ID   NSRP1_HUMAN             Reviewed;         558 AA.
AC   Q9H0G5; Q6FI71;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   02-JUN-2021, entry version 147.
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   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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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 GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, AND
RP   IDENTIFICATION BY 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-248; SER-254 AND
RP   SER-255, AND IDENTIFICATION BY 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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-254 AND SER-255, AND
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, AND
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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   FUNCTION, INTERACTION WITH SRSF1 AND SRSF2, RNA-BINDING, MUTAGENESIS OF
RP   536-ARG-ASP-537, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-33; SER-248; SER-254
RP   AND SER-255, 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-33; SER-248 AND THR-275, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-210, 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   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-281, 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   -!- FUNCTION: RNA-binding protein that mediates pre-mRNA alternative
CC       splicing regulation. {ECO:0000269|PubMed:21296756}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with SRSF1. Interacts (via C-
CC       terminus) with SRSF2. {ECO:0000269|PubMed:21296756}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21296756}. Nucleus
CC       speckle {ECO:0000269|PubMed:21296756}. Note=Colocalizes with splicing
CC       factors SRSF1 and SRSF2 in speckles.
CC   -!- TISSUE SPECIFICITY: Expressed in dendritic cells, T-cells, B-cells and
CC       natural killer cells. Expressed in secondary lymphoid organs such as
CC       spleen and mesenteric, axillary and brachial lymph nodes.
CC       {ECO:0000269|PubMed:21296756}.
CC   -!- INDUCTION: Up-regulated in motile T-cells.
CC       {ECO:0000269|PubMed:21296756}.
CC   -!- SIMILARITY: Belongs to the NSRP1 family. {ECO:0000305}.
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DR   EMBL; AL136806; CAB66740.1; -; mRNA.
DR   EMBL; CR533555; CAG38586.1; -; mRNA.
DR   EMBL; AC104984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC040118; AAH40118.1; -; mRNA.
DR   EMBL; BC105044; AAI05045.1; -; mRNA.
DR   EMBL; BC105046; AAI05047.1; -; mRNA.
DR   CCDS; CCDS11255.1; -.
DR   RefSeq; NP_001248396.1; NM_001261467.1.
DR   RefSeq; NP_115517.1; NM_032141.3.
DR   SMR; Q9H0G5; -.
DR   BioGRID; 123876; 50.
DR   IntAct; Q9H0G5; 21.
DR   MINT; Q9H0G5; -.
DR   STRING; 9606.ENSP00000247026; -.
DR   iPTMnet; Q9H0G5; -.
DR   PhosphoSitePlus; Q9H0G5; -.
DR   BioMuta; NSRP1; -.
DR   DMDM; 74733524; -.
DR   EPD; Q9H0G5; -.
DR   jPOST; Q9H0G5; -.
DR   MassIVE; Q9H0G5; -.
DR   MaxQB; Q9H0G5; -.
DR   PaxDb; Q9H0G5; -.
DR   PeptideAtlas; Q9H0G5; -.
DR   PRIDE; Q9H0G5; -.
DR   ProteomicsDB; 80276; -.
DR   Antibodypedia; 2855; 103 antibodies.
DR   DNASU; 84081; -.
DR   Ensembl; ENST00000247026; ENSP00000247026; ENSG00000126653.
DR   GeneID; 84081; -.
DR   KEGG; hsa:84081; -.
DR   UCSC; uc002heu.5; human.
DR   CTD; 84081; -.
DR   DisGeNET; 84081; -.
DR   GeneCards; NSRP1; -.
DR   HGNC; HGNC:25305; NSRP1.
DR   HPA; ENSG00000126653; Low tissue specificity.
DR   MIM; 616173; gene.
DR   neXtProt; NX_Q9H0G5; -.
DR   OpenTargets; ENSG00000126653; -.
DR   PharmGKB; PA142672171; -.
DR   VEuPathDB; HostDB:ENSG00000126653.15; -.
DR   eggNOG; KOG2117; Eukaryota.
DR   GeneTree; ENSGT00940000154049; -.
DR   HOGENOM; CLU_548527_0_0_1; -.
DR   InParanoid; Q9H0G5; -.
DR   OMA; IYDEMQQ; -.
DR   OrthoDB; 1613087at2759; -.
DR   PhylomeDB; Q9H0G5; -.
DR   TreeFam; TF319359; -.
DR   PathwayCommons; Q9H0G5; -.
DR   BioGRID-ORCS; 84081; 124 hits in 995 CRISPR screens.
DR   ChiTaRS; NSRP1; human.
DR   GeneWiki; CCDC55_(gene); -.
DR   GenomeRNAi; 84081; -.
DR   Pharos; Q9H0G5; Tbio.
DR   PRO; PR:Q9H0G5; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9H0G5; protein.
DR   Bgee; ENSG00000126653; Expressed in sural nerve and 214 other tissues.
DR   ExpressionAtlas; Q9H0G5; baseline and differential.
DR   Genevisible; Q9H0G5; HS.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0032502; P:developmental process; IMP:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR018612; DUF2040.
DR   InterPro; IPR042816; Nsrp1.
DR   PANTHER; PTHR31938; PTHR31938; 1.
DR   Pfam; PF09745; DUF2040; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT   CHAIN           1..558
FT                   /note="Nuclear speckle splicing regulatory protein 1"
FT                   /id="PRO_0000240434"
FT   REGION          21..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..170
FT                   /note="Necessary for alternative splicing activity"
FT   REGION          204..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          104..170
FT                   /evidence="ECO:0000255"
FT   COILED          379..427
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        40..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..534
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:21406692"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT   MOD_RES         275
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         457
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4FZU3"
FT   CROSSLNK        199
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        210
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447"
FT   CROSSLNK        281
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         86
FT                   /note="K -> T (in dbSNP:rs11544945)"
FT                   /id="VAR_054104"
FT   MUTAGEN         536..537
FT                   /note="RD->AA: Inhibits nuclear localization and
FT                   alternative splicing activity."
FT                   /evidence="ECO:0000269|PubMed:21296756"
FT   CONFLICT        270
FT                   /note="E -> G (in Ref. 1; CAG38586)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   558 AA;  66390 MW;  99B7BDBCFD06F98D CRC64;
     MAIPGRQYGL ILPKKTQQLH PVLQKPSVFG NDSDDDDETS VSESLQREAA KKQAMKQTKL
     EIQKALAEDA TVYEYDSIYD EMQKKKEENN PKLLLGKDRK PKYIHNLLKA VEIRKKEQEK
     RMEKKIQRER EMEKGEFDDK EAFVTSAYKK KLQERAEEEE REKRAAALEA CLDVTKQKDL
     SGFYRHLLNQ AVGEEEVPKC SFREARSGIK EEKSRGFSNE VSSKNRIPQE KCILQTDVKV
     EENPDADSDF DAKSSADDEI EETRVNCRRE KVIETPENDF KHHRSQNHSR SPSEERGHST
     RHHTKGSRTS RGHEKREDQH QQKQSRDQEN HYTDRDYRKE RDSHRHREAS HRDSHWKRHE
     QEDKPRARDQ RERSDRVWKR EKDREKYSQR EQERDRQQND QNRPSEKGEK EEKSKAKEEH
     MKVRKERYEN NDKYRDREKR EVGVQSSERN QDRKESSPNS RAKDKFLDQE RSNKMRNMAK
     DKERNQEKPS NSESSLGAKH RLTEEGQEKG KEQERPPEAV SKFAKRNNEE TVMSARDRYL
     ARQMARVNAK TYIEKEDD
//