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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). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. May stimulate the ATPase activity of the catalytic subunit of the complex (PubMed:10078207). 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 postmitotic 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 postmitotic 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).2 PublicationsBy similarity2 Publications

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • DNA binding Source: InterPro
  • protein N-terminus binding Source: UniProtKB
  • transcription coactivator activity Source: BHF-UCL

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator
Biological processNeurogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-3214858. RMTs methylate histone arginines.
R-HSA-8939243. RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
SIGNORiQ92922.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000173473.10.
HGNCiHGNC:11104. SMARCC1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi6599.
OpenTargetsiENSG00000173473.
PharmGKBiPA35954.

Polymorphism and mutation databases

BioMutaiSMARCC1.
DMDMi209572723.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001971152 – 1105SWI/SNF complex subunit SMARCC1Add BLAST1104

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Cross-linki179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei310PhosphoserineCombined sources1
Modified residuei328PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei335PhosphothreonineCombined sources1
Modified residuei345N6-acetyllysineCombined sources1
Modified residuei346N6-acetyllysineCombined sources1
Modified residuei350PhosphoserineCombined sources1
Modified residuei354N6-acetyllysineCombined sources1
Modified residuei357PhosphoserineCombined sources1
Modified residuei359N6-acetyllysine; alternateCombined sources1
Cross-linki359Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei398PhosphothreonineCombined sources1
Modified residuei573PhosphoserineCombined sources1
Cross-linki592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki739Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki796Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei822PhosphoserineCombined sources1
Modified residuei825PhosphoserineCombined sources1
Cross-linki829Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki856Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei948N6-acetyllysineCombined sources1
Modified residuei1064Asymmetric dimethylarginineBy similarity1

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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ92922.
MaxQBiQ92922.
PaxDbiQ92922.
PeptideAtlasiQ92922.
PRIDEiQ92922.

PTM databases

iPTMnetiQ92922.
PhosphoSitePlusiQ92922.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000173473.
CleanExiHS_SMARCC1.
ExpressionAtlasiQ92922. baseline and differential.
GenevisibleiQ92922. HS.

Organism-specific databases

HPAiCAB011576.
CAB016336.
HPA024352.
HPA026853.

Interactioni

Subunit structurei

Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (Probable). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3 (PubMed:18765789). 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). Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:22952240, PubMed:26601204). May also interact with the SIN3A histone deacetylase transcription repressor complex in conjunction with SMARCA2 and SMARCA4 (PubMed:11238380). 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 (PubMed:9891079). Interacts with NR3C1 and SMARD1 (PubMed:12917342). Interacts with TRIP12; leading to disrupt interaction between TRIP12 and SMARCE1 and prevent SMARCE1 ubiquitination (PubMed:20111005). Interacts with CEBPB (when not methylated)(PubMed:20829358). Interacts with KDM6B (By similarity).2 PublicationsBy similarity6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112483. 132 interactors.
CORUMiQ92922.
DIPiDIP-27545N.
DIP-33044N.
IntActiQ92922. 69 interactors.
MINTiMINT-1137868.
STRINGi9606.ENSP00000254480.

Structurei

Secondary structure

11105
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi453 – 455Combined sources3
Helixi465 – 470Combined sources6
Helixi472 – 474Combined sources3
Helixi484 – 500Combined sources17
Helixi508 – 512Combined sources5
Helixi519 – 531Combined sources13
Beta strandi534 – 536Combined sources3
Helixi625 – 637Combined sources13
Beta strandi638 – 640Combined sources3
Helixi642 – 649Combined sources8
Helixi654 – 661Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YUSNMR-A610-675[»]
5GJKX-ray2.05A447-540[»]
ProteinModelPortaliQ92922.
SMRiQ92922.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92922.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini449 – 546SWIRMPROSITE-ProRule annotationAdd BLAST98
Domaini618 – 669SANTPROSITE-ProRule annotationAdd BLAST52

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili914 – 946Sequence analysisAdd BLAST33

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi329 – 336Poly-Pro8
Compositional biasi769 – 863Glu-richAdd BLAST95
Compositional biasi867 – 878Poly-AlaAdd BLAST12
Compositional biasi977 – 1105Pro-richAdd BLAST129

Sequence similaritiesi

Belongs to the SMARCC family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1279. Eukaryota.
COG5259. LUCA.
GeneTreeiENSGT00390000018166.
HOGENOMiHOG000047736.
HOVERGENiHBG054849.
InParanoidiQ92922.
KOiK11649.
OMAiYKKYVHA.
OrthoDBiEOG091G06AJ.
PhylomeDBiQ92922.
TreeFamiTF314710.

Family and domain databases

CDDicd00024. CHROMO. 1 hit.
Gene3Di1.10.10.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiView protein in InterPro
IPR030087. BAF155.
IPR036420. BRCT_dom_sf.
IPR000953. Chromo/chromo_shadow_dom.
IPR009057. Homeobox-like_sf.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR032451. SMARCC_C.
IPR032450. SMARCC_N.
IPR007526. SWIRM.
IPR032448. SWIRM-assoc.
IPR036388. WH-like_DNA-bd_sf.
PANTHERiPTHR12802:SF9. PTHR12802:SF9. 1 hit.
PfamiView protein in Pfam
PF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
PF16495. SWIRM-assoc_1. 1 hit.
PF16496. SWIRM-assoc_2. 1 hit.
PF16498. SWIRM-assoc_3. 1 hit.
SMARTiView protein in SMART
SM00298. CHROMO. 1 hit.
SM00717. SANT. 1 hit.
SUPFAMiSSF46689. SSF46689. 2 hits.
SSF52113. SSF52113. 2 hits.
PROSITEiView protein in PROSITE
PS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19 – 22SGIA → FGDS in AAC50693 (PubMed:8804307).Curated4
Sequence conflicti497T → S in AAC50693 (PubMed:8804307).Curated1
Sequence conflicti528 – 529FL → GG in AAC50693 (PubMed:8804307).Curated2
Sequence conflicti564 – 570SGLVPLH → LACASD in AAC50693 (PubMed:8804307).Curated7
Sequence conflicti622E → G in AAC50693 (PubMed:8804307).Curated1
Sequence conflicti842 – 843TD → SS in AAC50693 (PubMed:8804307).Curated2
Sequence conflicti916E → G in AAC50693 (PubMed:8804307).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0208831075P → H. Corresponds to variant dbSNP:rs3772406Ensembl.1

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.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSMRC1_HUMAN
AccessioniPrimary (citable) accession number: Q92922
Secondary accession number(s): Q17RS0, Q6P172, Q8IWH2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 14, 2008
Last modified: November 22, 2017
This is version 178 of the entry and version 3 of the sequence. See 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