Reviewed, UniProtKB/Swiss-Prot Q96I25 (SPF45_HUMAN)

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) [Complete 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
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	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 protein binding Inferred from physical interaction. Source: UniProtKB
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

49

G-patch

Domain

306 – 385

80

RRM

Amino acid modifications

Modified residue

21

1

N6-acetyllysine Ref.12

Modified residue

71

1

Phosphothreonine Ref.4

Modified residue

155

1

Phosphoserine Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13

Modified residue

169

1

Phosphoserine Ref.9 Ref.11 Ref.6

Modified residue

204

1

Phosphoserine Ref.5

Experimental info

Sequence conflict

214

1

Y → H in AAH09064. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

401

Helix Strand Turn

Details...

Beta strand

305 – 313

9

Helix

323 – 329

7

Helix

330 – 333

4

Beta strand

336 – 343

8

Turn

349 – 351

3

Beta strand

352 – 361

10

Helix

362 – 372

11

Beta strand

383 – 386

4

Helix

389 – 393

5

Sequences

	Sequence		Length	Mass (Da)
	Q96I25-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 99FA8C5E5E998554	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

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: 15489334] [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: 9731529] [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: 12015979] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71 AND SER-155, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-204, MASS SPECTROMETRY.
[6]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, MASS SPECTROMETRY.
[7]	"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: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, MASS SPECTROMETRY. Tissue: T-cell.
[8]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, MASS SPECTROMETRY. Tissue: Liver.
[9]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-169, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-169, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, MASS SPECTROMETRY.
[13]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, 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.
NP_116294.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29409N.

IntAct

Q96I25. 1 interaction.

STRING

Q96I25.

PTM databases

PhosphoSite

Q96I25.

Proteomic databases

PeptideAtlas

Q96I25.

PRIDE

Q96I25.

Genome annotation databases

Ensembl

ENST00000379888; ENSP00000369218; ENSG00000134453; Homo sapiens. [Genome view]
ENST00000446108; ENSP00000388638; ENSG00000134453; Homo sapiens. [Genome view]

GeneID

84991.

KEGG

hsa:84991.

UCSC

uc001ijb.1. human.

Organism-specific databases

CTD

84991.

GeneCards

GC10P006171.

H-InvDB

HIX0008618.

HGNC

HGNC:16944. RBM17.

MIM

606935. gene.

PharmGKB

PA134860993.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG608718.

HOVERGEN

HBG059363.

InParanoid

Q96I25.

OMA

SDERQIV.

OrthoDB

EOG9RBT4P.

PhylomeDB

Q96I25.

Gene expression databases

ArrayExpress

Q96I25.

Bgee

Q96I25.

CleanEx

HS_RBM17.

Genevestigator

Q96I25.

GermOnline

ENSG00000134453. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000467. G_patch.
IPR003954. RNA-recognition_dom1.
IPR016967. Splicing_factor_SPF45.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

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 Resources

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:	March 2, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.