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Q96I25

- SPF45_HUMAN

UniProt

Q96I25 - SPF45_HUMAN

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Protein
Splicing factor 45
Gene
RBM17, SPF45
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. RNA splicing Source: UniProtKB-KW
  2. mRNA processing Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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.
Mutagenesisi319 – 3191D → K: Abolishes interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing.
Mutagenesisi375 – 3751R → A: Impairs interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing.
Mutagenesisi376 – 3761Y → A: Impairs interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing.
Mutagenesisi377 – 3771F → A: Impairs interaction with SF1 and U2AF2 and abolishes interaction with SF3B1. Abolishes regulation of alternative splicing.

Organism-specific databases

PharmGKBiPA134860993.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 401400Splicing factor 45
PRO_0000081903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei21 – 211N6-acetyllysine1 Publication
Modified residuei41 – 411N6-acetyllysine By 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.

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

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.

Miscellaneous databases

EvolutionaryTraceiQ96I25.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini235 – 28349G-patch
Add
BLAST
Domaini306 – 38580RRM
Add
BLAST

Sequence similaritiesi

Contains 1 G-patch domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti214 – 2141Y → H in AAH09064. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 117 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

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