P84103 (SRSF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/arginine-rich splicing factor 3

Alternative name(s):
Pre-mRNA-splicing factor SRP20
Splicing factor, arginine/serine-rich 3

Gene names

Name:	SRSF3
Synonyms:	SFRS3, SRP20

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in RNA processing in relation with cellular proliferation and/or maturation.
Subunit structure	Interacts with CPSF6, RBMY1A1 and SREK1/SFRS12. Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Extensively phosphorylated on serine residues in the RS domain By similarity. Ref.9 Ref.10 Ref.11 Ref.13
Sequence similarities	Belongs to the splicing factor SR family. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	mRNA 3'-end processing Traceable author statement. Source: Reactome mRNA export from nucleus Traceable author statement. Source: Reactome nuclear mRNA splicing, via spliceosome Traceable author statement. Source: Reactome termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular component	nucleoplasm Traceable author statement. Source: Reactome
Molecular function	RNA binding Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 164

164

Serine/arginine-rich splicing factor 3

PRO_0000081923

Regions

Domain

10 – 83

74

RRM

Repeat

119 – 133

15

B-1

Repeat

149 – 164

16

B-2

Region

119 – 164

46

2 X approximate repeats, basic

Compositional bias

86 – 164

79

Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.13

Modified residue

5

1

Phosphoserine Ref.13

Modified residue

23

1

N6-acetyllysine Ref.12

Modified residue

81

1

Phosphoserine Ref.9

Modified residue

95

1

Phosphoserine Ref.10 Ref.11

Modified residue

108

1

Phosphoserine Ref.9

Modified residue

138

1

Phosphoserine Ref.9

Modified residue

140

1

Phosphoserine Ref.9

Modified residue

148

1

Phosphoserine Ref.9

Modified residue

150

1

Phosphoserine Ref.9

Modified residue

152

1

Phosphoserine Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

164

Helix Strand Turn

Details...

Beta strand

2 – 15

14

Turn

18 – 20

3

Helix

23 – 31

9

Beta strand

37 – 45

9

Beta strand

48 – 52

5

Helix

56 – 65

10

Beta strand

67 – 69

3

Beta strand

77 – 80

4

Sequences

	Sequence		Length	Mass (Da)
	P84103 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 02F0A5EE33FF28A0	FASTA	164	19,330
	10 20 30 40 50 60 MHRDSCPLDC KVYVGNLGNN GNKTELERAF GYYGPLRSVW VARNPPGFAF VEFEDPRDAA 70 80 90 100 110 120 DAVRELDGRT LCGCRVRVEL SNGEKRSRNR GPPPSWGRRP RDDYRRRSPP PRRRSPRRRS 130 140 150 160 FSRSRSRSLS RDRRRERSLS RERNHKPSRS FSRSRSRSRS NERK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SR proteins: a conserved family of pre-mRNA splicing factors." Zahler A.M., Lane W.S., Stolk J.A., Roth M.B. Genes Dev. 6:837-847(1992) [PubMed: 1577277] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-37 AND 54-64.
[2]	"Identification and characterization of novel full-length cDNAs differentially expressed in hematopoietic lineages." Liu W.L., Wang M., Tang D., Rodgers G. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Brain and Placenta.
[6]	"Identification and characterization of a novel serine-arginine-rich splicing regulatory protein." Barnard D.C., Patton J.G. Mol. Cell. Biol. 20:3049-3057(2000) [PubMed: 10757789] [Abstract] Cited for: INTERACTION WITH SREK1.
[7]	"The role of potential splicing factors including RBMY, RBMX, hnRNPG-T and STAR proteins in spermatogenesis." Elliott D.J. Int. J. Androl. 27:328-334(2004) [PubMed: 15595951] [Abstract] Cited for: INTERACTION WITH RBMY1A1.
[8]	"Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization." Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M. J. Biol. Chem. 279:35788-35797(2004) [PubMed: 15169763] [Abstract] Cited for: INTERACTION WITH CPSF6.
[9]	"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 SER-81; SER-108; SER-138; SER-140; SER-148; SER-150 AND SER-152, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-95, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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-23, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L10838 mRNA. Translation: AAA36648.1.
AF107405 mRNA. Translation: AAD44523.1.
BT007017 mRNA. Translation: AAP35663.1.
Z85986 Genomic DNA. Translation: CAI19115.1.
BC000914 mRNA. Translation: AAH00914.1.
BC069018 mRNA. Translation: AAH69018.1.

IPI

IPI00010204.

PIR

I54089.

RefSeq

NP_003008.1. NM_003017.4.

UniGene

Hs.405144.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I2Y	NMR	-	A	1-86	[»]
2I38	NMR	-	A	1-86	[»]

ProteinModelPortal

P84103.

SMR

P84103. Positions 3-86.

ModBase

Search...

Protein-protein interaction databases

IntAct

P84103. 15 interactions.

MINT

MINT-5002707.

STRING

P84103.

PTM databases

PhosphoSite

P84103.

Polymorphism databases

DMDM

51338672.

Proteomic databases

PRIDE

P84103.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373715; ENSP00000362820; ENSG00000112081.

GeneID

6428.

KEGG

hsa:6428.

UCSC

uc003omj.1. human.

Organism-specific databases

CTD

6428.

GeneCards

GC06P036562.

H-InvDB

HIX0005822.

HGNC

HGNC:10785. SRSF3.

HPA

CAB012986.

MIM

603364. gene.

neXtProt

NX_P84103.

PharmGKB

PA35701.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20565.

GeneTree

ENSGT00560000076881.

HOGENOM

HBG756718.

HOVERGEN

HBG107480.

InParanoid

P84103.

OMA

PRRSYRS.

OrthoDB

EOG4VDQ12.

PhylomeDB

P84103.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

P84103.

Bgee

P84103.

CleanEx

HS_SFRS3.

Genevestigator

P84103.

GermOnline

ENSG00000112081. Homo sapiens.

Family and domain databases

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

KO

K12892.

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

24965.

SOURCE

Search...

Entry information

Entry name

SRSF3_HUMAN

Accession

Primary (citable) accession number: P84103
Secondary accession number(s): O08831, P23152, Q5R3K0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 85 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.