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Protein

Heterogeneous nuclear ribonucleoprotein K

Gene

Hnrnpk

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  1. RNA binding Source: UniProtKB-KW
  2. single-stranded DNA binding Source: RGD

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. RNA splicing Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_341557. Processing of Capped Intron-Containing Pre-mRNA.
REACT_353271. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi71058. Hnrnpk.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Nucleusnucleoplasm By similarity
  3. Cell projectionpodosome By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB-SubCell
  4. nucleoplasm Source: UniProtKB-SubCell
  5. podosome Source: UniProtKB-SubCell
  6. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Heterogeneous nuclear ribonucleoprotein KPRO_0000050099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei75 – 751PhosphoserineBy similarity
Modified residuei116 – 1161PhosphoserineBy similarity
Modified residuei198 – 1981N6-acetyllysineBy similarity
Modified residuei214 – 2141PhosphoserineBy similarity
Modified residuei216 – 2161PhosphoserineBy similarity
Modified residuei284 – 2841PhosphoserineBy similarity
Modified residuei296 – 2961Omega-N-methylated arginineBy similarity
Modified residuei299 – 2991Omega-N-methylated arginineBy similarity
Modified residuei379 – 3791PhosphoserineBy similarity
Modified residuei380 – 3801PhosphotyrosineBy similarity
Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By 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

PhosphoSiteiP61980.

Expressioni

Gene expression databases

ExpressionAtlasiP61980. baseline.
GenevestigatoriP61980.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi250729. 2 interactions.
IntActiP61980. 81 interactions.
MINTiMINT-1505757.

Structurei

3D structure databases

ProteinModelPortaliP61980.
SMRiP61980. Positions 45-216, 385-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 10463KH 1PROSITE-ProRule annotationAdd
BLAST
Repeati54 – 76231-1Add
BLAST
Repeati59 – 6243-1
Domaini144 – 20966KH 2PROSITE-ProRule annotationAdd
BLAST
Repeati245 – 25062-1
Repeati257 – 26043-2
Repeati267 – 27043-3
Repeati295 – 29843-4
Repeati324 – 32962-2
Domaini387 – 45165KH 3PROSITE-ProRule annotationAdd
BLAST
Repeati399 – 421231-2Add
BLAST
Repeati404 – 40743-5

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 276276Necessary for interaction with DDX1By similarityAdd
BLAST
Regioni54 – 4213682 X 22 AA approximate repeatsAdd
BLAST
Regioni59 – 4073495 X 4 AA repeats of G-X-G-GAdd
BLAST
Regioni209 – 337129Interaction with ZIK1By similarityAdd
BLAST
Regioni236 – 27338RNA-binding RGG-boxAdd
BLAST
Regioni245 – 329852 X 6 AA approximate repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi289 – 2946Poly-Pro
Compositional biasi310 – 3156Poly-Pro

Sequence similaritiesi

Contains 3 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG285495.
GeneTreeiENSGT00760000119144.
HOGENOMiHOG000019764.
HOVERGENiHBG051916.
InParanoidiP61980.
KOiK12886.

Family and domain databases

Gene3Di3.30.1370.10. 3 hits.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012987. ROK_N.
[Graphical view]
PfamiPF00013. KH_1. 3 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 3 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 3 hits.
PROSITEiPS50084. KH_TYPE_1. 3 hits.
[Graphical view]

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_006253554.2.
UniGeneiRn.11854.

Genome annotation databases

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

Cross-referencesi

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_006253554.2.
UniGeneiRn.11854.

3D structure databases

ProteinModelPortaliP61980.
SMRiP61980. Positions 45-216, 385-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250729. 2 interactions.
IntActiP61980. 81 interactions.
MINTiMINT-1505757.

PTM databases

PhosphoSiteiP61980.

2D gel databases

World-2DPAGE0004:P61980.

Proteomic databases

PaxDbiP61980.
PRIDEiP61980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3190.
RGDi71058. Hnrnpk.

Phylogenomic databases

eggNOGiNOG285495.
GeneTreeiENSGT00760000119144.
HOGENOMiHOG000019764.
HOVERGENiHBG051916.
InParanoidiP61980.
KOiK12886.

Enzyme and pathway databases

ReactomeiREACT_341557. Processing of Capped Intron-Containing Pre-mRNA.
REACT_353271. mRNA Splicing - Major Pathway.

Miscellaneous databases

NextBioi620239.
PROiP61980.

Gene expression databases

ExpressionAtlasiP61980. baseline.
GenevestigatoriP61980.

Family and domain databases

Gene3Di3.30.1370.10. 3 hits.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012987. ROK_N.
[Graphical view]
PfamiPF00013. KH_1. 3 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 3 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 3 hits.
PROSITEiPS50084. KH_TYPE_1. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of a single-stranded DNA binding protein that specifically recognizes deoxycytidine stretch."
    Ito K., Sato K., Endo H.
    Nucleic Acids Res. 22:53-58(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Donryu.
    Tissue: Liver.
  2. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 149-163, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  3. "hnRNP K interacts with RNA binding motif protein 42 and functions in the maintenance of cellular ATP level during stress conditions."
    Fukuda T., Naiki T., Saito M., Irie K.
    Genes Cells 14:113-128(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBM42.

Entry informationi

Entry nameiHNRPK_RAT
AccessioniPrimary (citable) accession number: P61980
Secondary accession number(s): Q07244
, Q15671, Q60577, Q922Y7, Q96J62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 1, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.