CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020610
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Structural maintenance of chromosomes protein 1A 
Protein Synonyms/Alias
 SMC protein 1A; SMC-1-alpha; SMC-1A; Chromosome segregation protein SmcB; Sb1.8 
Gene Name
 Smc1a 
Gene Synonyms/Alias
 Sb1.8; Smc1; Smc1l1; Smcb 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
324KSLQNAQKHYKKRKGacetylation[1]
540AVTKVLGKNMDAIIVacetylation[2]
540AVTKVLGKNMDAIIVubiquitination[3]
561RDCIQYIKEQRGEPEubiquitination[3]
637FGGHQRHKTVALDGTubiquitination[3]
713HGLQMRLKYSQSDLEacetylation[2]
1037KLESVRDKFQETSDEacetylation[1]
Reference
 [1] 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]
 [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] 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
 Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms 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. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. 
Sequence Annotation
 NP_BIND 32 39 ATP (Potential).
 REGION 504 666 Flexible hinge.
 MOD_RES 358 358 Phosphoserine (By similarity).
 MOD_RES 360 360 Phosphoserine (By similarity).
 MOD_RES 648 648 N6-acetyllysine (By similarity).
 MOD_RES 713 713 N6-acetyllysine (By similarity).
 MOD_RES 957 957 Phosphoserine (By similarity).
 MOD_RES 966 966 Phosphoserine (By similarity).
 MOD_RES 970 970 Phosphoserine (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
 1233 AA 
Protein Sequence
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT 60
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE 120
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE 180
DTQFNYHRKK NIAAERKEAK QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK 240
ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK 300
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS 360
QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK 420
IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV 480
MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK 540
NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY 600
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK 660
AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE 720
QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF 780
CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ 840
TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG 900
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGSSQGE 960
ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI 1020
AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN 1080
IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL 1140
LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL 1200
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ 1233 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0000776; C:kinetochore; ISS:UniProtKB.
 GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; ISS:UniProtKB.
 GO:0036033; F:mediator complex binding; IDA:MGI.
 GO:0000075; P:cell cycle checkpoint; ISS:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0030261; P:chromosome condensation; IEA:InterPro.
 GO:0006310; P:DNA recombination; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0007126; P:meiosis; ISS:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0032876; P:negative regulation of DNA endoreduplication; IEA:Compara.
 GO:0009314; P:response to radiation; ISS:UniProtKB.
 GO:0042770; P:signal transduction in response to DNA damage; ISS:UniProtKB.
 GO:0007062; P:sister chromatid cohesion; IEA:Compara.
 GO:0019827; P:stem cell maintenance; IMP:MGI. 
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