CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008324
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kinetochore-associated protein 1 
Protein Synonyms/Alias
 Rough deal homolog; HsROD; Rod; hRod 
Gene Name
 KNTC1 
Gene Synonyms/Alias
 KIAA0166 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
43LVKISSEKASLNPKIubiquitination[1, 2, 3]
185NVDFSTAKKLQGQIKubiquitination[1, 2, 3]
254LIDAEIIKGAKKFQLubiquitination[2]
437KSNHILEKLALSSVDubiquitination[1]
459QQLVDDAKENLHKIQubiquitination[1]
494QEMLNYAKTRLLKKEubiquitination[1, 3]
513LIYSDGLKEVLRAHAubiquitination[1, 3]
605QKLCPWFKNDVIPFVubiquitination[2]
625EGQIILAKWLEQAARubiquitination[2, 4, 5]
713LALSDFEKENTTTIVubiquitination[1]
726IVFRMFDKVLAPELIubiquitination[1]
739LIPSILEKFIRVYMRubiquitination[3]
838KLLQESYKLMEMKKLubiquitination[2]
859REVNLLNKEIMRVVRacetylation[6]
859REVNLLNKEIMRVVRubiquitination[2]
870RVVRYILKQDVPSSLubiquitination[1, 3]
946QEEPDHSKEGKAWRMubiquitination[2]
957AWRMSVAKTSVDILKubiquitination[2]
1029AHEVAQAKHKPGSTPubiquitination[2, 7]
1031EVAQAKHKPGSTPEPubiquitination[1, 2]
1051RSPSMESKLHRQALAubiquitination[2]
1086NIKTALKKCSDLFKYubiquitination[2]
1307FGETTLVKSRHVVMEubiquitination[1, 3]
1316RHVVMELKEKAVIFIacetylation[8]
1413QWGIRLGKLGISFQPubiquitination[1, 2, 3, 7, 9]
1497RHPKLLAKALEMVPLubiquitination[1]
1557NQALSILKHLKSYRRubiquitination[1, 3]
1653KLKPKLLKLTQAKSSubiquitination[2]
1658LLKLTQAKSSTLINKubiquitination[1, 3]
1665KSSTLINKEITKITQubiquitination[1]
1731SQDEKREKAEALLKKubiquitination[1]
1802PDIHAAAKEIAEVNEubiquitination[1, 3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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] 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]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] 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]
 [9] 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
Functional Description
 Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. 
Sequence Annotation
  
Keyword
 Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2209 AA 
Protein Sequence
MWNDIELLTN DDTGSGYLSV GSRKEHGTAL YQVDLLVKIS SEKASLNPKI QACSLSDGFI 60
IVADQSVILL DSICRSLQLH LVFDTEVDVV GLCQEGKFLL VGERSGNLHL IHVTSKQTLL 120
TNAFVQKAND ENRRTYQNLV IEKDGSNEGT YYMLLLTYSG FFCITNLQLL KIQQAIENVD 180
FSTAKKLQGQ IKSSFISTEN YHTLGCLSLV AGDLASEVPV IIGGTGNCAF SKWEPDSSKK 240
GMTVKNLIDA EIIKGAKKFQ LIDNLLFVLD TDNVLSLWDI YTLTPVWNWP SLHVEEFLLT 300
TEADSPSSVT WQGITNLKLI ALTASANKKM KNLMVYSLPT MEILYSLEVS SVSSLVQTGI 360
STDTIYLLEG VCKNDPKLSE DSVSVLVLRC LTEALPENRL SRLLHKHRFA EAESFAIQFG 420
LDVELVYKVK SNHILEKLAL SSVDASEQTE WQQLVDDAKE NLHKIQDDEF VVNYCLKAQW 480
ITYETTQEML NYAKTRLLKK EDKTALIYSD GLKEVLRAHA KLTTFYGAFG PEKFSGSSWI 540
EFLNNEDDLK DIFLQLKEGN LVCAQYLWLR HRANFESRFD VKMLESLLNS MSASVSLQKL 600
CPWFKNDVIP FVRRTVPEGQ IILAKWLEQA ARNLELTDKA NWPENGLQLA EIFFTAEKTD 660
ELGLASSWHW ISLKDYQNTE EVCQLRTLVN NLRELITLHR KYNCKLALSD FEKENTTTIV 720
FRMFDKVLAP ELIPSILEKF IRVYMREHDL QEEELLLLYI EDLLNRCSSK STSLFETAWE 780
AKAMAVIACL SDTDLIFDAV LKIMYAAVVP WSAAVEQLVK QHLEMDHPKV KLLQESYKLM 840
EMKKLLRGYG IREVNLLNKE IMRVVRYILK QDVPSSLEDA LKVAQAFMLS DDEIYSLRII 900
DLIDREQGED CLLLLKSLPP AEAEKTAERV IIWARLALQE EPDHSKEGKA WRMSVAKTSV 960
DILKILCDIQ KDNLQKKDEC EEMLKLFKEV ASLQENFEVF LSFEDYSNSS LVADLREQHI 1020
KAHEVAQAKH KPGSTPEPIA AEVRSPSMES KLHRQALALQ MSKQELEAEL TLRALKDGNI 1080
KTALKKCSDL FKYHCNADTG KLLFLTCQKL CQMLADNVPV TVPVGLNLPS MIHDLASQAA 1140
TICSPDFLLD ALELCKHTLM AVELSRQCQM DDCGILMKAS FGTHKDPYEE WSYSDFFSED 1200
GIVLESQMVL PVIYELISSL VPLAESKRYP LESTSLPYCS LNEGDGLVLP VINSISALLQ 1260
NLQESSQWEL ALRFVVGSFG TCLQHSVSNF MNATLSEKLF GETTLVKSRH VVMELKEKAV 1320
IFIRENATTL LHKVFNCRLV DLDLALGYCT LLPQKDVFEN LWKLIDKAWQ NYDKILAISL 1380
VGSELASLYQ EIEMGLKFRE LSTDAQWGIR LGKLGISFQP VFRQHFLTKK DLIKALVENI 1440
DMDTSLILEY CSTFQLDCDA VLQLFIETLL HNTNAGQGQG DASMDSAKRR HPKLLAKALE 1500
MVPLLTSTKD LVISLSGILH KLDPYDYEMI EVVLKVIERA DEKITNININ QALSILKHLK 1560
SYRRISPPVD LEYQYMLEHV ITLPSAAQTR LPFHLIFFGT AQNFWKILST ELSEESFPTL 1620
LLISKLMKFS LDTLYVSTAK HVFEKKLKPK LLKLTQAKSS TLINKEITKI TQTIESCLLS 1680
IVNPEWAVAI AISLAQDIPE GSFKISALKF CLYLAERWLQ NIPSQDEKRE KAEALLKKLH 1740
IQYRRSGTEA VLIAHKLNTE EYLRVIGKPA HLIVSLYEHP SINQRIQNSS GTDYPDIHAA 1800
AKEIAEVNEI NLEKVWDMLL EKWLCPSTKP GEKPSELFEL QEDEALRRVQ YLLLSRPIDY 1860
SSRMLFVFAT STTTTLGMHQ LTFAHRTRAL QCLFYLADKE TIESLFKKPI EEVKSYLRCI 1920
TFLASFETLN IPITYELFCS SPKEGMIKGL WKNHSHESMA VRLVTELCLE YKIYDLQLWN 1980
GLLQKLLGFN MIPYLRKVLK AISSIHSLWQ VPYFSKAWQR VIQIPLLSAS CPLSPDQLSD 2040
CSESLIAVLE CPVSGDLDLI GVARQYIQLE LPAFALACLM LMPHSEKRHQ QIKNFLGSCD 2100
PQVILKQLEE HMNTGQLAGF SHQIRSLILN NIINKKEFGI LAKTKYFQML KMHAMNTNNI 2160
TELVNYLAND LSLDEASVLI TEYSKHCGKP VPPDTAPCEI LKMFLSGLS 2209 
Gene Ontology
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005828; C:kinetochore microtubule; IDA:UniProtKB.
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0007093; P:mitotic cell cycle checkpoint; IDA:UniProtKB.
 GO:0006461; P:protein complex assembly; NAS:UniProtKB.
 GO:0007096; P:regulation of exit from mitosis; NAS:UniProtKB. 
Interpro
 IPR019527; RZZ-complex_KNTC1/ROD_C. 
Pfam
 PF10493; Rod_C 
SMART
  
PROSITE
  
PRINTS