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Centromere-associated protein E (Centromere protein E) (CENP-E) (Kinesin-7) (Kinesin-related protein CENPE)

 CENPE_HUMAN             Reviewed;        2701 AA.
Q02224; A6NKY9; A8K2U7; Q4LE75;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 2.
28-MAR-2018, entry version 185.
RecName: Full=Centromere-associated protein E;
AltName: Full=Centromere protein E;
Short=CENP-E;
AltName: Full=Kinesin-7 {ECO:0000303|PubMed:25908662};
AltName: Full=Kinesin-related protein CENPE;
Flags: Precursor;
Name=CENPE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS LEU-1535 AND
MET-2090.
PubMed=1406971; DOI=10.1038/359536a0;
Yen T.J., Li G., Schaar B.T., Szilak I., Cleveland D.W.;
"CENP-E is a putative kinetochore motor that accumulates just before
mitosis.";
Nature 359:536-539(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1126 (ISOFORMS 1/2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
FUNCTION.
PubMed=7889940;
Thrower D.A., Jordan M.A., Schaar B.T., Yen T.J., Wilson L.;
"Mitotic HeLa cells contain a CENP-E-associated minus end-directed
microtubule motor.";
EMBO J. 14:918-926(1995).
[7]
INTERACTION WITH CENPF AND BUB1B, AND SUBCELLULAR LOCATION.
PubMed=9763420; DOI=10.1083/jcb.143.1.49;
Chan G.K.T., Schaar B.T., Yen T.J.;
"Characterization of the kinetochore binding domain of CENP-E reveals
interactions with the kinetochore proteins CENP-F and hBUBR1.";
J. Cell Biol. 143:49-63(1998).
[8]
ISOPRENYLATION AT CYS-2698.
PubMed=10852915; DOI=10.1074/jbc.M003469200;
Ashar H.R., James L., Gray K., Carr D., Black S., Armstrong L.,
Bishop W.R., Kirschmeier P.;
"Farnesyl transferase inhibitors block the farnesylation of CENP-E and
CENP-F and alter the association of CENP-E with the microtubules.";
J. Biol. Chem. 275:30451-30457(2000).
[9]
INTERACTION WITH PRC1.
PubMed=15297875; DOI=10.1038/sj.emboj.7600347;
Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.;
"Essential roles of KIF4 and its binding partner PRC1 in organized
central spindle midzone formation.";
EMBO J. 23:3237-3248(2004).
[10]
FUNCTION, INTERACTION WITH NUF2, AND SUBCELLULAR LOCATION.
PubMed=17535814; DOI=10.1074/jbc.M609026200;
Liu D., Ding X., Du J., Cai X., Huang Y., Ward T., Shaw A., Yang Y.,
Hu R., Jin C., Yao X.;
"Human NUF2 interacts with centromere-associated protein E and is
essential for a stable spindle microtubule-kinetochore attachment.";
J. Biol. Chem. 282:21415-21424(2007).
[11]
INTERACTION WITH SEPT7, AND SUBCELLULAR LOCATION.
PubMed=18460473; DOI=10.1074/jbc.M710591200;
Zhu M., Wang F., Yan F., Yao P.Y., Du J., Gao X., Wang X., Wu Q.,
Ward T., Li J., Kioko S., Hu R., Xie W., Ding X., Yao X.;
"Septin 7 interacts with centromere-associated protein E and is
required for its kinetochore localization.";
J. Biol. Chem. 283:18916-18925(2008).
[12]
SUMOYLATION, AND SUBCELLULAR LOCATION.
PubMed=18374647; DOI=10.1016/j.molcel.2008.01.013;
Zhang X.-D., Goeres J., Zhang H., Yen T.J., Porter A.C.G.,
Matunis M.J.;
"SUMO-2/3 modification and binding regulate the association of CENP-E
with kinetochores and progression through mitosis.";
Mol. Cell 29:729-741(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2647, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
INTERACTION WITH KIF18A AND BUB1B.
PubMed=19625775; DOI=10.4161/cc.8.16.9366;
Huang Y., Yao Y., Xu H.-Z., Wang Z.-G., Lu L., Dai W.;
"Defects in chromosome congression and mitotic progression in KIF18A-
deficient cells are partly mediated through impaired functions of
CENP-E.";
Cell Cycle 8:2643-2649(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
INTERACTION WITH SKAP.
PubMed=22110139; DOI=10.1074/jbc.M111.277194;
Huang Y., Wang W., Yao P., Wang X., Liu X., Zhuang X., Yan F.,
Zhou J., Du J., Ward T., Zou H., Zhang J., Fang G., Ding X., Dou Z.,
Yao X.;
"CENP-E kinesin interacts with SKAP protein to orchestrate accurate
chromosome segregation in mitosis.";
J. Biol. Chem. 287:1500-1509(2012).
[17]
FUNCTION.
PubMed=23891108; DOI=10.1016/j.cub.2013.06.040;
Shrestha R.L., Draviam V.M.;
"Lateral to end-on conversion of chromosome-microtubule attachment
requires kinesins CENP-E and MCAK.";
Curr. Biol. 23:1514-1526(2013).
[18]
ERRATUM.
Shrestha R.L., Draviam V.M.;
Curr. Biol. 23:2440-2441(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611; SER-2083; SER-2389;
SER-2639 AND SER-2651, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
FUNCTION.
PubMed=23955301; DOI=10.1038/ncb2831;
Gudimchuk N., Vitre B., Kim Y., Kiyatkin A., Cleveland D.W.,
Ataullakhanov F.I., Grishchuk E.L.;
"Kinetochore kinesin CENP-E is a processive bi-directional tracker of
dynamic microtubule tips.";
Nat. Cell Biol. 15:1079-1088(2013).
[21]
INVOLVEMENT IN MCPH13, VARIANTS MCPH13 ASN-933 AND GLU-1355,
CHARACTERIZATION OF VARIANTS MCPH13 ASN-933 AND GLU-1355, AND VARIANTS
LEU-1535 AND MET-2090.
PubMed=24748105; DOI=10.1007/s00439-014-1443-3;
Mirzaa G.M., Vitre B., Carpenter G., Abramowicz I., Gleeson J.G.,
Paciorkowski A.R., Cleveland D.W., Dobyns W.B., O'Driscoll M.;
"Mutations in CENPE define a novel kinetochore-centromeric mechanism
for microcephalic primordial dwarfism.";
Hum. Genet. 133:1023-1039(2014).
[22]
INTERACTION WITH CTCF, AND SUBCELLULAR LOCATION.
PubMed=26321640; DOI=10.1016/j.celrep.2015.08.005;
Xiao T., Wongtrakoongate P., Trainor C., Felsenfeld G.;
"CTCF recruits centromeric protein CENP-E to the
pericentromeric/centromeric regions of chromosomes through unusual
CTCF-binding sites.";
Cell Rep. 12:1704-1714(2015).
[23]
INTERACTION WITH TRAPPC12, AND SUBCELLULAR LOCATION.
PubMed=25918224; DOI=10.1083/jcb.201501090;
Milev M.P., Hasaj B., Saint-Dic D., Snounou S., Zhao Q., Sacher M.;
"TRAMM/TrappC12 plays a role in chromosome congression, kinetochore
stability, and CENP-E recruitment.";
J. Cell Biol. 209:221-234(2015).
[24]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25395579; DOI=10.1242/jcs.163659;
Bancroft J., Auckland P., Samora C.P., McAinsh A.D.;
"Chromosome congression is promoted by CENP-Q- and CENP-E-dependent
pathways.";
J. Cell Sci. 128:171-184(2015).
[25]
FUNCTION.
PubMed=25743205; DOI=10.1038/ncomms7447;
Iemura K., Tanaka K.;
"Chromokinesin Kid and kinetochore kinesin CENP-E differentially
support chromosome congression without end-on attachment to
microtubules.";
Nat. Commun. 6:6447-6447(2015).
[26]
FUNCTION.
PubMed=25908662; DOI=10.1126/science.aaa5175;
Barisic M., Silva e Sousa R., Tripathy S.K., Magiera M.M.,
Zaytsev A.V., Pereira A.L., Janke C., Grishchuk E.L., Maiato H.;
"Mitosis. Microtubule detyrosination guides chromosomes during
mitosis.";
Science 348:799-803(2015).
[27]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-342 IN COMPLEX WITH ADP,
PROTEIN SEQUENCE OF 2-7, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBUNIT.
PubMed=15236970; DOI=10.1016/j.jmb.2004.05.053;
Garcia-Saez I., Yen T., Wade R.H., Kozielski F.;
"Crystal structure of the motor domain of the human kinetochore
protein CENP-E.";
J. Mol. Biol. 340:1107-1116(2004).
-!- FUNCTION: Microtubule plus-end-directed kinetochore motor which
plays an important role in chromosome congression, microtubule-
kinetochore conjugation and spindle assembly checkpoint
activation. Drives chromosome congression (alignment of
chromosomes at the spindle equator resulting in the formation of
the metaphase plate) by mediating the lateral sliding of polar
chromosomes along spindle microtubules towards the spindle equator
and by aiding the establishment and maintenance of connections
between kinetochores and spindle microtubules (PubMed:7889940,
PubMed:23891108, PubMed:25395579). The transport of pole-proximal
chromosomes towards the spindle equator is favored by microtubule
tracks that are detyrosinated (PubMed:25908662). Acts as a
processive bi-directional tracker of dynamic microtubule tips;
after chromosomes have congressed, continues to play an active
role at kinetochores, enhancing their links with dynamic
microtubule ends (PubMed:23955301). Suppresses chromosome
congression in NDC80-depleted cells and contributes positively to
congression only when microtubules are stabilized
(PubMed:25743205). Plays an important role in the formation of
stable attachments between kinetochores and spindle microtubules
(PubMed:17535814) The stabilization of kinetochore-microtubule
attachment also requires CENPE-dependent localization of other
proteins to the kinetochore including BUB1B, MAD1 and MAD2. Plays
a role in spindle assembly checkpoint activation (SAC) via its
interaction with BUB1B resulting in the activation of its kinase
activity, which is important for activating SAC. Necessary for the
mitotic checkpoint signal at individual kinetochores to prevent
aneuploidy due to single chromosome loss (By similarity).
{ECO:0000250|UniProtKB:Q6RT24, ECO:0000269|PubMed:17535814,
ECO:0000269|PubMed:23891108, ECO:0000269|PubMed:23955301,
ECO:0000269|PubMed:25395579, ECO:0000269|PubMed:25743205,
ECO:0000269|PubMed:25908662, ECO:0000269|PubMed:7889940}.
-!- SUBUNIT: Monomer (PubMed:15236970). Interacts with CENPF
(PubMed:9763420). Interacts with BUB1B (PubMed:9763420,
PubMed:19625775). Interacts with SEPT7 (PubMed:18460473).
Interacts with KIF18A (PubMed:19625775). Interacts with PRC1
(PubMed:15297875). Interacts with NUF2; this interaction
determines kinetochore localization (PubMed:17535814). Interacts
with SKAP; this interaction greatly favors SKAP binding to
microtubules (PubMed:22110139). Interacts with TRAPPC12
(PubMed:25918224). Interacts with CTCF (PubMed:25395579).
{ECO:0000269|PubMed:15236970, ECO:0000269|PubMed:15297875,
ECO:0000269|PubMed:17535814, ECO:0000269|PubMed:18460473,
ECO:0000269|PubMed:19625775, ECO:0000269|PubMed:22110139,
ECO:0000269|PubMed:25395579, ECO:0000269|PubMed:25918224,
ECO:0000269|PubMed:9763420}.
-!- INTERACTION:
O60566:BUB1B; NbExp=4; IntAct=EBI-1375040, EBI-1001438;
Q9Y6D9:MAD1L1; NbExp=2; IntAct=EBI-11108893, EBI-742610;
Q9BZD4:NUF2; NbExp=9; IntAct=EBI-1375040, EBI-724102;
-!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:17535814, ECO:0000269|PubMed:18374647,
ECO:0000269|PubMed:18460473, ECO:0000269|PubMed:25395579,
ECO:0000269|PubMed:25918224, ECO:0000269|PubMed:9763420}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:9763420}.
Chromosome, centromere {ECO:0000269|PubMed:26321640}.
Note=Associates with kinetochores during congression (as early as
prometaphase), relocates to the spindle midzone at anaphase, and
is quantitatively discarded at the end of the cell division (By
similarity). Recruited to the kinetochore in a SEPT7, CENPQ and
TRAPPC12-dependent manner (PubMed:18460473, PubMed:25918224,
PubMed:25395579). Recruited to the pericentromeric/centromeric
regions of the chromosome in a CTCF-dependent manner
(PubMed:26321640). {ECO:0000250|UniProtKB:Q6RT24,
ECO:0000269|PubMed:18460473, ECO:0000269|PubMed:25395579,
ECO:0000269|PubMed:25918224, ECO:0000269|PubMed:26321640}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q02224-1; Sequence=Displayed;
Name=2;
IsoId=Q02224-2; Sequence=VSP_028822;
Name=3;
IsoId=Q02224-3; Sequence=VSP_028820, VSP_028821;
-!- DOMAIN: The protein is composed of a N-terminal kinesin-motor
domain involved in the chromosome movements, a long coil-coiled
region involved in the homodimerization and an inhibitory C-tail
involved in autoinhibition of the N-terminal catalytic part.
{ECO:0000250}.
-!- PTM: The C-terminal inhibitory domain is phosphorylated.
Phosphorylation relieves autoinhibition of the kinetochore motor
(By similarity). {ECO:0000250}.
-!- PTM: Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the
association to the kinetochore. {ECO:0000269|PubMed:18374647}.
-!- DISEASE: Microcephaly 13, primary, autosomal recessive (MCPH13)
[MIM:616051]: A form of microcephaly, a disease defined as a head
circumference more than 3 standard deviations below the age-
related mean. Brain weight is markedly reduced and the cerebral
cortex is disproportionately small. {ECO:0000269|PubMed:24748105}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
-!- SEQUENCE CAUTION:
Sequence=BAE06078.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; Z15005; CAA78727.1; -; mRNA.
EMBL; AB209996; BAE06078.1; ALT_INIT; mRNA.
EMBL; AC079919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX06171.1; -; Genomic_DNA.
EMBL; AK290362; BAF83051.1; -; mRNA.
CCDS; CCDS34042.1; -. [Q02224-1]
CCDS; CCDS68768.1; -. [Q02224-3]
PIR; S28261; S28261.
RefSeq; NP_001273663.1; NM_001286734.1. [Q02224-3]
RefSeq; NP_001804.2; NM_001813.2. [Q02224-1]
UniGene; Hs.75573; -.
PDB; 1T5C; X-ray; 2.50 A; A/B=2-342.
PDB; 5JVP; X-ray; 2.10 A; A/B/C/D/E/F=336-371.
PDBsum; 1T5C; -.
PDBsum; 5JVP; -.
ProteinModelPortal; Q02224; -.
SMR; Q02224; -.
BioGrid; 107491; 41.
DIP; DIP-38902N; -.
IntAct; Q02224; 25.
MINT; Q02224; -.
STRING; 9606.ENSP00000265148; -.
BindingDB; Q02224; -.
ChEMBL; CHEMBL5870; -.
DrugBank; DB06097; GSK-923295.
iPTMnet; Q02224; -.
PhosphoSitePlus; Q02224; -.
BioMuta; CENPE; -.
DMDM; 160358869; -.
EPD; Q02224; -.
MaxQB; Q02224; -.
PaxDb; Q02224; -.
PeptideAtlas; Q02224; -.
PRIDE; Q02224; -.
Ensembl; ENST00000265148; ENSP00000265148; ENSG00000138778. [Q02224-1]
Ensembl; ENST00000380026; ENSP00000369365; ENSG00000138778. [Q02224-3]
GeneID; 1062; -.
KEGG; hsa:1062; -.
UCSC; uc003hxb.1; human. [Q02224-1]
CTD; 1062; -.
DisGeNET; 1062; -.
EuPathDB; HostDB:ENSG00000138778.11; -.
GeneCards; CENPE; -.
H-InvDB; HIX0031416; -.
HGNC; HGNC:1856; CENPE.
HPA; HPA042294; -.
MalaCards; CENPE; -.
MIM; 117143; gene.
MIM; 616051; phenotype.
neXtProt; NX_Q02224; -.
OpenTargets; ENSG00000138778; -.
PharmGKB; PA26400; -.
eggNOG; KOG0242; Eukaryota.
eggNOG; COG5059; LUCA.
GeneTree; ENSGT00910000143992; -.
HOGENOM; HOG000111540; -.
HOVERGEN; HBG097734; -.
InParanoid; Q02224; -.
KO; K11498; -.
OMA; SVCRASW; -.
OrthoDB; EOG091G0CFT; -.
PhylomeDB; Q02224; -.
TreeFam; TF330343; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-983189; Kinesins.
SIGNOR; Q02224; -.
ChiTaRS; CENPE; human.
EvolutionaryTrace; Q02224; -.
GeneWiki; Centromere_protein_E; -.
GenomeRNAi; 1062; -.
PRO; PR:Q02224; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138778; -.
CleanEx; HS_CENPE; -.
ExpressionAtlas; Q02224; baseline and differential.
Genevisible; Q02224; HS.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0005828; C:kinetochore microtubule; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IMP:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
GO; GO:0043515; F:kinetochore binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0051382; P:kinetochore assembly; NAS:UniProtKB.
GO; GO:0099607; P:lateral attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0051310; P:metaphase plate congression; IMP:UniProtKB.
GO; GO:0099606; P:microtubule plus-end directed mitotic chromosome migration; IDA:UniProtKB.
GO; GO:0007018; P:microtubule-based movement; TAS:Reactome.
GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IDA:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR027640; Kinesin-like_fam.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24115; PTHR24115; 7.
Pfam; PF00225; Kinesin; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00129; KISc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell cycle;
Cell division; Centromere; Chromosome; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Developmental protein;
Direct protein sequencing; Disease mutation; Kinetochore; Lipoprotein;
Methylation; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
Phosphoprotein; Polymorphism; Prenylation; Primary microcephaly;
Reference proteome; Ubl conjugation.
CHAIN 1 2698 Centromere-associated protein E.
/FTId=PRO_0000125436.
PROPEP 2699 2701 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000396742.
DOMAIN 6 329 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
NP_BIND 86 93 ATP.
REGION 2126 2476 Kinetochore-binding domain.
REGION 2510 2698 Globular autoinhibitory domain.
{ECO:0000250}.
COILED 336 2590 {ECO:0000255}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2083 2083 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2389 2389 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2639 2639 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2647 2647 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2651 2651 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2698 2698 Cysteine methyl ester. {ECO:0000305}.
LIPID 2698 2698 S-farnesyl cysteine.
{ECO:0000269|PubMed:10852915}.
VAR_SEQ 549 573 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_028820.
VAR_SEQ 1972 2068 IQELQKKELQLLRVKEDVNMSHKKINEMEQLKKQFEAQNLS
MQSVRMDNFQLTKKLHESLEEIRIVAKERDELRRIKESLKM
ERDQFIATLREMIAR -> Q (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_028821.
VAR_SEQ 2131 2166 Missing (in isoform 2).
{ECO:0000303|PubMed:1406971}.
/FTId=VSP_028822.
VARIANT 933 933 D -> N (in MCPH13; results in defective
mitotic spindle formation and chromosome
segregation; results in delayed mitotic
progression; dbSNP:rs144716013).
{ECO:0000269|PubMed:24748105}.
/FTId=VAR_072429.
VARIANT 1355 1355 K -> E (in MCPH13; results in defective
mitotic spindle formation and chromosome
segregation; results in delayed mitotic
progression; dbSNP:rs141488085).
{ECO:0000269|PubMed:24748105}.
/FTId=VAR_072430.
VARIANT 1535 1535 F -> L (in dbSNP:rs2615542).
{ECO:0000269|PubMed:1406971,
ECO:0000269|PubMed:24748105}.
/FTId=VAR_049689.
VARIANT 1581 1581 S -> R (in dbSNP:rs35100664).
/FTId=VAR_049690.
VARIANT 1911 1911 S -> T (in dbSNP:rs1381657).
/FTId=VAR_059370.
VARIANT 1925 1925 E -> D (in dbSNP:rs2306106).
/FTId=VAR_049691.
VARIANT 2090 2090 T -> M (in dbSNP:rs2243682).
{ECO:0000269|PubMed:1406971,
ECO:0000269|PubMed:24748105}.
/FTId=VAR_049692.
CONFLICT 51 51 R -> H (in Ref. 5; BAF83051).
{ECO:0000305}.
CONFLICT 300 300 A -> P (in Ref. 1; CAA78727).
{ECO:0000305}.
CONFLICT 440 440 F -> S (in Ref. 2; BAE06078).
{ECO:0000305}.
CONFLICT 566 566 A -> R (in Ref. 1; CAA78727).
{ECO:0000305}.
CONFLICT 902 902 T -> P (in Ref. 1; CAA78727).
{ECO:0000305}.
CONFLICT 1297 1297 E -> K (in Ref. 1; CAA78727).
{ECO:0000305}.
CONFLICT 1546 1546 K -> N (in Ref. 1; CAA78727).
{ECO:0000305}.
CONFLICT 1876 1876 K -> E (in Ref. 1; CAA78727).
{ECO:0000305}.
CONFLICT 2008 2017 AQNLSMQSVR -> PNYLCKCE (in Ref. 1;
CAA78727). {ECO:0000305}.
CONFLICT 2190 2190 S -> C (in Ref. 1; CAA78727).
{ECO:0000305}.
STRAND 7 13 {ECO:0000244|PDB:1T5C}.
TURN 22 25 {ECO:0000244|PDB:1T5C}.
STRAND 31 34 {ECO:0000244|PDB:1T5C}.
STRAND 37 40 {ECO:0000244|PDB:1T5C}.
STRAND 46 48 {ECO:0000244|PDB:1T5C}.
HELIX 59 65 {ECO:0000244|PDB:1T5C}.
HELIX 68 75 {ECO:0000244|PDB:1T5C}.
STRAND 80 87 {ECO:0000244|PDB:1T5C}.
HELIX 92 96 {ECO:0000244|PDB:1T5C}.
STRAND 100 103 {ECO:0000244|PDB:1T5C}.
HELIX 105 116 {ECO:0000244|PDB:1T5C}.
HELIX 117 119 {ECO:0000244|PDB:1T5C}.
STRAND 123 135 {ECO:0000244|PDB:1T5C}.
STRAND 138 146 {ECO:0000244|PDB:1T5C}.
TURN 157 159 {ECO:0000244|PDB:1T5C}.
HELIX 175 187 {ECO:0000244|PDB:1T5C}.
STRAND 190 197 {ECO:0000244|PDB:1T5C}.
TURN 199 202 {ECO:0000244|PDB:1T5C}.
STRAND 204 215 {ECO:0000244|PDB:1T5C}.
STRAND 226 235 {ECO:0000244|PDB:1T5C}.
HELIX 239 241 {ECO:0000244|PDB:1T5C}.
STRAND 254 256 {ECO:0000244|PDB:1T5C}.
HELIX 260 274 {ECO:0000244|PDB:1T5C}.
HELIX 283 285 {ECO:0000244|PDB:1T5C}.
HELIX 287 291 {ECO:0000244|PDB:1T5C}.
HELIX 293 295 {ECO:0000244|PDB:1T5C}.
STRAND 298 308 {ECO:0000244|PDB:1T5C}.
HELIX 314 326 {ECO:0000244|PDB:1T5C}.
HELIX 341 376 {ECO:0000244|PDB:5JVP}.
SEQUENCE 2701 AA; 316415 MW; 4BC59C2EF0B02D88 CRC64;
MAEEGAVAVC VRVRPLNSRE ESLGETAQVY WKTDNNVIYQ VDGSKSFNFD RVFHGNETTK
NVYEEIAAPI IDSAIQGYNG TIFAYGQTAS GKTYTMMGSE DHLGVIPRAI HDIFQKIKKF
PDREFLLRVS YMEIYNETIT DLLCGTQKMK PLIIREDVNR NVYVADLTEE VVYTSEMALK
WITKGEKSRH YGETKMNQRS SRSHTIFRMI LESREKGEPS NCEGSVKVSH LNLVDLAGSE
RAAQTGAAGV RLKEGCNINR SLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA
KTRIICTITP VSFDETLTAL QFASTAKYMK NTPYVNEVST DEALLKRYRK EIMDLKKQLE
EVSLETRAQA MEKDQLAQLL EEKDLLQKVQ NEKIENLTRM LVTSSSLTLQ QELKAKRKRR
VTWCLGKINK MKNSNYADQF NIPTNITTKT HKLSINLLRE IDESVCSESD VFSNTLDTLS
EIEWNPATKL LNQENIESEL NSLRADYDNL VLDYEQLRTE KEEMELKLKE KNDLDEFEAL
ERKTKKDQEM QLIHEISNLK NLVKHAEVYN QDLENELSSK VELLREKEDQ IKKLQEYIDS
QKLENIKMDL SYSLESIEDP KQMKQTLFDA ETVALDAKRE SAFLRSENLE LKEKMKELAT
TYKQMENDIQ LYQSQLEAKK KMQVDLEKEL QSAFNEITKL TSLIDGKVPK DLLCNLELEG
KITDLQKELN KEVEENEALR EEVILLSELK SLPSEVERLR KEIQDKSEEL HIITSEKDKL
FSEVVHKESR VQGLLEEIGK TKDDLATTQS NYKSTDQEFQ NFKTLHMDFE QKYKMVLEEN
ERMNQEIVNL SKEAQKFDSS LGALKTELSY KTQELQEKTR EVQERLNEME QLKEQLENRD
STLQTVEREK TLITEKLQQT LEEVKTLTQE KDDLKQLQES LQIERDQLKS DIHDTVNMNI
DTQEQLRNAL ESLKQHQETI NTLKSKISEE VSRNLHMEEN TGETKDEFQQ KMVGIDKKQD
LEAKNTQTLT ADVKDNEIIE QQRKIFSLIQ EKNELQQMLE SVIAEKEQLK TDLKENIEMT
IENQEELRLL GDELKKQQEI VAQEKNHAIK KEGELSRTCD RLAEVEEKLK EKSQQLQEKQ
QQLLNVQEEM SEMQKKINEI ENLKNELKNK ELTLEHMETE RLELAQKLNE NYEEVKSITK
ERKVLKELQK SFETERDHLR GYIREIEATG LQTKEELKIA HIHLKEHQET IDELRRSVSE
KTAQIINTQD LEKSHTKLQE EIPVLHEEQE LLPNVKEVSE TQETMNELEL LTEQSTTKDS
TTLARIEMER LRLNEKFQES QEEIKSLTKE RDNLKTIKEA LEVKHDQLKE HIRETLAKIQ
ESQSKQEQSL NMKEKDNETT KIVSEMEQFK PKDSALLRIE IEMLGLSKRL QESHDEMKSV
AKEKDDLQRL QEVLQSESDQ LKENIKEIVA KHLETEEELK VAHCCLKEQE ETINELRVNL
SEKETEISTI QKQLEAINDK LQNKIQEIYE KEEQFNIKQI SEVQEKVNEL KQFKEHRKAK
DSALQSIESK MLELTNRLQE SQEEIQIMIK EKEEMKRVQE ALQIERDQLK ENTKEIVAKM
KESQEKEYQF LKMTAVNETQ EKMCEIEHLK EQFETQKLNL ENIETENIRL TQILHENLEE
MRSVTKERDD LRSVEETLKV ERDQLKENLR ETITRDLEKQ EELKIVHMHL KEHQETIDKL
RGIVSEKTNE ISNMQKDLEH SNDALKAQDL KIQEELRIAH MHLKEQQETI DKLRGIVSEK
TDKLSNMQKD LENSNAKLQE KIQELKANEH QLITLKKDVN ETQKKVSEME QLKKQIKDQS
LTLSKLEIEN LNLAQKLHEN LEEMKSVMKE RDNLRRVEET LKLERDQLKE SLQETKARDL
EIQQELKTAR MLSKEHKETV DKLREKISEK TIQISDIQKD LDKSKDELQK KIQELQKKEL
QLLRVKEDVN MSHKKINEME QLKKQFEAQN LSMQSVRMDN FQLTKKLHES LEEIRIVAKE
RDELRRIKES LKMERDQFIA TLREMIARDR QNHQVKPEKR LLSDGQQHLT ESLREKCSRI
KELLKRYSEM DDHYECLNRL SLDLEKEIEF QKELSMRVKA NLSLPYLQTK HIEKLFTANQ
RCSMEFHRIM KKLKYVLSYV TKIKEEQHES INKFEMDFID EVEKQKELLI KIQHLQQDCD
VPSRELRDLK LNQNMDLHIE EILKDFSESE FPSIKTEFQQ VLSNRKEMTQ FLEEWLNTRF
DIEKLKNGIQ KENDRICQVN NFFNNRIIAI MNESTEFEER SATISKEWEQ DLKSLKEKNE
KLFKNYQTLK TSLASGAQVN PTTQDNKNPH VTSRATQLTT EKIRELENSL HEAKESAMHK
ESKIIKMQKE LEVTNDIIAK LQAKVHESNK CLEKTKETIQ VLQDKVALGA KPYKEEIEDL
KMKLVKIDLE KMKNAKEFEK EISATKATVE YQKEVIRLLR ENLRRSQQAQ DTSVISEHTD
PQPSNKPLTC GGGSGIVQNT KALILKSEHI RLEKEISKLK QQNEQLIKQK NELLSNNQHL
SNEVKTWKER TLKREAHKQV TCENSPKSPK VTGTASKKKQ ITPSQCKERN LQDPVPKESP
KSCFFDSRSK SLPSPHPVRY FDNSSLGLCP EVQNAGAESV DSQPGPWHAS SGKDVPECKT
Q


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