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Protein

Nuclear speckle splicing regulatory protein 1

Gene

NSRP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA-binding protein that mediates pre-mRNA alternative splicing regulation.1 Publication

GO - Molecular functioni

  • mRNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • developmental process Source: UniProtKB
  • mRNA processing Source: UniProtKB-KW
  • nucleocytoplasmic transport Source: UniProtKB
  • regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  • RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear speckle splicing regulatory protein 1
Alternative name(s):
Coiled-coil domain-containing protein 55
Nuclear speckle-related protein 70
Short name:
NSrp70
Gene namesi
Name:NSRP1
Synonyms:CCDC55, NSRP70
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:25305. NSRP1.

Subcellular locationi

GO - Cellular componenti

  • intracellular ribonucleoprotein complex Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi536 – 5372RD → AA: Inhibits nuclear localization and alternative splicing activity. 1 Publication

Organism-specific databases

PharmGKBiPA142672171.

Polymorphism and mutation databases

BioMutaiNSRP1.
DMDMi74733524.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Nuclear speckle splicing regulatory protein 1PRO_0000240434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei33 – 331PhosphoserineCombined sources
Cross-linki210 – 210Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei248 – 2481PhosphoserineCombined sources
Modified residuei254 – 2541PhosphoserineCombined sources
Modified residuei255 – 2551PhosphoserineCombined sources
Modified residuei275 – 2751PhosphothreonineCombined sources
Modified residuei457 – 4571PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9H0G5.
MaxQBiQ9H0G5.
PaxDbiQ9H0G5.
PRIDEiQ9H0G5.

PTM databases

iPTMnetiQ9H0G5.
PhosphoSiteiQ9H0G5.

Expressioni

Tissue specificityi

Expressed in dendritic cells, T-cells, B-cells and natural killer cells. Expressed in secondary lymphoid organs such as spleen and mesenteric, axillary and brachial lymph nodes.1 Publication

Inductioni

Up-regulated in motile T-cells.1 Publication

Gene expression databases

BgeeiQ9H0G5.
CleanExiHS_CCDC55.
ExpressionAtlasiQ9H0G5. baseline and differential.
GenevisibleiQ9H0G5. HS.

Organism-specific databases

HPAiHPA015593.
HPA015603.

Interactioni

Subunit structurei

Interacts (via C-terminus) with SRSF1. Interacts (via C-terminus) with SRSF2.1 Publication

Protein-protein interaction databases

BioGridi123876. 18 interactions.
IntActiQ9H0G5. 10 interactions.
MINTiMINT-2817156.
STRINGi9606.ENSP00000247026.

Structurei

3D structure databases

ProteinModelPortaliQ9H0G5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 17065Necessary for alternative splicing activityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili104 – 17067Sequence analysisAdd
BLAST
Coiled coili379 – 42749Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 376Poly-Asp
Compositional biasi282 – 35978His-richAdd
BLAST

Sequence similaritiesi

Belongs to the NSRP1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2117. Eukaryota.
ENOG410Z5A1. LUCA.
GeneTreeiENSGT00730000111127.
HOVERGENiHBG081043.
InParanoidiQ9H0G5.
KOiK13206.
OMAiQQNDQNR.
OrthoDBiEOG7FR7JN.
PhylomeDBiQ9H0G5.
TreeFamiTF319359.

Family and domain databases

InterProiIPR018612. DUF2040.
[Graphical view]
PfamiPF09745. DUF2040. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H0G5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIPGRQYGL ILPKKTQQLH PVLQKPSVFG NDSDDDDETS VSESLQREAA
60 70 80 90 100
KKQAMKQTKL EIQKALAEDA TVYEYDSIYD EMQKKKEENN PKLLLGKDRK
110 120 130 140 150
PKYIHNLLKA VEIRKKEQEK RMEKKIQRER EMEKGEFDDK EAFVTSAYKK
160 170 180 190 200
KLQERAEEEE REKRAAALEA CLDVTKQKDL SGFYRHLLNQ AVGEEEVPKC
210 220 230 240 250
SFREARSGIK EEKSRGFSNE VSSKNRIPQE KCILQTDVKV EENPDADSDF
260 270 280 290 300
DAKSSADDEI EETRVNCRRE KVIETPENDF KHHRSQNHSR SPSEERGHST
310 320 330 340 350
RHHTKGSRTS RGHEKREDQH QQKQSRDQEN HYTDRDYRKE RDSHRHREAS
360 370 380 390 400
HRDSHWKRHE QEDKPRARDQ RERSDRVWKR EKDREKYSQR EQERDRQQND
410 420 430 440 450
QNRPSEKGEK EEKSKAKEEH MKVRKERYEN NDKYRDREKR EVGVQSSERN
460 470 480 490 500
QDRKESSPNS RAKDKFLDQE RSNKMRNMAK DKERNQEKPS NSESSLGAKH
510 520 530 540 550
RLTEEGQEKG KEQERPPEAV SKFAKRNNEE TVMSARDRYL ARQMARVNAK

TYIEKEDD
Length:558
Mass (Da):66,390
Last modified:March 1, 2001 - v1
Checksum:i99B7BDBCFD06F98D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti270 – 2701E → G in CAG38586 (PubMed:11230166).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861K → T.
Corresponds to variant rs11544945 [ dbSNP | Ensembl ].
VAR_054104

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136806 mRNA. Translation: CAB66740.1.
CR533555 mRNA. Translation: CAG38586.1.
AC104984 Genomic DNA. No translation available.
BC040118 mRNA. Translation: AAH40118.1.
BC105044 mRNA. Translation: AAI05045.1.
BC105046 mRNA. Translation: AAI05047.1.
CCDSiCCDS11255.1.
RefSeqiNP_001248396.1. NM_001261467.1.
NP_115517.1. NM_032141.3.
UniGeneiHs.462663.

Genome annotation databases

EnsembliENST00000247026; ENSP00000247026; ENSG00000126653.
GeneIDi84081.
KEGGihsa:84081.
UCSCiuc002heu.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136806 mRNA. Translation: CAB66740.1.
CR533555 mRNA. Translation: CAG38586.1.
AC104984 Genomic DNA. No translation available.
BC040118 mRNA. Translation: AAH40118.1.
BC105044 mRNA. Translation: AAI05045.1.
BC105046 mRNA. Translation: AAI05047.1.
CCDSiCCDS11255.1.
RefSeqiNP_001248396.1. NM_001261467.1.
NP_115517.1. NM_032141.3.
UniGeneiHs.462663.

3D structure databases

ProteinModelPortaliQ9H0G5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123876. 18 interactions.
IntActiQ9H0G5. 10 interactions.
MINTiMINT-2817156.
STRINGi9606.ENSP00000247026.

PTM databases

iPTMnetiQ9H0G5.
PhosphoSiteiQ9H0G5.

Polymorphism and mutation databases

BioMutaiNSRP1.
DMDMi74733524.

Proteomic databases

EPDiQ9H0G5.
MaxQBiQ9H0G5.
PaxDbiQ9H0G5.
PRIDEiQ9H0G5.

Protocols and materials databases

DNASUi84081.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247026; ENSP00000247026; ENSG00000126653.
GeneIDi84081.
KEGGihsa:84081.
UCSCiuc002heu.5. human.

Organism-specific databases

CTDi84081.
GeneCardsiNSRP1.
HGNCiHGNC:25305. NSRP1.
HPAiHPA015593.
HPA015603.
MIMi616173. gene.
neXtProtiNX_Q9H0G5.
PharmGKBiPA142672171.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2117. Eukaryota.
ENOG410Z5A1. LUCA.
GeneTreeiENSGT00730000111127.
HOVERGENiHBG081043.
InParanoidiQ9H0G5.
KOiK13206.
OMAiQQNDQNR.
OrthoDBiEOG7FR7JN.
PhylomeDBiQ9H0G5.
TreeFamiTF319359.

Miscellaneous databases

ChiTaRSiNSRP1. human.
GeneWikiiCCDC55_(gene).
GenomeRNAii84081.
NextBioi73307.
PROiQ9H0G5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H0G5.
CleanExiHS_CCDC55.
ExpressionAtlasiQ9H0G5. baseline and differential.
GenevisibleiQ9H0G5. HS.

Family and domain databases

InterProiIPR018612. DUF2040.
[Graphical view]
PfamiPF09745. DUF2040. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-248; SER-254 AND SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-254 AND SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "NSrp70 is a novel nuclear speckle-related protein that modulates alternative pre-mRNA splicing in vivo."
    Kim Y.D., Lee J.Y., Oh K.M., Araki M., Araki K., Yamamura K.I., Jun C.D.
    Nucleic Acids Res. 39:4300-4314(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRSF1 AND SRSF2, RNA-BINDING, MUTAGENESIS OF 536-ARG-ASP-537, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-33; SER-248; SER-254 AND SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNSRP1_HUMAN
AccessioniPrimary (citable) accession number: Q9H0G5
Secondary accession number(s): Q6FI71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.