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P09661

- RU2A_HUMAN

UniProt

P09661 - RU2A_HUMAN

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Protein

U2 small nuclear ribonucleoprotein A'

Gene

SNRPA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
U2 small nuclear ribonucleoprotein A'
Short name:
U2 snRNP A'
Gene namesi
Name:SNRPA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11152. SNRPA1.

Subcellular locationi

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. small nuclear ribonucleoprotein complex Source: ProtInc
  5. spliceosomal complex Source: HGNC
  6. U2 snRNP Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35994.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 255254U2 small nuclear ribonucleoprotein A'PRO_0000074173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721N6-acetyllysine1 Publication
Modified residuei178 – 1781Phosphoserine1 Publication
Modified residuei197 – 1971Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09661.
PaxDbiP09661.
PeptideAtlasiP09661.
PRIDEiP09661.

PTM databases

PhosphoSiteiP09661.

Expressioni

Gene expression databases

BgeeiP09661.
CleanExiHS_SNRPA1.
ExpressionAtlasiP09661. baseline.
GenevestigatoriP09661.

Organism-specific databases

HPAiHPA045622.
HPA048499.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. 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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SNRPB2P085792EBI-876439,EBI-1053651

Protein-protein interaction databases

BioGridi112511. 122 interactions.
DIPiDIP-625N.
IntActiP09661. 13 interactions.
MINTiMINT-3007227.
STRINGi9606.ENSP00000254193.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 105Combined sources
Beta strandi14 – 163Combined sources
Beta strandi22 – 254Combined sources
Helixi37 – 404Combined sources
Beta strandi45 – 484Combined sources
Beta strandi68 – 703Combined sources
Helixi83 – 864Combined sources
Beta strandi92 – 943Combined sources
Helixi103 – 1119Combined sources
Beta strandi117 – 1193Combined sources
Helixi124 – 1274Combined sources
Helixi131 – 1388Combined sources
Beta strandi143 – 1453Combined sources
Helixi152 – 1609Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9NX-ray2.38A/C1-176[»]
ProteinModelPortaliP09661.
SMRiP09661. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09661.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati20 – 4122LRR 1Add
BLAST
Repeati43 – 6422LRR 2Add
BLAST
Repeati65 – 8622LRR 3Add
BLAST
Repeati89 – 11022LRR 4Add
BLAST
Domaini123 – 16139LRRCTAdd
BLAST

Sequence similaritiesi

Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00510000047131.
HOGENOMiHOG000175472.
HOVERGENiHBG007330.
KOiK11092.
OMAiSMQYINP.
OrthoDBiEOG7966HF.
PhylomeDBiP09661.
TreeFamiTF313776.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTiSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09661-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKLTAELIE QAAQYTNAVR DRELDLRGYK IPVIENLGAT LDQFDAIDFS
60 70 80 90 100
DNEIRKLDGF PLLRRLKTLL VNNNRICRIG EGLDQALPCL TELILTNNSL
110 120 130 140 150
VELGDLDPLA SLKSLTYLSI LRNPVTNKKH YRLYVIYKVP QVRVLDFQKV
160 170 180 190 200
KLKERQEAEK MFKGKRGAQL AKDIARRSKT FNPGAGLPTD KKKGGPSPGD
210 220 230 240 250
VEAIKNAIAN ASTLAEVERL KGLLQSGQIP GRERRSGPTD DGEEEMEEDT

VTNGS
Length:255
Mass (Da):28,416
Last modified:May 23, 2003 - v2
Checksum:i25902F07992B7209
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931K → R in CAA31838. (PubMed:2928112)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti234 – 2341R → H.
Corresponds to variant rs1050843 [ dbSNP | Ensembl ].
VAR_052030

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13482 mRNA. Translation: CAA31838.1.
AK312200 mRNA. Translation: BAG35133.1.
CH471101 Genomic DNA. Translation: EAX02300.1.
BC022816 mRNA. Translation: AAH22816.1.
BC071717 mRNA. Translation: AAH71717.1.
CCDSiCCDS10391.1.
PIRiS03616.
RefSeqiNP_003081.2. NM_003090.2.
UniGeneiHs.528763.

Genome annotation databases

EnsembliENST00000254193; ENSP00000254193; ENSG00000131876.
GeneIDi6627.
KEGGihsa:6627.
UCSCiuc002bww.3. human.

Polymorphism databases

DMDMi31077165.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13482 mRNA. Translation: CAA31838.1 .
AK312200 mRNA. Translation: BAG35133.1 .
CH471101 Genomic DNA. Translation: EAX02300.1 .
BC022816 mRNA. Translation: AAH22816.1 .
BC071717 mRNA. Translation: AAH71717.1 .
CCDSi CCDS10391.1.
PIRi S03616.
RefSeqi NP_003081.2. NM_003090.2.
UniGenei Hs.528763.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A9N X-ray 2.38 A/C 1-176 [» ]
ProteinModelPortali P09661.
SMRi P09661. Positions 2-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112511. 122 interactions.
DIPi DIP-625N.
IntActi P09661. 13 interactions.
MINTi MINT-3007227.
STRINGi 9606.ENSP00000254193.

PTM databases

PhosphoSitei P09661.

Polymorphism databases

DMDMi 31077165.

Proteomic databases

MaxQBi P09661.
PaxDbi P09661.
PeptideAtlasi P09661.
PRIDEi P09661.

Protocols and materials databases

DNASUi 6627.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000254193 ; ENSP00000254193 ; ENSG00000131876 .
GeneIDi 6627.
KEGGi hsa:6627.
UCSCi uc002bww.3. human.

Organism-specific databases

CTDi 6627.
GeneCardsi GC15M101821.
H-InvDB HIX0203213.
HGNCi HGNC:11152. SNRPA1.
HPAi HPA045622.
HPA048499.
MIMi 603521. gene.
neXtProti NX_P09661.
PharmGKBi PA35994.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
GeneTreei ENSGT00510000047131.
HOGENOMi HOG000175472.
HOVERGENi HBG007330.
KOi K11092.
OMAi SMQYINP.
OrthoDBi EOG7966HF.
PhylomeDBi P09661.
TreeFami TF313776.

Enzyme and pathway databases

Reactomei REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

EvolutionaryTracei P09661.
GeneWikii SNRPA1.
GenomeRNAii 6627.
NextBioi 25813.
PROi P09661.
SOURCEi Search...

Gene expression databases

Bgeei P09661.
CleanExi HS_SNRPA1.
ExpressionAtlasi P09661. baseline.
Genevestigatori P09661.

Family and domain databases

InterProi IPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view ]
SMARTi SM00446. LRRcap. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the cDNA for the human U2 snRNA-specific A' protein."
    Sillekens P.T.G., Beijer R.P., Habets W.J., van Venrooij W.J.
    Nucleic Acids Res. 17:1893-1906(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Skeletal muscle.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Muscle and Urinary bladder.
  5. Bienvenut W.V., Heiserich L., Gottlieb E.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-20; 114-122; 133-143 AND 222-232, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  6. Cited for: IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRNP70; SRRM1 AND SRRM2.
  7. "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 SNRNP70; SRRM1 AND TRA2B.
  8. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structure of the spliceosomal U2B'-U2A' protein complex bound to a fragment of U2 small nuclear RNA."
    Price S.R., Evans P.R., Nagai K.
    Nature 394:645-650(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-176.

Entry informationi

Entry nameiRU2A_HUMAN
AccessioniPrimary (citable) accession number: P09661
Secondary accession number(s): B2R5I6, Q8TBD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 23, 2003
Last modified: November 26, 2014
This is version 151 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3