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P61978 (HNRPK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein K

Short name=hnRNP K
Alternative name(s):
Transformation up-regulated nuclear protein
Short name=TUNP
Gene names
Name:HNRNPK
Synonyms:HNRPK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.13 Ref.23 Ref.29

Subunit structure

Interacts with RBM42 and ZIK1. Interacts with BRDT By similarity. Identified in the spliceosome C complex. Interacts with ANKRD28. Interacts with HCV core protein. Interacts with ASFV p30 protein. Interacts with DDX1. Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation. Interacts with p53/TP53. Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.18

Subcellular location

Cytoplasm. Nucleusnucleoplasm. Cell projectionpodosome. Note: Recruited to p53/TP53-responsive promoters, in the presence of functional p53/TP53. In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear. Ref.1 Ref.13 Ref.28

Induction

By DNA damage, including ionizing radiations and phleomycin treatment or UV irradiation. This induction requires ATM kinase activity (ionizing radiations and phleomycin) or ATR activity (UV irradiation). Up-regulation is due to protein stabilization. Constitutive protein levels are controlled by MDM2-mediated ubiquitination and degradation via the proteasome pathway. Ref.13

Post-translational modification

Arg-296 and Arg-299 are dimethylated, probably to asymmetric dimethylarginine.

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. Ref.29

Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination. Ref.13 Ref.29

O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. Ref.27

Sequence similarities

Contains 3 KH domains.

Mass spectrometry

Isoform 1: Molecular mass is 50976.25 Da from positions 1 - 463. Determined by MALDI. Ref.11

Sequence caution

The sequence BAD92799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA 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
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Traceable author statement Ref.2. Source: ProtInc

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.12. Source: UniProtKB

positive regulation of low-density lipoprotein particle receptor biosynthetic process

Inferred from mutant phenotype PubMed 20371611. Source: BHF-UCL

positive regulation of receptor-mediated endocytosis

Inferred from mutant phenotype PubMed 20371611. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20371611. Source: BHF-UCL

regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20371611. Source: BHF-UCL

regulation of low-density lipoprotein particle clearance

Inferred from mutant phenotype PubMed 20371611. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 16130169. Source: ProtInc

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.12. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell projection

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Traceable author statement PubMed 16130169. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nuclear chromatin

Inferred from direct assay PubMed 20371611. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

podosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Traceable author statement Ref.2. Source: ProtInc

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from mutant phenotype PubMed 20371611. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from mutant phenotype PubMed 20371611. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21821029. Source: IntAct

single-stranded DNA binding

Traceable author statement PubMed 20371611. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61978-1)

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: P61978-2)

The sequence of this isoform differs from the canonical sequence as follows:
     459-463: SGKFF → ADVEGF
Isoform 3 (identifier: P61978-3)

The sequence of this isoform differs from the canonical sequence as follows:
     111-134: Missing.
     459-463: SGKFF → ADVEGF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Heterogeneous nuclear ribonucleoprotein K
PRO_0000050096

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
Region35 – 197163Interaction with ASFV p30
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 Ref.7 Ref.21 Ref.30
Modified residue1161Phosphoserine Ref.20
Modified residue1981N6-acetyllysine By similarity
Modified residue2141Phosphoserine Ref.26
Modified residue2161Phosphoserine Ref.16 Ref.20 Ref.22 Ref.24 Ref.26
Modified residue2841Phosphoserine Ref.14 Ref.15 Ref.20 Ref.24 Ref.26
Modified residue3791Phosphoserine Ref.16 Ref.24 Ref.26
Modified residue3801Phosphotyrosine Ref.22
Cross-link422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.29

Natural variations

Alternative sequence111 – 13424Missing in isoform 3.
VSP_021669
Alternative sequence459 – 4635SGKFF → ADVEGF in isoform 2 and isoform 3.
VSP_002822

Experimental info

Mutagenesis4221K → R: Loss of sumoylation. Loss of TP53 transcriptional stimulation. Ref.29
Mutagenesis4241D → A: Loss of sumoylation. Ref.29
Sequence conflict321A → D in CAA51267. Ref.2

Secondary structure

................ 463
Helix Strand Turn

Details...

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: C98A78A7462BF776
Show »

FASTA44048,562

References

« Hide 'large scale' references
[1]"Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein."
Matunis M.J., Michael W.M., Dreyfuss G.
Mol. Cell. Biol. 12:164-171(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]"Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing."
Dejgaard K., Leffers H., Rasmussen H.H., Madsen P., Kruse T.A., Gesser B., Nielsen H., Celis J.E.
J. Mol. Biol. 236:33-48(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Muscle.
[7]Bienvenut W.V., Vousden K.H., Lukashchuk N.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-52; 70-103; 149-163; 192-201; 208-219; 317-325; 378-405 AND 423-456, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[8]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 38-46; 149-163; 208-219; 306-316 AND 378-396, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K."
Hsieh T.-Y., Matsumoto M., Chou H.-C., Schneider R., Hwang S.B., Lee A.S., Lai M.M.C.
J. Biol. Chem. 273:17651-17659(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN.
[10]"An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein K."
Chen H.C., Lin W.C., Tsay Y.G., Lee S.C., Chang C.J.
J. Biol. Chem. 277:40403-40409(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX1.
[11]"Cluster analysis of an extensive human breast cancer cell line protein expression map database."
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Tissue: Mammary cancer.
[12]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[13]"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: FUNCTION, INTERACTION WITH MDM2 AND TP53, SUBCELLULAR LOCATION, UBIQUITINATION, INDUCTION.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K."
Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.
Cell. Signal. 18:1769-1778(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKRD28, PHOSPHORYLATION AT SER-284.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"African swine fever virus protein p30 interaction with heterogeneous nuclear ribonucleoprotein K (hnRNP-K) during infection."
Hernaez B., Escribano J.M., Alonso C.
FEBS Lett. 582:3275-3280(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASFV PROTEIN P30.
[19]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-216 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND TYR-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"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.
[24]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-284 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-216; SER-284 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition."
Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.
Biochim. Biophys. Acta 1820:1839-1848(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[28]"Proteomic analysis of podosome fractions from macrophages reveals similarities to spreading initiation centres."
Cervero P., Himmel M., Kruger M., Linder S.
Eur. J. Cell Biol. 91:908-922(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[29]"DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation."
Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.
J. Biol. Chem. 287:30789-30799(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUMOYLATION AT LYS-422, UBIQUITINATION, MUTAGENESIS OF LYS-422 AND ASP-424.
[30]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor."
Baber J.L., Libutti D., Levens D., Tjandra N.
J. Mol. Biol. 289:949-962(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 375-463.
[32]"Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA."
Braddock D.T., Baber J.L., Levens D., Clore G.M.
EMBO J. 21:3476-3485(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 379-463 IN COMPLEX WITH SINGLE-STRANDED DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S74678 mRNA. Translation: AAB20770.1.
X72727 mRNA. Translation: CAA51267.1.
AB209562 mRNA. Translation: BAD92799.1. Different initiation.
AL354733 Genomic DNA. Translation: CAI16020.1.
CH471089 Genomic DNA. Translation: EAW62675.1.
BC000355 mRNA. Translation: AAH00355.1.
BC014980 mRNA. Translation: AAH14980.1.
CCDSCCDS6667.1.
CCDS6668.1. [P61978-2]
PIRS43363.
RefSeqNP_002131.2. NM_002140.3. [P61978-2]
NP_112552.1. NM_031262.2. [P61978-1]
NP_112553.1. NM_031263.2. [P61978-2]
XP_005252017.1. XM_005251960.1. [P61978-2]
XP_005252018.1. XM_005251961.1. [P61978-1]
XP_005252020.1. XM_005251963.2. [P61978-3]
XP_005252021.1. XM_005251964.1. [P61978-3]
XP_005252022.1. XM_005251965.1. [P61978-3]
UniGeneHs.522257.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J5KNMR-A379-463[»]
1KHMNMR-A379-463[»]
1ZZIX-ray1.80A/B385-463[»]
1ZZJX-ray2.30A/B/C385-463[»]
1ZZKX-ray0.95A385-463[»]
ProteinModelPortalP61978.
SMRP61978. Positions 45-216, 385-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109431. 205 interactions.
DIPDIP-31805N.
IntActP61978. 99 interactions.
MINTMINT-225422.
STRING9606.ENSP00000365439.

PTM databases

PhosphoSiteP61978.

Polymorphism databases

DMDM48429103.

2D gel databases

SWISS-2DPAGEP61978.

Proteomic databases

MaxQBP61978.
PaxDbP61978.
PRIDEP61978.

Protocols and materials databases

DNASU3190.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351839; ENSP00000317788; ENSG00000165119. [P61978-1]
ENST00000360384; ENSP00000353552; ENSG00000165119. [P61978-1]
ENST00000376263; ENSP00000365439; ENSG00000165119. [P61978-2]
ENST00000376264; ENSP00000365440; ENSG00000165119. [P61978-1]
ENST00000376281; ENSP00000365458; ENSG00000165119. [P61978-2]
GeneID3190.
KEGGhsa:3190.
UCSCuc004ang.4. human.
uc004anh.4. human. [P61978-3]

Organism-specific databases

CTD3190.
GeneCardsGC09M086582.
HGNCHGNC:5044. HNRNPK.
HPACAB004435.
CAB016225.
HPA007644.
HPA044105.
MIM600712. gene.
neXtProtNX_P61978.
PharmGKBPA162391350.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285495.
HOVERGENHBG051916.
KOK12886.
OMAKALRTDX.
OrthoDBEOG7CZK81.
PhylomeDBP61978.
TreeFamTF316335.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP61978.
BgeeP61978.
CleanExHS_HNRNPK.
GenevestigatorP61978.

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

ChiTaRSHNRNPK. human.
EvolutionaryTraceP61978.
GeneWikiHNRPK.
GenomeRNAi3190.
NextBio12686.
PMAP-CutDBP61978.
PROP61978.
SOURCESearch...

Entry information

Entry nameHNRPK_HUMAN
AccessionPrimary (citable) accession number: P61978
Secondary accession number(s): Q07244 expand/collapse secondary AC list , Q15671, Q59F98, Q5T6W4, Q60577, Q922Y7, Q96J62
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM