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Protein

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5

Gene

Smarca5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2118ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: MGI
  • chromatin assembly or disassembly Source: MGI
  • chromatin remodeling Source: MGI
  • chromatin silencing at rDNA Source: UniProtKB
  • DNA-templated transcription, initiation Source: MGI
  • double-strand break repair Source: BHF-UCL
  • nucleosome assembly Source: MGI
  • nucleosome positioning Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Names & Taxonomyi

Protein namesi
Recommended name:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 (EC:3.6.4.-)
Alternative name(s):
Sucrose nonfermenting protein 2 homolog
Short name:
mSnf2h
Gene namesi
Name:Smarca5
Synonyms:Snf2h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1935129. Smarca5.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • chromatin silencing complex Source: UniProtKB
  • condensed chromosome Source: MGI
  • ISWI-type complex Source: MGI
  • nuclear replication fork Source: Ensembl
  • nucleolus Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • NURF complex Source: MGI
  • RSF complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10511050SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5PRO_0000074355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei55 – 551PhosphothreonineCombined sources
Modified residuei65 – 651PhosphoserineCombined sources
Modified residuei112 – 1121PhosphothreonineCombined sources
Modified residuei115 – 1151PhosphoserineBy similarity
Modified residuei136 – 1361PhosphoserineBy similarity
Modified residuei170 – 1701PhosphoserineBy similarity
Modified residuei439 – 4391N6-acetyllysineCombined sources
Modified residuei754 – 7541PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ91ZW3.
MaxQBiQ91ZW3.
PaxDbiQ91ZW3.
PeptideAtlasiQ91ZW3.
PRIDEiQ91ZW3.

PTM databases

iPTMnetiQ91ZW3.
PhosphoSiteiQ91ZW3.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Developmental stagei

Expressed in CD34-positive erythrocyte progenitor cells. Down-regulated upon differentiation.1 Publication

Gene expression databases

BgeeiQ91ZW3.
GenevisibleiQ91ZW3. MM.

Interactioni

Subunit structurei

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 HBXAP; 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. Interacts with BEND3 (By similarity).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Baz1bQ9Z2772EBI-927547,EBI-927576
MafP548432EBI-927547,EBI-3842521

Protein-protein interaction databases

BioGridi220300. 15 interactions.
DIPiDIP-36073N.
IntActiQ91ZW3. 15 interactions.
MINTiMINT-1867515.
STRINGi10090.ENSMUSP00000044361.

Structurei

3D structure databases

ProteinModelPortaliQ91ZW3.
SMRiQ91ZW3. Positions 742-1020.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini191 – 356166Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini486 – 637152Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini839 – 89153SANT 1PROSITE-ProRule annotationAdd
BLAST
Domaini942 – 100665SANT 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi307 – 3104DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 137Poly-Pro

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 2 SANT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0385. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00830000128349.
HOGENOMiHOG000192862.
HOVERGENiHBG056329.
InParanoidiQ91ZW3.
KOiK11654.
OMAiCTRFEES.
OrthoDBiEOG71K625.
PhylomeDBiQ91ZW3.
TreeFamiTF300674.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009057. Homeodomain-like.
IPR029915. ISWI.
IPR015194. ISWI_HAND-dom.
IPR027417. P-loop_NTPase.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR015195. SLIDE.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF691. PTHR10799:SF691. 3 hits.
PfamiPF13892. DBINO. 1 hit.
PF09110. HAND. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09111. SLIDE. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF101224. SSF101224. 1 hit.
SSF46689. SSF46689. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91ZW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAVEPPPP PPPESAPSKP SAAGAGGSSS GNKGGPEGGA APAAPCAAGS
60 70 80 90 100
GPADTEMEEV FDHGSPGKQK EIQEPDPTYE EKMQTDRANR FEYLLKQTEL
110 120 130 140 150
FAHFIQPAAQ KTPTSPLKMK PGRPRVKKDE KQNLLSVGDY RHRRTEQEED
160 170 180 190 200
EELLTESSKA TNVCTRFEDS PSYVKWGKLR DYQVRGLNWL ISLYENGING
210 220 230 240 250
ILADEMGLGK TLQTISLLGY MKHYRNIPGP HMVLVPKSTL HNWMSEFKKW
260 270 280 290 300
VPTLRSVCLI GDKEQRAAFV RDVLLPGEWD VCVTSYEMLI KEKSVFKKFN
310 320 330 340 350
WRYLVIDEAH RIKNEKSKLS EIVREFKTTN RLLLTGTPLQ NNLHELWSLL
360 370 380 390 400
NFLLPDVFNS ADDFDSWFDT NNCLGDQKLV ERLHMVLRPF LLRRIKADVE
410 420 430 440 450
KSLPPKKEVK IYVGLSKMQR EWYTRILMKD IDILNSAGKM DKMRLLNILM
460 470 480 490 500
QLRKCCNHPY LFDGAEPGPP YTTDMHLVTN SGKMVVLDKL LPKLKEQGSR
510 520 530 540 550
VLIFSQMTRV LDILEDYCMW RNYEYCRLDG QTPHDERQDS INAYNEPNST
560 570 580 590 600
KFVFMLSTRA GGLGINLATA DVVILYDSDW NPQVDLQAMD RAHRIGQTKT
610 620 630 640 650
VRVFRFITDN TVEERIVERA EMKLRLDSIV IQQGRLVDQN LNKIGKDEML
660 670 680 690 700
QMIRHGATHV FASKESEITD EDIDGILERG AKKTAEMNEK LSKMGESSLR
710 720 730 740 750
NFTMDTESSV YNFEGEDYRE KQKIAFTEWI EPPKRERKAN YAVDAYFREA
760 770 780 790 800
LRVSEPKAPK APRPPKQPNV QDFQFFPPRL FELLEKEILY YRKTIGYKVP
810 820 830 840 850
RSPDLPNAAQ AQKEEQLKID EAEPLNDEEL EEKEKLLTQG FTNWNKRDFN
860 870 880 890 900
QFIKANEKWG RDDIENIARE VEGKTPEEVI EYSAVFWERC NELQDIEKIM
910 920 930 940 950
AQIERGEARI QRRISIKKAL DTKIGRYKAP FHQLRISYGT NKGKNYTEEE
960 970 980 990 1000
DRFLICMLHK LGFDKENVYD ELRQCIRNSP QFRFDWFLKS RTAMELQRRC
1010 1020 1030 1040 1050
NTLITLIERE NMELEEKEKA EKKKRGPKPS TQKRKMDGAP DGRGRKKKLK

L
Length:1,051
Mass (Da):121,627
Last modified:December 1, 2001 - v1
Checksum:iC6CB69E7FADE73FC
GO

Sequence cautioni

The sequence AAH21922.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 452AP → GS in AAK52454 (PubMed:11359880).Curated
Sequence conflicti143 – 1431R → C in AAK52454 (PubMed:11359880).Curated
Sequence conflicti157 – 1571S → R in AAK52454 (PubMed:11359880).Curated
Sequence conflicti249 – 2491K → R in AAK52454 (PubMed:11359880).Curated
Sequence conflicti318 – 3181K → N in AAK52454 (PubMed:11359880).Curated
Sequence conflicti373 – 3731C → S in AAK52454 (PubMed:11359880).Curated
Sequence conflicti498 – 4981G → S in AAK52454 (PubMed:11359880).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF375046 mRNA. Translation: AAL25793.1.
AF325921 mRNA. Translation: AAK52454.1.
BC021922 mRNA. Translation: AAH21922.1. Different initiation.
BC053069 mRNA. Translation: AAH53069.1.
AK039811 mRNA. Translation: BAC30458.1.
AK052320 mRNA. Translation: BAC34934.2.
CCDSiCCDS22442.1.
RefSeqiNP_444354.2. NM_053124.2.
UniGeneiMm.246803.
Mm.474173.

Genome annotation databases

EnsembliENSMUST00000043359; ENSMUSP00000044361; ENSMUSG00000031715.
GeneIDi93762.
KEGGimmu:93762.
UCSCiuc009mja.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF375046 mRNA. Translation: AAL25793.1.
AF325921 mRNA. Translation: AAK52454.1.
BC021922 mRNA. Translation: AAH21922.1. Different initiation.
BC053069 mRNA. Translation: AAH53069.1.
AK039811 mRNA. Translation: BAC30458.1.
AK052320 mRNA. Translation: BAC34934.2.
CCDSiCCDS22442.1.
RefSeqiNP_444354.2. NM_053124.2.
UniGeneiMm.246803.
Mm.474173.

3D structure databases

ProteinModelPortaliQ91ZW3.
SMRiQ91ZW3. Positions 742-1020.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220300. 15 interactions.
DIPiDIP-36073N.
IntActiQ91ZW3. 15 interactions.
MINTiMINT-1867515.
STRINGi10090.ENSMUSP00000044361.

PTM databases

iPTMnetiQ91ZW3.
PhosphoSiteiQ91ZW3.

Proteomic databases

EPDiQ91ZW3.
MaxQBiQ91ZW3.
PaxDbiQ91ZW3.
PeptideAtlasiQ91ZW3.
PRIDEiQ91ZW3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043359; ENSMUSP00000044361; ENSMUSG00000031715.
GeneIDi93762.
KEGGimmu:93762.
UCSCiuc009mja.2. mouse.

Organism-specific databases

CTDi8467.
MGIiMGI:1935129. Smarca5.

Phylogenomic databases

eggNOGiKOG0385. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00830000128349.
HOGENOMiHOG000192862.
HOVERGENiHBG056329.
InParanoidiQ91ZW3.
KOiK11654.
OMAiCTRFEES.
OrthoDBiEOG71K625.
PhylomeDBiQ91ZW3.
TreeFamiTF300674.

Enzyme and pathway databases

ReactomeiR-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Miscellaneous databases

PROiQ91ZW3.
SOURCEiSearch...

Gene expression databases

BgeeiQ91ZW3.
GenevisibleiQ91ZW3. MM.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009057. Homeodomain-like.
IPR029915. ISWI.
IPR015194. ISWI_HAND-dom.
IPR027417. P-loop_NTPase.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR015195. SLIDE.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF691. PTHR10799:SF691. 3 hits.
PfamiPF13892. DBINO. 1 hit.
PF09110. HAND. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09111. SLIDE. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF101224. SSF101224. 1 hit.
SSF46689. SSF46689. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Tissue: Erythroleukemia.
  2. "Cloning and characterization of the murine Imitation Switch (ISWI) genes: differential expression patterns suggest distinct developmental roles for Snf2h and Snf2l."
    Lazzaro M.A., Picketts D.J.
    J. Neurochem. 77:1145-1156(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary gland.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-1007.
    Strain: C57BL/6J.
    Tissue: Heart and Thymus.
  5. "NoRC -- a novel member of mammalian ISWI-containing chromatin remodeling machines."
    Strohner R., Nemeth A., Jansa P., Hofmann-Rohrer U., Santoro R., Laengst G., Grummt I.
    EMBO J. 20:4892-4900(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NORC COMPLEX, INTERACTION WITH BAZ2A.
  6. "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 WICH COMPLEX, INTERACTION WITH BAZ1B.
  7. "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription."
    Zhou Y., Santoro R., Grummt I.
    EMBO J. 21:4632-4640(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NORC COMPLEX, INTERACTION WITH BAZ2A AND HDAC1.
  8. "The nucleolar remodeling complex NoRC mediates heterochromatin formation and silencing of ribosomal gene transcription."
    Santoro R., Li J., Grummt I.
    Nat. Genet. 32:393-396(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BAZ2A; DNMT1; DNMT3B AND HDAC1.
  9. "The ISWI ATPase Snf2h is required for early mouse development."
    Stopka T., Skoultchi A.I.
    Proc. Natl. Acad. Sci. U.S.A. 100:14097-14102(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: REVIEW, CHARACTERIZATION OF ISWI COMPLEXES.
  11. "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription."
    Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T., Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.
    EMBO Rep. 7:525-530(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYO1C.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: FUNCTION, INTERACTION WITH BAZ1B.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55; SER-65 AND THR-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Spleen and Testis.
  16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSMCA5_MOUSE
AccessioniPrimary (citable) accession number: Q91ZW3
Secondary accession number(s): Q8C791
, Q8CA22, Q8VDG1, Q925M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.