ID HNRPK_RAT Reviewed; 463 AA. AC P61980; Q07244; Q15671; Q60577; Q922Y7; Q96J62; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 1. DT 27-MAR-2024, entry version 174. DE RecName: Full=Heterogeneous nuclear ribonucleoprotein K; DE Short=hnRNP K; DE AltName: Full=dC stretch-binding protein; DE Short=CSBP; GN Name=Hnrnpk; Synonyms=Hnrpk; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Donryu; TISSUE=Liver; RX PubMed=8127654; DOI=10.1093/nar/22.1.53; RA Ito K., Sato K., Endo H.; RT "Cloning and characterization of a single-stranded DNA binding protein that RT specifically recognizes deoxycytidine stretch."; RL Nucleic Acids Res. 22:53-58(1994). RN [2] RP PROTEIN SEQUENCE OF 149-163, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus; RA Lubec G., Chen W.-Q.; RL Submitted (APR-2007) to UniProtKB. RN [3] RP INTERACTION WITH RBM42. RX PubMed=19170760; DOI=10.1111/j.1365-2443.2008.01256.x; RA Fukuda T., Naiki T., Saito M., Irie K.; RT "hnRNP K interacts with RNA binding motif protein 42 and functions in the RT maintenance of cellular ATP level during stress conditions."; RL Genes Cells 14:113-128(2009). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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 (By similarity). CC Interacts with ANKRD28 and ZIK1 (By similarity). Interacts with DDX1 CC (By similarity). Interacts with MDM2; this interaction leads to CC ubiquitination and proteasomal degradation (By similarity). Interacts CC with p53/TP53 (By similarity). Interacts with BRDT (By similarity). CC Interacts with RBM42 (PubMed:19170760). Interacts with IVNS1ABP (By CC similarity). Interacts with PPIA/CYPA (By similarity). Part of a CC transcription inhibitory ribonucleoprotein complex composed at least of CC the circular RNA circZNF827, ZNF827 and HNRNPL (By similarity). CC {ECO:0000250|UniProtKB:P61978, ECO:0000250|UniProtKB:P61979, CC ECO:0000269|PubMed:19170760}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D17711; BAA04566.1; -; mRNA. DR PIR; S41495; S41495. DR RefSeq; NP_476482.1; NM_057141.1. DR RefSeq; XP_006253616.1; XM_006253554.3. DR AlphaFoldDB; P61980; -. DR SMR; P61980; -. DR BioGRID; 250729; 7. DR IntAct; P61980; 84. DR MINT; P61980; -. DR STRING; 10116.ENSRNOP00000025980; -. DR GlyGen; P61980; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61980; -. DR PhosphoSitePlus; P61980; -. DR SwissPalm; P61980; -. DR jPOST; P61980; -. DR PaxDb; 10116-ENSRNOP00000025980; -. DR GeneID; 117282; -. DR KEGG; rno:117282; -. DR UCSC; RGD:71058; rat. DR AGR; RGD:71058; -. DR CTD; 3190; -. DR RGD; 71058; Hnrnpk. DR VEuPathDB; HostDB:ENSRNOG00000019113; -. DR eggNOG; KOG2192; Eukaryota. DR InParanoid; P61980; -. DR OrthoDB; 465127at2759; -. DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway. DR Reactome; R-RNO-72203; Processing of Capped Intron-Containing Pre-mRNA. DR PRO; PR:P61980; -. DR Proteomes; UP000002494; Chromosome 17. DR Bgee; ENSRNOG00000019113; Expressed in thymus and 19 other cell types or tissues. DR ExpressionAtlas; P61980; baseline and differential. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW. DR GO; GO:0043679; C:axon terminus; IDA:RGD. DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD. DR GO; GO:0005938; C:cell cortex; IDA:RGD. DR GO; GO:0000785; C:chromatin; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:RGD. DR GO; GO:0043197; C:dendritic spine; IDA:RGD. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell. DR GO; GO:0098794; C:postsynapse; IDA:SynGO. DR GO; GO:0032993; C:protein-DNA complex; IDA:RGD. DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0042805; F:actinin binding; IPI:RGD. DR GO; GO:0051117; F:ATPase binding; IPI:RGD. DR GO; GO:1990829; F:C-rich single-stranded DNA binding; IDA:RGD. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:RGD. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD. DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0005521; F:lamin binding; IPI:RGD. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:1990715; F:mRNA CDS binding; IDA:RGD. DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IDA:RGD. DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:RGD. DR GO; GO:0003723; F:RNA binding; ISO:RGD. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:RGD. DR GO; GO:0006953; P:acute-phase response; IEP:RGD. DR GO; GO:0043010; P:camera-type eye development; IEP:RGD. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD. DR GO; GO:1904322; P:cellular response to forskolin; IDA:RGD. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:RGD. DR GO; GO:0071284; P:cellular response to lead ion; IEP:RGD. DR GO; GO:0072752; P:cellular response to rapamycin; IEP:RGD. DR GO; GO:0021549; P:cerebellum development; IEP:RGD. DR GO; GO:0021987; P:cerebral cortex development; IDA:RGD. DR GO; GO:0021766; P:hippocampus development; IEP:RGD. DR GO; GO:0001822; P:kidney development; IEP:RGD. DR GO; GO:0001889; P:liver development; IEP:RGD. DR GO; GO:0030324; P:lung development; IEP:RGD. DR GO; GO:0008584; P:male gonad development; IEP:RGD. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD. DR GO; GO:2000173; P:negative regulation of branching morphogenesis of a nerve; IMP:RGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISO:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD. DR GO; GO:0001541; P:ovarian follicle development; IMP:RGD. DR GO; GO:0007422; P:peripheral nervous system development; IEP:RGD. DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:RGD. DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD. DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD. DR GO; GO:0031643; P:positive regulation of myelination; IMP:RGD. DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD. DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:RGD. DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:RGD. DR GO; GO:0033120; P:positive regulation of RNA splicing; IMP:RGD. DR GO; GO:0090129; P:positive regulation of synapse maturation; IMP:RGD. DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:1902165; P:regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD. DR GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; ISO:RGD. DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:RGD. DR GO; GO:0014823; P:response to activity; IEP:RGD. DR GO; GO:1902074; P:response to salt; IEP:RGD. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0048538; P:thymus development; IEP:RGD. DR CDD; cd22432; KH-I_HNRNPK_rpt1; 1. DR CDD; cd22433; KH-I_HNRNPK_rpt2; 1. DR CDD; cd22434; KH-I_HNRNPK_rpt3; 1. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 3. 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:SF344; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; 1. DR PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1. DR Pfam; PF00013; KH_1; 3. DR Pfam; PF08067; ROKNT; 1. DR SMART; SM00322; KH; 3. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 3. DR PROSITE; PS50084; KH_TYPE_1; 3. DR World-2DPAGE; 0004:P61980; -. DR Genevisible; P61980; RN. PE 1: Evidence at protein level; KW Acetylation; Activator; Cell junction; Cell projection; Cytoplasm; KW Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond; KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding; KW Spliceosome; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..463 FT /note="Heterogeneous nuclear ribonucleoprotein K" FT /id="PRO_0000050099" 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:0007744|PubMed:22673903" 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 463 AA; 50976 MW; 0F70EE169B2A064A CRC64; METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT SQLPLESDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL FQECCPHSTD 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 LQNSVKQYSG KFF //