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Q96BT3 (CENPT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centromere protein T

Short name=CENP-T
Alternative name(s):
Interphase centromere complex protein 22
Gene names
Name:CENPT
Synonyms:C16orf56, ICEN22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3 Ref.13 Ref.14

Subunit structure

Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and 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. Ref.4 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15

Subcellular location

Nucleus. Chromosomecentromerekinetochore. 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. Ref.3 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15

Domain

The largest part of the sequence forms an elongated and flexible stalk structure that is connected to a C-terminal globular domain with a histone-type fold By similarity.

Post-translational modification

Dynamically phosphorylated at Ser-47 and probably also other sites during the cell cycle. Phosphorylated at Ser-47 during G2 phase, metaphase and anaphase, but not during telophase or G1 phase. Ref.13

Sequence similarities

Belongs to the CENPT family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96BT3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96BT3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     289-299: PGKPAQFLAGE → ECVALVAWSQI
     300-561: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96BT3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     68-151: SVGRSAHIQA...TLAPGLLAPG → VSTQPTDPKG...NCPRIFHPDA
     152-561: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 561561Centromere protein T
PRO_0000249514

Regions

Region93 – 421329Flexible stalk domain By similarity

Amino acid modifications

Modified residue471Phosphoserine Ref.12 Ref.13
Modified residue851Phosphothreonine Ref.12
Modified residue3731Phosphoserine Ref.5
Modified residue3851Phosphoserine Ref.5
Modified residue3861Phosphoserine Ref.5
Modified residue3971Phosphoserine Ref.6 Ref.11 Ref.12

Natural variations

Alternative sequence68 – 15184SVGRS…LLAPG → VSTQPTDPKGPWLPRGGGLR SSSALEPTLRKSQGRRTDWL LGASPIVCWQIGPYSGQWAL GGTDTSDAAEEHPTNCPRIF HPDA in isoform 3.
VSP_020455
Alternative sequence152 – 561410Missing in isoform 3.
VSP_020456
Alternative sequence289 – 29911PGKPAQFLAGE → ECVALVAWSQI in isoform 2.
VSP_020457
Alternative sequence300 – 561262Missing in isoform 2.
VSP_020458
Natural variant1151P → L.
Corresponds to variant rs12102580 [ dbSNP | Ensembl ].
VAR_027421

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 295848C52AAF7DF1

FASTA56160,423
        10         20         30         40         50         60 
MADHNPDSDS TPRTLLRRVL DTADPRTPRR PRSARAGARR ALLETASPRK LSGQTRTIAR 

        70         80         90        100        110        120 
GRSHGARSVG RSAHIQASGH LEEQTPRTLL KNILLTAPES SILMPESVVK PVPAPQAVQP 

       130        140        150        160        170        180 
SRQESSCGSL ELQLPELEPP TTLAPGLLAP GRRKQRLRLS VFQQGVDQGL SLSQEPQGNA 

       190        200        210        220        230        240 
DASSLTRSLN LTFATPLQPQ SVQRPGLARR PPARRAVDVG AFLRDLRDTS LAPPNIVLED 

       250        260        270        280        290        300 
TQPFSQPMVG SPNVYHSLPC TPHTGAEDAE QAAGRKTQSS GPGLQKNSPG KPAQFLAGEA 

       310        320        330        340        350        360 
EEVNAFALGF LSTSSGVSGE DEVEPLHDGV EEAEKKMEEE GVSVSEMEAT GAQGPSRVEE 

       370        380        390        400        410        420 
AEGHTEVTEA EGSQGTAEAD GPGASSGDED ASGRAASPES ASSTPESLQA RRHHQFLEPA 

       430        440        450        460        470        480 
PAPGAAVLSS EPAEPLLVRH PPRPRTTGPR PRQDPHKAGL SHYVKLFSFY AKMPMERKAL 

       490        500        510        520        530        540 
EMVEKCLDKY FQHLCDDLEV FAAHAGRKTV KPEDLELLMR RQGLVTDQVS LHVLVERHLP 

       550        560 
LEYRQLLIPC AYSGNSVFPA Q 

« Hide

Isoform 2 [UniParc].

Checksum: 437895CBF0AD00DC
Show »

FASTA29932,170
Isoform 3 [UniParc].

Checksum: 4A936224C3E78049
Show »

FASTA15116,434

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Brain and Lung.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung and Uterus.
[3]"Comprehensive analysis of the ICEN (Interphase Centromere Complex) components enriched in the CENP-A chromatin of human cells."
Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., Goshima N., Nomura F., Nomura N., Yoda K.
Genes Cells 11:673-684(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]"The human CENP-A centromeric nucleosome-associated complex."
Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III, Cleveland D.W.
Nat. Cell Biol. 8:458-469(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPH; CENPM; CENPN AND CENPU.
[5]"ATM and ATR substrate analysis reveals extensive protein networks responsive 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-385 AND SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[6]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Cancer-upregulated gene 2 (CUG2), a new component of centromere complex, is required for kinetochore function."
Kim H., Lee M., Lee S., Park B., Koh W., Lee D.J., Lim D.S., Lee S.
Mol. Cells 27:697-701(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH CENPA AND CENPW.
[9]"CCAN makes multiple contacts with centromeric DNA to provide distinct pathways to the outer kinetochore."
Hori T., Amano M., Suzuki A., Backer C.B., Welburn J.P., Dong Y., McEwen B.F., Shang W.-H., Suzuki E., Okawa K., Cheeseman I.M., Fukagawa T.
Cell 135:1039-1052(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CENPW.
[10]"Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-A and CENP-B."
Hellwig D., Muench S., Orthaus S., Hoischen C., Hemmerich P., Diekmann S.
J. Biophotonics 1:245-254(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CENPA AND CENPB.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-85 AND SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Induced ectopic kinetochore assembly bypasses the requirement for CENP-A nucleosomes."
Gascoigne K.E., Takeuchi K., Suzuki A., Hori T., Fukagawa T., Cheeseman I.M.
Cell 145:410-422(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPW, PHOSPHORYLATION AT SER-47.
[14]"Premitotic assembly of human CENPs -T and -W switches centromeric chromatin to a mitotic state."
Prendergast L., van Vuuren C., Kaczmarczyk A., Doering V., Hellwig D., Quinn N., Hoischen C., Diekmann S., Sullivan K.F.
PLoS Biol. 9:E1001082-E1001082(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH HISTONE H3, INTERACTION WITH CENPW, SUBCELLULAR LOCATION.
[15]"CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like fold."
Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T., Morikawa K., Cheeseman I.M., Fukagawa T.
Cell 148:487-501(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK023173 mRNA. Translation: BAB14445.1.
AK055237 mRNA. Translation: BAB70884.1.
BC007642 mRNA. Translation: AAH07642.1.
BC007864 mRNA. Translation: AAH07864.2.
BC015202 mRNA. Translation: AAH15202.2.
CCDSCCDS42182.1. [Q96BT3-1]
RefSeqNP_079358.3. NM_025082.3. [Q96BT3-1]
UniGeneHs.288382.

3D structure databases

ProteinModelPortalQ96BT3.
SMRQ96BT3. Positions 465-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123143. 9 interactions.
IntActQ96BT3. 6 interactions.
MINTMINT-1376718.
STRING9606.ENSP00000219172.

PTM databases

PhosphoSiteQ96BT3.

Polymorphism databases

DMDM74760746.

Proteomic databases

MaxQBQ96BT3.
PaxDbQ96BT3.
PRIDEQ96BT3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219172; ENSP00000219172; ENSG00000102901. [Q96BT3-1]
ENST00000440851; ENSP00000400140; ENSG00000102901. [Q96BT3-1]
ENST00000562787; ENSP00000457810; ENSG00000102901. [Q96BT3-1]
GeneID80152.
KEGGhsa:80152.
UCSCuc002eun.4. human. [Q96BT3-1]

Organism-specific databases

CTD80152.
GeneCardsGC16M067862.
HGNCHGNC:25787. CENPT.
HPAHPA048059.
HPA058036.
MIM611510. gene.
neXtProtNX_Q96BT3.
PharmGKBPA142672263.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26624.
HOGENOMHOG000111545.
HOVERGENHBG081089.
InParanoidQ96BT3.
KOK11512.
OMAFSFYAKM.
OrthoDBEOG7TQV2Z.
PhylomeDBQ96BT3.
TreeFamTF332946.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ96BT3.
BgeeQ96BT3.
CleanExHS_CENPT.
GenevestigatorQ96BT3.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR028255. CENP-T.
IPR009072. Histone-fold.
[Graphical view]
PANTHERPTHR14857. PTHR14857. 1 hit.
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCENPT. human.
GeneWikiCENPT.
GenomeRNAi80152.
NextBio70440.
PROQ96BT3.
SOURCESearch...

Entry information

Entry nameCENPT_HUMAN
AccessionPrimary (citable) accession number: Q96BT3
Secondary accession number(s): Q96I29 expand/collapse secondary AC list , Q96IC6, Q96NK9, Q9H901
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM