Heterogeneous nuclear ribonucleoprotein K

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P61980 (HNRPK_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Protein existence	Evidence 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.4
Subcellular location	Cytoplasm By similarity. Nucleus › nucleoplasm 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator Repressor Ribonucleoprotein
PTM	Acetylation Glycoprotein Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW single-stranded DNA binding Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 463

463

Heterogeneous nuclear ribonucleoprotein K

PRO_0000050099

Regions

Domain

42 – 104

KH 1

Repeat

54 – 76

1-1

Repeat

59 – 62

3-1

Domain

144 – 209

KH 2

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

Repeat

399 – 421

1-2

Repeat

404 – 407

3-5

Region

1 – 276

276

Necessary for interaction with DDX1 By similarity

Region

54 – 421

368

2 X 22 AA approximate repeats

Region

59 – 407

349

5 X 4 AA repeats of G-X-G-G

Region

209 – 337

129

Interaction with ZIK1 By similarity

Region

236 – 273

RNA-binding RGG-box

Region

245 – 329

2 X 6 AA approximate repeats

Compositional bias

289 – 294

Poly-Pro

Compositional bias

310 – 315

Poly-Pro

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

116

Phosphoserine By similarity

Modified residue

214

Phosphoserine By similarity

Modified residue

216

Phosphoserine By similarity

Modified residue

284

Phosphoserine Ref.3

Modified residue

296

Omega-N-methylated arginine By similarity

Modified residue

299

Omega-N-methylated arginine By similarity

Modified residue

379

Phosphoserine By similarity

Modified residue

380

Phosphotyrosine By similarity

Cross-link

422

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P61980 [UniParc].

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

FASTA

463

50,976

        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

	« Hide 'large scale' referencesShow 'large scale' 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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
[3]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
[4]	"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.
IPI	IPI00780608.
PIR	S41495.
RefSeq	NP_476482.1. NM_057141.1.
UniGene	Rn.11854.
3D structure databases
ProteinModelPortal	P61980.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61980. 80 interactions.
MINT	MINT-1505757.
PTM databases
PhosphoSite	P61980.
2D gel databases
World-2DPAGE	0004:P61980.
Proteomic databases
PaxDb	P61980.
PRIDE	P61980.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000025916; ENSRNOP00000025915; ENSRNOG00000019113.
GeneID	117282.
KEGG	rno:117282.
UCSC	RGD:71058. rat.
Organism-specific databases
CTD	3190.
RGD	71058. Hnrnpk.
Phylogenomic databases
eggNOG	NOG285495.
GeneTree	ENSGT00550000074311.
HOGENOM	HOG000019764.
HOVERGEN	HBG051916.
InParanoid	P61980.
KO	K12886.
Gene expression databases
ArrayExpress	P61980.
Genevestigator	P61980.
GermOnline	ENSRNOG00000019113. Rattus norvegicus.
Family and domain databases
InterPro	IPR004087. KH_dom. IPR004088. KH_dom_type_1. IPR012987. ROK_N. [Graphical view]
Pfam	PF00013. KH_1. 3 hits. PF08067. ROKNT. 1 hit. [Graphical view]
SMART	SM00322. KH. 3 hits. [Graphical view]
PROSITE	PS50084. KH_TYPE_1. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	620239.

Entry information

Entry name

HNRPK_RAT

Accession

Primary (citable) accession number: P61980
Secondary accession number(s): Q07244

Q96J62

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents