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Heterogeneous nuclear ribonucleoprotein K (hnRNP K) (dC stretch-binding protein) (CSBP)

 HNRPK_RAT               Reviewed;         463 AA.
P61980; Q07244; Q15671; Q60577; Q922Y7; Q96J62;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
25-OCT-2017, entry version 137.
RecName: Full=Heterogeneous nuclear ribonucleoprotein K;
Short=hnRNP K;
AltName: Full=dC stretch-binding protein;
Short=CSBP;
Name=Hnrnpk; Synonyms=Hnrpk;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Donryu; TISSUE=Liver;
PubMed=8127654; DOI=10.1093/nar/22.1.53;
Ito K., Sato K., Endo H.;
"Cloning and characterization of a single-stranded DNA binding protein
that specifically recognizes deoxycytidine stretch.";
Nucleic Acids Res. 22:53-58(1994).
[2]
PROTEIN SEQUENCE OF 149-163, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[3]
INTERACTION WITH RBM42.
PubMed=19170760; DOI=10.1111/j.1365-2443.2008.01256.x;
Fukuda T., Naiki T., Saito M., Irie K.;
"hnRNP K interacts with RNA binding motif protein 42 and functions in
the maintenance of cellular ATP level during stress conditions.";
Genes Cells 14:113-128(2009).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
ANKRD28 and ZIK1. Interacts with DDX1 (By similarity). Interacts
with MDM2; this interaction leads to ubiquitination and
proteasomal degradation. Interacts with p53/TP53. Interacts with
BRDT (By similarity). Interacts with RBM42. {ECO:0000250,
ECO:0000269|PubMed:19170760}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61978}.
Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61978}. Cell
projection, podosome {ECO:0000250|UniProtKB:P61978}.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by MDM2. Doxorubicin treatment does not affect
monoubiquitination, but slightly decreases HNRNPK poly-
ubiquitination (By similarity). {ECO:0000250}.
-!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent
manner. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; D17711; BAA04566.1; -; mRNA.
PIR; S41495; S41495.
RefSeq; NP_476482.1; NM_057141.1.
RefSeq; XP_006253616.1; XM_006253554.3.
UniGene; Rn.11854; -.
ProteinModelPortal; P61980; -.
SMR; P61980; -.
BioGrid; 250729; 2.
IntAct; P61980; 82.
MINT; MINT-1505757; -.
STRING; 10116.ENSRNOP00000025980; -.
iPTMnet; P61980; -.
PhosphoSitePlus; P61980; -.
World-2DPAGE; 0004:P61980; -.
PaxDb; P61980; -.
PRIDE; P61980; -.
Ensembl; ENSRNOT00000025916; ENSRNOP00000025915; ENSRNOG00000019113.
GeneID; 117282; -.
KEGG; rno:117282; -.
UCSC; RGD:71058; rat.
CTD; 3190; -.
RGD; 71058; Hnrnpk.
eggNOG; KOG2192; Eukaryota.
eggNOG; ENOG4111GSB; LUCA.
GeneTree; ENSGT00760000119144; -.
HOGENOM; HOG000019764; -.
HOVERGEN; HBG051916; -.
InParanoid; P61980; -.
KO; K12886; -.
Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
PRO; PR:P61980; -.
Proteomes; UP000002494; Chromosome 17.
Bgee; ENSRNOG00000019113; -.
ExpressionAtlas; P61980; baseline.
Genevisible; P61980; RN.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0005938; C:cell cortex; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0032993; C:protein-DNA complex; IDA:RGD.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0042805; F:actinin binding; IPI:RGD.
GO; GO:0051117; F:ATPase binding; IPI:RGD.
GO; GO:1990829; F:C-rich single-stranded DNA binding; IDA:RGD.
GO; GO:0001159; F:core promoter proximal region DNA binding; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
GO; GO:0005521; F:lamin binding; IPI:RGD.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
GO; GO:1990715; F:mRNA CDS binding; IDA:RGD.
GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:RGD.
GO; GO:0003697; F:single-stranded DNA binding; IDA:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0006953; P:acute-phase response; IEP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0043010; P:camera-type eye development; IEP:RGD.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD.
GO; GO:1904322; P:cellular response to forskolin; IDA:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:RGD.
GO; GO:0072752; P:cellular response to rapamycin; IEP:RGD.
GO; GO:0007417; P:central nervous system development; IEP:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IDA:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:2000173; P:negative regulation of branching morphogenesis of a nerve; IMP:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:0032091; P:negative regulation of protein binding; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
GO; GO:0007422; P:peripheral nervous system development; IEP:RGD.
GO; GO:1903861; P:positive regulation of dendrite extension; IMP:RGD.
GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:RGD.
GO; GO:0033120; P:positive regulation of RNA splicing; IMP:RGD.
GO; GO:0090129; P:positive regulation of synapse maturation; IMP:RGD.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:1902074; P:response to salt; IEP:RGD.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0048538; P:thymus development; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 3.
InterPro; IPR033090; hnRNP_K.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
InterPro; IPR012987; ROK_N.
PANTHER; PTHR10288:SF221; PTHR10288:SF221; 1.
Pfam; PF00013; KH_1; 3.
Pfam; PF08067; ROKNT; 1.
SMART; SM00322; KH; 3.
SUPFAM; SSF54791; SSF54791; 3.
PROSITE; PS50084; KH_TYPE_1; 3.
1: Evidence at protein level;
Acetylation; Activator; Cell junction; Cell projection;
Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
Glycoprotein; Isopeptide bond; Methylation; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; Ribonucleoprotein; RNA-binding; Spliceosome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 463 Heterogeneous nuclear ribonucleoprotein
K.
/FTId=PRO_0000050099.
DOMAIN 42 104 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 54 76 1-1.
REPEAT 59 62 3-1.
DOMAIN 144 209 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 245 250 2-1.
REPEAT 257 260 3-2.
REPEAT 267 270 3-3.
REPEAT 295 298 3-4.
REPEAT 324 329 2-2.
DOMAIN 387 451 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 399 421 1-2.
REPEAT 404 407 3-5.
REGION 1 276 Necessary for interaction with DDX1.
{ECO:0000250}.
REGION 54 421 2 X 22 AA approximate repeats.
REGION 59 407 5 X 4 AA repeats of G-X-G-G.
REGION 209 337 Interaction with ZIK1. {ECO:0000250}.
REGION 236 273 RNA-binding RGG-box.
REGION 245 329 2 X 6 AA approximate repeats.
COMPBIAS 289 294 Poly-Pro.
COMPBIAS 310 315 Poly-Pro.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 34 34 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 39 39 Phosphothreonine.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 198 198 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 219 219 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 296 296 Omega-N-methylated arginine.
{ECO:0000250}.
MOD_RES 299 299 Omega-N-methylated arginine.
{ECO:0000250}.
MOD_RES 316 316 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 377 377 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 380 380 Phosphotyrosine.
{ECO:0000250|UniProtKB:P61978}.
MOD_RES 405 405 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 34 34 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 34 34 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 52 52 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 60 60 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 219 219 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 405 405 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P61978}.
CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P61978}.
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


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