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P61979 (HNRPK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein K

Short name=hnRNP K
Gene names
Name:Hnrnpk
Synonyms:Hnrpk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity. 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. Ref.7

Subunit structure

Identified in the spliceosome C complex By similarity. Interacts with ANKRD28 and RBM42. 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 ZIK1. Interacts with BRDT. Ref.5 Ref.8

Subcellular location

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

Induction

By DNA damage. This up-regulation is due to protein stabilization. The constitutive protein levels are controlled by MDM2-mediated ubiquitination and degradation via the proteasome pathway. Ref.6

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 processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentCell junction
Cell projection
Cytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
RNA-binding
   Molecular functionActivator
Repressor
Ribonucleoprotein
   PTMAcetylation
Glycoprotein
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype Ref.7. Source: MGI

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell projection

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

podosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from direct assay Ref.7. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61979-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P61979-2)

The sequence of this isoform differs from the canonical sequence as follows:
     459-463: SGKFF → ADVEGF
Isoform 3 (identifier: P61979-3)

The sequence of this isoform differs from the canonical sequence as follows:
     111-134: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Heterogeneous nuclear ribonucleoprotein K
PRO_0000050097

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
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 Ref.9
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

Natural variations

Alternative sequence111 – 13424Missing in isoform 3.
VSP_012581
Alternative sequence459 – 4635SGKFF → ADVEGF in isoform 2.
VSP_010622

Experimental info

Sequence conflict1321C → V in AAA21731. Ref.1
Sequence conflict1361Q → P in AAA21731. Ref.1
Sequence conflict1541S → T in AAA21731. Ref.1
Sequence conflict3341D → S in AAA21731. Ref.1
Sequence conflict3501D → E in AAA21731. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [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

Isoform 2 [UniParc] [UniParc].

Checksum: 0B4EC22FE4534A06
Show »

FASTA46451,028
Isoform 3 [UniParc].

Checksum: 7BCA66B4E39776DB
Show »

FASTA43948,510

References

« Hide 'large scale' references
[1]"Purification, cloning, and expression of a murine phosphoprotein that binds the kappa B motif in vitro identifies it as the homolog of the human heterogeneous nuclear ribonucleoprotein K protein. Description of a novel DNA-dependent phosphorylation process."
Ostrowski J., van Seuningen I., Seger R., Rauch C.T., Sleath P.R., McMullen B.A., Bomsztyk K.
J. Biol. Chem. 269:17626-17634(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
Tissue: Lymphoma.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Spinal ganglion, Testis and Thymus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 149-163 AND 207-219, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[5]"Zik1, a transcriptional repressor that interacts with the heterogeneous nuclear ribonucleoprotein particle K protein."
Denisenko O.N., O'Neill B., Ostrowski J., Van Seuningen I., Bomsztyk K.
J. Biol. Chem. 271:27701-27706(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZIK1.
[6]"hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage."
Moumen A., Masterson P., O'Connor M.J., Jackson S.P.
Cell 123:1065-1078(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response."
Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J., Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D., Regev A., Lander E.S., Jacks T., Rinn J.L.
Cell 142:409-419(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The testis-specific double bromodomain-containing protein BRDT forms a complex with multiple spliceosome components and is required for mRNA splicing and 3'-UTR truncation in round spermatids."
Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.
Nucleic Acids Res. 40:7162-7175(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRDT.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L31961 mRNA. Translation: AAA21731.1.
AK011428 mRNA. Translation: BAB27614.1.
AK051313 mRNA. Translation: BAC34601.1.
AK078777 mRNA. Translation: BAC37389.1.
AK088462 mRNA. Translation: BAC40368.1.
BC006694 mRNA. Translation: AAH06694.1.
RefSeqNP_079555.1. NM_025279.2.
XP_006517164.1. XM_006517101.1.
XP_006517165.1. XM_006517102.1.
XP_006517166.1. XM_006517103.1.
XP_006517167.1. XM_006517104.1.
XP_006517170.1. XM_006517107.1.
UniGeneMm.142872.

3D structure databases

ProteinModelPortalP61979.
SMRP61979. Positions 45-216, 385-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200359. 4 interactions.
IntActP61979. 12 interactions.
MINTMINT-1510077.

PTM databases

PhosphoSiteP61979.

2D gel databases

REPRODUCTION-2DPAGEIPI00223253.
P61979.

Proteomic databases

PaxDbP61979.
PRIDEP61979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043269; ENSMUSP00000039269; ENSMUSG00000021546. [P61979-1]
ENSMUST00000116403; ENSMUSP00000112104; ENSMUSG00000021546. [P61979-2]
ENSMUST00000176207; ENSMUSP00000135354; ENSMUSG00000021546. [P61979-3]
GeneID15387.
KEGGmmu:15387.
UCSCuc007qtw.1. mouse.
uc007qty.1. mouse. [P61979-3]

Organism-specific databases

CTD3190.
MGIMGI:99894. Hnrnpk.

Phylogenomic databases

eggNOGNOG285495.
GeneTreeENSGT00730000110620.
HOVERGENHBG051916.
KOK12886.
OMAKALRTDX.
OrthoDBEOG7CZK81.
TreeFamTF316335.

Gene expression databases

ArrayExpressP61979.
BgeeP61979.
GenevestigatorP61979.

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

NextBio12686.
PROP61979.
SOURCESearch...

Entry information

Entry nameHNRPK_MOUSE
AccessionPrimary (citable) accession number: P61979
Secondary accession number(s): Q07244 expand/collapse secondary AC list , Q15671, Q60577, Q8BGQ8, 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 114 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot