CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022133
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Structural maintenance of chromosomes protein 4 
Protein Synonyms/Alias
 SMC protein 4; SMC-4; Chromosome-associated polypeptide C; hCAP-C; XCAP-C homolog 
Gene Name
 SMC4 
Gene Synonyms/Alias
 CAPC; SMC4L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
93HIVNQNFKSYAGEKIubiquitination[1]
99FKSYAGEKILGPFHKubiquitination[1]
106KILGPFHKRFSCIIGubiquitination[1]
153IHNSDEHKDIQSCTVubiquitination[1]
170HFQKIIDKEGDDYEVubiquitination[1]
202SVYHISGKKKTFKDVubiquitination[1, 2, 3, 4]
203VYHISGKKKTFKDVGubiquitination[1]
204YHISGKKKTFKDVGNubiquitination[1]
207SGKKKTFKDVGNLLRubiquitination[1, 2, 3, 4, 5]
239VEQIAMMKPKGQTEHubiquitination[1]
241QIAMMKPKGQTEHDEubiquitination[1]
268GRLNEPIKVLCRRVEubiquitination[1]
293NRVKMVEKEKDALEGubiquitination[1]
341IAEMETQKEKIHEDTubiquitination[1]
343EMETQKEKIHEDTKEubiquitination[1]
349EKIHEDTKEINEKSNubiquitination[1]
381KKLNKITKFIEENKEacetylation[6]
389FIEENKEKFTQLDLEubiquitination[2, 4]
413HATSKAKKLEKQLQKubiquitination[2, 4]
416SKAKKLEKQLQKDKEubiquitination[1]
434EFKSIPAKSNNIINEubiquitination[1]
573TQEETNFKSLVHDLFubiquitination[1]
587FQKVEEAKSSLAMNRubiquitination[1]
598AMNRSRGKVLDAIIQubiquitination[1]
607LDAIIQEKKSGRIPGubiquitination[3]
679DKMAVWAKKMTEIQTacetylation[6]
698PRLFDLVKVKDEKIRubiquitination[5]
760GGGSKVMKGRMGSSLubiquitination[1]
797AMQIQEQKVQLEERVubiquitination[1, 3]
820EMRNTLEKFTASIQRubiquitination[1]
853VLATAPDKKKQKLLEubiquitination[1]
855ATAPDKKKQKLLEENubiquitination[1]
905KLKAQQDKLDKINKQubiquitination[1]
998RNLLQELKVIQENEHubiquitination[1]
1009ENEHALQKDALSIKLubiquitination[1]
1033AEHNSKIKYWHKEISubiquitination[1]
1037SKIKYWHKEISKISLacetylation[6]
1098GAIAEYKKKEELYLQubiquitination[1]
1099AIAEYKKKEELYLQRubiquitination[1]
1112QRVAELDKITYERDSubiquitination[1, 2, 4]
1129QAYEDLRKQRLNEFMubiquitination[3]
1187PPKKSWKKIFNLSGGubiquitination[1, 2, 4, 5]
1267DRLIGIYKTYNITKSubiquitination[1, 2, 3, 4, 5]
1273YKTYNITKSVAVNPKubiquitination[1, 3]
1280KSVAVNPKEIASKGLubiquitination[1, 3]
1285NPKEIASKGLC****ubiquitination[1, 3, 7]
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] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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
 Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. 
Sequence Annotation
 NP_BIND 113 120 ATP (Potential).
 REGION 589 766 Flexible hinge.
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 28 28 Phosphoserine.
 MOD_RES 39 39 Phosphothreonine.
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 50 50 Phosphoserine.
 MOD_RES 143 143 Phosphoserine.
 MOD_RES 679 679 N6-acetyllysine.
 MOD_RES 1056 1056 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil; Complete proteome; Cytoplasm; DNA condensation; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1288 AA 
Protein Sequence
MPRKGTQPST ARRREEGPPP PSPDGASSDA EPEPPSGRTE SPATAAETAS EELDNRSLEE 60
ILNSIPPPPP PAMTNEAGAP RLMITHIVNQ NFKSYAGEKI LGPFHKRFSC IIGPNGSGKS 120
NVIDSMLFVF GYRAQKIRSK KLSVLIHNSD EHKDIQSCTV EVHFQKIIDK EGDDYEVIPN 180
SNFYVSRTAC RDNTSVYHIS GKKKTFKDVG NLLRSHGIDL DHNRFLILQG EVEQIAMMKP 240
KGQTEHDEGM LEYLEDIIGC GRLNEPIKVL CRRVEILNEH RGEKLNRVKM VEKEKDALEG 300
EKNIAIEFLT LENEIFRKKN HVCQYYIYEL QKRIAEMETQ KEKIHEDTKE INEKSNILSN 360
EMKAKNKDVK DTEKKLNKIT KFIEENKEKF TQLDLEDVQV REKLKHATSK AKKLEKQLQK 420
DKEKVEEFKS IPAKSNNIIN ETTTRNNALE KEKEKEEKKL KEVMDSLKQE TQGLQKEKES 480
REKELMGFSK SVNEARSKMD VAQSELDIYL SRHNTAVSQL TKAKEALIAA SETLKERKAA 540
IRDIEGKLPQ TEQELKEKEK ELQKLTQEET NFKSLVHDLF QKVEEAKSSL AMNRSRGKVL 600
DAIIQEKKSG RIPGIYGRLG DLGAIDEKYD VAISSCCHAL DYIVVDSIDI AQECVNFLKR 660
QNIGVATFIG LDKMAVWAKK MTEIQTPENT PRLFDLVKVK DEKIRQAFYF ALRDTLVADN 720
LDQATRVAYQ KDRRWRVVTL QGQIIEQSGT MTGGGSKVMK GRMGSSLVIE ISEEEVNKME 780
SQLQNDSKKA MQIQEQKVQL EERVVKLRHS EREMRNTLEK FTASIQRLIE QEEYLNVQVK 840
ELEANVLATA PDKKKQKLLE ENVSAFKTEY DAVAEKAGKV EAEVKRLHNT IVEINNHKLK 900
AQQDKLDKIN KQLDECASAI TKAQVAIKTA DRNLQKAQDS VLRTEKEIKD TEKEVDDLTA 960
ELKSLEDKAA EVVKNTNAAE ESLPEIQKEH RNLLQELKVI QENEHALQKD ALSIKLKLEQ 1020
IDGHIAEHNS KIKYWHKEIS KISLHPIEDN PIEEISVLSP EDLEAIKNPD SITNQIALLE 1080
ARCHEMKPNL GAIAEYKKKE ELYLQRVAEL DKITYERDSF RQAYEDLRKQ RLNEFMAGFY 1140
IITNKLKENY QMLTLGGDAE LELVDSLDPF SEGIMFSVRP PKKSWKKIFN LSGGEKTLSS 1200
LALVFALHHY KPTPLYFMDE IDAALDFKNV SIVAFYIYEQ TKNAQFIIIS LRNNMFEISD 1260
RLIGIYKTYN ITKSVAVNPK EIASKGLC 1288 
Gene Ontology
 GO:0000796; C:condensin complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; TAS:UniProtKB.
 GO:0005524; F:ATP binding; TAS:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0006310; P:DNA recombination; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:InterPro.
 GO:0051383; P:kinetochore organization; IEA:Compara.
 GO:0010032; P:meiotic chromosome condensation; IEA:Compara.
 GO:0045132; P:meiotic chromosome segregation; IEA:Compara.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
 GO:0007062; P:sister chromatid cohesion; IEA:InterPro. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR003395; RecF/RecN/SMC.
 IPR024704; SMC.
 IPR010935; SMC_hinge. 
Pfam
 PF06470; SMC_hinge
 PF02463; SMC_N 
SMART
 SM00968; SMC_hinge 
PROSITE
  
PRINTS