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UniProtKB/Swiss-Prot entry Q96I25


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SPF45_HUMAN
Primary accession number Q96I25
Secondary accession number Q96GY6
Integrated into Swiss-Prot on September 19, 2003
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 67)
Name and origin of the protein
Protein name Splicing factor 45
Synonyms 45 kDa-splicing factor
RNA-binding motif protein 17
Gene name
Name: RBM17
Synonyms: SPF45
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, Testis, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION WITH THE SPLICEOSOME.
DOI=10.1038/1700; PubMed=9731529 [NCBI, ExPASy, EBI, Israel, Japan]
Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M.;
"Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex.";
Nat. Genet. 20:46-50(1998).
[3]
FUNCTION.
DOI=10.1016/S0092-8674(02)00730-4; PubMed=12015979 [NCBI, ExPASy, EBI, Israel, Japan]
Lallena M.J., Chalmers K.J., Llamazares S., Lamond A.I., Valcarcel J.;
"Splicing regulation at the second catalytic step by Sex-lethal involves 3' splice site recognition by SPF45.";
Cell 109:285-296(2002).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71 AND SER-155, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-204, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-169, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: 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.
  • SUBUNIT: Binds SXL. Associates with the spliceosome.
  • SUBCELLULAR LOCATION: Nucleus.
  • SIMILARITY: Contains 1 G-patch domain.
  • SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BC007871; AAH07871.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009064; AAH09064.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039322; AAH39322.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00176706; -.
RefSeq NP_001139019.1; -.
NP_116294.1; -.
UniGene Hs.498548
3D structure databases
PDB
2PE8; X-ray; 2.00 A; A=301-401.[ExPASy / RCSB / EBI]
2PEH; X-ray; 2.11 A; A/B=301-401.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2PE8; -.
2PEH; -.
ModBase Q96I25.
Protein-protein interaction databases
IntAct Q96I25; 1.
PTM databases
PhosphoSite Q96I25; -.
Organism-specific databases
GeneCards GC10P006171; -.
H-InvDB HIX0008618; -.
HGNC HGNC:16944; RBM17.
GenAtlas RBM17.
MIM 606935; gene. [NCBI / EBI]
PharmGKB PA134860993; -.
Gene expression databases
ArrayExpress Q96I25; -.
Bgee Q96I25; -.
CleanEx HS_RBM17; -.
GermOnline ENSG00000134453; Homo sapiens.
Ontologies
GO
GO:0005681; Cellular component: spliceosome (inferred from electronic annotation from UniProtKB-KW).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006397; Biological process: mRNA processing (inferred from electronic annotation from UniProtKB-KW).
GO:0008380; Biological process: RNA splicing (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR000467; G_patch.
IPR003954; RRM_1.
IPR000504; RRM_RNP1.
IPR016967; Splicing_factor_SPF45.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
Pfam PF01585; G-patch; 1.
PF00076; RRM_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF031066; Splicing_factor_SPF45; 1.
SMART SM00443; G_patch; 1.
SM00361; RRM_1; 1.
SMART graphical view of domain structure.
PROSITE PS50174; G_PATCH; 1.
PS50102; RRM; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q96I25; -.
PRIDE Q96I25; -.
Genome annotation databases
Ensembl ENSG00000134453; Homo sapiens. [Contig view]
GeneID 84991; -.
KEGG hsa:84991; -.
Phylogenomic databases
HOGENOM Q96I25; -.
HOVERGEN Q96I25; -.
OMA Q96I25; PPVYDEQ.
Other
NextBio 75577; -.
SOURCE RBM17; Homo sapiens.
ProtoNet Q96I25.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; RNA-binding; Spliceosome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   401  401     Splicing factor 45. PRO_0000081903
DOMAIN   235   283  49     G-patch. 
DOMAIN   306   385  80     RRM. 
MOD_RES   71    71        Phosphothreonine. 
MOD_RES   155   155        Phosphoserine. 
MOD_RES   169   169        Phosphoserine. 
MOD_RES   204   204        Phosphoserine. 
CONFLICT   214   214        Y -> H (in Ref. 1; AAH09064). 
STRAND   305   313  9      
HELIX   323   329  7      
HELIX   330   333  4      
STRAND   336   343  8      
TURN   349   351  3      
STRAND   352   361  10      
HELIX   362   372  11      
STRAND   383   386  4      
HELIX   389   393  5      
Sequence information
Length: 401 AA [This is the length of the unprocessed precursor] Molecular weight: 44962 Da [This is the MW of the unprocessed precursor] CRC64: 99FA8C5E5E998554 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLYDDLGVE TSDSKTEGWS KNFKLLQSQL QVKKAALTQA KSQRTKQSTV LAPVIDLKRG 

        70         80         90        100        110        120 
GSSDDRQIVD TPPHVAAGLK DPVPSGFSAG EVLIPLADEY DPMFPNDYEK VVKRQREERQ 

       130        140        150        160        170        180 
RQRELERQKE IEEREKRRKD RHEASGFARR PDPDSDEDED YERERRKRSM GGAAIAPPTS 

       190        200        210        220        230        240 
LVEKDKELPR DFPYEEDSRP RSQSSKAAIP PPVYEEQDRP RSPTGPSNSF LANMGGTVAH 

       250        260        270        280        290        300 
KIMQKYGFRE GQGLGKHEQG LSTALSVEKT SKRGGKIIVG DATEKDASKK SDSNPLTEIL 

       310        320        330        340        350        360 
KCPTKVVLLR NMVGAGEVDE DLEVETKEEC EKYGKVGKCV IFEIPGAPDD EAVRIFLEFE 

       370        380        390        400 
RVESAIKAVV DLNGRYFGGR VVKACFYNLD KFRVLDLAEQ V 

Q96I25 in FASTA format

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