HNRNPK
entrez
3190
canonical
uniprot
P61978
canonical
ensembl
ENSG00000165119
resolver
ensp
ENSP00000353552
resolver
ensp
ENSP00000365439
resolver
ensp
ENSP00000365458
resolver
ensp
ENSP00000409456
resolver
ensp
ENSP00000515617
resolver
ensp
ENSP00000515620
resolver
ensp
ENSP00000515621
resolver
ensp
ENSP00000515624
resolver
ensp
ENSP00000515626
resolver
ensp
ENSP00000616184
resolver
ensp
ENSP00000643892
resolver
enst
ENST00000704007
resolver
enst
ENST00000704008
resolver
enst
ENST00000704013
resolver
genesymbol
HNRNPK
resolver
genesymbol_syn
HNRPK
resolver
hgnc
HGNC:5044
resolver
uniprot
A0A994J4C3
resolver
uniprot
B4DUQ1
resolver
uniprot
Q07244
resolver
uniprot
Q15671
resolver
uniprot
Q59F98
resolver
uniprot
Q5T6W4
resolver
uniprot
Q60577
resolver
uniprot
Q6IBN1
resolver
uniprot
Q922Y7
resolver
uniprot
Q96J62
resolver
uniprot_entry
A0A994J4C3_HUMAN
resolver
uniprot_entry
B4DUQ1_HUMAN
resolver
uniprot_entry
HNRPK_HUMAN
resolver
uniprot_sec
Q07244
resolver
uniprot_sec
Q15671
resolver
uniprot_sec
Q59F98
resolver
uniprot_sec
Q5T6W4
resolver
uniprot_sec
Q60577
resolver
uniprot_sec
Q6IBN1
resolver
uniprot_sec
Q922Y7
resolver
uniprot_sec
Q96J62
resolver
amino_acid_sequence
METEQPEETFPNTETNGEFGKRPAEDMEEEQAFKRSRNTDEMVELRILLQSKNAGAVIGKGGKNIKALRTDYNASVSVPDSSGPERILSISADIETIGEILKKIIPTLEEGLQLPSPTATSQLPLESDAVECLNYQHYKGSDFDCELRLLIHQSLAGGIIGVKGAKIKELRENTQTTIKLFQECCPHSTDRVVLIGGKPDRVVECIKIILDLISESPIKGRAQPYDPNFYDETYDYGGFTMMFDDRRGRPVGFPMRGRGGFDRMPPGRGGRPMPPSRRDYDDMSPRRGPPPPPPGRGGRGGSRARNLPLPPPPPPRGGDLMAYDRRGRPGDRYDGMVGFSADETWDSAIDTWSPSEWQMAYEPQGGSGYDYSYAGGRGSYGDLGGPIITTQVTIPKDLAGSIIGKGGQRIKQIRHESGASIKIDEPLEGSEDRIITITGTQDQIQNAQYLLQNSVKQYSGKFF
uniprot
proteins
disease_involvement
DISEASE: Au-Kline syndrome (AUKS) [MIM:616580]: A disorder characterized by intellectual disability, facial dysmorphism, cardiac defects, and connective tissue and skeletal abnormalities. Dysmorphic features include long palpebral fissures, ptosis, a broad prominent nasal bridge, hypoplastic alae nasi, an open downturned mouth, ears with underdeveloped and thick helices, high palate, and a unique tongue with a prominent median crease. Hypotonia, hyporeflexia, and high pain tolerance are additional features. {ECO:0000269|PubMed:26173930}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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. 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). {ECO:0000269|PubMed:16360036, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22825850, ECO:0000269|PubMed:33174841}.
uniprot
proteins
mass_dalton
50976
uniprot
proteins
mutagenesis
MUTAGEN 422; /note="K->R: Loss of sumoylation. Loss of TP53 transcriptional stimulation."; /evidence="ECO:0000269|PubMed:22825850"; MUTAGEN 424; /note="D->A: Loss of sumoylation."; /evidence="ECO:0000269|PubMed:22825850
uniprot
proteins
post_translational_modification
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. {ECO:0000269|PubMed:16564677, ECO:0000269|PubMed:22825850, ECO:0000269|PubMed:8107114}.; PTM: Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination. {ECO:0000269|PubMed:22825850}.; PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000269|PubMed:22967762}.
uniprot
proteins
pubmed
10369774
uniprot
proteins
pubmed
11840567
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
12093748
uniprot
proteins
pubmed
12183465
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16360036
uniprot
proteins
pubmed
16564677
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
1729596
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18775702
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20673990
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22721921
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22825850
uniprot
proteins
pubmed
22967762
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23825951
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25678563
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26173930
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30538201
uniprot
proteins
pubmed
33174841
uniprot
proteins
pubmed
39389056
uniprot
proteins
pubmed
8107114
uniprot
proteins
pubmed
9651361
uniprot
proteins
sequence_length
463
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1729596}. Nucleus, nucleoplasm {ECO:0000269|PubMed:1729596, ECO:0000269|PubMed:18775702, ECO:0000269|PubMed:22721921}. Cell projection, podosome {ECO:0000269|PubMed:22721921}. Note=In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear (PubMed:18775702).
uniprot
proteins