NSRP1_MOUSE
ID NSRP1_MOUSE Reviewed; 542 AA.
AC Q5NCR9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Nuclear speckle splicing regulatory protein 1;
DE AltName: Full=Coiled-coil domain-containing protein 55;
DE AltName: Full=Nuclear speckle-related protein 70;
DE Short=NSrp70;
GN Name=Nsrp1; Synonyms=Ccdc55, Nsrp70;
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].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-31; SER-33 AND
RP SER-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=21296756; DOI=10.1093/nar/gkq1267;
RA Kim Y.D., Lee J.Y., Oh K.M., Araki M., Araki K., Yamamura K.I., Jun C.D.;
RT "NSrp70 is a novel nuclear speckle-related protein that modulates
RT alternative pre-mRNA splicing in vivo.";
RL Nucleic Acids Res. 39:4300-4314(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-277, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: RNA-binding protein that mediates pre-mRNA alternative
CC splicing regulation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with SRSF1. Interacts (via C-
CC terminus) with SRSF2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}. Note=Colocalizes with splicing factors SRSF1 and SRSF2
CC in speckles. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show early embryonic lethality shortly after
CC implantation. {ECO:0000269|PubMed:21296756}.
CC -!- SIMILARITY: Belongs to the NSRP1 family. {ECO:0000305}.
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DR EMBL; AK168573; BAE40443.1; -; mRNA.
DR EMBL; AL603842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089560; AAH89560.1; -; mRNA.
DR CCDS; CCDS25075.1; -.
DR RefSeq; NP_001012309.1; NM_001012309.2.
DR AlphaFoldDB; Q5NCR9; -.
DR SMR; Q5NCR9; -.
DR BioGRID; 231915; 3.
DR STRING; 10090.ENSMUSP00000099552; -.
DR iPTMnet; Q5NCR9; -.
DR PhosphoSitePlus; Q5NCR9; -.
DR EPD; Q5NCR9; -.
DR jPOST; Q5NCR9; -.
DR MaxQB; Q5NCR9; -.
DR PaxDb; Q5NCR9; -.
DR PeptideAtlas; Q5NCR9; -.
DR PRIDE; Q5NCR9; -.
DR ProteomicsDB; 295532; -.
DR Antibodypedia; 2855; 111 antibodies from 23 providers.
DR DNASU; 237859; -.
DR Ensembl; ENSMUST00000102494; ENSMUSP00000099552; ENSMUSG00000037958.
DR GeneID; 237859; -.
DR KEGG; mmu:237859; -.
DR UCSC; uc007kgg.2; mouse.
DR CTD; 84081; -.
DR MGI; MGI:2144305; Nsrp1.
DR VEuPathDB; HostDB:ENSMUSG00000037958; -.
DR eggNOG; KOG2117; Eukaryota.
DR GeneTree; ENSGT00940000154049; -.
DR HOGENOM; CLU_548527_0_0_1; -.
DR InParanoid; Q5NCR9; -.
DR OMA; IYDEMQQ; -.
DR OrthoDB; 1613087at2759; -.
DR PhylomeDB; Q5NCR9; -.
DR TreeFam; TF319359; -.
DR BioGRID-ORCS; 237859; 7 hits in 39 CRISPR screens.
DR ChiTaRS; Nsrp1; mouse.
DR PRO; PR:Q5NCR9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5NCR9; protein.
DR Bgee; ENSMUSG00000037958; Expressed in animal zygote and 228 other tissues.
DR ExpressionAtlas; Q5NCR9; baseline and differential.
DR Genevisible; Q5NCR9; MM.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0032502; P:developmental process; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR042816; Nsrp1.
DR InterPro; IPR018612; NSRP1_N.
DR PANTHER; PTHR31938; PTHR31938; 1.
DR Pfam; PF09745; DUF2040; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..542
FT /note="Nuclear speckle splicing regulatory protein 1"
FT /id="PRO_0000240435"
FT REGION 21..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..169
FT /note="Necessary for alternative splicing activity"
FT /evidence="ECO:0000250"
FT REGION 190..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 103..172
FT /evidence="ECO:0000255"
FT COILED 372..413
FT /evidence="ECO:0000255"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 277
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4FZU3"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
SQ SEQUENCE 542 AA; 63799 MW; CF97836AEDB0F721 CRC64;
MAIPGRQYGL ILPKKTQPLH RVLQKPSVFG SDSDDDETSV SESLQREAAK KQAMKQTKLE
IQKALAEDST VYEYDSVYDE MQKKKEENNP KLLPGKDRKP KYIHNLLKAV EIRKKEQEKR
MEKKIQRERE MENGEFDDKE AFVTSAYKKK LEERAEEEER EKRAAALEAH LDVTKQKDLS
GFYRHLLNQA VGEEAAPKSS FREARTVIKE EKLRGYPDET NSESRPPQQS CVLQRGAQEA
EENPDADREF DDESSEDGEK RDHKVKSRGE DTGASMKHPK HHKNRAHSRS SSEERGLGTK
HHSRGSQSRG HEHQDRQSRD QESCHKDRSH REEKSSHRHR EASHKDHYWK KHEQEDKLKG
REQEERQDRE GKREKYSSRE QERDRQRNDH DRYSEKEKKR KEKEEHTKAR RERCEDSGKH
REREKPEGHG QSSERHRDRR ESSPRSRPKD DLDQERSSKA RNTEKDKGEQ GKPSHSETSL
ATKHRLAEER PEKGSEQERP PEAVSKFAKR SNEETVMSAR DRYLARQMAR INAKTYIEKE
DD
