CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007767
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Antigen KI-67 
Protein Synonyms/Alias
  
Gene Name
 MKI67 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11TRRLVTIKRSGVDGPubiquitination[1]
46IQLPVVSKQHCKIEIubiquitination[1]
83IDEPVRLKHGDVITIubiquitination[1, 2, 3]
136FSSDPDEKAQDSKAYubiquitination[1, 3, 4]
141DEKAQDSKAYSKITEubiquitination[1]
145QDSKAYSKITEGKVSubiquitination[1, 2, 4]
150YSKITEGKVSGNPQVubiquitination[3, 4]
163QVHIKNVKEDSTADDubiquitination[1, 4]
219VSRYGELKSVPTTQCubiquitination[3]
232QCLDNSKKNESPFWKubiquitination[3]
254ELDVKSQKENVLQYCubiquitination[1]
263NVLQYCRKSGLQTDYmethylation[5]
263NVLQYCRKSGLQTDYubiquitination[1]
274QTDYATEKESADGLQubiquitination[4]
331ESVQTPSKAVGASFPubiquitination[4]
388EGFKAGDKTLTPRKLacetylation[3]
414DAADSATKPENLSSKubiquitination[4]
421KPENLSSKTRGSIPTubiquitination[1, 3, 4]
502ESEGIPLKRRRVSFGubiquitination[4]
537GEAPTKRKSLVMHTPubiquitination[6, 7]
549HTPPVLKKIIKEQPQubiquitination[1]
552PVLKKIIKEQPQPSGubiquitination[1, 4, 8]
560EQPQPSGKQESGSEIubiquitination[3]
608TAPASSSKSQTEVPKubiquitination[1, 3, 4]
620VPKRGGRKSGNLPSKmethylation[5]
645ILQMICSKRRSGASEubiquitination[1, 2, 8]
659EANLIVAKSWADVVKubiquitination[1, 3, 4, 6, 7, 8]
666KSWADVVKLGAKQTQubiquitination[1, 6, 7, 8]
697RRPATPKKPVGEVHSubiquitination[1]
745NNFISNQKMDFKEDLubiquitination[1, 4, 6, 7, 8, 9]
749SNQKMDFKEDLSGIAubiquitination[1, 4, 9]
760SGIAEMFKTPVKEQPubiquitination[1, 4, 9]
857KMTSLETKTSDTETEubiquitination[1, 4]
867DTETEPSKTVSTANRubiquitination[1, 4]
993LQTQDHAKAPKSEKGacetylation[10]
1035SLGKVGVKEELLAVGubiquitination[1, 3, 6, 7, 8]
1043EELLAVGKFTRTSGEubiquitination[6, 7, 8]
1093KKWPRTPKEEAQSLEubiquitination[4, 9]
1248VAAGKTTKIPCDSPQubiquitination[1]
1294NLMPSAGKAMHTPKPubiquitination[9]
1330TENLTGSKRRPQTPKubiquitination[1, 3, 4]
1402LEKRDVQKELSALKKubiquitination[8]
1517QSKRSLRKVDVEEEFsumoylation[11]
1549KPAVSGEKNIYAFMGubiquitination[6, 7]
1592LEDLAGFKELFQTRGubiquitination[1, 4, 6, 7, 8, 9]
1616KTAKVACKSSQPDPDmethylation[5]
1639RLKTSLGKVGVKEELacetylation[10]
1703QLRTPKGKSEVPEDLubiquitination[4]
1902KLTPSAGKAMHTPKAacetylation[12]
1927FVGTPVEKLDLLGNLubiquitination[4, 9]
1938LGNLPGSKRRPQTPKubiquitination[4, 8, 9]
1949QTPKEKAKALEDLAGubiquitination[4]
1975EESMTDDKITEVSCKubiquitination[9]
2005RLKISLGKVGVKEEVacetylation[10, 12]
2080LEDLAGFKELFQTPDubiquitination[4]
2138VEELSALKQLTQTTHubiquitination[6, 7]
2187QPRTPKGKAQPLEDLubiquitination[4]
2264KRTPSVGKAMDTPKPacetylation[10]
2289FMGTPVQKLDLPGNLubiquitination[6, 7]
2300PGNLPGSKRWPQTPKubiquitination[8]
2320LEDLAGFKELFQTPGubiquitination[4]
2410FVETPVQKLDLLGNLubiquitination[9]
2601TDTATSTKRCPKTRPubiquitination[4]
2652VLKQRAKKKPNPVEEmethylation[5]
2734RVQKVQVKEEPSAVKsumoylation[13]
2967RRVLRAPKVEPVGDVubiquitination[4]
3087QDSVPENKGISLRSRubiquitination[4]
3180SGGQKSAKVLMQNQKubiquitination[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] 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]
 [3] 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]
 [4] 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]
 [5] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] System-wide changes to SUMO modifications in response to heat shock.
 Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT.
 Sci Signal. 2009 May 26;2(72):ra24. [PMID: 19471022]
 [12] Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics.
 Yang YY, Grammel M, Hang HC.
 Bioorg Med Chem Lett. 2011 Sep 1;21(17):4976-9. [PMID: 21669532]
 [13] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634
Functional Description
 Thought to be required for maintaining cell proliferation. 
Sequence Annotation
 DOMAIN 27 76 FHA.
 REPEAT 1000 1112 1.
 REPEAT 1122 1234 2.
 REPEAT 1244 1356 3.
 REPEAT 1366 1477 4.
 REPEAT 1487 1598 5.
 REPEAT 1608 1720 6.
 REPEAT 1730 1842 7.
 REPEAT 1851 1964 8.
 REPEAT 1974 2086 9.
 REPEAT 2096 2204 10.
 REPEAT 2214 2326 11.
 REPEAT 2335 2447 12.
 REPEAT 2457 2569 13.
 REPEAT 2579 2689 14.
 REPEAT 2699 2808 15.
 REPEAT 2818 2928 16.
 NP_BIND 3034 3041 ATP (Potential).
 REGION 1000 2928 16 X 122 AA approximate repeats.
 MOD_RES 125 125 Phosphoserine.
 MOD_RES 264 264 Phosphoserine.
 MOD_RES 308 308 Phosphoserine.
 MOD_RES 328 328 Phosphothreonine.
 MOD_RES 347 347 Phosphothreonine.
 MOD_RES 352 352 Phosphoserine.
 MOD_RES 357 357 Phosphoserine.
 MOD_RES 401 401 Phosphothreonine.
 MOD_RES 579 579 Phosphoserine.
 MOD_RES 584 584 Phosphoserine.
 MOD_RES 648 648 Phosphoserine.
 MOD_RES 761 761 Phosphothreonine.
 MOD_RES 859 859 Phosphoserine.
 MOD_RES 1017 1017 Phosphothreonine.
 MOD_RES 1071 1071 Phosphoserine.
 MOD_RES 1091 1091 Phosphothreonine.
 MOD_RES 1098 1098 Phosphoserine.
 MOD_RES 1111 1111 Phosphothreonine.
 MOD_RES 1131 1131 Phosphoserine.
 MOD_RES 1139 1139 Phosphothreonine.
 MOD_RES 1142 1142 Phosphoserine.
 MOD_RES 1167 1167 Phosphothreonine.
 MOD_RES 1193 1193 Phosphothreonine.
 MOD_RES 1207 1207 Phosphoserine.
 MOD_RES 1233 1233 Phosphothreonine.
 MOD_RES 1253 1253 Phosphoserine.
 MOD_RES 1256 1256 Phosphoserine.
 MOD_RES 1261 1261 Phosphothreonine.
 MOD_RES 1298 1298 Phosphothreonine.
 MOD_RES 1315 1315 Phosphothreonine.
 MOD_RES 1327 1327 Phosphothreonine.
 MOD_RES 1329 1329 Phosphoserine.
 MOD_RES 1335 1335 Phosphothreonine.
 MOD_RES 1355 1355 Phosphothreonine.
 MOD_RES 1376 1376 Phosphoserine.
 MOD_RES 1383 1383 Phosphothreonine.
 MOD_RES 1496 1496 Phosphoserine.
 MOD_RES 1503 1503 Phosphothreonine.
 MOD_RES 1506 1506 Phosphoserine.
 MOD_RES 1540 1540 Phosphothreonine.
 MOD_RES 1552 1552 Phosphotyrosine.
 MOD_RES 1557 1557 Phosphothreonine.
 MOD_RES 1569 1569 Phosphothreonine.
 MOD_RES 1571 1571 Phosphoserine.
 MOD_RES 1639 1639 N6-acetyllysine.
 MOD_RES 1679 1679 Phosphoserine.
 MOD_RES 1689 1689 Phosphoserine.
 MOD_RES 1719 1719 Phosphothreonine.
 MOD_RES 1721 1721 Phosphoserine.
 MOD_RES 1740 1740 Phosphoserine.
 MOD_RES 1747 1747 Phosphothreonine.
 MOD_RES 1764 1764 Phosphothreonine.
 MOD_RES 1784 1784 Phosphothreonine.
 MOD_RES 1801 1801 Phosphothreonine.
 MOD_RES 1815 1815 Phosphoserine.
 MOD_RES 1841 1841 Phosphothreonine.
 MOD_RES 1861 1861 Phosphoserine.
 MOD_RES 1864 1864 Phosphoserine.
 MOD_RES 1869 1869 Phosphothreonine.
 MOD_RES 1897 1897 Phosphothreonine.
 MOD_RES 1923 1923 Phosphothreonine.
 MOD_RES 1937 1937 Phosphoserine.
 MOD_RES 1963 1963 Phosphothreonine.
 MOD_RES 1983 1983 Phosphoserine.
 MOD_RES 2005 2005 N6-acetyllysine.
 MOD_RES 2065 2065 Phosphothreonine.
 MOD_RES 2072 2072 Phosphoserine.
 MOD_RES 2085 2085 Phosphothreonine.
 MOD_RES 2105 2105 Phosphoserine.
 MOD_RES 2113 2113 Phosphothreonine.
 MOD_RES 2135 2135 Phosphoserine.
 MOD_RES 2203 2203 Phosphothreonine.
 MOD_RES 2223 2223 Phosphoserine.
 MOD_RES 2231 2231 Phosphothreonine.
 MOD_RES 2233 2233 Phosphothreonine.
 MOD_RES 2239 2239 Phosphoserine.
 MOD_RES 2268 2268 Phosphothreonine.
 MOD_RES 2285 2285 Phosphothreonine.
 MOD_RES 2325 2325 Phosphothreonine.
 MOD_RES 2328 2328 Phosphothreonine.
 MOD_RES 2333 2333 Phosphothreonine.
 MOD_RES 2344 2344 Phosphoserine.
 MOD_RES 2352 2352 Phosphothreonine.
 MOD_RES 2389 2389 Phosphothreonine.
 MOD_RES 2395 2395 Phosphoserine.
 MOD_RES 2406 2406 Phosphothreonine.
 MOD_RES 2420 2420 Phosphoserine.
 MOD_RES 2446 2446 Phosphothreonine.
 MOD_RES 2528 2528 Phosphoserine.
 MOD_RES 2588 2588 Phosphoserine.
 MOD_RES 2708 2708 Phosphoserine.
 MOD_RES 2827 2827 Phosphoserine.
 MOD_RES 2828 2828 Phosphoserine.
 MOD_RES 3041 3041 Phosphoserine.
 MOD_RES 3128 3128 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle; Chromosome; Complete proteome; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3256 AA 
Protein Sequence
MWPTRRLVTI KRSGVDGPHF PLSLSTCLFG RGIECDIRIQ LPVVSKQHCK IEIHEQEAIL 60
HNFSSTNPTQ VNGSVIDEPV RLKHGDVITI IDRSFRYENE SLQNGRKSTE FPRKIREQEP 120
ARRVSRSSFS SDPDEKAQDS KAYSKITEGK VSGNPQVHIK NVKEDSTADD SKDSVAQGTT 180
NVHSSEHAGR NGRNAADPIS GDFKEISSVK LVSRYGELKS VPTTQCLDNS KKNESPFWKL 240
YESVKKELDV KSQKENVLQY CRKSGLQTDY ATEKESADGL QGETQLLVSR KSRPKSGGSG 300
HAVAEPASPE QELDQNKGKG RDVESVQTPS KAVGASFPLY EPAKMKTPVQ YSQQQNSPQK 360
HKNKDLYTTG RRESVNLGKS EGFKAGDKTL TPRKLSTRNR TPAKVEDAAD SATKPENLSS 420
KTRGSIPTDV EVLPTETEIH NEPFLTLWLT QVERKIQKDS LSKPEKLGTT AGQMCSGLPG 480
LSSVDINNFG DSINESEGIP LKRRRVSFGG HLRPELFDEN LPPNTPLKRG EAPTKRKSLV 540
MHTPPVLKKI IKEQPQPSGK QESGSEIHVE VKAQSLVISP PAPSPRKTPV ASDQRRRSCK 600
TAPASSSKSQ TEVPKRGGRK SGNLPSKRVS ISRSQHDILQ MICSKRRSGA SEANLIVAKS 660
WADVVKLGAK QTQTKVIKHG PQRSMNKRQR RPATPKKPVG EVHSQFSTGH ANSPCTIIIG 720
KAHTEKVHVP ARPYRVLNNF ISNQKMDFKE DLSGIAEMFK TPVKEQPQLT STCHIAISNS 780
ENLLGKQFQG TDSGEEPLLP TSESFGGNVF FSAQNAAKQP SDKCSASPPL RRQCIRENGN 840
VAKTPRNTYK MTSLETKTSD TETEPSKTVS TANRSGRSTE FRNIQKLPVE SKSEETNTEI 900
VECILKRGQK ATLLQQRREG EMKEIERPFE TYKENIELKE NDEKMKAMKR SRTWGQKCAP 960
MSDLTDLKSL PDTELMKDTA RGQNLLQTQD HAKAPKSEKG KITKMPCQSL QPEPINTPTH 1020
TKQQLKASLG KVGVKEELLA VGKFTRTSGE TTHTHREPAG DGKSIRTFKE SPKQILDPAA 1080
RVTGMKKWPR TPKEEAQSLE DLAGFKELFQ TPGPSEESMT DEKTTKIACK SPPPESVDTP 1140
TSTKQWPKRS LRKADVEEEF LALRKLTPSA GKAMLTPKPA GGDEKDIKAF MGTPVQKLDL 1200
AGTLPGSKRQ LQTPKEKAQA LEDLAGFKEL FQTPGHTEEL VAAGKTTKIP CDSPQSDPVD 1260
TPTSTKQRPK RSIRKADVEG ELLACRNLMP SAGKAMHTPK PSVGEEKDII IFVGTPVQKL 1320
DLTENLTGSK RRPQTPKEEA QALEDLTGFK ELFQTPGHTE EAVAAGKTTK MPCESSPPES 1380
ADTPTSTRRQ PKTPLEKRDV QKELSALKKL TQTSGETTHT DKVPGGEDKS INAFRETAKQ 1440
KLDPAASVTG SKRHPKTKEK AQPLEDLAGL KELFQTPVCT DKPTTHEKTT KIACRSQPDP 1500
VDTPTSSKPQ SKRSLRKVDV EEEFFALRKR TPSAGKAMHT PKPAVSGEKN IYAFMGTPVQ 1560
KLDLTENLTG SKRRLQTPKE KAQALEDLAG FKELFQTRGH TEESMTNDKT AKVACKSSQP 1620
DPDKNPASSK RRLKTSLGKV GVKEELLAVG KLTQTSGETT HTHTEPTGDG KSMKAFMESP 1680
KQILDSAASL TGSKRQLRTP KGKSEVPEDL AGFIELFQTP SHTKESMTNE KTTKVSYRAS 1740
QPDLVDTPTS SKPQPKRSLR KADTEEEFLA FRKQTPSAGK AMHTPKPAVG EEKDINTFLG 1800
TPVQKLDQPG NLPGSNRRLQ TRKEKAQALE ELTGFRELFQ TPCTDNPTTD EKTTKKILCK 1860
SPQSDPADTP TNTKQRPKRS LKKADVEEEF LAFRKLTPSA GKAMHTPKAA VGEEKDINTF 1920
VGTPVEKLDL LGNLPGSKRR PQTPKEKAKA LEDLAGFKEL FQTPGHTEES MTDDKITEVS 1980
CKSPQPDPVK TPTSSKQRLK ISLGKVGVKE EVLPVGKLTQ TSGKTTQTHR ETAGDGKSIK 2040
AFKESAKQML DPANYGTGME RWPRTPKEEA QSLEDLAGFK ELFQTPDHTE ESTTDDKTTK 2100
IACKSPPPES MDTPTSTRRR PKTPLGKRDI VEELSALKQL TQTTHTDKVP GDEDKGINVF 2160
RETAKQKLDP AASVTGSKRQ PRTPKGKAQP LEDLAGLKEL FQTPICTDKP TTHEKTTKIA 2220
CRSPQPDPVG TPTIFKPQSK RSLRKADVEE ESLALRKRTP SVGKAMDTPK PAGGDEKDMK 2280
AFMGTPVQKL DLPGNLPGSK RWPQTPKEKA QALEDLAGFK ELFQTPGTDK PTTDEKTTKI 2340
ACKSPQPDPV DTPASTKQRP KRNLRKADVE EEFLALRKRT PSAGKAMDTP KPAVSDEKNI 2400
NTFVETPVQK LDLLGNLPGS KRQPQTPKEK AEALEDLVGF KELFQTPGHT EESMTDDKIT 2460
EVSCKSPQPE SFKTSRSSKQ RLKIPLVKVD MKEEPLAVSK LTRTSGETTQ THTEPTGDSK 2520
SIKAFKESPK QILDPAASVT GSRRQLRTRK EKARALEDLV DFKELFSAPG HTEESMTIDK 2580
NTKIPCKSPP PELTDTATST KRCPKTRPRK EVKEELSAVE RLTQTSGQST HTHKEPASGD 2640
EGIKVLKQRA KKKPNPVEEE PSRRRPRAPK EKAQPLEDLA GFTELSETSG HTQESLTAGK 2700
ATKIPCESPP LEVVDTTAST KRHLRTRVQK VQVKEEPSAV KFTQTSGETT DADKEPAGED 2760
KGIKALKESA KQTPAPAASV TGSRRRPRAP RESAQAIEDL AGFKDPAAGH TEESMTDDKT 2820
TKIPCKSSPE LEDTATSSKR RPRTRAQKVE VKEELLAVGK LTQTSGETTH TDKEPVGEGK 2880
GTKAFKQPAK RKLDAEDVIG SRRQPRAPKE KAQPLEDLAS FQELSQTPGH TEELANGAAD 2940
SFTSAPKQTP DSGKPLKISR RVLRAPKVEP VGDVVSTRDP VKSQSKSNTS LPPLPFKRGG 3000
GKDGSVTGTK RLRCMPAPEE IVEELPASKK QRVAPRARGK SSEPVVIMKR SLRTSAKRIE 3060
PAEELNSNDM KTNKEEHKLQ DSVPENKGIS LRSRRQNKTE AEQQITEVFV LAERIEINRN 3120
EKKPMKTSPE MDIQNPDDGA RKPIPRDKVT ENKRCLRSAR QNESSQPKVA EESGGQKSAK 3180
VLMQNQKGKG EAGNSDSMCL RSRKTKSQPA ASTLESKSVQ RVTRSVKRCA ENPKKAEDNV 3240
CVKKIRTRSH RDSEDI 3256 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IEA:Compara.
 GO:0000793; C:condensed chromosome; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; TAS:UniProtKB.
 GO:0007126; P:meiosis; IEA:Compara. 
Interpro
 IPR000253; FHA_dom.
 IPR012568; K167R.
 IPR008984; SMAD_FHA_domain. 
Pfam
 PF00498; FHA
 PF08065; K167R 
SMART
 SM00240; FHA 
PROSITE
 PS50006; FHA_DOMAIN 
PRINTS