HNRPK_MOUSE
ID HNRPK_MOUSE Reviewed; 463 AA.
AC P61979; Q07244; Q15671; Q60577; Q8BGQ8; Q922Y7; Q96J62;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein K;
DE Short=hnRNP K;
GN Name=Hnrnpk; Synonyms=Hnrpk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lymphoma;
RX PubMed=8021272; DOI=10.1016/s0021-9258(17)32487-0;
RA Ostrowski J., van Seuningen I., Seger R., Rauch C.T., Sleath P.R.,
RA McMullen B.A., Bomsztyk K.;
RT "Purification, cloning, and expression of a murine phosphoprotein that
RT binds the kappa B motif in vitro identifies it as the homolog of the human
RT heterogeneous nuclear ribonucleoprotein K protein. Description of a novel
RT DNA-dependent phosphorylation process.";
RL J. Biol. Chem. 269:17626-17634(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spinal ganglion, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 149-163 AND 207-219, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH ZIK1.
RX PubMed=8910362; DOI=10.1074/jbc.271.44.27701;
RA Denisenko O.N., O'Neill B., Ostrowski J., Van Seuningen I., Bomsztyk K.;
RT "Zik1, a transcriptional repressor that interacts with the heterogeneous
RT nuclear ribonucleoprotein particle K protein.";
RL J. Biol. Chem. 271:27701-27706(1996).
RN [6]
RP INDUCTION.
RX PubMed=16360036; DOI=10.1016/j.cell.2005.09.032;
RA Moumen A., Masterson P., O'Connor M.J., Jackson S.P.;
RT "hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response
RT to DNA damage.";
RL Cell 123:1065-1078(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP FUNCTION.
RX PubMed=20673990; DOI=10.1016/j.cell.2010.06.040;
RA Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J.,
RA Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D.,
RA Regev A., Lander E.S., Jacks T., Rinn J.L.;
RT "A large intergenic noncoding RNA induced by p53 mediates global gene
RT repression in the p53 response.";
RL Cell 142:409-419(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP INTERACTION WITH BRDT.
RX PubMed=22570411; DOI=10.1093/nar/gks342;
RA Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.;
RT "The testis-specific double bromodomain-containing protein BRDT forms a
RT complex with multiple spliceosome components and is required for mRNA
RT splicing and 3'-UTR truncation in round spermatids.";
RL Nucleic Acids Res. 40:7162-7175(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-198 AND LYS-405,
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-316 AND ARG-377, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 (By similarity). As far as
CC transcription repression is concerned, acts by interacting with long
CC intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53.
CC This interaction is necessary for the induction of apoptosis, but not
CC cell cycle arrest. As part of a ribonucleoprotein complex composed at
CC least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates
CC the complex on chromatin, may negatively regulate the transcription of
CC genes involved in neuronal differentiation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P61978,
CC ECO:0000269|PubMed:20673990}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC Interacts with ANKRD28 and RBM42 (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 ZIK1 (PubMed:8910362).
CC Interacts with BRDT (PubMed:22570411). 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:P61980,
CC ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:8910362}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61978}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61978}. Cell projection,
CC podosome {ECO:0000250|UniProtKB:P61978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P61979-1, Q07244-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P61979-2, Q07244-2;
CC Sequence=VSP_010622;
CC Name=3;
CC IsoId=P61979-3; Sequence=VSP_012581;
CC -!- INDUCTION: By DNA damage. This up-regulation is due to protein
CC stabilization. The constitutive protein levels are controlled by MDM2-
CC mediated ubiquitination and degradation via the proteasome pathway.
CC {ECO:0000269|PubMed:16360036}.
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; L31961; AAA21731.1; -; mRNA.
DR EMBL; AK011428; BAB27614.1; -; mRNA.
DR EMBL; AK051313; BAC34601.1; -; mRNA.
DR EMBL; AK078777; BAC37389.1; -; mRNA.
DR EMBL; AK088462; BAC40368.1; -; mRNA.
DR EMBL; BC006694; AAH06694.1; -; mRNA.
DR CCDS; CCDS49283.1; -.
DR CCDS; CCDS79197.1; -. [P61979-3]
DR CCDS; CCDS79199.1; -. [P61979-2]
DR RefSeq; NP_001288269.1; NM_001301340.1. [P61979-2]
DR RefSeq; NP_001288270.1; NM_001301341.1. [P61979-2]
DR RefSeq; NP_001288272.1; NM_001301343.1. [P61979-2]
DR RefSeq; NP_001288273.1; NM_001301344.1.
DR RefSeq; NP_001288274.1; NM_001301345.1. [P61979-3]
DR RefSeq; NP_079555.1; NM_025279.3. [P61979-1]
DR RefSeq; XP_006517166.1; XM_006517103.3. [P61979-2]
DR RefSeq; XP_006517167.1; XM_006517104.2. [P61979-2]
DR RefSeq; XP_017170884.1; XM_017315395.1.
DR RefSeq; XP_017170885.1; XM_017315396.1.
DR AlphaFoldDB; P61979; -.
DR SMR; P61979; -.
DR BioGRID; 200359; 263.
DR IntAct; P61979; 16.
DR MINT; P61979; -.
DR STRING; 10090.ENSMUSP00000039269; -.
DR iPTMnet; P61979; -.
DR PhosphoSitePlus; P61979; -.
DR SwissPalm; P61979; -.
DR REPRODUCTION-2DPAGE; IPI00223253; -.
DR REPRODUCTION-2DPAGE; P61979; -.
DR EPD; P61979; -.
DR jPOST; P61979; -.
DR MaxQB; P61979; -.
DR PaxDb; P61979; -.
DR PeptideAtlas; P61979; -.
DR PRIDE; P61979; -.
DR ProteomicsDB; 269620; -.
DR ProteomicsDB; 269621; -. [P61979-2]
DR ProteomicsDB; 269622; -. [P61979-3]
DR Antibodypedia; 2214; 618 antibodies from 40 providers.
DR DNASU; 15387; -.
DR Ensembl; ENSMUST00000043269; ENSMUSP00000039269; ENSMUSG00000021546. [P61979-1]
DR Ensembl; ENSMUST00000116403; ENSMUSP00000112104; ENSMUSG00000021546. [P61979-2]
DR Ensembl; ENSMUST00000176207; ENSMUSP00000135354; ENSMUSG00000021546. [P61979-3]
DR Ensembl; ENSMUST00000224182; ENSMUSP00000153253; ENSMUSG00000021546. [P61979-2]
DR Ensembl; ENSMUST00000225674; ENSMUSP00000152935; ENSMUSG00000021546. [P61979-2]
DR GeneID; 15387; -.
DR KEGG; mmu:15387; -.
DR UCSC; uc007qtx.2; mouse.
DR UCSC; uc007qty.2; mouse. [P61979-3]
DR CTD; 3190; -.
DR MGI; MGI:99894; Hnrnpk.
DR VEuPathDB; HostDB:ENSMUSG00000021546; -.
DR eggNOG; KOG2192; Eukaryota.
DR GeneTree; ENSGT00940000153434; -.
DR InParanoid; P61979; -.
DR OMA; SSWERFP; -.
DR TreeFam; TF316335; -.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 15387; 27 hits in 76 CRISPR screens.
DR ChiTaRS; Hnrnpk; mouse.
DR PRO; PR:P61979; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P61979; protein.
DR Bgee; ENSMUSG00000021546; Expressed in embryonic post-anal tail and 73 other tissues.
DR ExpressionAtlas; P61979; baseline and differential.
DR Genevisible; P61979; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0042805; F:actinin binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:1990829; F:C-rich single-stranded DNA binding; ISO:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005521; F:lamin binding; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990715; F:mRNA CDS binding; ISO:MGI.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:1904322; P:cellular response to forskolin; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0021987; P:cerebral cortex development; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000173; P:negative regulation of branching morphogenesis of a nerve; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISO:MGI.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISO:MGI.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
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; IMP:MGI.
DR GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cell junction;
KW Cell projection; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Glycoprotein; Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Ribonucleoprotein; RNA-binding; Spliceosome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..463
FT /note="Heterogeneous nuclear ribonucleoprotein K"
FT /id="PRO_0000050097"
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:0000269|PubMed:8910362"
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:0007744|PubMed:23806337"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:19144319"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61978"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:24129315"
FT MOD_RES 377
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
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:0007744|PubMed:23806337"
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"
FT VAR_SEQ 111..134
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012581"
FT VAR_SEQ 459..463
FT /note="SGKFF -> ADVEGF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8021272"
FT /id="VSP_010622"
FT CONFLICT 132
FT /note="C -> V (in Ref. 1; AAA21731)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="Q -> P (in Ref. 1; AAA21731)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> T (in Ref. 1; AAA21731)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="D -> S (in Ref. 1; AAA21731)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="D -> E (in Ref. 1; AAA21731)"
FT /evidence="ECO:0000305"
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
