Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96I25 (SPF45_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Splicing factor 45
Alternative name(s):
45 kDa-splicing factor
RNA-binding motif protein 17
Gene names
Name:RBM17
Synonyms:SPF45
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.3

Subunit structure

Binds SXL. Associates with the spliceosome.

Subcellular location

Nucleus Ref.2.

Sequence similarities

Contains 1 G-patch domain.

Contains 1 RRM (RNA recognition motif) domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 401400Splicing factor 45
PRO_0000081903

Regions

Domain235 – 28349G-patch
Domain306 – 38580RRM

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.14
Modified residue211N6-acetyllysine Ref.10
Modified residue411N6-acetyllysine By similarity
Modified residue711Phosphothreonine Ref.4 Ref.13
Modified residue1551Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.11 Ref.13
Modified residue1691Phosphoserine Ref.6 Ref.11
Modified residue2221Phosphoserine Ref.11 Ref.13

Experimental info

Sequence conflict2141Y → H in AAH09064. Ref.1

Secondary structure

................ 401
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96I25 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 99FA8C5E5E998554

FASTA40144,962
        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 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC007871 mRNA. Translation: AAH07871.1.
BC009064 mRNA. Translation: AAH09064.1.
BC039322 mRNA. Translation: AAH39322.1.
CCDSCCDS7077.1.
RefSeqNP_001139019.1. NM_001145547.1.
NP_116294.1. NM_032905.4.
UniGeneHs.498548.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PE8X-ray2.00A301-401[»]
2PEHX-ray2.11A/B301-401[»]
ProteinModelPortalQ96I25.
SMRQ96I25. Positions 301-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124416. 24 interactions.
DIPDIP-29409N.
IntActQ96I25. 19 interactions.
MINTMINT-3053773.
STRING9606.ENSP00000369218.

PTM databases

PhosphoSiteQ96I25.

Polymorphism databases

DMDM34925383.

Proteomic databases

MaxQBQ96I25.
PaxDbQ96I25.
PeptideAtlasQ96I25.
PRIDEQ96I25.

Protocols and materials databases

DNASU84991.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379888; ENSP00000369218; ENSG00000134453.
ENST00000446108; ENSP00000388638; ENSG00000134453.
GeneID84991.
KEGGhsa:84991.
UCSCuc001ijb.3. human.

Organism-specific databases

CTD84991.
GeneCardsGC10P006130.
HGNCHGNC:16944. RBM17.
HPAHPA037477.
HPA037478.
MIM606935. gene.
neXtProtNX_Q96I25.
PharmGKBPA134860993.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317167.
HOGENOMHOG000231726.
HOVERGENHBG059363.
InParanoidQ96I25.
KOK12840.
OMASDERQIV.
OrthoDBEOG7HMS13.
PhylomeDBQ96I25.
TreeFamTF313987.

Gene expression databases

ArrayExpressQ96I25.
BgeeQ96I25.
CleanExHS_RBM17.
GenevestigatorQ96I25.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR000467. G_patch_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR003954. RRM_dom_euk.
IPR016967. Splicing_factor_SPF45.
[Graphical view]
PfamPF01585. G-patch. 1 hit.
[Graphical view]
PIRSFPIRSF031066. Splicing_factor_SPF45. 1 hit.
SMARTSM00443. G_patch. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
PROSITEPS50174. G_PATCH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96I25.
GeneWikiRBM17.
GenomeRNAi84991.
NextBio75577.
PROQ96I25.
SOURCESearch...

Entry information

Entry nameSPF45_HUMAN
AccessionPrimary (citable) accession number: Q96I25
Secondary accession number(s): Q96GY6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM