CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021884
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Scm-like with four MBT domains protein 1 
Protein Synonyms/Alias
  
Gene Name
 Sfmbt1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
792HLDSNPLKWSVADVVubiquitination[1]
Reference
 [1] 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
 Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis. 
Sequence Annotation
 REPEAT 20 120 MBT 1.
 REPEAT 128 232 MBT 2.
 REPEAT 242 346 MBT 3.
 REPEAT 354 451 MBT 4.
 DOMAIN 793 861 SAM.
 MOD_RES 772 772 Phosphoserine (By similarity).  
Keyword
 Chromatin regulator; Complete proteome; Differentiation; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Spermatogenesis; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 863 AA 
Protein Sequence
MSGEQQLDAD LGSGVEVEEF SWEDYLEETG STTVPYASFK HVDIRLQNGF APGMKLEVAL 60
KNDPETYWVA TIITACEQLL LLRYEGYGED RKADFWCDIR KAGLYPIGWC QQNKKTLEAP 120
EGIRDKVSDW NAFLQQTLIG ACGPPVSLLE GLRNGRNPLD LIAPGSKLEC QDFRDSLSTW 180
LVTVVENIGG RLKLRYEGLE SRDGFEHWLY YLDPFLHHIG WAAQQGCDLQ PPLAIKHLKS 240
EADWQEILAK VKEEEPLPSY LFKDKQVIGT HEFSINMKLE AVDPWSPFGI SPATIAKVFD 300
DKYFLVEMDD LRPEDHTRRS FVCHANSPGI FPVQWSLKNG LHINPPPGFR SQDFDWADYL 360
KQCGAEAAPQ KCFPQSISEH QFKENMKLEA VNPLFPEEVC IATVTAVRGS YLWLQLEGSK 420
KPVPEFIVSA ESMNIFPLGW CETNGHPLST PRRARGHKLR KIAVVQPEKQ ILSSRTVHEG 480
LKNQLNSTHS VMINGKYCCP KIYFNHRCFS GPYLNKGRIA ELPQCVGPGN CVLVLREVLT 540
LLINAAYKPS RVLRELQLDK DSVWHGCGEV LKAKYKGKSY RATVEIVRTA DRVTEFCRQT 600
CIKLECCPNL FGPRMVLDTC SENCSVLTKT KYTHYYGKKK NKRIGRPPGG HSNLSCALKK 660
SSKRRKRRKN IFVHKKKRSS ASVDNTPVGS PQGSGGEDEE DADDGDEDSL TEGSTSEQQE 720
ELQEESEVSE KKSSSSSPTQ SETPTPLPPD TQTNKRDAQT SSVSDDENKP PSPKEIRIEV 780
DERLHLDSNP LKWSVADVVR FIRSTDCAPL ARIFLDQEID GQALLLLTLP TVQECMDLKL 840
GPAIKLCHHI ERIKFAFYEQ FAN 863 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR021987; DUF3588.
 IPR004092; Mbt.
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR021129; SAM_type1. 
Pfam
 PF12140; DUF3588
 PF02820; MBT
 PF00536; SAM_1 
SMART
 SM00561; MBT
 SM00454; SAM 
PROSITE
 PS51079; MBT
 PS50105; SAM_DOMAIN 
PRINTS