SR140_MOUSE
ID SR140_MOUSE Reviewed; 1029 AA.
AC Q6NV83; E9QK93; Q9CSW7; Q9CT00;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=U2 snRNP-associated SURP motif-containing protein;
DE AltName: Full=140 kDa Ser/Arg-rich domain protein;
DE AltName: Full=U2-associated protein SR140;
GN Name=U2surp; Synonyms=Sr140;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Trophoblast stem cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-197 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-338 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND SER-800, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBUNIT: Interacts with ERBB4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6NV83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NV83-2; Sequence=VSP_023526;
CC Name=3;
CC IsoId=Q6NV83-3; Sequence=VSP_023525;
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AC159895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068265; AAH68265.1; -; mRNA.
DR EMBL; AK011588; BAB27718.1; -; mRNA.
DR EMBL; AK011796; BAB27847.1; -; mRNA.
DR CCDS; CCDS40727.1; -. [Q6NV83-3]
DR CCDS; CCDS52889.1; -. [Q6NV83-1]
DR CCDS; CCDS90640.1; -. [Q6NV83-2]
DR RefSeq; NP_001108449.1; NM_001114977.1. [Q6NV83-1]
DR RefSeq; NP_080752.2; NM_026476.2. [Q6NV83-3]
DR RefSeq; XP_006511447.1; XM_006511384.3.
DR AlphaFoldDB; Q6NV83; -.
DR SMR; Q6NV83; -.
DR BioGRID; 212565; 6.
DR IntAct; Q6NV83; 1.
DR MINT; Q6NV83; -.
DR STRING; 10090.ENSMUSP00000078602; -.
DR iPTMnet; Q6NV83; -.
DR PhosphoSitePlus; Q6NV83; -.
DR SwissPalm; Q6NV83; -.
DR EPD; Q6NV83; -.
DR jPOST; Q6NV83; -.
DR MaxQB; Q6NV83; -.
DR PaxDb; Q6NV83; -.
DR PeptideAtlas; Q6NV83; -.
DR PRIDE; Q6NV83; -.
DR ProteomicsDB; 254552; -. [Q6NV83-1]
DR ProteomicsDB; 254553; -. [Q6NV83-2]
DR ProteomicsDB; 254554; -. [Q6NV83-3]
DR Antibodypedia; 48172; 139 antibodies from 23 providers.
DR DNASU; 67958; -.
DR Ensembl; ENSMUST00000078374; ENSMUSP00000077482; ENSMUSG00000032407. [Q6NV83-3]
DR Ensembl; ENSMUST00000079659; ENSMUSP00000078602; ENSMUSG00000032407. [Q6NV83-1]
DR Ensembl; ENSMUST00000217176; ENSMUSP00000151121; ENSMUSG00000032407. [Q6NV83-2]
DR GeneID; 67958; -.
DR KEGG; mmu:67958; -.
DR UCSC; uc009rba.2; mouse. [Q6NV83-3]
DR UCSC; uc009rbb.2; mouse. [Q6NV83-1]
DR UCSC; uc009rbd.1; mouse. [Q6NV83-2]
DR CTD; 23350; -.
DR MGI; MGI:1915208; U2surp.
DR VEuPathDB; HostDB:ENSMUSG00000032407; -.
DR eggNOG; KOG0151; Eukaryota.
DR GeneTree; ENSGT00390000010687; -.
DR HOGENOM; CLU_010743_1_0_1; -.
DR InParanoid; Q6NV83; -.
DR OMA; FKNGPVW; -.
DR OrthoDB; 523911at2759; -.
DR PhylomeDB; Q6NV83; -.
DR TreeFam; TF318729; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 67958; 20 hits in 76 CRISPR screens.
DR ChiTaRS; U2surp; mouse.
DR PRO; PR:Q6NV83; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6NV83; protein.
DR Bgee; ENSMUSG00000032407; Expressed in pharyngeal arch 2 and 246 other tissues.
DR ExpressionAtlas; Q6NV83; baseline and differential.
DR Genevisible; Q6NV83; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd12223; RRM_SR140; 1.
DR Gene3D; 1.10.10.790; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR013170; mRNA_splic_Cwf21_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR035009; SR140_RRM.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF08312; cwf21; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM01115; cwf21; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00648; SWAP; 1.
DR SUPFAM; SSF109905; SSF109905; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50128; SURP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CHAIN 2..1029
FT /note="U2 snRNP-associated SURP motif-containing protein"
FT /id="PRO_0000280071"
FT DOMAIN 274..355
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 430..473
FT /note="SURP motif"
FT DOMAIN 534..679
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..121
FT /evidence="ECO:0000255"
FT COILED 192..232
FT /evidence="ECO:0000255"
FT COILED 837..915
FT /evidence="ECO:0000255"
FT COMPBIAS 7..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..806
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1029
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 719
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 760
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 931
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 749
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 760
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 829
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 832
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT VAR_SEQ 31..74
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023525"
FT VAR_SEQ 256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023526"
FT CONFLICT 327
FT /note="N -> S (in Ref. 2; AAH68265)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="K -> R (in Ref. 2; AAH68265)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="L -> P (in Ref. 2; AAH68265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1029 AA; 118261 MW; EB4A067CE542A452 CRC64;
MADKTPGGSQ KASSKNRSSD VHSSGSSDAH MDASGPSDSD MPSRTRPKSP RKHNYRNESS
RESLCDSPHQ NLSRPLLENK LKAFSIGKMS TAKRTLSKKE QEELKKKEDE KAAAEIYEEF
LAAFEGSDGN KVKTFVRGGV VNAAKDEHET DEKRGKIYKP SSRFADQKNP PNQSSNERPP
SLLVIETKKP PLKKGEKEKK KSNLELFKEE LKQIQEERDE RHKTKGRLSR FEPPQSDSDG
QRRSMDVPSR RNRSSGVLDD YAPGSHDVGD PSTTNLYLGN INPQMNEEML CQEFGRFGPL
ASVKIMWPRT DEERARERNC GFVAFMNRRD AERALKNLNG KMIMSFEMKL GWGKAVPIPP
HPIYIPPSMM EHTLPPPPSG LPFNAQPRER LKNPNAPMLP PPKNKEDFEK TLSQAIVKVV
IPTERNLLAL IHRMIEFVVR EGPMFEAMIM NREINNPMFR FLFENQTPAH VYYRWKLYSI
LQGDSPTKWR TEDFRMFKNG SFWRPPPLNP YLHGMSEEQE TEAFVEEPSK KGALKEEQRD
KLEEILRGLT PRKNDIGDAM VFCLNNAEAA EEIVDCITES LSILKTPLPK KIARLYLVSD
VLYNSSAKVA NASYYRKFFE TKLCQIFSDL NATYRTIQGH LQSENFKQRV MTCFRAWEDW
AIYPEPFLIK LQNIFLGLVN IIEEKETEDV PDDLDGAPIE EELDGAPLED VDGIPIDATP
IDDLDGVPIK SLDDDLDGVP LDATEDSKKN EPIFKVAPSK WEAVDESELE AQAVTTSKWE
LFDQHEESEE EENQNQEEES EDEEDTQSSK SEEHHLYSNP VREEATESKF SKYSEMSEEK
RAKLREIELK VMKFQDELES GKRPKKPGQS FQEQVEHYRD KLLQREKEKE LERERERDKK
DKEKLESRSK DKKEKDECTP TRKERKRRHS TSPSPSRSSS GRRVKSPSPK SERSERSERS
HKESSRSRSS HKDSPRDASK KAKRSPSGSR TPKRSRRSRS RSPKKSGKKS RSQSRSPHRS
HKKSKKNKH
