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Q6PDM2

- SRSF1_MOUSE

UniProt

Q6PDM2 - SRSF1_MOUSE

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Protein

Serine/arginine-rich splicing factor 1

Gene
Srsf1, Sfrs1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. mRNA binding Source: MGI
  2. nucleotide binding Source: InterPro
  3. protein binding Source: IntAct
  4. RNA binding Source: UniProtKB
  5. RS domain binding Source: MGI

GO - Biological processi

  1. cardiac muscle contraction Source: MGI
  2. in utero embryonic development Source: MGI
  3. mRNA 5'-splice site recognition Source: UniProtKB
  4. mRNA transport Source: UniProtKB-KW
  5. RNA splicing Source: MGI
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 1
Alternative name(s):
ASF/SF2
Pre-mRNA-splicing factor SRp30a
Splicing factor, arginine/serine-rich 1
Gene namesi
Name:Srsf1
Synonyms:Sfrs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:98283. Srsf1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Nucleus speckle By similarity
Note: Shuttles between the nucleus and the cytoplasm By similarity.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
  3. exon-exon junction complex Source: Ensembl
  4. nuclear speck Source: MGI
  5. nucleoplasm Source: UniProtKB
  6. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 248247Serine/arginine-rich splicing factor 1PRO_0000081912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine Reviewed prediction
Modified residuei2 – 21Phosphoserine By similarity
Modified residuei38 – 381N6-acetyllysine By similarity
Modified residuei93 – 931Asymmetric dimethylarginine By similarity
Modified residuei97 – 971Asymmetric dimethylarginine By similarity
Modified residuei109 – 1091Asymmetric dimethylarginine By similarity
Modified residuei179 – 1791N6-acetyllysine By similarity
Modified residuei199 – 1991Phosphoserine1 Publication
Modified residuei201 – 2011Phosphoserine1 Publication
Modified residuei205 – 2051Phosphoserine By similarity
Modified residuei231 – 2311Phosphoserine By similarity
Modified residuei234 – 2341Phosphoserine By similarity
Modified residuei238 – 2381Phosphoserine By similarity

Post-translational modificationi

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.1 Publication
Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles By similarity.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ6PDM2.
PaxDbiQ6PDM2.
PRIDEiQ6PDM2.

PTM databases

PhosphoSiteiQ6PDM2.

Expressioni

Gene expression databases

ArrayExpressiQ6PDM2.
BgeeiQ6PDM2.
CleanExiMM_SFRS1.
GenevestigatoriQ6PDM2.

Interactioni

Subunit structurei

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. 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) By similarity. Interacts with SRPK1 and a sliding docking interaction is essential for its sequential and processive phosphorylation by SRPK1. Interacts with NXF1 By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
Hexim1Q8R4094EBI-2550360,EBI-6261031
Polr2aP087752EBI-2550360,EBI-2549849
Tial1P703183EBI-2550360,EBI-299820
Traf5P701912EBI-2550360,EBI-523899

Protein-protein interaction databases

BioGridi225922. 8 interactions.
DIPiDIP-48723N.
IntActiQ6PDM2. 10 interactions.
MINTiMINT-1867664.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi122 – 1276
Helixi134 – 1418
Helixi142 – 1443
Beta strandi147 – 1526
Beta strandi156 – 1649
Helixi165 – 17410
Beta strandi175 – 1817
Beta strandi187 – 19610

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4CNMR-A113-207[»]
ProteinModelPortaliQ6PDM2.
SMRiQ6PDM2. Positions 6-102, 116-197.

Miscellaneous databases

EvolutionaryTraceiQ6PDM2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9176RRM 1Add
BLAST
Domaini121 – 19575RRM 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 24750Interacts with SAFB1 By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi94 – 11320Gly-rich (hinge region)Add
BLAST
Compositional biasi198 – 24750Arg/Ser-rich (RS domain)Add
BLAST

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiB2KGJ5.
KOiK12890.
OrthoDBiEOG76X620.
PhylomeDBiQ6PDM2.
TreeFamiTF106261.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR029538. SRSF1.
[Graphical view]
PANTHERiPTHR10548:SF87. PTHR10548:SF87. 1 hit.
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6PDM2-1) [UniParc]FASTAAdd to Basket

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

MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR    50
RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG 100
GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA 150
DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP 200
SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRT 248
Length:248
Mass (Da):27,745
Last modified:January 23, 2007 - v3
Checksum:iC28A0B2F112EA713
GO
Isoform 2 (identifier: Q6PDM2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-203: GETAYIRVKVDGPRSPSYG → VGYTLILFFGQNWIQFS
     204-248: Missing.

Note: May be due to intron retention.

Show »
Length:201
Mass (Da):22,320
Checksum:i16B6D495BD77613F
GO
Isoform 3 (identifier: Q6PDM2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-199: GETAYIRVKVDGPRS → TYLKRWIKNALD
     200-248: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:196
Mass (Da):21,807
Checksum:i6723D202662FF71D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei185 – 20319GETAY…SPSYG → VGYTLILFFGQNWIQFS in isoform 2. VSP_013770Add
BLAST
Alternative sequencei185 – 19915GETAY…DGPRS → TYLKRWIKNALD in isoform 3. VSP_013771Add
BLAST
Alternative sequencei200 – 24849Missing in isoform 3. VSP_013772Add
BLAST
Alternative sequencei204 – 24845Missing in isoform 2. VSP_013773Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191S → A in BAC25546. 1 Publication
Sequence conflicti162 – 1643FVR → CVP in BAC25546. 1 Publication
Sequence conflicti185 – 1851G → W in BAC25546. 1 Publication
Sequence conflicti191 – 1966RVKVDG → PRIVDR in BAC25546. 1 Publication
Sequence conflicti209 – 2102SR → VC in BAC25546. 1 Publication
Sequence conflicti226 – 2283YSP → DSR in BAC25546. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK018176 mRNA. Translation: BAC25546.1.
AK078715 mRNA. Translation: BAC37367.1.
AK150535 mRNA. Translation: BAE29641.1.
AL593853 Genomic DNA. Translation: CAI24416.1.
CU406964 Genomic DNA. Translation: CAQ51705.1.
BC046773 mRNA. Translation: AAH46773.1.
BC058627 mRNA. Translation: AAH58627.1.
CCDSiCCDS36273.1. [Q6PDM2-1]
CCDS36274.1. [Q6PDM2-2]
PIRiS26404.
RefSeqiNP_001071635.1. NM_001078167.2. [Q6PDM2-2]
NP_775550.2. NM_173374.4. [Q6PDM2-1]
XP_006543028.1. XM_006542965.1. [Q6PDM2-1]
UniGeneiMm.391719.

Genome annotation databases

EnsembliENSMUST00000079866; ENSMUSP00000133517; ENSMUSG00000018379. [Q6PDM2-2]
ENSMUST00000139129; ENSMUSP00000120595; ENSMUSG00000018379. [Q6PDM2-1]
GeneIDi102641923.
110809.
KEGGimmu:102641923.
mmu:110809.
UCSCiuc007kvc.1. mouse. [Q6PDM2-1]
uc007kvd.1. mouse. [Q6PDM2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK018176 mRNA. Translation: BAC25546.1 .
AK078715 mRNA. Translation: BAC37367.1 .
AK150535 mRNA. Translation: BAE29641.1 .
AL593853 Genomic DNA. Translation: CAI24416.1 .
CU406964 Genomic DNA. Translation: CAQ51705.1 .
BC046773 mRNA. Translation: AAH46773.1 .
BC058627 mRNA. Translation: AAH58627.1 .
CCDSi CCDS36273.1. [Q6PDM2-1 ]
CCDS36274.1. [Q6PDM2-2 ]
PIRi S26404.
RefSeqi NP_001071635.1. NM_001078167.2. [Q6PDM2-2 ]
NP_775550.2. NM_173374.4. [Q6PDM2-1 ]
XP_006543028.1. XM_006542965.1. [Q6PDM2-1 ]
UniGenei Mm.391719.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X4C NMR - A 113-207 [» ]
ProteinModelPortali Q6PDM2.
SMRi Q6PDM2. Positions 6-102, 116-197.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 225922. 8 interactions.
DIPi DIP-48723N.
IntActi Q6PDM2. 10 interactions.
MINTi MINT-1867664.

PTM databases

PhosphoSitei Q6PDM2.

Proteomic databases

MaxQBi Q6PDM2.
PaxDbi Q6PDM2.
PRIDEi Q6PDM2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000079866 ; ENSMUSP00000133517 ; ENSMUSG00000018379 . [Q6PDM2-2 ]
ENSMUST00000139129 ; ENSMUSP00000120595 ; ENSMUSG00000018379 . [Q6PDM2-1 ]
GeneIDi 102641923.
110809.
KEGGi mmu:102641923.
mmu:110809.
UCSCi uc007kvc.1. mouse. [Q6PDM2-1 ]
uc007kvd.1. mouse. [Q6PDM2-2 ]

Organism-specific databases

CTDi 6426.
MGIi MGI:98283. Srsf1.

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00700000104103.
HOVERGENi HBG002295.
InParanoidi B2KGJ5.
KOi K12890.
OrthoDBi EOG76X620.
PhylomeDBi Q6PDM2.
TreeFami TF106261.

Miscellaneous databases

EvolutionaryTracei Q6PDM2.
NextBioi 364697.
PROi Q6PDM2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6PDM2.
Bgeei Q6PDM2.
CleanExi MM_SFRS1.
Genevestigatori Q6PDM2.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR029538. SRSF1.
[Graphical view ]
PANTHERi PTHR10548:SF87. PTHR10548:SF87. 1 hit.
Pfami PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Bone marrow macrophage, Eye and Medulla oblongata.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Embryonic brain.
  4. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 18-28.
    Tissue: Brain.
  5. "Characterization and comparison of four serine- and arginine-rich (SR) protein kinases."
    Nayler O., Stamm S., Ullrich A.
    Biochem. J. 326:693-700(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CLK1; CLK2; CLK3 AND CLK4.
  6. "ASF/SF2-regulated CaMKIIdelta alternative splicing temporally reprograms excitation-contraction coupling in cardiac muscle."
    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.
    Cell 120:59-72(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. "Solution structure of RRM domain in splicing factor 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 113-207.

Entry informationi

Entry nameiSRSF1_MOUSE
AccessioniPrimary (citable) accession number: Q6PDM2
Secondary accession number(s): B2KGJ5
, Q3UCH2, Q5SXC5, Q8BJV3, Q8C1H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi