SREK1_MOUSE
ID SREK1_MOUSE Reviewed; 494 AA.
AC Q8BZX4; Q8BLM8; Q8BWK7; Q8BYK0; Q8BYZ4;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Splicing regulatory glutamine/lysine-rich protein 1;
DE AltName: Full=Serine/arginine-rich-splicing regulatory protein 86;
DE Short=SRrp86;
DE AltName: Full=Splicing factor, arginine/serine-rich 12;
GN Name=Srek1; Synonyms=Sfrs12, Srrp86;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-397 (ISOFORM 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Embryonic heart, Embryonic lung, Spinal cord, and
RC Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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).
CC -!- FUNCTION: Participates in the regulation of alternative splicing by
CC modulating the activity of other splice facors. Inhibits the splicing
CC activity of SFRS1, SFRS2 and SFRS6. Augments the splicing activity of
CC SFRS3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Binds SFRS1, SFRS2, SFRS3 and SFRS6. Interacts with
CC the spliceosome. Interacts with SREK1IP1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZX4-2; Sequence=VSP_008400;
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AK033354; BAC28243.1; -; mRNA.
DR EMBL; AK037115; BAC29709.2; -; mRNA.
DR EMBL; AK039311; BAC30314.1; -; mRNA.
DR EMBL; AK044086; BAC31767.1; -; mRNA.
DR EMBL; AK052265; BAC34905.2; -; mRNA.
DR EMBL; BC070460; AAH70460.1; -; mRNA.
DR CCDS; CCDS26743.1; -. [Q8BZX4-1]
DR CCDS; CCDS88513.1; -. [Q8BZX4-2]
DR RefSeq; NP_766180.1; NM_172592.2. [Q8BZX4-1]
DR RefSeq; XP_006517669.1; XM_006517606.2.
DR RefSeq; XP_006517670.1; XM_006517607.3. [Q8BZX4-1]
DR RefSeq; XP_017170986.1; XM_017315497.1.
DR AlphaFoldDB; Q8BZX4; -.
DR SMR; Q8BZX4; -.
DR BioGRID; 230045; 2.
DR STRING; 10090.ENSMUSP00000074196; -.
DR iPTMnet; Q8BZX4; -.
DR PhosphoSitePlus; Q8BZX4; -.
DR EPD; Q8BZX4; -.
DR MaxQB; Q8BZX4; -.
DR PaxDb; Q8BZX4; -.
DR PeptideAtlas; Q8BZX4; -.
DR PRIDE; Q8BZX4; -.
DR ProteomicsDB; 263341; -. [Q8BZX4-1]
DR ProteomicsDB; 263342; -. [Q8BZX4-2]
DR DNASU; 218543; -.
DR Ensembl; ENSMUST00000074616; ENSMUSP00000074196; ENSMUSG00000032621. [Q8BZX4-2]
DR Ensembl; ENSMUST00000210489; ENSMUSP00000147737; ENSMUSG00000032621. [Q8BZX4-1]
DR GeneID; 218543; -.
DR KEGG; mmu:218543; -.
DR UCSC; uc007rsh.1; mouse. [Q8BZX4-1]
DR UCSC; uc007rsj.1; mouse. [Q8BZX4-2]
DR CTD; 140890; -.
DR MGI; MGI:2145245; Srek1.
DR VEuPathDB; HostDB:ENSMUSG00000032621; -.
DR eggNOG; KOG4676; Eukaryota.
DR GeneTree; ENSGT01030000235193; -.
DR HOGENOM; CLU_030029_2_0_1; -.
DR InParanoid; Q8BZX4; -.
DR OMA; QTSVIHA; -.
DR OrthoDB; 1460556at2759; -.
DR PhylomeDB; Q8BZX4; -.
DR TreeFam; TF106266; -.
DR BioGRID-ORCS; 218543; 9 hits in 73 CRISPR screens.
DR ChiTaRS; Srek1; mouse.
DR PRO; PR:Q8BZX4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BZX4; protein.
DR Bgee; ENSMUSG00000032621; Expressed in undifferentiated genital tubercle and 257 other tissues.
DR ExpressionAtlas; Q8BZX4; baseline and differential.
DR Genevisible; Q8BZX4; MM.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12260; RRM2_SREK1; 1.
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 InterPro; IPR034192; SREK1_RRM2.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..494
FT /note="Splicing regulatory glutamine/lysine-rich protein 1"
FT /id="PRO_0000081941"
FT DOMAIN 69..145
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 176..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..261
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..393
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXA9"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXA9"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXA9"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXA9"
FT VAR_SEQ 1
FT /note="M -> MNSGGGFGLGLGFGLFPTTVIQVTNLSSAVTSEQMRTLFSFLGEIEE
FT LRLYPPDNTPLAFSSKVCYIKFRDPSSVGVAQHLTNTVFIDRALIVVPCAEGKIPEEAK
FT ALSLLAPAPTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008400"
FT CONFLICT 401
FT /note="E -> G (in Ref. 1; BAC29709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56763 MW; 2451AD74522C7C5D CRC64;
MTSLVPGAGL LPIPTSSPLT AVSSLGVSLS SLGAIPAAAL DPNITTLGEI PQPPLMGNVD
PSKIDEIRRT VYVGNLNSQT TTADQLLEFF KQVGEVKFVR MAGDETQPTR FAFVEFADQN
SVPRALAFNG VMFGDRPLKI NHSNNAIVKP PEMTPQAAAK ELEEVMKRVR EAQSFISAAI
EPESGKSNER KGGRSRSHTR SKSRSSSKSH SRRKRSQSKH RSRSHNRSRS RQKDRRRSKS
PHKKRSKSRE RRKSRSRSRS RDKRKDTREK VKERVKEKER EKEREREKDR EKDKERGKNK
DKDREKEKDH EKERDKEKEK EQDKDKEREK DRSKETDEKR KKEKKSRTPP RSYNASRRSR
STSRERRRRR SRSSSRSPRT SKTVKRKSSR SPSPRGRNKK EKKREKERDH ISDRRERERS
TSTKKSSGDR DGKEKVEKST TPVKEKEHSK ESDATVSKAA DEKGSPRTED EGKVQHNGNC
QPNEESPCSK ADAV
