CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020615
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 segregation protein SmcD; Mad member-interacting protein 1 
Gene Name
 Smc3 
Gene Synonyms/Alias
 Bam; Bmh; Cspg6; Mmip1; Smc3l1; Smcd 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
105LRRVIGAKKDQYFLDacetylation[1, 2, 3, 4, 5]
106RRVIGAKKDQYFLDKacetylation[1, 2, 3, 4, 5]
140SNPYYIVKQGKINQMacetylation[2]
194EKINELLKYIEERLHubiquitination[6]
889DLDNSIDKTEAGIKEacetylation[5]
Reference
 [1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] 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]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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 (By similarity).
 MOD_RES 106 106 N6-acetyllysine (By similarity).
 MOD_RES 140 140 N6-acetyllysine (By similarity).
 MOD_RES 783 783 Phosphothreonine (By similarity).
 MOD_RES 787 787 Phosphoserine.
 MOD_RES 1013 1013 Phosphoserine.
 MOD_RES 1065 1065 Phosphoserine.
 MOD_RES 1067 1067 Phosphoserine.
 MOD_RES 1074 1074 Phosphoserine.
 MOD_RES 1083 1083 Phosphoserine.
 MOD_RES 1190 1190 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; DNA damage; DNA repair; Meiosis; 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 SINKVLEHFR 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:0000785; C:chromatin; ISS:UniProtKB.
 GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0000800; C:lateral element; IDA:MGI.
 GO:0016363; C:nuclear matrix; ISS:UniProtKB.
 GO:0034991; C:nuclear meiotic cohesin complex; IDA:MGI.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000922; C:spindle pole; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IDA:MGI.
 GO:0045502; F:dynein binding; ISS:UniProtKB.
 GO:0036033; F:mediator complex binding; IDA:MGI.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0051276; P:chromosome organization; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0007126; P:meiosis; ISS:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
 GO:0032876; P:negative regulation of DNA endoreduplication; IEA:Compara.
 GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
 GO:0007165; P:signal transduction; ISS:UniProtKB.
 GO:0019827; P:stem cell maintenance; IMP:MGI. 
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