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Q04692

- SMRCD_MOUSE

UniProt

Q04692 - SMRCD_MOUSE

Protein

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

Gene

Smarcad1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (28 Mar 2003)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi516 – 5249ATPPROSITE-ProRule annotation
    Nucleotide bindingi892 – 8998ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. helicase activity Source: UniProtKB-KW

    GO - Biological processi

    1. ATP-dependent chromatin remodeling Source: UniProtKB
    2. chromosome separation Source: UniProtKB
    3. DNA double-strand break processing Source: UniProtKB
    4. histone H3 deacetylation Source: UniProtKB
    5. histone H4 deacetylation Source: UniProtKB
    6. regulation of DNA recombination Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator, Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Smarcad1
    Synonyms:Etl1, Kiaa1122
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:95453. Smarcad1.

    Subcellular locationi

    Nucleus 3 Publications. 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.By similarity

    GO - Cellular componenti

    1. heterochromatin Source: UniProtKB
    2. nuclear replication fork Source: Ensembl
    3. nucleus Source: UniProtKB
    4. site of double-strand break Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Deficient mice have reduced viability and show growth retardation, skeletal dysplasia and impaired fertility.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10211021SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1PRO_0000074357Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei54 – 541PhosphothreonineBy similarity
    Modified residuei57 – 571PhosphoserineBy similarity
    Modified residuei79 – 791PhosphoserineBy similarity
    Modified residuei124 – 1241PhosphoserineBy similarity
    Modified residuei127 – 1271PhosphoserineBy similarity
    Modified residuei132 – 1321PhosphoserineBy similarity
    Modified residuei144 – 1441Phosphoserine1 Publication
    Modified residuei145 – 1451Phosphoserine1 Publication
    Modified residuei151 – 1511PhosphoserineBy similarity
    Modified residuei210 – 2101PhosphoserineBy similarity
    Modified residuei213 – 2131PhosphoserineBy similarity
    Modified residuei235 – 2351PhosphoserineBy similarity
    Modified residuei238 – 2381PhosphoserineBy similarity
    Modified residuei298 – 2981PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ04692.
    PaxDbiQ04692.
    PRIDEiQ04692.

    PTM databases

    PhosphoSiteiQ04692.

    Expressioni

    Developmental stagei

    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.1 Publication

    Gene expression databases

    BgeeiQ04692.
    GenevestigatoriQ04692.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi199524. 2 interactions.
    STRINGi10090.ENSMUSP00000031984.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04692.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini156 – 19843CUE 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini247 – 29044CUE 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini504 – 672169Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini853 – 1005153Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi623 – 6264DEGH box
    Motifi716 – 73318Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi1000 – 10034DEAD box

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 2 CUE domains.PROSITE-ProRule annotation
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00630000089890.
    HOGENOMiHOG000172362.
    HOVERGENiHBG055804.
    InParanoidiQ04692.
    KOiK14439.
    OMAiKNQRGIQ.
    OrthoDBiEOG7QNVKC.
    PhylomeDBiQ04692.
    TreeFamiTF105768.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR003892. CUE.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51140. CUE. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q04692-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MNLFNLDRFR FEKRSKIEEA PEAAPQPSQA RPSSPISLSA EEENAEGEGS     50
    RANTPDSDVT EKTEDSSVPE PPDNERKASL SCFQNQRAIQ EYIDLSSDTE 100
    DVSPNCSSTV QEKKFSKDTV IIVSEPSEDE ESHDLPSVTR RNDSSELEDL 150
    SELEDLKDAK LQTLKELFPQ RSDSDLLKLI ESTSTMDGAI AAALLMFGDA 200
    GGGPRKRKLS SSSEEDDVND DQSVKQPRGD RGEESNESAE ASSNWEKQES 250
    IVLKLQKEFP NFDKQELREV LKEHEWMYTE ALESLKVFAE DQDVQCASQS 300
    EVTNGKEVAR NQNYSKNATK IKMKQKISVK PQNGFNKKRK KNVFNPKKAV 350
    EDSEYDSGSD AGSSLDEDYS SCEEVMEDGY KGKILHFLQV SSIAELTLIP 400
    KCSQKKAQKI TELRPFNNWE ALFTKMSKIN GLSEDLIWNC KTVIQERDVV 450
    IRLMNKCEDI SNKLTKQVTM LTGNGGGWNR EQPSLLNQSL SLKPYQKVGL 500
    NWLALVHKHG LNGILADEMG LGKTIQAIAF LAYLFQEGNK GPHLIVVPAS 550
    TIDNWLREVN LWCPSLNVLC YYGSQEERKQ IRFNIHNKYE DYNVIVTTYN 600
    CAISSSDDRS LFRRLKLNYA IFDEGHMLKN MGSIRYQHLM TINARNRLLL 650
    TGTPVQNNLL ELMSLLNFVM PHMFSSSTSE IRRMFSSKTK PADEQSIYEK 700
    ERIAHAKQII KPFILRRVKE EVLKLLPPKK DRIELCAMSE KQEQLYSGLF 750
    NRLKKSINNL EKNTEMCNVM MQLRKMANHP LLHRQYYTPE KLKEMSQLML 800
    KEPTHCEANP DLIFEDMEVM TDFELHVLCK QYQHINSYQL DMDLILDSGK 850
    FRALGCILSE LKQKGDRVVL FSQFTMMLDI LEVLLKHHQH RYLRLDGKTQ 900
    ISERIHLIDE FNTDMDIFVF LLSTKAGGLG INLTSANVVI LHDIDCNPYN 950
    DKQAEDRCHR VGQTKEVLVI KLISQGTIEE SMLKINQQKL KLEQDMTTVD 1000
    EADEGSMPAD IATLLKTSMG L 1021
    Length:1,021
    Mass (Da):116,451
    Last modified:March 28, 2003 - v2
    Checksum:iE3237AA2B135538A
    GO
    Isoform 2 (identifier: Q04692-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-185: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:836
    Mass (Da):95,787
    Checksum:iDD7B56518C73242B
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti857 – 8571I → S in CAA49560. (PubMed:1489724)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 185185Missing in isoform 2. 1 PublicationVSP_007080Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS20204.1. [Q04692-1]
    PIRiA56559.
    RefSeqiNP_001240321.1. NM_001253392.1. [Q04692-2]
    NP_031984.1. NM_007958.1. [Q04692-1]
    XP_006505572.1. XM_006505509.1. [Q04692-1]
    XP_006505573.1. XM_006505510.1. [Q04692-1]
    XP_006505574.1. XM_006505511.1. [Q04692-2]
    XP_006505575.1. XM_006505512.1. [Q04692-2]
    UniGeneiMm.99113.

    Genome annotation databases

    EnsembliENSMUST00000031984; ENSMUSP00000031984; ENSMUSG00000029920. [Q04692-1]
    GeneIDi13990.
    KEGGimmu:13990.
    UCSCiuc009ced.1. mouse. [Q04692-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS20204.1. [Q04692-1 ]
    PIRi A56559.
    RefSeqi NP_001240321.1. NM_001253392.1. [Q04692-2 ]
    NP_031984.1. NM_007958.1. [Q04692-1 ]
    XP_006505572.1. XM_006505509.1. [Q04692-1 ]
    XP_006505573.1. XM_006505510.1. [Q04692-1 ]
    XP_006505574.1. XM_006505511.1. [Q04692-2 ]
    XP_006505575.1. XM_006505512.1. [Q04692-2 ]
    UniGenei Mm.99113.

    3D structure databases

    ProteinModelPortali Q04692.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199524. 2 interactions.
    STRINGi 10090.ENSMUSP00000031984.

    PTM databases

    PhosphoSitei Q04692.

    Proteomic databases

    MaxQBi Q04692.
    PaxDbi Q04692.
    PRIDEi Q04692.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031984 ; ENSMUSP00000031984 ; ENSMUSG00000029920 . [Q04692-1 ]
    GeneIDi 13990.
    KEGGi mmu:13990.
    UCSCi uc009ced.1. mouse. [Q04692-1 ]

    Organism-specific databases

    CTDi 56916.
    MGIi MGI:95453. Smarcad1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0553.
    GeneTreei ENSGT00630000089890.
    HOGENOMi HOG000172362.
    HOVERGENi HBG055804.
    InParanoidi Q04692.
    KOi K14439.
    OMAi KNQRGIQ.
    OrthoDBi EOG7QNVKC.
    PhylomeDBi Q04692.
    TreeFami TF105768.

    Miscellaneous databases

    NextBioi 284868.
    PROi Q04692.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q04692.
    Genevestigatori Q04692.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR003892. CUE.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51140. CUE. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiSMRCD_MOUSE
    AccessioniPrimary (citable) accession number: Q04692
    Secondary accession number(s): Q3UGK6, Q3UYR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 28, 2003
    Last sequence update: March 28, 2003
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3