CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020444
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Centrosomal protein KIAA1731 
Protein Synonyms/Alias
  
Gene Name
 KIAA1731 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23NEEAFILKEDYERRRubiquitination[1]
78WEESQTQKIQNLEKLubiquitination[1, 2, 3, 4]
84QKIQNLEKLYLASLRubiquitination[1]
101GEGHRQAKENEPDLDubiquitination[1, 2, 4]
136LKVQKNQKEILLKQKubiquitination[1]
181LFENIEVKRISAVKTubiquitination[1]
227KRLEELQKQAAQERMubiquitination[1, 2]
239ERMERFEKAHVRGFQubiquitination[1]
259HLAQNQEKLMKELKQubiquitination[1]
265EKLMKELKQLQQEDLubiquitination[1, 2]
384KTQQIPSKVLFKKLLubiquitination[1]
398LNKIRSQKSLWTIKSubiquitination[1]
435ESGTIASKERTLSSGubiquitination[1, 2, 4]
519IMEIEEQKQKQLELLubiquitination[2]
533LEQIEQQKLRLETDCubiquitination[2]
724ETQQRDYKLVPKDSEubiquitination[1, 4]
728RDYKLVPKDSETLSRubiquitination[1]
806PVKVESGKIQEPFSAubiquitination[1, 4]
858QEQLDLQKKVLQATQubiquitination[1, 2, 5]
859EQLDLQKKVLQATQEubiquitination[1]
875QEQLLLCKQKEVEQQubiquitination[1, 3]
877QLLLCKQKEVEQQTGubiquitination[1]
935VISQLQDKRLSLSQPubiquitination[1, 2]
951LSQQNNFKFLQEQLNubiquitination[1]
961QEQLNIQKDSLQARRubiquitination[1, 2, 4]
1027QHSSKSEKGLVSCQSubiquitination[1]
1066LLQEQLTKQRDTLQAubiquitination[1, 2]
1093QRDLGDSKSGLVSSSubiquitination[1, 2, 3]
1117VASQASAKAEPRRIQubiquitination[1, 3]
1131QELYLSEKENVGPSCubiquitination[1]
1180QRVILGAKEGTQEFVubiquitination[1]
1195HTESELEKRISSEQTubiquitination[1, 2]
1235TIPLSHPKIPRCQERubiquitination[1]
1352QPQQDNLKALQEQLAubiquitination[1, 2, 3, 4, 6, 7]
1484QKELVLSKPCKFEEKubiquitination[1]
1487LVLSKPCKFEEKVSSubiquitination[1]
1491KPCKFEEKVSSEHFIubiquitination[1]
1516QQQLDTQKKAIRSIQubiquitination[1, 3]
1517QQLDTQKKAIRSIQEubiquitination[1]
1539QRLSELEKRVSSEQVubiquitination[1, 4]
1565ADSERTQKSFPTKSNubiquitination[1]
1570TQKSFPTKSNDTLPSubiquitination[1]
1594DRLLSLSKPILPQQDubiquitination[1]
1619EVMYSYEKPQEELSLubiquitination[1]
1628QEELSLNKQRKLNKSubiquitination[1]
1631LSLNKQRKLNKSESAubiquitination[1]
1649IPSLFLPKETEHSFIubiquitination[1]
1664PLPFAEAKPKSTCELubiquitination[1, 4]
1666PFAEAKPKSTCELYSubiquitination[1]
1712QDNLGLQKQLDLQREubiquitination[1, 2, 3, 4]
1726EVLHYSQKAQEKLLVubiquitination[1]
1730YSQKAQEKLLVQRQTubiquitination[1]
1751QKHEETLKDFFKDSQubiquitination[1]
1761FKDSQISKPTVENDLubiquitination[1, 2, 4]
1769PTVENDLKTQKMGQLubiquitination[1, 2]
1772ENDLKTQKMGQLRDWubiquitination[1]
1867GRTSILGKPGIYEDRubiquitination[1]
2206RDSSQGMKNQNYPSEubiquitination[2]
2346SLTTQNEKYFENSAEubiquitination[2]
2565YNQLAEVKQQKEEKTubiquitination[1, 4]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] 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
Functional Description
 May be involved in centriole formation or stability. 
Sequence Annotation
 REGION 2478 2601 ALMS motif.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2601 AA 
Protein Sequence
MKRKVVNTHK LRLSPNEEAF ILKEDYERRR KLRLLQVREQ ERDIALQIRE DIKQRRNQQF 60
TRLAEELRAE WEESQTQKIQ NLEKLYLASL RSMGEGHRQA KENEPDLDAL AQRAAERKRK 120
ADLRHKEALK VQKNQKEILL KQKTWHIKAR KEALLVEKER SAKITSLPPP PPTLFENIEV 180
KRISAVKTNS STYHHLHTFV NRETDTKRPD ARLAAEEEAK RLEELQKQAA QERMERFEKA 240
HVRGFQAMKK IHLAQNQEKL MKELKQLQQE DLARRRQTVA QMPPQLVELP YKRSEMKEDW 300
QRELEFAFED MYNADRKVKG NLILHLEPEP LPTVTNQIQD EELDLSMEQE NLGAAEDLPV 360
TEAEICSSET DVPLVMKTQQ IPSKVLFKKL LNKIRSQKSL WTIKSMSEDE SEMITTVSEI 420
ESKAPTVESG TIASKERTLS SGQEQVVESD TLTIESGPLA SEDKPLSCGT NSGKEQEINE 480
TLPITTVAQS SVLLHPQEAA ARIRMSARQK QIMEIEEQKQ KQLELLEQIE QQKLRLETDC 540
FRAQLEEEKR KKTQPTGVGI APASCPVISD EDSHRQMIRN YQHQLLQQNR LHRQSVETAR 600
KQLLEYQTML KGRCPSVSAP SLITDSVISV PSWKSERPTA ISEHWDQGQR LKLSPNKYQP 660
IQPIQTSKLE QDHFQVARQN HFPQRQVETT ETLRASDILT NQALESQEHL RQFSQTETQQ 720
RDYKLVPKDS ETLSRALSHD RQLISQDARK ISETFGATTF QSLESQQLFS ENSENISYHL 780
TEPSSFVPLV PQHSFSSLPV KVESGKIQEP FSAMSKSTVS TSHSIISQMH DRPLLPSENI 840
TAQQGNMKAL QEQLDLQKKV LQATQEAQEQ LLLCKQKEVE QQTGLSVFLP LVTPDSSALL 900
PSAKADLGRI QESSPTKNNI AVSSDHHVIS QLQDKRLSLS QPILSQQNNF KFLQEQLNIQ 960
KDSLQARREA QEVLYVHKQS ELDRRVCSEQ AEPSFPFQVA QHTFTSLPSA DTKSGKIQEQ 1020
HSSKSEKGLV SCQSDIPISQ DGSLSFLQQF LPLHDSLKLL QEQLTKQRDT LQARHEAQVE 1080
LLLHRQRDLG DSKSGLVSSS SSPVVVQHSV ASQASAKAEP RRIQELYLSE KENVGPSCHL 1140
IIPTFQDKSL SFPQHSLAQQ ENLTILQEQS QIQRVILGAK EGTQEFVHTE SELEKRISSE 1200
QTGTSSSLSQ VDESERFQEC ISIKSDSTIP LSHPKIPRCQ ERLLRVSQHM LPLQDNLEEH 1260
QAWLDTEKEA FHFSQKTQEN TSSEQTGSSS FIPQLVQLSF TSLASAESGT ILEPLFTESE 1320
SKIFSSHLQI PQLQDRLLRI SQLIQPQQDN LKALQEQLAT QREAIILARQ EAREELLLHQ 1380
SEWEGRISPE QVDTSSLPLV PQHSFASLPL NESERNQEPC SINSDNIVSS GHSEIPTLPD 1440
GLLGLSHLVL PQQDNLIALE EHLHAQTDFL PSIEKTQKEL VLSKPCKFEE KVSSEHFIQS 1500
HHGDLQALQQ QLDTQKKAIR SIQEVQEELL LQRLSELEKR VSSEQVCSSS FVSQVPVADS 1560
ERTQKSFPTK SNDTLPSSHR EIPRLQDRLL SLSKPILPQQ DNMTAQLDAQ REVMYSYEKP 1620
QEELSLNKQR KLNKSESAEH TIPSLFLPKE TEHSFIPLPF AEAKPKSTCE LYSSQNEHAA 1680
PPSNPVIPGF QDRLLSFSQS VLTQQDNLGL QKQLDLQREV LHYSQKAQEK LLVQRQTALQ 1740
QQIQKHEETL KDFFKDSQIS KPTVENDLKT QKMGQLRDWF PNTQDLAGND QENIRHADRN 1800
NSDDNHLASE DTSAKQSGEH LEKDLGRRSS KPPVAKVKCG LDLNQHELSA IQEVESPAIG 1860
RTSILGKPGI YEDRDPLRVS ISREQSFFGS PLAHDPFSCL QLVGQENVCG DDYDEAVKLK 1920
ESVVENHAVL SYAVEEEHAY LGPTVKPDDK AKTLSYEPLS SATVSTGSLL SYENTDLSLT 1980
DPESFSEHMD DSKQESTTSK EEETNIISSI VPSTQDIYQR QNSSDVHKSL LPAVDETTCG 2040
HTHFQQMIDK YINEANLIPE KTDLQELEHI FPNLHHQLFK PLEPHPDFDL SSSSSGISPD 2100
NRDFYQRSDS SSESHCATGL SKSTVYFTAL RRTSMHSSLN TSPNQQPDTN LAHVGAHSFA 2160
TENIIGGSEQ CFEQLQPEYS SQEESQHADL PSIFSIEARD SSQGMKNQNY PSEEHTEILQ 2220
NKKKIVHFQL SIGNLSSVYS SSDEANVFDQ LNVQHSTPCG SNSSECSTKH QLESRKESMG 2280
FEELSKRGVV TMLQSQGLIE DNKNETCRVL DINPQVEETD SRLCVRTVEM GTSIQAPYSL 2340
TTQNEKYFEN SAETDIPKIT KKLSQLGESE LFASSGSFSL QSSIPVWETE TGHGIMEEPE 2400
LTLISTTDTS IAEMDFANLT LEEKSENEAK CFFQVSEFLP LVSATEASDY PAVSELSIEK 2460
PRTASTETPR RLTPVPGSLQ EAFIKRKKSF MERSHQRQKE IRNKIHVSEN SQIKTVKEKP 2520
SISSSVSRLK GVNKVRASFP EDRKTTQALR HQRGLRLYNQ LAEVKQQKEE KTKQEAYAQN 2580
RARAKEFHKK TLEKLRAKNT C 2601 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB. 
Interpro
 IPR026615; KIAA1731. 
Pfam
  
SMART
  
PROSITE
  
PRINTS