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Protein

U1 small nuclear ribonucleoprotein 70 kDa

Gene

SNRNP70

Organism
Homo sapiens (Human)
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.

GO - Molecular functioni

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

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA processing Source: ProtInc
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. positive regulation of mRNA splicing, via spliceosome Source: Ensembl
  5. regulation of RNA splicing Source: UniProtKB
  6. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_467. 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:RNPU1Z, RPU1, SNRP70, U1AP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11150. SNRNP70.

Subcellular locationi

Nucleus. Nucleus speckle By similarity. Nucleusnucleoplasm By similarity
Note: Colocalizes with SCNM1 and LUC7L2 in nuclear speckles.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35992.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 437436U1 small nuclear ribonucleoprotein 70 kDaPRO_0000081880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine2 Publications
Modified residuei118 – 1181N6-acetyllysine1 Publication
Modified residuei226 – 2261Phosphoserine8 Publications
Modified residuei268 – 2681Phosphoserine1 Publication
Modified residuei320 – 3201Phosphoserine5 Publications
Modified residuei410 – 4101Phosphoserine6 Publications

Post-translational modificationi

The N-terminus is blocked.
Extensively phosphorylated on serine residues in the C-terminal region.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP08621.
PaxDbiP08621.
PRIDEiP08621.

PTM databases

PhosphoSiteiP08621.

Miscellaneous databases

PMAP-CutDBP08621.

Expressioni

Gene expression databases

BgeeiP08621.
ExpressionAtlasiP08621. baseline and differential.
GenevestigatoriP08621.

Organism-specific databases

HPAiCAB001718.
HPA042050.
HPA043516.

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 ZRANB2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CLK2P497602EBI-1049228,EBI-750020
SRPK2P783623EBI-1049228,EBI-593303

Protein-protein interaction databases

BioGridi112509. 108 interactions.
DIPiDIP-29406N.
IntActiP08621. 44 interactions.
MINTiMINT-5004037.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104Combined sources
Helixi29 – 313Combined sources
Helixi42 – 476Combined sources
Helixi51 – 533Combined sources
Helixi63 – 8624Combined sources
Helixi91 – 933Combined sources
Helixi101 – 1033Combined sources
Beta strandi104 – 1096Combined sources
Helixi116 – 1249Combined sources
Beta strandi129 – 1368Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 15311Combined sources
Helixi154 – 16310Combined sources
Beta strandi175 – 1784Combined sources
Turni181 – 1833Combined sources
Helixi190 – 1923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L5INMR-A131-151[»]
2L5JNMR-A131-151[»]
3CW1X-ray5.496/7/8/K1-216[»]
3PGWX-ray4.40L/S1-437[»]
4PJOX-ray3.30K/N/k/n2-60[»]
4PKDX-ray2.50B60-215[»]
ProteinModelPortaliP08621.
SMRiP08621. Positions 114-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08621.

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 – 3144Poly-Gly
Compositional biasi344 – 39350Arg/Asp/Glu-rich (mixed charge)Add
BLAST
Compositional biasi394 – 3985Poly-Gly

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00530000063750.
InParanoidiP08621.
KOiK11093.
OMAiGNESRDM.
OrthoDBiEOG79W96V.
PhylomeDBiP08621.
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08621-1) [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 KEERRRSRER SKDKDRDRKR RSSRSRERAR
310 320 330 340 350
RERERKEELR GGGGDMAEPS EAGDAPPDDG PPGELGPDGP DGPEEKGRDR
360 370 380 390 400
DRERRRSHRS ERERRRDRDR DRDRDREHKR GERGSERGRD EARGGGGGQD
410 420 430
NGLEGLGNDS RDMYMESEGG DGYLAPENGY LMEAAPE
Length:437
Mass (Da):51,557
Last modified:July 31, 1988 - v2
Checksum:iF1020BF5C40CF97D
GO
Isoform 2 (identifier: P08621-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     223-231: Missing.

Show »
Length:428
Mass (Da):50,618
Checksum:iEEBC1CE4E8B9DBDA
GO
Isoform 3 (identifier: P08621-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     160-166: AYKHADG → TTQLACS
     167-437: Missing.

Show »
Length:166
Mass (Da):19,790
Checksum:iE90F034A08D3E79C
GO
Isoform 4 (identifier: P08621-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: MTQFLPPNLL...EYEHERDMHS → MEQALHRFGR...PLPLPTSVTA

Show »
Length:341
Mass (Da):39,191
Checksum:i390967CC272E50E9
GO

Sequence cautioni

The sequence CAA28352.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA29964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA29966.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 159159MTQFL…RDMHS → MEQALHRFGRGLVWLSVAWL SVGRVRVRDDGDTGRGFCRA GPVLTRGPSGDSSPLPLPTS VTA in isoform 4. 1 PublicationVSP_005847Add
BLAST
Alternative sequencei160 – 1667AYKHADG → TTQLACS in isoform 3. 1 PublicationVSP_005848
Alternative sequencei167 – 437271Missing in isoform 3. 1 PublicationVSP_005849Add
BLAST
Alternative sequencei223 – 2319Missing in isoform 2. CuratedVSP_005850

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12756.1. [P08621-1]
CCDS74417.1. [P08621-2]
PIRiA25707.
S00674.
RefSeqiNP_001287998.1. NM_001301069.1. [P08621-2]
NP_003080.2. NM_003089.5. [P08621-1]
UniGeneiHs.467097.

Genome annotation databases

EnsembliENST00000221448; ENSP00000221448; ENSG00000104852. [P08621-2]
ENST00000401730; ENSP00000385077; ENSG00000104852. [P08621-3]
ENST00000595231; ENSP00000471006; ENSG00000104852. [P08621-3]
ENST00000598441; ENSP00000472998; ENSG00000104852. [P08621-1]
ENST00000601065; ENSP00000468952; ENSG00000104852. [P08621-3]
GeneIDi6625.
KEGGihsa:6625.
UCSCiuc002pmk.3. human. [P08621-1]

Polymorphism databases

DMDMi13635663.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12756.1. [P08621-1]
CCDS74417.1. [P08621-2]
PIRiA25707.
S00674.
RefSeqiNP_001287998.1. NM_001301069.1. [P08621-2]
NP_003080.2. NM_003089.5. [P08621-1]
UniGeneiHs.467097.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L5INMR-A131-151[»]
2L5JNMR-A131-151[»]
3CW1X-ray5.496/7/8/K1-216[»]
3PGWX-ray4.40L/S1-437[»]
4PJOX-ray3.30K/N/k/n2-60[»]
4PKDX-ray2.50B60-215[»]
ProteinModelPortaliP08621.
SMRiP08621. Positions 114-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112509. 108 interactions.
DIPiDIP-29406N.
IntActiP08621. 44 interactions.
MINTiMINT-5004037.

PTM databases

PhosphoSiteiP08621.

Polymorphism databases

DMDMi13635663.

Proteomic databases

MaxQBiP08621.
PaxDbiP08621.
PRIDEiP08621.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221448; ENSP00000221448; ENSG00000104852. [P08621-2]
ENST00000401730; ENSP00000385077; ENSG00000104852. [P08621-3]
ENST00000595231; ENSP00000471006; ENSG00000104852. [P08621-3]
ENST00000598441; ENSP00000472998; ENSG00000104852. [P08621-1]
ENST00000601065; ENSP00000468952; ENSG00000104852. [P08621-3]
GeneIDi6625.
KEGGihsa:6625.
UCSCiuc002pmk.3. human. [P08621-1]

Organism-specific databases

CTDi6625.
GeneCardsiGC19P049588.
HGNCiHGNC:11150. SNRNP70.
HPAiCAB001718.
HPA042050.
HPA043516.
MIMi180740. gene.
neXtProtiNX_P08621.
PharmGKBiPA35992.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00530000063750.
InParanoidiP08621.
KOiK11093.
OMAiGNESRDM.
OrthoDBiEOG79W96V.
PhylomeDBiP08621.
TreeFamiTF314215.

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSNRNP70. human.
EvolutionaryTraceiP08621.
GeneWikiiSnRNP70.
GenomeRNAii6625.
NextBioi25805.
PMAP-CutDBP08621.
PROiP08621.
SOURCEiSearch...

Gene expression databases

BgeeiP08621.
ExpressionAtlasiP08621. baseline and differential.
GenevestigatoriP08621.

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. "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(1985) [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(1986) [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(1988) [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(1989) [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(1994) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Prostate.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Testis.
  8. 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(2003) [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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 219-348, PHOSPHORYLATION.
  11. 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(1997) [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(1998) [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(2000) [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(2000) [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(2002) [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(2003) [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(2003) [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(2005) [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(2005) [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(2006) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. 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(2008) [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. 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(2008) [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(2008) [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(2009) [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. 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(2010) [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(2011) [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].
  32. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  33. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-216 IN SPLICEOSOMAL U1 SNRNP.

Entry informationi

Entry nameiRU17_HUMAN
AccessioniPrimary (citable) accession number: P08621
Secondary accession number(s): B3KUA3
, P78493, P78494, Q15364, Q15686, Q15687, Q15689, Q99377, Q9UE45, Q9UE46, Q9UE47, Q9UE48, Q9UFQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1988
Last sequence update: July 31, 1988
Last modified: March 31, 2015
This is version 180 of the entry and version 2 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

Miscellaneous

Major ribonucleoprotein antigen recognized by the sera from patients with autoimmune diseases, such as systemic lupus erythematosus.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.