CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015125
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mis18-binding protein 1 
Protein Synonyms/Alias
 Kinetochore-associated protein KNL-2 homolog; HsKNL-2; P243 
Gene Name
 MIS18BP1 
Gene Synonyms/Alias
 C14orf106; KIAA1903; KNL2; M18BP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MIATPLKHSRIYLPubiquitination[1, 2]
47TPVKDLVKYQNSSLKubiquitination[1, 2]
54KYQNSSLKLNDHKKNubiquitination[2]
65HKKNQFLKMTTFNNKubiquitination[1, 3, 4]
113ANYESPGKIFLRMKEubiquitination[1, 2, 3, 4]
141SSLLEPQKSGNNETFubiquitination[2]
171CEEKENNKSFQSDDSubiquitination[2, 5]
201NDIFLPVKQKIQCQQubiquitination[2, 5, 6]
203IFLPVKQKIQCQQEKubiquitination[2]
211IQCQQEKKAPLHNLTubiquitination[2]
248LTRAQLAKQIFHSKEubiquitination[1, 2]
337TGLPGSMKDTCKIVLubiquitination[2]
341GSMKDTCKIVLATPRubiquitination[1, 2]
378QTVTNGLKKNQVVQLubiquitination[2]
379TVTNGLKKNQVVQLQubiquitination[2]
447MIDQISMKEAGYPNYubiquitination[2, 5]
458YPNYLIRKFMFGFPEubiquitination[3, 4]
534DCDNLELKSNKHSESubiquitination[2, 6, 7]
537NLELKSNKHSESPGAubiquitination[2, 8]
557CHSNCQNKPTLRFPDubiquitination[2]
587SNQELIGKKEYKMSSubiquitination[2, 5]
647YMAINQKKAYILVTPubiquitination[2, 3, 4, 7]
656YILVTPLKSRKVIEQubiquitination[1, 2]
676NLSAGTIKAVTDFVIubiquitination[2]
688FVIPECQKKSPISKSubiquitination[2]
689VIPECQKKSPISKSMubiquitination[2, 7]
694QKKSPISKSMGTLENubiquitination[5]
707ENTFEGHKSKNKEDCubiquitination[2]
709TFEGHKSKNKEDCDEubiquitination[2]
711EGHKSKNKEDCDERDubiquitination[2, 7]
727LTVNRKIKISNLEKEubiquitination[2, 7]
733IKISNLEKEQMLTSDubiquitination[1, 7]
742QMLTSDFKKNTRLLPubiquitination[2, 7]
743MLTSDFKKNTRLLPKubiquitination[2]
797KTKAGNTKEAVVHLRubiquitination[2, 7]
831SENEFYIKQKKARPSubiquitination[2]
840KKARPSVKETLQKSGubiquitination[2]
845SVKETLQKSGVRKEFubiquitination[2]
850LQKSGVRKEFPITEAubiquitination[1, 3, 4]
883QDKEWNEKELQKLHCubiquitination[2]
887WNEKELQKLHCAFASubiquitination[2]
899FASLPKHKPGFWSEVubiquitination[2]
921SPEECQRKYMENPRGubiquitination[2]
956KRGDADQKQTIKITAubiquitination[5]
964QTIKITAKVGTLKRKubiquitination[7]
983EFLEQLPKDDHDDFFubiquitination[2]
1034SVIFPLVKTPQCQHVubiquitination[1]
1056INRNDCDKYVFRMQKubiquitination[2]
1066FRMQKYHKSNGGIVWubiquitination[2, 3, 4]
1078IVWGNIKKKLVETDFubiquitination[2]
1079VWGNIKKKLVETDFSubiquitination[2, 7]
1093STPTPRRKTPFNTDLubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. 
Sequence Annotation
 DOMAIN 875 930 SANT.
 MOD_RES 110 110 Phosphoserine.
 MOD_RES 135 135 Phosphoserine.
 MOD_RES 172 172 Phosphoserine.
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 653 653 Phosphothreonine.
 MOD_RES 772 772 Phosphoserine.
 MOD_RES 773 773 Phosphoserine.
 MOD_RES 821 821 Phosphothreonine.
 MOD_RES 824 824 Phosphoserine.
 MOD_RES 860 860 Phosphoserine.
 MOD_RES 1008 1008 Phosphoserine.
 MOD_RES 1086 1086 Phosphoserine.
 MOD_RES 1087 1087 Phosphothreonine.
 MOD_RES 1089 1089 Phosphothreonine.
 MOD_RES 1104 1104 Phosphoserine.
 MOD_RES 1116 1116 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; DNA-binding; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1132 AA 
Protein Sequence
MIATPLKHSR IYLPPEASSQ RRNLPMDAIF FDSIPSGTLT PVKDLVKYQN SSLKLNDHKK 60
NQFLKMTTFN NKNIFQSTML TEATTSNSSL DISAIKPNKD GLKNKANYES PGKIFLRMKE 120
KVLRDKQEQP SRNSSLLEPQ KSGNNETFTP NRVEKKKLQH TYLCEEKENN KSFQSDDSSL 180
RASVQGVPLE SSNNDIFLPV KQKIQCQQEK KAPLHNLTYE LPTLNQEQEN FLAVEARNKT 240
LTRAQLAKQI FHSKESIVAT TKSKKDTFVL ESVDSADEQF QNTNAETLST NCIPIKNGSL 300
LMVSDSERTT EGTSQQKVKE GNGKTVPGET GLPGSMKDTC KIVLATPRLH ITIPRRSKRN 360
ISKLSPPRIF QTVTNGLKKN QVVQLQEWMI KSINNNTAIC VEGKLIDVTN IYWHSNVIIE 420
RIEHNKLRTI SGNVYILKGM IDQISMKEAG YPNYLIRKFM FGFPENWKEH IDNFLEQLRA 480
GEKNREKTKQ KQKTGRSVRD IRKSMKNDAR ENQTDTAQRA TTTYDFDCDN LELKSNKHSE 540
SPGATELNMC HSNCQNKPTL RFPDDQVNNT IQNGGGDDLS NQELIGKKEY KMSSKKLKIG 600
ERTNERIIKS QKQETTEELD VSIDILTSRE QFFSDEERKY MAINQKKAYI LVTPLKSRKV 660
IEQRCMRYNL SAGTIKAVTD FVIPECQKKS PISKSMGTLE NTFEGHKSKN KEDCDERDLL 720
TVNRKIKISN LEKEQMLTSD FKKNTRLLPK LKKIENQVAM SFYKHQSSPD LSSEESETEK 780
EIKRKAEVKK TKAGNTKEAV VHLRKSTRNT SNIPVILEPE TEESENEFYI KQKKARPSVK 840
ETLQKSGVRK EFPITEAVGS DKTNRHPLEC LPGLIQDKEW NEKELQKLHC AFASLPKHKP 900
GFWSEVAAAV GSRSPEECQR KYMENPRGKG SQKHVTKKKP ANSKGQNGKR GDADQKQTIK 960
ITAKVGTLKR KQQMREFLEQ LPKDDHDDFF STTPLQHQRI LLPSFQDSED DDDILPNMDK 1020
NPTTPSSVIF PLVKTPQCQH VSPGMLGSIN RNDCDKYVFR MQKYHKSNGG IVWGNIKKKL 1080
VETDFSTPTP RRKTPFNTDL GENSGIGKLF TNAVESLDEE EKDYYFSNSD SA 1132 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW. 
Interpro
 IPR009057; Homeodomain-like.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom.
 IPR015216; SANTA. 
Pfam
 PF09133; SANTA 
SMART
 SM00717; SANT 
PROSITE
 PS51293; SANT 
PRINTS