Splicing factor 45 - Homo sapiens (Human)

Contribute

Send feedback

Read comments (?) or add your own

Q96I25 (SPF45_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Splicing factor 45

Alternative name(s):
45 kDa-splicing factor
RNA-binding motif protein 17

Gene names

Name:	RBM17
Synonyms:	SPF45

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay. Source: HPA spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 401

401

Splicing factor 45

PRO_0000081903

Regions

Domain

235 – 283

G-patch

Domain

306 – 385

RRM

Amino acid modifications

Modified residue

N6-acetyllysine Ref.9

Modified residue

Phosphothreonine Ref.4 Ref.12

Modified residue

155

Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12

Modified residue

169

Phosphoserine Ref.6 Ref.10

Modified residue

222

Phosphoserine Ref.10 Ref.12

Experimental info

Sequence conflict

214

Y → H in AAH09064. Ref.1

Secondary structure

401

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q96I25 [UniParc].

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

FASTA

401

44,962

        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' referencesShow '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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[8]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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, MASS SPECTROMETRY.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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, MASS SPECTROMETRY.
+	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.

IPI

IPI00176706.

RefSeq

NP_001139019.1. NM_001145547.1.
NP_116294.1. NM_032905.4.

UniGene

Hs.498548.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PE8	X-ray	2.00	A	301-401	[»]
2PEH	X-ray	2.11	A/B	301-401	[»]

ProteinModelPortal

Q96I25.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29409N.

IntAct

Q96I25. 8 interactions.

MINT

MINT-3053773.

STRING

9606.ENSP00000369218.

PTM databases

PhosphoSite

Q96I25.

Polymorphism databases

DMDM

34925383.

Proteomic databases

PaxDb

Q96I25.

PeptideAtlas

Q96I25.

PRIDE

Q96I25.

Protocols and materials databases

DNASU

84991.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379888; ENSP00000369218; ENSG00000134453.
ENST00000446108; ENSP00000388638; ENSG00000134453.

GeneID

84991.

KEGG

hsa:84991.

UCSC

uc001ijb.3. human.

Organism-specific databases

CTD

84991.

GeneCards

GC10P006130.

HGNC

HGNC:16944. RBM17.

HPA

HPA037477.

MIM

606935. gene.

neXtProt

NX_Q96I25.

PharmGKB

PA134860993.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG317167.

HOGENOM

HOG000231726.

HOVERGEN

HBG059363.

InParanoid

Q96I25.

K12840.

OMA

IPPPVYD.

OrthoDB

EOG48SGTF.

PhylomeDB

Q96I25.

Gene expression databases

ArrayExpress

Q96I25.

Bgee

Q96I25.

CleanEx

HS_RBM17.

Genevestigator

Q96I25.

GermOnline

ENSG00000134453. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR000467. G_patch_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR003954. RRM_dom_euk.
IPR016967. Splicing_factor_SPF45.
[Graphical view]

Pfam

PF01585. G-patch. 1 hit.
[Graphical view]

PIRSF

PIRSF031066. Splicing_factor_SPF45. 1 hit.

SMART

SM00443. G_patch. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]

PROSITE

PS50174. G_PATCH. 1 hit.
PS50102. RRM. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q96I25.

GenomeRNAi

84991.

NextBio

75577.

SOURCE

Search...

Entry information

Entry name

SPF45_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 10

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents