Q96BT3 (CENPT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Centromere protein T
Short name=CENP-T

Alternative name(s):
Interphase centromere complex protein 22

Gene names

Name:	CENPT
Synonyms:	C16orf56, ICEN22

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Protein existence	Evidence 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.12 Ref.13
Subunit structure	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. Ref.4 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14
Subcellular location	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. Ref.3 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14
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.12
Sequence similarities	Belongs to the CENPT family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Kinetochore Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from mutant phenotype Ref.12. Source: UniProtKB kinetochore assembly Inferred from mutant phenotype Ref.12. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome
Cellular_component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome kinetochore Inferred from direct assay Ref.12. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 561	561	Centromere protein T		PRO_0000249514
Regions
	Region	93 – 421	329	Flexible stalk domain By similarity
Amino acid modifications
	Modified residue	47	1	Phosphoserine Ref.11 Ref.12
	Modified residue	85	1	Phosphothreonine Ref.11
	Modified residue	373	1	Phosphoserine Ref.5
	Modified residue	385	1	Phosphoserine Ref.5
	Modified residue	386	1	Phosphoserine Ref.5
	Modified residue	397	1	Phosphoserine Ref.6 Ref.10 Ref.11
Natural variations
	Alternative sequence	68 – 151	84	SVGRS…LLAPG → VSTQPTDPKGPWLPRGGGLR SSSALEPTLRKSQGRRTDWL LGASPIVCWQIGPYSGQWAL GGTDTSDAAEEHPTNCPRIF HPDA in isoform 3.		VSP_020455
	Alternative sequence	152 – 561	410	Missing in isoform 3.		VSP_020456
	Alternative sequence	289 – 299	11	PGKPAQFLAGE → ECVALVAWSQI in isoform 2.		VSP_020457
	Alternative sequence	300 – 561	262	Missing in isoform 2.		VSP_020458
	Natural variant	115	1	P → L. Corresponds to variant rs12102580 [ dbSNP | Ensembl ].		VAR_027421

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 295848C52AAF7DF1	FASTA	561	60,423
	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
	Isoform 2 [UniParc]. Checksum: 437895CBF0AD00DC	FASTA	299	32,170
	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 TQPFSQPMVG SPNVYHSLPC TPHTGAEDAE QAAGRKTQSS GPGLQKNSEC VALVAWSQI
	Isoform 3 [UniParc]. Checksum: 4A936224C3E78049	FASTA	151	16,434
	10 20 30 40 50 60 MADHNPDSDS TPRTLLRRVL DTADPRTPRR PRSARAGARR ALLETASPRK LSGQTRTIAR 70 80 90 100 110 120 GRSHGARVST QPTDPKGPWL PRGGGLRSSS ALEPTLRKSQ GRRTDWLLGA SPIVCWQIGP 130 140 150 YSGQWALGGT DTSDAAEEHP TNCPRIFHPD A

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"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.
[14]	"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.
IPI	IPI00465368. IPI00643513. IPI00787249.
RefSeq	NP_079358.3. NM_025082.3.
UniGene	Hs.288382.
3D structure databases
ProteinModelPortal	Q96BT3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96BT3. 6 interactions.
MINT	MINT-1376718.
STRING	9606.ENSP00000219172.
PTM databases
PhosphoSite	Q96BT3.
Polymorphism databases
DMDM	74760746.
Proteomic databases
PaxDb	Q96BT3.
PRIDE	Q96BT3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219172; ENSP00000219172; ENSG00000102901. ENST00000440851; ENSP00000400140; ENSG00000102901. ENST00000562787; ENSP00000457810; ENSG00000102901.
GeneID	80152.
KEGG	hsa:80152.
UCSC	uc002eun.4. human.
Organism-specific databases
CTD	80152.
GeneCards	GC16M067862.
HGNC	HGNC:25787. CENPT.
MIM	611510. gene.
neXtProt	NX_Q96BT3.
PharmGKB	PA142672263.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG26624.
HOGENOM	HOG000111545.
HOVERGEN	HBG081089.
InParanoid	Q96BT3.
KO	K11512.
OMA	HLEEQTP.
OrthoDB	EOG4HHP2S.
PhylomeDB	Q96BT3.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q96BT3.
Bgee	Q96BT3.
CleanEx	HS_CENPT.
Genevestigator	Q96BT3.
GermOnline	ENSG00000102901. Homo sapiens.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	CENPT. human.
GenomeRNAi	80152.
NextBio	70440.
SOURCE	Search...

Entry information

Entry name

CENPT_HUMAN

Accession

Primary (citable) accession number: Q96BT3
Secondary accession number(s): Q96I29 , Q96IC6, Q96NK9, Q9H901

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	March 1, 2004
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.