O60264 (SMCA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
Short name=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin A5
EC=3.6.4.-

Alternative name(s):
Sucrose nonfermenting protein 2 homolog
Short name=hSNF2H

Gene names

Name:	SMARCA5
Synonyms:	SNF2H, WCRF135

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1052 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	Helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity. Complexes containing SMARCA5 are capable of forming ordered nucleosome arrays on chromatin; this may require intact histone H4 tails. Also required for replication of pericentric heterochromatin in S-phase specifically in conjunction with BAZ1A. Probably plays a role in repression of polI dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14
Subunit structure	Catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. Each complex contains subunits which may regulate the specificity or catalytic activity of SMARCA5. ACF/WCRF contains BAZ1A; CHRAC contains BAZ1A, CHRAC1, and POLE3; RSF contains RSF1; WICH contains BAZ1B/WSTF. SMARCA5 is the catalytic subunit of the NoRC chromatin-remodeling complex, which also contains BAZ2A/TIP5. The BAZ2A/TIP5 subunit of NoRC also interacts with DNMT1, DNMT3B and HDAC1, which allows NoRC to actively suppress rDNA transcription by a combination of nucleosome remodeling, histone deacetylation, and DNA methylation. Catalytic subunit of SMARCA5/cohesin/NuRD complexes. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with MYO1C By similarity. Ref.3 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14
Subcellular location	Nucleus Ref.8.
Tissue specificity	Ubiquitously expressed.
Developmental stage	Overexpressed in CD34-positive erythrocyte progenitor cells in acute myeloid leukemia. Down-regulation correlates with hematologic remission following chemotherapy. Ref.4
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. ISWI subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 2 SANT domains.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chromatin regulator Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CENP-A containing nucleosome assembly at centromere Traceable author statement. Source: Reactome DNA-templated transcription, initiation Inferred from direct assay PubMed 9836642. Source: UniProtKB chromatin silencing at rDNA Inferred from electronic annotation. Source: Ensembl double-strand break repair Inferred from electronic annotation. Source: Ensembl embryo development Inferred from electronic annotation. Source: Ensembl nucleosome positioning Inferred from direct assay PubMed 9836642. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	NURF complex Inferred from direct assay PubMed 20850016. Source: UniProtKB RSF complex Inferred from physical interaction PubMed 9836642. Source: UniProtKB chromatin silencing complex Inferred from electronic annotation. Source: Ensembl condensed chromosome Inferred from direct assay Ref.10. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from direct assay Ref.10. Source: UniProtKB ATPase activity Inferred from direct assay Ref.10. Source: UniProtKB DNA binding Inferred from direct assay Ref.10. Source: UniProtKB chromatin binding Inferred from electronic annotation. Source: InterPro helicase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAZ1B	Q9UIG0	6	EBI-352588,EBI-927482
HIST2H4B	P62805	2	EBI-352588,EBI-302023
RSF1	Q96T23	5	EBI-352588,EBI-926768

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.18
	Chain	2 – 1052	1051	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5		PRO_0000074354
Regions
	Domain	192 – 357	166	Helicase ATP-binding
	Domain	487 – 638	152	Helicase C-terminal
	Domain	840 – 892	53	SANT 1
	Domain	943 – 1007	65	SANT 2
	Nucleotide binding	205 – 212	8	ATP Probable
	Motif	308 – 311	4	DEAH box
	Compositional bias	7 – 13	7	Poly-Pro
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.18
	Modified residue	66	1	Phosphoserine Ref.15 Ref.16 Ref.17 Ref.19
	Modified residue	113	1	Phosphothreonine Ref.21 Ref.23
	Modified residue	116	1	Phosphoserine Ref.17 Ref.23
	Modified residue	137	1	Phosphoserine Ref.17 Ref.21
	Modified residue	440	1	N6-acetyllysine Ref.20
	Modified residue	825	1	Phosphoserine Ref.21 Ref.23
Experimental info
	Mutagenesis	211	1	K → R: Loss of ATP hydrolysis and no association of the SMARCA5/cohesin/NuRD complex with chromatin. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	O60264 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 6CC8CB25BAF7A876	FASTA	1,052	121,905
	10 20 30 40 50 60 MSSAAEPPPP PPPESAPSKP AASIASGGSN SSNKGGPEGV AAQAVASAAS AGPADAEMEE 70 80 90 100 110 120 IFDDASPGKQ KEIQEPDPTY EEKMQTDRAN RFEYLLKQTE LFAHFIQPAA QKTPTSPLKM 130 140 150 160 170 180 KPGRPRIKKD EKQNLLSVGD YRHRRTEQEE DEELLTESSK ATNVCTRFED SPSYVKWGKL 190 200 210 220 230 240 RDYQVRGLNW LISLYENGIN GILADEMGLG KTLQTISLLG YMKHYRNIPG PHMVLVPKST 250 260 270 280 290 300 LHNWMSEFKR WVPTLRSVCL IGDKEQRAAF VRDVLLPGEW DVCVTSYEML IKEKSVFKKF 310 320 330 340 350 360 NWRYLVIDEA HRIKNEKSKL SEIVREFKTT NRLLLTGTPL QNNLHELWSL LNFLLPDVFN 370 380 390 400 410 420 SADDFDSWFD TNNCLGDQKL VERLHMVLRP FLLRRIKADV EKSLPPKKEV KIYVGLSKMQ 430 440 450 460 470 480 REWYTRILMK DIDILNSAGK MDKMRLLNIL MQLRKCCNHP YLFDGAEPGP PYTTDMHLVT 490 500 510 520 530 540 NSGKMVVLDK LLPKLKEQGS RVLIFSQMTR VLDILEDYCM WRNYEYCRLD GQTPHDERQD 550 560 570 580 590 600 SINAYNEPNS TKFVFMLSTR AGGLGINLAT ADVVILYDSD WNPQVDLQAM DRAHRIGQTK 610 620 630 640 650 660 TVRVFRFITD NTVEERIVER AEMKLRLDSI VIQQGRLVDQ NLNKIGKDEM LQMIRHGATH 670 680 690 700 710 720 VFASKESEIT DEDIDGILER GAKKTAEMNE KLSKMGESSL RNFTMDTESS VYNFEGEDYR 730 740 750 760 770 780 EKQKIAFTEW IEPPKRERKA NYAVDAYFRE ALRVSEPKAP KAPRPPKQPN VQDFQFFPPR 790 800 810 820 830 840 LFELLEKEIL FYRKTIGYKV PRNPELPNAA QAQKEEQLKI DEAESLNDEE LEEKEKLLTQ 850 860 870 880 890 900 GFTNWNKRDF NQFIKANEKW GRDDIENIAR EVEGKTPEEV IEYSAVFWER CNELQDIEKI 910 920 930 940 950 960 MAQIERGEAR IQRRISIKKA LDTKIGRYKA PFHQLRISYG TNKGKNYTEE EDRFLICMLH 970 980 990 1000 1010 1020 KLGFDKENVY DELRQCIRNS PQFRFDWFLK SRTAMELQRR CNTLITLIER ENMELEEKEK 1030 1040 1050 AEKKKRGPKP STQKRKMDGA PDGRGRKKKL KL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and mapping of SMARCA5 encoding hSNF2H, a novel human homologue of Drosophila ISWI." Aihara T., Miyoshi Y., Koyama K., Suzuki M., Takahashi E., Monden M., Nakamura Y. Cytogenet. Cell Genet. 81:191-193(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[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: Lymph.
[3]	"HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins." Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V., Becker P.B., Bickmore W.A., Varga-Weisz P.D. EMBO J. 19:3377-3387(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE CHRAC COMPLEX WITH BAZ1A; CHRAC1 AND POLE3.
[4]	"Chromatin remodeling gene SMARCA5 is dysregulated in primitive hematopoietic cells of acute leukemia." Stopka T., Zakova D., Fuchs O., Kubrova O., Blafkova J., Jelinek J., Necas E., Zivny J. Leukemia 14:1247-1252(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[5]	"A family of chromatin remodeling factors related to Williams syndrome transcription factor." Bochar D.A., Savard J., Wang W., Lafleur D.W., Moore P., Cote J., Shiekhattar R. Proc. Natl. Acad. Sci. U.S.A. 97:1038-1043(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE ACF/WCRF COMPLEX WITH BAZ1A.
[6]	"Functional differences between the human ATP-dependent nucleosome remodeling proteins BRG1 and SNF2H." Aalfs J.D., Narlikar G.J., Kingston R.E. J. Biol. Chem. 276:34270-34278(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci." Bozhenok L., Wade P.A., Varga-Weisz P. EMBO J. 21:2231-2241(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE WHICH COMPLEX WITH BAZ1B.
[8]	"An ACF1-ISWI chromatin-remodeling complex is required for DNA replication through heterochromatin." Collins N., Poot R.A., Kukimoto I., Garcia-Jimenez C., Dellaire G., Varga-Weisz P.D. Nat. Genet. 32:627-632(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE ACF/WCRF COMPLEX WITH BAZ1A.
[9]	"A chromatin remodelling complex that loads cohesin onto human chromosomes." Hakimi M.-A., Bochar D.A., Schmiesing J.A., Dong Y., Barak O.G., Speicher D.W., Yokomori K., Shiekhattar R. Nature 418:994-998(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SMARCA5/COHESIN/NURD COMPLEX, MUTAGENESIS OF LYS-211.
[10]	"Functional analysis of the subunits of the chromatin assembly factor RSF." Loyola A., Huang J.-Y., LeRoy G., Hu S., Wang Y.-H., Donnelly R.J., Lane W.S., Lee S.-C., Reinberg D. Mol. Cell. Biol. 23:6759-6768(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE RSF COMPLEX WITH HBXAP.
[11]	"Functional diversity of ISWI complexes." Dirscherl S.S., Krebs J.E. Biochem. Cell Biol. 82:482-489(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW, CHARACTERIZATION OF ISWI COMPLEXES.
[12]	"The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci." Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D. Nat. Cell Biol. 6:1236-1244(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BAZ1B.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription." Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K. J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE B-WICH COMPLEX.
[15]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[16]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[17]	"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-66; SER-116 AND SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[18]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[19]	"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-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[20]	"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-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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 THR-113; SER-137 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[22]	"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].
[23]	"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-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB010882 mRNA. Translation: BAA25173.1. BC023144 mRNA. Translation: AAH23144.1.
RefSeq	NP_003592.3. NM_003601.3.
UniGene	Hs.558422.
3D structure databases
ProteinModelPortal	O60264.
SMR	O60264. Positions 107-703, 743-1021.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	114045. 82 interactions.
DIP	DIP-33204N.
IntAct	O60264. 20 interactions.
MINT	MINT-2981772.
STRING	9606.ENSP00000283131.
PTM databases
PhosphoSite	O60264.
Proteomic databases
PaxDb	O60264.
PeptideAtlas	O60264.
PRIDE	O60264.
Protocols and materials databases
DNASU	8467.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000283131; ENSP00000283131; ENSG00000153147.
GeneID	8467.
KEGG	hsa:8467.
UCSC	uc003ijg.3. human.
Organism-specific databases
CTD	8467.
GeneCards	GC04P144434.
HGNC	HGNC:11101. SMARCA5.
HPA	CAB005227. HPA008751.
MIM	603375. gene.
neXtProt	NX_O60264.
Orphanet	370334. Extraskeletal Ewing sarcoma.
PharmGKB	PA35951.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0553.
HOGENOM	HOG000192862.
HOVERGEN	HBG056329.
InParanoid	O60264.
KO	K11654.
OMA	EDYCHWR.
OrthoDB	EOG71K625.
PhylomeDB	O60264.
TreeFam	TF300674.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle.
Gene expression databases
ArrayExpress	O60264.
Bgee	O60264.
CleanEx	HS_SMARCA5.
Genevestigator	O60264.
Family and domain databases
Gene3D	1.10.10.60. 2 hits.
InterPro	IPR020838. DBINO. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR009057. Homeodomain-like. IPR015194. ISWI_HAND-dom. IPR027417. P-loop_NTPase. IPR001005. SANT/Myb. IPR017884. SANT_dom. IPR015195. SLIDE. IPR000330. SNF2_N. [Graphical view]
Pfam	PF13892. DBINO. 1 hit. PF09110. HAND. 1 hit. PF00271. Helicase_C. 1 hit. PF09111. SLIDE. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. SM00717. SANT. 2 hits. [Graphical view]
SUPFAM	SSF101224. SSF101224. 1 hit. SSF46689. SSF46689. 2 hits. SSF52540. SSF52540. 2 hits.
PROSITE	PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51293. SANT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GeneWiki	SMARCA5.
GenomeRNAi	8467.
NextBio	31688.
PRO	O60264.
SOURCE	Search...

Entry information

Entry name

SMCA5_HUMAN

Accession

Primary (citable) accession number: O60264

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2004
Last sequence update:	August 1, 1998
Last modified:	March 19, 2014
This is version 133 of the entry and version 1 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.