CENPN_HUMAN - dbPTM
CENPN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPN_HUMAN
UniProt AC Q96H22
Protein Name Centromere protein N
Gene Name CENPN
Organism Homo sapiens (Human).
Sequence Length 339
Subcellular Localization Nucleus. Chromosome, centromere, kinetochore. Localizes exclusively in the kinetochore domain of centromeres. Kinetochore-bound levels decrease when cells enter mitosis and increase again when cells exit mitosis.
Protein Description Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate..
Protein Sequence MDETVAEFIKRTILKIPMNELTTILKAWDFLSENQLQTVNFRQRKESVVQHLIHLCEEKRASISDAALLDIIYMQFHQHQKVWEVFQMSKGPGEDVDLFDMKQFKNSFKKILQRALKNVTVSFRETEENAVWIRIAWGTQYTKPNQYKPTYVVYYSQTPYAFTSSSMLRRNTPLLGQALTIASKHHQIVKMDLRSRYLDSLKAIVFKQYNQTFETHNSTTPLQERSLGLDINMDSRIIHENIVEKERVQRITQETFGDYPQPQLEFAQYKLETKFKSGLNGSILAEREEPLRCLIKFSSPHLLEALKSLAPAGIADAPLSPLLTCIPNKRMNYFKIRDK
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
10UbiquitinationETVAEFIKRTILKIP
HHHHHHHHHHHHCCC		49.13-
15 (in isoform 1)Ubiquitination-40.7021890473
15 (in isoform 2)Ubiquitination-40.7021906983
15UbiquitinationFIKRTILKIPMNELT
HHHHHHHCCCHHHHH		40.7021906983
22PhosphorylationKIPMNELTTILKAWD
CCCHHHHHHHHHHHH		12.9520860994
45UbiquitinationTVNFRQRKESVVQHL
ECCHHHHHHHHHHHH		46.1029967540
82UbiquitinationQFHQHQKVWEVFQMS
HHHHHHHHHHHHHCC		4.1923503661
85UbiquitinationQHQKVWEVFQMSKGP
HHHHHHHHHHCCCCC		2.0727667366
90 (in isoform 2)Ubiquitination-64.8821906983
90 (in isoform 1)Ubiquitination-64.8821890473
90UbiquitinationWEVFQMSKGPGEDVD
HHHHHCCCCCCCCCC		64.88906983
97UbiquitinationKGPGEDVDLFDMKQF
CCCCCCCCHHCHHHH		54.6727667366
102UbiquitinationDVDLFDMKQFKNSFK
CCCHHCHHHHHHHHH		55.1921906983
102 (in isoform 1)Ubiquitination-55.1921890473
102 (in isoform 2)Ubiquitination-55.1921906983
105UbiquitinationLFDMKQFKNSFKKIL
HHCHHHHHHHHHHHH		49.5427667366
117 (in isoform 1)Ubiquitination-48.6821890473
117 (in isoform 2)Ubiquitination-48.6821906983
117UbiquitinationKILQRALKNVTVSFR
HHHHHHHCCCEEEEE		48.6821906983
150PhosphorylationKPNQYKPTYVVYYSQ
CCCCCCCEEEEEEEC		25.4624043423
151PhosphorylationPNQYKPTYVVYYSQT
CCCCCCEEEEEEECC		9.1024043423
154PhosphorylationYKPTYVVYYSQTPYA
CCCEEEEEEECCCCE		6.3224043423
155PhosphorylationKPTYVVYYSQTPYAF
CCEEEEEEECCCCEE		5.2324043423
156PhosphorylationPTYVVYYSQTPYAFT
CEEEEEEECCCCEEC		15.1924043423
158PhosphorylationYVVYYSQTPYAFTSS
EEEEEECCCCEECCH		16.6024043423
160PhosphorylationVYYSQTPYAFTSSSM
EEEECCCCEECCHHH		20.1024043423
163PhosphorylationSQTPYAFTSSSMLRR
ECCCCEECCHHHHHC		21.3724043423
164PhosphorylationQTPYAFTSSSMLRRN
CCCCEECCHHHHHCC		17.6024043423
165PhosphorylationTPYAFTSSSMLRRNT
CCCEECCHHHHHCCC		19.4024043423
166PhosphorylationPYAFTSSSMLRRNTP
CCEECCHHHHHCCCC		22.9224043423
170UbiquitinationTSSSMLRRNTPLLGQ
CCHHHHHCCCCHHHH		47.6229967540
172PhosphorylationSSMLRRNTPLLGQAL
HHHHHCCCCHHHHHH		17.32-
180PhosphorylationPLLGQALTIASKHHQ
CHHHHHHHHHHHHCH		19.95-
182UbiquitinationLGQALTIASKHHQIV
HHHHHHHHHHHCHHC		13.8021963094
183PhosphorylationGQALTIASKHHQIVK
HHHHHHHHHHCHHCC		28.77-
187UbiquitinationTIASKHHQIVKMDLR
HHHHHHCHHCCHHHH		41.7221890473
187UbiquitinationTIASKHHQIVKMDLR
HHHHHHCHHCCHHHH		41.7221890473
190UbiquitinationSKHHQIVKMDLRSRY
HHHCHHCCHHHHHHH		28.4629967540
202 (in isoform 1)Ubiquitination-39.7621890473
202UbiquitinationSRYLDSLKAIVFKQY
HHHHHHHHHHHHHHH		39.7621906983
207UbiquitinationSLKAIVFKQYNQTFE
HHHHHHHHHHHHHHC		40.7621890473
207 (in isoform 1)Ubiquitination-40.7621890473
207UbiquitinationSLKAIVFKQYNQTFE
HHHHHHHHHHHHHHC		40.7622817900
211UbiquitinationIVFKQYNQTFETHNS
HHHHHHHHHHCCCCC		42.5033845483
212PhosphorylationVFKQYNQTFETHNST
HHHHHHHHHCCCCCC		21.5720860994
215PhosphorylationQYNQTFETHNSTTPL
HHHHHHCCCCCCCCC		23.3630266825
218PhosphorylationQTFETHNSTTPLQER
HHHCCCCCCCCCHHH		26.5030266825
219PhosphorylationTFETHNSTTPLQERS
HHCCCCCCCCCHHHH		37.4425849741
220PhosphorylationFETHNSTTPLQERSL
HCCCCCCCCCHHHHC		23.0930266825
225UbiquitinationSTTPLQERSLGLDIN
CCCCCHHHHCCCCCC		24.9933845483
226PhosphorylationTTPLQERSLGLDINM
CCCCHHHHCCCCCCC		26.4930266825
235PhosphorylationGLDINMDSRIIHENI
CCCCCCCCCHHHCHH		18.0130266825
236UbiquitinationLDINMDSRIIHENIV
CCCCCCCCHHHCHHH		27.8421963094
240UbiquitinationMDSRIIHENIVEKER
CCCCHHHCHHHCHHH		37.9422817900
242UbiquitinationSRIIHENIVEKERVQ
CCHHHCHHHCHHHHH		3.7421890473
242UbiquitinationSRIIHENIVEKERVQ
CCHHHCHHHCHHHHH		3.7421890473
245UbiquitinationIHENIVEKERVQRIT
HHCHHHCHHHHHHHH		39.6721906983
245 (in isoform 1)Ubiquitination-39.6721890473
250UbiquitinationVEKERVQRITQETFG
HCHHHHHHHHHHHHC		30.9421963094
254UbiquitinationRVQRITQETFGDYPQ
HHHHHHHHHHCCCCC		37.1422817900
256UbiquitinationQRITQETFGDYPQPQ
HHHHHHHHCCCCCHH		7.4421890473
256UbiquitinationQRITQETFGDYPQPQ
HHHHHHHHCCCCCHH		7.4421890473
270UbiquitinationQLEFAQYKLETKFKS
HHHHHHHHHHHHHCC		27.9721906983
270 (in isoform 1)Ubiquitination-27.9721890473
274UbiquitinationAQYKLETKFKSGLNG
HHHHHHHHHCCCCCC		41.2322817900
276 (in isoform 1)Ubiquitination-45.2121890473
276UbiquitinationYKLETKFKSGLNGSI
HHHHHHHCCCCCCCC		45.2121890473
276UbiquitinationYKLETKFKSGLNGSI
HHHHHHHCCCCCCCC		45.2122817900
277PhosphorylationKLETKFKSGLNGSIL
HHHHHHCCCCCCCCC		52.2030266825
282PhosphorylationFKSGLNGSILAEREE
HCCCCCCCCCCCCCC		17.2329255136
295UbiquitinationEEPLRCLIKFSSPHL
CCCHHHEEEECCHHH		4.9229967540
296UbiquitinationEPLRCLIKFSSPHLL
CCHHHEEEECCHHHH		26.67-
299PhosphorylationRCLIKFSSPHLLEAL
HHEEEECCHHHHHHH		21.3325159151
309UbiquitinationLLEALKSLAPAGIAD
HHHHHHHHCCCCCCC		6.7329967540
320PhosphorylationGIADAPLSPLLTCIP
CCCCCCCCHHHHCCC		16.6724719451
329AcetylationLLTCIPNKRMNYFKI
HHHCCCCCCCCCEEE		47.9026051181
329UbiquitinationLLTCIPNKRMNYFKI
HHHCCCCCCCCCEEE		47.9029967540
333PhosphorylationIPNKRMNYFKIRDK-
CCCCCCCCEEECCC-		9.26-
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 CENPN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CENPN_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 CENPN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CENPI_HUMANCENPIphysical
16622419
CENPL_HUMANCENPLphysical
16622419
CENPO_HUMANCENPOphysical
16622419
CENPK_HUMANCENPKphysical
16622419
CENPP_HUMANCENPPphysical
16622419
CENPQ_HUMANCENPQphysical
16622419
CENPH_HUMANCENPHphysical
16622419
CENPM_HUMANCENPMphysical
16622419
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 CENPN_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.
"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-226 AND SER-282, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-282, ANDMASS SPECTROMETRY.
"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-226 AND SER-282, ANDMASS SPECTROMETRY.
"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-226, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory