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O60264

- SMCA5_HUMAN

UniProt

O60264 - SMCA5_HUMAN

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Protein

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

Gene

SMARCA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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.7 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi205 – 2128ATPCurated

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. chromatin binding Source: InterPro
  4. DNA binding Source: UniProtKB
  5. helicase activity Source: ProtInc

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. ATP-dependent chromatin remodeling Source: BHF-UCL
  3. CENP-A containing nucleosome assembly Source: Reactome
  4. chromatin remodeling Source: UniProtKB
  5. chromatin silencing at rDNA Source: Ensembl
  6. DNA-templated transcription, initiation Source: UniProtKB
  7. double-strand break repair Source: Ensembl
  8. nucleosome assembly Source: UniProtKB
  9. nucleosome positioning Source: UniProtKB
  10. regulation of transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_200856. NoRC negatively regulates rRNA expression.
REACT_22186. 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.-)
Short name:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin A5
Alternative name(s):
Sucrose nonfermenting protein 2 homolog
Short name:
hSNF2H
Gene namesi
Name:SMARCA5
Synonyms:SNF2H, WCRF135
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11101. SMARCA5.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. chromatin silencing complex Source: Ensembl
  2. condensed chromosome Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. NURF complex Source: UniProtKB
  6. RSF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi211 – 2111K → R: Loss of ATP hydrolysis and no association of the SMARCA5/cohesin/NuRD complex with chromatin. 1 Publication

Organism-specific databases

Orphaneti370334. Extraskeletal Ewing sarcoma.
PharmGKBiPA35951.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10521051SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5PRO_0000074354Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei66 – 661Phosphoserine4 Publications
Modified residuei113 – 1131Phosphothreonine1 Publication
Modified residuei116 – 1161Phosphoserine1 Publication
Modified residuei137 – 1371Phosphoserine2 Publications
Modified residuei440 – 4401N6-acetyllysine1 Publication
Modified residuei825 – 8251Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO60264.
PaxDbiO60264.
PeptideAtlasiO60264.
PRIDEiO60264.

PTM databases

PhosphoSiteiO60264.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Developmental stagei

Overexpressed in CD34-positive erythrocyte progenitor cells in acute myeloid leukemia. Down-regulation correlates with hematologic remission following chemotherapy.1 Publication

Gene expression databases

BgeeiO60264.
CleanExiHS_SMARCA5.
ExpressionAtlasiO60264. baseline and differential.
GenevestigatoriO60264.

Organism-specific databases

HPAiCAB005227.
HPA008751.

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 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BAZ1BQ9UIG06EBI-352588,EBI-927482
HIST2H4BP628052EBI-352588,EBI-302023
RSF1Q96T235EBI-352588,EBI-926768

Protein-protein interaction databases

BioGridi114045. 90 interactions.
DIPiDIP-33204N.
IntActiO60264. 20 interactions.
MINTiMINT-2981772.
STRINGi9606.ENSP00000283131.

Structurei

3D structure databases

ProteinModelPortaliO60264.
SMRiO60264. Positions 107-700, 743-1021.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 357166Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini487 – 638152Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini840 – 89253SANT 1PROSITE-ProRule annotationAdd
BLAST
Domaini943 – 100765SANT 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi308 – 3114DEAH box

Compositional bias

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

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.Curated
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

eggNOGiCOG0553.
GeneTreeiENSGT00680000100002.
HOGENOMiHOG000192862.
HOVERGENiHBG056329.
InParanoidiO60264.
KOiK11654.
OMAiCTRFEES.
OrthoDBiEOG71K625.
PhylomeDBiO60264.
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:SF575. PTHR10799:SF575. 1 hit.
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.

O60264-1 [UniParc]FASTAAdd to Basket

« Hide

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

KL
Length:1,052
Mass (Da):121,905
Last modified:August 1, 1998 - v1
Checksum:i6CC8CB25BAF7A876
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010882 mRNA. Translation: BAA25173.1.
BC023144 mRNA. Translation: AAH23144.1.
CCDSiCCDS3761.1.
RefSeqiNP_003592.3. NM_003601.3.
UniGeneiHs.558422.

Genome annotation databases

EnsembliENST00000283131; ENSP00000283131; ENSG00000153147.
GeneIDi8467.
KEGGihsa:8467.
UCSCiuc003ijg.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 AB010882 mRNA. Translation: BAA25173.1 .
BC023144 mRNA. Translation: AAH23144.1 .
CCDSi CCDS3761.1.
RefSeqi NP_003592.3. NM_003601.3.
UniGenei Hs.558422.

3D structure databases

ProteinModelPortali O60264.
SMRi O60264. Positions 107-700, 743-1021.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114045. 90 interactions.
DIPi DIP-33204N.
IntActi O60264. 20 interactions.
MINTi MINT-2981772.
STRINGi 9606.ENSP00000283131.

PTM databases

PhosphoSitei O60264.

Proteomic databases

MaxQBi O60264.
PaxDbi O60264.
PeptideAtlasi O60264.
PRIDEi O60264.

Protocols and materials databases

DNASUi 8467.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000283131 ; ENSP00000283131 ; ENSG00000153147 .
GeneIDi 8467.
KEGGi hsa:8467.
UCSCi uc003ijg.3. human.

Organism-specific databases

CTDi 8467.
GeneCardsi GC04P144434.
HGNCi HGNC:11101. SMARCA5.
HPAi CAB005227.
HPA008751.
MIMi 603375. gene.
neXtProti NX_O60264.
Orphaneti 370334. Extraskeletal Ewing sarcoma.
PharmGKBi PA35951.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00680000100002.
HOGENOMi HOG000192862.
HOVERGENi HBG056329.
InParanoidi O60264.
KOi K11654.
OMAi CTRFEES.
OrthoDBi EOG71K625.
PhylomeDBi O60264.
TreeFami TF300674.

Enzyme and pathway databases

Reactomei REACT_200856. NoRC negatively regulates rRNA expression.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.

Miscellaneous databases

ChiTaRSi SMARCA5. human.
GeneWikii SMARCA5.
GenomeRNAii 8467.
NextBioi 31688.
PROi O60264.
SOURCEi Search...

Gene expression databases

Bgeei O60264.
CleanExi HS_SMARCA5.
ExpressionAtlasi O60264. baseline and differential.
Genevestigatori O60264.

Family and domain databases

Gene3Di 1.10.10.60. 2 hits.
3.40.50.300. 2 hits.
InterProi IPR020838. 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 ]
PANTHERi PTHR10799:SF575. PTHR10799:SF575. 1 hit.
Pfami PF13892. DBINO. 1 hit.
PF09110. HAND. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09111. SLIDE. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view ]
SUPFAMi SSF101224. SSF101224. 1 hit.
SSF46689. SSF46689. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiSMCA5_HUMAN
AccessioniPrimary (citable) accession number: O60264
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: August 1, 1998
Last modified: January 7, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.
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