Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/arginine-rich splicing factor 10

Gene

Srsf10

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

Functioni

Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. Also acts as a splicing factor that specifically promotes exon skipping during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (By similarity). May be involved in regulation of alternative splicing in neurons (PubMed:10583508).By similarity1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: MGI
  • RNA binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • cytoplasmic transport Source: UniProtKB
  • mRNA export from nucleus Source: UniProtKB
  • mRNA splice site selection Source: UniProtKB
  • mRNA splicing, via spliceosome Source: MGI
  • negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • RNA splicing, via transesterification reactions Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 10
Alternative name(s):
FUS-interacting serine-arginine-rich protein 1
Neural-salient serine/arginine-rich protein
Neural-specific SR protein
Splicing factor, arginine/serine-rich 13A
TLS-associated protein with Ser-Arg repeats
Short name:
TASR
Short name:
TLS-associated protein with SR repeats
TLS-associated serine-arginine protein
Short name:
TLS-associated SR protein
Gene namesi
Name:Srsf10
Synonyms:Fusip1, Nssr, Sfrs13a, Srsf13a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1333805. Srsf10.

Subcellular locationi

  • Nucleus speckle 1 Publication

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Serine/arginine-rich splicing factor 10PRO_0000081594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei108 – 1081PhosphoserineBy similarity
Modified residuei129 – 1291PhosphoserineBy similarity
Modified residuei131 – 1311PhosphoserineBy similarity
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei158 – 1581PhosphoserineBy similarity
Modified residuei160 – 1601PhosphoserineBy similarity
Isoform 3 (identifier: Q9R0U0-3)
Modified residuei158 – 1581PhosphoserineCombined sources
Modified residuei160 – 1601PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated. Fully dephosphorylated in mitosis and partially dephosphorylated on heat shock.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9R0U0.
MaxQBiQ9R0U0.
PaxDbiQ9R0U0.
PRIDEiQ9R0U0.

PTM databases

iPTMnetiQ9R0U0.
PhosphoSiteiQ9R0U0.

Expressioni

Tissue specificityi

Widely expressed, with high levels in brain and testis.1 Publication

Gene expression databases

BgeeiQ9R0U0.
CleanExiMM_FUSIP1.
ExpressionAtlasiQ9R0U0. baseline and differential.
GenevisibleiQ9R0U0. MM.

Interactioni

Subunit structurei

The phosphorylated but not the dephosphorylated form interacts with TRA2B/SFRS10. The dephosphorylated form interacts with SNRNP70. Interacts with FUS C-terminus. Interacts with YTHDC1, leading to inhibit RNA-binding activity of SRSF10.By similarity

GO - Molecular functioni

  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi199597. 2 interactions.
IntActiQ9R0U0. 1 interaction.
MINTiMINT-4095399.
STRINGi10090.ENSMUSP00000101479.

Structurei

3D structure databases

ProteinModelPortaliQ9R0U0.
SMRiQ9R0U0. Positions 10-116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 8879RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi106 – 260155Arg/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

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104403.
HOVERGENiHBG107480.
InParanoidiQ9R0U0.
KOiK12900.
OMAiFAYVQYT.
OrthoDBiEOG73BVG8.
TreeFamiTF351864.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R0U0-1) [UniParc]FASTAAdd to basket

Also known as: TASR-1, NSSR1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSRYLRPPNT SLFVRNVADD TRSEDLRREF GRYGPIVDVY VPLDFYTRRP
60 70 80 90 100
RGFAYVQFED VRDAEDALHN LDRKWICGRQ IEIQFAQGDR KTPNQMKAKE
110 120 130 140 150
GRNVYSSSRY DDYDRYRRSR SRSYERRRSR SRSFDYNYRR SYSPRNSRPT
160 170 180 190 200
GRPRRSRSHS DNDRFKHRNR SFSRSKSNSR SRSKSQPKKE MKAKSRSRSA
210 220 230 240 250
SHTKTRGTSK TDSKTHYKSG SRYEKESRKK EPPRSKSQSR SQSRSRSKSR
260
SRSWTSPKSS GH
Length:262
Mass (Da):31,301
Last modified:May 24, 2004 - v2
Checksum:i205F95D36CBBFAB4
GO
Isoform 2 (identifier: Q9R0U0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-147: Missing.

Show »
Length:261
Mass (Da):31,213
Checksum:iA07499B11D4C7570
GO
Isoform 3 (identifier: Q9R0U0-3) [UniParc]FASTAAdd to basket

Also known as: TASR-2, NSSR2

The sequence of this isoform differs from the canonical sequence as follows:
     165-183: FKHRNRSFSRSKSNSRSRS → PNCSWNTQYSSAYYTSRKI
     184-262: Missing.

Show »
Length:183
Mass (Da):22,222
Checksum:i4AA87CAA9B51A131
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221R → Q in AAH37591 (PubMed:15489334).Curated
Sequence conflicti154 – 1541R → T in BAA35092 (PubMed:10583508).Curated
Sequence conflicti154 – 1541R → T in BAA35093 (PubMed:10583508).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei147 – 1471Missing in isoform 2. 1 PublicationVSP_010426
Alternative sequencei165 – 18319FKHRN…SRSRS → PNCSWNTQYSSAYYTSRKI in isoform 3. 2 PublicationsVSP_010427Add
BLAST
Alternative sequencei184 – 26279Missing in isoform 3. 2 PublicationsVSP_010428Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042383 mRNA. Translation: AAC70916.1.
AB015894 mRNA. Translation: BAA35092.1.
AB015895 mRNA. Translation: BAA35093.1.
AF060490 mRNA. Translation: AAC26715.1.
AK014345 mRNA. Translation: BAB29286.1.
AK168524 mRNA. Translation: BAE40403.1.
AK168558 mRNA. Translation: BAE40431.1.
AL672076 Genomic DNA. Translation: CAM15892.1.
AL672076 Genomic DNA. Translation: CAM15893.1.
BC037591 mRNA. Translation: AAH37591.1.
BC043060 mRNA. Translation: AAH43060.1.
BC083082 mRNA. Translation: AAH83082.1.
CCDSiCCDS18791.1. [Q9R0U0-3]
CCDS38922.1. [Q9R0U0-1]
CCDS71493.1. [Q9R0U0-2]
RefSeqiNP_001073856.1. NM_001080387.2. [Q9R0U0-1]
NP_001271124.1. NM_001284195.1. [Q9R0U0-2]
NP_001271125.1. NM_001284196.1.
NP_034308.1. NM_010178.3. [Q9R0U0-3]
UniGeneiMm.10229.
Mm.472035.

Genome annotation databases

EnsembliENSMUST00000097844; ENSMUSP00000095455; ENSMUSG00000028676. [Q9R0U0-2]
ENSMUST00000105853; ENSMUSP00000101479; ENSMUSG00000028676. [Q9R0U0-1]
ENSMUST00000126641; ENSMUSP00000114564; ENSMUSG00000028676. [Q9R0U0-3]
GeneIDi14105.
KEGGimmu:14105.
UCSCiuc008vhd.2. mouse. [Q9R0U0-2]
uc033ifn.1. mouse. [Q9R0U0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042383 mRNA. Translation: AAC70916.1.
AB015894 mRNA. Translation: BAA35092.1.
AB015895 mRNA. Translation: BAA35093.1.
AF060490 mRNA. Translation: AAC26715.1.
AK014345 mRNA. Translation: BAB29286.1.
AK168524 mRNA. Translation: BAE40403.1.
AK168558 mRNA. Translation: BAE40431.1.
AL672076 Genomic DNA. Translation: CAM15892.1.
AL672076 Genomic DNA. Translation: CAM15893.1.
BC037591 mRNA. Translation: AAH37591.1.
BC043060 mRNA. Translation: AAH43060.1.
BC083082 mRNA. Translation: AAH83082.1.
CCDSiCCDS18791.1. [Q9R0U0-3]
CCDS38922.1. [Q9R0U0-1]
CCDS71493.1. [Q9R0U0-2]
RefSeqiNP_001073856.1. NM_001080387.2. [Q9R0U0-1]
NP_001271124.1. NM_001284195.1. [Q9R0U0-2]
NP_001271125.1. NM_001284196.1.
NP_034308.1. NM_010178.3. [Q9R0U0-3]
UniGeneiMm.10229.
Mm.472035.

3D structure databases

ProteinModelPortaliQ9R0U0.
SMRiQ9R0U0. Positions 10-116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199597. 2 interactions.
IntActiQ9R0U0. 1 interaction.
MINTiMINT-4095399.
STRINGi10090.ENSMUSP00000101479.

PTM databases

iPTMnetiQ9R0U0.
PhosphoSiteiQ9R0U0.

Proteomic databases

EPDiQ9R0U0.
MaxQBiQ9R0U0.
PaxDbiQ9R0U0.
PRIDEiQ9R0U0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000097844; ENSMUSP00000095455; ENSMUSG00000028676. [Q9R0U0-2]
ENSMUST00000105853; ENSMUSP00000101479; ENSMUSG00000028676. [Q9R0U0-1]
ENSMUST00000126641; ENSMUSP00000114564; ENSMUSG00000028676. [Q9R0U0-3]
GeneIDi14105.
KEGGimmu:14105.
UCSCiuc008vhd.2. mouse. [Q9R0U0-2]
uc033ifn.1. mouse. [Q9R0U0-1]

Organism-specific databases

CTDi10772.
MGIiMGI:1333805. Srsf10.

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104403.
HOVERGENiHBG107480.
InParanoidiQ9R0U0.
KOiK12900.
OMAiFAYVQYT.
OrthoDBiEOG73BVG8.
TreeFamiTF351864.

Miscellaneous databases

ChiTaRSiSrsf10. mouse.
NextBioi285142.
PROiQ9R0U0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0U0.
CleanExiMM_FUSIP1.
ExpressionAtlasiQ9R0U0. baseline and differential.
GenevisibleiQ9R0U0. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 3).
  2. "Cloning and characterization of two neural-salient serine/arginine-rich (NSSR) proteins involved in the regulation of alternative splicing in neurones."
    Komatsu M., Kominami E., Arahata K., Tsukahara T.
    Genes Cells 4:593-606(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins."
    Yang L., Embree L.J., Hickstein D.D.
    Mol. Cell. Biol. 20:3345-3354(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Amnion and Embryo.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and FVB/N-3.
    Tissue: Brain and Limb.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 AND SER-160 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSRS10_MOUSE
AccessioniPrimary (citable) accession number: Q9R0U0
Secondary accession number(s): B1AV44
, B1AV45, O70307, O88468, Q3TGW7, Q8CFZ1, Q9R0T9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: May 11, 2016
This is version 140 of the entry and version 2 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.