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Protein

Serine/arginine-rich splicing factor 2

Gene

Srsf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA (By similarity). Can bind to the myelin basic protein (MBP) gene MB3 regulatory region and increase transcription of the mbp promoter in cells derived from the CNS. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment (By similarity).By similarity1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: MGI
  • pre-mRNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.
R-MMU-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 2
Alternative name(s):
Protein PR264
Putative myelin regulatory factor 1
Short name:
MRF-1
Splicing component, 35 kDa
Splicing factor SC35
Short name:
SC-35
Splicing factor, arginine/serine-rich 2
Gene namesi
Name:Srsf2
Synonyms:Pr264, Sfrs10, Sfrs2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98284. Srsf2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • nuclear speck Source: MGI
  • nucleus Source: MGI
  • spliceosomal complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 221220Serine/arginine-rich splicing factor 2PRO_0000081919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei22 – 221PhosphothreonineBy similarity
Modified residuei25 – 251PhosphothreonineBy similarity
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei52 – 521N6-acetyllysineBy similarity
Modified residuei189 – 1891PhosphoserineBy similarity
Modified residuei191 – 1911PhosphoserineBy similarity
Modified residuei204 – 2041PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei208 – 2081PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei220 – 2201PhosphoserineBy similarity

Post-translational modificationi

Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by SRPK2 and this causes its redistribution from the nuclear speckle to nucleoplasm and controls cell fate decision in response to cisplatin treatment. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2 nuclear translocation (By similarity).By similarity
Acetylation on Lys-52 by KAT5/TIP60 promotes its proteasomal degradation. This effect is counterbalanced by HDAC6, which positively controls SRSF2 protein level by deacetylating it and preventing its proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ62093.
MaxQBiQ62093.
PaxDbiQ62093.
PRIDEiQ62093.

PTM databases

iPTMnetiQ62093.
PhosphoSiteiQ62093.

Expressioni

Tissue specificityi

Expressed in all the tissues examined; liver, kidney, spleen, heart, lung and brain.1 Publication

Gene expression databases

BgeeiQ62093.
CleanExiMM_SFRS2.
ExpressionAtlasiQ62093. baseline and differential.
GenevisibleiQ62093. MM.

Interactioni

Subunit structurei

Interacts with CCNL1 and CCNL2. Interacts with SCAF11. Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus) (By similarity). In vitro, self-associates and binds SRSF1/SFRS1 (ASF/SF2), SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with BRDT.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdk9Q99J952EBI-2550402,EBI-2654963
Hexim1Q8R4094EBI-2550402,EBI-6261031
Polr2aP087752EBI-2550402,EBI-2549849

Protein-protein interaction databases

BioGridi203188. 4 interactions.
DIPiDIP-44831N.
IntActiQ62093. 9 interactions.
MINTiMINT-1540061.
STRINGi10090.ENSMUSP00000090059.

Structurei

3D structure databases

ProteinModelPortaliQ62093.
SMRiQ62093. Positions 9-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 9279RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi111 – 1166Gly-rich (hinge region)
Compositional biasi117 – 221105Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4207. Eukaryota.
ENOG4111NJ8. LUCA.
GeneTreeiENSGT00700000104403.
HOVERGENiHBG107480.
InParanoidiQ62093.
KOiK12891.
OMAiINSFNIM.
OrthoDBiEOG73BVG8.
TreeFamiTF106262.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62093-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYGRPPPDV EGMTSLKVDN LTYRTSPDTL RRVFEKYGRV GDVYIPRDRY
60 70 80 90 100
TKESRGFAFV RFHDKRDAED AMDAMDGAVL DGRELRVQMA RYGRPPDSHH
110 120 130 140 150
SRRGPPPRRY GGGGYGRRSR SPRRRRRSRS RSRSRSRSRS RSRYSRSKSR
160 170 180 190 200
SRTRSRSRST SKSRSARRSK SKSSSVSRSR SRSRSRSRSR SPPPVSKRES
210 220
KSRSRSKSPP KSPEEEGAVS S
Length:221
Mass (Da):25,476
Last modified:January 23, 2007 - v4
Checksum:i68121AC4D35714FA
GO

Sequence cautioni

The sequence AAA64595.1 differs from that shown. Reason: Frameshift at positions 56, 125 and 141. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 672RD → PH in AAA64595 (PubMed:7527040).Curated
Sequence conflicti89 – 891M → L in AAA64595 (PubMed:7527040).Curated
Sequence conflicti120 – 1201Missing (PubMed:7527040).Curated
Sequence conflicti218 – 2181A → E in AAA64595 (PubMed:7527040).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14648 mRNA. Translation: AAA64595.1. Frameshift.
AF077858 mRNA. Translation: AAC71000.1.
AK086103 mRNA. Translation: BAC39610.1.
AK088042 mRNA. Translation: BAC40111.1.
AK165670 mRNA. Translation: BAE38330.1.
BC005493 mRNA. Translation: AAH05493.1.
X98511 Genomic DNA. Translation: CAA67134.1.
CCDSiCCDS25680.1.
PIRiA55335.
RefSeqiNP_035488.1. NM_011358.2.
XP_006532704.1. XM_006532641.2.
XP_011247137.1. XM_011248835.1.
UniGeneiMm.21841.
Mm.429312.
Mm.469331.

Genome annotation databases

EnsembliENSMUST00000092404; ENSMUSP00000090059; ENSMUSG00000034120.
ENSMUST00000136914; ENSMUSP00000120086; ENSMUSG00000034120.
ENSMUST00000190993; ENSMUSP00000140016; ENSMUSG00000034120.
GeneIDi20382.
KEGGimmu:20382.
UCSCiuc007mmn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14648 mRNA. Translation: AAA64595.1. Frameshift.
AF077858 mRNA. Translation: AAC71000.1.
AK086103 mRNA. Translation: BAC39610.1.
AK088042 mRNA. Translation: BAC40111.1.
AK165670 mRNA. Translation: BAE38330.1.
BC005493 mRNA. Translation: AAH05493.1.
X98511 Genomic DNA. Translation: CAA67134.1.
CCDSiCCDS25680.1.
PIRiA55335.
RefSeqiNP_035488.1. NM_011358.2.
XP_006532704.1. XM_006532641.2.
XP_011247137.1. XM_011248835.1.
UniGeneiMm.21841.
Mm.429312.
Mm.469331.

3D structure databases

ProteinModelPortaliQ62093.
SMRiQ62093. Positions 9-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203188. 4 interactions.
DIPiDIP-44831N.
IntActiQ62093. 9 interactions.
MINTiMINT-1540061.
STRINGi10090.ENSMUSP00000090059.

PTM databases

iPTMnetiQ62093.
PhosphoSiteiQ62093.

Proteomic databases

EPDiQ62093.
MaxQBiQ62093.
PaxDbiQ62093.
PRIDEiQ62093.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092404; ENSMUSP00000090059; ENSMUSG00000034120.
ENSMUST00000136914; ENSMUSP00000120086; ENSMUSG00000034120.
ENSMUST00000190993; ENSMUSP00000140016; ENSMUSG00000034120.
GeneIDi20382.
KEGGimmu:20382.
UCSCiuc007mmn.2. mouse.

Organism-specific databases

CTDi6427.
MGIiMGI:98284. Srsf2.

Phylogenomic databases

eggNOGiKOG4207. Eukaryota.
ENOG4111NJ8. LUCA.
GeneTreeiENSGT00700000104403.
HOVERGENiHBG107480.
InParanoidiQ62093.
KOiK12891.
OMAiINSFNIM.
OrthoDBiEOG73BVG8.
TreeFamiTF106262.

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.
R-MMU-72187. mRNA 3'-end processing.

Miscellaneous databases

ChiTaRSiSrsf2. mouse.
NextBioi298298.
PROiQ62093.
SOURCEiSearch...

Gene expression databases

BgeeiQ62093.
CleanExiMM_SFRS2.
ExpressionAtlasiQ62093. baseline and differential.
GenevisibleiQ62093. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of MRF-1, a brain-derived DNA-binding protein with a capacity to regulate expression of myelin basic protein gene."
    Haque N.S., Buchberg A.M., Khalili K.
    J. Biol. Chem. 269:31149-31156(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN MBP REGULATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing."
    Yang L., Embree L.J., Tsai S., Hickstein D.D.
    J. Biol. Chem. 273:27761-27764(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Bone marrow and Thymus.
  4. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  5. Gaillard C., Perbal B.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
    Strain: 129/Sv.
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-206; SER-208 AND SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Spleen and Testis.
  7. "The testis-specific double bromodomain-containing protein BRDT forms a complex with multiple spliceosome components and is required for mRNA splicing and 3'-UTR truncation in round spermatids."
    Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.
    Nucleic Acids Res. 40:7162-7175(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRDT.

Entry informationi

Entry nameiSRSF2_MOUSE
AccessioniPrimary (citable) accession number: Q62093
Secondary accession number(s): Q542L3, Q60701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.