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Protein

Serine/arginine-rich splicing factor 6

Gene

SRSF6

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

Functioni

Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing.4 Publications

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • pre-mRNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

  • alternative mRNA splicing, via spliceosome Source: UniProtKB
  • mRNA 3'-end processing Source: Reactome
  • mRNA export from nucleus Source: Reactome
  • mRNA splice site selection Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • negative regulation of cell death Source: MGI
  • negative regulation of keratinocyte differentiation Source: UniProtKB
  • negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • positive regulation of epithelial cell proliferation involved in lung morphogenesis Source: MGI
  • regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  • regulation of keratinocyte proliferation Source: UniProtKB
  • regulation of wound healing Source: UniProtKB
  • RNA export from nucleus Source: Reactome
  • termination of RNA polymerase II transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Repressor

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 6
Alternative name(s):
Pre-mRNA-splicing factor SRP55
Splicing factor, arginine/serine-rich 6
Gene namesi
Name:SRSF6
Synonyms:SFRS6, SRP55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:10788. SRSF6.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi280 – 2801S → A: No effect on regulation of alternative splicing of MAPT/Tau exon 10 by DYRK1A. 1 Publication
Mutagenesisi303 – 3031S → A: Abolishes regulatory effect of DYRK1A on alternative splicing of MAPT/Tau exon 10. 1 Publication
Mutagenesisi316 – 3161S → A: No effect on regulation of alternative splicing of MAPT/Tau exon 10 by DYRK1A. 1 Publication

Organism-specific databases

PharmGKBiPA35704.

Polymorphism and mutation databases

BioMutaiSRSF6.
DMDMi20981728.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Serine/arginine-rich splicing factor 6PRO_0000081930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451PhosphoserineCombined sources
Modified residuei81 – 811PhosphoserineCombined sources
Modified residuei84 – 841PhosphoserineCombined sources
Modified residuei165 – 1651N6-acetyllysineBy similarity
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei303 – 3031Phosphoserine; by DYRK1ACombined sources1 Publication
Modified residuei314 – 3141PhosphoserineCombined sources
Modified residuei316 – 3161PhosphoserineCombined sources

Post-translational modificationi

Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by DYRK1A modulates alternative splice site selection and inhibits the expression of MAPT/Tau exon 10.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13247.
MaxQBiQ13247.
PaxDbiQ13247.
PRIDEiQ13247.
TopDownProteomicsiQ13247-1. [Q13247-1]

PTM databases

iPTMnetiQ13247.
PhosphoSiteiQ13247.
SwissPalmiQ13247.

Expressioni

Gene expression databases

BgeeiQ13247.
CleanExiHS_SFRS6.
GenevisibleiQ13247. HS.

Organism-specific databases

HPAiCAB034889.
HPA029005.

Interactioni

Subunit structurei

Binds SREK1/SFRS12. Interacts with DYRK1A.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LUC7L2Q9Y3833EBI-745230,EBI-352851

Protein-protein interaction databases

BioGridi112329. 60 interactions.
IntActiQ13247. 30 interactions.
MINTiMINT-1474667.
STRINGi9606.ENSP00000244020.

Structurei

3D structure databases

ProteinModelPortaliQ13247.
SMRiQ13247. Positions 3-83, 99-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7272RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini110 – 18374RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi87 – 904Gly-rich (hinge region)
Compositional biasi184 – 343160Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0106. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ13247.
KOiK12893.
OMAiRDGYSYS.
OrthoDBiEOG7H1JPR.
PhylomeDBiQ13247.
TreeFamiTF351335.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform SRP55-1 (identifier: Q13247-1) [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
MPRVYIGRLS YNVREKDIQR FFSGYGRLLE VDLKNGYGFV EFEDSRDADD
60 70 80 90 100
AVYELNGKEL CGERVIVEHA RGPRRDRDGY SYGSRSGGGG YSSRRTSGRD
110 120 130 140 150
KYGPPVRTEY RLIVENLSSR CSWQDLKDFM RQAGEVTYAD AHKERTNEGV
160 170 180 190 200
IEFRSYSDMK RALDKLDGTE INGRNIRLIE DKPRTSHRRS YSGSRSRSRS
210 220 230 240 250
RRRSRSRSRR SSRSRSRSIS KSRSRSRSRS KGRSRSRSKG RKSRSKSKSK
260 270 280 290 300
PKSDRGSHSH SRSRSKDEYE KSRSRSRSRS PKENGKGDIK SKSRSRSQSR
310 320 330 340
SNSPLPVPPS KARSVSPPPK RATSRSRSRS RSKSRSRSRS SSRD
Length:344
Mass (Da):39,587
Last modified:May 15, 2002 - v2
Checksum:i72305506CE948B94
GO
Isoform SRP55-2 (identifier: Q13247-2) [UniParc]FASTAAdd to basket

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

Show »
Length:135
Mass (Da):15,498
Checksum:i2D03ECF8A6F25E19
GO
Isoform SRP55-3 (identifier: Q13247-3) [UniParc]FASTAAdd to basket

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

Show »
Length:335
Mass (Da):38,419
Checksum:i396E9091AD0B7DD1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641R → H in AAA93073 (PubMed:7556075).Curated
Sequence conflicti64 – 641R → H in AAA93071 (PubMed:7556075).Curated
Sequence conflicti64 – 641R → H in AAA93072 (PubMed:7556075).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035489

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei86 – 13550SGGGG…RQAGE → MTNGAEAVSTEAKMTAFPDW PWLFHTLCDPCPMTLWLTLP EAMTTAAFCH in isoform SRP55-2. 2 PublicationsVSP_005869Add
BLAST
Alternative sequencei136 – 344209Missing in isoform SRP55-2. 2 PublicationsVSP_005870Add
BLAST
Alternative sequencei313 – 34432RSVSP…SSSRD → LKLGARFMSQQGTESLYSLA SSC in isoform SRP55-3. 1 PublicationVSP_005871Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13318.1. [Q13247-1]
PIRiS59043.
RefSeqiNP_006266.2. NM_006275.5. [Q13247-1]
UniGeneiHs.684950.
Hs.725336.

Genome annotation databases

EnsembliENST00000244020; ENSP00000244020; ENSG00000124193. [Q13247-1]
ENST00000483871; ENSP00000433544; ENSG00000124193. [Q13247-2]
GeneIDi6431.
KEGGihsa:6431.
UCSCiuc010zwg.3. human. [Q13247-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13318.1. [Q13247-1]
PIRiS59043.
RefSeqiNP_006266.2. NM_006275.5. [Q13247-1]
UniGeneiHs.684950.
Hs.725336.

3D structure databases

ProteinModelPortaliQ13247.
SMRiQ13247. Positions 3-83, 99-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112329. 60 interactions.
IntActiQ13247. 30 interactions.
MINTiMINT-1474667.
STRINGi9606.ENSP00000244020.

PTM databases

iPTMnetiQ13247.
PhosphoSiteiQ13247.
SwissPalmiQ13247.

Polymorphism and mutation databases

BioMutaiSRSF6.
DMDMi20981728.

Proteomic databases

EPDiQ13247.
MaxQBiQ13247.
PaxDbiQ13247.
PRIDEiQ13247.
TopDownProteomicsiQ13247-1. [Q13247-1]

Protocols and materials databases

DNASUi6431.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244020; ENSP00000244020; ENSG00000124193. [Q13247-1]
ENST00000483871; ENSP00000433544; ENSG00000124193. [Q13247-2]
GeneIDi6431.
KEGGihsa:6431.
UCSCiuc010zwg.3. human. [Q13247-1]

Organism-specific databases

CTDi6431.
GeneCardsiSRSF6.
HGNCiHGNC:10788. SRSF6.
HPAiCAB034889.
HPA029005.
MIMi601944. gene.
neXtProtiNX_Q13247.
PharmGKBiPA35704.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0106. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ13247.
KOiK12893.
OMAiRDGYSYS.
OrthoDBiEOG7H1JPR.
PhylomeDBiQ13247.
TreeFamiTF351335.

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.

Miscellaneous databases

ChiTaRSiSRSF6. human.
GeneWikiiSFRS6.
GenomeRNAii6431.
PROiQ13247.
SOURCEiSearch...

Gene expression databases

BgeeiQ13247.
CleanExiHS_SFRS6.
GenevisibleiQ13247. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SREK1.
  8. "SRp55 is a regulator of calcitonin/CGRP alternative RNA splicing."
    Tran Q., Roesser J.R.
    Biochemistry 42:951-957(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-314 AND SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299 AND SER-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-303; SER-314 AND SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-84; SER-303; SER-314 AND SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) modulates serine/arginine-rich protein 55 (SRp55)-promoted Tau exon 10 inclusion."
    Yin X., Jin N., Gu J., Shi J., Zhou J., Gong C.X., Iqbal K., Grundke-Iqbal I., Liu F.
    J. Biol. Chem. 287:30497-30506(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DYRK1A, FUNCTION, PHOSPHORYLATION AT SER-303, MUTAGENESIS OF SER-280; SER-303 AND SER-316.
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Splicing factor SRSF6 promotes hyperplasia of sensitized skin."
    Jensen M.A., Wilkinson J.E., Krainer A.R.
    Nat. Struct. Mol. Biol. 21:189-197(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-145.

Entry informationi

Entry nameiSRSF6_HUMAN
AccessioniPrimary (citable) accession number: Q13247
Secondary accession number(s): B7Z6J3
, E1P5W6, Q13244, Q13245, Q96J06, Q9UJB8, Q9Y3N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 15, 2002
Last modified: June 8, 2016
This is version 173 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.