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Protein

SWI/SNF complex subunit SMARCC1

Gene

SMARCC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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 N-terminus binding Source: UniProtKB
  4. transcription coactivator activity Source: BHF-UCL

GO - Biological processi

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

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Neurogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_264545. RMTs methylate histone arginines.

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 Componenti: 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: UniProtKB
  4. nucleoplasm Source: HPA
  5. protein complex Source: UniProtKB
  6. SWI/SNF complex Source: UniProtKB
  7. XY body Source: Ensembl
Complete GO annotation...

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 – 3101Phosphoserine2 Publications
Modified residuei328 – 3281Phosphoserine5 Publications
Modified residuei330 – 3301Phosphoserine5 Publications
Modified residuei335 – 3351Phosphothreonine2 Publications
Modified residuei345 – 3451N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-acetyllysine1 Publication
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei354 – 3541N6-acetyllysine1 Publication
Modified residuei357 – 3571Phosphoserine2 Publications
Modified residuei359 – 3591N6-acetyllysine1 Publication
Modified residuei398 – 3981Phosphothreonine1 Publication
Modified residuei573 – 5731Phosphoserine1 Publication
Modified residuei822 – 8221Phosphoserine1 Publication
Modified residuei825 – 8251Phosphoserine1 Publication
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.1 Publication

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

BgeeiQ92922.
CleanExiHS_SMARCC1.
ExpressionAtlasiQ92922. baseline and differential.
GenevestigatoriQ92922.

Organism-specific databases

HPAiCAB011576.
CAB016336.
HPA024352.
HPA026853.

Interactioni

Subunit structurei

Component of a number of multiprotein chromatin-remodeling complexes: Swi/Snf-A (BAF), Swi/Snf-B (PBAF), Brm, Brg1(I) and Brg1(II). Each of the 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. 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 similarity5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112483. 104 interactions.
DIPiDIP-27545N.
DIP-33044N.
IntActiQ92922. 31 interactions.
MINTiMINT-1137868.
STRINGi9606.ENSP00000254480.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000018166.
HOGENOMiHOG000047736.
HOVERGENiHBG054849.
InParanoidiQ92922.
KOiK11649.
OMAiYKKYVHA.
OrthoDBiEOG7T4MJH.
PhylomeDBiQ92922.
TreeFamiTF314710.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.10.60. 1 hit.
InterProiIPR030087. BAF155.
IPR001357. BRCT_dom.
IPR000953. Chromo/shadow_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12802:SF9. PTHR12802:SF9. 1 hit.
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

        10         20         30         40         50
MAAAAGGGGP GTAVGATGSG IAAAAAGLAV YRRKDGGPAT KFWESPETVS
60 70 80 90 100
QLDSVRVWLG KHYKKYVHAD APTNKTLAGL VVQLLQFQED AFGKHVTNPA
110 120 130 140 150
FTKLPAKCFM DFKAGGALCH ILGAAYKYKN EQGWRRFDLQ NPSRMDRNVE
160 170 180 190 200
MFMNIEKTLV QNNCLTRPNI YLIPDIDLKL ANKLKDIIKR HQGTFTDEKS
210 220 230 240 250
KASHHIYPYS SSQDDEEWLR PVMRKEKQVL VHWGFYPDSY DTWVHSNDVD
260 270 280 290 300
AEIEDPPIPE KPWKVHVKWI LDTDIFNEWM NEEDYEVDEN RKPVSFRQRI
310 320 330 340 350
STKNEEPVRS PERRDRKASA NARKRKHSPS PPPPTPTESR KKSGKKGQAS
360 370 380 390 400
LYGKRRSQKE EDEQEDLTKD MEDPTPVPNI EEVVLPKNVN LKKDSENTPV
410 420 430 440 450
KGGTVADLDE QDEETVTAGG KEDEDPAKGD QSRSVDLGED NVTEQTNHII
460 470 480 490 500
IPSYASWFDY NCIHVIERRA LPEFFNGKNK SKTPEIYLAY RNFMIDTYRL
510 520 530 540 550
NPQEYLTSTA CRRNLTGDVC AVMRVHAFLE QWGLVNYQVD PESRPMAMGP
560 570 580 590 600
PPTPHFNVLA DTPSGLVPLH LRSPQVPAAQ QMLNFPEKNK EKPVDLQNFG
610 620 630 640 650
LRTDIYSKKT LAKSKGASAG REWTEQETLL LLEALEMYKD DWNKVSEHVG
660 670 680 690 700
SRTQDECILH FLRLPIEDPY LENSDASLGP LAYQPVPFSQ SGNPVMSTVA
710 720 730 740 750
FLASVVDPRV ASAAAKAALE EFSRVREEVP LELVEAHVKK VQEAARASGK
760 770 780 790 800
VDPTYGLESS CIAGTGPDEP EKLEGAEEEK MEADPDGQQP EKAENKVENE
810 820 830 840 850
TDEGDKAQDG ENEKNSEKEQ DSEVSEDTKS EEKETEENKE LTDTCKERES
860 870 880 890 900
DTGKKKVEHE ISEGNVATAA AAALASAATK AKHLAAVEER KIKSLVALLV
910 920 930 940 950
ETQMKKLEIK LRHFEELETI MDREKEALEQ QRQQLLTERQ NFHMEQLKYA
960 970 980 990 1000
ELRARQQMEQ QQHGQNPQQA HQHSGGPGLA PLGAAGHPGM MPHQQPPPYP
1010 1020 1030 1040 1050
LMHHQMPPPH PPQPGQIPGP GSMMPGQHMP GRMIPTVAAN IHPSGSGPTP
1060 1070 1080 1090 1100
PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ QPPPPPPADG VPPPPAPGPP

ASAAP
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.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH65253.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi112483. 104 interactions.
DIPiDIP-27545N.
DIP-33044N.
IntActiQ92922. 31 interactions.
MINTiMINT-1137868.
STRINGi9606.ENSP00000254480.

PTM databases

PhosphoSiteiQ92922.

Polymorphism databases

DMDMi209572723.

Proteomic databases

MaxQBiQ92922.
PaxDbiQ92922.
PRIDEiQ92922.

Protocols and materials databases

DNASUi6599.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6599.
GeneCardsiGC03M047626.
H-InvDBHIX0030795.
HGNCiHGNC:11104. SMARCC1.
HPAiCAB011576.
CAB016336.
HPA024352.
HPA026853.
MIMi601732. gene.
neXtProtiNX_Q92922.
PharmGKBiPA35954.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5259.
GeneTreeiENSGT00390000018166.
HOGENOMiHOG000047736.
HOVERGENiHBG054849.
InParanoidiQ92922.
KOiK11649.
OMAiYKKYVHA.
OrthoDBiEOG7T4MJH.
PhylomeDBiQ92922.
TreeFamiTF314710.

Enzyme and pathway databases

ReactomeiREACT_264545. RMTs methylate histone arginines.

Miscellaneous databases

ChiTaRSiSMARCC1. human.
EvolutionaryTraceiQ92922.
GeneWikiiSMARCC1.
GenomeRNAii6599.
NextBioi25671.
PROiQ92922.
SOURCEiSearch...

Gene expression databases

BgeeiQ92922.
CleanExiHS_SMARCC1.
ExpressionAtlasiQ92922. baseline and differential.
GenevestigatoriQ92922.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.10.60. 1 hit.
InterProiIPR030087. BAF155.
IPR001357. BRCT_dom.
IPR000953. Chromo/shadow_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12802:SF9. PTHR12802:SF9. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1995) [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(2003) [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 (JUN-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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THE G2/M TRANSITION.
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. 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.
  8. "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(2008) [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.
  9. "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(2008) [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].
  10. "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(2009) [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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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(2010) [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].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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(1998) [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(1998) [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(1999) [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(2000) [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(2002) [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(2007) [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(2009) [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 (MAR-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: April 1, 2015
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.