Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
CENPT (human)

Overview
CENPT 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. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Part of a centromere complex consisting of CENPA, CENPT and CENPW. Part of a centromere complex consisting of histone H3, CENPT and CENPW. Interacts (via N-terminus) with the NDC80 complex (Probable). Component of a heterotetrameric CENP-T-W-S-X complex composed of APITD1/CENPS, STRA13/CENPX, CENPT and CENPW. Interacts directly with CENPW. Binds DNA. Belongs to the CENPT family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: DNA replication
Cellular Component: kinetochore; nuclear membrane; cytoplasm; nucleolus; cytosol; nucleus; chromosome, pericentric region
Molecular Function: protein binding; DNA binding; protein heterodimerization activity
Biological Process: mitosis; kinetochore assembly; mitotic cell cycle; chromosome organization and biogenesis; chromosome segregation
Reference #:  Q96BT3 (UniProtKB)
Alt. Names/Synonyms: C16orf56; CENP-T; CENPT; Centromere protein T; FLJ13111; FLJ43376; ICEN22; Interphase centromere complex protein 22
Gene Symbols: CENPT
Molecular weight: 60,423 Da
Basal Isoelectric point: 6.14  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CENPT

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
1 1 T11-p HNPDSDStPRTLLRR
1 23 T27-p LDTADPRtPRRPRSA
0 1 T45-p ARRALLEtAsPRKLS
1 8 S47-p RALLEtAsPRKLSGQ
0 1 T57-p KLSGQTRtIARGRSH
1 8 T85-p SGHLEEQtPRTLLKN
1 0 S101 LLTAPESSILMPESV
0 13 S125-p VQPSRQEsSCGSLEL
0 2 S188-p DASSLTRsLNLtFAt
0 2 T192-p LTRsLNLtFAtPLQP
1 1 T195-p sLNLtFAtPLQPQSV
0 1 C260 NVYHSLPCTPHTGAE
0 1 S343-p KMEEEGVsVSEMEAT
0 1 - gap
0 1 - gap
0 1 - under review  
0 1 S373-p EVTEAEGsQGTAEAD
0 1 S385-p EADGPGAssGDEDAS
0 1 S386-p ADGPGAssGDEDASG
1 7 S397-p DASGRAAsPESASSt
1 0 T404-p sPESASStPEsLQAR
0 1 S407-p SASStPEsLQARRHH
  CENPT iso2  
T11 HNPDSDSTPRTLLRR
T27-p LDTADPRtPRRPRSA
T45 ARRALLETASPRKLS
S47 RALLETASPRKLSGQ
T57 KLSGQTRTIARGRSH
T85 SGHLEEQTPRTLLKN
S101 LLTAPESSILMPESV
S125 VQPSRQESSCGSLEL
S188 DASSLTRSLNLTFAT
T192 LTRSLNLTFATPLQP
T195 SLNLTFATPLQPQSV
C260 NVYHSLPCTPHTGAE
- under review  
- gap
- gap
- under review  
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

 
T12 SFSDGDPTVRTLLRR
T28 LETADSRTPMRRRST
T46 AQRRRSQTPYSNRQG
Y48 RRRSQTPYSNRQGSQ
T58 RQGSQTKTSARKQSH
T86 RGRLEEQTPRTLLRN
S102 LLTAPESSTVMPDPV
S126-p ARSSRREsSRGSLEL
S191 DVSSLASSFNLTFVL
T195 LASSFNLTFVLPGQP
L198 SFNLTFVLPGQPETV
S279-p SGKHSLPsPSRPGVE
S306 TRLQSRMSRSGPAAs
S313-p SRSGPAAsPsPFLEP
S315-p SGPAAsPsPFLEPQP
P324 FLEPQPPPAEPREAV
S333 EPREAVGSNEAAEPK
S345 EPKDQEGSSGYEETS
S346 PKDQEGSSGYEETSA
S357 ETSARPASGELSSST
T364 SGELSSSTHDSLPAE
S367 LSSSTHDSLPAEQPP
  rat

 
T12 SSPDGDPTIRTLLRH
T28 LDTADSHTPRRRQST
T46 PQRRRSQTPYSKRQG
Y48 RRRSQTPYSKRQGSQ
T58 RQGSQRKTSTRKHSH
T86 HGHLEEQTPRTLLQN
S102 LLTAPESSTVMPNPV
S126 ARPSRRGSSRGSLEL
S189 DGSSLASSFNLSFVP
S193 LASSFNLSFVPSVQP
P196 SFNLSFVPSVQPQTV
N277 SVHHSLPNPSQTEVE
- under review  
S313 SRAGFGASPLPFSEP
L315 AGFGASPLPFSEPQP
S324-p FSEPQPQsPELREAV
S333 ELREAVGSKEAEEPK
S345 EPKDLEGSSGDEETS
S346 PKDLEGSSGDEETSG
S357 ETSGMPASRELSSSA
A364 SRELSSSAQDLLLAE
L367 LSSSAQDLLLAEEPH
  chicken

 
G6 __MDGRVGLRASRRA
A14 LRASRRAAPTPRVAV
R32 PRHRARVREQEPVVS
Q34 HRARVREQEPVVSAM
S44 VVSAMSGSGLGKENK
T72-p FSELDNAtPRVMLRK
S88-p IQNQPQVsPLALQTV
S113 EPPSQRTSSTVELQL
S171 LDSTLVRSLRMSVGS
S175 LVRSLRMSVGSVMAP
S178 SLRMSVGSVMAPDTV
R305 TDERRTLRFSEKDLI
- under review  
Q406 VAEGTEHQDSPKAEL
S408 EGTEHQDSPKAELQM
- under review  
Q443 PLKEAVEQTGEIERG
A463 LDAAEEEATDDESDK
T464 DAAEEEATDDESDKE
S475 SDKEDHESEEISMKT
T482 SEEISMKTPMFVHAA
F485 ISMKTPMFVHAAAYR
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.