIEE
HHHCCCCHHCCCHHH
42.9820873877
328UbiquitinationNIEERPIKAAIGERK
CHHHCCHHHHHCCCC
34.15-
337PhosphorylationAIGERKQTFEDYLEE
HHCCCCHHHHHHHHH
31.84-
341PhosphorylationRKQTFEDYLEEQIQL
CCHHHHHHHHHHHHH
14.60-
399UbiquitinationFQKGKESKLVTNQST
HHCCCHHCCCCCCCC
48.33-
402PhosphorylationGKESKLVTNQSTSED
CCHHCCCCCCCCCCC
37.6728842319
405PhosphorylationSKLVTNQSTSEDQPL
HCCCCCCCCCCCCCH
35.6523186163
406PhosphorylationKLVTNQSTSEDQPLF
CCCCCCCCCCCCCHH
26.7724114839
407PhosphorylationLVTNQSTSEDQPLFK
CCCCCCCCCCCCHHH
44.4124114839
448PhosphorylationDSKARTKSGSVTLSQ
CCCCCCCCCCEECCC
35.37-
452PhosphorylationRTKSGSVTLSQKPKM
CCCCCCEECCCCCCE
23.53-
466AcetylationMLKCSNRKSLSPSGL
EEECCCCCCCCCCCC
61.0611924539
467PhosphorylationLKCSNRKSLSPSGLK
EECCCCCCCCCCCCE
30.7325159151
469PhosphorylationCSNRKSLSPSGLKIQ
CCCCCCCCCCCCEEE
24.9025159151
471PhosphorylationNRKSLSPSGLKIQTG
CCCCCCCCCCEEECC
54.0724732914
497PhosphorylationKFENKVTSNNKENVT
EEECCCCCCCCCCCC
41.20-
508UbiquitinationENVTECPKPCDTGCT
CCCCCCCCCCCCCCC
70.68-
519UbiquitinationTGCTGWNKTQGKDRL
CCCCCCCCCCCCCCC
35.40-
529PhosphorylationGKDRLPLSTGPASRL
CCCCCCCCCCHHHHH
29.4028555341
539UbiquitinationPASRLAAKSPIRETM
HHHHHHHCCCHHHHH
51.67-
540PhosphorylationASRLAAKSPIRETMK
HHHHHHCCCHHHHHH
22.3425159151
545PhosphorylationAKSPIRETMKESESS
HCCCHHHHHHHCCCC
24.5623186163
551PhosphorylationETMKESESSLDVSLQ
HHHHHCCCCCCHHHH
45.5426471730
552PhosphorylationTMKESESSLDVSLQK
HHHHCCCCCCHHHHH
25.2422468782
556PhosphorylationSESSLDVSLQKKLET
CCCCCCHHHHHHHHH
25.4219691289
560UbiquitinationLDVSLQKKLETWERE
CCHHHHHHHHHHHHH
38.30-
560UbiquitinationLDVSLQKKLETWERE
CCHHHHHHHHHHHHH
38.30-
589PhosphorylationEQAADEISFSSNSSF
HHHCHHCCCCCCCHH
19.6120531387
595PhosphorylationISFSSNSSFVLKILE
CCCCCCCHHHHHHHH
24.5120531387
614PhosphorylationICKGHRMSSTPVKAV
HHCCCCCCCCCCCCC
30.89-
615PhosphorylationCKGHRMSSTPVKAVP
HCCCCCCCCCCCCCC
27.64-
616PhosphorylationKGHRMSSTPVKAVPQ
CCCCCCCCCCCCCCC
25.46-
624UbiquitinationPVKAVPQKTNPADPI
CCCCCCCCCCCCCCC
44.17-
625PhosphorylationVKAVPQKTNPADPIS
CCCCCCCCCCCCCCC
40.98-
643PhosphorylationRSEDLDHTAREKESE
CCHHCCCHHHHHHHH
27.38-
656UbiquitinationSECEVAPKQLHSLSS
HHCCCCHHHHHCCCC
56.61-
660PhosphorylationVAPKQLHSLSSADEL
CCHHHHHCCCCHHHH
38.2428555341
662PhosphorylationPKQLHSLSSADELRE
HHHHHCCCCHHHHHH
26.8823186163
663PhosphorylationKQLHSLSSADELREQ
HHHHCCCCHHHHHHC
45.0623917254
680UbiquitinationKIRKAVQKSTSENQT
HHHHHHHHCCCCCCC
49.45-
681PhosphorylationIRKAVQKSTSENQTE
HHHHHHHCCCCCCCC
21.78-
682PhosphorylationRKAVQKSTSENQTEW
HHHHHHCCCCCCCCC
47.28-
683PhosphorylationKAVQKSTSENQTEWN
HHHHHCCCCCCCCCC
41.46-
704PhosphorylationVPNSDSSTDSEEQLD
CCCCCCCCCCHHHCC
47.71-
717PhosphorylationLDVTIKPSTEDRERG
CCEEECCCHHHHHCC
39.15-
726PhosphorylationEDRERGISSREDSPQ
HHHHCCCCCCCCCCC
26.6030108239
727PhosphorylationDRERGISSREDSPQV
HHHCCCCCCCCCCCC
37.4630108239
731PhosphorylationGISSREDSPQVCDDK
CCCCCCCCCCCCCCC
16.6921815630
759PhosphorylationRDVDLDLSDKDYSSD
HCCCCCCCCCCCCCC
42.1329255136
763PhosphorylationLDLSDKDYSSDESIM
CCCCCCCCCCCHHHH
18.8021406692
764PhosphorylationDLSDKDYSSDESIME
CCCCCCCCCCHHHHH
41.2522199227
765PhosphorylationLSDKDYSSDESIMES
CCCCCCCCCHHHHHH
38.8922496350
768PhosphorylationKDYSSDESIMESIKH
CCCCCCHHHHHHHHH
32.0222496350
772PhosphorylationSDESIMESIKHKVSE
CCHHHHHHHHHHCCC
21.4021406692
776AcetylationIMESIKHKVSEPSRS
HHHHHHHHCCCCCCC
42.327683477
781PhosphorylationKHKVSEPSRSSSLSL
HHHCCCCCCCCCCCC
40.52-
783PhosphorylationKVSEPSRSSSLSLSK
HCCCCCCCCCCCCCC
28.7228985074
784PhosphorylationVSEPSRSSSLSLSKM
CCCCCCCCCCCCCCC
33.9024719451
785PhosphorylationSEPSRSSSLSLSKMD
CCCCCCCCCCCCCCC
24.1919007248
787PhosphorylationPSRSSSLSLSKMDFD
CCCCCCCCCCCCCCC
32.3223312004
789PhosphorylationRSSSLSLSKMDFDDE
CCCCCCCCCCCCCCC
23.6630576142
790AcetylationSSSLSLSKMDFDDER
CCCCCCCCCCCCCCC
48.027683489
798PhosphorylationMDFDDERTWTDLEEN
CCCCCCCCCCHHHHH
30.57-
800PhosphorylationFDDERTWTDLEENLC
CCCCCCCCHHHHHCC
30.05-
857PhosphorylationDLSKSRRSRSPPTSE
CCCHHCCCCCCCCHH
35.6826055452
859PhosphorylationSKSRRSRSPPTSELM
CHHCCCCCCCCHHHH
36.1626055452
862PhosphorylationRRSRSPPTSELMMKF
CCCCCCCCHHHHHHH
37.9126074081
863PhosphorylationRSRSPPTSELMMKFF
CCCCCCCHHHHHHHC
34.2122115753
888UbiquitinationSHLGNELKLNISQDQ
CCCCCEEEEEECCCC
33.05-
892PhosphorylationNELKLNISQDQPPGD
CEEEEEECCCCCCCC
26.9919691289
915PhosphorylationEKIIELETEIEKFKA
HHHHHHHHHHHHHHH
55.6926074081
929UbiquitinationAENASLAKLRIERES
HHCCHHHHHHHHHHH
43.52-
979UbiquitinationKERKVFEKYTTAART
HHHHHHHHHHHHHHH
36.11-
1000UbiquitinationREEIQTLKQQIADLR
HHHHHHHHHHHHHHH
43.47-
1081PhosphorylationTSVRFQNSQISSGTQ
CEEEECCCCCCCCCC
20.36-
1107PhosphorylationQGNPPRRSKSAPPRD
CCCCCCCCCCCCCCC
32.0423312004
1109PhosphorylationNPPRRSKSAPPRDLG
CCCCCCCCCCCCCCC
47.4516516142
1125PhosphorylationLDKGQAASPREPLEP
CCCCCCCCCCCCCCC
27.7520860994
1253UbiquitinationTFPDQTVKNLFPDGQ
ECCCHHHHHCCCCCC
51.85-
1296UbiquitinationELHTAQFKRREYPDG
EEEEEEECCCCCCCC
38.17-

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
467SPhosphorylationKinaseAURKAO14965
GPS
589SPhosphorylationKinasePLK2Q9NYY3
Uniprot
595SPhosphorylationKinasePLK2Q9NYY3
Uniprot
595SPhosphorylationKinasePLK4O00444
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
589SPhosphorylation

20531387
595SPhosphorylation

20531387
595SPhosphorylation

20531387

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 CENPJ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STA5A_MOUSEStat5aphysical
12198240
TBG1_HUMANTUBG1physical
11003675
41_HUMANEPB41physical
11003675
CBP_HUMANCREBBPphysical
15687488
CBP_HUMANCREBBPgenetic
15687488
CEP55_HUMANCEP55physical
24613305
CP131_HUMANCEP131physical
24613305
NEDD1_HUMANNEDD1physical
24613305
PLK1_HUMANPLK1physical
24613305
CE120_HUMANCEP120physical
24613305
CP110_HUMANCCP110physical
24613305
CEP85_HUMANCEP85physical
24613305
CLAP1_HUMANCLASP1physical
24613305
CKAP2_HUMANCKAP2physical
24613305
MIB1_HUMANMIB1physical
24613305
STIL_HUMANSTILphysical
24613305
TTK_HUMANTTKphysical
24613305
LZTS2_HUMANLZTS2physical
24613305
K1671_HUMANKIAA1671physical
24613305
CEP97_HUMANCEP97physical
24613305
IQEC1_HUMANIQSEC1physical
24613305
KIF14_HUMANKIF14physical
24613305
PCNT_HUMANPCNTphysical
24613305
KIF7_HUMANKIF7physical
24613305
TALD3_HUMANKIAA0586physical
24613305
ALMS1_HUMANALMS1physical
24613305
C2CD3_HUMANC2CD3physical
24613305
CDC7_HUMANCDC7physical
24613305
ABCE1_HUMANABCE1physical
26638075
ABLM1_HUMANABLIM1physical
26638075
PUR8_HUMANADSLphysical
26638075
ALMS1_HUMANALMS1physical
26638075
AP3B1_HUMANAP3B1physical
26638075
AP3D1_HUMANAP3D1physical
26638075
ATX10_HUMANATXN10physical
26638075
CP131_HUMANCEP131physical
26638075
BI2L1_HUMANBAIAP2L1physical
26638075
BTF3_HUMANBTF3physical
26638075
AAR2_HUMANAAR2physical
26638075
CE051_HUMANC5orf51physical
26638075
ARMT1_HUMANC6orf211physical
26638075
RABL6_HUMANRABL6physical
26638075
CAMP1_HUMANCAMSAP1physical
26638075
CAMP2_HUMANCAMSAP2physical
26638075
CC138_HUMANCCDC138physical
26638075
CC85C_HUMANCCDC85Cphysical
26638075
CP110_HUMANCCP110physical
26638075
CENPH_HUMANCENPHphysical
26638075
CE170_HUMANCEP170physical
26638075
CEP76_HUMANCEP76physical
26638075
CEP85_HUMANCEP85physical
26638075
CEP97_HUMANCEP97physical
26638075
KCRB_HUMANCKBphysical
26638075
CLAP1_HUMANCLASP1physical
26638075
CNOT1_HUMANCNOT1physical
26638075
CNO10_HUMANCNOT10physical
26638075
COMD4_HUMANCOMMD4physical
26638075
CSN3_HUMANCOPS3physical
26638075
CRTC3_HUMANCRTC3physical
26638075
CSPP1_HUMANCSPP1physical
26638075
DCP1B_HUMANDCP1Bphysical
26638075
DDX54_HUMANDDX54physical
26638075
DVL3_HUMANDVL3physical
26638075
ENOG_HUMANENO2physical
26638075
WAC2A_HUMANFAM21Aphysical
26638075
FBX22_HUMANFBXO22physical
26638075
FERM2_HUMANFERMT2physical
26638075
GPTC1_HUMANGPATCH1physical
26638075
GPX1_HUMANGPX1physical
26638075
HAUS1_HUMANHAUS1physical
26638075
HAUS3_HUMANHAUS3physical
26638075
HAUS6_HUMANHAUS6physical
26638075
HAUS7_HUMANHAUS7physical
26638075
HAUS8_HUMANHAUS8physical
26638075
IBTK_HUMANIBTKphysical
26638075
IPO9_HUMANIPO9physical
26638075
MOONR_HUMANKIAA0753physical
26638075
KIF14_HUMANKIF14physical
26638075
LRC49_HUMANLRRC49physical
26638075
MARE2_HUMANMAPRE2physical
26638075
M21D2_HUMANMB21D2physical
26638075
AF10_HUMANMLLT10physical
26638075
PHOCN_HUMANMOB4physical
26638075
MPP9_HUMANMPHOSPH9physical
26638075
NAA10_HUMANNAA10physical
26638075
NEDD1_HUMANNEDD1physical
26638075
OFD1_HUMANOFD1physical
26638075
PALLD_HUMANPALLDphysical
26638075
PCM1_HUMANPCM1physical
26638075
PFD4_HUMANPFDN4physical
26638075
PKN2_HUMANPKN2physical
26638075
PLK1_HUMANPLK1physical
26638075
PRS6B_HUMANPSMC4physical
26638075
PTN12_HUMANPTPN12physical
26638075
RAB18_HUMANRAB18physical
26638075
TF65_HUMANRELAphysical
26638075
RFC5_HUMANRFC5physical
26638075
RIOK2_HUMANRIOK2physical
26638075
SDCG3_HUMANSDCCAG3physical
26638075
SC16A_HUMANSEC16Aphysical
26638075
SC23A_HUMANSEC23Aphysical
26638075
SC23B_HUMANSEC23Bphysical
26638075
SC24B_HUMANSEC24Bphysical
26638075
SMG7_HUMANSMG7physical
26638075
SNX27_HUMANSNX27physical
26638075
ADIP_HUMANSSX2IPphysical
26638075
TCHP_HUMANTCHPphysical
26638075
TNIP1_HUMANTNIP1physical
26638075
TNR6A_HUMANTNRC6Aphysical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
ASPP2_HUMANTP53BP2physical
26638075
TPGS1_HUMANTPGS1physical
26638075
TRIO_HUMANTRIOphysical
26638075
TTK_HUMANTTKphysical
26638075
UN45A_HUMANUNC45Aphysical
26638075
VCIP1_HUMANVCPIP1physical
26638075
WRP73_HUMANWRAP73physical
26638075
XRN1_HUMANXRN1physical
26638075
1433E_HUMANYWHAEphysical
26638075
1433G_HUMANYWHAGphysical
26638075
1433F_HUMANYWHAHphysical
26638075
NAB1_HUMANNAB1physical
26496610
PCM1_HUMANPCM1physical
26496610
1433B_HUMANYWHABphysical
26496610
1433F_HUMANYWHAHphysical
26496610
CP110_HUMANCCP110physical
26496610
CP131_HUMANCEP131physical
26496610
CLAP2_HUMANCLASP2physical
26496610
CLAP1_HUMANCLASP1physical
26496610
GEMI5_HUMANGEMIN5physical
26496610
PPHLN_HUMANPPHLN1physical
26496610
CRTC3_HUMANCRTC3physical
26496610
KLC2_HUMANKLC2physical
26496610
PRR3_HUMANPRR3physical
26496610
DLRB1_HUMANDYNLRB1physical
26496610
PHLB3_HUMANPHLDB3physical
26496610

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608393Microcephaly 6, primary, autosomal recessive (MCPH6)
613676Seckel syndrome 4 (SCKL4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CENPJ_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"PLK2 phosphorylation is critical for CPAP function in procentrioleformation during the centrosome cycle.";
Chang J., Cizmecioglu O., Hoffmann I., Rhee K.;
EMBO J. 29:2395-2406(2010).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-589 ANDSER-595, AND MUTAGENESIS OF SER-589 AND SER-595.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785 AND SER-892, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1109, AND MASSSPECTROMETRY.

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