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O75494 (SRS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:SRSF10
Synonyms:FUSIP1, FUSIP2, SFRS13A, TASR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Nucleus speckle. Cytoplasm Ref.3.

Tissue specificity

Widely expressed. Ref.3 Ref.5

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

Sequence similarities

Belongs to the splicing factor SR family.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing, via transesterification reactions

Inferred from direct assay Ref.1. Source: UniProtKB

cytoplasmic transport

Inferred from direct assay Ref.3. Source: UniProtKB

mRNA export from nucleus

Non-traceable author statement Ref.3. Source: UniProtKB

mRNA splice site selection

Inferred from direct assay Ref.1. Source: UniProtKB

mRNA splicing, via spliceosome

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay Ref.3. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

spliceosomal tri-snRNP complex assembly

Non-traceable author statement Ref.3. Source: UniProtKB

   Cellular_componentcytoplasm

Non-traceable author statement Ref.3. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

nucleus

Inferred by curator Ref.1. Source: UniProtKB

   Molecular_functionRNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

RS domain binding

Non-traceable author statement Ref.3. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

unfolded protein binding

Non-traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 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: Contains a phosphoserine at position 168 (By similarity).
Isoform 4 (identifier: O75494-4)

The sequence of this isoform differs from the canonical sequence as follows:
     164-173: RFKHRNRSFS → SQVSKKKNER
     174-183: Missing.
     184-262: Missing.
Note: Contains a phosphoserine at position 158. Contains a phosphoserine at position 160.
Isoform 5 (identifier: O75494-5)

The sequence of this isoform differs from the canonical sequence as follows:
     146-165: NSRPTGRPRRSRSHSDNDRF → KPNCSWNTQYSSAYYTSRKI
     166-173: Missing.
     174-183: Missing.
     184-262: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: O75494-6)

The sequence of this isoform differs from the canonical sequence as follows:
     147-147: Missing.
     165-183: FKHRNRSFSRSKSNSRSRS → PNCSWNTQYSSAYYTSRKI
     184-262: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 262262Serine/arginine-rich splicing factor 10
PRO_0000081593

Regions

Domain10 – 8879RRM
Compositional bias106 – 260155Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue1061Phosphoserine Ref.15
Modified residue1081Phosphoserine Ref.15
Modified residue1291Phosphoserine Ref.11
Modified residue1311Phosphoserine Ref.11 Ref.13 Ref.15
Modified residue1331Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15
Modified residue1581Phosphoserine Ref.13 Ref.15
Modified residue1601Phosphoserine Ref.13 Ref.15

Natural variations

Alternative sequence146 – 16520NSRPT…DNDRF → KPNCSWNTQYSSAYYTSRKI in isoform 5.
VSP_043697
Alternative sequence1471Missing in isoform 2 and isoform 6.
VSP_010421
Alternative sequence164 – 17310RFKHRNRSFS → SQVSKKKNER in isoform 4.
VSP_010422
Alternative sequence165 – 18319FKHRN…SRSRS → PNCSWNTQYSSAYYTSRKI in isoform 3 and isoform 6.
VSP_010424
Alternative sequence166 – 1738Missing in isoform 5.
VSP_043698
Alternative sequence174 – 18310Missing in isoform 4 and isoform 5.
VSP_010423
Alternative sequence184 – 26279Missing in isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_010425

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TASR-1) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 205F95D36CBBFAB4

FASTA26231,301
        10         20         30         40         50         60 
MSRYLRPPNT SLFVRNVADD TRSEDLRREF GRYGPIVDVY VPLDFYTRRP RGFAYVQFED 

        70         80         90        100        110        120 
VRDAEDALHN LDRKWICGRQ IEIQFAQGDR KTPNQMKAKE GRNVYSSSRY DDYDRYRRSR 

       130        140        150        160        170        180 
SRSYERRRSR SRSFDYNYRR SYSPRNSRPT GRPRRSRSHS DNDRFKHRNR SFSRSKSNSR 

       190        200        210        220        230        240 
SRSKSQPKKE MKAKSRSRSA SHTKTRGTSK TDSKTHYKSG SRYEKESRKK EPPRSKSQSR 

       250        260 
SQSRSRSKSR SRSWTSPKSS GH 

« Hide

Isoform 2 [UniParc].

Checksum: A07499B11D4C7570
Show »

FASTA26131,213
Isoform 3 (TASR-2) (SRp38-2) [UniParc].

Checksum: 4AA87CAA9B51A131
Show »

FASTA18322,222
Isoform 4 [UniParc].

Checksum: 4AB40FBF24846495
Show »

FASTA17321,000
Isoform 5 [UniParc].

Checksum: 6CB98688C53A9F69
Show »

FASTA16520,117
Isoform 6 [UniParc].

Checksum: F99356E1D895987D
Show »

FASTA18222,135

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] (ISOFORMS 2; 3 AND 5).
Tissue: Thalamus.
[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. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH SNRNP70 AND TRA2B.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-131 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-131; SER-133; SER-158 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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] [Europe PMC] [Abstract]
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-106; SER-108; SER-131 AND SER-133, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 AND SER-160 (ISOFORM 4), 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.
AK296175 mRNA. Translation: BAG58911.1.
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.
CCDSCCDS30629.1. [O75494-3]
CCDS30630.1. [O75494-1]
CCDS53280.1. [O75494-5]
CCDS53281.1. [O75494-6]
CCDS53282.1. [O75494-2]
CCDS53283.1. [O75494-4]
RefSeqNP_001177934.1. NM_001191005.1. [O75494-2]
NP_001177935.1. NM_001191006.1. [O75494-4]
NP_001177936.1. NM_001191007.1. [O75494-6]
NP_001177938.1. NM_001191009.1. [O75494-5]
NP_006616.1. NM_006625.4. [O75494-3]
NP_473357.1. NM_054016.2. [O75494-1]
UniGeneHs.3530.

3D structure databases

ProteinModelPortalO75494.
SMRO75494. Positions 10-116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115990. 50 interactions.
IntActO75494. 16 interactions.
MINTMINT-5002282.

PTM databases

PhosphoSiteO75494.

Proteomic databases

MaxQBO75494.
PaxDbO75494.
PRIDEO75494.

Protocols and materials databases

DNASU10772.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343255; ENSP00000344149; ENSG00000188529. [O75494-2]
ENST00000344989; ENSP00000342913; ENSG00000188529. [O75494-3]
ENST00000374452; ENSP00000363576; ENSG00000188529. [O75494-4]
ENST00000453840; ENSP00000388991; ENSG00000188529. [O75494-6]
ENST00000484146; ENSP00000419813; ENSG00000188529. [O75494-5]
ENST00000492112; ENSP00000420195; ENSG00000188529. [O75494-1]
GeneID10772.
KEGGhsa:100996657.
hsa:10772.
UCSCuc021oin.1. human. [O75494-4]
uc021oio.1. human. [O75494-3]
uc021oiq.1. human. [O75494-5]
uc021oir.1. human. [O75494-1]
uc021ois.1. human. [O75494-2]

Organism-specific databases

CTD10772.
GeneCardsGC01M024293.
HGNCHGNC:16713. SRSF10.
MIM605221. gene.
neXtProtNX_O75494.
PharmGKBPA28427.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG312850.
HOVERGENHBG107480.
InParanoidO75494.
KOK12900.
OrthoDBEOG73BVG8.
PhylomeDBO75494.
TreeFamTF351864.

Gene expression databases

ArrayExpressO75494.
BgeeO75494.
GenevestigatorO75494.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFUSIP1.
NextBio40903.
PROO75494.
SOURCESearch...

Entry information

Entry nameSRS10_HUMAN
AccessionPrimary (citable) accession number: O75494
Secondary accession number(s): A6NFM6 expand/collapse secondary AC list , A6NI42, A6NIU7, B4DJP9, O60572, Q5JRH9, Q5JRI0, Q5JRI2, Q5JRI3, Q5JRI4, Q96G09, Q96P17
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM