CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023314
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Structural maintenance of chromosomes protein 3 
Protein Synonyms/Alias
 SMC protein 3; SMC-3; Basement membrane-associated chondroitin proteoglycan; Bamacan; Chondroitin sulfate proteoglycan 6; Chromosome-associated polypeptide; hCAP 
Gene Name
 SMC3 
Gene Synonyms/Alias
 BAM; BMH; CSPG6; SMC3L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26IVDPFSSKHNVIVGRubiquitination[1, 2, 3, 4, 5]
105LRRVIGAKKDQYFLDacetylation[5, 6, 7, 8, 9, 10, 11]
106RRVIGAKKDQYFLDKacetylation[5, 6, 7, 8, 9, 10, 11]
106RRVIGAKKDQYFLDKubiquitination[3]
118LDKKMVTKNDVMNLLubiquitination[2]
140SNPYYIVKQGKINQMacetylation[7, 10]
140SNPYYIVKQGKINQMubiquitination[2, 3, 5]
143YYIVKQGKINQMATAubiquitination[2, 3, 12]
180EESISLMKETEGKREubiquitination[2]
188ETEGKREKINELLKYubiquitination[1, 4]
194EKINELLKYIEERLHubiquitination[1, 2, 3, 4, 5, 12, 13]
215EELAQYQKWDKMRRAacetylation[7]
215EELAQYQKWDKMRRAubiquitination[1, 3, 4, 12]
308QRTKLELKAKDLQDEubiquitination[12]
310TKLELKAKDLQDELAubiquitination[12]
336ERQKLLEKIEEKQKEacetylation[7, 10, 11]
486EQQALAAKREDLEKKubiquitination[2]
503LLRAATGKAILNGIDubiquitination[3]
592VTFLPLNKLDVRDTAubiquitination[2, 3]
612DAIPMISKLRYNPRFubiquitination[2, 3]
795QLSLEDQKRVDALNDubiquitination[2]
889DLDNSIDKTEAGIKEubiquitination[2]
956LPQEAFEKYQTLSLKacetylation[11]
956LPQEAFEKYQTLSLKubiquitination[1, 4]
963KYQTLSLKQLFRKLEubiquitination[1, 4]
968SLKQLFRKLEQCNTEacetylation[5]
985KYSHVNKKALDQFVNubiquitination[1, 4]
997FVNFSEQKEKLIKRQubiquitination[2]
1012EELDRGYKSIMELMNubiquitination[1, 4]
1025MNVLELRKYEAIQLTubiquitination[1, 4]
1034EAIQLTFKQVSKNFSubiquitination[1, 4, 14]
1038LTFKQVSKNFSEVFQubiquitination[1, 4]
1046NFSEVFQKLVPGGKAubiquitination[2]
1059KATLVMKKGDVEGSQubiquitination[2, 12]
1105IRVSFTGKQGEMREMubiquitination[2, 3]
1190ADKFYGVKFRNKVSHacetylation[7]
1190ADKFYGVKFRNKVSHubiquitination[1, 2, 4]
1194YGVKFRNKVSHIDVIubiquitination[2, 12]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [6] Acetylation of Smc3 by Eco1 is required for S phase sister chromatid cohesion in both human and yeast.
 Zhang J, Shi X, Li Y, Kim BJ, Jia J, Huang Z, Yang T, Fu X, Jung SY, Wang Y, Zhang P, Kim ST, Pan X, Qin J.
 Mol Cell. 2008 Jul 11;31(1):143-51. [PMID: 18614053]
 [7] 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]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [9] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [11] 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]
 [12] 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]
 [13] 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]
 [14] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 
Functional Description
 Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement. 
Sequence Annotation
 NP_BIND 32 39 ATP (Potential).
 REGION 505 667 Flexible hinge.
 MOD_RES 105 105 N6-acetyllysine.
 MOD_RES 106 106 N6-acetyllysine.
 MOD_RES 140 140 N6-acetyllysine.
 MOD_RES 783 783 Phosphothreonine.
 MOD_RES 787 787 Phosphoserine.
 MOD_RES 1013 1013 Phosphoserine (By similarity).
 MOD_RES 1065 1065 Phosphoserine.
 MOD_RES 1067 1067 Phosphoserine.
 MOD_RES 1074 1074 Phosphoserine (By similarity).
 MOD_RES 1083 1083 Phosphoserine.
 MOD_RES 1190 1190 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Disease mutation; DNA damage; DNA repair; Meiosis; Mental retardation; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1217 AA 
Protein Sequence
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ 60
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND 120
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK 180
ETEGKREKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD 240
ELSAKRETSG EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK 300
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FNSVKEKEER 360
GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL 420
EDTEANKEKN LEQYNKLDQD LNEVKARVEE LDRKYYEVKN KKDELQSERN YLWREENAEQ 480
QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLDHFR RKGINQHVQN GYHGIVMNNF 540
ECEPAFYTCV EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY 600
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH 660
RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL RRNIERINNE IDQLMNQMQQ 720
IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE 780
LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL 840
DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS 900
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL 960
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV 1020
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DVEGSQSQDE GEGSGESERG 1080
SGSQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY 1140
LFDEIDQALD AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV 1200
ITAEMAKDFV EDDTTHG 1217 
Gene Ontology
 GO:0005604; C:basement membrane; TAS:ProtInc.
 GO:0000785; C:chromatin; IDA:UniProtKB.
 GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000800; C:lateral element; IEA:Compara.
 GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0034991; C:nuclear meiotic cohesin complex; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0045502; F:dynein binding; IDA:UniProtKB.
 GO:0003777; F:microtubule motor activity; NAS:UniProtKB.
 GO:0000910; P:cytokinesis; TAS:Reactome.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0007126; P:meiosis; IDA:UniProtKB.
 GO:0007067; P:mitosis; TAS:ProtInc.
 GO:0007052; P:mitotic spindle organization; IEP:UniProtKB.
 GO:0032876; P:negative regulation of DNA endoreduplication; IMP:BHF-UCL.
 GO:0007165; P:signal transduction; IDA:UniProtKB.
 GO:0007062; P:sister chromatid cohesion; NAS:UniProtKB.
 GO:0019827; P:stem cell maintenance; IEA:Compara. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR003395; RecF/RecN/SMC.
 IPR010935; SMC_hinge. 
Pfam
 PF06470; SMC_hinge
 PF02463; SMC_N 
SMART
 SM00968; SMC_hinge 
PROSITE
  
PRINTS