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Protein

Heterogeneous nuclear ribonucleoprotein K

Gene

Hnrnpk

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • C-rich single-stranded DNA binding Source: RGD
  • double-stranded DNA binding Source: RGD
  • mRNA 3'-UTR binding Source: RGD
  • mRNA CDS binding Source: RGD
  • pre-mRNA 3'-splice site binding Source: RGD
  • proximal promoter sequence-specific DNA binding Source: RGD
  • ribonucleoprotein complex binding Source: RGD
  • single-stranded DNA binding Source: RGD

GO - Biological processi

  • acute-phase response Source: RGD
  • aging Source: RGD
  • camera-type eye development Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to forskolin Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • cellular response to rapamycin Source: RGD
  • central nervous system development Source: RGD
  • cerebellum development Source: RGD
  • cerebral cortex development Source: RGD
  • hippocampus development Source: RGD
  • kidney development Source: RGD
  • liver development Source: RGD
  • lung development Source: RGD
  • mRNA processing Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of branching morphogenesis of a nerve Source: RGD
  • negative regulation of gene expression Source: RGD
  • negative regulation of protein binding Source: RGD
  • negative regulation of transcription by RNA polymerase II Source: RGD
  • ovarian follicle development Source: RGD
  • peripheral nervous system development Source: RGD
  • positive regulation of dendrite extension Source: RGD
  • positive regulation of dendritic spine development Source: RGD
  • positive regulation of long-term synaptic potentiation Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of protein localization to cell surface Source: RGD
  • positive regulation of RNA splicing Source: RGD
  • positive regulation of synapse maturation Source: RGD
  • positive regulation of synaptic transmission Source: RGD
  • regulation of transcription by RNA polymerase II Source: RGD
  • response to activity Source: RGD
  • response to salt Source: RGD
  • RNA splicing Source: UniProtKB-KW
  • thymus development Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionActivator, DNA-binding, Repressor, Ribonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-RNO-72163 mRNA Splicing - Major Pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein K
Short name:
hnRNP K
Alternative name(s):
dC stretch-binding protein
Short name:
CSBP
Gene namesi
Name:Hnrnpk
Synonyms:Hnrpk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi71058 Hnrnpk

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000500991 – 463Heterogeneous nuclear ribonucleoprotein KAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei34N6-acetyllysine; alternateBy similarity1
Cross-linki34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei36PhosphoserineBy similarity1
Modified residuei39PhosphothreonineBy similarity1
Cross-linki52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei75PhosphoserineBy similarity1
Modified residuei116PhosphoserineCombined sources1
Cross-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei198N6-acetyllysineBy similarity1
Modified residuei214PhosphoserineBy similarity1
Modified residuei216PhosphoserineBy similarity1
Modified residuei219N6-succinyllysine; alternateBy similarity1
Cross-linki219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei284PhosphoserineBy similarity1
Modified residuei296Omega-N-methylated arginineBy similarity1
Modified residuei299Omega-N-methylated arginineBy similarity1
Modified residuei316Omega-N-methylarginineBy similarity1
Modified residuei377Omega-N-methylarginineBy similarity1
Modified residuei379PhosphoserineBy similarity1
Modified residuei380PhosphotyrosineBy similarity1
Modified residuei405N6-acetyllysine; alternateBy similarity1
Cross-linki405Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei420PhosphoserineBy similarity1
Cross-linki422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity

Post-translational modificationi

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).By similarity
Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination (By similarity).By similarity
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP61980
PRIDEiP61980

2D gel databases

World-2DPAGE0004:P61980

PTM databases

iPTMnetiP61980
PhosphoSitePlusiP61980
SwissPalmiP61980

Expressioni

Gene expression databases

BgeeiENSRNOG00000019113
ExpressionAtlasiP61980 baseline and differential
GenevisibleiP61980 RN

Interactioni

Subunit structurei

Identified in the spliceosome C complex (By similarity). Interacts with ANKRD28 and ZIK1 (By similarity). Interacts with DDX1 (By similarity). Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation (By similarity). Interacts with p53/TP53 (By similarity). Interacts with BRDT (By similarity). Interacts with RBM42 (PubMed:19170760). Interacts with IVNS1ABP (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi250729, 2 interactors
IntActiP61980, 82 interactors
MINTiP61980
STRINGi10116.ENSRNOP00000025980

Structurei

3D structure databases

ProteinModelPortaliP61980
SMRiP61980
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 104KH 1PROSITE-ProRule annotationAdd BLAST63
Repeati54 – 761-1Add BLAST23
Repeati59 – 623-14
Domaini144 – 209KH 2PROSITE-ProRule annotationAdd BLAST66
Repeati245 – 2502-16
Repeati257 – 2603-24
Repeati267 – 2703-34
Repeati295 – 2983-44
Repeati324 – 3292-26
Domaini387 – 451KH 3PROSITE-ProRule annotationAdd BLAST65
Repeati399 – 4211-2Add BLAST23
Repeati404 – 4073-54

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 276Necessary for interaction with DDX1By similarityAdd BLAST276
Regioni54 – 4212 X 22 AA approximate repeatsAdd BLAST368
Regioni59 – 4075 X 4 AA repeats of G-X-G-GAdd BLAST349
Regioni209 – 337Interaction with ZIK1By similarityAdd BLAST129
Regioni236 – 273RNA-binding RGG-boxAdd BLAST38
Regioni245 – 3292 X 6 AA approximate repeatsAdd BLAST85

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi289 – 294Poly-Pro6
Compositional biasi310 – 315Poly-Pro6

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2192 Eukaryota
ENOG4111GSB LUCA
GeneTreeiENSGT00760000119144
HOGENOMiHOG000019764
HOVERGENiHBG051916
InParanoidiP61980
KOiK12886

Family and domain databases

Gene3Di3.30.1370.10, 3 hits
InterProiView protein in InterPro
IPR033090 hnRNP_K
IPR004087 KH_dom
IPR004088 KH_dom_type_1
IPR036612 KH_dom_type_1_sf
IPR012987 ROK_N
PANTHERiPTHR10288:SF221 PTHR10288:SF221, 1 hit
PfamiView protein in Pfam
PF00013 KH_1, 3 hits
PF08067 ROKNT, 1 hit
SMARTiView protein in SMART
SM00322 KH, 3 hits
SUPFAMiSSF54791 SSF54791, 3 hits
PROSITEiView protein in PROSITE
PS50084 KH_TYPE_1, 3 hits

Sequencei

Sequence statusi: Complete.

P61980-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ
60 70 80 90 100
SKNAGAVIGK GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI
110 120 130 140 150
LKKIIPTLEE GLQLPSPTAT SQLPLESDAV ECLNYQHYKG SDFDCELRLL
160 170 180 190 200
IHQSLAGGII GVKGAKIKEL RENTQTTIKL FQECCPHSTD RVVLIGGKPD
210 220 230 240 250
RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT MMFDDRRGRP
260 270 280 290 300
VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG
310 320 330 340 350
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID
360 370 380 390 400
TWSPSEWQMA YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG
410 420 430 440 450
SIIGKGGQRI KQIRHESGAS IKIDEPLEGS EDRIITITGT QDQIQNAQYL
460
LQNSVKQYSG KFF
Length:463
Mass (Da):50,976
Last modified:June 7, 2004 - v1
Checksum:i0F70EE169B2A064A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17711 mRNA Translation: BAA04566.1
PIRiS41495
RefSeqiNP_476482.1, NM_057141.1
XP_006253616.1, XM_006253554.3
UniGeneiRn.11854

Genome annotation databases

EnsembliENSRNOT00000025916; ENSRNOP00000025915; ENSRNOG00000019113
GeneIDi117282
KEGGirno:117282
UCSCiRGD:71058 rat

Similar proteinsi

Entry informationi

Entry nameiHNRPK_RAT
AccessioniPrimary (citable) accession number: P61980
Secondary accession number(s): Q07244
, Q15671, Q60577, Q922Y7, Q96J62
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: May 23, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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