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Q07955

- SRSF1_HUMAN

UniProt

Q07955 - SRSF1_HUMAN

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Protein

Serine/arginine-rich splicing factor 1

Gene

SRSF1

Organism
Homo sapiens (Human)
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. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. 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. poly(A) RNA binding Source: UniProtKB
  4. RNA binding Source: UniProtKB

GO - Biological processi

  1. cardiac muscle contraction Source: Ensembl
  2. gene expression Source: Reactome
  3. in utero embryonic development Source: Ensembl
  4. mRNA 3'-end processing Source: Reactome
  5. mRNA 5'-splice site recognition Source: UniProtKB
  6. mRNA export from nucleus Source: Reactome
  7. mRNA processing Source: ProtInc
  8. mRNA splice site selection Source: ProtInc
  9. mRNA splicing, via spliceosome Source: UniProtKB
  10. regulation of mRNA splicing, via spliceosome Source: InterPro
  11. regulation of mRNA stability Source: InterPro
  12. regulation of transcription, DNA-templated Source: InterPro
  13. regulation of translation Source: InterPro
  14. RNA splicing Source: Reactome
  15. termination of RNA polymerase II transcription Source: Reactome
  16. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 1
Alternative name(s):
Alternative-splicing factor 1
Short name:
ASF-1
Splicing factor, arginine/serine-rich 1
pre-mRNA-splicing factor SF2, P33 subunit
Gene namesi
Name:SRSF1
Synonyms:ASF, SF2, SF2P33, SFRS1
ORF Names:OK/SW-cl.3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:10780. SRSF1.

Subcellular locationi

Cytoplasm. Nucleus speckle
Note: In nuclear speckles. Shuttles between the nucleus and the cytoplasm.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProt
  4. nuclear speck Source: MGI
  5. nucleoplasm Source: UniProtKB
  6. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 592FV → SR in FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding. 1 Publication
Mutagenesisi93 – 931R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-97 and Ala-109. 1 Publication
Mutagenesisi97 – 971R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-109. 1 Publication
Mutagenesisi109 – 1091R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-97. 1 Publication
Mutagenesisi162 – 1632FV → SR in FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding. 1 Publication
Mutagenesisi162 – 1621F → A in AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding. 1 Publication
Mutagenesisi162 – 1621F → D: Reduced nucleocytoplasmic shuttling; when associated with D-190. 1 Publication
Mutagenesisi180 – 1801F → D: Reduced nucleocytoplasmic shuttling; when associated with D-162. 1 Publication
Mutagenesisi182 – 24867Missing in MR-B; strongly inhibits splicing. 1 PublicationAdd
BLAST
Mutagenesisi182 – 19918Missing in MR-E; loss of ability to activate splicing. 1 PublicationAdd
BLAST
Mutagenesisi192 – 24857Missing in MR-A; loss of ability to activate splicing. 1 PublicationAdd
BLAST
Mutagenesisi192 – 1998Missing in MR-D; loss of ability to activate splicing. 1 Publication
Mutagenesisi199 – 22426Missing in RS-A; loss of ability to activate splicing but retains splice site switching. 1 PublicationAdd
BLAST
Mutagenesisi215 – 24834Missing in RS-C; loss of ability to activate splicing but retains splice site switching. 1 PublicationAdd
BLAST
Mutagenesisi226 – 24823Missing in RS-B; retains both splice activation and splice site switching activity. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA35696.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 248247Serine/arginine-rich splicing factor 1PRO_0000081911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei38 – 381N6-acetyllysine1 Publication
Modified residuei93 – 931Asymmetric dimethylarginine1 Publication
Modified residuei97 – 971Asymmetric dimethylarginine1 Publication
Modified residuei109 – 1091Asymmetric dimethylarginine1 Publication
Modified residuei179 – 1791N6-acetyllysine1 Publication
Modified residuei199 – 1991Phosphoserine3 Publications
Modified residuei201 – 2011PhosphoserineBy similarity
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei231 – 2311Phosphoserine1 Publication
Modified residuei234 – 2341Phosphoserine1 Publication
Modified residuei238 – 2381Phosphoserine1 Publication

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ07955.
PaxDbiQ07955.
PeptideAtlasiQ07955.
PRIDEiQ07955.

PTM databases

PhosphoSiteiQ07955.

Miscellaneous databases

PMAP-CutDBQ07955.

Expressioni

Gene expression databases

BgeeiQ07955.
CleanExiHS_SFRS1.
ExpressionAtlasiQ07955. baseline and differential.
GenevestigatoriQ07955.

Organism-specific databases

HPAiCAB013073.

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. 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 NXF1.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CIR1Q86X953EBI-398920,EBI-627102
NFYAP235115EBI-398920,EBI-389739
NXF1Q9UBU95EBI-398920,EBI-398874
SRPK1Q96SB43EBI-398920,EBI-539478
Srpk1O705515EBI-398920,EBI-593343From a different organism.
Srpk2O547813EBI-398920,EBI-593325From a different organism.
TRAF5O004632EBI-398920,EBI-523498

Protein-protein interaction databases

BioGridi112324. 145 interactions.
DIPiDIP-2155N.
IntActiQ07955. 49 interactions.
MINTiMINT-5000565.
STRINGi9606.ENSP00000258962.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 228
Helixi29 – 368
Helixi37 – 393
Beta strandi42 – 476
Beta strandi50 – 545
Beta strandi57 – 626
Helixi64 – 7411
Beta strandi85 – 873
Beta strandi110 – 1134
Beta strandi122 – 1276
Helixi134 – 1418
Helixi142 – 1443
Beta strandi147 – 1526
Beta strandi158 – 1647
Helixi165 – 17410
Turni175 – 1773
Beta strandi179 – 1813
Beta strandi183 – 1853
Beta strandi187 – 1893
Beta strandi191 – 1977
Beta strandi202 – 2043
Beta strandi206 – 2083

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4ANMR-A1-96[»]
2M7SNMR-A106-195[»]
2M8DNMR-B107-196[»]
2O3DNMR-A107-215[»]
3BEGX-ray2.90B105-219[»]
4C0OX-ray2.56C/D106-230[»]
ProteinModelPortaliQ07955.
SMRiQ07955. Positions 6-102, 116-197.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07955.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9176RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini121 – 19575RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 24750Interacts with SAFB1Add
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.1 Publication

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ07955.
KOiK12890.
OrthoDBiEOG76X620.
PhylomeDBiQ07955.
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 ASF-1 (identifier: Q07955-1) [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

        10         20         30         40         50
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR
60 70 80 90 100
RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG
110 120 130 140 150
GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA
160 170 180 190 200
DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP
210 220 230 240
SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRT
Length:248
Mass (Da):27,745
Last modified:January 23, 2007 - v2
Checksum:iC28A0B2F112EA713
GO
Isoform ASF-2 (identifier: Q07955-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-248: GETAYIRVKV...PRHSRSRSRT → FCLSNREKLP...NCFVQNGLKC

Show »
Length:292
Mass (Da):31,999
Checksum:iC9502AC70F373EAC
GO
Isoform ASF-3 (identifier: Q07955-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-201: GETAYIRVKVDGPRSPS → VGYTRILFFDQNWIQWS
     202-248: Missing.

Note: May be due to intron retention.

Show »
Length:201
Mass (Da):22,460
Checksum:iB9AC6495A491613D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891P → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_035488

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei185 – 24864GETAY…SRSRT → FCLSNREKLPTSGLKLMGPE VQVMEDLDLEAVVVAEAVAE ATAGVAVTPQGEAEDHHAIL PVIADLALVHKMIGDTFCRT HVVYSFPLFSTIFSFFNSNC FVQNGLKC in isoform ASF-2. 1 PublicationVSP_005856Add
BLAST
Alternative sequencei185 – 20117GETAY…PRSPS → VGYTRILFFDQNWIQWS in isoform ASF-3. 1 PublicationVSP_005857Add
BLAST
Alternative sequencei202 – 24847Missing in isoform ASF-3. 1 PublicationVSP_005858Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M72709 mRNA. Translation: AAA35565.1.
M72709 mRNA. Translation: AAA35564.1.
M69040 mRNA. Translation: AAA03476.1.
AB062124 mRNA. Translation: BAB93456.1.
AK312781 mRNA. Translation: BAG35644.1.
CH471109 Genomic DNA. Translation: EAW94485.1.
CH471109 Genomic DNA. Translation: EAW94486.1.
BC010264 mRNA. Translation: AAH10264.1.
BC033785 mRNA. Translation: AAH33785.1.
CCDSiCCDS11600.1. [Q07955-1]
CCDS58580.1. [Q07955-3]
PIRiA40040.
B40040.
C40040.
RefSeqiNP_001071634.1. NM_001078166.1. [Q07955-3]
NP_008855.1. NM_006924.4. [Q07955-1]
UniGeneiHs.68714.
Hs.710026.
Hs.744140.

Genome annotation databases

EnsembliENST00000258962; ENSP00000258962; ENSG00000136450. [Q07955-1]
ENST00000581979; ENSP00000463223; ENSG00000136450. [Q07955-3]
ENST00000582730; ENSP00000462215; ENSG00000136450. [Q07955-3]
GeneIDi6426.
KEGGihsa:6426.
UCSCiuc002ivi.3. human. [Q07955-1]
uc002ivj.3. human. [Q07955-3]

Polymorphism databases

DMDMi730773.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M72709 mRNA. Translation: AAA35565.1 .
M72709 mRNA. Translation: AAA35564.1 .
M69040 mRNA. Translation: AAA03476.1 .
AB062124 mRNA. Translation: BAB93456.1 .
AK312781 mRNA. Translation: BAG35644.1 .
CH471109 Genomic DNA. Translation: EAW94485.1 .
CH471109 Genomic DNA. Translation: EAW94486.1 .
BC010264 mRNA. Translation: AAH10264.1 .
BC033785 mRNA. Translation: AAH33785.1 .
CCDSi CCDS11600.1. [Q07955-1 ]
CCDS58580.1. [Q07955-3 ]
PIRi A40040.
B40040.
C40040.
RefSeqi NP_001071634.1. NM_001078166.1. [Q07955-3 ]
NP_008855.1. NM_006924.4. [Q07955-1 ]
UniGenei Hs.68714.
Hs.710026.
Hs.744140.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X4A NMR - A 1-96 [» ]
2M7S NMR - A 106-195 [» ]
2M8D NMR - B 107-196 [» ]
2O3D NMR - A 107-215 [» ]
3BEG X-ray 2.90 B 105-219 [» ]
4C0O X-ray 2.56 C/D 106-230 [» ]
ProteinModelPortali Q07955.
SMRi Q07955. Positions 6-102, 116-197.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112324. 145 interactions.
DIPi DIP-2155N.
IntActi Q07955. 49 interactions.
MINTi MINT-5000565.
STRINGi 9606.ENSP00000258962.

PTM databases

PhosphoSitei Q07955.

Polymorphism databases

DMDMi 730773.

Proteomic databases

MaxQBi Q07955.
PaxDbi Q07955.
PeptideAtlasi Q07955.
PRIDEi Q07955.

Protocols and materials databases

DNASUi 6426.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258962 ; ENSP00000258962 ; ENSG00000136450 . [Q07955-1 ]
ENST00000581979 ; ENSP00000463223 ; ENSG00000136450 . [Q07955-3 ]
ENST00000582730 ; ENSP00000462215 ; ENSG00000136450 . [Q07955-3 ]
GeneIDi 6426.
KEGGi hsa:6426.
UCSCi uc002ivi.3. human. [Q07955-1 ]
uc002ivj.3. human. [Q07955-3 ]

Organism-specific databases

CTDi 6426.
GeneCardsi GC17M056079.
H-InvDB HIX0173551.
HGNCi HGNC:10780. SRSF1.
HPAi CAB013073.
MIMi 600812. gene.
neXtProti NX_Q07955.
PharmGKBi PA35696.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00700000104103.
HOVERGENi HBG002295.
InParanoidi Q07955.
KOi K12890.
OrthoDBi EOG76X620.
PhylomeDBi Q07955.
TreeFami TF106261.

Enzyme and pathway databases

Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi SRSF1. human.
EvolutionaryTracei Q07955.
GeneWikii ASF/SF2.
GenomeRNAii 6426.
NextBioi 24955.
PMAP-CutDB Q07955.
PROi Q07955.
SOURCEi Search...

Gene expression databases

Bgeei Q07955.
CleanExi HS_SFRS1.
ExpressionAtlasi Q07955. baseline and differential.
Genevestigatori Q07955.

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. "Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators."
    Ge H., Zuo P., Manley J.L.
    Cell 66:373-382(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ASF-1 AND ASF-2), PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING.
  2. "Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators."
    Krainer A.R., Mayeda A., Kozak D., Binns G.
    Cell 66:383-394(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ASF-1), PROTEIN SEQUENCE OF 144-161 AND 167-175.
  3. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ASF-1).
    Tissue: Colon adenocarcinoma.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ASF-1).
    Tissue: Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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 ASF-1 AND ASF-3).
    Tissue: Brain and Placenta.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 18-28; 31-38; 52-65; 75-83; 123-138 AND 143-164, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 123-140.
  9. "Two members of a conserved family of nuclear phosphoproteins are involved in pre-mRNA splicing."
    Mayeda A., Zahler A.M., Krainer A.R., Roth M.B.
    Proc. Natl. Acad. Sci. U.S.A. 89:1301-1304(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "Specific interactions between proteins implicated in splice site selection and regulated alternative splicing."
    Wu J.Y., Maniatis T.
    Cell 75:1061-1070(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION IN SPLICEOSOME ASSEMBLY.
  11. "Functional domains of the human splicing factor ASF/SF2."
    Zuo P., Manley J.L.
    EMBO J. 12:4727-4737(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, CHARACTERIZATION OF FUNCTIONAL DOMAINS.
  12. "Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors."
    Kohtz J.D., Jamison S.F., Will C.L., Zuo P., Luehrmann R., Garcia-Blanco M.A., Manley J.L.
    Nature 368:119-124(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECRUITMENT OF U1-70K TO PRE-MRNA.
  13. "The human splicing factor ASF/SF2 can specifically recognize pre-mRNA 5' splice sites."
    Zuo P., Manley J.L.
    Proc. Natl. Acad. Sci. U.S.A. 91:3363-3367(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECOGNITION OF PRE-MRNA 5'SPLICE SITES.
  14. "The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities."
    Tacke R., Manley J.L.
    EMBO J. 14:3540-3551(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING SPECIFICITY.
  15. "A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA."
    Tronchere H., Wang J., Fu X.D.
    Nature 388:397-400(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZRSR2.
  16. "A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm."
    Caceres J.F., Screaton G.R., Krainer A.R.
    Genes Dev. 12:55-66(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-162 AND PHE-180.
  17. "A novel transcriptional coactivator, p52, functionally interacts with the essential splicing factor ASF/SF2."
    Ge H., Si Y., Wolffe A.P.
    Mol. Cell 2:751-759(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSIP1.
  18. Cited for: INTERACTION WITH SAFB/SAFB1.
  19. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SREK1.
  20. "Nuclear export and retention signals in the RS domain of SR proteins."
    Cazalla D., Zhu J., Manche L., Huber E., Krainer A.R., Caceres J.F.
    Mol. Cell. Biol. 22:6871-6882(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  21. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  22. "SR splicing factors serve as adapter proteins for TAP-dependent mRNA export."
    Huang Y., Gattoni R., Stevenin J., Steitz J.A.
    Mol. Cell 11:837-843(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NXF1.
  23. "Processive phosphorylation of alternative splicing factor/splicing factor 2."
    Aubol B.E., Chakrabarti S., Ngo J., Shaffer J., Nolen B., Fu X.-D., Ghosh G., Adams J.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12601-12606(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SERINE RESIDUES, SUBCELLULAR LOCATION, INTERACTION WITH SRPK1.
  24. "A novel SR-related protein is required for the second step of pre-mRNA splicing."
    Cazalla D., Newton K., Caceres J.F.
    Mol. Cell. Biol. 25:2969-2980(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSRC1.
  25. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Ordered multi-site phosphorylation of the splicing factor ASF/SF2 by SRPK1."
    Ma C.T., Velazquez-Dones A., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.
    J. Mol. Biol. 376:55-68(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY SRPK1, THE MECHANISM OF PHOSPHORYATION.
  27. "Adaptable molecular interactions guide phosphorylation of the SR protein ASF/SF2 by SRPK1."
    Hagopian J.C., Ma C.T., Meade B.R., Albuquerque C.P., Ngo J.C., Ghosh G., Jennings P.A., Fu X.D., Adams J.A.
    J. Mol. Biol. 382:894-909(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY SRPK1, THE MECHANISM OF PHOSPHORYATION.
  28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-205; SER-231; SER-234 AND SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "Allosteric interactions direct binding and phosphorylation of ASF/SF2 by SRPK1."
    Huynh N., Ma C.T., Giang N., Hagopian J., Ngo J., Adams J., Ghosh G.
    Biochemistry 48:11432-11440(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY SRPK1, THE MECHANISM OF PHOSPHORYATION.
  30. "Regiospecific phosphorylation control of the SR protein ASF/SF2 by SRPK1."
    Ma C.T., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.
    J. Mol. Biol. 390:618-634(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY SRPK1, THE MECHANISM OF PHOSPHORYATION.
  31. "Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins."
    Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., Blencowe B.J., Morris Q., Hughes T.R.
    Nat. Biotechnol. 27:667-670(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  32. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38 AND LYS-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF."
    Sinha R., Allemand E., Zhang Z., Karni R., Myers M.P., Krainer A.R.
    Mol. Cell. Biol. 30:2762-2774(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-93; ARG-97 AND ARG-109, MUTAGENESIS OF ARG-93; ARG-97 AND ARG-109, SUBCELLULAR LOCATION.
  34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "NSrp70 is a novel nuclear speckle-related protein that modulates alternative pre-mRNA splicing in vivo."
    Kim Y.D., Lee J.Y., Oh K.M., Araki M., Araki K., Yamamura K.I., Jun C.D.
    Nucleic Acids Res. 39:4300-4314(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC55.
  37. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  38. "Solution structure of RRM domain in splicing factor SF2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-98.
  39. "A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1."
    Ngo J.C., Giang K., Chakrabarti S., Ma C.T., Huynh N., Hagopian J.C., Dorrestein P.C., Fu X.D., Adams J.A., Ghosh G.
    Mol. Cell 29:563-576(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 105-219 IN COMPLEX WITH SRPK1, MECHANISM OF ITS PHOSPHORYLATION BY SRPK1, DOMAIN RRM.
  40. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-89.

Entry informationi

Entry nameiSRSF1_HUMAN
AccessioniPrimary (citable) accession number: Q07955
Secondary accession number(s): B2R6Z7, D3DTZ3, Q13809
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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