PNISR_MOUSE
ID PNISR_MOUSE Reviewed; 805 AA.
AC A2AJT4; Q9CS92;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Arginine/serine-rich protein PNISR;
DE AltName: Full=Serine/arginine-rich-splicing regulatory protein 130;
DE Short=SRrp130;
DE AltName: Full=Splicing factor, arginine/serine-rich 130;
DE AltName: Full=Splicing factor, arginine/serine-rich 18;
GN Name=Pnisr; Synonyms=Sfrs18, Srrp130;
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] OF 1-695.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-304, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, 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 PNN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AL772187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK017507; BAB30779.3; -; mRNA.
DR CCDS; CCDS89720.1; -.
DR AlphaFoldDB; A2AJT4; -.
DR STRING; 10090.ENSMUSP00000029911; -.
DR iPTMnet; A2AJT4; -.
DR PhosphoSitePlus; A2AJT4; -.
DR EPD; A2AJT4; -.
DR jPOST; A2AJT4; -.
DR MaxQB; A2AJT4; -.
DR PaxDb; A2AJT4; -.
DR PeptideAtlas; A2AJT4; -.
DR PRIDE; A2AJT4; -.
DR ProteomicsDB; 289704; -.
DR Antibodypedia; 32003; 33 antibodies from 15 providers.
DR Ensembl; ENSMUST00000098238; ENSMUSP00000095840; ENSMUSG00000028248.
DR MGI; MGI:1913875; Pnisr.
DR VEuPathDB; HostDB:ENSMUSG00000028248; -.
DR eggNOG; ENOG502QUV0; Eukaryota.
DR GeneTree; ENSGT00730000111138; -.
DR InParanoid; A2AJT4; -.
DR OMA; RHKHKSE; -.
DR ChiTaRS; Pnisr; mouse.
DR PRO; PR:A2AJT4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AJT4; protein.
DR Bgee; ENSMUSG00000028248; Expressed in metanephric cortical collecting duct and 236 other tissues.
DR ExpressionAtlas; A2AJT4; baseline and differential.
DR Genevisible; A2AJT4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR InterPro; IPR031937; PNISR.
DR PANTHER; PTHR31518; PTHR31518; 2.
DR Pfam; PF15996; PNISR; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..805
FT /note="Arginine/serine-rich protein PNISR"
FT /id="PRO_0000292655"
FT REGION 75..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 237..276
FT /evidence="ECO:0000255"
FT COILED 427..461
FT /evidence="ECO:0000255"
FT COMPBIAS 75..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..576
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..635
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..805
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT CROSSLNK 703
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TF01"
FT CONFLICT 695
FT /note="Q -> R (in Ref. 2; BAB30779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 92115 MW; B73F082E7C486D39 CRC64;
MWDQGGQPWQ QWPLNQQQWM QSFQHQQDPS QIDWAALAQA WIAQREASGQ QSIVEQPPGM
MPNGQDMSAM ESGPNNHGNF QGDSNFNRMW QPEWGMHQQP PHPPPEQPWM PPAPGPMDIV
PPSEDSNSQD SGEFAPDNRH IFNQNNHNFG GPPDNFAVGP VNQFDYQHGA AFGPPQGGFH
PPYWQPGPPG PPAPTQNRRE RPPSFRDRQR SPIALPVKQE PPQIDAVKRR TLPAWIREGL
EKMEREKQKK LEKERMEQQR SQLSKKEKKA TEDAEGGDGP RLPQRSKFDS DEEDEDAENL
EAVSSGKVTR SPSPAPQEEH SEPEMTEEEK EYQMMLLTKM LLTEILLDVT DEEIYYVAKD
AHRKATKAPA KQLAQSSALA SLTGLGGLGG YGSGDSEDER SDRGSESSDT DDEELRHRIR
QKQEAFWRKE KEQQLLQDKQ IEEEKQQTER VTKEMNEFIH REQNSLSLLE ASEADRDAVN
DKKRTPNEAP SVLEPKREHK GKEKERGSRS GSSSSGSSSS GSRTSSSSSS VSSSSYSSSS
GSSCTSSRSS SPKRRKRPSR SRSPPAKARR SRSRSYSRRV KVDSSRTRGK LRDRRRSNRS
SIERERRRNR SPSRDRRRSR SRSRDRRTNR SSRSRSRDRR KIEDPRGNLS GNSHKHKGEA
KEQDRKKERS RSVDKDRRKK DKERDRELDK RKEKQKREEK DFKFSSQDDR LKRKRESERT
FCRSGSISVK VIRHDSRQDS KKNATKDSKR HSGSDSSGRS SSESPGSSKE KKAKKPKHSR
SRSLEKSQRS GKKASRKHKS KSRSR
