Q13247 (SRSF6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/arginine-rich splicing factor 6

Alternative name(s):
Pre-mRNA-splicing factor SRP55
Splicing factor, arginine/serine-rich 6

Gene names

Name:	SRSF6
Synonyms:	SFRS6, SRP55

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. Ref.8
Subunit structure	Binds SREK1/SFRS12.
Subcellular location	Nucleus.
Post-translational modification	Extensively phosphorylated on serine residues in the RS domain By similarity. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
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	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	mRNA 3'-end processing Traceable author statement. Source: Reactome mRNA export from nucleus Traceable author statement. Source: Reactome mRNA splice site selection Traceable author statement. Source: ProtInc negative regulation of nuclear mRNA splicing, via spliceosome Inferred from direct assay Ref.8. Source: UniProtKB termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular component	nucleoplasm Traceable author statement. Source: Reactome
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform SRP55-1 (identifier: Q13247-1)

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 SRP55-2 (identifier: Q13247-2)

The sequence of this isoform differs from the canonical sequence as follows:
     86-135: SGGGGYSSRR...LKDFMRQAGE → MTNGAEAVST...EAMTTAAFCH
     136-344: Missing.

Isoform SRP55-3 (identifier: Q13247-3)

The sequence of this isoform differs from the canonical sequence as follows:
     313-344: RSVSPPPKRATSRSRSRSRSKSRSRSRSSSRD → LKLGARFMSQQGTESLYSLASSC

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	Serine/arginine-rich splicing factor 6		PRO_0000081930
Regions
	Domain	1 – 72	72	RRM 1
	Domain	110 – 183	74	RRM 2
	Compositional bias	87 – 90	4	Gly-rich (hinge region)
	Compositional bias	184 – 343	160	Arg/Ser-rich (RS domain)
Amino acid modifications
	Modified residue	45	1	Phosphoserine Ref.10 Ref.17
	Modified residue	101	1	N6-acetyllysine Ref.18
	Modified residue	259	1	Phosphoserine Ref.10
	Modified residue	297	1	Phosphoserine Ref.10 Ref.15
	Modified residue	299	1	Phosphoserine Ref.10 Ref.15
	Modified residue	301	1	Phosphoserine Ref.9 Ref.10 Ref.16
	Modified residue	303	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	314	1	Phosphoserine Ref.9 Ref.10 Ref.12 Ref.15 Ref.16
	Modified residue	316	1	Phosphoserine Ref.9 Ref.10 Ref.12 Ref.15 Ref.16
Natural variations
	Alternative sequence	86 – 135	50	SGGGG…RQAGE → MTNGAEAVSTEAKMTAFPDW PWLFHTLCDPCPMTLWLTLP EAMTTAAFCH in isoform SRP55-2.		VSP_005869
	Alternative sequence	136 – 344	209	Missing in isoform SRP55-2.		VSP_005870
	Alternative sequence	313 – 344	32	RSVSP…SSSRD → LKLGARFMSQQGTESLYSLA SSC in isoform SRP55-3.		VSP_005871
	Natural variant	145	1	R → Q in a colorectal cancer sample; somatic mutation. Ref.20		VAR_035489
Experimental info
	Sequence conflict	64	1	R → H in AAA93073. Ref.1
	Sequence conflict	64	1	R → H in AAA93071. Ref.1
	Sequence conflict	64	1	R → H in AAA93072. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform SRP55-1 [UniParc]. Last modified May 15, 2002. Version 2. Checksum: 72305506CE948B94	FASTA	344	39,587
	10 20 30 40 50 60 MPRVYIGRLS YNVREKDIQR FFSGYGRLLE VDLKNGYGFV EFEDSRDADD AVYELNGKEL 70 80 90 100 110 120 CGERVIVEHA RGPRRDRDGY SYGSRSGGGG YSSRRTSGRD KYGPPVRTEY RLIVENLSSR 130 140 150 160 170 180 CSWQDLKDFM RQAGEVTYAD AHKERTNEGV IEFRSYSDMK RALDKLDGTE INGRNIRLIE 190 200 210 220 230 240 DKPRTSHRRS YSGSRSRSRS RRRSRSRSRR SSRSRSRSIS KSRSRSRSRS KGRSRSRSKG 250 260 270 280 290 300 RKSRSKSKSK PKSDRGSHSH SRSRSKDEYE KSRSRSRSRS PKENGKGDIK SKSRSRSQSR 310 320 330 340 SNSPLPVPPS KARSVSPPPK RATSRSRSRS RSKSRSRSRS SSRD
	Isoform SRP55-2 [UniParc]. Checksum: 2D03ECF8A6F25E19	FASTA	135	15,498
	10 20 30 40 50 60 MPRVYIGRLS YNVREKDIQR FFSGYGRLLE VDLKNGYGFV EFEDSRDADD AVYELNGKEL 70 80 90 100 110 120 CGERVIVEHA RGPRRDRDGY SYGSRMTNGA EAVSTEAKMT AFPDWPWLFH TLCDPCPMTL 130 WLTLPEAMTT AAFCH
	Isoform SRP55-3 [UniParc]. Checksum: 396E9091AD0B7DD1	FASTA	335	38,419
	10 20 30 40 50 60 MPRVYIGRLS YNVREKDIQR FFSGYGRLLE VDLKNGYGFV EFEDSRDADD AVYELNGKEL 70 80 90 100 110 120 CGERVIVEHA RGPRRDRDGY SYGSRSGGGG YSSRRTSGRD KYGPPVRTEY RLIVENLSSR 130 140 150 160 170 180 CSWQDLKDFM RQAGEVTYAD AHKERTNEGV IEFRSYSDMK RALDKLDGTE INGRNIRLIE 190 200 210 220 230 240 DKPRTSHRRS YSGSRSRSRS RRRSRSRSRR SSRSRSRSIS KSRSRSRSRS KGRSRSRSKG 250 260 270 280 290 300 RKSRSKSKSK PKSDRGSHSH SRSRSKDEYE KSRSRSRSRS PKENGKGDIK SKSRSRSQSR 310 320 330 SNSPLPVPPS KALKLGARFM SQQGTESLYS LASSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of three members of the human SR family of pre-mRNA splicing factors." Screaton G.R., Caceres J.F., Mayeda A., Bell M.V., Plebanski M., Jackson D.G., Bell J.I., Krainer A.R. EMBO J. 14:4336-4349(1995) [PubMed: 7556075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SRP55-1; SRP55-2 AND SRP55-3). Tissue: Colon.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP55-2). Tissue: Placenta.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[5]	"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] (ISOFORM SRP55-1). Tissue: Placenta.
[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 21-27 AND 47-55.
[7]	"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 SREK1.
[8]	"Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors." Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A. J. Neurochem. 88:1078-1090(2004) [PubMed: 15009664] [Abstract] Cited for: FUNCTION.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-314 AND SER-316, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-45; SER-259; SER-297; SER-299; SER-301; SER-303; SER-314 AND SER-316, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-303, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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-303; SER-314 AND SER-316, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-303, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-297; SER-299; SER-303; SER-314 AND SER-316, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-303; SER-314 AND SER-316, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-303, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, MASS SPECTROMETRY.
[19]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"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] GLN-145.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U30883 mRNA. Translation: AAA93073.1. U30828 mRNA. Translation: AAA93071.1. U30829 mRNA. Translation: AAA93072.1. AK300411 mRNA. Translation: BAH13279.1. AL031681 Genomic DNA. Translation: CAB43960.1. CH471077 Genomic DNA. Translation: EAW75964.1. CH471077 Genomic DNA. Translation: EAW75967.1. BC006832 mRNA. Translation: AAH06832.1.
IPI	IPI00012345. IPI00018203. IPI00215879.
PIR	S59043.
RefSeq	NP_006266.2. NM_006275.5.
UniGene	Hs.708261.
3D structure databases
ProteinModelPortal	Q13247.
SMR	Q13247. Positions 2-184.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13247. 6 interactions.
MINT	MINT-1474667.
STRING	Q13247.
PTM databases
PhosphoSite	Q13247.
Polymorphism databases
DMDM	20981728.
Proteomic databases
PRIDE	Q13247.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000244020; ENSP00000244020; ENSG00000124193. ENST00000328748; ENSP00000362251; ENSG00000124193.
GeneID	6431.
KEGG	hsa:6431.
UCSC	uc002xkj.1. human.
Organism-specific databases
CTD	6431.
GeneCards	GC20P042087.
H-InvDB	HIX0015826.
HGNC	HGNC:10788. SRSF6.
HPA	CAB034889. HPA029005.
MIM	601944. gene.
neXtProt	NX_Q13247.
PharmGKB	PA165392673. PA35704.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20171.
GeneTree	ENSGT00560000076885.
HOGENOM	HBG756718.
HOVERGEN	HBG002295.
InParanoid	Q13247.
OMA	XGGGGYS.
OrthoDB	EOG41C6X9.
PhylomeDB	Q13247.
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	Q13247.
Bgee	Q13247.
CleanEx	HS_SFRS6.
Genevestigator	Q13247.
GermOnline	ENSG00000124193. Homo sapiens.
Family and domain databases
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
KO	K12893.
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
NextBio	24979.
SOURCE	Search...

Entry information

Entry name

SRSF6_HUMAN

Accession

Primary (citable) accession number: Q13247
Secondary accession number(s): B7Z6J3 , E1P5W6, Q13244, Q13245, Q96J06, Q9UJB8, Q9Y3N7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 15, 2002
Last modified:	January 25, 2012
This is version 127 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.