SRSF8_HUMAN
ID SRSF8_HUMAN Reviewed; 282 AA.
AC Q9BRL6; B2R6B8; Q6PF01; Q96TA3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Serine/arginine-rich splicing factor 8;
DE AltName: Full=Pre-mRNA-splicing factor SRP46;
DE Short=Splicing factor SRp46;
DE AltName: Full=Splicing factor, arginine/serine-rich 2B;
GN Name=SRSF8; Synonyms=SFRS2B, SRP46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION,
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta, and Thymus;
RX PubMed=9671500; DOI=10.1128/mcb.18.8.4924;
RA Soret J., Gattoni R., Guyon C., Sureau A., Popielarz M., Le Rouzic E.,
RA Dumon S., Apiou F., Dutrillaux B., Voss H., Ansorge W., Stevenin J.,
RA Perbal B.;
RT "Characterization of SRp46, a novel human SR splicing factor encoded by a
RT PR264/SC35 retropseudogene.";
RL Mol. Cell. Biol. 18:4924-4934(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-26; SER-156; SER-158;
RP SER-171; SER-173 AND SER-196, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP STRUCTURE BY NMR OF 8-97.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA-binding domain in SRP46 splicing factor.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Involved in pre-mRNA alternative splicing.
CC {ECO:0000269|PubMed:9671500}.
CC -!- INTERACTION:
CC Q9BRL6; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-6380719, EBI-539478;
CC Q9BRL6; P78362: SRPK2; NbExp=2; IntAct=EBI-6380719, EBI-593303;
CC Q9BRL6-2; P49761: CLK3; NbExp=3; IntAct=EBI-10976394, EBI-745579;
CC Q9BRL6-2; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-10976394, EBI-10176379;
CC Q9BRL6-2; P78362: SRPK2; NbExp=3; IntAct=EBI-10976394, EBI-593303;
CC Q9BRL6-2; P84103: SRSF3; NbExp=3; IntAct=EBI-10976394, EBI-372557;
CC Q9BRL6-2; P62995: TRA2B; NbExp=3; IntAct=EBI-10976394, EBI-725485;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9671500}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRL6-2; Sequence=VSP_028026;
CC -!- TISSUE SPECIFICITY: Strongly expressed in pancreas, spleen and
CC prostate. Weakly expressed in lung, liver and thymus.
CC {ECO:0000269|PubMed:9671500}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AF031165; AAK54350.1; -; Genomic_DNA.
DR EMBL; AF031166; AAK54351.1; -; mRNA.
DR EMBL; AK023379; BAG51186.1; -; mRNA.
DR EMBL; AK312514; BAG35415.1; -; mRNA.
DR EMBL; CH471065; EAW66954.1; -; Genomic_DNA.
DR EMBL; BC057783; AAH57783.1; -; mRNA.
DR CCDS; CCDS73370.1; -. [Q9BRL6-1]
DR RefSeq; NP_115285.1; NM_032102.3. [Q9BRL6-1]
DR RefSeq; XP_016872631.1; XM_017017142.1. [Q9BRL6-1]
DR PDB; 2DNM; NMR; -; A=8-97.
DR PDBsum; 2DNM; -.
DR AlphaFoldDB; Q9BRL6; -.
DR SMR; Q9BRL6; -.
DR BioGRID; 116132; 178.
DR IntAct; Q9BRL6; 36.
DR STRING; 9606.ENSP00000480140; -.
DR iPTMnet; Q9BRL6; -.
DR PhosphoSitePlus; Q9BRL6; -.
DR BioMuta; SRSF8; -.
DR DMDM; 74761217; -.
DR EPD; Q9BRL6; -.
DR jPOST; Q9BRL6; -.
DR MassIVE; Q9BRL6; -.
DR MaxQB; Q9BRL6; -.
DR PeptideAtlas; Q9BRL6; -.
DR PRIDE; Q9BRL6; -.
DR ProteomicsDB; 78785; -. [Q9BRL6-1]
DR ProteomicsDB; 78786; -. [Q9BRL6-2]
DR Antibodypedia; 73322; 130 antibodies from 20 providers.
DR DNASU; 10929; -.
DR Ensembl; ENST00000587424.3; ENSP00000480140.1; ENSG00000263465.5. [Q9BRL6-1]
DR GeneID; 10929; -.
DR KEGG; hsa:10929; -.
DR MANE-Select; ENST00000587424.3; ENSP00000480140.1; NM_032102.4; NP_115285.1.
DR UCSC; uc031ybj.2; human. [Q9BRL6-1]
DR CTD; 10929; -.
DR DisGeNET; 10929; -.
DR GeneCards; SRSF8; -.
DR HGNC; HGNC:16988; SRSF8.
DR HPA; ENSG00000263465; Low tissue specificity.
DR MIM; 603269; gene.
DR neXtProt; NX_Q9BRL6; -.
DR OpenTargets; ENSG00000263465; -.
DR PharmGKB; PA165543687; -.
DR VEuPathDB; HostDB:ENSG00000263465; -.
DR eggNOG; KOG4207; Eukaryota.
DR GeneTree; ENSGT00940000154883; -.
DR HOGENOM; CLU_012062_10_3_1; -.
DR InParanoid; Q9BRL6; -.
DR OMA; FHDQRDA; -.
DR PathwayCommons; Q9BRL6; -.
DR SignaLink; Q9BRL6; -.
DR BioGRID-ORCS; 10929; 12 hits in 187 CRISPR screens.
DR ChiTaRS; SRSF8; human.
DR EvolutionaryTrace; Q9BRL6; -.
DR GenomeRNAi; 10929; -.
DR Pharos; Q9BRL6; Tbio.
DR PRO; PR:Q9BRL6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BRL6; protein.
DR Bgee; ENSG00000263465; Expressed in tendon of biceps brachii and 219 other tissues.
DR ExpressionAtlas; Q9BRL6; baseline and differential.
DR Genevisible; Q9BRL6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..282
FT /note="Serine/arginine-rich splicing factor 8"
FT /id="PRO_0000304412"
FT DOMAIN 14..92
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 91..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..152
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 114..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028026"
FT CONFLICT 156
FT /note="S -> G (in Ref. 4; AAH57783)"
FT /evidence="ECO:0000305"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2DNM"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2DNM"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2DNM"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:2DNM"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2DNM"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:2DNM"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:2DNM"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2DNM"
SQ SEQUENCE 282 AA; 32288 MW; A6FB97C88247EE0C CRC64;
MSCGRPPPDV DGMITLKVDN LTYRTSPDSL RRVFEKYGRV GDVYIPREPH TKAPRGFAFV
RFHDRRDAQD AEAAMDGAEL DGRELRVQVA RYGRRDLPRS RQGEPRGRSR GGGYGRRSRS
YGRRSRSPRR RHRSRSRGPS CSRSRSRSRY RGSRYSRSPY SRSPYSRSRY SRSPYSRSRY
RESRYGGSHY SSSGYSNSRY SRYHSSRSHS KSGSSTSSRS ASTSKSSSAR RSKSSSVSRS
RSRSRSSSMT RSPPRVSKRK SKSRSRSKRP PKSPEEEGQM SS
