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Details on Person UniProt:P61978 HNRNPK
| Class:Id | ReferenceGeneProduct:71944 |
|---|---|
| _chainChangeLog | chain:1-463 added on Sat February 7 2015 |
| _displayName | UniProt:P61978 HNRNPK |
| _timestamp | 2025-08-15 21:30:40 |
| chain | chain:1-463 |
| checksum | 0F70EE169B2A064A |
| comment | FUNCTION One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841).SUBUNIT Identified in the spliceosome C complex (PubMed:11991638). Part of a transcription inhibitory ribonucleoprotein complex composed at least of the circular RNA circZNF827, ZNF827 and HNRNPL (PubMed:33174841). Interacts with RBM42 and ZIK1 (By similarity). Interacts with BRDT (By similarity). Interacts with ANKRD28 (PubMed:16564677). Interacts with ASFV p30 protein (PubMed:18775702). Interacts with DDX1 (PubMed:12183465). Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation (PubMed:16360036). Interacts with p53/TP53 (PubMed:16360036). Interacts with IVNS1ABP (via BACK domain); the interaction is direct (PubMed:23825951, PubMed:30538201). Interacts with PPIA/CYPA (PubMed:25678563).SUBUNIT (Microbial infection) Interacts with HCV core protein (PubMed:9651361).INTERACTION Recruited to p53/TP53-responsive promoters, in the presence of functional p53/TP53 (PubMed:16360036). In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear (PubMed:18775702).ALTERNATIVE PRODUCTS By DNA damage, including ionizing radiations and phleomycin treatment or UV irradiation. This induction requires ATM kinase activity (ionizing radiations and phleomycin) or ATR activity (UV irradiation). Up-regulation is due to protein stabilization. Constitutive protein levels are controlled by MDM2-mediated ubiquitination and degradation via the proteasome pathway.PTM Arg-296 and Arg-299 are dimethylated, probably to asymmetric dimethylarginine.PTM Sumoylated by CBX4. Sumoylation is increased upon DNA damage, such as that produced by doxorubicin, etoposide, UV light and camptothecin, due to enhanced CBX4 phosphorylation by HIPK2 under these conditions.PTM Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination.PTM O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.MASS SPECTROMETRY The disease is caused by variants affecting the gene represented in this entry.SEQUENCE CAUTION Extended N-terminus. |
| description | recommendedName: Heterogeneous nuclear ribonucleoprotein K shortName: hnRNP K alternativeName: Transformation up-regulated nuclear protein shortName: TUNP |
| geneName | HNRNPK HNRPK |
| identifier | P61978 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Activator Alternative splicing Cell junction Cell projection Cytoplasm Direct protein sequencing DNA-binding Glycoprotein Host-virus interaction Intellectual disability Isopeptide bond Methylation mRNA processing mRNA splicing Nucleus Phosphoprotein Proteomics identification Reference proteome Repeat Repressor Ribonucleoprotein RNA-binding Spliceosome Transcription Transcription regulation Ubl conjugation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | HNRNPK |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8992497] ENSEMBL:ENSG00000165119 HNRNPK [Homo sapiens] |
| secondaryIdentifier | HNRPK_HUMAN Q07244 Q15671 Q59F98 Q5T6W4 Q60577 Q6IBN1 Q922Y7 Q96J62 |
| sequenceLength | 463 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:153200] UniProt:P61978-2 HNRNPK [Homo sapiens] [ReferenceIsoform:232103] UniProt:P61978-3 HNRNPK [Homo sapiens] [ReferenceIsoform:404613] UniProt:P61978-1 HNRNPK [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:71945] HNRNPK [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:4570532] polySUMO2-K422-HNRNPK [nucleoplasm] [Homo sapiens] |
| (referenceSequence) | [GroupModifiedResidue:4570468] sumoylated lysine (polySUMO2 [nucleoplasm]) at 422 |
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No pathways have been reviewed or authored by UniProt:P61978 HNRNPK (71944)
