P31942 · HNRH3_HUMAN

  • Protein
    Heterogeneous nuclear ribonucleoprotein H3
  • Gene
    HNRNPH3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentribonucleoprotein complex
Cellular Componentspliceosomal complex
Molecular FunctionRNA binding
Biological Processepithelial cell differentiation
Biological ProcessmRNA splicing, via spliceosome
Biological Processregulation of RNA splicing
Biological ProcessRNA processing
Biological ProcessRNA splicing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Heterogeneous nuclear ribonucleoprotein H3
  • Short names
    hnRNP H3
  • Alternative names
    • Heterogeneous nuclear ribonucleoprotein 2H9 (hnRNP 2H9)

Gene names

    • Name
      HNRNPH3
    • Synonyms
      HNRPH3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P31942
  • Secondary accessions
    • A8K682
    • B3KRE1
    • Q9BSX1
    • Q9NP53
    • Q9NP96

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_020333163in dbSNP:rs2273903
Natural variantVAR_052226284in dbSNP:rs16925347

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 259 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue, chain, cross-link, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue1UniProtN-acetylmethionine
ChainPRO_00000818611-346UniProtHeterogeneous nuclear ribonucleoprotein H3
Cross-link6UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link67UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue116UniProtIn isoform P31942-2; Omega-N-methylarginine
Modified residue121UniProtAsymmetric dimethylarginine
Modified residue121UniProtIn isoform P31942-2; Omega-N-methylarginine
Modified residue129UniProtIn isoform P31942-2; Omega-N-methylarginine
Modified residue174UniProtOmega-N-methylarginine
Modified residue (large scale data)207PRIDEPhosphothreonine
Modified residue216UniProtPhosphoserine
Modified residue (large scale data)216PRIDEPhosphoserine
Modified residue (large scale data)270PRIDEPhosphothreonine
Modified residue (large scale data)275PRIDEPhosphoserine
Modified residue (large scale data)280PRIDEPhosphoserine
Modified residue287UniProtOmega-N-methylarginine
Modified residue296UniProtPhosphotyrosine
Modified residue (large scale data)296PRIDEPhosphotyrosine
Modified residue298UniProtPhosphoserine
Modified residue (large scale data)298PRIDEPhosphoserine
Modified residue (large scale data)308PRIDEPhosphotyrosine
Modified residue314UniProtPhosphothreonine
Modified residue (large scale data)314PRIDEPhosphothreonine
Modified residue323UniProtOmega-N-methylarginine
Modified residue (large scale data)328PRIDEPhosphoserine
Modified residue (large scale data)331PRIDEPhosphotyrosine
Modified residue343UniProtOmega-N-methylarginine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain16-93RRM 1
Domain195-270RRM 2

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (6)
  • Sequence status
    Complete

This entry describes 6 isoforms produced by Alternative splicing.

P31942-1

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.

  • Length
    346
  • Mass (Da)
    36,926
  • Last updated
    2002-09-19 v2
  • Checksum
    F7D14C2947930E9E
MDWVMKHNGPNDASDGTVRLRGLPFGCSKEEIVQFFQGLEIVPNGITLTMDYQGRSTGEAFVQFASKEIAENALGKHKERIGHRYIEIFRSSRSEIKGFYDPPRRLLGQRPGPYDRPIGGRGGYYGAGRGSMYDRMRRGGDGYDGGYGGFDDYGGYNNYGYGNDGFDDRMRDGRGMGGHGYGGAGDASSGFHGGHFVHMRGLPFRATENDIANFFSPLNPIRVHIDIGADGRATGEADVEFVTHEDAVAAMSKDKNNMQHRYIELFLNSTPGGGSGMGGSGMGGYGRDGMDNQGGYGSVGRMGMGNNYSGGYGTPDGLGGYGRGGGGSGGYYGQGGMSGGGWRGMY

P31942-2

  • Name
    2
  • Synonyms
    2H9A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P31942-3

  • Name
    3
  • Synonyms
    2H9B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P31942-4

  • Name
    4
  • Synonyms
    2H9C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P31942-5

  • Name
    5
  • Synonyms
    2H9D
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P31942-6

  • Name
    6
  • Synonyms
    2H9E
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0058381-49in isoform 3
Alternative sequenceVSP_0058391-131in isoform 4 and isoform 5
Alternative sequenceVSP_0058411-137in isoform 6
Alternative sequenceVSP_005840132-146in isoform 2
Alternative sequenceVSP_005842138-145in isoform 6
Alternative sequenceVSP_005843259-276in isoform 5 and isoform 6
Alternative sequenceVSP_005844277-346in isoform 5 and isoform 6

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L32610
EMBL· GenBank· DDBJ
AAD45179.1
EMBL· GenBank· DDBJ
mRNA
AF132360
EMBL· GenBank· DDBJ
AAF68843.1
EMBL· GenBank· DDBJ
Genomic DNA
AF132360
EMBL· GenBank· DDBJ
AAF68844.1
EMBL· GenBank· DDBJ
Genomic DNA
AF132360
EMBL· GenBank· DDBJ
AAF68845.1
EMBL· GenBank· DDBJ
Genomic DNA
AF132360
EMBL· GenBank· DDBJ
AAF68846.1
EMBL· GenBank· DDBJ
Genomic DNA
AF132360
EMBL· GenBank· DDBJ
AAF68847.1
EMBL· GenBank· DDBJ
Genomic DNA
AF132360
EMBL· GenBank· DDBJ
AAF68848.1
EMBL· GenBank· DDBJ
Genomic DNA
AF132361
EMBL· GenBank· DDBJ
AAF68849.1
EMBL· GenBank· DDBJ
mRNA
AF132362
EMBL· GenBank· DDBJ
AAF68850.1
EMBL· GenBank· DDBJ
mRNA
AF132363
EMBL· GenBank· DDBJ
AAF68851.1
EMBL· GenBank· DDBJ
mRNA
AF132364
EMBL· GenBank· DDBJ
AAF68852.1
EMBL· GenBank· DDBJ
mRNA
AK091411
EMBL· GenBank· DDBJ
BAG52353.1
EMBL· GenBank· DDBJ
mRNA
AK291547
EMBL· GenBank· DDBJ
BAF84236.1
EMBL· GenBank· DDBJ
mRNA
AL117395
EMBL· GenBank· DDBJ
CAB55897.1
EMBL· GenBank· DDBJ
mRNA
CH471083
EMBL· GenBank· DDBJ
EAW54281.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471083
EMBL· GenBank· DDBJ
EAW54282.1
EMBL· GenBank· DDBJ
Genomic DNA
BC004511
EMBL· GenBank· DDBJ
AAH04511.2
EMBL· GenBank· DDBJ
mRNA
BC039824
EMBL· GenBank· DDBJ
AAH39824.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp