P08621 (RU17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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	Interacts with SCNM1 By similarity. 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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18
Subcellular location	Nucleus. Nucleus speckle By similarity. Nucleus › nucleoplasm By similarity. Note: Colocalizes with SCNM1 and LUC7L2 in nuclear speckles By similarity.
Post-translational modification	The N-terminus is blocked. Extensively phosphorylated on serine residues in the C-terminal region. Ref.10
Miscellaneous	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.
Sequence caution	The sequence CAA28352.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA29964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA29966.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred from direct assay Ref.11. Source: UniProtKB regulation of RNA splicing Inferred from mutant phenotype Ref.3. Source: UniProtKB
Cellular_component	nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome spliceosomal complex Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	RNA binding Inferred from mutant phenotype Ref.3. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CLK2	P49760	2	EBI-1049228,EBI-750020

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

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

79

RRM

Compositional bias

231 – 310

80

Arg/Glu-rich (mixed charge)

Compositional bias

311 – 314

4

Poly-Gly

Compositional bias

344 – 393

50

Arg/Asp/Glu-rich (mixed charge)

Compositional bias

394 – 398

5

Poly-Gly

Amino acid modifications

Modified residue

118

1

N6-acetyllysine Ref.26

Modified residue

226

1

Phosphoserine Ref.17 Ref.19 Ref.21 Ref.23 Ref.24 Ref.27 Ref.29

Modified residue

268

1

Phosphoserine Ref.27

Modified residue

320

1

Phosphoserine Ref.19 Ref.25 Ref.27 Ref.29

Modified residue

410

1

Phosphoserine Ref.19 Ref.20 Ref.22 Ref.25 Ref.27 Ref.29

Natural variations

Alternative sequence

1 – 159

159

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

VSP_005847

Alternative sequence

160 – 166

7

AYKHADG → TTQLACS in isoform 3.

VSP_005848

Alternative sequence

167 – 437

271

Missing in isoform 3.

VSP_005849

Alternative sequence

223 – 231

9

Missing in isoform 2.

VSP_005850

Secondary structure

1

.

.

.

.

437

Helix Strand Turn

Details...

Turn

139 – 141

3

Turn

142 – 150

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1988. Version 2. Checksum: F1020BF5C40CF97D	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
	Isoform 2 [UniParc]. Checksum: EEBC1CE4E8B9DBDA	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
	Isoform 3 [UniParc]. Checksum: E90F034A08D3E79C	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
	Isoform 4 [UniParc]. Checksum: 390967CC272E50E9	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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Prostate.
[7]	"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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Testis.
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORM 1). Tissue: Placenta.
[10]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 219-348, PHOSPHORYLATION.
[11]	"A coactivator of pre-mRNA splicing." Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A. Genes Dev. 12:996-1009(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRPA1; SRRM1 AND SRRM2.
[12]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCAF11.
[13]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH SNRPA1; SRRM1 AND TRA2B.
[14]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZRANB2.
[15]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SFPQ.
[16]	"Association of polyadenylation cleavage factor I with U1 snRNP." Awasthi S., Alwine J.C. RNA 9:1400-1409(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NUDT21/CPSF5 AND CPSF6.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SFRS13A.
[19]	"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-226; SER-320 AND SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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 SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY.
[25]	"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-320 AND SER-410, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, MASS SPECTROMETRY.
[27]	"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-226; SER-268; SER-320 AND SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]	"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-226; SER-320 AND SER-410, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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 , M57929, M57930, M57932, M57934, M57937 Genomic DNA. Translation: AAA36572.1.
M57939 , M57929, M57930, M57932, M57934, M57937 Genomic DNA. Translation: AAA36573.1.
M57935 , M57929, M57930, M57932, M57934 Genomic DNA. Translation: AAA36571.1.
AK096783 mRNA. Translation: BAG53365.1.
X84841 mRNA. Translation: CAA59278.1.
AL117507 mRNA. Translation: CAB55969.1.
CH471177 Genomic DNA. Translation: EAW52449.1.
BC001315 mRNA. Translation: AAH01315.1.

IPI

IPI00219483.
IPI00219484.
IPI00219485.
IPI00290204.

PIR

A25707.
S00674.

RefSeq

NP_003080.2. NM_003089.4.

UniGene

Hs.467097.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L5I	NMR	-	A	131-151	[»]
2L5J	NMR	-	A	131-151	[»]
3CW1	X-ray	5.49	6/7/8/K	1-216	[»]
3PGW	X-ray	4.40	L/S	1-437	[»]

ProteinModelPortal

P08621.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29406N.

IntAct

P08621. 21 interactions.

MINT

MINT-5004037.

PTM databases

PhosphoSite

P08621.

Polymorphism databases

DMDM

13635663.

Proteomic databases

PaxDb

P08621.

PRIDE

P08621.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221448; ENSP00000221448; ENSG00000104852.
ENST00000401730; ENSP00000385077; ENSG00000104852.
ENST00000595231; ENSP00000471006; ENSG00000104852.
ENST00000598441; ENSP00000472998; ENSG00000104852.
ENST00000601065; ENSP00000468952; ENSG00000104852.

GeneID

6625.

KEGG

hsa:6625.

UCSC

uc002pmk.3. human.

Organism-specific databases

CTD

6625.

GeneCards

GC19P049588.

HGNC

HGNC:11150. SNRNP70.

HPA

CAB001718.

MIM

180740. gene.

neXtProt

NX_P08621.

PharmGKB

PA35992.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

InParanoid

P08621.

KO

K11093.

OMA

KKSRGYL.

OrthoDB

EOG4CJVJ7.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P08621.

Bgee

P08621.

Genevestigator

P08621.

GermOnline

ENSG00000104852. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR022023. U1snRNP70_N.
[Graphical view]

Pfam

PF00076. RRM_1. 1 hit.
PF12220. U1snRNP70_N. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SNRNP70. human.

EvolutionaryTrace

P08621.

GenomeRNAi

6625.

NextBio

25805.

PMAP-CutDB

P08621.

SOURCE

Search...

Entry information

Entry name

RU17_HUMAN

Accession

Primary (citable) accession number: P08621
Secondary accession number(s): B3KUA3 , P78493, P78494, Q15364, Q15686, Q15687, Q15689, Q99377, Q9UE45, Q9UE46, Q9UE47, Q9UE48, Q9UFQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 159 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.