CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001555
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromosome-associated kinesin KIF4A 
Protein Synonyms/Alias
 Chromokinesin-A 
Gene Name
 KIF4A 
Gene Synonyms/Alias
 KIF4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
235KNSSFRSKLHLVDLAubiquitination[1, 2]
429LTEQANEKMNAKLEEubiquitination[1]
433ANEKMNAKLEELRQHubiquitination[1]
593KKDANQAKLSERRRKacetylation[3]
715AAANKRLKDALQKQRubiquitination[1]
840QIADLQQKLLDAESEubiquitination[4, 5]
868LEAKCALKYLIGELVacetylation[6]
883SSKIQVSKLESSLKQacetylation[3]
955LEESVSEKEQQLLSTubiquitination[4, 5]
1095CKGWCGNKQCGCRKQubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Motor protein that translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. May play a role in mitotic chromosomal positioning and bipolar spindle stabilization. 
Sequence Annotation
 DOMAIN 1 349 Kinesin-motor.
 NP_BIND 88 95 ATP (By similarity).
 REGION 663 1232 Interaction with PRC1.
 REGION 1000 1232 Globular.
 MOTIF 793 798 Nuclear localization signal.
 MOD_RES 799 799 Phosphothreonine.
 MOD_RES 801 801 Phosphoserine.
 MOD_RES 951 951 Phosphoserine.
 MOD_RES 995 995 Phosphothreonine.
 MOD_RES 1001 1001 Phosphoserine.
 MOD_RES 1013 1013 Phosphoserine.
 MOD_RES 1017 1017 Phosphoserine.
 MOD_RES 1028 1028 Phosphoserine.
 MOD_RES 1181 1181 Phosphothreonine.
 MOD_RES 1186 1186 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding; Microtubule; Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1232 AA 
Protein Sequence
MKEEVKGIPV RVALRCRPLV PKEISEGCQM CLSFVPGEPQ VVVGTDKSFT YDFVFDPSTE 60
QEEVFNTAVA PLIKGVFKGY NATVLAYGQT GSGKTYSMGG AYTAEQENEP TVGVIPRVIQ 120
LLFKEIDKKS DFEFTLKVSY LEIYNEEILD LLCPSREKAQ INIREDPKEG IKIVGLTEKT 180
VLVALDTVSC LEQGNNSRTV ASTAMNSQSS RSHAIFTISL EQRKKSDKNS SFRSKLHLVD 240
LAGSERQKKT KAEGDRLKEG ININRGLLCL GNVISALGDD KKGGFVPYRD SKLTRLLQDS 300
LGGNSHTLMI ACVSPADSNL EETLNTLRYA DRARKIKNKP IVNIDPQTAE LNHLKQQVQQ 360
LQVLLLQAHG GTLPGSITVE PSENLQSLME KNQSLVEENE KLSRGLSEAA GQTAQMLERI 420
ILTEQANEKM NAKLEELRQH AACKLDLQKL VETLEDQELK ENVEIICNLQ QLITQLSDET 480
VACMAAAIDT AVEQEAQVET SPETSRSSDA FTTQHALRQA QMSKELVELN KALALKEALA 540
RKMTQNDSQL QPIQYQYQDN IKELELEVIN LQKEKEELVL ELQTAKKDAN QAKLSERRRK 600
RLQELEGQIA DLKKKLNEQS KLLKLKESTE RTVSKLNQEI RMMKNQRVQL MRQMKEDAEK 660
FRQWKQKKDK EVIQLKERDR KRQYELLKLE RNFQKQSNVL RRKTEEAAAA NKRLKDALQK 720
QREVADKRKE TQSRGMEGTA ARVKNWLGNE IEVMVSTEEA KRHLNDLLED RKILAQDVAQ 780
LKEKKESGEN PPPKLRRRTF SLTEVRGQVS ESEDSITKQI ESLETEMEFR SAQIADLQQK 840
LLDAESEDRP KQRWENIATI LEAKCALKYL IGELVSSKIQ VSKLESSLKQ SKTSCADMQK 900
MLFEERNHFA EIETELQAEL VRMEQQHQEK VLYLLSQLQQ SQMAEKQLEE SVSEKEQQLL 960
STLKCQDEEL EKMREVCEQN QQLLRENEII KQKLTLLQVA SRQKHLPKDT LLSPDSSFEY 1020
VPPKPKPSRV KEKFLEQSMD IEDLKYCSEH SVNEHEDGDG DDDEGDDEEW KPTKLVKVSR 1080
KNIQGCSCKG WCGNKQCGCR KQKSDCGVDC CCDPTKCRNR QQGKDSLGTV ERTQDSEGSF 1140
KLEDPTEVTP GLSFFNPVCA TPNSKILKEM CDVEQVLSKK TPPAPSPFDL PELKHVATEY 1200
QENKAPGKKK KRALASNTSF FSGCSPIEEE AH 1232 
Gene Ontology
 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005875; C:microtubule associated complex; IEA:InterPro.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005876; C:spindle microtubule; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003777; F:microtubule motor activity; TAS:ProtInc.
 GO:0008089; P:anterograde axon cargo transport; TAS:ProtInc.
 GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0006996; P:organelle organization; TAS:ProtInc. 
Interpro
 IPR027327; KIF4.
 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.