U1 small nuclear ribonucleoprotein 70 kDa

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Reviewed, UniProtKB/Swiss-Prot P08621 (RU17_HUMAN)

Last modified June 16, 2009. Version 116. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    U1 small nuclear ribonucleoprotein 70 kDa
      Short name=U1 snRNP 70 kDa
      Short name=snRNP70
      Short name=U1-70K

Gene names

Name:	SNRNP70
Synonyms:	RNPU1Z, RPU1, SNRP70, U1AP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Mediates the splicing of pre-mRNA by binding to the loop I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA.
Subunit structure	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 FUSIP1 and SFPQ. Interacts with NUDT21/CPSF5, CPSF6, SFRS2IP, and ZRANB2. Ref.10 Ref.12 Ref.13 Ref.14 Ref.16
Subcellular location	Nucleus.
Post-translational modification	The N-terminus is blocked. Extensively phosphorylated on serine residues in the C-terminal region. Ref.8 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Involvement in disease	Major ribonucleoprotein antigen recognized by the sera from patients with autoimmune diseases, such as systemic lupus erythematosus.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.

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Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Ref.9 Inferred from direct assay. Source: UniProtKB regulation of RNA splicing Ref.3 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	spliceosome Ref.9 Inferred from direct assay. Source: UniProtKB
Molecular function	RNA binding Ref.1 Ref.3 Inferred from mutant phenotype. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Ref.10 Ref.14 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
GSK3B	P49841	1	EBI-1049228,EBI-373586
RNPS1	Q15287	1	EBI-1049228,EBI-395959

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Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P08621-1) 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.

Isoform 2 (identifier: P08621-2) The sequence of this isoform differs from the canonical sequence as follows: 223-231: Missing.

Isoform 3 (identifier: P08621-3) The sequence of this isoform differs from the canonical sequence as follows: 160-166: AYKHADG → TTQLACS 167-437: Missing.

Isoform 4 (identifier: P08621-4) The sequence of this isoform differs from the canonical sequence as follows: 1-159: MTQFLPPNLL...EYEHERDMHS → MEQALHRFGR...PLPLPTSVTA

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 437

437

U1 small nuclear ribonucleoprotein 70 kDa

PRO_0000081880

Regions

Domain

103 – 181

RRM

Compositional bias

231 – 310

Arg/Glu-rich (mixed charge)

Compositional bias

311 – 314

Poly-Gly

Compositional bias

344 – 393

Arg/Asp/Glu-rich (mixed charge)

Compositional bias

394 – 398

Poly-Gly

Amino acid modifications

Modified residue

126

Phosphotyrosine Ref.19

Modified residue

226

Phosphoserine Ref.15 Ref.17 Ref.20 Ref.21 Ref.22

Modified residue

266

Phosphoserine Ref.17

Modified residue

268

Phosphoserine Ref.17

Modified residue

320

Phosphoserine Ref.17 Ref.22

Modified residue

410

Phosphoserine Ref.17 Ref.18 Ref.21 Ref.22

Natural variations

Alternative sequence

1 – 159

159

MTQFL…RDMHS → MEQALHRFGRGLVWLSVAWL SVGRVRVRDDGDTGRGFCRA GPVLTRGPSGDSSPLPLPTS VTA in isoform 4.

VSP_005847

Alternative sequence

160 – 166

AYKHADG → TTQLACS in isoform 3.

VSP_005848

Alternative sequence

167 – 437

271

Missing in isoform 3.

VSP_005849

Alternative sequence

223 – 231

Missing in isoform 2.

VSP_005850

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Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified August 1, 1988. Version 2. Checksum: F1020BF5C40CF97D Show »	FASTA	437	51,557
10 20 30 40 50 60 MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED PRDAPPPTRA 70 80 90 100 110 120 ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD AFKTLFVARV NYDTTESKLR 130 140 150 160 170 180 REFEVYGPIK RIHMVYSKRS GKPRGYAFIE YEHERDMHSA YKHADGKKID GRRVLVDVER 190 200 210 220 230 240 GRTVKGWRPR RLGGGLGGTR RGGADVNIRH SGRDDTSRYD ERPGPSPLPH RDRDRDRERE 250 260 270 280 290 300 RRERSRERDK ERERRRSRSR DRRRRSRSRD KEERRRSRER SKDKDRDRKR RSSRSRERAR 310 320 330 340 350 360 RERERKEELR GGGGDMAEPS EAGDAPPDDG PPGELGPDGP DGPEEKGRDR DRERRRSHRS 370 380 390 400 410 420 ERERRRDRDR DRDRDREHKR GERGSERGRD EARGGGGGQD NGLEGLGNDS RDMYMESEGG 430 DGYLAPENGY LMEAAPE « Hide
Isoform 2. Checksum: EEBC1CE4E8B9DBDA Show »	FASTA	428	50,618
10 20 30 40 50 60 MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED PRDAPPPTRA 70 80 90 100 110 120 ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD AFKTLFVARV NYDTTESKLR 130 140 150 160 170 180 REFEVYGPIK RIHMVYSKRS GKPRGYAFIE YEHERDMHSA YKHADGKKID GRRVLVDVER 190 200 210 220 230 240 GRTVKGWRPR RLGGGLGGTR RGGADVNIRH SGRDDTSRYD ERDRDRDRER ERRERSRERD 250 260 270 280 290 300 KERERRRSRS RDRRRRSRSR DKEERRRSRE RSKDKDRDRK RRSSRSRERA RRERERKEEL 310 320 330 340 350 360 RGGGGDMAEP SEAGDAPPDD GPPGELGPDG PDGPEEKGRD RDRERRRSHR SERERRRDRD 370 380 390 400 410 420 RDRDRDREHK RGERGSERGR DEARGGGGGQ DNGLEGLGND SRDMYMESEG GDGYLAPENG YLMEAAPE « Hide
Isoform 3. Checksum: E90F034A08D3E79C Show »	FASTA	166	19,790
10 20 30 40 50 60 MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED PRDAPPPTRA 70 80 90 100 110 120 ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD AFKTLFVARV NYDTTESKLR 130 140 150 160 REFEVYGPIK RIHMVYSKRS GKPRGYAFIE YEHERDMHST TQLACS « Hide
Isoform 4. Checksum: 390967CC272E50E9 Show »	FASTA	341	39,191
10 20 30 40 50 60 MEQALHRFGR GLVWLSVAWL SVGRVRVRDD GDTGRGFCRA GPVLTRGPSG DSSPLPLPTS 70 80 90 100 110 120 VTAAYKHADG KKIDGRRVLV DVERGRTVKG WRPRRLGGGL GGTRRGGADV NIRHSGRDDT 130 140 150 160 170 180 SRYDERPGPS PLPHRDRDRD RERERRERSR ERDKERERRR SRSRDRRRRS RSRDKEERRR 190 200 210 220 230 240 SRERSKDKDR DRKRRSSRSR ERARRERERK EELRGGGGDM AEPSEAGDAP PDDGPPGELG 250 260 270 280 290 300 PDGPDGPEEK GRDRDRERRR SHRSERERRR DRDRDRDRDR EHKRGERGSE RGRDEARGGG 310 320 330 340 GGQDNGLEGL GNDSRDMYME SEGGDGYLAP ENGYLMEAAP E « Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the human cDNA for the U1 RNA-associated 70K protein." Theissen H., Etzerodt M., Reuter R., Schneider C., Lottspeich F., Argos P., Luehrmann R., Philipson L. EMBO J. 5:3209-3217(1986) [PubMed: 3028775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"The human U1-70K snRNP protein: cDNA cloning, chromosomal localization, expression, alternative splicing and RNA-binding." Spritz R.A., Strunk K., Surowy C.S., Hoch S.O., Barton D.E., Francke U. Nucleic Acids Res. 15:10373-10391(1987) [PubMed: 2447561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[3]	"A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein." Query C.C., Bentley R.C., Keene J.D. Cell 57:89-101(1989) [PubMed: 2467746] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING DOMAIN.
[4]	"Human U1-70K ribonucleoprotein antigen gene: organization, nucleotide sequence, and mapping to locus 19q13.3." Spritz R.A., Strunk K., Surowy C.S., Mohrenweiser H.W. Genomics 8:371-379(1990) [PubMed: 2147422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
[5]	"Identification of an inhibitory element within the human 68-kDa (U1) ribonucleoprotein antigen." Northemann W., Berg H., Stahnke G., Walter M., Hunt N., Fenning S. Protein Expr. Purif. 6:748-756(1995) [PubMed: 8746626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Testis.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[8]	"Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors." Woppmann A., Will C.L., Kornstaedt U., Zuo P., Manley J.L., Luehrmann R. Nucleic Acids Res. 21:2815-2822(1993) [PubMed: 8332490] [Abstract] Cited for: PROTEIN SEQUENCE OF 219-348, PHOSPHORYLATION.
[9]	"A coactivator of pre-mRNA splicing." Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A. Genes Dev. 12:996-1009(1998) [PubMed: 9531537] [Abstract] Cited for: IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRPA1; SRRM1 AND SRRM2.
[10]	"Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing." Zhang W.-J., Wu J.Y. Mol. Cell. Biol. 18:676-684(1998) [PubMed: 9447963] [Abstract] Cited for: INTERACTION WITH SFRS2IP.
[11]	"The SRm160/300 splicing coactivator is required for exon-enhancer function." Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J. Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999) [PubMed: 10339552] [Abstract] Cited for: IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH SNRPA1; SRRM1 AND TRA2B.
[12]	"ZNF265 -- a novel spliceosomal protein able to induce alternative splicing." Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J., Rasko J.E.J. J. Cell Biol. 154:25-32(2001) [PubMed: 11448987] [Abstract] Cited for: INTERACTION WITH ZRANB2.
[13]	"Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions." Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J., Zipori D. Mol. Biol. Cell 12:2328-2340(2001) [PubMed: 11514619] [Abstract] Cited for: INTERACTION WITH SFPQ.
[14]	"Association of polyadenylation cleavage factor I with U1 snRNP." Awasthi S., Alwine J.C. RNA 9:1400-1409(2003) [PubMed: 14561889] [Abstract] Cited for: INTERACTION WITH NUDT21/CPSF5 AND CPSF6.
[15]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: T-cell.
[16]	"Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock." Shin C., Feng Y., Manley J.L. Nature 427:553-558(2004) [PubMed: 14765198] [Abstract] Cited for: INTERACTION WITH FUSIP1.
[17]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-266; SER-268; SER-320 AND SER-410, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-126, MASS SPECTROMETRY.
[20]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: Epithelium.
[21]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-410, MASS SPECTROMETRY.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-320 AND SER-410, MASS SPECTROMETRY.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X04654 mRNA. Translation: CAA28352.1. Different initiation.
X06814 mRNA. Translation: CAA29963.1.
X06815 mRNA. Translation: CAA29964.1. Different initiation.
X06817 mRNA. Translation: CAA29966.1. Different initiation.
X07402 mRNA. Translation: CAA30304.1.
X06816 mRNA. Translation: CAA29965.1.
X06812 mRNA. Translation: CAA29961.1.
X06811 mRNA. Translation: CAA29960.1.
X07401 mRNA. Translation: CAA30303.1.
X07403 mRNA. Translation: CAA30305.1.
M22636 mRNA. Translation: AAA03001.1.
M57939

M57937 Genomic DNA. Translation: AAA36572.1.
M57939

M57937 Genomic DNA. Translation: AAA36573.1.
M57935

M57934 Genomic DNA. Translation: AAA36571.1.
X84841 mRNA. Translation: CAA59278.1.
AL117507 mRNA. Translation: CAB55969.1.
BC001315 mRNA. Translation: AAH01315.1.

IPI

IPI00219483.
IPI00219484.
IPI00219485.
IPI00290204.

PIR

A25707.
S00674.

RefSeq

NP_003080.2.

UniGene

Hs.467097

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CW1	X-ray	5.49	6/7/8/K	1-216	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P08621. 3 interactions.

PTM databases

PhosphoSite

P08621.

Proteomic databases

PRIDE

P08621.

Genome annotation databases

Ensembl

ENSG00000104852. Homo sapiens. [Contig view]

GeneID

6625.

KEGG

hsa:6625.

Organism-specific databases

GeneCards

GC19P054285.

H-InvDB

HIX0015316.
HIX0020490.

HGNC

HGNC:11150. SNRNP70.

HPA

CAB001718.

MIM

180740. gene.

PharmGKB

PA35992.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P08621.

OMA

P08621. GRDMYME.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P08621.

Bgee

P08621.

GermOnline

ENSG00000104852. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

25805.

PMAP-CutDB

P08621.

SOURCE

Search...

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Entry information

Entry name

RU17_HUMAN

Accession

Primary (citable) accession number: P08621
Secondary accession number(s): P78493

Q9UFQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents