O75494 (SRS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 119.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Serine/arginine-rich splicing factor 10 Alternative name(s): 40 kDa SR-repressor protein Short name=SRrp40 FUS-interacting serine-arginine-rich protein 1 Splicing factor SRp38 Splicing factor, arginine/serine-rich 13A TLS-associated protein with Ser-Arg repeats Short name=TASR Short name=TLS-associated protein with SR repeats TLS-associated serine-arginine protein Short name=TLS-associated SR protein | ||||
| Gene names |
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| 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 | 262 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. May be involved in regulation of alternative splicing in neurons, with isoform 1 acting as a positive and isoform 3 as a negative regulator. Ref.3 Ref.4 Ref.9 |
| Subunit structure | The phosphorylated but not the dephosphorylated form interacts with TRA2B/SFRS10. The dephosphorylated form interacts with SNRNP70. Isoform 1 and isoform 3 interact with FUS C-terminus. Ref.1 Ref.9 |
| Subcellular location | |
| Tissue specificity | |
| Post-translational modification | Phosphorylated. Fully dephosphorylated in mitosis and partially dephosphorylated on heat shock. Isoform 3 is phosphorylated on Ser-168 By similarity. Ref.4 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 |
| Sequence similarities | Belongs to the splicing factor SR family. Contains 1 RRM (RNA recognition motif) domain. |
Ontologies
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O75494-1) Also known as: TASR-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 2 (identifier: O75494-2) The sequence of this isoform differs from the canonical sequence as follows: 147-147: Missing. | ||||||
| Isoform 3 (identifier: O75494-3) Also known as: TASR-2; SRp38-2; The sequence of this isoform differs from the canonical sequence as follows: 165-183: FKHRNRSFSRSKSNSRSRS → PNCSWNTQYSSAYYTSRKI 184-262: Missing. | ||||||
| Note: Phosphorylated on Ser-168 (By similarity). | ||||||
| Isoform 4 (identifier: O75494-4) The sequence of this isoform differs from the canonical sequence as follows: 164-173: RFKHRNRSFS → SQVSKKKNER 174-262: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 262 | 262 | Serine/arginine-rich splicing factor 10 | PRO_0000081593 | |||||
Regions | |||||||||
| Domain | 10 – 88 | 79 | RRM | ||||||
| Compositional bias | 106 – 260 | 155 | Arg/Ser-rich (RS domain) | ||||||
Amino acid modifications | |||||||||
| Modified residue | 110 | 1 | Phosphotyrosine Ref.11 | ||||||
| Modified residue | 119 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 121 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 129 | 1 | Phosphoserine Ref.11 Ref.12 Ref.14 | ||||||
| Modified residue | 131 | 1 | Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 | ||||||
| Modified residue | 133 | 1 | Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 | ||||||
| Modified residue | 156 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 158 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 160 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 235 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 251 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 253 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 255 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 256 | 1 | Phosphoserine Ref.11 | ||||||
Natural variations | |||||||||
| Alternative sequence | 147 | 1 | Missing in isoform 2. | VSP_010421 | |||||
| Alternative sequence | 164 – 173 | 10 | RFKHRNRSFS → SQVSKKKNER in isoform 4. | VSP_010422 | |||||
| Alternative sequence | 165 – 183 | 19 | FKHRN…SRSRS → PNCSWNTQYSSAYYTSRKI in isoform 3. | VSP_010424 | |||||
| Alternative sequence | 174 – 262 | 89 | Missing in isoform 4. | VSP_010423 | |||||
| Alternative sequence | 184 – 262 | 79 | Missing in isoform 3. | VSP_010425 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing." Yang L., Embree L.J., Tsai S., Hickstein D.D. J. Biol. Chem. 273:27761-27764(1998) [PubMed: 9774382] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH FUS. Tissue: Leukemia. |
| [2] | "TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins." Yang L., Embree L.J., Hickstein D.D. Mol. Cell. Biol. 20:3345-3354(2000) [PubMed: 10779324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [3] | "Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing." Cowper A.E., Caceres J.F., Mayeda A., Screaton G.R. J. Biol. Chem. 276:48908-48914(2001) [PubMed: 11684676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [4] | "The SR protein SRp38 represses splicing in M Phase cells." Shin C., Manley J.L. Cell 111:407-417(2002) [PubMed: 12419250] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, PHOSPHORYLATION. |
| [5] | "Characterization and expression of the human gene encoding two translocation liposarcoma protein-associated serine-arginine (TASR) proteins." Clinton J.M., Chansky H.A., Odell D.D., Zielinska-Kwiatkowska A., Hickstein D.D., Yang L. Gene 284:141-147(2002) [PubMed: 11891055] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), TISSUE SPECIFICITY. |
| [6] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). |
| [7] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [8] | "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 1 AND 3). Tissue: Muscle, Placenta and Uterus. |
| [9] | "Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock." Shin C., Feng Y., Manley J.L. Nature 427:553-558(2004) [PubMed: 14765198] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH SNRNP70 AND TRA2B. |
| [10] | "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-133, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [11] | "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 TYR-110; SER-129; SER-131; SER-133; SER-156; SER-158; SER-160; SER-235; SER-251; SER-253; THR-255 AND SER-256, 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-129; SER-131 AND SER-133, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [13] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-133, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "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-129; SER-131 AND SER-133, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [15] | "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-133, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [16] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, MASS SPECTROMETRY. |
| [17] | "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]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF047448 mRNA. Translation: AAC70918.1. AF067730 mRNA. Translation: AAC26727.1. AF449427 mRNA. Translation: AAL57514.1. AY150180 mRNA. Translation: AAN65380.1. AY150181 mRNA. Translation: AAN65381.1. AF419331 mRNA. Translation: AAL16665.1. AF419332 Genomic DNA. Translation: AAL16666.1. AY048592 Genomic DNA. Translation: AAL06098.1. AY048592 Genomic DNA. Translation: AAL06099.1. AK001286 mRNA. Translation: BAA91601.1. AK001656 mRNA. Translation: BAG50956.1. AL590609 Genomic DNA. Translation: CAI14807.1. AL590609 Genomic DNA. Translation: CAI14803.1. AL590609 Genomic DNA. Translation: CAI14805.1. AL590609 Genomic DNA. Translation: CAI14808.1. BC001107 mRNA. Translation: AAH01107.1. BC005039 mRNA. Translation: AAH05039.1. BC010074 mRNA. Translation: AAH10074.1. |
| IPI | IPI00009071. IPI00074587. IPI00386662. IPI00412643. |
| RefSeq | NP_001177934.1. NM_001191005.1. NP_001177935.1. NM_001191006.1. NP_006616.1. NM_006625.4. NP_473357.1. NM_054016.2. XP_003119129.1. XM_003119081.2. XP_003119130.1. XM_003119082.1. XP_003119131.1. XM_003119083.2. |
| UniGene | Hs.3530. Hs.652334. |
3D structure databases | |
| ProteinModelPortal | O75494. |
| SMR | O75494. Positions 6-90. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O75494. 4 interactions. |
| MINT | MINT-5002282. |
| STRING | O75494. |
PTM databases | |
| PhosphoSite | O75494. |
Proteomic databases | |
| PRIDE | O75494. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000374449; ENSP00000363573; ENSG00000215699. ENST00000492112; ENSP00000420195; ENSG00000188529. |
| GeneID | 100505793. 10772. |
| KEGG | hsa:100505793. hsa:10772. |
| UCSC | uc009vqx.1. human. uc009vra.1. human. |
Organism-specific databases | |
| CTD | 10772. |
| GeneCards | GC01M024293. GC01M7J0035. |
| HGNC | HGNC:16713. SRSF10. |
| MIM | 605221. gene. |
| neXtProt | NX_O75494. |
| PharmGKB | PA165752451. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG11471. |
| HOVERGEN | HBG107480. |
| InParanoid | O75494. |
| OMA | FAYVQYT. |
| OrthoDB | EOG4HMJBR. |
| PhylomeDB | O75494. |
Gene expression databases | |
| ArrayExpress | O75494. |
| Bgee | O75494. |
| Genevestigator | O75494. |
| GermOnline | ENSG00000188529. 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. 1 hit. |
| KO | K12900. |
| Pfam | PF00076. RRM_1. 1 hit. [Graphical view] |
| SMART | SM00360. RRM. 1 hit. [Graphical view] |
| PROSITE | PS50102. RRM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 40903. |
| SOURCE | Search... |
Entry information
| Entry name | SRS10_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O75494 Secondary accession number(s): A6NFM6 Q96P17 | ||||||||
| Entry history |
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| 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. | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

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