CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038682
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Centromere-associated protein E 
Protein Synonyms/Alias
  
Gene Name
 Cenpe 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
590KVKLLKEKEEQIKNLacetylation[1]
844LEERERLKQEIGALSacetylation[2]
1935EKCFRIEKLLKRYSEacetylation[3]
1938FRIEKLLKRYSEMANacetylation[3]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [3] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Microtubule; Motor protein; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2471 AA 
Protein Sequence
MAEEASVAVC VRVRPLNSRE EELGEATHIY WKTDKNAIYQ SDGGKSFQFD RVFDSNETTK 60
NVYEEIAVPI ISSAIQGYNG TIFAYGQTAS GKTHTMMGSE DCLGVIPRAI HDIFQRIKKF 120
PEREFLLRVS YMEIYNETIT DLLCNAQKMK PLIIREDTNR TVYVSDLTEE VVYTAEMALK 180
WLATGEKNRH YGITKMNQRS SRSHTIFRMI LESREKAEPS NCDGSVKVSH LNLVDLAGSE 240
RAAQTGAEGV RLKEGCFINR NLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA 300
KTRIICTITP ASLDETLTTL QFASTAKYMK NTPYVNEVSN DEALLKRYRR EIADLRKQLE 360
EVNTKTRAQE MEKDQLAQLL DEKDLLQKVQ DEKINNLKRM LVTSSSIALQ QELEIKRKRR 420
VTWCYGKMKD SNYEKEFKVP TSITTRKRKT SVTSLRENSL MKFGESAASS EFEMLNNTLE 480
SLAEVEWSSA TTLLSEENVE SELNSLNAQY NDLVLDYEQL RRENEDLKLK LKEKNELEEF 540
ELLEQKEERD QEMQLMHEVS NLKNLIKHAE EYNQDLENDL SSKVKLLKEK EEQIKNLQEY 600
IDAQKSEKMK IDLSYTSDAT EDLKQAMRTL SDLDTVALDA KKESAFLRSE NLELKEKINE 660
LSDSRKQMES DIQMYQRQLE AKKKMQTDLD KELQLAFQEI SKLSALVDGK GLLSNLELEK 720
RITDLQKELN KEAEEKQTLQ EEVNLLSELK SLPSEVETLR RELYEKSEEL HIITTEREKL 780
FSEMAHKDSR IQGLLEEIGN TRDDLATSQL SRRGSDGEWQ ALESLHAELE HRHAGVLEER 840
ERLKQEIGAL SKEAESLAFS LDSVKAELSH KTQELEQKTV EGQERLNKME ALREELESRD 900
SSLQSVEKEK VLLTEKLQQA LKEVKALTQE KKNLKQLQES LQTERDQLRS DIQDTVNMNI 960
DTQEQLLNAL ESLKQHQETI NMLKMKAAEE LSDNLHVKDR GGARDEAQQK MDGIDEQNES 1020
AHTLLGGGKD NEVTEEQRKI DSLMQENSGL QQTLESVRAE KEQLKMDLKE NIEMSIENQE 1080
ELRILRDELK RQQEVAAQEK DHATEKTQEL SRTQERLAKT EEKLEEKNQK LQETQQQLLS 1140
TQEAMSKLQA KVIDMESLQN EFRNQGLALE RVETEKLELA QRLHESYEEV KSITKERNDL 1200
KELQESFEIE KKQLKEYARE IEAAGLQTKE ELNIAHANLK EYQEIITELR GSISENEAQG 1260
ASTQDTAKSA PELQGEVPEQ ELLPVVKEAR HSAEKVNGLE PVGAHSRTVH SMTMEGIEIE 1320
NLRLTKKLEE SQMEISCLTR EREDLRRTQE TLQVECTQLK EDARRTLANH LETEEELNLA 1380
RCCLKEQENK IDTLITSLSQ RETELSSVRG QLALTTAELE RKVQELCEKQ EELTRKETSE 1440
AQGKMSELEQ LRELLLAQAS ALQNAESDRL RLNTQLEESQ EEMKTLREER EELRRMQEAL 1500
HVESEQQKES MKEISSKLQE LQNKEYECLA MKTINETQGS RCEMDHLNQQ LEAQKSTLEK 1560
VEMENVNLTQ RLHETLEEMR SVAKERDELW SMEERLTVER DQLKKSLEET VTKGMEKEEE 1620
LRVAHVHLEE HQETINKLRK MVSDYTDEIS HTQGDLKHTN AVVEAQNQDL REKEHQLSQV 1680
KADLRETVDQ MEQLKKKLEA QSSTLESREI EKLELTQQLN ENLKKITLVT KENDSLKIMD 1740
EALREERDQL RKSLQQTEAR DLENQEKLRI AHMNLKEHQE TIDRLMETMS EKTEEISNMK 1800
MELENVNMKL QEKVQELKTS ERQRVKLKAD ASEAKKELKE QGLTLSKIEM ENLNLAQKIH 1860
ENLEEMKSVR KERDDLKKLE EILRMERDQL KDNLREAMLK AHQNHEETMK CGKGLLCAGE 1920
YCTGRLREKC FRIEKLLKRY SEMANDYECL NKVSLDLERE TKTQKELSVT VRTKLSLPHT 1980
QTKEMEKLLT ANQRCSLEFH RALKRLKYVL SSIARIKEEQ HESINKREMA FIQEVEKQNE 2040
LQIQIQSLSQ TYRIPARDLQ IKLSQEMDLH IEEMLKDFSE NDFLTIKTEV QQVLNNRKEI 2100
TEFLGKWLNT LFDTENLKST IQKENKSIGL VNNFYHSRIT AMINESTEFE ERSATRSKDL 2160
DQYLKSLKET TEQLSEVYQT LTASQSVVHL HPTVQPSTRD SERPQAASGA EQLTSKNKIA 2220
LGAVPYKEEI EDLKMQLVKS DLEKKATAKE FDKKILSLKA TVEHQEEMIR LLRENLRGHQ 2280
QAQDTSMISE QDSQLLSKPL TCGGGSGIVQ STKALILKSE YKRMGSEISK LKQQNEQLRK 2340
QNNQLLSDNS QLSNEVKTWE ERTLKRDSYR ETTCENSPKS PKVTRTDSKR RQNTTSQCRA 2400
QNLQDPVPKD SPKSWFFDNR SKSLPAPHPI RYFDNSSLGL CPEPDDVENV EPKTDLCQAS 2460
LEKDVSQCKT Q 2471 
Gene Ontology
 GO:0000940; C:condensed chromosome outer kinetochore; IDA:MGI.
 GO:0000778; C:condensed nuclear chromosome kinetochore; IDA:MGI.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005875; C:microtubule associated complex; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0043515; F:kinetochore binding; IEA:Compara.
 GO:0003777; F:microtubule motor activity; IEA:InterPro.
 GO:0008608; P:attachment of spindle microtubules to kinetochore; TAS:MGI.
 GO:0007018; P:microtubule-based movement; IEA:InterPro.
 GO:0045860; P:positive regulation of protein kinase activity; IEA:Compara. 
Interpro
 IPR019821; Kinesin_motor_CS.
 IPR001752; Kinesin_motor_dom.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00225; Kinesin 
SMART
 SM00129; KISc 
PROSITE
 PS00411; KINESIN_MOTOR_DOMAIN1
 PS50067; KINESIN_MOTOR_DOMAIN2 
PRINTS
 PR00380; KINESINHEAVY.