Reviewed, UniProtKB/Swiss-Prot Q07955 (SFRS1_HUMAN)

Names and origin

Protein names

Recommended name:
    Splicing factor, arginine/serine-rich 1
Alternative name(s):
    pre-mRNA-splicing factor SF2, P33 subunit
    Alternative-splicing factor 1
      Short name=ASF-1

Gene names

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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. 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.9 Ref.10
Subunit structure	Consists of two polypeptides of p32 and p33. In vitro, binds SFRS1 (ASF/SF2), SNRNP70 and U2AF1 but not U2AF2. Binds SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF. Interacts with SRPK1. Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Ref.8 Ref.14 Ref.15 Ref.16 Ref.19
Subcellular location	Cytoplasm. Nucleus speckle. Note: In nuclear speckles. Shuttles between the nucleus and the cytoplasm. Ref.19 Ref.13 Ref.17
Domain	Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling. Ref.9
Post-translational modification	Extensively phosphorylated on serine residues in the RS domain. This may regulate nucleocytoplasmic shuttling. Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Arg-97 is dimethylated, probably to asymmetric dimethylarginine. Ref.20
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 Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	mRNA splice site selection Ref.2 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CIR	Q86X95	1	EBI-398920,EBI-627102
NFYA	P23511	1	EBI-398920,EBI-389739
NXF1	Q9UBU9	3	EBI-398920,EBI-398874
RNPS1	Q15287	1	EBI-398920,EBI-395959
SRPK1	Q96SB4	1	EBI-398920,EBI-539478
Srpk1	O70551	4	EBI-398920,EBI-593343	From a different organism.
Srpk2	O54781	2	EBI-398920,EBI-593325	From a different organism.
YWHAQ	P27348	1	EBI-398920,EBI-359854

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 248

247

Splicing factor, arginine/serine-rich 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 Potential

Modified residue

2

1

Phosphoserine Ref.19 Ref.22

Modified residue

93

1

Omega-N-methylarginine Ref.20

Modified residue

97

1

Omega-N-methylated arginine Ref.20

Modified residue

109

1

Omega-N-methylarginine Ref.20

Modified residue

189

1

Phosphotyrosine Ref.19 Ref.21

Modified residue

199

1

Phosphoserine Ref.19 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Modified residue

201

1

Phosphoserine Ref.19 Ref.24 Ref.26 Ref.27

Modified residue

202

1

Phosphotyrosine Ref.19 Ref.27

Modified residue

205

1

Phosphoserine Ref.19 Ref.22 Ref.24 Ref.26 Ref.27

Modified residue

231

1

Phosphoserine Ref.19 Ref.27

Modified residue

234

1

Phosphoserine Ref.19 Ref.27

Modified residue

237

1

Phosphotyrosine Ref.19 Ref.27

Modified residue

238

1

Phosphoserine Ref.19 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.30

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.13

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.13

Mutagenesis

162

1

F → D: Reduced nucleocytoplasmic shuttling; when associated with D-190. Ref.13

Mutagenesis

180

1

F → D: Reduced nucleocytoplasmic shuttling; when associated with D-162. Ref.13

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

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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

122 – 126

5

Helix

134 – 141

8

Helix

142 – 144

3

Beta strand

147 – 152

6

Beta strand

156 – 164

9

Helix

165 – 173

9

Turn

174 – 177

4

Beta strand

178 – 182

5

Turn

183 – 185

3

Beta strand

186 – 194

9

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. 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. 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: 1855257] [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: 1830244] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ASF-1 AND ASF-3). Tissue: Brain and Placenta.
[5]	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.
[6]	"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: 1577277] [Abstract] Cited for: PROTEIN SEQUENCE OF 123-140.
[7]	"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: 1741384] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Specific interactions between proteins implicated in splice site selection and regulated alternative splicing." Wu J.Y., Maniatis T. Cell 75:1061-1070(1993) [PubMed: 8261509] [Abstract] Cited for: INTERACTION IN SPLICEOSOME ASSEMBLY.
[9]	"Functional domains of the human splicing factor ASF/SF2." Zuo P., Manley J.L. EMBO J. 12:4727-4737(1993) [PubMed: 8223481] [Abstract] Cited for: MUTAGENESIS, CHARACTERIZATION OF FUNCTIONAL DOMAINS.
[10]	"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: 8139654] [Abstract] Cited for: FUNCTION IN RECRUITMENT OF U1-70K TO PRE-MRNA.
[11]	"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: 7512732] [Abstract] Cited for: RECOGNITION OF PRE-MRNA 5'SPLICE SITES.
[12]	"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: 7543047] [Abstract] Cited for: RNA-BINDING SPECIFICITY.
[13]	"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: 9420331] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-162 AND PHE-180.
[14]	"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: 9885563] [Abstract] Cited for: INTERACTION WITH PSIP1.
[15]	"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: 9671816] [Abstract] Cited for: INTERACTION WITH SAFB/SAFB1.
[16]	"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: 10757789] [Abstract] Cited for: INTERACTION WITH SFRS12.
[17]	"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: 12215544] [Abstract] Cited for: SUBCELLULAR LOCATION.
[18]	"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: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[19]	"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: 14555757] [Abstract] Cited for: PHOSPHORYLATION AT SERINE RESIDUES, SUBCELLULAR LOCATION, INTERACTION WITH SRPK1.
[20]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-93; ARG-97 AND ARG-109, MASS SPECTROMETRY.
[21]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-189, MASS SPECTROMETRY.
[22]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-199 AND SER-205, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, MASS SPECTROMETRY. Tissue: Epithelium.
[24]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-201 AND SER-205, MASS SPECTROMETRY.
[25]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, MASS SPECTROMETRY.
[26]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-201 AND SER-205, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-201; TYR-202; SER-205; SER-231; SER-234; TYR-237 AND SER-238, MASS SPECTROMETRY.
[28]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[29]	"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.
[30]	"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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-89.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M72709 mRNA. Translation: AAA35565.1.
M72709 mRNA. Translation: AAA35564.1.
M69040 mRNA. Translation: AAA03476.1.
AB062124 mRNA. Translation: BAB93456.1.
BC010264 mRNA. Translation: AAH10264.1.
BC033785 mRNA. Translation: AAH33785.1.

IPI

IPI00215884.
IPI00218591.
IPI00218592.

PIR

A40040.
B40040.
C40040.

RefSeq

NP_008855.1.

UniGene

Hs.68714

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2155N.

IntAct

Q07955. 15 interactions.

PTM databases

PhosphoSite

Q07955.

Proteomic databases

PeptideAtlas

Q07955.

PRIDE

Q07955.

Genome annotation databases

Ensembl

ENSG00000136450. Homo sapiens. [Contig view]

GeneID

6426.

UCSC

uc002ivi.1. human.
uc002ivj.1. human.

Organism-specific databases

GeneCards

GC17M053435.

H-InvDB

HIX0014024.

HGNC

HGNC:10780. SFRS1.

HPA

CAB013073.

MIM

600812. gene.

PharmGKB

PA35696.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q07955.

OMA

Q07955. QVMEDLD.

Enzyme and pathway databases

Reactome

REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1788. Transcription.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q07955.

Bgee

Q07955.

CleanEx

HS_SFRS1.

GermOnline

ENSG00000136450. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.

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 Resources

NextBio

24955.

PMAP-CutDB

Q07955.

SOURCE

Search...

Entry information

Entry name

SFRS1_HUMAN

Accession

Primary (citable) accession number: Q07955
Secondary accession number(s): Q13809

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)