CENPT_HUMAN - dbPTM
CENPT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CENPT_HUMAN
UniProt AC Q96BT3
Protein Name Centromere protein T
Gene Name CENPT
Organism Homo sapiens (Human).
Sequence Length 561
Subcellular Localization Nucleus. Chromosome, centromere . Chromosome, centromere, kinetochore . Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Localizes to the inner kinetochore, and may connect it to the outer kinetoc
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. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis..
Protein Sequence MADHNPDSDSTPRTLLRRVLDTADPRTPRRPRSARAGARRALLETASPRKLSGQTRTIARGRSHGARSVGRSAHIQASGHLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQAVQPSRQESSCGSLELQLPELEPPTTLAPGLLAPGRRKQRLRLSVFQQGVDQGLSLSQEPQGNADASSLTRSLNLTFATPLQPQSVQRPGLARRPPARRAVDVGAFLRDLRDTSLAPPNIVLEDTQPFSQPMVGSPNVYHSLPCTPHTGAEDAEQAAGRKTQSSGPGLQKNSPGKPAQFLAGEAEEVNAFALGFLSTSSGVSGEDEVEPLHDGVEEAEKKMEEEGVSVSEMEATGAQGPSRVEEAEGHTEVTEAEGSQGTAEADGPGASSGDEDASGRAASPESASSTPESLQARRHHQFLEPAPAPGAAVLSSEPAEPLLVRHPPRPRTTGPRPRQDPHKAGLSHYVKLFSFYAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVLVERHLPLEYRQLLIPCAYSGNSVFPAQ
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
2Acetylation------MADHNPDSD
------CCCCCCCCC		27.11-
8PhosphorylationMADHNPDSDSTPRTL
CCCCCCCCCCCHHHH		34.4228450419
10PhosphorylationDHNPDSDSTPRTLLR
CCCCCCCCCHHHHHH		44.2419691289
11PhosphorylationHNPDSDSTPRTLLRR
CCCCCCCCHHHHHHH		23.0619691289
22PhosphorylationLLRRVLDTADPRTPR
HHHHHHHCCCCCCCC		28.8825404012
27PhosphorylationLDTADPRTPRRPRSA
HHCCCCCCCCCCCHH		26.9127273156
45PhosphorylationARRALLETASPRKLS
HHHHHHHHCCCCCCC		32.1928176443
47PhosphorylationRALLETASPRKLSGQ
HHHHHHCCCCCCCCC		32.4329255136
52PhosphorylationTASPRKLSGQTRTIA
HCCCCCCCCCCEECC		31.7130387612
57PhosphorylationKLSGQTRTIARGRSH
CCCCCCEECCCCCCC		23.5220068231
63 (in isoform 3)Phosphorylation-29.1522210691
69 (in isoform 3)Phosphorylation-6.5122210691
70 (in isoform 3)Phosphorylation-21.0422210691
72PhosphorylationGARSVGRSAHIQASG
CCCCCCCCCCCCCCC		20.4728450419
78PhosphorylationRSAHIQASGHLEEQT
CCCCCCCCCCCCCCC		15.4628450419
85PhosphorylationSGHLEEQTPRTLLKN
CCCCCCCCHHHHHHH		20.3021712546
96PhosphorylationLLKNILLTAPESSIL
HHHHHHHHCCCHHCC		36.4028348404
100PhosphorylationILLTAPESSILMPES
HHHHCCCHHCCCCHH		22.9428348404
101PhosphorylationLLTAPESSILMPESV
HHHCCCHHCCCCHHH		20.3424719451
107PhosphorylationSSILMPESVVKPVPA
HHCCCCHHHCCCCCC		26.7528122231
121PhosphorylationAPQAVQPSRQESSCG
CCCCCCCCCCCCCCC		29.5128122231
125PhosphorylationVQPSRQESSCGSLEL
CCCCCCCCCCCCEEE		23.6922817900
173PhosphorylationVDQGLSLSQEPQGNA
HHCCCCCCCCCCCCC		29.17-
183PhosphorylationPQGNADASSLTRSLN
CCCCCCHHHHHHHCC		26.8220068231
184PhosphorylationQGNADASSLTRSLNL
CCCCCHHHHHHHCCC		35.1720068231
186PhosphorylationNADASSLTRSLNLTF
CCCHHHHHHHCCCEE		21.8420068231
188PhosphorylationDASSLTRSLNLTFAT
CHHHHHHHCCCEEEC		19.1730266825
192PhosphorylationLTRSLNLTFATPLQP
HHHHCCCEEECCCCC		15.3430266825
195PhosphorylationSLNLTFATPLQPQSV
HCCCEEECCCCCCCC		21.9726055452
201PhosphorylationATPLQPQSVQRPGLA
ECCCCCCCCCCCCCC		27.2222199227
245PhosphorylationLEDTQPFSQPMVGSP
ECCCCCCCCCCCCCC		39.8026074081
251PhosphorylationFSQPMVGSPNVYHSL
CCCCCCCCCCEEECC		11.2426074081
255PhosphorylationMVGSPNVYHSLPCTP
CCCCCCEEECCCCCC		7.7326074081
257PhosphorylationGSPNVYHSLPCTPHT
CCCCEEECCCCCCCC		19.1326074081
261PhosphorylationVYHSLPCTPHTGAED
EEECCCCCCCCCHHH		19.0326074081
264PhosphorylationSLPCTPHTGAEDAEQ
CCCCCCCCCHHHHHH		39.0126074081
279PhosphorylationAAGRKTQSSGPGLQK
HCCCCCCCCCCCCCC		42.3625159151
280PhosphorylationAGRKTQSSGPGLQKN
CCCCCCCCCCCCCCC		38.9126425664
315PhosphorylationLGFLSTSSGVSGEDE
HHHCCCCCCCCCCCC		43.2122468782
343PhosphorylationKMEEEGVSVSEMEAT
HHHHCCCCHHHHHHC		30.6825849741
345PhosphorylationEEEGVSVSEMEATGA
HHCCCCHHHHHHCCC		24.5830266825
350PhosphorylationSVSEMEATGAQGPSR
CHHHHHHCCCCCCCC		21.5323186163
356PhosphorylationATGAQGPSRVEEAEG
HCCCCCCCCHHCCCC		56.6424275569
373PhosphorylationEVTEAEGSQGTAEAD
EEEECCCCCCCCCCC		19.5517525332
385PhosphorylationEADGPGASSGDEDAS
CCCCCCCCCCCCCCC		40.5425849741
386PhosphorylationADGPGASSGDEDASG
CCCCCCCCCCCCCCC		50.1317525332
397PhosphorylationDASGRAASPESASST
CCCCCCCCHHHHCCC		28.3729255136
400PhosphorylationGRAASPESASSTPES
CCCCCHHHHCCCHHH		36.5130266825
402PhosphorylationAASPESASSTPESLQ
CCCHHHHCCCHHHHH		43.9830266825
403PhosphorylationASPESASSTPESLQA
CCHHHHCCCHHHHHH		47.9329255136
404PhosphorylationSPESASSTPESLQAR
CHHHHCCCHHHHHHH		28.6929255136
407PhosphorylationSASSTPESLQARRHH
HHCCCHHHHHHHHHH		27.3029255136
429PhosphorylationAPGAAVLSSEPAEPL
CCCCEEECCCCCCCC		26.5126714015
430PhosphorylationPGAAVLSSEPAEPLL
CCCEEECCCCCCCCE		43.3626714015
457UbiquitinationRPRQDPHKAGLSHYV
CCCCCCCCCCHHHHH		49.92-
461PhosphorylationDPHKAGLSHYVKLFS
CCCCCCHHHHHHHHH		16.3220068231
463PhosphorylationHKAGLSHYVKLFSFY
CCCCHHHHHHHHHHH		8.9020068231
468PhosphorylationSHYVKLFSFYAKMPM
HHHHHHHHHHHCCCH		27.9920068231
470PhosphorylationYVKLFSFYAKMPMER
HHHHHHHHHCCCHHH		12.2420068231
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 CENPT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
47SPhosphorylation

20068231
47SPhosphorylation

20068231
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 CENPT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHX29_HUMANDHX29physical
16169070
CENPU_HUMANCENPUphysical
21454580
A4_HUMANAPPphysical
21832049
CSN5_HUMANCOPS5physical
23926101
CENPW_HUMANCENPWphysical
23926101
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 CENPT_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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-10; THR-11; THR-45;SER-47; THR-85 AND SER-201, ACETYLATION [LARGE SCALE ANALYSIS] ATALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Induced ectopic kinetochore assembly bypasses the requirement forCENP-A nucleosomes.";
Gascoigne K.E., Takeuchi K., Suzuki A., Hori T., Fukagawa T.,Cheeseman I.M.;
Cell 145:410-422(2011).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPW, ANDPHOSPHORYLATION AT SER-47.
"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-397, AND MASSSPECTROMETRY.
"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-397, 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-397, 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-10; THR-11; THR-45;SER-47; THR-85 AND SER-201, ACETYLATION [LARGE SCALE ANALYSIS] ATALA-2, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-385 ANDSER-386, 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-188, AND MASSSPECTROMETRY.

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