Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Centromere protein T  

UniProtKB / Swiss-Prot ID :  CENPT_HUMAN

Gene Name (Synonyms) : 
CENPT, C16orf56, ICEN22  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Chromosome, centromere, kinetochore. Note=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 kinetochore via its N-terminus. 

Protein Function :  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 MADHNPDSDSTPRTLLRRVLDTADPRTPRRPRSARAGARRALLETASPRKLSGQTRTIARGRSHGARSVG...
Predicted Secondary Structure CCCCCCCCCCHHHHHHHHHHHHCCCCCCCCCHHHHCCHHHHHHHCCCHHHHCCCHHHHHHCCCCCCHHHC...
Protein Variant
LocationDescription
115P -> L (in dbSNP:rs12102580). VAR_027421
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADHNP
---CCCCCC
27.11UniProtKB
Link-
10PhosphoserinePDSDSTPRT
CCCCCHHHH
44.24HPRD
Link-
10Phosphoserine.PDSDSTPRT
CCCCCHHHH
44.24UniProtKB
Link-
11PhosphothreonineDSDSTPRTL
CCCCHHHHH
23.06HPRD
Link-
11PhosphothreonineDSDSTPRTL
CCCCHHHHH
23.06Phosphositeplus
Link-
11Phosphothreonine.DSDSTPRTL
CCCCHHHHH
23.06UniProtKB
Link-
27PhosphothreonineADPRTPRRP
CCCCCCCCC
26.91Phosphositeplus
Link-
45PhosphothreonineALLETASPR
HHHHCCCHH
32.19HPRD
Link-
45PhosphothreonineALLETASPR
HHHHCCCHH
32.19Phosphositeplus
Link-
45Phosphothreonine.ALLETASPR
HHHHCCCHH
32.19UniProtKB
Link-
47PhosphoserineLETASPRKL
HHCCCHHHH
32.43HPRD
Link-
47PhosphoserineLETASPRKL
HHCCCHHHH
32.43Phosphositeplus
Link-
47Phosphoserine.LETASPRKL
HHCCCHHHH
32.43UniProtKB
Link-
57PhosphothreonineGQTRTIARG
CCHHHHHHC
23.52HPRD
Link-
57PhosphothreonineGQTRTIARG
CCHHHHHHC
23.52Phosphositeplus
Link-
85PhosphothreonineLEEQTPRTL
CHHCCHHHH
20.30HPRD
Link-
85PhosphothreonineLEEQTPRTL
CHHCCHHHH
20.30Phosphositeplus
Link-
85Phosphothreonine.LEEQTPRTL
CHHCCHHHH
20.30UniProtKB
Link-
184PhosphoserineADASSLTRS
CCHHHHHHH
35.17HPRD
Link-
188PhosphoserineSLTRSLNLT
HHHHHHHCC
19.17HPRD
Link-
188PhosphoserineSLTRSLNLT
HHHHHHHCC
19.17PhosphoELM
Link-
188PhosphoserineSLTRSLNLT
HHHHHHHCC
19.17Phosphositeplus
Link-
188PhosphoserineSLTRSLNLT
HHHHHHHCC
19.17SysPTM
Link-
188Phosphoserine.SLTRSLNLT
HHHHHHHCC
19.17UniProtKB
Link-
192PhosphothreonineSLNLTFATP
HHHCCCCCC
15.34HPRD
Link-
192PhosphothreonineSLNLTFATP
HHHCCCCCC
15.34PhosphoELM
Link-
192PhosphothreonineSLNLTFATP
HHHCCCCCC
15.34Phosphositeplus
Link-
192PhosphothreonineSLNLTFATP
HHHCCCCCC
15.34SysPTM
Link-
195PhosphothreonineLTFATPLQP
CCCCCCCCC
21.97HPRD
Link-
195PhosphothreonineLTFATPLQP
CCCCCCCCC
21.97PhosphoELM
Link-
195PhosphothreonineLTFATPLQP
CCCCCCCCC
21.97Phosphositeplus
Link-
195PhosphothreonineLTFATPLQP
CCCCCCCCC
21.97SysPTM
Link-
201PhosphoserineLQPQSVQRP
CCCCCCCCC
27.22HPRD
Link-
201Phosphoserine.LQPQSVQRP
CCCCCCCCC
27.22UniProtKB
Link-
373PhosphoserineEAEGSQGTA
CCCCCCCCC
19.55HPRD
Link-
373PhosphoserineEAEGSQGTA
CCCCCCCCC
19.55PhosphoELM
Link-
373PhosphoserineEAEGSQGTA
CCCCCCCCC
19.55Phosphositeplus
Link-
373Phosphoserine.EAEGSQGTA
CCCCCCCCC
19.55UniProtKB
Link-
385PhosphoserineGPGASSGDE
CCCCCCCCC
40.54HPRD
Link-
385PhosphoserineGPGASSGDE
CCCCCCCCC
40.54PhosphoELM
Link-
385PhosphoserineGPGASSGDE
CCCCCCCCC
40.54Phosphositeplus
Link-
385Phosphoserine.GPGASSGDE
CCCCCCCCC
40.54UniProtKB
Link-
386PhosphoserinePGASSGDED
CCCCCCCCC
50.13HPRD
Link-
386PhosphoserinePGASSGDED
CCCCCCCCC
50.13PhosphoELM
Link-
386PhosphoserinePGASSGDED
CCCCCCCCC
50.13Phosphositeplus
Link-
386Phosphoserine.PGASSGDED
CCCCCCCCC
50.13UniProtKB
Link-
397PhosphoserineGRAASPESA
CCCCCCCCC
28.37HPRD
Link-
397PhosphoserineGRAASPESA
CCCCCCCCC
28.37HPRD
Link-
397PhosphoserineGRAASPESA
CCCCCCCCC
28.37PhosphoELM
Link-
397PhosphoserineGRAASPESA
CCCCCCCCC
28.37Phosphositeplus
Link-
397PhosphoserineGRAASPESA
CCCCCCCCC
28.37SysPTM
Link-
397Phosphoserine.GRAASPESA
CCCCCCCCC
28.37UniProtKB
Link-
400PhosphoserineASPESASST
CCCCCCCCC
36.51Phosphositeplus
Link-
403PhosphoserineESASSTPES
CCCCCCCCC
47.93Phosphositeplus
Link-
404PhosphothreonineSASSTPESL
CCCCCCCCC
28.69HPRD
Link-
404PhosphothreonineSASSTPESL
CCCCCCCCC
28.69Phosphositeplus
Link-
407PhosphoserineSTPESLQAR
CCCCCCCCC
27.30HPRD
Link-
407PhosphoserineSTPESLQAR
CCCCCCCCC
27.30Phosphositeplus
Link-
461PhosphoserineKAGLSHYVK
CCCCCCEEE
16.32HPRD
Link-
463PhosphotyrosineGLSHYVKLF
CCCCEEEEE
8.90HPRD
Link-
468PhosphoserineVKLFSFYAK
EEEEEEECC
27.99HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SYUB_HUMANphysical interactionMINT-64283MINT16169070
Q86VL0_HUMANphysical interactionMINT-64829MINT16169070
DHX29_HUMANphysical interactionEBI-734541
intact16169070
COAC_HUMANphysical interactionEBI-736748
intact16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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
"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.
"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.
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures