Human Gene HNRNPK (ENST00000376281.8) from GENCODE V43
Description: Homo sapiens heterogeneous nuclear ribonucleoprotein K (HNRNPK), transcript variant 1, mRNA. (from RefSeq NM_002140) RefSeq Summary (NM_002140): This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene is located in the nucleoplasm and has three repeats of KH domains that binds to RNAs. It is distinct among other hnRNP proteins in its binding preference; it binds tenaciously to poly(C). This protein is also thought to have a role during cell cycle progession. Several alternatively spliced transcript variants have been described for this gene, however, not all of them are fully characterized. [provided by RefSeq, Jul 2008]. Gencode Transcript: ENST00000376281.8 Gencode Gene: ENSG00000165119.22 Transcript (Including UTRs) Position: hg38 chr9:83,968,083-83,980,604 Size: 12,522 Total Exon Count: 17 Strand: - Coding Region Position: hg38 chr9:83,969,407-83,978,252 Size: 8,846 Coding Exon Count: 15
ID:HNRPK_HUMAN DESCRIPTION: RecName: Full=Heterogeneous nuclear ribonucleoprotein K; Short=hnRNP K; AltName: Full=Transformation up-regulated nuclear protein; Short=TUNP; 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. SUBUNIT: Interacts with RBM42 and ZIK1. Interacts with BRDT (By similarity). Identified in the spliceosome C complex. Interacts with ANKRD28. Interacts with HCV core protein. Interacts with ASFV p30 protein. Interacts with DDX1. Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation. Interacts with p53/TP53. INTERACTION: Q96PU8:QKI; NbExp=3; IntAct=EBI-304185, EBI-945792; Q9H3D4:TP63; NbExp=2; IntAct=EBI-304185, EBI-2337775; SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Note=Recruited to p53/TP53-responsive promoters, in the presence of functional p53/TP53. In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear. INDUCTION: 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. MASS SPECTROMETRY: Mass=50976.25; Method=MALDI; Range=1-463 (P61978-1); Source=PubMed:11840567; SIMILARITY: Contains 3 KH domains. SEQUENCE CAUTION: Sequence=BAD92799.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P61978
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0000398 mRNA splicing, via spliceosome GO:0006351 transcription, DNA-templated GO:0006355 regulation of transcription, DNA-templated GO:0006357 regulation of transcription from RNA polymerase II promoter GO:0006366 transcription from RNA polymerase II promoter GO:0006396 RNA processing GO:0006397 mRNA processing GO:0007165 signal transduction GO:0008380 RNA splicing GO:0010988 regulation of low-density lipoprotein particle clearance GO:0016032 viral process GO:0016070 RNA metabolic process GO:0043066 negative regulation of apoptotic process GO:0045716 positive regulation of low-density lipoprotein particle receptor biosynthetic process GO:0045944 positive regulation of transcription from RNA polymerase II promoter GO:0048025 negative regulation of mRNA splicing, via spliceosome GO:0048260 positive regulation of receptor-mediated endocytosis GO:0072369 regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter GO:1902165 regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator