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Q92922

- SMRC1_HUMAN

UniProt

Q92922 - SMRC1_HUMAN

Protein

SWI/SNF complex subunit SMARCC1

Gene

SMARCC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). May stimulate the ATPase activity of the catalytic subunit of the complex. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth By similarity.By similarity

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. DNA binding Source: InterPro
    3. protein binding Source: UniProtKB
    4. protein N-terminus binding Source: UniProtKB
    5. transcription coactivator activity Source: BHF-UCL

    GO - Biological processi

    1. ATP-dependent chromatin remodeling Source: UniProt
    2. chromatin remodeling Source: UniProtKB
    3. insulin receptor signaling pathway Source: Ensembl
    4. nervous system development Source: UniProtKB-KW
    5. nucleosome disassembly Source: BHF-UCL
    6. organ morphogenesis Source: Ensembl
    7. positive regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Neurogenesis, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SWI/SNF complex subunit SMARCC1
    Alternative name(s):
    BRG1-associated factor 155
    Short name:
    BAF155
    SWI/SNF complex 155 kDa subunit
    SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1
    Gene namesi
    Name:SMARCC1
    Synonyms:BAF155
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11104. SMARCC1.

    Subcellular locationi

    GO - Cellular componenti

    1. nBAF complex Source: UniProtKB
    2. npBAF complex Source: UniProtKB
    3. nuclear chromatin Source: UniProt
    4. nucleus Source: HPA
    5. protein complex Source: UniProt
    6. SWI/SNF complex Source: UniProtKB
    7. XY body Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35954.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 11051104SWI/SNF complex subunit SMARCC1PRO_0000197115Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei310 – 3101Phosphoserine3 Publications
    Modified residuei328 – 3281Phosphoserine5 Publications
    Modified residuei330 – 3301Phosphoserine5 Publications
    Modified residuei335 – 3351Phosphothreonine3 Publications
    Modified residuei345 – 3451N6-acetyllysine1 Publication
    Modified residuei346 – 3461N6-acetyllysine1 Publication
    Modified residuei350 – 3501Phosphoserine2 Publications
    Modified residuei354 – 3541N6-acetyllysine1 Publication
    Modified residuei357 – 3571Phosphoserine3 Publications
    Modified residuei359 – 3591N6-acetyllysine1 Publication
    Modified residuei398 – 3981Phosphothreonine2 Publications
    Modified residuei573 – 5731Phosphoserine2 Publications
    Modified residuei822 – 8221Phosphoserine2 Publications
    Modified residuei825 – 8251Phosphoserine2 Publications
    Modified residuei948 – 9481N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated on undefined residues at the G2/M transition by ERK1 and other kinases. This may contribute to cell cycle specific inactivation of remodeling complexes containing the phosphorylated protein.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92922.
    PaxDbiQ92922.
    PRIDEiQ92922.

    PTM databases

    PhosphoSiteiQ92922.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, muscle, placenta, lung, liver, muscle, kidney and pancreas.

    Gene expression databases

    ArrayExpressiQ92922.
    BgeeiQ92922.
    CleanExiHS_SMARCC1.
    GenevestigatoriQ92922.

    Organism-specific databases

    HPAiCAB011576.
    CAB016336.
    HPA024352.
    HPA026853.

    Interactioni

    Subunit structurei

    Component of 6 multiprotein chromatin-remodeling complexes: Swi/Snf-A (BAF), Swi/Snf-B (PBAF), Brm, Brg1(I), WINAC and Brg1(II). Each of the five complexes contains a catalytic subunit (either SMARCA4 or SMARCA2), and at least SMARCE1, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCC2 and SMARCB1. Other subunits specific to each of the complexes may also be present. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. May also interact with the SIN3A histone deacetylase transcription repressor complex in conjunction with SMARCA2 and SMARCA4. The minimal complex composed of SMARCC1 and SMARCA4 seems to be able to associate with cyclin such as CCNE1 or transcription factors such as KLF1 or GATA1. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with NR3C1 and SMARD1. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin By similarity. Interacts with TRIP12; leading to disrupt interaction between TRIP12 and SMARCE1 and prevent SMARCE1 ubiquitination.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CARM1Q86X554EBI-355653,EBI-2339854
    SMARCA4P5153225EBI-355653,EBI-302489
    SMARCD1Q96GM53EBI-355653,EBI-358489

    Protein-protein interaction databases

    BioGridi112483. 96 interactions.
    DIPiDIP-27545N.
    DIP-33044N.
    IntActiQ92922. 30 interactions.
    MINTiMINT-1137868.
    STRINGi9606.ENSP00000254480.

    Structurei

    Secondary structure

    1
    1105
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi625 – 63713
    Beta strandi638 – 6403
    Helixi642 – 6498
    Helixi654 – 6618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YUSNMR-A610-675[»]
    ProteinModelPortaliQ92922.
    SMRiQ92922. Positions 455-539, 607-676.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92922.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini449 – 54698SWIRMPROSITE-ProRule annotationAdd
    BLAST
    Domaini618 – 66952SANTPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili914 – 94633Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi329 – 3368Poly-Pro
    Compositional biasi769 – 86395Glu-richAdd
    BLAST
    Compositional biasi867 – 87812Poly-AlaAdd
    BLAST
    Compositional biasi977 – 1105129Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SMARCC family.Curated
    Contains 1 SANT domain.PROSITE-ProRule annotation
    Contains 1 SWIRM domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5259.
    HOGENOMiHOG000047736.
    HOVERGENiHBG054849.
    InParanoidiQ92922.
    KOiK11649.
    OMAiYKKYVHA.
    OrthoDBiEOG7T4MJH.
    PhylomeDBiQ92922.
    TreeFamiTF314710.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.10.60. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR000953. Chromo_domain/shadow.
    IPR009057. Homeodomain-like.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    IPR007526. SWIRM.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00249. Myb_DNA-binding. 1 hit.
    PF04433. SWIRM. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 1 hit.
    SM00717. SANT. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 2 hits.
    SSF52113. SSF52113. 2 hits.
    PROSITEiPS51293. SANT. 1 hit.
    PS50934. SWIRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q92922-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAAGGGGP GTAVGATGSG IAAAAAGLAV YRRKDGGPAT KFWESPETVS     50
    QLDSVRVWLG KHYKKYVHAD APTNKTLAGL VVQLLQFQED AFGKHVTNPA 100
    FTKLPAKCFM DFKAGGALCH ILGAAYKYKN EQGWRRFDLQ NPSRMDRNVE 150
    MFMNIEKTLV QNNCLTRPNI YLIPDIDLKL ANKLKDIIKR HQGTFTDEKS 200
    KASHHIYPYS SSQDDEEWLR PVMRKEKQVL VHWGFYPDSY DTWVHSNDVD 250
    AEIEDPPIPE KPWKVHVKWI LDTDIFNEWM NEEDYEVDEN RKPVSFRQRI 300
    STKNEEPVRS PERRDRKASA NARKRKHSPS PPPPTPTESR KKSGKKGQAS 350
    LYGKRRSQKE EDEQEDLTKD MEDPTPVPNI EEVVLPKNVN LKKDSENTPV 400
    KGGTVADLDE QDEETVTAGG KEDEDPAKGD QSRSVDLGED NVTEQTNHII 450
    IPSYASWFDY NCIHVIERRA LPEFFNGKNK SKTPEIYLAY RNFMIDTYRL 500
    NPQEYLTSTA CRRNLTGDVC AVMRVHAFLE QWGLVNYQVD PESRPMAMGP 550
    PPTPHFNVLA DTPSGLVPLH LRSPQVPAAQ QMLNFPEKNK EKPVDLQNFG 600
    LRTDIYSKKT LAKSKGASAG REWTEQETLL LLEALEMYKD DWNKVSEHVG 650
    SRTQDECILH FLRLPIEDPY LENSDASLGP LAYQPVPFSQ SGNPVMSTVA 700
    FLASVVDPRV ASAAAKAALE EFSRVREEVP LELVEAHVKK VQEAARASGK 750
    VDPTYGLESS CIAGTGPDEP EKLEGAEEEK MEADPDGQQP EKAENKVENE 800
    TDEGDKAQDG ENEKNSEKEQ DSEVSEDTKS EEKETEENKE LTDTCKERES 850
    DTGKKKVEHE ISEGNVATAA AAALASAATK AKHLAAVEER KIKSLVALLV 900
    ETQMKKLEIK LRHFEELETI MDREKEALEQ QRQQLLTERQ NFHMEQLKYA 950
    ELRARQQMEQ QQHGQNPQQA HQHSGGPGLA PLGAAGHPGM MPHQQPPPYP 1000
    LMHHQMPPPH PPQPGQIPGP GSMMPGQHMP GRMIPTVAAN IHPSGSGPTP 1050
    PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ QPPPPPPADG VPPPPAPGPP 1100
    ASAAP 1105
    Length:1,105
    Mass (Da):122,867
    Last modified:October 14, 2008 - v3
    Checksum:iEDA6FF5B0472AEA9
    GO

    Sequence cautioni

    The sequence AAH39843.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH65253.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 224SGIA → FGDS in AAC50693. (PubMed:8804307)Curated
    Sequence conflicti497 – 4971T → S in AAC50693. (PubMed:8804307)Curated
    Sequence conflicti528 – 5292FL → GG in AAC50693. (PubMed:8804307)Curated
    Sequence conflicti564 – 5707SGLVPLH → LACASD in AAC50693. (PubMed:8804307)Curated
    Sequence conflicti622 – 6221E → G in AAC50693. (PubMed:8804307)Curated
    Sequence conflicti842 – 8432TD → SS in AAC50693. (PubMed:8804307)Curated
    Sequence conflicti916 – 9161E → G in AAC50693. (PubMed:8804307)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1075 – 10751P → H.
    Corresponds to variant rs3772406 [ dbSNP | Ensembl ].
    VAR_020883

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66615 mRNA. Translation: AAC50693.1.
    BC039843 mRNA. Translation: AAH39843.1. Sequence problems.
    BC065253 mRNA. Translation: AAH65253.1. Sequence problems.
    BC113465 mRNA. Translation: AAI13466.1.
    BC117213 mRNA. Translation: AAI17214.1.
    CCDSiCCDS2758.1.
    RefSeqiNP_003065.3. NM_003074.3.
    UniGeneiHs.476179.

    Genome annotation databases

    EnsembliENST00000254480; ENSP00000254480; ENSG00000173473.
    GeneIDi6599.
    KEGGihsa:6599.
    UCSCiuc003crq.2. human.

    Polymorphism databases

    DMDMi209572723.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66615 mRNA. Translation: AAC50693.1 .
    BC039843 mRNA. Translation: AAH39843.1 . Sequence problems.
    BC065253 mRNA. Translation: AAH65253.1 . Sequence problems.
    BC113465 mRNA. Translation: AAI13466.1 .
    BC117213 mRNA. Translation: AAI17214.1 .
    CCDSi CCDS2758.1.
    RefSeqi NP_003065.3. NM_003074.3.
    UniGenei Hs.476179.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YUS NMR - A 610-675 [» ]
    ProteinModelPortali Q92922.
    SMRi Q92922. Positions 455-539, 607-676.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112483. 96 interactions.
    DIPi DIP-27545N.
    DIP-33044N.
    IntActi Q92922. 30 interactions.
    MINTi MINT-1137868.
    STRINGi 9606.ENSP00000254480.

    PTM databases

    PhosphoSitei Q92922.

    Polymorphism databases

    DMDMi 209572723.

    Proteomic databases

    MaxQBi Q92922.
    PaxDbi Q92922.
    PRIDEi Q92922.

    Protocols and materials databases

    DNASUi 6599.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254480 ; ENSP00000254480 ; ENSG00000173473 .
    GeneIDi 6599.
    KEGGi hsa:6599.
    UCSCi uc003crq.2. human.

    Organism-specific databases

    CTDi 6599.
    GeneCardsi GC03M047626.
    H-InvDB HIX0030795.
    HGNCi HGNC:11104. SMARCC1.
    HPAi CAB011576.
    CAB016336.
    HPA024352.
    HPA026853.
    MIMi 601732. gene.
    neXtProti NX_Q92922.
    PharmGKBi PA35954.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5259.
    HOGENOMi HOG000047736.
    HOVERGENi HBG054849.
    InParanoidi Q92922.
    KOi K11649.
    OMAi YKKYVHA.
    OrthoDBi EOG7T4MJH.
    PhylomeDBi Q92922.
    TreeFami TF314710.

    Miscellaneous databases

    ChiTaRSi SMARCC1. human.
    EvolutionaryTracei Q92922.
    GeneWikii SMARCC1.
    GenomeRNAii 6599.
    NextBioi 25671.
    PROi Q92922.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92922.
    Bgeei Q92922.
    CleanExi HS_SMARCC1.
    Genevestigatori Q92922.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.10.60. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR000953. Chromo_domain/shadow.
    IPR009057. Homeodomain-like.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    IPR007526. SWIRM.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00249. Myb_DNA-binding. 1 hit.
    PF04433. SWIRM. 1 hit.
    [Graphical view ]
    SMARTi SM00298. CHROMO. 1 hit.
    SM00717. SANT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 2 hits.
    SSF52113. SSF52113. 2 hits.
    PROSITEi PS51293. SANT. 1 hit.
    PS50934. SWIRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Diversity and specialization of mammalian SWI/SNF complexes."
      Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.
      Genes Dev. 10:2117-2130(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Tissue: Brain, Eye and Testis.
    3. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-32; 470-478; 483-491; 591-602; 653-663; 717-724 AND 894-905, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary carcinoma.
    4. "Mitotic inactivation of a human SWI/SNF chromatin remodeling complex."
      Sif S., Stukenberg P.T., Kirschner M.W., Kingston R.E.
      Genes Dev. 12:2842-2851(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THE G2/M TRANSITION.
    5. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
      Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
      Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
    6. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-330; THR-335 AND SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-345; LYS-346; LYS-354; LYS-359 AND LYS-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-328; SER-330; SER-357 AND SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-330; THR-335; SER-350; THR-398; SER-822 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits."
      Phelan M.L., Sif S., Narlikar G.J., Kingston R.E.
      Mol. Cell 3:247-253(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STIMULATION OF THE CHROMATIN-REMODELING ACTIVITY OF SMARCA4.
    16. "Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest."
      Shanahan F., Seghezzi W., Parry D., Mahony D., Lees E.
      Mol. Cell. Biol. 19:1460-1469(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCNE1.
    17. "Functional selectivity of recombinant mammalian SWI/SNF subunits."
      Kadam S., McAlpine G.S., Phelan M.L., Kingston R.E., Jones K.A., Emerson B.M.
      Genes Dev. 14:2441-2451(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes."
      Sif S., Saurin A.J., Imbalzano A.N., Kingston R.E.
      Genes Dev. 15:603-618(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIN3A.
    19. "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
      Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
      Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR3C1 AND SMARD1.
    20. "Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
      Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
      Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    21. "Ubiquitin-dependent and ubiquitin-independent control of subunit stoichiometry in the SWI/SNF complex."
      Keppler B.R., Archer T.K.
      J. Biol. Chem. 285:35665-35674(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIP12.
    22. "Solution structure of the SANT domain of human SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 607-676.

    Entry informationi

    Entry nameiSMRC1_HUMAN
    AccessioniPrimary (citable) accession number: Q92922
    Secondary accession number(s): Q17RS0, Q6P172, Q8IWH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3