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Protein

Serine/arginine-rich splicing factor 10

Gene

SRSF10

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

Functioni

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.3 Publications

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: UniProtKB
  4. RS domain binding Source: UniProtKB
  5. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. cytoplasmic transport Source: UniProtKB
  2. mRNA export from nucleus Source: UniProtKB
  3. mRNA splice site selection Source: UniProtKB
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  6. regulation of transcription, DNA-templated Source: UniProtKB
  7. RNA splicing, via transesterification reactions Source: UniProtKB
  8. spliceosomal tri-snRNP complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:SRSF10
Synonyms:FUSIP1, FUSIP2, SFRS13A, TASR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16713. SRSF10.

Subcellular locationi

Nucleus speckle 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nuclear speck Source: UniProtKB-SubCell
  3. nucleoplasm Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Serine/arginine-rich splicing factor 10PRO_0000081593Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphoserine1 Publication
Modified residuei108 – 1081Phosphoserine1 Publication
Modified residuei129 – 1291Phosphoserine1 Publication
Modified residuei131 – 1311Phosphoserine3 Publications
Modified residuei133 – 1331Phosphoserine4 Publications
Modified residuei158 – 1581Phosphoserine1 Publication
Modified residuei160 – 1601Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated. Fully dephosphorylated in mitosis and partially dephosphorylated on heat shock. Isoform 3 is phosphorylated on Ser-168 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75494.
PaxDbiO75494.
PRIDEiO75494.

PTM databases

PhosphoSiteiO75494.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiO75494.
ExpressionAtlasiO75494. baseline and differential.
GenevestigatoriO75494.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi115990. 56 interactions.
IntActiO75494. 16 interactions.
MINTiMINT-5002282.

Structurei

3D structure databases

ProteinModelPortaliO75494.
SMRiO75494. Positions 10-116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 8879RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi106 – 260155Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG312850.
GeneTreeiENSGT00700000104403.
HOVERGENiHBG107480.
InParanoidiO75494.
KOiK12900.
OMAiQRERSIS.
OrthoDBiEOG73BVG8.
PhylomeDBiO75494.
TreeFamiTF351864.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75494-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSRYLRPPNT SLFVRNVADD TRSEDLRREF GRYGPIVDVY VPLDFYTRRP
60 70 80 90 100
RGFAYVQFED VRDAEDALHN LDRKWICGRQ IEIQFAQGDR KTPNQMKAKE
110 120 130 140 150
GRNVYSSSRY DDYDRYRRSR SRSYERRRSR SRSFDYNYRR SYSPRNSRPT
160 170 180 190 200
GRPRRSRSHS DNDRFKHRNR SFSRSKSNSR SRSKSQPKKE MKAKSRSRSA
210 220 230 240 250
SHTKTRGTSK TDSKTHYKSG SRYEKESRKK EPPRSKSQSR SQSRSRSKSR
260
SRSWTSPKSS GH
Length:262
Mass (Da):31,301
Last modified:November 1, 1998 - v1
Checksum:i205F95D36CBBFAB4
GO
Isoform 2 (identifier: O75494-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-147: Missing.

Show »
Length:261
Mass (Da):31,213
Checksum:iA07499B11D4C7570
GO
Isoform 3 (identifier: O75494-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:183
Mass (Da):22,222
Checksum:i4AA87CAA9B51A131
GO
Isoform 4 (identifier: O75494-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:173
Mass (Da):21,000
Checksum:i4AB40FBF24846495
GO
Isoform 5 (identifier: O75494-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:165
Mass (Da):20,117
Checksum:i6CB98688C53A9F69
GO
Isoform 6 (identifier: O75494-6) [UniParc]FASTAAdd to Basket

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.

Show »
Length:182
Mass (Da):22,135
Checksum:iF99356E1D895987D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei146 – 16520NSRPT…DNDRF → KPNCSWNTQYSSAYYTSRKI in isoform 5. 1 PublicationVSP_043697Add
BLAST
Alternative sequencei147 – 1471Missing in isoform 2 and isoform 6. 1 PublicationVSP_010421
Alternative sequencei164 – 17310RFKHRNRSFS → SQVSKKKNER in isoform 4. CuratedVSP_010422
Alternative sequencei165 – 18319FKHRN…SRSRS → PNCSWNTQYSSAYYTSRKI in isoform 3 and isoform 6. 4 PublicationsVSP_010424Add
BLAST
Alternative sequencei166 – 1738Missing in isoform 5. 1 PublicationVSP_043698
Alternative sequencei174 – 18310Missing in isoform 4 and isoform 5. 1 PublicationVSP_010423
Alternative sequencei184 – 26279Missing in isoform 3, isoform 4, isoform 5 and isoform 6. 4 PublicationsVSP_010425Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30629.1. [O75494-3]
CCDS30630.1. [O75494-1]
CCDS53280.1. [O75494-5]
CCDS53281.1. [O75494-6]
CCDS53282.1. [O75494-2]
CCDS53283.1. [O75494-4]
RefSeqiNP_001177934.1. NM_001191005.2. [O75494-2]
NP_001177935.1. NM_001191006.2. [O75494-4]
NP_001177936.1. NM_001191007.2. [O75494-6]
NP_001177938.1. NM_001191009.2. [O75494-5]
NP_006616.1. NM_006625.5. [O75494-3]
NP_473357.1. NM_054016.3. [O75494-1]
UniGeneiHs.3530.

Genome annotation databases

EnsembliENST00000343255; 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]
GeneIDi10772.
KEGGihsa:10772.
UCSCiuc021oin.1. human. [O75494-4]
uc021oio.1. human. [O75494-3]
uc021oiq.1. human. [O75494-5]
uc021oir.1. human. [O75494-1]
uc021ois.1. human. [O75494-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30629.1. [O75494-3]
CCDS30630.1. [O75494-1]
CCDS53280.1. [O75494-5]
CCDS53281.1. [O75494-6]
CCDS53282.1. [O75494-2]
CCDS53283.1. [O75494-4]
RefSeqiNP_001177934.1. NM_001191005.2. [O75494-2]
NP_001177935.1. NM_001191006.2. [O75494-4]
NP_001177936.1. NM_001191007.2. [O75494-6]
NP_001177938.1. NM_001191009.2. [O75494-5]
NP_006616.1. NM_006625.5. [O75494-3]
NP_473357.1. NM_054016.3. [O75494-1]
UniGeneiHs.3530.

3D structure databases

ProteinModelPortaliO75494.
SMRiO75494. Positions 10-116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115990. 56 interactions.
IntActiO75494. 16 interactions.
MINTiMINT-5002282.

PTM databases

PhosphoSiteiO75494.

Proteomic databases

MaxQBiO75494.
PaxDbiO75494.
PRIDEiO75494.

Protocols and materials databases

DNASUi10772.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343255; 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]
GeneIDi10772.
KEGGihsa:10772.
UCSCiuc021oin.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

CTDi10772.
GeneCardsiGC01M024293.
HGNCiHGNC:16713. SRSF10.
MIMi605221. gene.
neXtProtiNX_O75494.
PharmGKBiPA28427.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG312850.
GeneTreeiENSGT00700000104403.
HOVERGENiHBG107480.
InParanoidiO75494.
KOiK12900.
OMAiQRERSIS.
OrthoDBiEOG73BVG8.
PhylomeDBiO75494.
TreeFamiTF351864.

Miscellaneous databases

GeneWikiiFUSIP1.
GenomeRNAii10772.
NextBioi40903.
PROiO75494.
SOURCEiSearch...

Gene expression databases

BgeeiO75494.
ExpressionAtlasiO75494. baseline and differential.
GenevestigatoriO75494.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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].

Entry informationi

Entry nameiSRS10_HUMAN
AccessioniPrimary (citable) accession number: O75494
Secondary accession number(s): A6NFM6
, A6NI42, A6NIU7, B4DJP9, O60572, Q5JRH9, Q5JRI0, Q5JRI2, Q5JRI3, Q5JRI4, Q96G09, Q96P17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1998
Last modified: January 7, 2015
This is version 150 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 1
    Human chromosome 1: 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

External Data

Dasty 3

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 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.