ID F7HML7_MACMU Unreviewed; 2701 AA.
AC F7HML7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Centromere protein E {ECO:0000313|Ensembl:ENSMMUP00000034930.3};
GN Name=CENPE {ECO:0000313|Ensembl:ENSMMUP00000034930.3,
GN ECO:0000313|VGNC:VGNC:71008};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000034930.3, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000034930.3}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000034930.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR SMR; F7HML7; -.
DR STRING; 9544.ENSMMUP00000034930; -.
DR Ensembl; ENSMMUT00000041920.3; ENSMMUP00000034930.3; ENSMMUG00000019089.4.
DR VEuPathDB; HostDB:ENSMMUG00000019089; -.
DR VGNC; VGNC:71008; CENPE.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000160597; -.
DR InParanoid; F7HML7; -.
DR OMA; MQSVEMD; -.
DR OrthoDB; 1118452at2759; -.
DR Proteomes; UP000006718; Chromosome 5.
DR Bgee; ENSMMUG00000019089; Expressed in colon and 15 other cell types or tissues.
DR ExpressionAtlas; F7HML7; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:1990023; C:mitotic spindle midzone; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043515; F:kinetochore binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IEA:Ensembl.
DR GO; GO:0051382; P:kinetochore assembly; IEA:Ensembl.
DR GO; GO:0099607; P:lateral attachment of mitotic spindle microtubules to kinetochore; IEA:Ensembl.
DR GO; GO:0099606; P:microtubule plus-end directed mitotic chromosome migration; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IEA:Ensembl.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:Ensembl.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
DR CDD; cd01374; KISc_CENP_E; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT DOMAIN 6..329
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 2355..2374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2507..2532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2600..2701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 338..365
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 493..604
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 634..776
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 833..993
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1052..1083
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1112..1288
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1323..1385
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1430..1538
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1564..2057
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2325..2352
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2376..2424
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2542..2590
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2601..2621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2622..2636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2701 AA; 316910 MW; 6CF054E358277400 CRC64;
MAEEGAVAVC VRVRPLNSRE ESLGETAQVY WKTDNNAIYQ VDGSKSFNFD RVFHGNETTK
NVYEEIAAPI IDSAIQGYNG TIFAYGQTAS GKTYTMMGSE DHLGVTPRAI HDIFQKIKKF
PDREFLLRVS YMEIYNETIT DLLCGTQKMK PLIIREDVNR NVYVADLTEE VVYTSEMALK
WITKGEKNRH YGETKMNQRS SRSHTIFRMI LESREKGEPS NCEGSVKVSH LNLVDLAGSE
RAAQTGAEGV RLKEGCNINR SLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA
KTRIICTITP VSFDETLTTL QFASTAKYMK NTPYVNEVST DEALLKRYRK EIMDLKKQLE
EVSLETRAQA MEKDQLAQLL EEKDLLQKVQ NEKIENLTRM LVTSSSLTSQ QELKAKRKRR
VTWCLGKINK MKNSNYVDQF NMPTNITTKT HKLSINVLGE IDESVCSESD VFSNTLDTLN
EIEWNPATKL LNQENIESEL NSLRADYDNL VLDYEQLRTE KEEMELKLKE KNDLDEFEAL
ERKTKKDQEM QLIHEISNLK NLVKHAEVYN QDLENELSSK VELLREKEDQ IKKLQEYIDS
QKLENIKMDL SYSLESIEDQ KQMKQTLFDA ETVALDAKRE SAFLRSENLE LKEKMQELAS
TYKQMENDIQ LYQSQLEAKK KMQVDLEKEL QSAFNEITKL TSLIDGKVPK DLLYNLELEG
KITDLQKELN KEVEENEALR KEVNLLSELK SLPSEVERLR KEIHDKSEEL HIITSEKHKL
FSEVVHKESR VQGLLEEIGK TKDDLATTQS NYKSTDQEFQ NFKSLHIDFE QKYKMVLEEN
ARMNQEIVNL SKEAQKFDSS LDALKTELSY KTQELQKKTC EVQERLNEME ELKEQLENRD
STLQTVEREK TLITEKLQQT LEEVKTLTQE KDDLKQLQKS LQIERDQLKS DIHDTVNMNI
DTQEQLRNAL ESLKQHQETI NTLKLKISEE VSRNLHMEEN TGETKDEFQQ KMVDIDKKQD
LEAKNTQTLT ADVKDDEIIE QQRKIFSLIQ EKNELQQVLE SVIAEKEQLK TDLKENIEMT
IENQEELRIL GDELKKQQEI VAQEKNHTIK KEEELSRTCD RLAEVEEKLK EKSQQLQEKQ
QQLLNVQEEM SEMQKKINEM ENLKNELKNK ELTLEHRETE RLGLAQKLNE NYEEMKSITK
ERKVLKELQE SFETERDQLR GYIREIEATG LQTKEELKIA HIHLKEHQET IDELRRSVSE
KTAQIINIQD LEKSYTKLQE EIPVLNEERE LLPNVKEVSE TQETVNELEL LEEQSTIKDS
TTLASIEMER LKLNEKFQES QEEIKSLTKE RDNLKMIKEA LEVKHDQLKE HIRETLAKIQ
ESQSKQEQSL NMKEKDNETT KILSEMEQFK PKDSALLRIE IEMLRLSKRL QESHDEMKSV
AKEKDDLQRL QEVLQSESDQ LKENIKEIAA KHLETEEELK VVHCCLKEQK ETIDELRVNI
SEKETEISTI QKELEAINDK LQNKIQEIYK KEEQLNIKRI SETQEKVNEL KQFKEYLKAK
DSTLQSIESK MLELTSRLQE SQEEIQIMIK EKEEMKRVQE ALQIERDQLQ ENTKEIIAKM
QESQEKEYQF LKMTAVNETQ EKMCEIEHLK EQFETQKLNL ENTETENIRL TQILHENLEE
MRSVTKERDD LRNVEETLKV ERDQLKENLR ETITRDLEKQ EELKIVHMYL KEHQETIDEL
RGIVSEKTNE ISNMQKDLEN SNAALKAQDL KKQEELRIAH MHLKEHQETI DKLRGIVSEK
TDKISNMQKD LENSNAKLQE KIQELKANEH QLFKLKKDVN ETQKKVSEME QLKKQIKDQS
LTLSKIETEN LNLAQKLHEN LEEMKSVMKE RDNLRRVEET LKLERDQLME SLQETKARDL
EIQQELKTAH MLSKEHKETI DKLREKILEK TTQISNIRKD LDKSKDELQK KIQELRKKEL
HLLRMKEDVN MSHKKINEME QLKKQFEAQN LSVQNVRMDN FQLTKKLHES LEEIRIVAKE
RDELRRIKES LKMERDQFVA TLREMIARDQ QNHQVKPEKR LLSDGQQHLT ESLREKCSRI
KELLKRYSEM DDHYECLNRL SLDLEKEIEI QKELSMRVKA NLSLPYLQTK QIEKLFTANQ
RCSMEFHRIM KKLKYVLSYV TKIKEEQHES INKFEMDFID EVEKQKELLI KIQHLQQDCD
VPSRELRDLK LNQNMDLHIE EILKDFSESE FPTIKTEFQQ ILSNRKEMTQ FLEEWLNTRF
DIEKLKNGIQ KENDRICQMN NFFNNRIIAI MNESTEFEER SATISKEWEQ DLKSLKEKNE
KLFKNYQTLK TSLASGAQVN PTTQDNKNPH VTSRATQLTT EKIRELENSL HEAKESAMHK
ESEIIKMQKE LEVTNDMIAK LQAKVNESNK CLETTKETIQ VLQDKVALGA KPYKEEIEDL
KTKLVKIDLE KMKNAKEFEK EISATKATVE YQKEVIRLLR ENLRRSQQAQ DTSMISEHTD
SQPSNKPLTC GGGSGIVQNT KALILKSEHI RLEKEISKLK QQNEQLIKQK NDLLSNNQHL
SNEVKTWKER TLKREAYKQV TCENSPKSPK VTGTASKKKQ ITPSQCKERN LHDPTPKESP
KSWFFDSRSK SLPSPHPVRY FDNSNLGLCP EVQNAGAESV DSQPGPWHAS SGKDVPECKT
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