CENPA_HUMAN - dbPTM
CENPA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPA_HUMAN
UniProt AC P49450
Protein Name Histone H3-like centromeric protein A
Gene Name CENPA
Organism Homo sapiens (Human).
Sequence Length 140
Subcellular Localization Nucleus . Chromosome, centromere, kinetochore . Chromosome, centromere . Localizes exclusively in the kinetochore domain of centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constric
Protein Description Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. [PubMed: 7962047]
Protein Sequence MGPRRRSRKPEAPRRRSPSPTPTPGPSRRGPSLGASSHQHSRRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTLFPKDVQLARRIRGLEEGLG
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
2Methylation------MGPRRRSRK
------CCCCCCCCC
25.1526543159
7Phosphorylation-MGPRRRSRKPEAPR
-CCCCCCCCCCCCCC
42.7326055452
17PhosphorylationPEAPRRRSPSPTPTP
CCCCCCCCCCCCCCC
28.1129255136
17 (in isoform 2)Phosphorylation-28.11-
19 (in isoform 2)Phosphorylation-42.52-
19PhosphorylationAPRRRSPSPTPTPGP
CCCCCCCCCCCCCCC
42.5229255136
21PhosphorylationRRRSPSPTPTPGPSR
CCCCCCCCCCCCCCC
44.1029255136
21 (in isoform 2)Phosphorylation-44.10-
23PhosphorylationRSPSPTPTPGPSRRG
CCCCCCCCCCCCCCC
43.2730266825
23 (in isoform 2)Phosphorylation-43.27-
27PhosphorylationPTPTPGPSRRGPSLG
CCCCCCCCCCCCCCC
40.2922167270
27 (in isoform 2)Phosphorylation-40.29-
32PhosphorylationGPSRRGPSLGASSHQ
CCCCCCCCCCCCCHH
42.1130576142
36PhosphorylationRGPSLGASSHQHSRR
CCCCCCCCCHHHHHH
26.9330576142
37PhosphorylationGPSLGASSHQHSRRR
CCCCCCCCHHHHHHH
26.9923927012
41PhosphorylationGASSHQHSRRRQGWL
CCCCHHHHHHHHHHH
22.4023927012
42MethylationASSHQHSRRRQGWLK
CCCHHHHHHHHHHHH
35.36-
68PhosphorylationLIRKLPFSRLAREIC
HHHHCCHHHHHHHHH
25.1711756469
124UbiquitinationGRVTLFPKDVQLARR
CCEEECHHHHHHHHH
64.30-

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
7SPhosphorylationKinaseAURAO14965
PSP
7SPhosphorylationKinaseAURBQ96GD4
PSP
19SPhosphorylationKinaseCDK2P24941
PSP
68SPhosphorylationKinaseCDK1P06493
PSP
-KUbiquitinationE3 ubiquitin ligaseICP0P08393
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1MMethylation

23818633
7SPhosphorylation

11756469
68SPhosphorylation

25556658
68SPhosphorylation

25556658

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 CENPA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZC3HD_HUMANZC3H13physical
15009096
RSF1_HUMANRSF1physical
15009096
VIR_HUMANKIAA1429physical
15009096
PHIP_HUMANPHIPphysical
15009096
SMCA5_HUMANSMARCA5physical
15009096
DDB1_HUMANDDB1physical
15009096
SRRT_HUMANSRRTphysical
15009096
KIF23_HUMANKIF23physical
15009096
ZFP91_HUMANZFP91physical
15009096
SHCBP_HUMANSHCBP1physical
15009096
CENPB_HUMANCENPBphysical
15009096
HSP7C_HUMANHSPA8physical
15009096
CENPT_HUMANCENPTphysical
15009096
FL2D_HUMANWTAPphysical
15009096
RING1_HUMANRING1physical
15009096
CBX8_HUMANCBX8physical
15009096
ACTB_HUMANACTBphysical
15009096
BMI1_HUMANBMI1physical
15009096
RING2_HUMANRNF2physical
15009096
CENPN_HUMANCENPNphysical
15009096
FBRL_HUMANFBLphysical
15009096
CENPH_HUMANCENPHphysical
15009096
CENPO_HUMANCENPOphysical
15009096
CENPK_HUMANCENPKphysical
15009096
CBX3_HUMANCBX3physical
15009096
CENPM_HUMANCENPMphysical
15009096
CENPA_HUMANCENPAphysical
15009096
H2AY_HUMANH2AFYphysical
15009096
H12_HUMANHIST1H1Cphysical
15009096
H33_HUMANH3F3Aphysical
15009096
H2A1D_HUMANHIST1H2ADphysical
15009096
H2B2E_HUMANHIST2H2BEphysical
15009096
CENPI_HUMANCENPIphysical
15009096
HJURP_HUMANHJURPphysical
19410544
RFA1_HUMANRPA1physical
19410544
RUVB1_HUMANRUVBL1physical
19410544
NPM_HUMANNPM1physical
19410544
CENPU_HUMANCENPUphysical
21454580
PRKDC_HUMANPRKDCphysical
20080577
HNRPU_HUMANHNRNPUphysical
20080577
HJURP_HUMANHJURPphysical
20080577
DDX3X_HUMANDDX3Xphysical
20080577
XRCC5_HUMANXRCC5physical
20080577
DDX5_HUMANDDX5physical
20080577
DDX17_HUMANDDX17physical
20080577
RUVB1_HUMANRUVBL1physical
20080577
RUVB2_HUMANRUVBL2physical
20080577
IF4A1_HUMANEIF4A1physical
20080577
NPM_HUMANNPM1physical
20080577
H2B1B_HUMANHIST1H2BBphysical
20080577
SP16H_HUMANSUPT16Hphysical
16622419
HJURP_HUMANHJURPphysical
16622419
NPM_HUMANNPM1physical
16622419
SSRP1_HUMANSSRP1physical
16622419
CENPB_HUMANCENPBphysical
16622419
CENPC_HUMANCENPCphysical
16622419
CENPH_HUMANCENPHphysical
16622419
CENPU_HUMANCENPUphysical
16622419
CENPM_HUMANCENPMphysical
16622419
CENPN_HUMANCENPNphysical
16622419
CENPT_HUMANCENPTphysical
16622419
H2AX_HUMANH2AFXphysical
16622419
H2AZ_HUMANH2AFZphysical
16622419
H2AY_HUMANH2AFYphysical
16622419
H11_HUMANHIST1H1Aphysical
16622419
H2A2C_HUMANHIST2H2ACphysical
16622419
H2B3B_HUMANHIST3H2BBphysical
16622419
DIAP3_HUMANDIAPH3physical
15085137
H2B1B_HUMANHIST1H2BBphysical
24530302
H33_HUMANH3F3Aphysical
24530302
CSN8_HUMANCOPS8physical
25727006
HJURP_HUMANHJURPphysical
25727006
CDK9_HUMANCDK9physical
26496610
PGK1_HUMANPGK1physical
26496610
RM19_HUMANMRPL19physical
26496610
ATP5H_HUMANATP5Hphysical
26496610
RM03_HUMANMRPL3physical
26496610
RT27_HUMANMRPS27physical
26496610
TMCO1_HUMANTMCO1physical
26496610
NOL8_HUMANNOL8physical
26496610
HJURP_HUMANHJURPphysical
26496610
TBC14_HUMANTBC1D14physical
26496610
DEFM_HUMANPDFphysical
26496610
BRCC3_HUMANBRCC3physical
26496610
RRP36_HUMANRRP36physical
26496610
RM54_HUMANMRPL54physical
26496610
HJURP_HUMANHJURPphysical
28514442
SP16H_HUMANSUPT16Hphysical
28514442
MS18B_HUMANOIP5physical
28514442
ARL10_HUMANARL10physical
28514442
MS18A_HUMANMIS18Aphysical
28514442
SSRP1_HUMANSSRP1physical
28514442
H2AY_HUMANH2AFYphysical
28514442
MCM4_HUMANMCM4physical
28514442

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 CENPA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19; THR-23 ANDSER-27, AND MASS SPECTROMETRY.
"Aurora-C and Aurora-B share phosphorylation and regulation of CENP-Aand Borealin during mitosis.";
Slattery S.D., Moore R.V., Brinkley B.R., Hall R.M.;
Cell Cycle 7:787-795(2008).
Cited for: PHOSPHORYLATION AT SER-7.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, AND MASSSPECTROMETRY.
"CENP-A phosphorylation by Aurora-A in prophase is required forenrichment of Aurora-B at inner centromeres and for kinetochorefunction.";
Kunitoku N., Sasayama T., Marumoto T., Zhang D., Honda S.,Kobayashi O., Hatakeyama K., Ushio Y., Saya H., Hirota T.;
Dev. Cell 5:853-864(2003).
Cited for: PHOSPHORYLATION AT SER-7, AND MUTAGENESIS OF SER-7.
"CENP-A is phosphorylated by Aurora B kinase and plays an unexpectedrole in completion of cytokinesis.";
Zeitlin S.G., Shelby R.D., Sullivan K.F.;
J. Cell Biol. 155:1147-1157(2001).
Cited for: PHOSPHORYLATION AT SER-7, AND MUTAGENESIS OF SER-7.

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