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O60264 (SMCA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1052 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentNucleus
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.10. Source: GOC

ATP-dependent chromatin remodeling

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

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 remodeling

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 assembly

Inferred from direct assay Ref.10. Source: UniProtKB

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_componentNURF 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

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionATP 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 10521051SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
PRO_0000074354

Regions

Domain192 – 357166Helicase ATP-binding
Domain487 – 638152Helicase C-terminal
Domain840 – 89253SANT 1
Domain943 – 100765SANT 2
Nucleotide binding205 – 2128ATP Probable
Motif308 – 3114DEAH box
Compositional bias7 – 137Poly-Pro

Amino acid modifications

Modified residue21N-acetylserine Ref.18
Modified residue661Phosphoserine Ref.15 Ref.16 Ref.17 Ref.19
Modified residue1131Phosphothreonine Ref.21
Modified residue1161Phosphoserine Ref.17
Modified residue1371Phosphoserine Ref.17 Ref.21
Modified residue4401N6-acetyllysine Ref.20
Modified residue8251Phosphoserine Ref.21 Ref.23

Experimental info

Mutagenesis2111K → R: Loss of ATP hydrolysis and no association of the SMARCA5/cohesin/NuRD complex with chromatin. Ref.9

Sequences

Sequence LengthMass (Da)Tools
O60264 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 6CC8CB25BAF7A876

FASTA1,052121,905
        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 

« Hide

References

« Hide '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.
RefSeqNP_003592.3. NM_003601.3.
UniGeneHs.558422.

3D structure databases

ProteinModelPortalO60264.
SMRO60264. Positions 107-703, 743-1021.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114045. 82 interactions.
DIPDIP-33204N.
IntActO60264. 20 interactions.
MINTMINT-2981772.
STRING9606.ENSP00000283131.

PTM databases

PhosphoSiteO60264.

Proteomic databases

PaxDbO60264.
PeptideAtlasO60264.
PRIDEO60264.

Protocols and materials databases

DNASU8467.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283131; ENSP00000283131; ENSG00000153147.
GeneID8467.
KEGGhsa:8467.
UCSCuc003ijg.3. human.

Organism-specific databases

CTD8467.
GeneCardsGC04P144434.
HGNCHGNC:11101. SMARCA5.
HPACAB005227.
HPA008751.
MIM603375. gene.
neXtProtNX_O60264.
Orphanet370334. Extraskeletal Ewing sarcoma.
PharmGKBPA35951.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000192862.
HOVERGENHBG056329.
InParanoidO60264.
KOK11654.
OMAEDYCHWR.
OrthoDBEOG71K625.
PhylomeDBO60264.
TreeFamTF300674.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressO60264.
BgeeO60264.
CleanExHS_SMARCA5.
GenevestigatorO60264.

Family and domain databases

Gene3D1.10.10.60. 2 hits.
3.40.50.300. 2 hits.
InterProIPR020838. 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]
PfamPF13892. DBINO. 1 hit.
PF09110. HAND. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09111. SLIDE. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMSSF101224. SSF101224. 1 hit.
SSF46689. SSF46689. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSMARCA5.
GenomeRNAi8467.
NextBio31688.
PROO60264.
SOURCESearch...

Entry information

Entry nameSMCA5_HUMAN
AccessionPrimary (citable) accession number: O60264
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 134 of the entry and version 1 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

MIM cross-references

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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM