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Reviewed, UniProtKB/Swiss-Prot Q07955 (SFRS1_HUMAN)

Last modified July 7, 2009. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete 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. 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 processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandRNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processmRNA splice site selection Ref.2

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

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 functionRNA 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...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 248247Splicing factor, arginine/serine-rich 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 Potential
Modified residue21Phosphoserine Ref.19 Ref.22
Modified residue931Omega-N-methylarginine Ref.20
Modified residue971Omega-N-methylated arginine Ref.20
Modified residue1091Omega-N-methylarginine Ref.20
Modified residue1891Phosphotyrosine Ref.19 Ref.21
Modified residue1991Phosphoserine Ref.19 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27
Modified residue2011Phosphoserine Ref.19 Ref.24 Ref.26 Ref.27
Modified residue2021Phosphotyrosine Ref.19 Ref.27
Modified residue2051Phosphoserine Ref.19 Ref.22 Ref.24 Ref.26 Ref.27
Modified residue2311Phosphoserine Ref.19 Ref.27
Modified residue2341Phosphoserine Ref.19 Ref.27
Modified residue2371Phosphotyrosine Ref.19 Ref.27
Modified residue2381Phosphoserine Ref.19 Ref.27

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.30
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.
Mutagenesis162 – 1632FV → SR in FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding. Ref.13
Mutagenesis1621F → A in AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding. Ref.13
Mutagenesis1621F → D: Reduced nucleocytoplasmic shuttling; when associated with D-190. Ref.13
Mutagenesis1801F → D: Reduced nucleocytoplasmic shuttling; when associated with D-162. Ref.13
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.

Checksum: C9502AC70F373EAC
Show »

FASTA29231,999
Isoform ASF-3.

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: 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. 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: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-89.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00215884.
IPI00218591.
IPI00218592.
PIRA40040.
B40040.
C40040.
RefSeqNP_008855.1.
UniGeneHs.68714

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1X4ANMR-A1-96[»]
2O3DNMR-A107-214[»]
3BEGX-ray2.90B105-219[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2155N.
IntActQ07955. 15 interactions.

PTM databases

PhosphoSiteQ07955.

Proteomic databases

PeptideAtlasQ07955.
PRIDEQ07955.

Genome annotation databases

EnsemblENSG00000136450. Homo sapiens. [Contig view]
GeneID6426.
UCSCuc002ivi.1. human.
uc002ivj.1. human.

Organism-specific databases

GeneCardsGC17M053435.
H-InvDBHIX0014024.
HGNCHGNC:10780. SFRS1.
HPACAB013073.
MIM600812. gene.
PharmGKBPA35696.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ07955.
OMAQ07955. QVMEDLD.

Enzyme and pathway databases

ReactomeREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1788. Transcription.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ07955.
BgeeQ07955.
CleanExHS_SFRS1.
GermOnlineENSG00000136450. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio24955.
PMAP-CutDBQ07955.
SOURCESearch...

Entry information

Entry nameSFRS1_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents