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O95391

- SLU7_HUMAN

UniProt

O95391 - SLU7_HUMAN

Protein

Pre-mRNA-splicing factor SLU7

Gene

SLU7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (03 Nov 2009)
      Previous versions | rss
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    Functioni

    Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri118 – 13518CCHC-typeAdd
    BLAST

    GO - Molecular functioni

    1. pre-mRNA 3'-splice site binding Source: HGNC
    2. protein binding Source: IntAct
    3. second spliceosomal transesterification activity Source: HGNC
    4. zinc ion binding Source: HGNC

    GO - Biological processi

    1. alternative mRNA splicing, via spliceosome Source: HGNC
    2. cellular response to heat Source: UniProtKB
    3. intracellular protein transport Source: UniProtKB
    4. mRNA 3'-splice site recognition Source: HGNC
    5. mRNA splicing, via spliceosome Source: UniProtKB
    6. RNA splicing, via transesterification reactions Source: HGNC

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pre-mRNA-splicing factor SLU7
    Short name:
    hSlu7
    Gene namesi
    Name:SLU7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:16939. SLU7.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Upon UV-C stress stimulus, the nuclear concentration of the protein decreases, affecting alternative splicing. Translocates from the nucleus to the cytoplasm after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. intracellular membrane-bounded organelle Source: HPA
    4. membrane Source: UniProtKB
    5. nuclear speck Source: HGNC
    6. nucleus Source: UniProtKB
    7. small nuclear ribonucleoprotein complex Source: HGNC
    8. spliceosomal complex Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi116 – 1161R → N: Abolishes nuclear localization. 1 Publication
    Mutagenesisi117 – 1171K → N: Abolishes nuclear localization. 1 Publication
    Mutagenesisi120 – 1201C → S: Induces a cytoplasmic localization; when associated with S-123; G-128 and S-133. 1 Publication
    Mutagenesisi123 – 1231C → S: Induces a cytoplasmic localization; when associated with S-120; G-128 and S-133. 1 Publication
    Mutagenesisi125 – 1262AM → VP: Does not affect nuclear localization.
    Mutagenesisi128 – 1281H → G: Induces a cytoplasmic localization; when associated with S-120; S-123 and S-133. 1 Publication
    Mutagenesisi129 – 1291K → N: Abolishes nuclear localization. 1 Publication
    Mutagenesisi133 – 1331C → S: Induces a cytoplasmic localization; when associated with S-120; S-123 and G-128. 1 Publication
    Mutagenesisi136 – 1361R → N: Abolishes nuclear localization.
    Mutagenesisi166 – 1661K → N: Abolishes nuclear localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA128394574.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 586585Pre-mRNA-splicing factor SLU7PRO_0000289194Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei215 – 2151Phosphoserine5 Publications
    Modified residuei227 – 2271Phosphoserine1 Publication
    Modified residuei235 – 2351Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95391.
    PaxDbiO95391.
    PRIDEiO95391.

    PTM databases

    PhosphoSiteiO95391.

    Miscellaneous databases

    PMAP-CutDBO95391.

    Expressioni

    Gene expression databases

    ArrayExpressiO95391.
    BgeeiO95391.
    CleanExiHS_SLU7.
    GenevestigatoriO95391.

    Organism-specific databases

    HPAiHPA035907.

    Interactioni

    Subunit structurei

    Component of late spliceosomal complexes. Associates with the spliceosome prior to recognition of the 3'-splice site for step II, probably during catalysis of step I.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRPF3O433952EBI-750559,EBI-744322
    PRPF8Q6P2Q92EBI-750559,EBI-538479
    SF3B2Q134352EBI-750559,EBI-749111
    WHSC1L1Q9BZ952EBI-750559,EBI-3390132

    Protein-protein interaction databases

    BioGridi115820. 22 interactions.
    IntActiO95391. 17 interactions.
    MINTiMINT-1467161.
    STRINGi9606.ENSP00000297151.

    Structurei

    3D structure databases

    ProteinModelPortaliO95391.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi129 – 16941Bipartite nuclear localization signalAdd
    BLAST

    Domaini

    The CCHC-type zinc finger is required to retain the protein within the nucleus and prevent its shuttle back to the cytoplasm via the CRM1 pathway.1 Publication

    Sequence similaritiesi

    Belongs to the SLU7 family.Curated
    Contains 1 CCHC-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri118 – 13518CCHC-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG251791.
    HOGENOMiHOG000194391.
    HOVERGENiHBG053287.
    InParanoidiO95391.
    KOiK12819.
    OMAiEECIIND.
    OrthoDBiEOG7GQXV9.
    PhylomeDBiO95391.
    TreeFamiTF105691.

    Family and domain databases

    InterProiIPR021715. Slu7.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF11708. Slu7. 1 hit.
    [Graphical view]
    SMARTiSM00343. ZnF_C2HC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O95391-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSATVVDAVN AAPLSGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA    50
    EVDEEGKDIN PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE 100
    WYKRGVKENS IITKYRKGAC ENCGAMTHKK KDCFERPRRV GAKFTGTNIA 150
    PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK IVEEYAKVDL AKRTLKAQKL 200
    QEELASGKLV EQANSPKHQW GEEEPNSQME KDHNSEDEDE DKYADDIDMP 250
    GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA 300
    GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL 350
    ELLYKSFKVK KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY 400
    SRHGTVIKGQ ERAVACSKYE EDVKIHNHTH IWGSYWKEGR WGYKCCHSFF 450
    KYSYCTGEAG KEIVNSEECI INEITGEESV KKPQTLMELH QEKLKEEKKK 500
    KKKKKKKHRK SSSDSDDEEK KHEKLKKALN AEEARLLHVK ETMQIDERKR 550
    PYNSMYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ 586
    Length:586
    Mass (Da):68,387
    Last modified:November 3, 2009 - v2
    Checksum:i237B8C8014EEAB6E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti111 – 1111I → V.1 Publication
    Corresponds to variant rs17856338 [ dbSNP | Ensembl ].
    VAR_032598
    Natural varianti229 – 2291M → T.5 Publications
    Corresponds to variant rs2961944 [ dbSNP | Ensembl ].
    VAR_032599

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF101074 mRNA. Translation: AAD13774.1.
    AC091842 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61554.1.
    CH471062 Genomic DNA. Translation: EAW61555.1.
    BC010634 mRNA. Translation: AAH10634.1.
    AY486334 mRNA. Translation: AAS59410.1.
    DQ174516 mRNA. Translation: ABA08382.1.
    DQ174517 mRNA. Translation: ABA08383.1.
    CCDSiCCDS4352.1.
    RefSeqiNP_006416.3. NM_006425.4.
    UniGeneiHs.435342.

    Genome annotation databases

    EnsembliENST00000297151; ENSP00000297151; ENSG00000164609.
    ENST00000520664; ENSP00000428362; ENSG00000164609.
    GeneIDi10569.
    KEGGihsa:10569.
    UCSCiuc003lyg.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF101074 mRNA. Translation: AAD13774.1 .
    AC091842 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61554.1 .
    CH471062 Genomic DNA. Translation: EAW61555.1 .
    BC010634 mRNA. Translation: AAH10634.1 .
    AY486334 mRNA. Translation: AAS59410.1 .
    DQ174516 mRNA. Translation: ABA08382.1 .
    DQ174517 mRNA. Translation: ABA08383.1 .
    CCDSi CCDS4352.1.
    RefSeqi NP_006416.3. NM_006425.4.
    UniGenei Hs.435342.

    3D structure databases

    ProteinModelPortali O95391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115820. 22 interactions.
    IntActi O95391. 17 interactions.
    MINTi MINT-1467161.
    STRINGi 9606.ENSP00000297151.

    PTM databases

    PhosphoSitei O95391.

    Proteomic databases

    MaxQBi O95391.
    PaxDbi O95391.
    PRIDEi O95391.

    Protocols and materials databases

    DNASUi 10569.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297151 ; ENSP00000297151 ; ENSG00000164609 .
    ENST00000520664 ; ENSP00000428362 ; ENSG00000164609 .
    GeneIDi 10569.
    KEGGi hsa:10569.
    UCSCi uc003lyg.3. human.

    Organism-specific databases

    CTDi 10569.
    GeneCardsi GC05M159762.
    HGNCi HGNC:16939. SLU7.
    HPAi HPA035907.
    MIMi 605974. gene.
    neXtProti NX_O95391.
    PharmGKBi PA128394574.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251791.
    HOGENOMi HOG000194391.
    HOVERGENi HBG053287.
    InParanoidi O95391.
    KOi K12819.
    OMAi EECIIND.
    OrthoDBi EOG7GQXV9.
    PhylomeDBi O95391.
    TreeFami TF105691.

    Miscellaneous databases

    ChiTaRSi SLU7. human.
    GeneWikii SLU7.
    GenomeRNAii 10569.
    NextBioi 40113.
    PMAP-CutDB O95391.
    PROi O95391.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95391.
    Bgeei O95391.
    CleanExi HS_SLU7.
    Genevestigatori O95391.

    Family and domain databases

    InterProi IPR021715. Slu7.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF11708. Slu7. 1 hit.
    [Graphical view ]
    SMARTi SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human step II splicing factor hSlu7 functions in restructuring the spliceosome between the catalytic steps of splicing."
      Chua K., Reed R.
      Genes Dev. 13:841-850(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATE SPLICEOSOMAL COMPLEX, VARIANT THR-229.
    2. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-229.
    4. "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], VARIANTS VAL-111 AND THR-229.
      Tissue: Eye.
    5. Holste D., Shomron N., Burge C.B.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-102.
      Tissue: Colon.
    6. "The RNA splicing factor hSlu7 is required for correct 3' splice-site choice."
      Chua K., Reed R.
      Nature 402:207-210(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The birth of an alternatively spliced exon: 3' splice-site selection in Alu exons."
      Lev-Maor G., Sorek R., Shomron N., Ast G.
      Science 300:1288-1291(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Splicing factor hSlu7 contains a unique functional domain required to retain the protein within the nucleus."
      Shomron N., Reznik M., Ast G.
      Mol. Biol. Cell 15:3782-3795(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN CCHC-TYPE ZINC-FINGER, ZINC-BINDING, MUTAGENESIS OF ARG-116; LYS-117; CYS-120; CYS-123; 125-ALA-MET-126; HIS-128; LYS-129; CYS-133 AND LYS-166.
    9. "Stress alters the subcellular distribution of hSlu7 and thus modulates alternative splicing."
      Shomron N., Alberstein M., Reznik M., Ast G.
      J. Cell Sci. 118:1151-1159(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. Erratum
      Shomron N., Alberstein M., Reznik M., Ast G.
      J. Cell Sci. 118:1331-1331(2005)
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, VARIANT [LARGE SCALE ANALYSIS] THR-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. "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 SER-215; SER-227 AND SER-235, VARIANT [LARGE SCALE ANALYSIS] THR-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7."
      Janowicz A., Michalak M., Krebs J.
      Biochim. Biophys. Acta 1813:1045-1049(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    17. "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-215 AND SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSLU7_HUMAN
    AccessioniPrimary (citable) accession number: O95391
    Secondary accession number(s): D3DQK2
    , Q3LUJ0, Q3LUJ1, Q6RXQ5, Q96FM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 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 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3