HNRPK_BOVIN
ID HNRPK_BOVIN Reviewed; 464 AA.
AC Q3T0D0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein K;
DE Short=hnRNP K;
GN Name=HNRNPK; Synonyms=HNRPK;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the major pre-mRNA-binding proteins. Binds tenaciously
CC to poly(C) sequences. Likely to play a role in the nuclear metabolism
CC of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich
CC sequences. Can also bind poly(C) single-stranded DNA. Plays an
CC important role in p53/TP53 response to DNA damage, acting at the level
CC of both transcription activation and repression. When sumoylated, acts
CC as a transcriptional coactivator of p53/TP53, playing a role in
CC p21/CDKN1A and 14-3-3 sigma/SFN induction. As far as transcription
CC repression is concerned, acts by interacting with long intergenic RNA
CC p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This
CC interaction is necessary for the induction of apoptosis, but not cell
CC cycle arrest (By similarity). As part of a ribonucleoprotein complex
CC composed at least of ZNF827, HNRNPL and the circular RNA circZNF827
CC that nucleates the complex on chromatin, may negatively regulate the
CC transcription of genes involved in neuronal differentiation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61978}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
CC ANKRD28, RBM42 and ZIK1. Interacts with DDX1. Interacts with MDM2; this
CC interaction leads to ubiquitination and proteasomal degradation.
CC Interacts with p53/TP53. Interacts with BRDT (By similarity). Interacts
CC with IVNS1ABP (By similarity).Interacts with PPIA/CYPA (By similarity).
CC Part of a transcription inhibitory ribonucleoprotein complex composed
CC at least of the circular RNA circZNF827, ZNF827 and HNRNPL (By
CC similarity). {ECO:0000250|UniProtKB:P61978,
CC ECO:0000250|UniProtKB:P61979, ECO:0000250|UniProtKB:P61980}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61978}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61978}. Cell projection,
CC podosome {ECO:0000250|UniProtKB:P61978}.
CC -!- PTM: Sumoylated by CBX4. Sumoylation is increased upon DNA damage, such
CC as that produced by doxorubicin, etoposide, UV light and camptothecin,
CC due to enhanced CBX4 phosphorylation by HIPK2 under these conditions
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by MDM2. Doxorubicin treatment does not affect
CC monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination
CC (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250}.
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DR EMBL; BC102450; AAI02451.1; -; mRNA.
DR RefSeq; NP_001029734.1; NM_001034562.1.
DR RefSeq; XP_005210386.1; XM_005210329.3.
DR RefSeq; XP_005210387.1; XM_005210330.2.
DR RefSeq; XP_005210388.1; XM_005210331.3.
DR AlphaFoldDB; Q3T0D0; -.
DR SMR; Q3T0D0; -.
DR STRING; 9913.ENSBTAP00000028162; -.
DR iPTMnet; Q3T0D0; -.
DR PaxDb; Q3T0D0; -.
DR PeptideAtlas; Q3T0D0; -.
DR PRIDE; Q3T0D0; -.
DR Ensembl; ENSBTAT00000028162; ENSBTAP00000028162; ENSBTAG00000021131.
DR GeneID; 528135; -.
DR KEGG; bta:528135; -.
DR CTD; 3190; -.
DR VEuPathDB; HostDB:ENSBTAG00000021131; -.
DR VGNC; VGNC:29897; HNRNPK.
DR eggNOG; KOG2192; Eukaryota.
DR GeneTree; ENSGT00940000153434; -.
DR HOGENOM; CLU_022670_5_1_1; -.
DR InParanoid; Q3T0D0; -.
DR OMA; SSWERFP; -.
DR OrthoDB; 394765at2759; -.
DR TreeFam; TF316335; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000021131; Expressed in spermatocyte and 105 other tissues.
DR ExpressionAtlas; Q3T0D0; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IEA:Ensembl.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:1902165; P:regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR033090; hnRNP_K.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012987; ROK_N.
DR PANTHER; PTHR10288:SF262; PTHR10288:SF262; 1.
DR Pfam; PF00013; KH_1; 3.
DR Pfam; PF08067; ROKNT; 1.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Cell junction; Cell projection; Cytoplasm;
KW DNA-binding; Glycoprotein; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Ribonucleoprotein; RNA-binding; Spliceosome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..464
FT /note="Heterogeneous nuclear ribonucleoprotein K"
FT /id="PRO_0000239836"
FT DOMAIN 42..104
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 54..76
FT /note="1-1"
FT REPEAT 59..62
FT /note="3-1"
FT DOMAIN 144..209
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 245..250
FT /note="2-1"
FT REPEAT 257..260
FT /note="3-2"
FT REPEAT 267..270
FT /note="3-3"
FT REPEAT 295..298
FT /note="3-4"
FT REPEAT 324..329
FT /note="2-2"
FT DOMAIN 387..451
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 399..421
FT /note="1-2"
FT REPEAT 404..407
FT /note="3-5"
FT REGION 1..276
FT /note="Necessary for interaction with DDX1"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..421
FT /note="2 X 22 AA approximate repeats"
FT REGION 59..407
FT /note="5 X 4 AA repeats of G-X-G-G"
FT REGION 209..337
FT /note="Interaction with ZIK1"
FT /evidence="ECO:0000250"
FT REGION 236..273
FT /note="RNA-binding RGG-box"
FT REGION 245..329
FT /note="2 X 6 AA approximate repeats"
FT REGION 250..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 34
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 219
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 316
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 377
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 380
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 405
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61978"
SQ SEQUENCE 464 AA; 51019 MW; 264011C2D457BF92 CRC64;
METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK
GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT
SQLPLESDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL
FQECCPQSTD RVVLIGGKPD RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT
MMFDDRRGRP VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID TWSPSEWQMA
YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG SIIGKGGQRI KQIRHESGAS
IKIDEPLEGS EDRIITITGT QDQIQNAQYL LQNSVKQYAD VEGF
