CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005685
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable global transcription activator SNF2L1 
Protein Synonyms/Alias
 ATP-dependent helicase SMARCA1; Nucleosome-remodeling factor subunit SNF2L; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1 
Gene Name
 SMARCA1 
Gene Synonyms/Alias
 SNF2L; SNF2L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
179EVSPSYVKGGPLRDYubiquitination[1, 2]
429MQREWYTKILMKDIDubiquitination[1]
639IVERAEIKLRLDSIVubiquitination[3]
662QQSNKLAKEEMLQMIubiquitination[1]
739EDYREKQKLGMVEWIubiquitination[3]
814YRKTIGYKVPRNPDIubiquitination[3]
851EETEEKEKLLTQGFTubiquitination[1]
870RDFNQFIKANEKYGRubiquitination[3]
944DAKIARYKAPFHQLRubiquitination[1, 3]
1025TLISLIEKENMEIEEubiquitination[2]
1038EERERAEKKKRATKTacetylation[4]
1039ERERAEKKKRATKTPacetylation[4]
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] 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] 
Functional Description
 Energy-transducing component of NURF (nucleosome- remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes. Both complexes facilitate the perturbation of chromatin structure in an ATP-dependent manner. Potentiates neurite outgrowth. May be involved in brain development by regulating En-1 and En-2 expression. May be involved in the development of luteal cells. 
Sequence Annotation
 DOMAIN 195 360 Helicase ATP-binding.
 DOMAIN 490 653 Helicase C-terminal.
 DOMAIN 855 907 SANT 1.
 DOMAIN 958 1022 SANT 2.
 NP_BIND 208 215 ATP (Potential).
 MOTIF 311 314 DEAH box.
 MOD_RES 116 116 Phosphoserine.
 MOD_RES 119 119 Phosphoserine.
 MOD_RES 954 954 Phosphotyrosine.  
Keyword
 Activator; Alternative splicing; ATP-binding; Chromatin regulator; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1054 AA 
Protein Sequence
MEQDTAAVAA TVAAADATAT IVVIEDEQPG PSTSQEEGAA AAATEATAAT EKGEKKKEKN 60
VSSFQLKLAA KAPKSEKEMD PEYEEKMKAD RAKRFEFLLK QTELFAHFIQ PSAQKSPTSP 120
LNMKLGRPRI KKDEKQSLIS AGDYRHRRTE QEEDEELLSE SRKTSNVCIR FEVSPSYVKG 180
GPLRDYQIRG LNWLISLYEN GVNGILADEM GLGKTLQTIA LLGYLKHYRN IPGPHMVLVP 240
KSTLHNWMNE FKRWVPSLRV ICFVGDKDAR AAFIRDEMMP GEWDVCVTSY EMVIKEKSVF 300
KKFHWRYLVI DEAHRIKNEK SKLSEIVREF KSTNRLLLTG TPLQNNLHEL WALLNFLLPD 360
VFNSADDFDS WFDTKNCLGD QKLVERLHAV LKPFLLRRIK TDVEKSLPPK KEIKIYLGLS 420
KMQREWYTKI LMKDIDVLNS SGKMDKMRLL NILMQLRKCC NHPYLFDGAE PGPPYTTDEH 480
IVSNSGKMVV LDKLLAKLKE QGSRVLIFSQ MTRLLDILED YCMWRGYEYC RLDGQTPHEE 540
REDKFLEVEF LGQREAIEAF NAPNSSKFIF MLSTRAGGLG INLASADVVI LYDSDWNPQV 600
DLQAMDRAHR IGQKKPVRVF RLITDNTVEE RIVERAEIKL RLDSIVIQQG RLIDQQSNKL 660
AKEEMLQMIR HGATHVFASK ESELTDEDIT TILERGEKKT AEMNERLQKM GESSLRNFRM 720
DIEQSLYKFE GEDYREKQKL GMVEWIEPPK RERKANYAVD AYFREALRVS EPKIPKAPRP 780
PKQPNVQDFQ FFPPRLFELL EKEILYYRKT IGYKVPRNPD IPNPALAQRE EQKKIDGAEP 840
LTPEETEEKE KLLTQGFTNW TKRDFNQFIK ANEKYGRDDI DNIAREVEGK SPEEVMEYSA 900
VFWERCNELQ DIEKIMAQIE RGEARIQRRI SIKKALDAKI ARYKAPFHQL RIQYGTSKGK 960
NYTEEEDRFL ICMLHKMGFD RENVYEELRQ CVRNAPQFRF DWFIKSRTAM EFQRRCNTLI 1020
SLIEKENMEI EERERAEKKK RATKTPMVKF SAFS 1054 
Gene Ontology
 GO:0090537; C:CERF complex; IDA:MGI.
 GO:0016589; C:NURF complex; IDA:UniProtKB.
 GO:0036310; F:annealing helicase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0004386; F:helicase activity; TAS:ProtInc.
 GO:0031491; F:nucleosome binding; IEA:InterPro.
 GO:0043044; P:ATP-dependent chromatin remodeling; IDA:MGI.
 GO:0007420; P:brain development; IMP:HGNC.
 GO:0030182; P:neuron differentiation; ISS:HGNC.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:HGNC.
 GO:0006351; P:transcription, DNA-dependent; IMP:HGNC. 
Interpro
 IPR020838; DBINO.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR009057; Homeodomain-like.
 IPR015194; ISWI_HAND-dom.
 IPR027417; P-loop_NTPase.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom.
 IPR015195; SLIDE.
 IPR000330; SNF2_N. 
Pfam
 PF13892; DBINO
 PF09110; HAND
 PF00271; Helicase_C
 PF09111; SLIDE
 PF00176; SNF2_N 
SMART
 SM00487; DEXDc
 SM00490; HELICc
 SM00717; SANT 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51293; SANT 
PRINTS