ID A0A2K5MZ92_CERAT Unreviewed; 2701 AA.
AC A0A2K5MZ92;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Centromere protein E {ECO:0000313|Ensembl:ENSCATP00000030568.1};
GN Name=CENPE {ECO:0000313|Ensembl:ENSCATP00000030568.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000030568.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000030568.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011884296.1; XM_012028906.1.
DR STRING; 9531.ENSCATP00000030568; -.
DR Ensembl; ENSCATT00000054831.1; ENSCATP00000030568.1; ENSCATG00000038459.1.
DR GeneID; 105571383; -.
DR KEGG; caty:105571383; -.
DR CTD; 1062; -.
DR GeneTree; ENSGT00940000160597; -.
DR OrthoDB; 1118452at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000038459; Expressed in bone marrow and 11 other cell types or tissues.
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: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; IEA:Ensembl.
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: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:UP000233060}.
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..2527
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..769
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 826..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..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; 316646 MW; CE7EA074EA3E4291 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 VSFDETLSTL QFASTAKYMK NTPYVNEVST DEALLKRYRK EIMDLKKQLE
EVSLETRAQA MEKDQLAQLL EEKDLLQKVQ NEKIENLTRM LVTSSSLTSQ QELKAKRKRR
VTWCLGKINK MKNSNYVDQF NMPTNITTKT HKLSVNLLGE 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 KEVEENEALQ KEVNLLSELK SLPSEVERLR KEIHDKSEEL YIITSEKDKL
FSEVVHKESR VQGLLEEIGK TKDDLATTQS NYKNTDQEFQ NFKSLHMDFE QKYKMVLEEN
ARMNQEIVNL SKEAQKFDSS LDALKTELSY KTQELQKKTC EVQERLNEME ELKEQLENRD
STLQTVEREK TLITEKLQQT LEEVKTLTQE KDDLKQLQES LQIERDQLKS DIHDTINMNI
DTQEQLRNAL ESLKQHQETI NTLKLKISEE VSRNLHMEES TGETKDEFQQ KMVGIDKKQD
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 LEKSYTILQE EIPVLNEERE LLPNVKEVSE TQETVNELEL LKEQSTIKDS
TTLASIEMER LKLNEKFQES QEEIKSLTKE RDNLKMIKEA LEVKHDQLKE HIRETLAKIQ
ESQSKQEQSL NMKEKDNETT KILSEMEEFK PKDSALLRIE IEMLRLSKRL QESHDEMKSV
AKEKDDLQRL QEVLQSESDQ LKENIKEIAA KHLETEEELK VVHCCLKEQK ETIDELRVNI
SEKETEISAI QKELEAINDK LQNKIQEIYK KEGQLNIKRI SETQEKVNEL KQFKEHLKAK
DSTLQSIESK MLELTSRLQE SQEEIQIMIK EKEEMKRVQE ALQIERDQLQ ENTKEIIAKM
QESQEKEYQF LKMTAVNETQ EKMCEIEHLK EQFETQKLNL ENIETENIRL TQILHENLEE
MRSVTKERDD LRSVEETLKV ERDQLKENLR ETITRDLEKQ EELKIVHMHL KEHQETIDEL
RGIVSEKTNE ISNMQKDLEN SNAALKAQDL KKQEELRIAH MHLKEHQETI DKLRGIVSEK
TDKISNMQKD LENSNAKLQE KIQELKANEH QLFKLKKDVN ETQKKVSEME QLKKQIKDQS
LTLSKIETEN LNLAQKLHEN LEEMKSVMKE RDNLRRVEET LKLERDQLME SLQETKARDL
EIQQELKTAH MLSKEHKETI DKLREKILEK ATQISNIQKD LDKSKDELQK KIQELRKKEL
HLLRMKEDVN MSHKKINEME QLKKQFEAQN LSMQNVRMDN FQLTKKLHES LEEIRIVAKE
RDELRRIKES LKMERDQFIA TLREMIARDQ QNHQVKPEKR LLSDGQQHLT ESLREKCSRI
KELLKRYSEM DDHYECLNRL SLDLEKEIEI QKELSMRVKA NLSLPYLQTK HIEKLFTANQ
RCSMEFHRIM KKLKYVLSYV TKIKEEQHES INKFEMDFID EVEKQKELLI KIQHLQQDCD
VPSRELRDLK LNQNMDLHTE EILKDFSESE FPTIKTEFQQ ILSNRKEMTQ FLEEWLNTRF
DIEKLKNGIQ KENDRICQMN NFFNNRIIAI MNESTEFEER SATISKEWEQ DLKSLKEKNE
KLFKNYQTLK TSLASGAQVN PTTQDNKNPH VTSRATQLTT EKIRELENSL HEAKESAMHK
ESKIIKMQKE 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
Q
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