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O60264

- SMCA5_HUMAN

UniProt

O60264 - SMCA5_HUMAN

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
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    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
    6. protein binding Source: UniProtKB

    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. embryo development Source: Ensembl
    9. nucleosome assembly Source: UniProtKB
    10. nucleosome positioning Source: UniProtKB
    11. regulation of transcription from RNA polymerase II promoter Source: ProtInc

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    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

    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

    ArrayExpressiO60264.
    BgeeiO60264.
    CleanExiHS_SMARCA5.
    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. 88 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

    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.
    HOGENOMiHOG000192862.
    HOVERGENiHBG056329.
    InParanoidiO60264.
    KOiK11654.
    OMAiPMSEMQV.
    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.
    IPR015194. ISWI_HAND-dom.
    IPR027417. P-loop_NTPase.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    IPR015195. SLIDE.
    IPR000330. SNF2_N.
    [Graphical view]
    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

    MSSAAEPPPP PPPESAPSKP AASIASGGSN SSNKGGPEGV AAQAVASAAS     50
    AGPADAEMEE IFDDASPGKQ KEIQEPDPTY EEKMQTDRAN RFEYLLKQTE 100
    LFAHFIQPAA QKTPTSPLKM KPGRPRIKKD EKQNLLSVGD YRHRRTEQEE 150
    DEELLTESSK ATNVCTRFED SPSYVKWGKL RDYQVRGLNW LISLYENGIN 200
    GILADEMGLG KTLQTISLLG YMKHYRNIPG PHMVLVPKST LHNWMSEFKR 250
    WVPTLRSVCL IGDKEQRAAF VRDVLLPGEW DVCVTSYEML IKEKSVFKKF 300
    NWRYLVIDEA HRIKNEKSKL SEIVREFKTT NRLLLTGTPL QNNLHELWSL 350
    LNFLLPDVFN SADDFDSWFD TNNCLGDQKL VERLHMVLRP FLLRRIKADV 400
    EKSLPPKKEV KIYVGLSKMQ REWYTRILMK DIDILNSAGK MDKMRLLNIL 450
    MQLRKCCNHP YLFDGAEPGP PYTTDMHLVT NSGKMVVLDK LLPKLKEQGS 500
    RVLIFSQMTR VLDILEDYCM WRNYEYCRLD GQTPHDERQD SINAYNEPNS 550
    TKFVFMLSTR AGGLGINLAT ADVVILYDSD WNPQVDLQAM DRAHRIGQTK 600
    TVRVFRFITD NTVEERIVER AEMKLRLDSI VIQQGRLVDQ NLNKIGKDEM 650
    LQMIRHGATH VFASKESEIT DEDIDGILER GAKKTAEMNE KLSKMGESSL 700
    RNFTMDTESS VYNFEGEDYR EKQKIAFTEW IEPPKRERKA NYAVDAYFRE 750
    ALRVSEPKAP KAPRPPKQPN VQDFQFFPPR LFELLEKEIL FYRKTIGYKV 800
    PRNPELPNAA QAQKEEQLKI DEAESLNDEE LEEKEKLLTQ GFTNWNKRDF 850
    NQFIKANEKW GRDDIENIAR EVEGKTPEEV IEYSAVFWER CNELQDIEKI 900
    MAQIERGEAR IQRRISIKKA LDTKIGRYKA PFHQLRISYG TNKGKNYTEE 950
    EDRFLICMLH KLGFDKENVY DELRQCIRNS PQFRFDWFLK SRTAMELQRR 1000
    CNTLITLIER ENMELEEKEK AEKKKRGPKP STQKRKMDGA PDGRGRKKKL 1050
    KL 1052
    Length:1,052
    Mass (Da):121,905
    Last modified:August 1, 1998 - v1
    Checksum:i6CC8CB25BAF7A876
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 88 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.
    HOGENOMi HOG000192862.
    HOVERGENi HBG056329.
    InParanoidi O60264.
    KOi K11654.
    OMAi PMSEMQV.
    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

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

    Gene expression databases

    ArrayExpressi O60264.
    Bgeei O60264.
    CleanExi HS_SMARCA5.
    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.
    IPR015194. ISWI_HAND-dom.
    IPR027417. P-loop_NTPase.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    IPR015195. SLIDE.
    IPR000330. SNF2_N.
    [Graphical view ]
    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

    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].

    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: October 1, 2014
    This is version 139 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