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P08621 (RU17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18

Subcellular location

Nucleus. Nucleus speckle By similarity. Nucleusnucleoplasm 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.24
Chain2 – 437436U1 small nuclear ribonucleoprotein 70 kDa
PRO_0000081880

Regions

Domain103 – 18179RRM
Compositional bias231 – 31080Arg/Glu-rich (mixed charge)
Compositional bias311 – 3144Poly-Gly
Compositional bias344 – 39350Arg/Asp/Glu-rich (mixed charge)
Compositional bias394 – 3985Poly-Gly

Amino acid modifications

Modified residue21N-acetylthreonine Ref.24 Ref.31
Modified residue1181N6-acetyllysine Ref.27
Modified residue2261Phosphoserine Ref.17 Ref.19 Ref.21 Ref.23 Ref.25 Ref.28 Ref.30
Modified residue2681Phosphoserine Ref.28
Modified residue3201Phosphoserine Ref.19 Ref.26 Ref.28 Ref.30
Modified residue4101Phosphoserine Ref.19 Ref.20 Ref.22 Ref.26 Ref.28 Ref.30

Natural variations

Alternative sequence1 – 159159MTQFL…RDMHS → MEQALHRFGRGLVWLSVAWL SVGRVRVRDDGDTGRGFCRA GPVLTRGPSGDSSPLPLPTS VTA in isoform 4.
VSP_005847
Alternative sequence160 – 1667AYKHADG → TTQLACS in isoform 3.
VSP_005848
Alternative sequence167 – 437271Missing in isoform 3.
VSP_005849
Alternative sequence223 – 2319Missing in isoform 2.
VSP_005850

Secondary structure

.... 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1988. Version 2.
Checksum: F1020BF5C40CF97D

FASTA43751,557
        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 [UniParc].

Checksum: EEBC1CE4E8B9DBDA
Show »

FASTA42850,618
Isoform 3 [UniParc].

Checksum: E90F034A08D3E79C
Show »

FASTA16619,790
Isoform 4 [UniParc].

Checksum: 390967CC272E50E9
Show »

FASTA34139,191

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[25]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"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].
[30]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-216 IN SPLICEOSOMAL U1 SNRNP.
+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 expand/collapse EMBL AC list , M57929, M57930, M57932, M57934, M57937 Genomic DNA. Translation: AAA36572.1.
M57939 expand/collapse EMBL AC list , M57929, M57930, M57932, M57934, M57937 Genomic DNA. Translation: AAA36573.1.
M57935 expand/collapse EMBL AC list , 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.
PIRA25707.
S00674.
RefSeqNP_003080.2. NM_003089.4.
XP_005259234.1. XM_005259177.1.
UniGeneHs.467097.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L5INMR-A131-151[»]
2L5JNMR-A131-151[»]
3CW1X-ray5.496/7/8/K1-216[»]
3PGWX-ray4.40L/S1-437[»]
ProteinModelPortalP08621.
SMRP08621. Positions 114-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112509. 99 interactions.
DIPDIP-29406N.
IntActP08621. 44 interactions.
MINTMINT-5004037.

PTM databases

PhosphoSiteP08621.

Polymorphism databases

DMDM13635663.

Proteomic databases

PaxDbP08621.
PRIDEP08621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221448; ENSP00000221448; ENSG00000104852. [P08621-2]
ENST00000401730; ENSP00000385077; ENSG00000104852. [P08621-3]
ENST00000595231; ENSP00000471006; ENSG00000104852. [P08621-3]
ENST00000598441; ENSP00000472998; ENSG00000104852. [P08621-1]
ENST00000601065; ENSP00000468952; ENSG00000104852. [P08621-3]
GeneID6625.
KEGGhsa:6625.
UCSCuc002pmk.3. human. [P08621-1]

Organism-specific databases

CTD6625.
GeneCardsGC19P049588.
HGNCHGNC:11150. SNRNP70.
HPACAB001718.
HPA042050.
HPA043516.
MIM180740. gene.
neXtProtNX_P08621.
PharmGKBPA35992.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
InParanoidP08621.
KOK11093.
OMADGRDMYM.
OrthoDBEOG79W96V.
PhylomeDBP08621.
TreeFamTF314215.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP08621.
BgeeP08621.
GenevestigatorP08621.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR022023. U1snRNP70_N.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
PF12220. U1snRNP70_N. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNRNP70. human.
EvolutionaryTraceP08621.
GeneWikiSnRNP70.
GenomeRNAi6625.
NextBio25805.
PMAP-CutDBP08621.
PROP08621.
SOURCESearch...

Entry information

Entry nameRU17_HUMAN
AccessionPrimary (citable) accession number: P08621
Secondary accession number(s): B3KUA3 expand/collapse secondary AC list , 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: April 16, 2014
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 19

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