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Protein

Serine/arginine-rich splicing factor 2

Gene

SRSF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. 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. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment.2 Publications

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • pre-mRNA binding Source: Ensembl
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72187. mRNA 3'-end processing.
SIGNORiQ01130.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 2
Alternative name(s):
Protein PR264
Splicing component, 35 kDa
Splicing factor SC35
Short name:
SC-35
Splicing factor, arginine/serine-rich 2
Gene namesi
Name:SRSF2
Synonyms:SFRS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10783. SRSF2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • spliceosomal complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35699.

Polymorphism and mutation databases

BioMutaiSRSF2.
DMDMi60416437.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 221220Serine/arginine-rich splicing factor 2PRO_0000081918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources1 Publication
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei22 – 221PhosphothreonineCombined sources
Modified residuei25 – 251PhosphothreonineCombined sources
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei52 – 521N6-acetyllysine1 Publication
Modified residuei189 – 1891PhosphoserineCombined sources
Modified residuei191 – 1911PhosphoserineCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei208 – 2081PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei220 – 2201PhosphoserineCombined sources

Post-translational modificationi

Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by SRPK2 and this causes its redistribution from the nuclear speckle to nucleoplasm and controls cell fate decision in response to cisplatin treatment. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2 nuclear translocation.2 Publications
Acetylation on Lys-52 by KAT5/TIP60 promotes its proteasomal degradation. This effect is counterbalanced by HDAC6, which positively controls SRSF2 protein level by deacetylating it and preventing its proteasomal degradation.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ01130.
MaxQBiQ01130.
PaxDbiQ01130.
PeptideAtlasiQ01130.
PRIDEiQ01130.
TopDownProteomicsiQ01130-1. [Q01130-1]

PTM databases

iPTMnetiQ01130.
PhosphoSiteiQ01130.
SwissPalmiQ01130.

Expressioni

Inductioni

Accumulates in a hypoacetylated/phosphorylated form in response to cisplatin treatment.

Gene expression databases

BgeeiQ01130.
CleanExiHS_SFRS2.
ExpressionAtlasiQ01130. baseline and differential.
GenevisibleiQ01130. HS.

Organism-specific databases

HPAiHPA049905.

Interactioni

Subunit structurei

Interacts with BRDT (By similarity). In vitro, self-associates and binds SRSF1/SFRS1 (ASF/SF2), SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with CCNL1 and CCNL2. Interacts with SCAF11. Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CIR1Q86X954EBI-627047,EBI-627102
KAT5Q929933EBI-627047,EBI-399080

Protein-protein interaction databases

BioGridi112325. 109 interactions.
DIPiDIP-33836N.
IntActiQ01130. 54 interactions.
MINTiMINT-2863034.
STRINGi9606.ENSP00000353089.

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Beta strandi16 – 194Combined sources
Helixi26 – 349Combined sources
Helixi35 – 373Combined sources
Beta strandi41 – 444Combined sources
Beta strandi49 – 535Combined sources
Beta strandi57 – 648Combined sources
Helixi65 – 7410Combined sources
Beta strandi79 – 846Combined sources
Beta strandi86 – 905Combined sources
Beta strandi91 – 944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KN4NMR-A9-101[»]
2LEANMR-A1-101[»]
2LEBNMR-A1-101[»]
2LECNMR-A1-101[»]
ProteinModelPortaliQ01130.
SMRiQ01130. Positions 9-101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01130.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 9279RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi111 – 1166Gly-rich (hinge region)
Compositional biasi117 – 221105Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4207. Eukaryota.
ENOG4111NJ8. LUCA.
GeneTreeiENSGT00700000104403.
HOVERGENiHBG107480.
InParanoidiQ01130.
KOiK12891.
OMAiNGSPEKQ.
TreeFamiTF106262.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q01130-1) [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
MSYGRPPPDV EGMTSLKVDN LTYRTSPDTL RRVFEKYGRV GDVYIPRDRY
60 70 80 90 100
TKESRGFAFV RFHDKRDAED AMDAMDGAVL DGRELRVQMA RYGRPPDSHH
110 120 130 140 150
SRRGPPPRRY GGGGYGRRSR SPRRRRRSRS RSRSRSRSRS RSRYSRSKSR
160 170 180 190 200
SRTRSRSRST SKSRSARRSK SKSSSVSRSR SRSRSRSRSR SPPPVSKRES
210 220
KSRSRSKSPP KSPEEEGAVS S
Length:221
Mass (Da):25,476
Last modified:January 23, 2007 - v4
Checksum:i68121AC4D35714FA
GO
Isoform 2 (identifier: Q01130-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     108-119: Missing.

Note: No experimental confirmation available.
Show »
Length:209
Mass (Da):24,153
Checksum:iE1229752981E5304
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381G → R in AAA60306 (PubMed:1373910).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei108 – 11912Missing in isoform 2. 1 PublicationVSP_056153Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90104 mRNA. Translation: AAA60306.1.
X62447 mRNA. Translation: CAA44307.1.
X75755 Genomic DNA. Translation: CAA53383.1.
BT007250 mRNA. Translation: AAP35914.1.
AK124792 mRNA. Translation: BAG54097.1.
AK297813 mRNA. Translation: BAG60151.1.
AC005837 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89439.1.
CH471099 Genomic DNA. Translation: EAW89448.1.
BC000339 mRNA. Translation: AAH00339.1.
BC001303 mRNA. Translation: AAH01303.1.
BC070086 mRNA. Translation: AAH70086.1.
L03693 Genomic DNA. Translation: AAA60162.1.
CCDSiCCDS11749.1. [Q01130-1]
RefSeqiNP_001182356.1. NM_001195427.1. [Q01130-1]
NP_003007.2. NM_003016.4. [Q01130-1]
UniGeneiHs.584801.

Genome annotation databases

EnsembliENST00000359995; ENSP00000353089; ENSG00000161547. [Q01130-1]
ENST00000392485; ENSP00000376276; ENSG00000161547. [Q01130-1]
ENST00000452355; ENSP00000391278; ENSG00000161547. [Q01130-1]
ENST00000508921; ENSP00000441780; ENSG00000161547. [Q01130-2]
ENST00000585202; ENSP00000462425; ENSG00000161547. [Q01130-1]
GeneIDi6427.
KEGGihsa:6427.
UCSCiuc002jsv.4. human. [Q01130-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90104 mRNA. Translation: AAA60306.1.
X62447 mRNA. Translation: CAA44307.1.
X75755 Genomic DNA. Translation: CAA53383.1.
BT007250 mRNA. Translation: AAP35914.1.
AK124792 mRNA. Translation: BAG54097.1.
AK297813 mRNA. Translation: BAG60151.1.
AC005837 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89439.1.
CH471099 Genomic DNA. Translation: EAW89448.1.
BC000339 mRNA. Translation: AAH00339.1.
BC001303 mRNA. Translation: AAH01303.1.
BC070086 mRNA. Translation: AAH70086.1.
L03693 Genomic DNA. Translation: AAA60162.1.
CCDSiCCDS11749.1. [Q01130-1]
RefSeqiNP_001182356.1. NM_001195427.1. [Q01130-1]
NP_003007.2. NM_003016.4. [Q01130-1]
UniGeneiHs.584801.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KN4NMR-A9-101[»]
2LEANMR-A1-101[»]
2LEBNMR-A1-101[»]
2LECNMR-A1-101[»]
ProteinModelPortaliQ01130.
SMRiQ01130. Positions 9-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112325. 109 interactions.
DIPiDIP-33836N.
IntActiQ01130. 54 interactions.
MINTiMINT-2863034.
STRINGi9606.ENSP00000353089.

PTM databases

iPTMnetiQ01130.
PhosphoSiteiQ01130.
SwissPalmiQ01130.

Polymorphism and mutation databases

BioMutaiSRSF2.
DMDMi60416437.

Proteomic databases

EPDiQ01130.
MaxQBiQ01130.
PaxDbiQ01130.
PeptideAtlasiQ01130.
PRIDEiQ01130.
TopDownProteomicsiQ01130-1. [Q01130-1]

Protocols and materials databases

DNASUi6427.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359995; ENSP00000353089; ENSG00000161547. [Q01130-1]
ENST00000392485; ENSP00000376276; ENSG00000161547. [Q01130-1]
ENST00000452355; ENSP00000391278; ENSG00000161547. [Q01130-1]
ENST00000508921; ENSP00000441780; ENSG00000161547. [Q01130-2]
ENST00000585202; ENSP00000462425; ENSG00000161547. [Q01130-1]
GeneIDi6427.
KEGGihsa:6427.
UCSCiuc002jsv.4. human. [Q01130-1]

Organism-specific databases

CTDi6427.
GeneCardsiSRSF2.
HGNCiHGNC:10783. SRSF2.
HPAiHPA049905.
MIMi600813. gene.
neXtProtiNX_Q01130.
PharmGKBiPA35699.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4207. Eukaryota.
ENOG4111NJ8. LUCA.
GeneTreeiENSGT00700000104403.
HOVERGENiHBG107480.
InParanoidiQ01130.
KOiK12891.
OMAiNGSPEKQ.
TreeFamiTF106262.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72187. mRNA 3'-end processing.
SIGNORiQ01130.

Miscellaneous databases

ChiTaRSiSRSF2. human.
EvolutionaryTraceiQ01130.
GeneWikiiSFRS2.
GenomeRNAii6427.
PROiQ01130.
SOURCEiSearch...

Gene expression databases

BgeeiQ01130.
CleanExiHS_SFRS2.
ExpressionAtlasiQ01130. baseline and differential.
GenevisibleiQ01130. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a complementary DNA that encodes the mammalian splicing factor SC35."
    Fu X.-D., Maniatis T.
    Science 256:535-538(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 67-84.
  2. "A potential splicing factor is encoded by the opposite strand of the trans-spliced c-myb exon."
    Vellard M., Sureau A., Soret J., Martinerie C., Perbal B.
    Proc. Natl. Acad. Sci. U.S.A. 89:2511-2515(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "Several mRNAs with variable 3' untranslated regions and different stability encode the human PR264/SC35 splicing factor."
    Sureau A., Perbal B.
    Proc. Natl. Acad. Sci. U.S.A. 91:932-936(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Caudate nucleus.
  6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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).
    Tissue: Lung, Placenta and Testis.
  9. "The PR264/c-myb connection: expression of a splicing factor modulated by a nuclear protooncogene."
    Sureau A., Soret J., Vellard M., Crochet J., Perbal B.
    Proc. Natl. Acad. Sci. U.S.A. 89:11683-11687(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
  10. Bienvenut W.V.
    Submitted (JUL-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  11. "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 67-83.
  12. "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.
  13. "Specific commitment of different pre-mRNAs to splicing by single SR proteins."
    Fu X.-D.
    Nature 365:82-85(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SPECIFICITY FOR BETA-GLOBIN MRNA.
  14. "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: INTERACTION WITH U1-70K.
  15. "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.
  16. "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.
  17. "Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
    Zhang W.-J., Wu J.Y.
    Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCAF11.
  18. "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.
  19. "Cyclin L is an RS domain protein involved in pre-mRNA splicing."
    Dickinson L.A., Edgar A.J., Ehley J., Gottesfeld J.M.
    J. Biol. Chem. 277:25465-25473(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCNL1.
  20. "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells."
    Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.
    J. Biol. Chem. 279:11639-11648(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCNL2.
  21. "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.
  22. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-208, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-204; SER-206; SER-208 AND SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons."
    Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.
    J. Biol. Chem. 284:24512-24525(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY SRPK2.
  26. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  27. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-22; THR-25; SER-26; SER-208 AND SER-212, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
    Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
    EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-52, PHOSPHORYLATION BY SRPK2.
  30. "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.
  31. "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; THR-22; SER-189; SER-191; SER-208; SER-212 AND SER-220, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  34. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSRSF2_HUMAN
AccessioniPrimary (citable) accession number: Q01130
Secondary accession number(s): B3KWD5, B4DN89, H0YG49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 194 of the entry and version 4 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.