CENPI_HUMAN - dbPTM
CENPI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPI_HUMAN
UniProt AC Q92674
Protein Name Centromere protein I
Gene Name CENPI
Organism Homo sapiens (Human).
Sequence Length 756
Subcellular Localization Nucleus. Chromosome, centromere. Localizes exclusively in the centromeres. 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. Required for the localization of CENPF, MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to kinetochores. Involved in the response of gonadal tissues to follicle-stimulating hormone..
Protein Sequence MSPQKRVKNVQAQNRTSQGSSSFQTTLSAWKVKQDPSNSKNISKHGQNNPVGDYEHADDQAEEDALQMAVGYFEKGPIKASQNKDKTLEKHLKTVENVAWKNGLASEEIDILLNIALSGKFGNAVNTRILKCMIPATVISEDSVVKAVSWLCVGKCSGSTKVLFYRWLVAMFDFIDRKEQINLLYGFFFASLQDDALCPYVCHLLYLLTKKENVKPFRVRKLLDLQAKMGMQPHLQALLSLYKFFAPALISVSLPVRKKIYFKNSENLWKTALLAVKQRNRGPSPEPLKLMLGPANVRPLKRKWNSLSVIPVLNSSSYTKECGKKEMSLSDCLNRSGSFPLEQLQSFPQLLQNIHCLELPSQMGSVLNNSLLLHYINCVRDEPVLLRFYYWLSQTLQEECIWYKVNNYEHGKEFTNFLDTIIRAECFLQEGFYSCEAFLYKSLPLWDGLCCRSQFLQLVSWIPFSSFSEVKPLLFDHLAQLFFTSTIYFKCSVLQSLKELLQNWLLWLSMDIHMKPVTNSPLETTLGGSMNSVSKLIHYVGWLSTTAMRLESNNTFLLHFILDFYEKVCDIYINYNLPLVVLFPPGIFYSALLSLDTSILNQLCFIMHRYRKNLTAAKKNELVQKTKSEFNFSSKTYQEFNHYLTSMVGCLWTSKPFGKGIYIDPEILEKTGVAEYKNSLNVVHHPSFLSYAVSFLLQESPEERTVNVSSIRGKKWSWYLDYLFSQGLQGLKLFIRSSVHHSSIPRAEGINCNNQY
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
16PhosphorylationNVQAQNRTSQGSSSF
CHHHCCCCCCCCCCH		32.7125159151
17PhosphorylationVQAQNRTSQGSSSFQ
HHHCCCCCCCCCCHH		29.3425159151
20PhosphorylationQNRTSQGSSSFQTTL
CCCCCCCCCCHHHHH		18.3825627689
21PhosphorylationNRTSQGSSSFQTTLS
CCCCCCCCCHHHHHH		41.8321712546
22PhosphorylationRTSQGSSSFQTTLSA
CCCCCCCCHHHHHHH		24.0725159151
25PhosphorylationQGSSSFQTTLSAWKV
CCCCCHHHHHHHEEE		27.9121712546
37PhosphorylationWKVKQDPSNSKNISK
EEEECCCCCCCCCHH		63.1229083192
39PhosphorylationVKQDPSNSKNISKHG
EECCCCCCCCCHHCC		31.2729083192
43PhosphorylationPSNSKNISKHGQNNP
CCCCCCCHHCCCCCC		28.1729083192
54PhosphorylationQNNPVGDYEHADDQA
CCCCCCCCCCCCHHH		12.0427642862
93UbiquitinationKTLEKHLKTVENVAW
HHHHHHHHHHHHHHH		50.69-
221UbiquitinationVKPFRVRKLLDLQAK
CCCCHHHHHHHHHHH		51.01-
240PhosphorylationPHLQALLSLYKFFAP
HHHHHHHHHHHHHHH		30.4225599653
242PhosphorylationLQALLSLYKFFAPAL
HHHHHHHHHHHHHHH		11.4525599653
270 (in isoform 2)Ubiquitination-27.3821890473
270 (in isoform 1)Ubiquitination-27.3821890473
270UbiquitinationKNSENLWKTALLAVK
ECCHHHHHHHHHHHH		27.3821890473
277UbiquitinationKTALLAVKQRNRGPS
HHHHHHHHHHCCCCC		37.62-
284PhosphorylationKQRNRGPSPEPLKLM
HHHCCCCCCCCCHHC		44.7329255136
301UbiquitinationPANVRPLKRKWNSLS
CCCCCCCCCCCCCCC		55.40-
306PhosphorylationPLKRKWNSLSVIPVL
CCCCCCCCCCCEEEC		22.3917494752
308PhosphorylationKRKWNSLSVIPVLNS
CCCCCCCCCEEECCC		20.1621214269
315PhosphorylationSVIPVLNSSSYTKEC
CCEEECCCCCCCCCC		19.2528348404
316PhosphorylationVIPVLNSSSYTKECG
CEEECCCCCCCCCCC		26.7017494752
317PhosphorylationIPVLNSSSYTKECGK
EEECCCCCCCCCCCC		36.3230631047
318PhosphorylationPVLNSSSYTKECGKK
EECCCCCCCCCCCCC		24.6318491316
325UbiquitinationYTKECGKKEMSLSDC
CCCCCCCCCCCHHHH		43.89-
328PhosphorylationECGKKEMSLSDCLNR
CCCCCCCCHHHHCCC		26.3028509920
330PhosphorylationGKKEMSLSDCLNRSG
CCCCCCHHHHCCCCC		20.9728509920
420PhosphorylationEFTNFLDTIIRAECF
HHHHHHHHHHHHHHH		22.05-
453PhosphorylationWDGLCCRSQFLQLVS
CCCEECHHHHHHHHH		16.0322210691
492PhosphorylationSTIYFKCSVLQSLKE
HHHHHHHHHHHHHHH		26.8420068231
496PhosphorylationFKCSVLQSLKELLQN
HHHHHHHHHHHHHHH		36.9320068231
518PhosphorylationDIHMKPVTNSPLETT
CCCCCCCCCCCCCCC		38.2125627689
520PhosphorylationHMKPVTNSPLETTLG
CCCCCCCCCCCCCCC		22.8425849741
524PhosphorylationVTNSPLETTLGGSMN
CCCCCCCCCCCCCHH		34.7025627689
525PhosphorylationTNSPLETTLGGSMNS
CCCCCCCCCCCCHHH		17.6525159151
529PhosphorylationLETTLGGSMNSVSKL
CCCCCCCCHHHHHHH		17.0019007248
532PhosphorylationTLGGSMNSVSKLIHY
CCCCCHHHHHHHHHH		21.0825332170
619UbiquitinationKNLTAAKKNELVQKT
CCCHHHHHHHHHHHH		51.43-
625UbiquitinationKKNELVQKTKSEFNF
HHHHHHHHHHHHCCC		50.90-
627UbiquitinationNELVQKTKSEFNFSS
HHHHHHHHHHCCCCC		55.83-
637PhosphorylationFNFSSKTYQEFNHYL
CCCCCHHHHHHHHHH		15.13-
642PhosphorylationKTYQEFNHYLTSMVG
HHHHHHHHHHHHHHH		25.05-
643PhosphorylationTYQEFNHYLTSMVGC
HHHHHHHHHHHHHHH		16.87-
659UbiquitinationWTSKPFGKGIYIDPE
HCCCCCCCCEECCHH		42.38-
670UbiquitinationIDPEILEKTGVAEYK
CCHHHHHHHCCCCHH		47.32-
700PhosphorylationVSFLLQESPEERTVN
HHHHHCCCCCCCEEE		25.3419007248
705PhosphorylationQESPEERTVNVSSIR
CCCCCCCEEEHHHHC		21.5120860994
709PhosphorylationEERTVNVSSIRGKKW
CCCEEEHHHHCCCCC		18.1620860994
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 ligaseRNF4P78317
PMID:20212317
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CENPI_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 CENPI_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 CENPI_HUMAN

loading...

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-520, 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-284; THR-525; SER-529AND SER-700, AND MASS 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-22, AND MASSSPECTROMETRY.

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