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P61980 (HNRPK_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein K

Short name=hnRNP K
Alternative name(s):
dC stretch-binding protein
Short name=CSBP
Gene names
Name:Hnrnpk
Synonyms:Hnrpk
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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. Ref.3

Subcellular location

Cytoplasm By similarity. Nucleusnucleoplasm By similarity. Cell projectionpodosome By similarity.

Post-translational modification

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.

Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination By similarity.

O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner By similarity.

Sequence similarities

Contains 3 KH domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Heterogeneous nuclear ribonucleoprotein K
PRO_0000050099

Regions

Domain42 – 10463KH 1
Repeat54 – 76231-1
Repeat59 – 6243-1
Domain144 – 20966KH 2
Repeat245 – 25062-1
Repeat257 – 26043-2
Repeat267 – 27043-3
Repeat295 – 29843-4
Repeat324 – 32962-2
Domain387 – 45165KH 3
Repeat399 – 421231-2
Repeat404 – 40743-5
Region1 – 276276Necessary for interaction with DDX1 By similarity
Region54 – 4213682 X 22 AA approximate repeats
Region59 – 4073495 X 4 AA repeats of G-X-G-G
Region209 – 337129Interaction with ZIK1 By similarity
Region236 – 27338RNA-binding RGG-box
Region245 – 329852 X 6 AA approximate repeats
Compositional bias289 – 2946Poly-Pro
Compositional bias310 – 3156Poly-Pro

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1161Phosphoserine By similarity
Modified residue1981N6-acetyllysine By similarity
Modified residue2141Phosphoserine By similarity
Modified residue2161Phosphoserine By similarity
Modified residue2841Phosphoserine By similarity
Modified residue2961Omega-N-methylated arginine By similarity
Modified residue2991Omega-N-methylated arginine By similarity
Modified residue3791Phosphoserine By similarity
Modified residue3801Phosphotyrosine By similarity
Cross-link422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
P61980 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 0F70EE169B2A064A

FASTA46350,976
        10         20         30         40         50         60 
METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK 

        70         80         90        100        110        120 
GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT 

       130        140        150        160        170        180 
SQLPLESDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL 

       190        200        210        220        230        240 
FQECCPHSTD RVVLIGGKPD RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT 

       250        260        270        280        290        300 
MMFDDRRGRP VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG 

       310        320        330        340        350        360 
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID TWSPSEWQMA 

       370        380        390        400        410        420 
YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG SIIGKGGQRI KQIRHESGAS 

       430        440        450        460 
IKIDEPLEGS EDRIITITGT QDQIQNAQYL LQNSVKQYSG KFF 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17711 mRNA. Translation: BAA04566.1.
PIRS41495.
RefSeqNP_476482.1. NM_057141.1.
XP_006253616.1. XM_006253554.1.
UniGeneRn.11854.

3D structure databases

ProteinModelPortalP61980.
SMRP61980. Positions 45-216, 385-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250729. 2 interactions.
IntActP61980. 81 interactions.
MINTMINT-1505757.

PTM databases

PhosphoSiteP61980.

2D gel databases

World-2DPAGE0004:P61980.

Proteomic databases

PaxDbP61980.
PRIDEP61980.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025916; ENSRNOP00000025915; ENSRNOG00000019113.
GeneID117282.
KEGGrno:117282.
UCSCRGD:71058. rat.

Organism-specific databases

CTD3190.
RGD71058. Hnrnpk.

Phylogenomic databases

eggNOGNOG285495.
GeneTreeENSGT00730000110620.
HOGENOMHOG000019764.
HOVERGENHBG051916.
InParanoidP61980.
KOK12886.

Gene expression databases

GenevestigatorP61980.

Family and domain databases

Gene3D3.30.1370.10. 3 hits.
InterProIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012987. ROK_N.
[Graphical view]
PfamPF00013. KH_1. 3 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]
SMARTSM00322. KH. 3 hits.
[Graphical view]
SUPFAMSSF54791. SSF54791. 3 hits.
PROSITEPS50084. KH_TYPE_1. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio620239.
PROP61980.

Entry information

Entry nameHNRPK_RAT
AccessionPrimary (citable) accession number: P61980
Secondary accession number(s): Q07244 expand/collapse secondary AC list , Q15671, Q60577, Q922Y7, Q96J62
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families