CENPO_HUMAN - dbPTM
CENPO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPO_HUMAN
UniProt AC Q9BU64
Protein Name Centromere protein O
Gene Name CENPO
Organism Homo sapiens (Human).
Sequence Length 300
Subcellular Localization Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.
Protein Description Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Modulates the kinetochore-bound levels of NDC80 complex..
Protein Sequence MEQANPLRPDGESKGGVLAHLERLETQVSRSRKQSEELQSVQAQEGALGTKIHKLRRLRDELRAVVRHRRASVKACIANVEPNQTVEINEQEALEEKLENVKAILQAYHFTGLSGKLTSRGVCVCISTAFEGNLLDSYFVDLVIQKPLRIHHHSVPVFIPLEEIAAKYLQTNIQHFLFSLCEYLNAYSGRKYQADRLQSDFAALLTGPLQRNPLCNLLSFTYKLDPGGQSFPFCARLLYKDLTATLPTDVTVTCQGVEVLSTSWEEQRASHETLFCTKPLHQVFASFTRKGEKLDMSLVS
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
26PhosphorylationAHLERLETQVSRSRK
HHHHHHHHHHHHHHH
38.57-
27UbiquitinationHLERLETQVSRSRKQ
HHHHHHHHHHHHHHH
23.0829967540
31PhosphorylationLETQVSRSRKQSEEL
HHHHHHHHHHHHHHH
36.0030576142
33UbiquitinationTQVSRSRKQSEELQS
HHHHHHHHHHHHHHH
60.4629967540
35PhosphorylationVSRSRKQSEELQSVQ
HHHHHHHHHHHHHHH
35.7523401153
40PhosphorylationKQSEELQSVQAQEGA
HHHHHHHHHHHHHCH
28.9030266825
45UbiquitinationLQSVQAQEGALGTKI
HHHHHHHHCHHHHHH
49.8329967540
51UbiquitinationQEGALGTKIHKLRRL
HHCHHHHHHHHHHHH
40.8029967540
72PhosphorylationVVRHRRASVKACIAN
HHHHHHHHHHHHEEC
23.49-
85PhosphorylationANVEPNQTVEINEQE
ECCCCCCEEEECHHH
27.0930266825
91UbiquitinationQTVEINEQEALEEKL
CEEEECHHHHHHHHH
36.4529967540
97UbiquitinationEQEALEEKLENVKAI
HHHHHHHHHHHHHHH
52.2929967540
154PhosphorylationPLRIHHHSVPVFIPL
CCCCCCCCCCEEEEH
24.61-
183PhosphorylationFLFSLCEYLNAYSGR
HHHHHHHHHHHHCCC
12.31-
253PhosphorylationLPTDVTVTCQGVEVL
CCCCCEEEECCEEEE
6.9727251275
261PhosphorylationCQGVEVLSTSWEEQR
ECCEEEEECCHHHHH
26.1027251275
262PhosphorylationQGVEVLSTSWEEQRA
CCEEEEECCHHHHHH
33.4327251275
263PhosphorylationGVEVLSTSWEEQRAS
CEEEEECCHHHHHHH
29.1619007248
290UbiquitinationVFASFTRKGEKLDMS
HHHHHCCCCCCCCCC
69.25-
293UbiquitinationSFTRKGEKLDMSLVS
HHCCCCCCCCCCCCC
59.46-
297PhosphorylationKGEKLDMSLVS----
CCCCCCCCCCC----
25.8620860994
300PhosphorylationKLDMSLVS-------
CCCCCCCC-------
39.5423186163

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

Oops, there are no upstream regulatory protein records of CENPO_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CENPO_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 CENPO_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CENPI_HUMANCENPIphysical
16622420
CENPP_HUMANCENPPphysical
16622420
CENPQ_HUMANCENPQphysical
16622420
CENPR_HUMANITGB3BPphysical
16622420
CENPU_HUMANCENPUphysical
16622420
KNL1_HUMANCASC5physical
16622420
CENPH_HUMANCENPHphysical
16622420
CENPN_HUMANCENPNphysical
16622420
ERI3_HUMANERI3physical
19447967
CENPP_HUMANCENPPphysical
25416956
ARL5B_HUMANARL5Bphysical
26186194
CENPQ_HUMANCENPQphysical
26186194
CENPR_HUMANITGB3BPphysical
26186194
CENPU_HUMANCENPUphysical
26186194
MTFR1_HUMANMTFR1physical
26186194
AT2B1_HUMANATP2B1physical
26496610
CENPC_HUMANCENPCphysical
26496610
CENPI_HUMANCENPIphysical
26496610
PLXB1_HUMANPLXNB1physical
26496610
STK3_HUMANSTK3physical
26496610
PABP2_HUMANPABPN1physical
26496610
MFHA1_HUMANMFHAS1physical
26496610
SC22B_HUMANSEC22Bphysical
26496610
CENPR_HUMANITGB3BPphysical
26496610
CENPQ_HUMANCENPQphysical
26496610
CENPN_HUMANCENPNphysical
26496610
S39AA_HUMANSLC39A10physical
26496610
CENPK_HUMANCENPKphysical
26496610
CENPH_HUMANCENPHphysical
26496610
CENPM_HUMANCENPMphysical
26496610
CENPU_HUMANCENPUphysical
26496610
CENPT_HUMANCENPTphysical
26496610
SMS2_HUMANSGMS2physical
26496610
CENPX_HUMANSTRA13physical
26496610
CENPS_HUMANAPITD1physical
26496610
CENPP_HUMANCENPPphysical
26496610
CENPR_HUMANITGB3BPphysical
28514442
CENPU_HUMANCENPUphysical
28514442
CENPQ_HUMANCENPQphysical
28514442
MTFR1_HUMANMTFR1physical
28514442
ARL5B_HUMANARL5Bphysical
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 CENPO_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-263, AND MASSSPECTROMETRY.

TOP