NSRP1_HUMAN
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 03-AUG-2022, entry version 151.
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 AlphaFoldDB; Q9H0G5; -.
DR SMR; Q9H0G5; -.
DR BioGRID; 123876; 144.
DR IntAct; Q9H0G5; 22.
DR MINT; Q9H0G5; -.
DR STRING; 9606.ENSP00000247026; -.
DR GlyGen; Q9H0G5; 1 site, 1 O-linked glycan (1 site).
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; 111 antibodies from 23 providers.
DR DNASU; 84081; -.
DR Ensembl; ENST00000247026.10; ENSP00000247026.5; ENSG00000126653.18.
DR GeneID; 84081; -.
DR KEGG; hsa:84081; -.
DR MANE-Select; ENST00000247026.10; ENSP00000247026.5; NM_032141.4; NP_115517.1.
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; -.
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 SignaLink; Q9H0G5; -.
DR BioGRID-ORCS; 84081; 130 hits in 1078 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 185 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; IPR042816; Nsrp1.
DR InterPro; IPR018612; NSRP1_N.
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
