Q07955 (SRSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SRSF1
Synonyms:	ASF, SF2, SF2P33, SFRS1
ORF Names:	OK/SW-cl.3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. 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. Ref.10 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.34
Subcellular location	Cytoplasm. Nucleus speckle. Note: In nuclear speckles. Shuttles between the nucleus and the cytoplasm. Ref.16 Ref.20 Ref.22
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.37
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.22 Ref.25 Ref.26 Ref.28 Ref.29 Ref.37 Arg-97 is dimethylated, probably to asymmetric dimethylarginine.
Sequence similarities	Belongs to the splicing factor SR family. Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle contraction Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara 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 termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular_component	catalytic 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
Molecular_function	RNA binding Inferred from direct assay Ref.30. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CIR1	Q86X95	3	EBI-398920,EBI-627102
NFYA	P23511	5	EBI-398920,EBI-389739
NXF1	Q9UBU9	5	EBI-398920,EBI-398874
SRPK1	Q96SB4	2	EBI-398920,EBI-539478
Srpk1	O70551	5	EBI-398920,EBI-593343	From a different organism.
Srpk2	O54781	3	EBI-398920,EBI-593325	From a different organism.

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.35

Chain

2 – 248

247

Serine/arginine-rich splicing factor 1

PRO_0000081911

Regions

Domain

16 – 91

76

RRM 1

Domain

121 – 195

75

RRM 2

Region

198 – 247

50

Interacts with SAFB1

Compositional bias

94 – 113

20

Gly-rich (hinge region)

Compositional bias

198 – 247

50

Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.35

Modified residue

2

1

Phosphoserine Ref.22 Ref.35

Modified residue

38

1

N6-acetyllysine Ref.31

Modified residue

179

1

N6-acetyllysine Ref.31

Modified residue

199

1

Phosphoserine Ref.22 Ref.27 Ref.32 Ref.35

Modified residue

201

1

Phosphoserine By similarity

Modified residue

205

1

Phosphoserine Ref.22 Ref.27

Modified residue

231

1

Phosphoserine Ref.22 Ref.27

Modified residue

234

1

Phosphoserine Ref.22 Ref.27

Modified residue

238

1

Phosphoserine Ref.22 Ref.27

Natural variations

Alternative sequence

185 – 248

64

GETAY…SRSRT → FCLSNREKLPTSGLKLMGPE VQVMEDLDLEAVVVAEAVAE ATAGVAVTPQGEAEDHHAIL PVIADLALVHKMIGDTFCRT HVVYSFPLFSTIFSFFNSNC FVQNGLKC in isoform ASF-2.

VSP_005856

Alternative sequence

185 – 201

17

GETAY…PRSPS → VGYTRILFFDQNWIQWS in isoform ASF-3.

VSP_005857

Alternative sequence

202 – 248

47

Missing in isoform ASF-3.

VSP_005858

Natural variant

89

1

P → S in a breast cancer sample; somatic mutation. Ref.38

VAR_035488

Experimental info

Mutagenesis

58 – 59

2

FV → SR in FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding.

Mutagenesis

162 – 163

2

FV → SR in FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding. Ref.16

Mutagenesis

162

1

F → A in AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding. Ref.16

Mutagenesis

162

1

F → D: Reduced nucleocytoplasmic shuttling; when associated with D-190. Ref.16

Mutagenesis

180

1

F → D: Reduced nucleocytoplasmic shuttling; when associated with D-162. Ref.16

Mutagenesis

182 – 248

67

Missing in MR-B; strongly inhibits splicing.

Mutagenesis

182 – 199

18

Missing in MR-E; loss of ability to activate splicing.

Mutagenesis

192 – 248

57

Missing in MR-A; loss of ability to activate splicing.

Mutagenesis

192 – 199

8

Missing in MR-D; loss of ability to activate splicing.

Mutagenesis

199 – 224

26

Missing in RS-A; loss of ability to activate splicing but retains splice site switching.

Mutagenesis

215 – 248

34

Missing in RS-C; loss of ability to activate splicing but retains splice site switching.

Mutagenesis

226 – 248

23

Missing in RS-B; retains both splice activation and splice site switching activity.

Secondary structure

1

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248

Helix Strand Turn

Details...

Beta strand

15 – 22

8

Helix

29 – 36

8

Helix

37 – 39

3

Beta strand

42 – 47

6

Beta strand

50 – 54

5

Beta strand

57 – 62

6

Helix

64 – 74

11

Beta strand

85 – 87

3

Beta strand

123 – 127

5

Helix

136 – 141

6

Helix

142 – 144

3

Beta strand

147 – 152

6

Beta strand

156 – 164

9

Helix

165 – 175

11

Beta strand

178 – 182

5

Turn

183 – 185

3

Beta strand

191 – 194

4

Beta strand

206 – 208

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform ASF-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: C28A0B2F112EA713	FASTA	248	27,745
	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
	Isoform ASF-2 [UniParc]. Checksum: C9502AC70F373EAC	FASTA	292	31,999
	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 RSHEFCLSNR EKLPTSGLKL MGPEVQVMED LDLEAVVVAE AVAEATAGVA VTPQGEAEDH 250 260 270 280 290 HAILPVIADL ALVHKMIGDT FCRTHVVYSF PLFSTIFSFF NSNCFVQNGL KC
	Isoform ASF-3 [UniParc]. Checksum: B9AC6495A491613D	FASTA	201	22,460
	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 RSHEVGYTRI LFFDQNWIQW S

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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, MASS SPECTROMETRY.
[32]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"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].
[34]	"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.
[35]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[36]	"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.
[37]	"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.
[38]	"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. , 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.

IPI

IPI00215884.
IPI00218591.
IPI00218592.

PIR

A40040.
B40040.
C40040.

RefSeq

NP_001071634.1. NM_001078166.1.
NP_008855.1. NM_006924.4.

UniGene

Hs.68714.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X4A	NMR	-	A	1-96	[»]
2O3D	NMR	-	A	107-214	[»]
3BEG	X-ray	2.90	B	105-219	[»]

ProteinModelPortal

Q07955.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2155N.

IntAct

Q07955. 31 interactions.

MINT

MINT-5000565.

STRING

9606.ENSP00000258962.

PTM databases

PhosphoSite

Q07955.

Polymorphism databases

DMDM

730773.

Proteomic databases

PaxDb

Q07955.

PeptideAtlas

Q07955.

PRIDE

Q07955.

Protocols and materials databases

DNASU

6426.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000258962; ENSP00000258962; ENSG00000136450.
ENST00000581979; ENSP00000463223; ENSG00000136450.
ENST00000582730; ENSP00000462215; ENSG00000136450.

GeneID

6426.

KEGG

hsa:6426.

UCSC

uc002ivi.3. human.
uc002ivj.3. human.

Organism-specific databases

CTD

6426.

GeneCards

GC17M056079.

H-InvDB

HIX0173551.

HGNC

HGNC:10780. SRSF1.

HPA

CAB013073.

MIM

600812. gene.

neXtProt

NX_Q07955.

PharmGKB

PA35696.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOVERGEN

HBG002295.

InParanoid

Q07955.

KO

K12890.

OMA

QVMEDLD.

PhylomeDB

Q07955.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

Q07955.

Bgee

Q07955.

CleanEx

HS_SFRS1.

Genevestigator

Q07955.

GermOnline

ENSG00000136450. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SRSF1. human.

EvolutionaryTrace

Q07955.

GenomeRNAi

6426.

NextBio

24955.

PMAP-CutDB

Q07955.

SOURCE

Search...

Entry information

Entry name

SRSF1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 165 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.