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Protein

U1 small nuclear ribonucleoprotein 70 kDa

Gene

Snrnp70

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA (By similarity).By similarity

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: MGI
  3. RNA binding Source: UniProtKB

GO - Biological processi

  1. mRNA splicing, via spliceosome Source: UniProtKB
  2. positive regulation of mRNA splicing, via spliceosome Source: MGI
  3. regulation of RNA splicing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_307866. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
U1 small nuclear ribonucleoprotein 70 kDa
Short name:
U1 snRNP 70 kDa
Short name:
U1-70K
Short name:
snRNP70
Gene namesi
Name:Snrnp70
Synonyms:Snrp70
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98341. Snrnp70.

Subcellular locationi

Nucleus speckle 1 Publication. Nucleusnucleoplasm 1 Publication
Note: Colocalizes with SCNM1 and LUC7L2 in nuclear speckles.

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB-SubCell
  2. nucleoplasm Source: MGI
  3. nucleus Source: MGI
  4. spliceosomal complex Source: UniProtKB
  5. U1 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 448447U1 small nuclear ribonucleoprotein 70 kDaPRO_0000081881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei118 – 1181N6-acetyllysineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei268 – 2681PhosphoserineBy similarity
Modified residuei332 – 3321PhosphoserineBy similarity
Modified residuei408 – 4081Phosphoserine2 Publications
Modified residuei419 – 4191Phosphoserine1 Publication

Post-translational modificationi

Extensively phosphorylated on serine residues in the C-terminal region.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ62376.
PaxDbiQ62376.
PRIDEiQ62376.

PTM databases

PhosphoSiteiQ62376.

Expressioni

Gene expression databases

BgeeiQ62376.
ExpressionAtlasiQ62376. baseline and differential.
GenevestigatoriQ62376.

Interactioni

Subunit structurei

U1 snRNP is composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Interacts with SCNM1. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRNP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Interacts with dephosphorylated SFRS13A and SFPQ. Interacts with NUDT21/CPSF5, CPSF6, SCAF11, and ZRANB2.1 Publication

Protein-protein interaction databases

BioGridi203376. 2 interactions.
IntActiQ62376. 2 interactions.
MINTiMINT-1868298.

Structurei

3D structure databases

ProteinModelPortaliQ62376.
SMRiQ62376. Positions 114-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 18179RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi231 – 31080Arg/Glu-rich (mixed charge)Add
BLAST
Compositional biasi311 – 32616Poly-GlyAdd
BLAST
Compositional biasi356 – 40348Arg/Asp/Glu-rich (mixed charge)Add
BLAST
Compositional biasi404 – 4096Poly-Gly

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00530000063750.
HOGENOMiHOG000236289.
HOVERGENiHBG094947.
InParanoidiQ62376.
KOiK11093.
OMAiGNESRDM.
OrthoDBiEOG79W96V.
PhylomeDBiQ62376.
TreeFamiTF314215.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR022023. U1snRNP70_N.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
PF12220. U1snRNP70_N. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q62376-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED
60 70 80 90 100
PRDAPPPTRA ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD
110 120 130 140 150
AFKTLFVARV NYDTTESKLR REFEVYGPIK RIHMVYSKRS GKPRGYAFIE
160 170 180 190 200
YEHERDMHSA YKHADGKKID GRRVLVDVER GRTVKGWRPR RLGGGLGGTR
210 220 230 240 250
RGGADVNIRH SGRDDTSRYD ERPGPSPLPH RDRDRDRERE RRERSRERDK
260 270 280 290 300
ERERRRSRSR DRRRRSRSRD KDERRRSRER SKDKDRDRKR RSSRSRERAR
310 320 330 340 350
RERERKEELR GGGGGGGGGS GGGGGGDMAE PSEAGDGAPD DGPPGELGPE
360 370 380 390 400
GPDGPEEKGR DRDRERRRSH RSERERRRDR DRDRDREHKR GERGSERGRD
410 420 430 440
EARGGGGSGQ DNGLEGLGSD GRDMYMEAEG GDGYMAPENG YLMEAAPE
Length:448
Mass (Da):51,992
Last modified:December 5, 2005 - v2
Checksum:i5B025A3B6992D0BD
GO
Isoform 2 (identifier: Q62376-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     160-166: AYKHADG → TTQLACS
     167-448: Missing.

Show »
Length:166
Mass (Da):19,790
Checksum:iE90F034A08D3E79C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti263 – 2631R → Q in CAA33777 (PubMed:2525092).Curated
Sequence conflicti281 – 2811S → T in CAA33777 (PubMed:2525092).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei160 – 1667AYKHADG → TTQLACS in isoform 2. CuratedVSP_005851
Alternative sequencei167 – 448282Missing in isoform 2. CuratedVSP_005852Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK133115 mRNA. Translation: BAE21515.1.
AK146729 mRNA. Translation: BAE27392.1.
X15769
, X15770, X15771, X15772, X15774, X15775, X15776 Genomic DNA. Translation: CAA33777.1.
CCDSiCCDS21240.1. [Q62376-1]
PIRiS04336.
S04824.
RefSeqiNP_033250.3. NM_009224.5. [Q62376-1]
XP_006540795.1. XM_006540732.2. [Q62376-1]
UniGeneiMm.216386.

Genome annotation databases

EnsembliENSMUST00000074575; ENSMUSP00000074160; ENSMUSG00000063511. [Q62376-1]
GeneIDi20637.
KEGGimmu:20637.
UCSCiuc009guw.1. mouse. [Q62376-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK133115 mRNA. Translation: BAE21515.1.
AK146729 mRNA. Translation: BAE27392.1.
X15769
, X15770, X15771, X15772, X15774, X15775, X15776 Genomic DNA. Translation: CAA33777.1.
CCDSiCCDS21240.1. [Q62376-1]
PIRiS04336.
S04824.
RefSeqiNP_033250.3. NM_009224.5. [Q62376-1]
XP_006540795.1. XM_006540732.2. [Q62376-1]
UniGeneiMm.216386.

3D structure databases

ProteinModelPortaliQ62376.
SMRiQ62376. Positions 114-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203376. 2 interactions.
IntActiQ62376. 2 interactions.
MINTiMINT-1868298.

PTM databases

PhosphoSiteiQ62376.

Proteomic databases

MaxQBiQ62376.
PaxDbiQ62376.
PRIDEiQ62376.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074575; ENSMUSP00000074160; ENSMUSG00000063511. [Q62376-1]
GeneIDi20637.
KEGGimmu:20637.
UCSCiuc009guw.1. mouse. [Q62376-1]

Organism-specific databases

CTDi6625.
MGIiMGI:98341. Snrnp70.

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00530000063750.
HOGENOMiHOG000236289.
HOVERGENiHBG094947.
InParanoidiQ62376.
KOiK11093.
OMAiGNESRDM.
OrthoDBiEOG79W96V.
PhylomeDBiQ62376.
TreeFamiTF314215.

Enzyme and pathway databases

ReactomeiREACT_307866. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSnrnp70. mouse.
NextBioi299035.
PROiQ62376.
SOURCEiSearch...

Gene expression databases

BgeeiQ62376.
ExpressionAtlasiQ62376. baseline and differential.
GenevestigatoriQ62376.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR022023. U1snRNP70_N.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
PF12220. U1snRNP70_N. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Kidney and Testis.
  2. "Analysis of genomic clones of the murine U1RNA-associated 70-kDa protein reveals a high evolutionary conservation of the protein between human and mouse."
    Hornig H., Fischer U., Costas M., Rauh A., Luehrmann R.
    Eur. J. Biochem. 182:45-50(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-448 (ISOFORMS 1 AND 2).
    Strain: BALB/c.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. "Evidence for a direct role of the disease modifier SCNM1 in splicing."
    Howell V.M., Jones J.M., Bergren S.K., Li L., Billi A.C., Avenarius M.R., Meisler M.H.
    Hum. Mol. Genet. 16:2506-2516(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCNM1, SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRU17_MOUSE
AccessioniPrimary (citable) accession number: Q62376
Secondary accession number(s): Q3UIW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2001
Last sequence update: December 5, 2005
Last modified: March 31, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.