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Q07955 (SRSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SRSF1
Synonyms:ASF, SF2, SF2P33, SFRS1
ORF Names:OK/SW-cl.3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.11 Ref.12

Subunit structure

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. Ref.10 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.36

Subcellular location

Cytoplasm. Nucleus speckle. Note: In nuclear speckles. Shuttles between the nucleus and the cytoplasm. Ref.16 Ref.20 Ref.23 Ref.33

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. Ref.11 Ref.39

Post-translational modification

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. Ref.23 Ref.26 Ref.27 Ref.29 Ref.30 Ref.39

Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles. Ref.33

Sequence similarities

Belongs to the splicing factor SR family.

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
mRNA transport
Transport
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandRNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA 5'-splice site recognition

Inferred from direct assay Ref.17. Source: UniProtKB

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA processing

Traceable author statement Ref.2. Source: ProtInc

mRNA splice site selection

Traceable author statement Ref.2. Source: ProtInc

mRNA splicing, via spliceosome

Inferred by curator Ref.21. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.21. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from direct assay PubMed 20797886. Source: MGI

nucleoplasm

Inferred from direct assay Ref.17. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 21984414. Source: MGI

   Molecular_functionRNA binding

Inferred from direct assay Ref.31. Source: UniProtKB

mRNA binding

Inferred from direct assay PubMed 21984414. Source: MGI

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform ASF-1 (identifier: Q07955-1)

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.
Isoform ASF-2 (identifier: Q07955-2)

The sequence of this isoform differs from the canonical sequence as follows:
     185-248: GETAYIRVKV...PRHSRSRSRT → FCLSNREKLP...NCFVQNGLKC
Isoform ASF-3 (identifier: Q07955-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.37
Chain2 – 248247Serine/arginine-rich splicing factor 1
PRO_0000081911

Regions

Domain16 – 9176RRM 1
Domain121 – 19575RRM 2
Region198 – 24750Interacts with SAFB1
Compositional bias94 – 11320Gly-rich (hinge region)
Compositional bias198 – 24750Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue21N-acetylserine Ref.37
Modified residue21Phosphoserine Ref.23 Ref.37
Modified residue381N6-acetyllysine Ref.32
Modified residue931Asymmetric dimethylarginine Ref.33
Modified residue971Asymmetric dimethylarginine Ref.33
Modified residue1091Asymmetric dimethylarginine Ref.33
Modified residue1791N6-acetyllysine Ref.32
Modified residue1991Phosphoserine Ref.23 Ref.28 Ref.34 Ref.37
Modified residue2011Phosphoserine By similarity
Modified residue2051Phosphoserine Ref.23 Ref.28
Modified residue2311Phosphoserine Ref.23 Ref.28
Modified residue2341Phosphoserine Ref.23 Ref.28
Modified residue2381Phosphoserine Ref.23 Ref.28

Natural variations

Alternative sequence185 – 24864GETAY…SRSRT → FCLSNREKLPTSGLKLMGPE VQVMEDLDLEAVVVAEAVAE ATAGVAVTPQGEAEDHHAIL PVIADLALVHKMIGDTFCRT HVVYSFPLFSTIFSFFNSNC FVQNGLKC in isoform ASF-2.
VSP_005856
Alternative sequence185 – 20117GETAY…PRSPS → VGYTRILFFDQNWIQWS in isoform ASF-3.
VSP_005857
Alternative sequence202 – 24847Missing in isoform ASF-3.
VSP_005858
Natural variant891P → S in a breast cancer sample; somatic mutation. Ref.40
VAR_035488

Experimental info

Mutagenesis58 – 592FV → SR in FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding.
Mutagenesis931R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-97 and Ala-109. Ref.33
Mutagenesis971R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-109. Ref.33
Mutagenesis1091R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-97. Ref.33
Mutagenesis162 – 1632FV → SR in FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding. Ref.16
Mutagenesis1621F → A in AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding. Ref.16
Mutagenesis1621F → D: Reduced nucleocytoplasmic shuttling; when associated with D-190. Ref.16
Mutagenesis1801F → D: Reduced nucleocytoplasmic shuttling; when associated with D-162. Ref.16
Mutagenesis182 – 24867Missing in MR-B; strongly inhibits splicing.
Mutagenesis182 – 19918Missing in MR-E; loss of ability to activate splicing.
Mutagenesis192 – 24857Missing in MR-A; loss of ability to activate splicing.
Mutagenesis192 – 1998Missing in MR-D; loss of ability to activate splicing.
Mutagenesis199 – 22426Missing in RS-A; loss of ability to activate splicing but retains splice site switching.
Mutagenesis215 – 24834Missing in RS-C; loss of ability to activate splicing but retains splice site switching.
Mutagenesis226 – 24823Missing in RS-B; retains both splice activation and splice site switching activity.

Secondary structure

......................................... 248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform ASF-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C28A0B2F112EA713

FASTA24827,745
        10         20         30         40         50         60 
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE 

        70         80         90        100        110        120 
FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE 

       130        140        150        160        170        180 
NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF 

       190        200        210        220        230        240 
RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR 


HSRSRSRT 

« Hide

Isoform ASF-2 [UniParc].

Checksum: C9502AC70F373EAC
Show »

FASTA29231,999
Isoform ASF-3 [UniParc].

Checksum: B9AC6495A491613D
Show »

FASTA20122,460

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements."
Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L., Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.
Nucleic Acids Res. 26:3542-3549(1998) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-89.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA40040.
B40040.
C40040.
RefSeqNP_001071634.1. NM_001078166.1.
NP_008855.1. NM_006924.4.
UniGeneHs.68714.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4ANMR-A1-96[»]
2M7SNMR-A106-195[»]
2M8DNMR-B107-196[»]
2O3DNMR-A107-214[»]
3BEGX-ray2.90B105-219[»]
4C0OX-ray2.56C/D106-230[»]
ProteinModelPortalQ07955.
SMRQ07955. Positions 6-102, 107-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112324. 135 interactions.
DIPDIP-2155N.
IntActQ07955. 49 interactions.
MINTMINT-5000565.
STRING9606.ENSP00000258962.

PTM databases

PhosphoSiteQ07955.

Polymorphism databases

DMDM730773.

Proteomic databases

PaxDbQ07955.
PeptideAtlasQ07955.
PRIDEQ07955.

Protocols and materials databases

DNASU6426.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258962; ENSP00000258962; ENSG00000136450. [Q07955-1]
ENST00000581979; ENSP00000463223; ENSG00000136450. [Q07955-3]
ENST00000582730; ENSP00000462215; ENSG00000136450. [Q07955-3]
GeneID6426.
KEGGhsa:6426.
UCSCuc002ivi.3. human. [Q07955-1]
uc002ivj.3. human. [Q07955-3]

Organism-specific databases

CTD6426.
GeneCardsGC17M056079.
H-InvDBHIX0173551.
HGNCHGNC:10780. SRSF1.
HPACAB013073.
MIM600812. gene.
neXtProtNX_Q07955.
PharmGKBPA35696.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOVERGENHBG002295.
InParanoidQ07955.
KOK12890.
OrthoDBEOG76X620.
PhylomeDBQ07955.
TreeFamTF106261.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ07955.
BgeeQ07955.
CleanExHS_SFRS1.
GenevestigatorQ07955.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRSF1. human.
EvolutionaryTraceQ07955.
GeneWikiASF/SF2.
GenomeRNAi6426.
NextBio24955.
PMAP-CutDBQ07955.
PROQ07955.
SOURCESearch...

Entry information

Entry nameSRSF1_HUMAN
AccessionPrimary (citable) accession number: Q07955
Secondary accession number(s): B2R6Z7, D3DTZ3, Q13809
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM