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Serine/arginine-rich splicing factor 1 (ASF/SF2) (Pre-mRNA-splicing factor SRp30a) (Splicing factor, arginine/serine-rich 1)

 SRSF1_MOUSE             Reviewed;         248 AA.
Q6PDM2; B2KGJ5; Q3UCH2; Q5SXC5; Q8BJV3; Q8C1H9;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
02-JUN-2021, entry version 175.
RecName: Full=Serine/arginine-rich splicing factor 1;
AltName: Full=ASF/SF2;
AltName: Full=Pre-mRNA-splicing factor SRp30a;
AltName: Full=Splicing factor, arginine/serine-rich 1;
Name=Srsf1; Synonyms=Sfrs1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, Eye, and Medulla oblongata;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryonic brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 18-28.
TISSUE=Brain;
Lubec G., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[5]
PHOSPHORYLATION BY CLK1; CLK2; CLK3 AND CLK4.
PubMed=9307018; DOI=10.1042/bj3260693;
Nayler O., Stamm S., Ullrich A.;
"Characterization and comparison of four serine- and arginine-rich (SR)
protein kinases.";
Biochem. J. 326:693-700(1997).
[6]
FUNCTION.
PubMed=15652482; DOI=10.1016/j.cell.2004.11.036;
Xu X., Yang D., Ding J.-H., Wang W., Chu P.-H., Dalton N.D., Wang H.-Y.,
Bermingham J.R. Jr., Ye Z., Liu F., Rosenfeld M.G., Manley J.L.,
Ross J. Jr., Chen J., Xiao R.-P., Cheng H., Fu X.-D.;
"ASF/SF2-regulated CaMKIIdelta alternative splicing temporally reprograms
excitation-contraction coupling in cardiac muscle.";
Cell 120:59-72(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-201, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of electron
capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[9]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-93; ARG-97 AND ARG-109, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[10]
STRUCTURE BY NMR OF 113-207.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RRM domain in splicing factor 2.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Plays a role in preventing exon skipping, ensuring the
accuracy of splicing and regulating alternative splicing. Interacts
with other spliceosomal components, via the RS domains, to form a
bridge between the 5'- and 3'-splice site binding components, U1 snRNP
and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-
containing pre-mRNA. Binds to purine-rich RNA sequences, either the
octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers,
AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif
in vitro. Three copies of the octamer constitute a powerful splicing
enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can
specifically activate ASE-dependent splicing (By similarity).
Specifically regulates alternative splicing of cardiac isoforms of
CAMK2D, LDB3/CYPHER and TNNT2/CTNT during heart remodeling at the
juvenile to adult transition. The inappropriate accumulation of a
neonatal and neuronal isoform of CAMKD2 in the adult heart results in
aberrant calcium handling and defective excitation-contraction coupling
in cardiomyocytes. May function as export adapter involved in mRNA
nuclear export through the TAP/NXF1 pathway (PubMed:15652482).
{ECO:0000250|UniProtKB:Q07955, ECO:0000269|PubMed:15652482}.
-!- SUBUNIT: Consists of two polypeptides of p32 and p33. In vitro, self-
associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds
SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF.
Interacts with SRPK1. Identified in the spliceosome C complex.
Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with
ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus). Interacts with
SRPK1 and a sliding docking interaction is essential for its sequential
and processive phosphorylation by SRPK1. Interacts with NXF1. Interacts
with CCNL1, CCNL2 and CDK11B. Interacts with RRP1B. Interacts (when
phosphorylated in its RS domain) with TNPO3; promoting nuclear import.
{ECO:0000250|UniProtKB:Q07955}.
-!- INTERACTION:
Q6PDM2; Q8R409: Hexim1; NbExp=4; IntAct=EBI-2550360, EBI-6261031;
Q6PDM2; P08775: Polr2a; NbExp=2; IntAct=EBI-2550360, EBI-2549849;
Q6PDM2; P70318: Tial1; NbExp=3; IntAct=EBI-2550360, EBI-299820;
Q6PDM2; P70191: Traf5; NbExp=2; IntAct=EBI-2550360, EBI-523899;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07955}. Nucleus
speckle {ECO:0000250|UniProtKB:Q07955}. Note=In nuclear speckles.
Shuttles between the nucleus and the cytoplasm. Nuclear import is
mediated via interaction with TNPO3. {ECO:0000250|UniProtKB:Q07955}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6PDM2-1; Sequence=Displayed;
Name=2;
IsoId=Q6PDM2-2; Sequence=VSP_013770, VSP_013773;
Name=3;
IsoId=Q6PDM2-3; Sequence=VSP_013771, VSP_013772;
-!- DOMAIN: The RRM 2 domain plays an important role in governing both the
binding mode and the phosphorylation mechanism of the RS domain by
SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly
directional (C-terminus to N-terminus) phosphorylation reaction in
which the RS domain slides through an extended electronegative channel
separating the docking groove of SRPK1 and the active site. RRM 2 binds
toward the periphery of the active site and guides the directional
phosphorylation mechanism. Both the RS domain and an RRM domain are
required for nucleocytoplasmic shuttling (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by
SRPK1 at multiple serines in its RS domain via a directional (C-
terminal to N-terminal) and a dual-track mechanism incorporating both
processive phosphorylation (in which the kinase stays attached to the
substrate after each round of phosphorylation) and distributive
phosphorylation steps (in which the kinase and substrate dissociate
after each phosphorylation event). The RS domain of SRSF1 binds to a
docking groove in the large lobe of the kinase domain of SRPK1 and this
induces certain structural changes in SRPK1 and/or RRM 2 domain of
SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation.
The cycles continue for several phosphorylation steps in a processive
manner (steps 1-8) until the last few phosphorylation steps
(approximately steps 9-12). During that time, a mechanical stress
induces the unfolding of the beta-4 motif in RRM 2, which then docks at
the docking groove of SRPK1. This also signals RRM 2 to begin to
dissociate, which facilitates SRSF1 dissociation after phosphorylation
is completed (By similarity). {ECO:0000250}.
-!- PTM: Asymmetrically dimethylated at arginines, probably by PRMT1,
methylation promotes localization to nuclear speckles. {ECO:0000250}.
-!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
{ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
premature stop codon in the mRNA, leading to nonsense-mediated mRNA
decay. {ECO:0000305}.
-!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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EMBL; AK018176; BAC25546.1; -; mRNA.
EMBL; AK078715; BAC37367.1; -; mRNA.
EMBL; AK150535; BAE29641.1; -; mRNA.
EMBL; AL593853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CU406964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC046773; AAH46773.1; -; mRNA.
EMBL; BC058627; AAH58627.1; -; mRNA.
CCDS; CCDS36273.1; -. [Q6PDM2-1]
CCDS; CCDS36274.1; -. [Q6PDM2-2]
PIR; S26404; S26404.
RefSeq; NP_001071635.1; NM_001078167.2. [Q6PDM2-2]
RefSeq; NP_775550.2; NM_173374.4. [Q6PDM2-1]
PDB; 1X4C; NMR; -; A=113-207.
PDBsum; 1X4C; -.
SMR; Q6PDM2; -.
BioGRID; 225922; 101.
DIP; DIP-48723N; -.
IntAct; Q6PDM2; 82.
MINT; Q6PDM2; -.
STRING; 10090.ENSMUSP00000120595; -.
iPTMnet; Q6PDM2; -.
PhosphoSitePlus; Q6PDM2; -.
SwissPalm; Q6PDM2; -.
EPD; Q6PDM2; -.
jPOST; Q6PDM2; -.
PaxDb; Q6PDM2; -.
PeptideAtlas; Q6PDM2; -.
PRIDE; Q6PDM2; -.
ProteomicsDB; 257410; -. [Q6PDM2-1]
ProteomicsDB; 257411; -. [Q6PDM2-2]
ProteomicsDB; 257412; -. [Q6PDM2-3]
TopDownProteomics; Q6PDM2-1; -. [Q6PDM2-1]
DNASU; 110809; -.
Ensembl; ENSMUST00000079866; ENSMUSP00000133517; ENSMUSG00000018379. [Q6PDM2-2]
Ensembl; ENSMUST00000139129; ENSMUSP00000120595; ENSMUSG00000018379. [Q6PDM2-1]
GeneID; 110809; -.
KEGG; mmu:110809; -.
UCSC; uc007kvc.2; mouse. [Q6PDM2-1]
UCSC; uc007kvd.2; mouse. [Q6PDM2-2]
CTD; 6426; -.
MGI; MGI:98283; Srsf1.
eggNOG; KOG0105; Eukaryota.
GeneTree; ENSGT00940000155585; -.
HOGENOM; CLU_012062_34_0_1; -.
InParanoid; Q6PDM2; -.
OMA; VDCRVMT; -.
OrthoDB; 1321443at2759; -.
PhylomeDB; Q6PDM2; -.
TreeFam; TF106261; -.
Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
Reactome; R-MMU-72187; mRNA 3'-end processing.
Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
BioGRID-ORCS; 110809; 23 hits in 53 CRISPR screens.
ChiTaRS; Srsf1; mouse.
EvolutionaryTrace; Q6PDM2; -.
PRO; PR:Q6PDM2; -.
Proteomes; UP000000589; Chromosome 11.
RNAct; Q6PDM2; protein.
Bgee; ENSMUSG00000018379; Expressed in telencephalon and 313 other tissues.
ExpressionAtlas; Q6PDM2; baseline and differential.
Genevisible; Q6PDM2; MM.
GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0044547; F:DNA topoisomerase binding; ISO:MGI.
GO; GO:0003729; F:mRNA binding; IMP:MGI.
GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0050733; F:RS domain binding; IPI:MGI.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:MGI.
GO; GO:0060048; P:cardiac muscle contraction; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IDA:MGI.
GO; GO:0000395; P:mRNA 5'-splice site recognition; ISS:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
GO; GO:0048255; P:mRNA stabilization; IDA:MGI.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0033120; P:positive regulation of RNA splicing; ISO:MGI.
GO; GO:0008380; P:RNA splicing; IDA:MGI.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
CDD; cd12597; RRM1_SRSF1; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034520; SRSF1_RRM1.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Methylation; mRNA processing;
mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
Repeat; RNA-binding; Spliceosome; Transport; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:Q07955"
CHAIN 2..248
/note="Serine/arginine-rich splicing factor 1"
/id="PRO_0000081912"
DOMAIN 16..91
/note="RRM 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
DOMAIN 121..195
/note="RRM 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
REGION 88..134
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 191..248
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 198..247
/note="Interaction with SAFB1"
/evidence="ECO:0000250"
COMPBIAS 205..225
/note="Basic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 234..248
/note="Basic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:Q07955, ECO:0000255"
MOD_RES 2
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 38
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 93
/note="Asymmetric dimethylarginine; alternate"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 93
/note="Omega-N-methylarginine; alternate"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 97
/note="Asymmetric dimethylarginine; alternate"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 97
/note="Omega-N-methylarginine; alternate"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 109
/note="Asymmetric dimethylarginine; alternate"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 109
/note="Omega-N-methylarginine; alternate"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 111
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 133
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 179
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 199
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19131326"
MOD_RES 201
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19131326"
MOD_RES 202
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 205
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 207
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 209
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 231
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 234
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q07955"
MOD_RES 238
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q07955"
CROSSLNK 30
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:Q07955"
CROSSLNK 38
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:Q07955"
VAR_SEQ 185..203
/note="GETAYIRVKVDGPRSPSYG -> VGYTLILFFGQNWIQFS (in isoform
2)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_013770"
VAR_SEQ 185..199
/note="GETAYIRVKVDGPRS -> TYLKRWIKNALD (in isoform 3)"
/evidence="ECO:0000305"
/id="VSP_013771"
VAR_SEQ 200..248
/note="Missing (in isoform 3)"
/evidence="ECO:0000305"
/id="VSP_013772"
VAR_SEQ 204..248
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_013773"
CONFLICT 119
/note="S -> A (in Ref. 1; BAC25546)"
/evidence="ECO:0000305"
CONFLICT 162..164
/note="FVR -> CVP (in Ref. 1; BAC25546)"
/evidence="ECO:0000305"
CONFLICT 185
/note="G -> W (in Ref. 1; BAC25546)"
/evidence="ECO:0000305"
CONFLICT 191..196
/note="RVKVDG -> PRIVDR (in Ref. 1; BAC25546)"
/evidence="ECO:0000305"
CONFLICT 209..210
/note="SR -> VC (in Ref. 1; BAC25546)"
/evidence="ECO:0000305"
CONFLICT 226..228
/note="YSP -> DSR (in Ref. 1; BAC25546)"
/evidence="ECO:0000305"
STRAND 122..127
/evidence="ECO:0007829|PDB:1X4C"
HELIX 134..141
/evidence="ECO:0007829|PDB:1X4C"
HELIX 142..144
/evidence="ECO:0007829|PDB:1X4C"
STRAND 147..152
/evidence="ECO:0007829|PDB:1X4C"
STRAND 156..164
/evidence="ECO:0007829|PDB:1X4C"
HELIX 165..174
/evidence="ECO:0007829|PDB:1X4C"
STRAND 175..181
/evidence="ECO:0007829|PDB:1X4C"
STRAND 187..196
/evidence="ECO:0007829|PDB:1X4C"
SEQUENCE 248 AA; 27745 MW; C28A0B2F112EA713 CRC64;
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE
FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE
NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF
RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR
HSRSRSRT


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Catalog number Product name Quantity
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PR-775 ASF per SF2 (SFRS1 or SRp30a)His Splicing Factor, Arginine per Serine-rich 1, Pre-mRNA Splicing Factor human, recombinant, Sf9 insect cells 5
EIAAB38025 Homo sapiens,Human,SCAF,SCAF1,Serine arginine-rich pre-mRNA splicing factor SR-A1,SFRS19,Splicing factor, arginine_serine-rich 19,SRA1,SR-A1,SR-related and CTD-associated factor 1,SR-related-CTD-assoc
EIAAB39954 40 kDa SR-repressor protein,FUS-interacting serine-arginine-rich protein 1,FUSIP1,FUSIP2,Homo sapiens,Human,Serine_arginine-rich splicing factor 10,SFRS13A,Splicing factor SRp38,Splicing factor, argin
EIAAB39961 ASF_SF2,Mouse,Mus musculus,Pre-mRNA-splicing factor SRp30a,Serine_arginine-rich splicing factor 1,Sfrs1,Splicing factor, arginine_serine-rich 1,Srsf1
EIAAB39962 Alternative-splicing factor 1,ASF,ASF-1,Homo sapiens,Human,OK_SW-cl.3,pre-mRNA-splicing factor SF2, P33 subunit,Serine_arginine-rich splicing factor 1,SF2,SF2P33,SFRS1,Splicing factor, arginine_serine
EIAAB39955 Arginine-rich 54 kDa nuclear protein,Homo sapiens,Human,p54,Serine_arginine-rich splicing factor 11,SFRS11,Splicing factor, arginine_serine-rich 11,SRSF11
EIAAB39976 Delayed-early protein HRS,Hrs,Mouse,Mus musculus,Pre-mRNA-splicing factor SRP40,Serine_arginine-rich splicing factor 5,Sfrs5,Splicing factor, arginine_serine-rich 5,Srsf5
EIAAB39983 Homo sapiens,Human,Pre-mRNA-splicing factor SRP46,Serine_arginine-rich splicing factor 8,SFRS2B,Splicing factor SRp46,Splicing factor, arginine_serine-rich 2B,SRP46,SRSF8
EIAAB39967 Homo sapiens,Human,Protein PR264,SC-35,Serine_arginine-rich splicing factor 2,SFRS2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,SRSF2
EH1318 Serine per arginine-rich splicing factor 2 Elisa Kit 96T
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RPR-352 Recombinant Human Serine arginine-Rich Splicing Factor 1 5
EH2379 Serine per arginine-rich splicing factor 1 Elisa Kit 96T
E1850h Rat ELISA Kit FOR Serine per arginine-rich splicing factor 5 96T
EIAAB39968 Bos taurus,Bovine,SC-35,Serine_arginine-rich splicing factor 2,SFRS2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,SRSF2
EIAAB39965 Rat,Rattus norvegicus,SC-35,Serine_arginine-rich splicing factor 2,Sfrs2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,Srsf2
EIAAB39975 Delayed-early protein HRS,Homo sapiens,HRS,Human,Pre-mRNA-splicing factor SRP40,Serine_arginine-rich splicing factor 5,SFRS5,Splicing factor, arginine_serine-rich 5,SRP40,SRSF5
EIAAB39973 Homo sapiens,Human,Pre-mRNA-splicing factor SRP75,Serine_arginine-rich splicing factor 4,SFRS4,Splicing factor, arginine_serine-rich 4,SRP001LB,SRP75,SRSF4
EIAAB39963 Pig,SC-35,Serine_arginine-rich splicing factor 2,SFRS2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,SRSF2,Sus scrofa
E0321c Mouse ELISA Kit FOR Serine per arginine-rich splicing factor 4 96T
E0485h Human ELISA Kit FOR Serine per arginine-rich splicing factor 9 96T
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K1737_HUMAN Mouse ELISA Kit FOR Serine per arginine-rich splicing factor 4 96T
E1213r Human ELISA Kit FOR Serine per arginine-rich splicing factor 8 96T
Pathways :
WP1983: Splicing factor NOVA regulated synpatic proteins
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP2148: Brain derived neurotrophic factor
WP272: Blood Clotting Cascade
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP2155: arginine biosynthesis
WP1621: Arginine and proline metabolism
WP2199: Seed Development
WP275: Arginine Biosynthesis
WP390: Serine-isocitrate lyase pathway
WP459: Serine Biosynthesis
WP54: Arginine degradation
WP2185: Purine metabolism
WP1659: Glycine, serine and threonine metabolism
WP218: Serine and Glycine biosynthesis

Related Genes :
[Srsf1 Sfrs1] Serine/arginine-rich splicing factor 1 (ASF/SF2) (Pre-mRNA-splicing factor SRp30a) (Splicing factor, arginine/serine-rich 1)
[SRSF1 ASF SF2 SF2P33 SFRS1 OK/SW-cl.3] Serine/arginine-rich splicing factor 1 (Alternative-splicing factor 1) (ASF-1) (Splicing factor, arginine/serine-rich 1) (pre-mRNA-splicing factor SF2, P33 subunit)
[SR30 SRP30 At1g09140 T12M4.19] Serine/arginine-rich splicing factor SR30 (At-SR30) (At-SRp30) (AtSR30) (SF2/ASF-like splicing modulator Srp30) (Serine-arginine rich RNA binding protein 30)
[SRSF9 SFRS9 SRP30C] Serine/arginine-rich splicing factor 9 (Pre-mRNA-splicing factor SRp30C) (Splicing factor, arginine/serine-rich 9)
[SRSF2 SFRS2] Serine/arginine-rich splicing factor 2 (Protein PR264) (Splicing component, 35 kDa) (Splicing factor SC35) (SC-35) (Splicing factor, arginine/serine-rich 2)
[SCL33 SR33 At1g55310 F7A10.15] Serine/arginine-rich SC35-like splicing factor SCL33 (At-SCL33) (AtSCL33) (SC35-like splicing factor 33) (Serine/arginine-rich splicing factor 33)
[SRSF7 SFRS7] Serine/arginine-rich splicing factor 7 (Splicing factor 9G8) (Splicing factor, arginine/serine-rich 7)
[SR45 RNPS1 At1g16610 F19K19.9] Serine/arginine-rich splicing factor SR45 (At-SR45) (AtSR45) (Serine/arginine-rich ribonucleoprotein 1)
[Srsf7 Sfrs7] Serine/arginine-rich splicing factor 7 (Splicing factor, arginine/serine-rich 7)
[SR45A TRA2 At1g07350 F22G5.31] Serine/arginine-rich splicing factor SR45a (At-SR45A) (AtSR45a) (Protein TRANSFORMER2-like) (atTra2)
[Clasrp Clasp Sfrs16 Srsf16 Swap2] CLK4-associating serine/arginine rich protein (Clk4-associating SR-related protein) (Serine/arginine-rich splicing factor 16) (Splicing factor, arginine/serine-rich 16) (Suppressor of white-apricot homolog 2)
[RS31 RSP31 At3g61860 F21F14.30] Serine/arginine-rich splicing factor RS31 (At-RSp31) (AtRS31)
[TRA2B SFRS10] Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (hTRA2-beta) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B)
[RS2Z33 RSZ33 At2g37340 F3G5.13] Serine/arginine-rich splicing factor RS2Z33 (RS-containing zinc finger protein 33) (At-RS2Z33) (At-RSZ33) (AtRSZ33)
[Tra2b Sfrs10] Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (RA301) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B)
[Tra2b Sfrs10 Silg41] Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (Silica-induced gene 41 protein) (SIG-41) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B)
[CLASRP SFRS16 SWAP2 UNQ2428/PRO4988] CLK4-associating serine/arginine rich protein (Splicing factor, arginine/serine-rich 16) (Suppressor of white-apricot homolog 2)
[SRPK1] SRSF protein kinase 1 (EC 2.7.11.1) (SFRS protein kinase 1) (Serine/arginine-rich protein-specific kinase 1) (SR-protein-specific kinase 1)
[SRSF1 SFRS1] Serine/arginine-rich splicing factor 1 (Splicing factor, arginine/serine-rich 1)
[SRSF1 SFRS1] Serine/arginine-rich splicing factor 1 (Splicing factor, arginine/serine-rich 1)
[rsp-2 srp-4 W02B12.2] Probable splicing factor, arginine/serine-rich 2 (CeSRp40) (RNA-binding protein srp-4)
[RBM23 RNPC4 PP239] Probable RNA-binding protein 23 (CAPER beta) (CAPERbeta) (RNA-binding motif protein 23) (RNA-binding region-containing protein 4) (Splicing factor SF2)
[SRSF7 SFRS7] Serine/arginine-rich splicing factor 7 (Splicing factor, arginine/serine-rich 7)
[fand fas CG6197] Pre-mRNA-splicing factor syf1 homolog (Pre-mRNA-splicing factor fandango) (Protein faint sausage)
[SRSF1 SFRS1] Serine/arginine-rich splicing factor 1 (Splicing factor, arginine/serine-rich 1)
[SRSF2 SFRS2] Serine/arginine-rich splicing factor 2 (Splicing component, 35 kDa) (Splicing factor SC35) (SC-35) (Splicing factor, arginine/serine-rich 2)
[rsp-6 srp-1 C33H5.12] Probable splicing factor, arginine/serine-rich 6 (CeSRp20) (RNA-binding protein srp-1)
[SRSF2 SFRS2] Serine/arginine-rich splicing factor 2 (Splicing component, 35 kDa) (Splicing factor SC35) (SC-35) (Splicing factor, arginine/serine-rich 2)
[CWC2 NTC40 SLC3 YDL209C D1041] Pre-mRNA-splicing factor CWC2 (Complexed with CEF1 protein 2) (PRP19-associated complex protein 40) (Synthetic lethal with CLF1 protein 3)
[rsp-3 Y111B2A.18] Probable splicing factor, arginine/serine-rich 3 (CeSF2) (CeSF2/ASF)

Bibliography :