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Q04692 (SMRCD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1

EC=3.6.4.12
Alternative name(s):
ATP-dependent helicase SMARCAD1
Enhancer trap locus homolog 1
Short name=Etl-1
Gene names
Name:Smarcad1
Synonyms:Etl1, Kiaa1122
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1021 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing By similarity.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Binds to DNA preferentially in the vicinity of transcriptional start sites. Interacts with MSH2 and TRIM28. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PCNA By similarity.

Subcellular location

Nucleus. Chromosome By similarity. Note: Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage By similarity. Ref.5 Ref.9 Ref.10

Developmental stage

Detected at low levels in fertilized and unfertilized eggs. Levels increased in two-cell embryos, decreased up to morula stage and were highest in blastocysts. Highly expressed in the inner cell mass of 3.5 day old blastocysts. Highly expressed in ectoderm and visceral endoderm at day 5.5. Detected throughout the brain and spinal cord at day 10 to 15. Detected in the basal layer of the epidermis after day 12.5, in particular on snout and distal on fore- and hindlimbs. Ref.5

Disruption phenotype

Deficient mice have reduced viability and show growth retardation, skeletal dysplasia and impaired fertility. Ref.6

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 2 CUE domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence BAC65736.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA49560.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP-dependent chromatin remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

DNA double-strand break processing

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome separation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3 deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4 deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA recombination

Inferred from sequence or structural similarity PubMed 11031099. Source: UniProtKB

   Cellular_componentheterochromatin

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear replication fork

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

site of double-strand break

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q04692-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q04692-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-185: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10211021SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1
PRO_0000074357

Regions

Domain156 – 19843CUE 1
Domain247 – 29044CUE 2
Domain504 – 672169Helicase ATP-binding
Domain853 – 1005153Helicase C-terminal
Nucleotide binding516 – 5249ATP By similarity
Nucleotide binding892 – 8998ATP By similarity
Motif623 – 6264DEGH box
Motif716 – 73318Nuclear localization signal Potential
Motif1000 – 10034DEAD box

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue541Phosphothreonine By similarity
Modified residue571Phosphoserine By similarity
Modified residue791Phosphoserine By similarity
Modified residue1241Phosphoserine By similarity
Modified residue1271Phosphoserine By similarity
Modified residue1321Phosphoserine By similarity
Modified residue1441Phosphoserine Ref.8
Modified residue1451Phosphoserine Ref.8
Modified residue1511Phosphoserine By similarity
Modified residue2101Phosphoserine By similarity
Modified residue2131Phosphoserine By similarity
Modified residue2351Phosphoserine By similarity
Modified residue2381Phosphoserine By similarity
Modified residue2981Phosphoserine By similarity

Natural variations

Alternative sequence1 – 185185Missing in isoform 2.
VSP_007080

Experimental info

Sequence conflict8571I → S in CAA49560. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 28, 2003. Version 2.
Checksum: E3237AA2B135538A

FASTA1,021116,451
        10         20         30         40         50         60 
MNLFNLDRFR FEKRSKIEEA PEAAPQPSQA RPSSPISLSA EEENAEGEGS RANTPDSDVT 

        70         80         90        100        110        120 
EKTEDSSVPE PPDNERKASL SCFQNQRAIQ EYIDLSSDTE DVSPNCSSTV QEKKFSKDTV 

       130        140        150        160        170        180 
IIVSEPSEDE ESHDLPSVTR RNDSSELEDL SELEDLKDAK LQTLKELFPQ RSDSDLLKLI 

       190        200        210        220        230        240 
ESTSTMDGAI AAALLMFGDA GGGPRKRKLS SSSEEDDVND DQSVKQPRGD RGEESNESAE 

       250        260        270        280        290        300 
ASSNWEKQES IVLKLQKEFP NFDKQELREV LKEHEWMYTE ALESLKVFAE DQDVQCASQS 

       310        320        330        340        350        360 
EVTNGKEVAR NQNYSKNATK IKMKQKISVK PQNGFNKKRK KNVFNPKKAV EDSEYDSGSD 

       370        380        390        400        410        420 
AGSSLDEDYS SCEEVMEDGY KGKILHFLQV SSIAELTLIP KCSQKKAQKI TELRPFNNWE 

       430        440        450        460        470        480 
ALFTKMSKIN GLSEDLIWNC KTVIQERDVV IRLMNKCEDI SNKLTKQVTM LTGNGGGWNR 

       490        500        510        520        530        540 
EQPSLLNQSL SLKPYQKVGL NWLALVHKHG LNGILADEMG LGKTIQAIAF LAYLFQEGNK 

       550        560        570        580        590        600 
GPHLIVVPAS TIDNWLREVN LWCPSLNVLC YYGSQEERKQ IRFNIHNKYE DYNVIVTTYN 

       610        620        630        640        650        660 
CAISSSDDRS LFRRLKLNYA IFDEGHMLKN MGSIRYQHLM TINARNRLLL TGTPVQNNLL 

       670        680        690        700        710        720 
ELMSLLNFVM PHMFSSSTSE IRRMFSSKTK PADEQSIYEK ERIAHAKQII KPFILRRVKE 

       730        740        750        760        770        780 
EVLKLLPPKK DRIELCAMSE KQEQLYSGLF NRLKKSINNL EKNTEMCNVM MQLRKMANHP 

       790        800        810        820        830        840 
LLHRQYYTPE KLKEMSQLML KEPTHCEANP DLIFEDMEVM TDFELHVLCK QYQHINSYQL 

       850        860        870        880        890        900 
DMDLILDSGK FRALGCILSE LKQKGDRVVL FSQFTMMLDI LEVLLKHHQH RYLRLDGKTQ 

       910        920        930        940        950        960 
ISERIHLIDE FNTDMDIFVF LLSTKAGGLG INLTSANVVI LHDIDCNPYN DKQAEDRCHR 

       970        980        990       1000       1010       1020 
VGQTKEVLVI KLISQGTIEE SMLKINQQKL KLEQDMTTVD EADEGSMPAD IATLLKTSMG 


L 

« Hide

Isoform 2 [UniParc].

Checksum: DD7B56518C73242B
Show »

FASTA83695,787

References

« Hide 'large scale' references
[1]"The mouse Enhancer trap locus 1 (Etl-1): a novel mammalian gene related to Drosophila and yeast transcriptional regulator genes."
Soininen R., Schoor M., Henseling U., Tepe C., Kisters-Woike B., Rossant J., Gossler A.
Mech. Dev. 39:111-123(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Embryo.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: FVB/N.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-760.
Strain: C57BL/6J.
Tissue: Testis.
[5]"The Etl-1 gene encodes a nuclear protein differentially expressed during early mouse development."
Schoor M., Schuster-Gossler K., Gossler A.
Dev. Dyn. 197:227-237(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[6]"Skeletal dysplasias, growth retardation, reduced postnatal survival, and impaired fertility in mice lacking the SNF2/SWI2 family member ETL1."
Schoor M., Schuster-Gossler K., Roopenian D., Gossler A.
Mech. Dev. 85:73-83(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Teratocarcinoma.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"The novel protein complex with SMARCAD1/KIAA1122 binds to the vicinity of TSS."
Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T., Ohara O., Koga H.
J. Mol. Biol. 382:257-265(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69942 mRNA. Translation: CAA49560.1. Different initiation.
AK122454 mRNA. Translation: BAC65736.1. Different initiation.
BC042442 mRNA. Translation: AAH42442.1.
AK134442 mRNA. Translation: BAE22146.1.
AK147884 mRNA. Translation: BAE28202.1.
PIRA56559.
RefSeqNP_001240321.1. NM_001253392.1.
NP_031984.1. NM_007958.1.
XP_006505572.1. XM_006505509.1.
XP_006505573.1. XM_006505510.1.
XP_006505574.1. XM_006505511.1.
XP_006505575.1. XM_006505512.1.
UniGeneMm.99113.

3D structure databases

ProteinModelPortalQ04692.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199524. 1 interaction.
STRING10090.ENSMUSP00000031984.

PTM databases

PhosphoSiteQ04692.

Proteomic databases

PaxDbQ04692.
PRIDEQ04692.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031984; ENSMUSP00000031984; ENSMUSG00000029920. [Q04692-1]
GeneID13990.
KEGGmmu:13990.
UCSCuc009ced.1. mouse. [Q04692-1]

Organism-specific databases

CTD56916.
MGIMGI:95453. Smarcad1.
RougeSearch...

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00630000089890.
HOGENOMHOG000172362.
HOVERGENHBG055804.
InParanoidQ04692.
KOK14439.
OMAKNQRGIQ.
OrthoDBEOG7QNVKC.
PhylomeDBQ04692.
TreeFamTF105768.

Gene expression databases

BgeeQ04692.
GenevestigatorQ04692.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003892. CUE.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS51140. CUE. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284868.
PROQ04692.
SOURCESearch...

Entry information

Entry nameSMRCD_MOUSE
AccessionPrimary (citable) accession number: Q04692
Secondary accession number(s): Q3UGK6, Q3UYR6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot