CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019555
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kinesin-like protein KIF20B 
Protein Synonyms/Alias
 Cancer/testis antigen 90; CT90; Kinesin-related motor interacting with PIN1; M-phase phosphoprotein 1; MPP1 
Gene Name
 KIF20B 
Gene Synonyms/Alias
 KRMP1; MPHOSPH1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
104ILGRLSEKSSGQMAQubiquitination[1]
112SSGQMAQKFSFSKVFubiquitination[1]
117AQKFSFSKVFGPATTubiquitination[1]
138GCIMQPVKDLLKGQSubiquitination[1]
190LQERLYTKMNLKPHRubiquitination[1]
216EKEEIASKSALLRQIubiquitination[1]
307LRLSQDVKGYSFIKDubiquitination[1]
424LKNSEKSKFQQHVPFubiquitination[1]
621AQREADFKETLLQERubiquitination[1]
643ERRLAIFKDLVGKCDubiquitination[1, 2]
648IFKDLVGKCDTREEAubiquitination[1]
1493QKYNADRKKWLEEKMubiquitination[3]
1494KYNADRKKWLEEKMMubiquitination[3]
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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Plus-end-directed motor enzyme that is required for completion of cytokinesis. 
Sequence Annotation
 DOMAIN 55 405 Kinesin-motor.
 NP_BIND 152 159 ATP (Potential).
 REGION 1560 1820 Interaction with PIN1.
 MOD_RES 303 303 Phosphoserine (By similarity).
 MOD_RES 488 488 Phosphoserine.
 MOD_RES 1644 1644 Phosphothreonine; by CDK1.
 MOD_RES 1658 1658 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1820 AA 
Protein Sequence
MESNFNQEGV PRPSYVFSAD PIARPSEINF DGIKLDLSHE FSLVAPNTEA NSFESKDYLQ 60
VCLRIRPFTQ SEKELESEGC VHILDSQTVV LKEPQCILGR LSEKSSGQMA QKFSFSKVFG 120
PATTQKEFFQ GCIMQPVKDL LKGQSRLIFT YGLTNSGKTY TFQGTEENIG ILPRTLNVLF 180
DSLQERLYTK MNLKPHRSRE YLRLSSEQEK EEIASKSALL RQIKEVTVHN DSDDTLYGSL 240
TNSLNISEFE ESIKDYEQAN LNMANSIKFS VWVSFFEIYN EYIYDLFVPV SSKFQKRKML 300
RLSQDVKGYS FIKDLQWIQV SDSKEAYRLL KLGIKHQSVA FTKLNNASSR SHSIFTVKIL 360
QIEDSEMSRV IRVSELSLCD LAGSERTMKT QNEGERLRET GNINTSLLTL GKCINVLKNS 420
EKSKFQQHVP FRESKLTHYF QSFFNGKGKI CMIVNISQCY LAYDETLNVL KFSAIAQKVC 480
VPDTLNSSQE KLFGPVKSSQ DVSLDSNSNS KILNVKRATI SWENSLEDLM EDEDLVEELE 540
NAEETQNVET KLLDEDLDKT LEENKAFISH EEKRKLLDLI EDLKKKLINE KKEKLTLEFK 600
IREEVTQEFT QYWAQREADF KETLLQEREI LEENAERRLA IFKDLVGKCD TREEAAKDIC 660
ATKVETEETH NYVGFEDIID SLQDNVADIK KQAEIAHLYI ASLPDPQEAT ACLELKFNQI 720
KAELAKTKGE LIKTKEELKK RENESDSLIQ ELETSNKKII TQNQRIKELI NIIDQKEDTI 780
NEFQNLKSHM ENTFKCNDKA DTSSLIINNK LICNETVEVP KDSKSKICSE RKRVNENELQ 840
QDEPPAKKGT TSAASSRRLR KLISKPKKGV NRTRQTEGHS LVSIHVSSAI TEDQKKSEEV 900
RPNIAEIEDI RVLQENNEGL RAFLLTIENE LKNEKEEKAE LNKQIVHFQQ ELSLSEKKNL 960
TLSKEVQQIQ SNYDIAIAEL HVQKSKNQEQ EEKIMKLSNE IETATRSITN NVSQIKLMHT 1020
KIDELRTLDS VSQISNIDLL NLRDLSNGSE EDNLPNTQLD LLGNDYLVSK QVKEYRIQEP 1080
NRENSFHSSI EAIWEECKEI VKASSKKSHQ IEELEQQIEK LQAEVKGYKD ENNRLKEKEH 1140
KNQDDLLKEK ETLIQQLKEE LQEKNVTLDV QIQHVVEGKR ALSELTQGVT CYKAKIKELE 1200
TILETQKVEC SHSAKLEQDI LEKESIILKL ERNLKEFQEH LQDSVKNTKD LNVKELKLKE 1260
EITQLTNNLQ DMKHLLQLKE EEEETNRQET EKLKEELSAS SARTQNLKAD LQRKEEDYAD 1320
LKEKLTDAKK QIKQVQKEVS VMRDEDKLLR IKINELEKKK NQCSQELDMK QRTIQQLKEQ 1380
LNNQKVEEAI QQYERACKDL NVKEKIIEDM RMTLEEQEQT QVEQDQVLEA KLEEVERLAT 1440
ELEKWKEKCN DLETKNNQRS NKEHENNTDV LGKLTNLQDE LQESEQKYNA DRKKWLEEKM 1500
MLITQAKEAE NIRNKEMKKY AEDRERFFKQ QNEMEILTAQ LTEKDSDLQK WREERDQLVA 1560
ALEIQLKALI SSNVQKDNEI EQLKRIISET SKIETQIMDI KPKRISSADP DKLQTEPLST 1620
SFEISRNKIE DGSVVLDSCE VSTENDQSTR FPKPELEIQF TPLQPNKMAV KHPGCTTPVT 1680
VKIPKARKRK SNEMEEDLVK CENKKNATPR TNLKFPISDD RNSSVKKEQK VAIRPSSKKT 1740
YSLRSQASII GVNLATKKKE GTLQKFGDFL QHSPSILQSK AKKIIETMSS SKLSNVEASK 1800
ENVSQPKRAK RKLYTSEISS PIDISGQVIL MDQKMKESDH QIIKRRLRTK TAK 1853 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005875; C:microtubule associated complex; IEA:InterPro.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IDA:UniProtKB.
 GO:0003777; F:microtubule motor activity; IEA:InterPro.
 GO:0007050; P:cell cycle arrest; NAS:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000087; P:M phase of mitotic cell cycle; TAS:ProtInc.
 GO:0007018; P:microtubule-based movement; IEA:InterPro.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007088; P:regulation of mitosis; NAS:UniProtKB. 
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.