Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q92922 (SMRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SMARCC1
Synonyms:BAF155
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.17

Subunit structure

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. Ref.5 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21

Subcellular location

Nucleus.

Tissue specificity

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

Post-translational modification

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. Ref.4

Sequence similarities

Belongs to the SMARCC family.

Contains 1 SANT domain.

Contains 1 SWIRM domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processNeurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin remodeling

Inferred from direct assay Ref.15Ref.17. Source: UniProtKB

insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

nucleosome disassembly

Inferred from direct assay PubMed 8895581. Source: BHF-UCL

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.17. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Non-traceable author statement Ref.1. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSWI/SNF complex

Inferred from direct assay Ref.15PubMed 11078522. Source: UniProtKB

WINAC complex

Inferred from direct assay Ref.5. Source: BHF-UCL

XY body

Inferred from electronic annotation. Source: Ensembl

nBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

npBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

chromatin binding

Inferred from electronic annotation. Source: Ensembl

protein N-terminus binding

Inferred from physical interaction Ref.19. Source: UniProtKB

transcription coactivator activity

Non-traceable author statement Ref.1. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 11051104SWI/SNF complex subunit SMARCC1
PRO_0000197115

Regions

Domain449 – 54698SWIRM
Domain618 – 66952SANT
Coiled coil914 – 94633 Potential
Compositional bias329 – 3368Poly-Pro
Compositional bias769 – 86395Glu-rich
Compositional bias867 – 87812Poly-Ala
Compositional bias977 – 1105129Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.14
Modified residue3101Phosphoserine Ref.4 Ref.7 Ref.11
Modified residue3281Phosphoserine Ref.4 Ref.8 Ref.9 Ref.11 Ref.13
Modified residue3301Phosphoserine Ref.4 Ref.8 Ref.9 Ref.11 Ref.13
Modified residue3351Phosphothreonine Ref.4 Ref.8 Ref.13
Modified residue3451N6-acetyllysine Ref.10
Modified residue3461N6-acetyllysine Ref.10
Modified residue3501Phosphoserine Ref.4 Ref.13
Modified residue3541N6-acetyllysine Ref.10
Modified residue3571Phosphoserine Ref.4 Ref.8 Ref.11
Modified residue3591N6-acetyllysine Ref.10
Modified residue3981Phosphothreonine Ref.4 Ref.13
Modified residue5731Phosphoserine Ref.4 Ref.11
Modified residue8221Phosphoserine Ref.4 Ref.13
Modified residue8251Phosphoserine Ref.4 Ref.13
Modified residue9481N6-acetyllysine Ref.10

Natural variations

Natural variant10751P → H.
Corresponds to variant rs3772406 [ dbSNP | Ensembl ].
VAR_020883

Experimental info

Sequence conflict19 – 224SGIA → FGDS in AAC50693. Ref.1
Sequence conflict4971T → S in AAC50693. Ref.1
Sequence conflict528 – 5292FL → GG in AAC50693. Ref.1
Sequence conflict564 – 5707SGLVPLH → LACASD in AAC50693. Ref.1
Sequence conflict6221E → G in AAC50693. Ref.1
Sequence conflict842 – 8432TD → SS in AAC50693. Ref.1
Sequence conflict9161E → G in AAC50693. Ref.1

Secondary structure

........ 1105
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92922 [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: EDA6FF5B0472AEA9

FASTA1,105122,867
        10         20         30         40         50         60 
MAAAAGGGGP GTAVGATGSG IAAAAAGLAV YRRKDGGPAT KFWESPETVS QLDSVRVWLG 

        70         80         90        100        110        120 
KHYKKYVHAD APTNKTLAGL VVQLLQFQED AFGKHVTNPA FTKLPAKCFM DFKAGGALCH 

       130        140        150        160        170        180 
ILGAAYKYKN EQGWRRFDLQ NPSRMDRNVE MFMNIEKTLV QNNCLTRPNI YLIPDIDLKL 

       190        200        210        220        230        240 
ANKLKDIIKR HQGTFTDEKS KASHHIYPYS SSQDDEEWLR PVMRKEKQVL VHWGFYPDSY 

       250        260        270        280        290        300 
DTWVHSNDVD AEIEDPPIPE KPWKVHVKWI LDTDIFNEWM NEEDYEVDEN RKPVSFRQRI 

       310        320        330        340        350        360 
STKNEEPVRS PERRDRKASA NARKRKHSPS PPPPTPTESR KKSGKKGQAS LYGKRRSQKE 

       370        380        390        400        410        420 
EDEQEDLTKD MEDPTPVPNI EEVVLPKNVN LKKDSENTPV KGGTVADLDE QDEETVTAGG 

       430        440        450        460        470        480 
KEDEDPAKGD QSRSVDLGED NVTEQTNHII IPSYASWFDY NCIHVIERRA LPEFFNGKNK 

       490        500        510        520        530        540 
SKTPEIYLAY RNFMIDTYRL NPQEYLTSTA CRRNLTGDVC AVMRVHAFLE QWGLVNYQVD 

       550        560        570        580        590        600 
PESRPMAMGP PPTPHFNVLA DTPSGLVPLH LRSPQVPAAQ QMLNFPEKNK EKPVDLQNFG 

       610        620        630        640        650        660 
LRTDIYSKKT LAKSKGASAG REWTEQETLL LLEALEMYKD DWNKVSEHVG SRTQDECILH 

       670        680        690        700        710        720 
FLRLPIEDPY LENSDASLGP LAYQPVPFSQ SGNPVMSTVA FLASVVDPRV ASAAAKAALE 

       730        740        750        760        770        780 
EFSRVREEVP LELVEAHVKK VQEAARASGK VDPTYGLESS CIAGTGPDEP EKLEGAEEEK 

       790        800        810        820        830        840 
MEADPDGQQP EKAENKVENE TDEGDKAQDG ENEKNSEKEQ DSEVSEDTKS EEKETEENKE 

       850        860        870        880        890        900 
LTDTCKERES DTGKKKVEHE ISEGNVATAA AAALASAATK AKHLAAVEER KIKSLVALLV 

       910        920        930        940        950        960 
ETQMKKLEIK LRHFEELETI MDREKEALEQ QRQQLLTERQ NFHMEQLKYA ELRARQQMEQ 

       970        980        990       1000       1010       1020 
QQHGQNPQQA HQHSGGPGLA PLGAAGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP 

      1030       1040       1050       1060       1070       1080 
GSMMPGQHMP GRMIPTVAAN IHPSGSGPTP PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ 

      1090       1100 
QPPPPPPADG VPPPPAPGPP ASAAP 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003065.3. NM_003074.3.
UniGeneHs.476179.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YUSNMR-A610-675[»]
ProteinModelPortalQ92922.
SMRQ92922. Positions 455-539, 607-676.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112483. 93 interactions.
DIPDIP-27545N.
DIP-33044N.
IntActQ92922. 30 interactions.
MINTMINT-1137868.
STRING9606.ENSP00000254480.

PTM databases

PhosphoSiteQ92922.

Polymorphism databases

DMDM209572723.

Proteomic databases

PaxDbQ92922.
PRIDEQ92922.

Protocols and materials databases

DNASU6599.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254480; ENSP00000254480; ENSG00000173473.
GeneID6599.
KEGGhsa:6599.
UCSCuc003crq.2. human.

Organism-specific databases

CTD6599.
GeneCardsGC03M047626.
H-InvDBHIX0030795.
HGNCHGNC:11104. SMARCC1.
HPACAB011576.
CAB016336.
HPA024352.
HPA026853.
MIM601732. gene.
neXtProtNX_Q92922.
PharmGKBPA35954.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5259.
HOGENOMHOG000047736.
HOVERGENHBG054849.
InParanoidQ92922.
KOK11649.
OMAYKKYVHA.
OrthoDBEOG7T4MJH.
PhylomeDBQ92922.
TreeFamTF314710.

Gene expression databases

ArrayExpressQ92922.
BgeeQ92922.
CleanExHS_SMARCC1.
GenevestigatorQ92922.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.10.60. 1 hit.
InterProIPR001357. BRCT_dom.
IPR000953. Chromo_domain/shadow.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
SSF52113. SSF52113. 2 hits.
PROSITEPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMARCC1. human.
EvolutionaryTraceQ92922.
GeneWikiSMARCC1.
GenomeRNAi6599.
NextBio25671.
PROQ92922.
SOURCESearch...

Entry information

Entry nameSMRC1_HUMAN
AccessionPrimary (citable) accession number: Q92922
Secondary accession number(s): Q17RS0, Q6P172, Q8IWH2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM