Q92922 (SMRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SMARCC1
Synonyms:	BAF155

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1105 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.16
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.15 Ref.17 Ref.18 Ref.19 Ref.20
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 process	Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Inferred from direct assay Ref.14Ref.16. Source: UniProtKB insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.16. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Non-traceable author statement Ref.1. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SWI/SNF complex Inferred from direct assay Ref.14PubMed 11078522. Source: UniProtKB WINAC complex Inferred from direct assay Ref.5. Source: BHF-UCL XY body Inferred from electronic annotation. Source: Compara nBAF complex Inferred from sequence or structural similarity. Source: UniProtKB npBAF complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro chromatin binding Inferred from electronic annotation. Source: Compara transcription coactivator activity Non-traceable author statement Ref.1. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMARCA4	P51532	9	EBI-355653,EBI-302489
SMARCD1	Q96GM5	2	EBI-355653,EBI-358489

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 1105

1104

SWI/SNF complex subunit SMARCC1

PRO_0000197115

Regions

Domain

449 – 546

98

SWIRM

Domain

618 – 669

52

SANT

Coiled coil

914 – 946

33

Potential

Compositional bias

329 – 336

8

Poly-Pro

Compositional bias

769 – 863

95

Glu-rich

Compositional bias

867 – 878

12

Poly-Ala

Compositional bias

977 – 1105

129

Pro-rich

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3

Modified residue

301

1

Phosphoserine By similarity

Modified residue

310

1

Phosphoserine Ref.4 Ref.7 Ref.11

Modified residue

328

1

Phosphoserine Ref.4 Ref.8 Ref.9 Ref.11 Ref.13

Modified residue

330

1

Phosphoserine Ref.4 Ref.8 Ref.9 Ref.11 Ref.13

Modified residue

335

1

Phosphothreonine Ref.4 Ref.8 Ref.13

Modified residue

337

1

Phosphothreonine By similarity

Modified residue

345

1

N6-acetyllysine Ref.10

Modified residue

346

1

N6-acetyllysine Ref.10

Modified residue

350

1

Phosphoserine Ref.4 Ref.13

Modified residue

354

1

N6-acetyllysine Ref.10

Modified residue

357

1

Phosphoserine Ref.4 Ref.8 Ref.11

Modified residue

359

1

N6-acetyllysine Ref.10

Modified residue

398

1

Phosphothreonine Ref.4 Ref.13

Modified residue

573

1

Phosphoserine Ref.4 Ref.11

Modified residue

822

1

Phosphoserine Ref.4 Ref.13

Modified residue

825

1

Phosphoserine Ref.4 Ref.13

Modified residue

948

1

N6-acetyllysine Ref.10

Natural variations

Natural variant

1075

1

P → H.
Corresponds to variant rs3772406 [ dbSNP | Ensembl ].

VAR_020883

Experimental info

Sequence conflict

19 – 22

4

SGIA → FGDS in AAC50693. Ref.1

Sequence conflict

497

1

T → S in AAC50693. Ref.1

Sequence conflict

528 – 529

2

FL → GG in AAC50693. Ref.1

Sequence conflict

564 – 570

7

SGLVPLH → LACASD in AAC50693. Ref.1

Sequence conflict

622

1

E → G in AAC50693. Ref.1

Sequence conflict

842 – 843

2

TD → SS in AAC50693. Ref.1

Sequence conflict

916

1

E → G in AAC50693. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

1105

Helix Strand Turn

Details...

Helix

625 – 637

13

Beta strand

638 – 640

3

Helix

642 – 649

8

Helix

654 – 661

8

Sequences

	Sequence		Length	Mass (Da)
	Q92922 [UniParc]. Last modified October 14, 2008. Version 3. Checksum: EDA6FF5B0472AEA9	FASTA	1,105	122,867
	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

References

	« Hide 'large scale' referencesShow '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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.

IPI

IPI00234252.

RefSeq

NP_003065.3. NM_003074.3.

UniGene

Hs.476179.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YUS	NMR	-	A	610-675	[»]

ProteinModelPortal

Q92922.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27545N.
DIP-33044N.

IntAct

Q92922. 19 interactions.

MINT

MINT-1137868.

STRING

9606.ENSP00000254480.

PTM databases

PhosphoSite

Q92922.

Polymorphism databases

DMDM

209572723.

Proteomic databases

PaxDb

Q92922.

PRIDE

Q92922.

Protocols and materials databases

DNASU

6599.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254480; ENSP00000254480; ENSG00000173473.

GeneID

6599.

KEGG

hsa:6599.

UCSC

uc003crq.2. human.

Organism-specific databases

CTD

6599.

GeneCards

GC03M047626.

H-InvDB

HIX0030795.

HGNC

HGNC:11104. SMARCC1.

HPA

CAB011576.
CAB016336.
HPA024352.
HPA026853.

MIM

601732. gene.

neXtProt

NX_Q92922.

PharmGKB

PA35954.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5259.

HOGENOM

HOG000047736.

HOVERGEN

HBG054849.

InParanoid

Q92922.

KO

K11649.

OMA

YKKYVHA.

OrthoDB

EOG4V9TSW.

PhylomeDB

Q92922.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_tf_pathway. Regulation of Androgen receptor activity.

Gene expression databases

ArrayExpress

Q92922.

Bgee

Q92922.

CleanEx

HS_SMARCC1.

Genevestigator

Q92922.

GermOnline

ENSG00000173473. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
1.10.10.60. 1 hit.

InterPro

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]

Pfam

PF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF46689. Homeodomain_like. 2 hits.

PROSITE

PS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SMARCC1. human.

EvolutionaryTrace

Q92922.

GenomeRNAi

6599.

NextBio

25671.

SOURCE

Search...

Entry information

Entry name

SMRC1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.