CENPB_HUMAN - dbPTM
CENPB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPB_HUMAN
UniProt AC P07199
Protein Name Major centromere autoantigen B
Gene Name CENPB
Organism Homo sapiens (Human).
Sequence Length 599
Subcellular Localization Nucleus . Chromosome, centromere .
Protein Description Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box. [PubMed: 11726497 May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes (Probable]
Protein Sequence MGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVSCSGVARARARNAAPRTPAAPASPAAVPSEGSGGSTTGWRAREEQPPSVAEGYASQDVFSATETSLWYDFLPDQAAGLCGGDGRPRQATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQAGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLAAQSLDTSGLRHVQLAFFPPGTVHPLERGVVQQVKGHYRQAMLLKAMAALEGQDPSGLQLGLTEALHFVAAAWQAVEPSDIAACFREAGFGGGPNATITTSLKSEGEEEEEEEEEEEEEEGEGEEEEEEGEEEEEEGGEGEELGEEEEVEEEGDVDSDEEEEEDEESSSEGLEAEDWAQGVVEAGGSFGAYGAQEEAQCPTLHFLEGGEDSDSDSEEEDDEEEDDEDEDDDDDEEDGDEVPVPSFGEAMAYFAMVKRYLTSFPIDDRVQSHILHLEHDLVHVTRKNHARQAGVRGLGHQS
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------MGPKRRQLT
------CCCCHHCCC		36.1123978223
55PhosphorylationNKRAILASERKYGVA
CCHHHHHHHCHHCHH		34.1924719451
58UbiquitinationAILASERKYGVASTC
HHHHHHCHHCHHHHC		42.1629967540
59PhosphorylationILASERKYGVASTCR
HHHHHCHHCHHHHCC		24.0528258704
64PhosphorylationRKYGVASTCRKTNKL
CHHCHHHHCCCCCCC		13.4428258704
68PhosphorylationVASTCRKTNKLSPYD
HHHHCCCCCCCCHHH		20.4521949786
70SumoylationSTCRKTNKLSPYDKL
HHCCCCCCCCHHHHH		56.42-
70UbiquitinationSTCRKTNKLSPYDKL
HHCCCCCCCCHHHHH		56.4229967540
70SumoylationSTCRKTNKLSPYDKL
HHCCCCCCCCHHHHH		56.42-
96UbiquitinationRAAGLPVKGIILKEK
HHCCCCCCEEEEHHH		42.3133845483
962-HydroxyisobutyrylationRAAGLPVKGIILKEK
HHCCCCCCEEEEHHH		42.31-
150PhosphorylationARNAAPRTPAAPASP
HHCCCCCCCCCCCCC		19.0723401153
156PhosphorylationRTPAAPASPAAVPSE
CCCCCCCCCCCCCCC		17.6425159151
162PhosphorylationASPAAVPSEGSGGST
CCCCCCCCCCCCCCC		48.2530266825
165PhosphorylationAAVPSEGSGGSTTGW
CCCCCCCCCCCCCCC		35.6123927012
168PhosphorylationPSEGSGGSTTGWRAR
CCCCCCCCCCCCCCC		26.7330278072
169PhosphorylationSEGSGGSTTGWRARE
CCCCCCCCCCCCCCC		32.3823927012
170PhosphorylationEGSGGSTTGWRAREE
CCCCCCCCCCCCCCC		36.1223927012
246UbiquitinationLPPLVAGKSAKPRAG
CCCCCCCCCCCCCCC		37.1933845483
246SumoylationLPPLVAGKSAKPRAG
CCCCCCCCCCCCCCC		37.1928112733
266AcetylationCDYTANSKGGVTTQA
CCCCCCCCCCHHHHH		60.5326051181
266UbiquitinationCDYTANSKGGVTTQA
CCCCCCCCCCHHHHH		60.5323000965
276UbiquitinationVTTQALAKYLKALDT
HHHHHHHHHHHHHHH		52.5521890473
276UbiquitinationVTTQALAKYLKALDT
HHHHHHHHHHHHHHH		52.5522817900
279UbiquitinationQALAKYLKALDTRMA
HHHHHHHHHHHHHHH		43.7633845483
303PhosphorylationAGRLAAQSLDTSGLR
HHHHHHHCCCCCCCC		24.40-
306PhosphorylationLAAQSLDTSGLRHVQ
HHHHCCCCCCCCCEE		29.9526462736
307PhosphorylationAAQSLDTSGLRHVQL
HHHCCCCCCCCCEEE		35.1826462736
334UbiquitinationRGVVQQVKGHYRQAM
CCHHHHHCCHHHHHH		35.3221890473
334UbiquitinationRGVVQQVKGHYRQAM
CCHHHHHCCHHHHHH		35.3222817900
396PhosphorylationFGGGPNATITTSLKS
CCCCCCCEEEEECCC		26.0420068231
398PhosphorylationGGPNATITTSLKSEG
CCCCCEEEEECCCCC		13.1328112733
399PhosphorylationGPNATITTSLKSEGE
CCCCEEEEECCCCCC		28.3630266825
400PhosphorylationPNATITTSLKSEGEE
CCCEEEEECCCCCCC		25.7530266825
486PhosphorylationGVVEAGGSFGAYGAQ
HHHHCCCCCCCCCCC		21.4219007248
599PhosphorylationVRGLGHQS-------
CCCCCCCC-------		36.1926853621
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
-KUbiquitinationE3 ubiquitin ligaseICP0P08393
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CENPB_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 CENPB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 CENPB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASSSPECTROMETRY.
"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-156 AND SER-486, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-165, ANDMASS SPECTROMETRY.

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