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Q96I25

- SPF45_HUMAN

UniProt

Q96I25 - SPF45_HUMAN

Protein

Splicing factor 45

Gene

RBM17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia.2 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. alternative mRNA splicing, via spliceosome Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Splicing factor 45
    Alternative name(s):
    45 kDa-splicing factor
    RNA-binding motif protein 17
    Gene namesi
    Name:RBM17
    Synonyms:SPF45
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:16944. RBM17.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA
    3. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi319 – 3191D → A: Impairs interaction with SF1; has minor effect on interaction with SF3B1 and U2AF2. 1 Publication
    Mutagenesisi319 – 3191D → K: Abolishes interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing. 1 Publication
    Mutagenesisi375 – 3751R → A: Impairs interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing. 1 Publication
    Mutagenesisi376 – 3761Y → A: Impairs interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing. 1 Publication
    Mutagenesisi377 – 3771F → A: Impairs interaction with SF1 and U2AF2 and abolishes interaction with SF3B1. Abolishes regulation of alternative splicing. 1 Publication

    Organism-specific databases

    PharmGKBiPA134860993.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 401400Splicing factor 45PRO_0000081903Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei21 – 211N6-acetyllysine1 Publication
    Modified residuei41 – 411N6-acetyllysineBy similarity
    Modified residuei71 – 711Phosphothreonine2 Publications
    Modified residuei155 – 1551Phosphoserine7 Publications
    Modified residuei169 – 1691Phosphoserine2 Publications
    Modified residuei222 – 2221Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96I25.
    PaxDbiQ96I25.
    PeptideAtlasiQ96I25.
    PRIDEiQ96I25.

    PTM databases

    PhosphoSiteiQ96I25.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96I25.
    BgeeiQ96I25.
    CleanExiHS_RBM17.
    GenevestigatoriQ96I25.

    Organism-specific databases

    HPAiHPA037477.
    HPA037478.

    Interactioni

    Subunit structurei

    Binds SXL. Associates with the spliceosome. Interacts with SF3B1, SF1 and U2AF2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DHX15O431432EBI-740272,EBI-1237044
    SF3B1O755332EBI-740272,EBI-876542
    SUGP1Q8IWZ82EBI-740272,EBI-2691671

    Protein-protein interaction databases

    BioGridi124416. 24 interactions.
    DIPiDIP-29409N.
    IntActiQ96I25. 19 interactions.
    MINTiMINT-3053773.
    STRINGi9606.ENSP00000369218.

    Structurei

    Secondary structure

    1
    401
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi305 – 3139
    Helixi323 – 3297
    Helixi330 – 3334
    Beta strandi336 – 3438
    Turni349 – 3513
    Beta strandi352 – 36110
    Helixi362 – 37211
    Beta strandi383 – 3864
    Helixi389 – 3935

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PE8X-ray2.00A301-401[»]
    2PEHX-ray2.11A/B301-401[»]
    ProteinModelPortaliQ96I25.
    SMRiQ96I25. Positions 301-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96I25.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini235 – 28349G-patchPROSITE-ProRule annotationAdd
    BLAST
    Domaini306 – 38580RRMAdd
    BLAST

    Sequence similaritiesi

    Contains 1 G-patch domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG317167.
    HOGENOMiHOG000231726.
    HOVERGENiHBG059363.
    InParanoidiQ96I25.
    KOiK12840.
    OMAiSDERQIV.
    OrthoDBiEOG7HMS13.
    PhylomeDBiQ96I25.
    TreeFamiTF313987.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR000467. G_patch_dom.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR003954. RRM_dom_euk.
    IPR016967. Splicing_factor_SPF45.
    [Graphical view]
    PfamiPF01585. G-patch. 1 hit.
    [Graphical view]
    PIRSFiPIRSF031066. Splicing_factor_SPF45. 1 hit.
    SMARTiSM00443. G_patch. 1 hit.
    SM00361. RRM_1. 1 hit.
    [Graphical view]
    PROSITEiPS50174. G_PATCH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q96I25-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLYDDLGVE TSDSKTEGWS KNFKLLQSQL QVKKAALTQA KSQRTKQSTV    50
    LAPVIDLKRG GSSDDRQIVD TPPHVAAGLK DPVPSGFSAG EVLIPLADEY 100
    DPMFPNDYEK VVKRQREERQ RQRELERQKE IEEREKRRKD RHEASGFARR 150
    PDPDSDEDED YERERRKRSM GGAAIAPPTS LVEKDKELPR DFPYEEDSRP 200
    RSQSSKAAIP PPVYEEQDRP RSPTGPSNSF LANMGGTVAH KIMQKYGFRE 250
    GQGLGKHEQG LSTALSVEKT SKRGGKIIVG DATEKDASKK SDSNPLTEIL 300
    KCPTKVVLLR NMVGAGEVDE DLEVETKEEC EKYGKVGKCV IFEIPGAPDD 350
    EAVRIFLEFE RVESAIKAVV DLNGRYFGGR VVKACFYNLD KFRVLDLAEQ 400
    V 401
    Length:401
    Mass (Da):44,962
    Last modified:December 1, 2001 - v1
    Checksum:i99FA8C5E5E998554
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti214 – 2141Y → H in AAH09064. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC007871 mRNA. Translation: AAH07871.1.
    BC009064 mRNA. Translation: AAH09064.1.
    BC039322 mRNA. Translation: AAH39322.1.
    CCDSiCCDS7077.1.
    RefSeqiNP_001139019.1. NM_001145547.1.
    NP_116294.1. NM_032905.4.
    UniGeneiHs.498548.

    Genome annotation databases

    EnsembliENST00000379888; ENSP00000369218; ENSG00000134453.
    ENST00000446108; ENSP00000388638; ENSG00000134453.
    GeneIDi84991.
    KEGGihsa:84991.
    UCSCiuc001ijb.3. human.

    Polymorphism databases

    DMDMi34925383.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC007871 mRNA. Translation: AAH07871.1 .
    BC009064 mRNA. Translation: AAH09064.1 .
    BC039322 mRNA. Translation: AAH39322.1 .
    CCDSi CCDS7077.1.
    RefSeqi NP_001139019.1. NM_001145547.1.
    NP_116294.1. NM_032905.4.
    UniGenei Hs.498548.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PE8 X-ray 2.00 A 301-401 [» ]
    2PEH X-ray 2.11 A/B 301-401 [» ]
    ProteinModelPortali Q96I25.
    SMRi Q96I25. Positions 301-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124416. 24 interactions.
    DIPi DIP-29409N.
    IntActi Q96I25. 19 interactions.
    MINTi MINT-3053773.
    STRINGi 9606.ENSP00000369218.

    PTM databases

    PhosphoSitei Q96I25.

    Polymorphism databases

    DMDMi 34925383.

    Proteomic databases

    MaxQBi Q96I25.
    PaxDbi Q96I25.
    PeptideAtlasi Q96I25.
    PRIDEi Q96I25.

    Protocols and materials databases

    DNASUi 84991.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379888 ; ENSP00000369218 ; ENSG00000134453 .
    ENST00000446108 ; ENSP00000388638 ; ENSG00000134453 .
    GeneIDi 84991.
    KEGGi hsa:84991.
    UCSCi uc001ijb.3. human.

    Organism-specific databases

    CTDi 84991.
    GeneCardsi GC10P006130.
    HGNCi HGNC:16944. RBM17.
    HPAi HPA037477.
    HPA037478.
    MIMi 606935. gene.
    neXtProti NX_Q96I25.
    PharmGKBi PA134860993.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317167.
    HOGENOMi HOG000231726.
    HOVERGENi HBG059363.
    InParanoidi Q96I25.
    KOi K12840.
    OMAi SDERQIV.
    OrthoDBi EOG7HMS13.
    PhylomeDBi Q96I25.
    TreeFami TF313987.

    Miscellaneous databases

    EvolutionaryTracei Q96I25.
    GeneWikii RBM17.
    GenomeRNAii 84991.
    NextBioi 75577.
    PROi Q96I25.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96I25.
    Bgeei Q96I25.
    CleanExi HS_RBM17.
    Genevestigatori Q96I25.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR000467. G_patch_dom.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR003954. RRM_dom_euk.
    IPR016967. Splicing_factor_SPF45.
    [Graphical view ]
    Pfami PF01585. G-patch. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF031066. Splicing_factor_SPF45. 1 hit.
    SMARTi SM00443. G_patch. 1 hit.
    SM00361. RRM_1. 1 hit.
    [Graphical view ]
    PROSITEi PS50174. G_PATCH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Eye, Testis and Uterus.
    2. "Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex."
      Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M.
      Nat. Genet. 20:46-50(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH THE SPLICEOSOME.
    3. "Splicing regulation at the second catalytic step by Sex-lethal involves 3' splice site recognition by SPF45."
      Lallena M.J., Chalmers K.J., Llamazares S., Lamond A.I., Valcarcel J.
      Cell 109:285-296(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "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 THR-71 AND SER-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "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].
    9. "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-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-155; SER-169 AND SER-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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 THR-71; SER-155 AND SER-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "U2AF-homology motif interactions are required for alternative splicing regulation by SPF45."
      Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J., Sattler M.
      Nat. Struct. Mol. Biol. 14:620-629(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 301-401 IN COMPLEX WITH SF3B1, FUNCTION, INTERACTION WITH SF3B1; SF1 AND U2AF2, MUTAGENESIS OF ASP-319; ARG-375; TYR-376 AND PHE-377.

    Entry informationi

    Entry nameiSPF45_HUMAN
    AccessioniPrimary (citable) accession number: Q96I25
    Secondary accession number(s): Q96GY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 118 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3