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Protein

Heterogeneous nuclear ribonucleoprotein A1

Gene

Hnrnpa1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection.

GO - Molecular functioni

  • annealing helicase activity Source: RGD
  • mRNA 3'-UTR binding Source: RGD
  • mRNA binding Source: RGD
  • nucleotide binding Source: InterPro
  • RNA binding Source: RGD
  • RNA strand annealing activity Source: RGD
  • sequence-specific mRNA binding Source: RGD
  • single-stranded DNA binding Source: HGNC
  • single-stranded RNA binding Source: RGD
  • transcription factor binding Source: RGD

GO - Biological processi

  • cellular response to epidermal growth factor stimulus Source: RGD
  • cellular response to potassium ion Source: RGD
  • cellular response to thapsigargin Source: RGD
  • cellular response to tunicamycin Source: RGD
  • lung development Source: RGD
  • male gonad development Source: RGD
  • mRNA processing Source: UniProtKB-KW
  • mRNA transport Source: UniProtKB-KW
  • nuclear export Source: HGNC
  • nuclear import Source: HGNC
  • positive regulation of action potential Source: RGD
  • positive regulation of gene expression Source: RGD
  • RNA metabolic process Source: RGD
  • RNA splicing Source: UniProtKB-KW
  • transformation of host cell by virus Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein A1
Short name:
hnRNP A1
Alternative name(s):
Helix-destabilizing protein
Short name:
HDP
Single-strand RNA-binding protein
hnRNP core protein A1
Cleaved into the following chain:
Gene namesi
Name:Hnrnpa1
Synonyms:Hnrpa1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69234. Hnrnpa1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes.By similarity

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • cytosol Source: RGD
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • nucleoplasm Source: HGNC
  • nucleoplasmic periphery of the nuclear pore complex Source: RGD
  • nucleus Source: RGD
  • spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000818311 – 320Heterogeneous nuclear ribonucleoprotein A1Add BLAST320
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004245132 – 320Heterogeneous nuclear ribonucleoprotein A1, N-terminally processedAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylserine; in Heterogeneous nuclear ribonucleoprotein A1, N-terminally processedBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei3N6-acetyllysineBy similarity1
Modified residuei4PhosphoserineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei22PhosphoserineBy similarity1
Cross-linki113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei192Phosphoserine; by MKNK2By similarity1
Modified residuei194Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei194Dimethylated arginine; alternateBy similarity1
Modified residuei194Omega-N-methylarginine; alternateBy similarity1
Modified residuei199PhosphoserineBy similarity1
Modified residuei206Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei206Dimethylated arginine; alternateBy similarity1
Modified residuei206Omega-N-methylarginine; alternateBy similarity1
Modified residuei218Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei218Omega-N-methylarginine; alternateBy similarity1
Modified residuei225Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei225Dimethylated arginine; alternateBy similarity1
Modified residuei225Omega-N-methylarginine; alternateBy similarity1
Modified residuei232Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei232Omega-N-methylarginine; alternateBy similarity1
Modified residuei284Omega-N-methylarginineBy similarity1
Modified residuei285PhosphoserineBy similarity1
Modified residuei298N6-acetyllysineBy similarity1
Modified residuei300Omega-N-methylarginineBy similarity1
Modified residuei309PhosphoserineBy similarity1
Modified residuei310Phosphoserine; by MKNK2By similarity1
Modified residuei311Phosphoserine; by MKNK2By similarity1
Modified residuei312Phosphoserine; by MKNK2By similarity1
Modified residuei313PhosphoserineBy similarity1
Modified residuei316PhosphoserineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP04256.
PRIDEiP04256.

PTM databases

iPTMnetiP04256.
PhosphoSitePlusiP04256.
SwissPalmiP04256.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with SEPT6, C9orf72, KHDRBS1, UBQLN2 (By similarity).By similarity

GO - Molecular functioni

  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi248211. 3 interactors.
IntActiP04256. 1 interactor.
STRINGi10116.ENSRNOP00000052160.

Structurei

3D structure databases

ProteinModelPortaliP04256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 97RRM 1PROSITE-ProRule annotationAdd BLAST84
Domaini105 – 184RRM 2PROSITE-ProRule annotationAdd BLAST80

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 94Globular A domainAdd BLAST91
Regioni95 – 185Globular B domainAdd BLAST91
Regioni218 – 240RNA-binding RGG-boxAdd BLAST23
Regioni268 – 305Nuclear targeting sequenceBy similarityAdd BLAST38

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi195 – 320Gly-richAdd BLAST126
Compositional biasi308 – 313Poly-Ser6

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
HOGENOMiHOG000234442.
HOVERGENiHBG002295.
InParanoidiP04256.
KOiK12741.
PhylomeDBiP04256.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR021662. HnRNPA1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF11627. HnRNPA1. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN
60 70 80 90 100
TKRSRGFGFV TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA
110 120 130 140 150
HLTVKKIFVG GIKEDTEEHH LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF
160 170 180 190 200
VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA LCKQEMASAS SSQRGRSGSG
210 220 230 240 250
NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS GDGYNGFGND
260 270 280 290 300
GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR
310 320
NQGGYGGSSS SSSYGSGRRF
Length:320
Mass (Da):34,212
Last modified:January 23, 2007 - v3
Checksum:i44FF5578B5AF8AE1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9E → G AA sequence (PubMed:2447078).Curated1
Sequence conflicti27D → E AA sequence (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12156 mRNA. Translation: AAA41314.1.
PIRiA38304.
RefSeqiNP_058944.1. NM_017248.1.
UniGeneiRn.228596.
Rn.25771.

Genome annotation databases

GeneIDi29578.
KEGGirno:29578.
UCSCiRGD:69234. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12156 mRNA. Translation: AAA41314.1.
PIRiA38304.
RefSeqiNP_058944.1. NM_017248.1.
UniGeneiRn.228596.
Rn.25771.

3D structure databases

ProteinModelPortaliP04256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248211. 3 interactors.
IntActiP04256. 1 interactor.
STRINGi10116.ENSRNOP00000052160.

PTM databases

iPTMnetiP04256.
PhosphoSitePlusiP04256.
SwissPalmiP04256.

Proteomic databases

PaxDbiP04256.
PRIDEiP04256.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29578.
KEGGirno:29578.
UCSCiRGD:69234. rat.

Organism-specific databases

CTDi3178.
RGDi69234. Hnrnpa1.

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
HOGENOMiHOG000234442.
HOVERGENiHBG002295.
InParanoidiP04256.
KOiK12741.
PhylomeDBiP04256.

Miscellaneous databases

PROiP04256.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR021662. HnRNPA1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF11627. HnRNPA1. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiROA1_RAT
AccessioniPrimary (citable) accession number: P04256
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.