Heterogeneous nuclear ribonucleoprotein A1

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P04256 (ROA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:	Hnrnpa1
Synonyms:	Hnrpa1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Identified in the spliceosome C complex. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with SEPT6 By similarity.
Subcellular location	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.
Post-translational modification	Sumoylated By similarity.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	Transport mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus Spliceosome
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA metabolic process Traceable author statement Ref.1. Source: RGD RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW nuclear export Inferred from sequence or structural similarity. Source: HGNC nuclear import Inferred from sequence or structural similarity. Source: HGNC
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: HGNC nucleoplasm Inferred from sequence or structural similarity. Source: HGNC spliceosomal complex Inferred from sequence or structural similarity. Source: HGNC
Molecular_function	RNA binding Traceable author statement Ref.1. Source: RGD nucleotide binding Inferred from electronic annotation. Source: InterPro single-stranded DNA binding Inferred from sequence or structural similarity. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 320

319

Heterogeneous nuclear ribonucleoprotein A1

PRO_0000081831

Regions

Domain

14 – 97

RRM 1

Domain

105 – 184

RRM 2

Region

4 – 94

Globular A domain

Region

95 – 185

Globular B domain

Region

218 – 240

RNA-binding RGG-box

Region

268 – 305

Nuclear targeting sequence By similarity

Compositional bias

195 – 320

126

Gly-rich

Compositional bias

308 – 313

Poly-Ser

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.5 Ref.6

Modified residue

192

Phosphoserine; by MKNK2 By similarity

Modified residue

194

Asymmetric dimethylarginine; alternate

Modified residue

194

Dimethylated arginine; alternate By similarity

Modified residue

199

Phosphoserine By similarity

Modified residue

206

Dimethylated arginine; alternate By similarity

Modified residue

206

Omega-N-methylarginine; alternate By similarity

Modified residue

225

Dimethylated arginine; alternate By similarity

Modified residue

225

Omega-N-methylarginine; alternate By similarity

Modified residue

298

N6-acetyllysine By similarity

Modified residue

310

Phosphoserine; by MKNK2 By similarity

Modified residue

311

Phosphoserine; by MKNK2 By similarity

Modified residue

312

Phosphoserine; by MKNK2 By similarity

Modified residue

313

Phosphoserine By similarity

Modified residue

316

Phosphoserine By similarity

Cross-link

113

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Sequence conflict

E → G AA sequence Ref.3

Sequence conflict

D → E AA sequence Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P04256 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 44FF5578B5AF8AE1
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FASTA

320

34,212

        10         20         30         40         50         60 
MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV 

        70         80         90        100        110        120 
TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH 

       130        140        150        160        170        180 
LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA 

       190        200        210        220        230        240 
LCKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS 

       250        260        270        280        290        300 
GDGYNGFGND GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR 

       310        320 
NQGGYGGSSS SSSYGSGRRF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of rodent helix-destabilizing protein revealed by cDNA cloning." Cobianchi F., Sengupta D.N., Zmudzka B.Z., Wilson S.H. J. Biol. Chem. 261:3536-3543(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	Cobianchi F. Submitted (MAY-1986) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 182.
[3]	"Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids." Cobianchi F., Karpel R.L., Williams K.R., Notario V., Wilson S.H. J. Biol. Chem. 263:1063-1071(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[4]	Lubec G., Diao W. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 16-31, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
[5]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
[6]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Renal collecting duct.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12156 mRNA. Translation: AAA41314.1.
IPI	IPI00421500.
PIR	A38304.
RefSeq	NP_058944.1. NM_017248.1.
UniGene	Rn.25771.
3D structure databases
ProteinModelPortal	P04256.
SMR	P04256. Positions 8-190.
ModBase	Search...
Protein-protein interaction databases
IntAct	P04256. 1 interaction.
PTM databases
PhosphoSite	P04256.
Proteomic databases
PaxDb	P04256.
PRIDE	P04256.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	29578.
KEGG	rno:29578.
UCSC	RGD:69234. rat.
Organism-specific databases
CTD	3178.
RGD	69234. Hnrnpa1.
Phylogenomic databases
eggNOG	COG0724.
HOGENOM	HOG000234442.
HOVERGEN	HBG002295.
KO	K12741.
Gene expression databases
ArrayExpress	P04256.
Genevestigator	P04256.
GermOnline	ENSRNOG00000036839. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.70.330. 2 hits.
InterPro	IPR021662. HnRNPA1. IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF11627. HnRNPA1. 1 hit. PF00076. RRM_1. 2 hits. [Graphical view]
SMART	SM00360. RRM. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	609678.

Entry information

Entry name

ROA1_RAT

Accession

Primary (citable) accession number: P04256

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents