Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

U1 small nuclear ribonucleoprotein A

Gene

SNRPA

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. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs.1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • RNA binding Source: UniProtKB
  • snRNA stem-loop binding Source: GO_Central
  • U1 snRNA binding Source: GO_Central
  • U1 snRNP binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
U1 small nuclear ribonucleoprotein A
Short name:
U1 snRNP A
Short name:
U1-A
Short name:
U1A
Gene namesi
Name:SNRPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11151. SNRPA.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • spliceosomal complex Source: HGNC
  • U1 snRNP Source: UniProtKB

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11T → V: Abolishes RNA binding. 1 Publication1
Mutagenesisi13Y → F: Substantially reduces RNA binding. 1 Publication1
Mutagenesisi15N → V: Abolishes RNA binding. 1 Publication1
Mutagenesisi16N → V: Substantially reduces RNA binding. 1 Publication1
Mutagenesisi52R → Q: Abolishes RNA binding. 1 Publication1

Organism-specific databases

DisGeNETi6626.
OpenTargetsiENSG00000077312.
PharmGKBiPA35993.

Chemistry databases

DrugBankiDB02175. Malonic acid.

Polymorphism and mutation databases

BioMutaiSNRPA.
DMDMi134092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000818872 – 282U1 small nuclear ribonucleoprotein AAdd BLAST281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei60N6-acetyllysineCombined sources1
Modified residuei131PhosphothreonineCombined sources1
Modified residuei152Omega-N-methylarginineCombined sources1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP09012.
MaxQBiP09012.
PaxDbiP09012.
PeptideAtlasiP09012.
PRIDEiP09012.
TopDownProteomicsiP09012.

PTM databases

iPTMnetiP09012.
PhosphoSitePlusiP09012.

Expressioni

Gene expression databases

BgeeiENSG00000077312.
CleanExiHS_SNRPA.
ExpressionAtlasiP09012. baseline and differential.
GenevisibleiP09012. HS.

Organism-specific databases

HPAiCAB004652.
HPA046440.
HPA054834.

Interactioni

Subunit structurei

U1 snRNP is composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a 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 SFPQ; component of a snRNP-free complex with SFPQ.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi112510. 95 interactors.
DIPiDIP-29407N.
IntActiP09012. 64 interactors.
MINTiMINT-125665.
STRINGi9606.ENSP00000243563.

Structurei

Secondary structure

1282
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 16Combined sources7
Beta strandi19 – 21Combined sources3
Helixi23 – 34Combined sources12
Helixi35 – 37Combined sources3
Beta strandi40 – 44Combined sources5
Helixi47 – 51Combined sources5
Beta strandi55 – 61Combined sources7
Helixi62 – 72Combined sources11
Turni77 – 79Combined sources3
Beta strandi83 – 86Combined sources4
Helixi93 – 96Combined sources4
Helixi97 – 100Combined sources4
Beta strandi208 – 213Combined sources6
Helixi221 – 229Combined sources9
Beta strandi234 – 238Combined sources5
Beta strandi246 – 253Combined sources8
Helixi254 – 263Combined sources10
Turni264 – 266Combined sources3
Helixi269 – 271Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AUDNMR-A2-102[»]
1DRZX-ray2.30A2-98[»]
1DZ5NMR-A/B2-102[»]
1FHTNMR-A2-117[»]
1M5KX-ray2.40C/F1-100[»]
1M5OX-ray2.20C/F1-100[»]
1M5PX-ray2.60C/F1-100[»]
1M5VX-ray2.40C/F1-100[»]
1NU4X-ray1.80A/B2-98[»]
1OIAX-ray2.40A/B1-95[»]
1SJ3X-ray2.20P1-100[»]
1SJ4X-ray2.70P1-100[»]
1SJFX-ray2.75A1-100[»]
1U6BX-ray3.10A1-98[»]
1URNX-ray1.92A/B/C2-98[»]
1VBXX-ray2.70A1-100[»]
1VBYX-ray2.90A1-100[»]
1VBZX-ray2.80A1-100[»]
1VC0X-ray2.50A1-100[»]
1VC5X-ray3.40A1-100[»]
1VC6X-ray2.80A1-100[»]
1ZZNX-ray3.37A1-98[»]
2A3JNMR-A3-80[»]
2NZ4X-ray2.50A/B/C/D5-98[»]
2OIHX-ray2.40A2-100[»]
2OJ3X-ray2.90A2-100[»]
2U1ANMR-A195-282[»]
3BO2X-ray3.31A4-98[»]
3BO3X-ray3.40A4-98[»]
3BO4X-ray3.33A4-98[»]
3CULX-ray2.80A/B1-96[»]
3CUNX-ray3.00A/B1-98[»]
3EGZX-ray2.20A1-98[»]
3G8SX-ray3.10A/B/C/D1-98[»]
3G8TX-ray3.00A/B/C/D1-98[»]
3G96X-ray3.01A/B/C/D1-98[»]
3G9CX-ray2.90A/B/C/D1-98[»]
3HHNX-ray2.99B/D2-98[»]
3IINX-ray4.18A4-98[»]
3IRWX-ray2.70P1-98[»]
3IWNX-ray3.20C/D6-96[»]
3K0JX-ray3.10A/B/C/D2-97[»]
3L3CX-ray2.85A/B/C/D7-96[»]
3MUMX-ray2.90P1-98[»]
3MURX-ray3.00P1-98[»]
3MUTX-ray3.00P1-98[»]
3MUVX-ray3.20P1-98[»]
3MXHX-ray2.30P1-98[»]
3P49X-ray3.55B1-98[»]
3PGWX-ray4.40A/P1-282[»]
3R1HX-ray3.15A/D1-98[»]
3R1LX-ray3.12A/D1-98[»]
3UCUX-ray2.80P1-98[»]
3UCZX-ray2.80P1-98[»]
3UD3X-ray3.10P1-98[»]
3UD4X-ray2.70P1-98[»]
3UTRmodel-B/D1-98[»]
4C4WX-ray2.95A/B/E/F1-102[»]
4PR6X-ray2.30A4-96[»]
4PRFX-ray2.40A1-100[»]
4W90X-ray3.12B6-96[»]
4W92X-ray3.21B6-96[»]
4YB1X-ray2.08P7-97[»]
5DDOX-ray3.10C/G2-98[»]
5DDPX-ray2.30C/D2-98[»]
5DDQX-ray2.40C/D2-98[»]
5DDRX-ray2.60C/D2-98[»]
5FJ4X-ray2.95A/B/E/F1-102[»]
ProteinModelPortaliP09012.
SMRiP09012.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09012.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 89RRM 1PROSITE-ProRule annotationAdd BLAST80
Domaini208 – 282RRM 2PROSITE-ProRule annotationAdd BLAST75

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi140 – 206Pro-richAdd BLAST67

Sequence similaritiesi

Belongs to the RRM U1 A/B'' family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4206. Eukaryota.
ENOG410XPZI. LUCA.
GeneTreeiENSGT00390000007046.
HOGENOMiHOG000217519.
HOVERGENiHBG000895.
InParanoidiP09012.
KOiK11091.
OMAiALHNYKL.
OrthoDBiEOG091G0NFU.
PhylomeDBiP09012.
TreeFamiTF313834.

Family and domain databases

CDDicd12477. RRM1_U1A. 1 hit.
cd12480. RRM2_U1A. 1 hit.
InterProiView protein in InterPro
IPR000504. RRM_dom.
IPR034407. U1A_RRM1.
IPR034409. U1A_RRM2.
PfamiView protein in Pfam
PF00076. RRM_1. 2 hits.
SMARTiView protein in SMART
SM00360. RRM. 2 hits.
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiView protein in PROSITE
PS50102. RRM. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P09012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVPETRPNH TIYINNLNEK IKKDELKKSL YAIFSQFGQI LDILVSRSLK
60 70 80 90 100
MRGQAFVIFK EVSSATNALR SMQGFPFYDK PMRIQYAKTD SDIIAKMKGT
110 120 130 140 150
FVERDRKREK RKPKSQETPA TKKAVQGGGA TPVVGAVQGP VPGMPPMTQA
160 170 180 190 200
PRIMHHMPGQ PPYMPPPGMI PPPGLAPGQI PPGAMPPQQL MPGQMPPAQP
210 220 230 240 250
LSENPPNHIL FLTNLPEETN ELMLSMLFNQ FPGFKEVRLV PGRHDIAFVE
260 270 280
FDNEVQAGAA RDALQGFKIT QNNAMKISFA KK
Length:282
Mass (Da):31,280
Last modified:January 23, 2007 - v3
Checksum:i9426E83EE5A22894
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60784
, M60779, M60780, M60781, M60782, M60783 Genomic DNA. Translation: AAA61245.1.
X06347 mRNA. Translation: CAA29653.1.
BC000405 mRNA. Translation: AAH00405.1.
BC008290 mRNA. Translation: AAH08290.1.
CCDSiCCDS12565.1.
PIRiJQ1528.
RefSeqiNP_004587.1. NM_004596.4.
UniGeneiHs.466775.

Genome annotation databases

EnsembliENST00000243563; ENSP00000243563; ENSG00000077312.
GeneIDi6626.
KEGGihsa:6626.
UCSCiuc002ooz.4. human.

Similar proteinsi

Entry informationi

Entry nameiSNRPA_HUMAN
AccessioniPrimary (citable) accession number: P09012
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 207 of the entry and version 3 of the sequence. See 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 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