CENPT_HUMAN
ID CENPT_HUMAN Reviewed; 561 AA.
AC Q96BT3; Q96I29; Q96IC6; Q96NK9; Q9H901;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Centromere protein T;
DE Short=CENP-T;
DE AltName: Full=Interphase centromere complex protein 22;
GN Name=CENPT; Synonyms=C16orf56, ICEN22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x;
RA Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y.,
RA Goshima N., Nomura F., Nomura N., Yoda K.;
RT "Comprehensive analysis of the ICEN (Interphase Centromere Complex)
RT components enriched in the CENP-A chromatin of human cells.";
RL Genes Cells 11:673-684(2006).
RN [4]
RP IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPH; CENPM;
RP CENPN AND CENPU.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-385 AND SER-386, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION IN COMPLEX WITH CENPA AND CENPW.
RX PubMed=19533040; DOI=10.1007/s10059-009-0083-2;
RA Kim H., Lee M., Lee S., Park B., Koh W., Lee D.J., Lim D.S., Lee S.;
RT "Cancer-upregulated gene 2 (CUG2), a new component of centromere complex,
RT is required for kinetochore function.";
RL Mol. Cells 27:697-701(2009).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CENPW.
RX PubMed=19070575; DOI=10.1016/j.cell.2008.10.019;
RA Hori T., Amano M., Suzuki A., Backer C.B., Welburn J.P., Dong Y.,
RA McEwen B.F., Shang W.-H., Suzuki E., Okawa K., Cheeseman I.M., Fukagawa T.;
RT "CCAN makes multiple contacts with centromeric DNA to provide distinct
RT pathways to the outer kinetochore.";
RL Cell 135:1039-1052(2008).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CENPA AND CENPB.
RX PubMed=19412974; DOI=10.1002/jbio.200810014;
RA Hellwig D., Muench S., Orthaus S., Hoischen C., Hemmerich P., Diekmann S.;
RT "Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-
RT A and CENP-B.";
RL J. Biophotonics 1:245-254(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-85 AND SER-397, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPW, POSSIBLE
RP INTERACTION WITH THE NDC80 COMPLEX, AND PHOSPHORYLATION AT SER-47.
RX PubMed=21529714; DOI=10.1016/j.cell.2011.03.031;
RA Gascoigne K.E., Takeuchi K., Suzuki A., Hori T., Fukagawa T.,
RA Cheeseman I.M.;
RT "Induced ectopic kinetochore assembly bypasses the requirement for CENP-A
RT nucleosomes.";
RL Cell 145:410-422(2011).
RN [14]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH HISTONE H3, INTERACTION WITH
RP CENPW, AND SUBCELLULAR LOCATION.
RX PubMed=21695110; DOI=10.1371/journal.pbio.1001082;
RA Prendergast L., van Vuuren C., Kaczmarczyk A., Doering V., Hellwig D.,
RA Quinn N., Hoischen C., Diekmann S., Sullivan K.F.;
RT "Premitotic assembly of human CENPs -T and -W switches centromeric
RT chromatin to a mitotic state.";
RL PLoS Biol. 9:E1001082-E1001082(2011).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CENPS; CENPW AND CEPNX.
RX PubMed=22304917; DOI=10.1016/j.cell.2011.11.061;
RA Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T.,
RA Morikawa K., Cheeseman I.M., Fukagawa T.;
RT "CENP-T-W-S-X forms a unique centromeric chromatin structure with a
RT histone-like fold.";
RL Cell 148:487-501(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-343 AND SER-397, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP IDENTIFICATION IN A CENTROMERIC COMPLEX.
RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H.,
RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T.,
RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P.,
RA Angelov D., Hamiche A., Dimitrov S.;
RT "The flexible ends of CENP-A nucleosome are required for mitotic
RT fidelity.";
RL Mol. Cell 63:674-685(2016).
RN [18]
RP INVOLVEMENT IN SSMGA.
RX PubMed=29228025; DOI=10.1371/journal.pone.0189324;
RA Hung C.Y., Volkmar B., Baker J.D., Bauer J.W., Gussoni E., Hainzl S.,
RA Klausegger A., Lorenzo J., Mihalek I., Rittinger O., Tekin M.,
RA Dallman J.E., Bodamer O.A.;
RT "A defect in the inner kinetochore protein CENPT causes a new syndrome of
RT severe growth failure.";
RL PLoS ONE 12:e0189324-e0189324(2017).
CC -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a
CC complex that plays a central role in assembly of kinetochore proteins,
CC mitotic progression and chromosome segregation. The CENPA-NAC complex
CC recruits the CENPA-CAD (nucleosome distal) complex and may be involved
CC in incorporation of newly synthesized CENPA into centromeres. Part of a
CC nucleosome-associated complex that binds specifically to histone H3-
CC containing nucleosomes at the centromere, as opposed to nucleosomes
CC containing CENPA. Component of the heterotetrameric CENP-T-W-S-X
CC complex that binds and supercoils DNA, and plays an important role in
CC kinetochore assembly. CENPT has a fundamental role in kinetochore
CC assembly and function. It is one of the inner kinetochore proteins,
CC with most further proteins binding downstream. Required for normal
CC chromosome organization and normal progress through mitosis.
CC {ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:21529714,
CC ECO:0000269|PubMed:21695110}.
CC -!- SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK,
CC CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is
CC probably recruited on centromeres by the CENPA-NAC complex, at least
CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU
CC (PubMed:16622419, PubMed:19533040, PubMed:19412974). Identified in a
CC centromeric complex containing histones H2A, H2B, H3 and H4, and at
CC least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1
CC (PubMed:19412974, PubMed:21695110, PubMed:27499292). Interacts (via N-
CC terminus) with the NDC80 complex (Probable). Heterodimer with CENPW;
CC this dimer coassembles with CENPS-CENPX heterodimers at centromeres to
CC form the tetrameric CENP-T-W-S-X complex (PubMed:19533040,
CC PubMed:19070575, PubMed:21529714, PubMed:21695110, PubMed:22304917).
CC {ECO:0000269|PubMed:16622419, ECO:0000269|PubMed:19070575,
CC ECO:0000269|PubMed:19412974, ECO:0000269|PubMed:19533040,
CC ECO:0000269|PubMed:21529714, ECO:0000269|PubMed:21695110,
CC ECO:0000269|PubMed:22304917, ECO:0000269|PubMed:27499292,
CC ECO:0000305|PubMed:21529714}.
CC -!- INTERACTION:
CC Q96BT3; Q5EE01: CENPW; NbExp=6; IntAct=EBI-719918, EBI-5529625;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere
CC {ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:19070575,
CC ECO:0000269|PubMed:19412974}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:19412974}. Note=Constitutively localizes to
CC centromeres throughout the cell cycle, and to kinetochores during
CC mitosis. Localizes to the inner kinetochore, and may connect it to the
CC outer kinetochore via its N-terminus. {ECO:0000269|PubMed:19412974}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96BT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96BT3-2; Sequence=VSP_020457, VSP_020458;
CC Name=3;
CC IsoId=Q96BT3-3; Sequence=VSP_020455, VSP_020456;
CC -!- DOMAIN: The largest part of the sequence forms an elongated and
CC flexible stalk structure that is connected to a C-terminal globular
CC domain with a histone-type fold. {ECO:0000250}.
CC -!- PTM: Dynamically phosphorylated at Ser-47 and probably also other sites
CC during the cell cycle. Phosphorylated at Ser-47 during G2 phase,
CC metaphase and anaphase, but not during telophase or G1 phase.
CC {ECO:0000269|PubMed:21529714}.
CC -!- DISEASE: Short stature and microcephaly with genital anomalies (SSMGA)
CC [MIM:618702]: An autosomal recessive disease characterized by growth
CC failure resulting in severe short stature, severe microcephaly, and
CC delayed and dissociated bone age. Additional features include global
CC psychomotor developmental delay, pubertal delay and genital anomalies.
CC {ECO:0000269|PubMed:29228025}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CENP-T/CNN1 family. {ECO:0000305}.
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DR EMBL; AK023173; BAB14445.1; -; mRNA.
DR EMBL; AK055237; BAB70884.1; -; mRNA.
DR EMBL; BC007642; AAH07642.1; -; mRNA.
DR EMBL; BC007864; AAH07864.2; -; mRNA.
DR EMBL; BC015202; AAH15202.2; -; mRNA.
DR CCDS; CCDS42182.1; -. [Q96BT3-1]
DR RefSeq; NP_079358.3; NM_025082.3. [Q96BT3-1]
DR AlphaFoldDB; Q96BT3; -.
DR SMR; Q96BT3; -.
DR BioGRID; 123143; 27.
DR ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR CORUM; Q96BT3; -.
DR IntAct; Q96BT3; 16.
DR MINT; Q96BT3; -.
DR STRING; 9606.ENSP00000457810; -.
DR iPTMnet; Q96BT3; -.
DR PhosphoSitePlus; Q96BT3; -.
DR BioMuta; CENPT; -.
DR DMDM; 74760746; -.
DR EPD; Q96BT3; -.
DR jPOST; Q96BT3; -.
DR MassIVE; Q96BT3; -.
DR MaxQB; Q96BT3; -.
DR PaxDb; Q96BT3; -.
DR PeptideAtlas; Q96BT3; -.
DR PRIDE; Q96BT3; -.
DR ProteomicsDB; 76109; -. [Q96BT3-1]
DR ProteomicsDB; 76110; -. [Q96BT3-2]
DR ProteomicsDB; 76111; -. [Q96BT3-3]
DR Antibodypedia; 29639; 99 antibodies from 24 providers.
DR DNASU; 80152; -.
DR Ensembl; ENST00000440851.6; ENSP00000400140.2; ENSG00000102901.13. [Q96BT3-1]
DR Ensembl; ENST00000562787.6; ENSP00000457810.1; ENSG00000102901.13. [Q96BT3-1]
DR GeneID; 80152; -.
DR KEGG; hsa:80152; -.
DR MANE-Select; ENST00000562787.6; ENSP00000457810.1; NM_025082.4; NP_079358.3.
DR UCSC; uc002eun.4; human. [Q96BT3-1]
DR CTD; 80152; -.
DR DisGeNET; 80152; -.
DR GeneCards; CENPT; -.
DR HGNC; HGNC:25787; CENPT.
DR HPA; ENSG00000102901; Low tissue specificity.
DR MalaCards; CENPT; -.
DR MIM; 611510; gene.
DR MIM; 618702; phenotype.
DR neXtProt; NX_Q96BT3; -.
DR OpenTargets; ENSG00000102901; -.
DR PharmGKB; PA142672263; -.
DR VEuPathDB; HostDB:ENSG00000102901; -.
DR eggNOG; ENOG502RZH1; Eukaryota.
DR GeneTree; ENSGT00390000003044; -.
DR InParanoid; Q96BT3; -.
DR OMA; HHQFPEP; -.
DR PhylomeDB; Q96BT3; -.
DR TreeFam; TF332946; -.
DR PathwayCommons; Q96BT3; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q96BT3; -.
DR SIGNOR; Q96BT3; -.
DR BioGRID-ORCS; 80152; 478 hits in 1078 CRISPR screens.
DR ChiTaRS; CENPT; human.
DR GeneWiki; CENPT; -.
DR GenomeRNAi; 80152; -.
DR Pharos; Q96BT3; Tbio.
DR PRO; PR:Q96BT3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96BT3; protein.
DR Bgee; ENSG00000102901; Expressed in right hemisphere of cerebellum and 103 other tissues.
DR ExpressionAtlas; Q96BT3; baseline and differential.
DR Genevisible; Q96BT3; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR028255; CENP-T.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR032373; CENP-T_N.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR46904; PTHR46904; 1.
DR Pfam; PF15511; CENP-T_C; 1.
DR Pfam; PF16171; CENP-T_N; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA-binding; Dwarfism; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..561
FT /note="Centromere protein T"
FT /id="PRO_0000249514"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..421
FT /note="Flexible stalk domain"
FT /evidence="ECO:0000250"
FT REGION 256..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21529714,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q561R1"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q561R1"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 68..151
FT /note="SVGRSAHIQASGHLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQAVQ
FT PSRQESSCGSLELQLPELEPPTTLAPGLLAPG -> VSTQPTDPKGPWLPRGGGLRSSS
FT ALEPTLRKSQGRRTDWLLGASPIVCWQIGPYSGQWALGGTDTSDAAEEHPTNCPRIFHP
FT DA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020455"
FT VAR_SEQ 152..561
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020456"
FT VAR_SEQ 289..299
FT /note="PGKPAQFLAGE -> ECVALVAWSQI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020457"
FT VAR_SEQ 300..561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020458"
FT VARIANT 115
FT /note="P -> L (in dbSNP:rs12102580)"
FT /id="VAR_027421"
SQ SEQUENCE 561 AA; 60423 MW; 295848C52AAF7DF1 CRC64;
MADHNPDSDS TPRTLLRRVL DTADPRTPRR PRSARAGARR ALLETASPRK LSGQTRTIAR
GRSHGARSVG RSAHIQASGH LEEQTPRTLL KNILLTAPES SILMPESVVK PVPAPQAVQP
SRQESSCGSL ELQLPELEPP TTLAPGLLAP GRRKQRLRLS VFQQGVDQGL SLSQEPQGNA
DASSLTRSLN LTFATPLQPQ SVQRPGLARR PPARRAVDVG AFLRDLRDTS LAPPNIVLED
TQPFSQPMVG SPNVYHSLPC TPHTGAEDAE QAAGRKTQSS GPGLQKNSPG KPAQFLAGEA
EEVNAFALGF LSTSSGVSGE DEVEPLHDGV EEAEKKMEEE GVSVSEMEAT GAQGPSRVEE
AEGHTEVTEA EGSQGTAEAD GPGASSGDED ASGRAASPES ASSTPESLQA RRHHQFLEPA
PAPGAAVLSS EPAEPLLVRH PPRPRTTGPR PRQDPHKAGL SHYVKLFSFY AKMPMERKAL
EMVEKCLDKY FQHLCDDLEV FAAHAGRKTV KPEDLELLMR RQGLVTDQVS LHVLVERHLP
LEYRQLLIPC AYSGNSVFPA Q
