PNISR_HUMAN
ID PNISR_HUMAN Reviewed; 805 AA.
AC Q8TF01; A8K540; E1P5D2; Q5T064; Q5T065; Q6P2B4; Q6P2N4; Q6PJ93; Q6PK36;
AC Q7Z640; Q8N2L1; Q8TF00; Q96K10; Q96SI3; Q96SM5; Q9P076; Q9P0C0; Q9Y4N3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Arginine/serine-rich protein PNISR;
DE AltName: Full=PNN-interacting serine/arginine-rich protein;
DE AltName: Full=SR-related protein;
DE AltName: Full=SR-rich protein;
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=C6orf111, SFRS18, SRRP130; ORFNames=HSPC261, HSPC306;
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 [MRNA] (ISOFORM 1), INTERACTION WITH PNN, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=14578391; DOI=10.1167/iovs.03-0240;
RA Zimowska G., Shi J., Munguba G., Jackson M.R., Alpatov R., Simmons M.N.,
RA Shi Y., Sugrue S.P.;
RT "Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal
RT epithelial cells.";
RL Invest. Ophthalmol. Vis. Sci. 44:4715-4723(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
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].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-497 (ISOFORM 1).
RC TISSUE=Blood, Pancreas, Placenta, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-499 AND 661-805.
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 507-805.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-290; SER-313;
RP SER-321 AND SER-726, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-211; SER-290;
RP SER-465; SER-467 AND THR-485, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-218, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-218; LYS-496 AND LYS-703, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SUBUNIT: Interacts with PNN. {ECO:0000269|PubMed:14578391}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:14578391}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TF01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TF01-2; Sequence=VSP_014458, VSP_014459;
CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, thymus,
CC spleen, kidney, liver, placenta and leukocytes.
CC {ECO:0000269|PubMed:14578391}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07791.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH19074.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH52638.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH64413.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH64640.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF314184; AAL76163.1; -; mRNA.
DR EMBL; AF314185; AAL76164.1; -; mRNA.
DR EMBL; AK027658; BAB55273.1; -; mRNA.
DR EMBL; AK027759; BAB55350.1; -; mRNA.
DR EMBL; AK027898; BAB55440.1; -; mRNA.
DR EMBL; AK074628; BAC11098.1; ALT_TERM; mRNA.
DR EMBL; AK291155; BAF83844.1; -; mRNA.
DR EMBL; AL513550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48476.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48477.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48479.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48481.1; -; Genomic_DNA.
DR EMBL; BC007791; AAH07791.1; ALT_SEQ; mRNA.
DR EMBL; BC019074; AAH19074.1; ALT_SEQ; mRNA.
DR EMBL; BC052638; AAH52638.1; ALT_SEQ; mRNA.
DR EMBL; BC064413; AAH64413.1; ALT_FRAME; mRNA.
DR EMBL; BC064640; AAH64640.1; ALT_SEQ; mRNA.
DR EMBL; AF161379; AAF28939.1; -; mRNA.
DR EMBL; AF161424; AAF28984.1; -; mRNA.
DR EMBL; AL080186; CAB45767.1; -; mRNA.
DR CCDS; CCDS5043.1; -. [Q8TF01-1]
DR PIR; T12483; T12483.
DR RefSeq; NP_001309334.1; NM_001322405.1. [Q8TF01-1]
DR RefSeq; NP_001309335.1; NM_001322406.1. [Q8TF01-1]
DR RefSeq; NP_001309337.1; NM_001322408.1. [Q8TF01-1]
DR RefSeq; NP_001309341.1; NM_001322412.1.
DR RefSeq; NP_001309342.1; NM_001322413.1.
DR RefSeq; NP_001309344.1; NM_001322415.1.
DR RefSeq; NP_056306.1; NM_015491.2. [Q8TF01-1]
DR RefSeq; NP_116259.2; NM_032870.3. [Q8TF01-1]
DR AlphaFoldDB; Q8TF01; -.
DR SMR; Q8TF01; -.
DR BioGRID; 117448; 43.
DR IntAct; Q8TF01; 19.
DR MINT; Q8TF01; -.
DR STRING; 9606.ENSP00000358242; -.
DR iPTMnet; Q8TF01; -.
DR PhosphoSitePlus; Q8TF01; -.
DR BioMuta; PNISR; -.
DR DMDM; 152031686; -.
DR EPD; Q8TF01; -.
DR jPOST; Q8TF01; -.
DR MassIVE; Q8TF01; -.
DR MaxQB; Q8TF01; -.
DR PaxDb; Q8TF01; -.
DR PeptideAtlas; Q8TF01; -.
DR PRIDE; Q8TF01; -.
DR ProteomicsDB; 74530; -. [Q8TF01-1]
DR ProteomicsDB; 74531; -. [Q8TF01-2]
DR Antibodypedia; 32003; 33 antibodies from 15 providers.
DR DNASU; 25957; -.
DR Ensembl; ENST00000369239.10; ENSP00000358242.5; ENSG00000132424.17. [Q8TF01-1]
DR Ensembl; ENST00000438806.5; ENSP00000387997.1; ENSG00000132424.17. [Q8TF01-1]
DR Ensembl; ENST00000647811.1; ENSP00000496842.1; ENSG00000132424.17. [Q8TF01-1]
DR GeneID; 25957; -.
DR KEGG; hsa:25957; -.
DR MANE-Select; ENST00000369239.10; ENSP00000358242.5; NM_032870.4; NP_116259.2.
DR UCSC; uc003ppo.5; human. [Q8TF01-1]
DR CTD; 25957; -.
DR DisGeNET; 25957; -.
DR GeneCards; PNISR; -.
DR HGNC; HGNC:21222; PNISR.
DR HPA; ENSG00000132424; Low tissue specificity.
DR MIM; 616653; gene.
DR neXtProt; NX_Q8TF01; -.
DR OpenTargets; ENSG00000132424; -.
DR PharmGKB; PA162402984; -.
DR VEuPathDB; HostDB:ENSG00000132424; -.
DR eggNOG; ENOG502QUV0; Eukaryota.
DR GeneTree; ENSGT00730000111138; -.
DR HOGENOM; CLU_372518_0_0_1; -.
DR InParanoid; Q8TF01; -.
DR OMA; RHKHKSE; -.
DR OrthoDB; 928665at2759; -.
DR PhylomeDB; Q8TF01; -.
DR TreeFam; TF332904; -.
DR PathwayCommons; Q8TF01; -.
DR SignaLink; Q8TF01; -.
DR BioGRID-ORCS; 25957; 344 hits in 1100 CRISPR screens.
DR ChiTaRS; PNISR; human.
DR GeneWiki; PNISR_(gene); -.
DR GenomeRNAi; 25957; -.
DR Pharos; Q8TF01; Tdark.
DR PRO; PR:Q8TF01; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8TF01; protein.
DR Bgee; ENSG00000132424; Expressed in right hemisphere of cerebellum and 201 other tissues.
DR ExpressionAtlas; Q8TF01; baseline and differential.
DR Genevisible; Q8TF01; HS.
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:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR InterPro; IPR031937; PNISR.
DR PANTHER; PTHR31518; PTHR31518; 2.
DR Pfam; PF15996; PNISR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..805
FT /note="Arginine/serine-rich protein PNISR"
FT /id="PRO_0000081947"
FT REGION 74..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 429..461
FT /evidence="ECO:0000255"
FT COILED 673..703
FT /evidence="ECO:0000255"
FT COMPBIAS 74..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 302..316
FT /note="Polar 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..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..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:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AJT4"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 703
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 368..413
FT /note="APAKQLAQSSALASLTGLGGLGGYGSGDSEDERSDRGSESSDTDDE -> GI
FT FWCFWFCFSWGILVLMTILAFFCCPCWISTRYLNILLHVLTLKD (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014458"
FT VAR_SEQ 414..805
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014459"
FT CONFLICT 34
FT /note="W -> R (in Ref. 2; BAB55350)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="K -> R (in Ref. 2; BAB55440)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="E -> G (in Ref. 2; BAB55273)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="R -> G (in Ref. 7; CAB45767)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="S -> P (in Ref. 1; AAL76163)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="Q -> R (in Ref. 7; CAB45767)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="V -> A (in Ref. 1; AAL76163/AAL76164)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="R -> KSSILFKVFCLIFKKN (in Ref. 6; AAF28939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 92577 MW; 7738BC276B6E80B2 CRC64;
MWDQGGQPWQ QWPLNQQQWM QSFQHQQDPS QIDWAALAQA WIAQREASGQ QSMVEQPPGM
MPNGQDMSTM ESGPNNHGNF QGDSNFNRMW QPEWGMHQQP PHPPPDQPWM PPTPGPMDIV
PPSEDSNSQD SGEFAPDNRH IFNQNNHNFG GPPDNFAVGP VNQFDYQHGA AFGPPQGGFH
PPYWQPGPPG PPAPPQNRRE RPSSFRDRQR SPIALPVKQE PPQIDAVKRR TLPAWIREGL
EKMEREKQKK LEKERMEQQR SQLSKKEKKA TEDAEGGDGP RLPQRSKFDS DEEEEDTENV
EAASSGKVTR SPSPVPQEEH SDPEMTEEEK EYQMMLLTKM LLTEILLDVT DEEIYYVAKD
AHRKATKAPA KQLAQSSALA SLTGLGGLGG YGSGDSEDER SDRGSESSDT DDEELRHRIR
QKQEAFWRKE KEQQLLHDKQ MEEEKQQTER VTKEMNEFIH KEQNSLSLLE AREADGDVVN
EKKRTPNETT SVLEPKKEHK EKEKQGRSRS GSSSSGSSSS NSRTSSTSST VSSSSYSSSS
GSSRTSSRSS SPKRKKRHSR SRSPTIKARR SRSRSYSRRI KIESNRARVK IRDRRRSNRN
SIERERRRNR SPSRERRRSR SRSRDRRTNR ASRSRSRDRR KIDDQRGNLS GNSHKHKGEA
KEQERKKERS RSIDKDRKKK DKEREREQDK RKEKQKREEK DFKFSSQDDR LKRKRESERT
FSRSGSISVK IIRHDSRQDS KKSTTKDSKK HSGSDSSGRS SSESPGSSKE KKAKKPKHSR
SRSVEKSQRS GKKASRKHKS KSRSR
