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Protein

Serine/arginine-rich splicing factor 9

Gene

SRSF9

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 can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10.8 Publications

GO - Molecular functioni

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

GO - Biological processi

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-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 9
Alternative name(s):
Pre-mRNA-splicing factor SRp30C
Splicing factor, arginine/serine-rich 9
Gene namesi
Name:SRSF9
Synonyms:SFRS9, SRP30C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:10791. SRSF9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35707.

Polymorphism and mutation databases

BioMutaiSRSF9.
DMDMi3929377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 221221Serine/arginine-rich splicing factor 9PRO_0000081935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891PhosphoserineCombined sources
Modified residuei192 – 1921PhosphotyrosineCombined sources
Modified residuei193 – 1931PhosphoserineCombined sources
Modified residuei195 – 1951PhosphoserineCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei208 – 2081PhosphoserineCombined sources
Modified residuei211 – 2111PhosphoserineCombined sources
Modified residuei214 – 2141PhosphotyrosineCombined sources
Modified residuei216 – 2161PhosphoserineCombined sources

Post-translational modificationi

Extensively phosphorylated on serine residues in the RS domain.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13242.
MaxQBiQ13242.
PaxDbiQ13242.
PeptideAtlasiQ13242.
PRIDEiQ13242.
TopDownProteomicsiQ13242.

PTM databases

iPTMnetiQ13242.
PhosphoSiteiQ13242.

Expressioni

Tissue specificityi

Expressed at high levels in the heart, kidney, pancreas and placenta, and at lower levels in the brain, liver, lung and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ13242.
CleanExiHS_SFRS9.
ExpressionAtlasiQ13242. baseline and differential.
GenevisibleiQ13242. HS.

Organism-specific databases

HPAiHPA049849.

Interactioni

Subunit structurei

Interacts with KHDRBS3 (By similarity). Interacts with NOL3/ARC/NOP30, NSEP1/YB-1/YB1, SAFB/SAFB1, SRSF6/SFRS6, TRA2B/SFRS10 and C1QBP. May also interact with DUSP11/PIR1.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HABP4Q5JVS02EBI-2949710,EBI-523625

Protein-protein interaction databases

BioGridi114231. 76 interactions.
DIPiDIP-40741N.
IntActiQ13242. 21 interactions.
MINTiMINT-133565.
STRINGi9606.ENSP00000229390.

Structurei

3D structure databases

ProteinModelPortaliQ13242.
SMRiQ13242. Positions 9-100, 104-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 8976RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini111 – 18777RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 20013Interacts with SAFB1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi91 – 10010Gly-rich (hinge region)
Compositional biasi188 – 20013Arg/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

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ13242.
KOiK12890.
OMAiTHERNSQ.
OrthoDBiEOG76X620.
PhylomeDBiQ13242.
TreeFamiTF106261.

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. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13242-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGWADERGG EGDGRIYVGN LPTDVREKDL EDLFYKYGRI REIELKNRHG
60 70 80 90 100
LVPFAFVRFE DPRDAEDAIY GRNGYDYGQC RLRVEFPRTY GGRGGWPRGG
110 120 130 140 150
RNGPPTRRSD FRVLVSGLPP SGSWQDLKDH MREAGDVCYA DVQKDGVGMV
160 170 180 190 200
EYLRKEDMEY ALRKLDDTKF RSHEGETSYI RVYPERSTSY GYSRSRSGSR
210 220
GRDSPYQSRG SPHYFSPFRP Y
Length:221
Mass (Da):25,542
Last modified:November 1, 1996 - v1
Checksum:i1EE7BD8601CD80C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30825 mRNA. Translation: AAA93069.1.
U87279, U87277, U87278 Genomic DNA. Translation: AAD00626.1.
AL021546 Genomic DNA. Translation: CAA16498.1.
BC093971 mRNA. Translation: AAH93971.1.
BC093973 mRNA. Translation: AAH93973.1.
CCDSiCCDS9199.1.
PIRiS59075.
RefSeqiNP_003760.1. NM_003769.2.
UniGeneiHs.706889.
Hs.744094.

Genome annotation databases

EnsembliENST00000229390; ENSP00000229390; ENSG00000111786.
GeneIDi8683.
KEGGihsa:8683.
UCSCiuc001tyi.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30825 mRNA. Translation: AAA93069.1.
U87279, U87277, U87278 Genomic DNA. Translation: AAD00626.1.
AL021546 Genomic DNA. Translation: CAA16498.1.
BC093971 mRNA. Translation: AAH93971.1.
BC093973 mRNA. Translation: AAH93973.1.
CCDSiCCDS9199.1.
PIRiS59075.
RefSeqiNP_003760.1. NM_003769.2.
UniGeneiHs.706889.
Hs.744094.

3D structure databases

ProteinModelPortaliQ13242.
SMRiQ13242. Positions 9-100, 104-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114231. 76 interactions.
DIPiDIP-40741N.
IntActiQ13242. 21 interactions.
MINTiMINT-133565.
STRINGi9606.ENSP00000229390.

PTM databases

iPTMnetiQ13242.
PhosphoSiteiQ13242.

Polymorphism and mutation databases

BioMutaiSRSF9.
DMDMi3929377.

Proteomic databases

EPDiQ13242.
MaxQBiQ13242.
PaxDbiQ13242.
PeptideAtlasiQ13242.
PRIDEiQ13242.
TopDownProteomicsiQ13242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229390; ENSP00000229390; ENSG00000111786.
GeneIDi8683.
KEGGihsa:8683.
UCSCiuc001tyi.4. human.

Organism-specific databases

CTDi8683.
GeneCardsiSRSF9.
HGNCiHGNC:10791. SRSF9.
HPAiHPA049849.
MIMi601943. gene.
neXtProtiNX_Q13242.
PharmGKBiPA35707.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ13242.
KOiK12890.
OMAiTHERNSQ.
OrthoDBiEOG76X620.
PhylomeDBiQ13242.
TreeFamiTF106261.

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-72187. mRNA 3'-end processing.

Miscellaneous databases

ChiTaRSiSRSF9. human.
GeneWikiiSFRS9.
GenomeRNAii8683.
NextBioi32569.
PROiQ13242.
SOURCEiSearch...

Gene expression databases

BgeeiQ13242.
CleanExiHS_SFRS9.
ExpressionAtlasiQ13242. baseline and differential.
GenevisibleiQ13242. 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. 1 hit.
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], FUNCTION.
    Tissue: Colon.
  2. "Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12."
    Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "PIR1, a novel phosphatase that exhibits high affinity to RNA ribonucleoprotein complexes."
    Yuan Y., Li D.-M., Sun H.
    J. Biol. Chem. 273:20347-20353(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP11.
  6. Cited for: INTERACTION WITH SAFB/SAFB1.
  7. "The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation."
    Petersen-Mahrt S.K., Estmer C., Ohrmalm C., Matthews D.A., Russell W.C., Akusjarvi G.
    EMBO J. 18:1014-1024(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1QBP.
  8. "Alternative splicing determines the intracellular localization of the novel nuclear protein Nop30 and its interaction with the splicing factor SRp30c."
    Stoss O., Schwaiger F.-W., Cooper T.A., Stamm S.
    J. Biol. Chem. 274:10951-10962(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOL3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Stress-induced nuclear bodies are sites of accumulation of pre-mRNA processing factors."
    Denegri M., Chiodi I., Corioni M., Cobianchi F., Riva S., Biamonti G.
    Mol. Biol. Cell 12:3502-3514(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAFB/SAFB1, SUBCELLULAR LOCATION.
  10. "SRp30c-dependent stimulation of survival motor neuron (SMN) exon 7 inclusion is facilitated by a direct interaction with hTra2 beta 1."
    Young P.J., DiDonato C.J., Hu D., Kothary R., Androphy E.J., Lorson C.L.
    Hum. Mol. Genet. 11:577-587(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRA2B.
  11. "SRp30c is a repressor of 3' splice site utilization."
    Simard M.J., Chabot B.
    Mol. Cell. Biol. 22:4001-4010(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  12. "Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection."
    Raffetseder U., Frye B., Rauen T., Juerchott K., Royer H.-D., Jansen P.L., Mertens P.R.
    J. Biol. Chem. 278:18241-18248(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NSEP1, SUBCELLULAR LOCATION.
  13. "Tra2 beta, SF2/ASF and SRp30c modulate the function of an exonic splicing enhancer in exon 10 of tau pre-mRNA."
    Kondo S., Yamamoto N., Murakami T., Okumura M., Mayeda A., Imaizumi K.
    Genes Cells 9:121-130(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "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.
  15. "Tau exons 2 and 10, which are misregulated in neurodegenerative diseases, are partly regulated by silencers which bind a SRp30c SRp55 complex that either recruits or antagonizes htra2beta1."
    Wang Y., Wang J., Gao L., Lafyatis R., Stamm S., Andreadis A.
    J. Biol. Chem. 280:14230-14239(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRSF6 AND TRA2B.
  16. "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-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; TYR-192; SER-195; SER-211 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "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-204; SER-211 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-189; SER-193; SER-204; SER-208; SER-211 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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-211 AND TYR-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSRSF9_HUMAN
AccessioniPrimary (citable) accession number: Q13242
Secondary accession number(s): Q52LD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 165 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.