P31942 · HNRH3_HUMAN
- ProteinHeterogeneous nuclear ribonucleoprotein H3
- GeneHNRNPH3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids346 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | ribonucleoprotein complex | |
Cellular Component | spliceosomal complex | |
Molecular Function | RNA binding | |
Biological Process | epithelial cell differentiation | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | regulation of RNA splicing | |
Biological Process | RNA processing | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHeterogeneous nuclear ribonucleoprotein H3
- Short nameshnRNP H3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP31942
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_020333 | 163 | in dbSNP:rs2273903 | |||
Sequence: N → S | ||||||
Natural variant | VAR_052226 | 284 | in dbSNP:rs16925347 | |||
Sequence: G → A |
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.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000081861 | 1-346 | UniProt | Heterogeneous nuclear ribonucleoprotein H3 | |||
Sequence: MDWVMKHNGPNDASDGTVRLRGLPFGCSKEEIVQFFQGLEIVPNGITLTMDYQGRSTGEAFVQFASKEIAENALGKHKERIGHRYIEIFRSSRSEIKGFYDPPRRLLGQRPGPYDRPIGGRGGYYGAGRGSMYDRMRRGGDGYDGGYGGFDDYGGYNNYGYGNDGFDDRMRDGRGMGGHGYGGAGDASSGFHGGHFVHMRGLPFRATENDIANFFSPLNPIRVHIDIGADGRATGEADVEFVTHEDAVAAMSKDKNNMQHRYIELFLNSTPGGGSGMGGSGMGGYGRDGMDNQGGYGSVGRMGMGNNYSGGYGTPDGLGGYGRGGGGSGGYYGQGGMSGGGWRGMY | |||||||
Cross-link | 6 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 67 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 116 | UniProt | In isoform P31942-2; Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 121 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 121 | UniProt | In isoform P31942-2; Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 129 | UniProt | In isoform P31942-2; Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 174 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 207 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 216 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 280 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 287 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 296 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 298 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 314 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 323 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 331 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 343 | UniProt | Omega-N-methylarginine | ||||
Sequence: R |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P31942 | HNRNPA1 P09651 | 3 | EBI-711437, EBI-352662 | |
BINARY | P31942-2 | PSME3 P61289 | 3 | EBI-16399628, EBI-355546 | |
BINARY | P31942-2 | RFFL Q8WZ73-3 | 3 | EBI-16399628, EBI-25839575 | |
BINARY | P31942-2 | SPATA46 Q5T0L3 | 3 | EBI-16399628, EBI-750105 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-93 | RRM 1 | ||||
Sequence: GTVRLRGLPFGCSKEEIVQFFQGLEIVPNGITLTMDYQGRSTGEAFVQFASKEIAENALGKHKERIGHRYIEIFRSSR | ||||||
Domain | 195-270 | RRM 2 | ||||
Sequence: HFVHMRGLPFRATENDIANFFSPLNPIRVHIDIGADGRATGEADVEFVTHEDAVAAMSKDKNNMQHRYIELFLNST |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length346
- Mass (Da)36,926
- Last updated2002-09-19 v2
- ChecksumF7D14C2947930E9E
P31942-2
- Name2
- Synonyms2H9A
- Differences from canonical
- 132-146: Missing
P31942-3
- Name3
- Synonyms2H9B
- Differences from canonical
- 1-49: Missing
P31942-4
- Name4
- Synonyms2H9C
- Differences from canonical
- 1-131: Missing
P31942-5
- Name5
- Synonyms2H9D
P31942-6
- Name6
- Synonyms2H9E
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_005838 | 1-49 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_005839 | 1-131 | in isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_005841 | 1-137 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_005840 | 132-146 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_005842 | 138-145 | in isoform 6 | |||
Sequence: RGGDGYDG → MCFSLNYT | ||||||
Alternative sequence | VSP_005843 | 259-276 | in isoform 5 and isoform 6 | |||
Sequence: QHRYIELFLNSTPGGGSG → RKWCLWHTILFPKREFIK | ||||||
Alternative sequence | VSP_005844 | 277-346 | in isoform 5 and isoform 6 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |