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P61978

- HNRPK_HUMAN

UniProt

P61978 - HNRPK_HUMAN

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Protein

Heterogeneous nuclear ribonucleoprotein K

Gene
HNRNPK, HNRPK
Organism
Homo sapiens (Human)
Status
Reviewed - 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 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.3 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. RNA binding Source: ProtInc
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  6. single-stranded DNA binding Source: BHF-UCL

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. positive regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
  4. positive regulation of receptor-mediated endocytosis Source: BHF-UCL
  5. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  6. regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  7. regulation of low-density lipoprotein particle clearance Source: BHF-UCL
  8. RNA processing Source: ProtInc
  9. RNA splicing Source: Reactome
  10. signal transduction Source: ProtInc
  11. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

Host-virus interaction, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein K
Short name:
hnRNP K
Alternative name(s):
Transformation up-regulated nuclear protein
Short name:
TUNP
Gene namesi
Name:HNRNPK
Synonyms:HNRPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:5044. HNRNPK.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. cell projection Source: UniProtKB-KW
  4. cytoplasm Source: ProtInc
  5. extracellular vesicular exosome Source: UniProt
  6. nuclear chromatin Source: BHF-UCL
  7. nucleoplasm Source: Reactome
  8. nucleus Source: HPA
  9. podosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi422 – 4221K → R: Loss of sumoylation. Loss of TP53 transcriptional stimulation. 1 Publication
Mutagenesisi424 – 4241D → A: Loss of sumoylation. 1 Publication

Organism-specific databases

PharmGKBiPA162391350.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Heterogeneous nuclear ribonucleoprotein KPRO_0000050096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei116 – 1161Phosphoserine1 Publication
Modified residuei198 – 1981N6-acetyllysine By similarity
Modified residuei214 – 2141Phosphoserine1 Publication
Modified residuei216 – 2161Phosphoserine5 Publications
Modified residuei284 – 2841Phosphoserine5 Publications
Modified residuei379 – 3791Phosphoserine3 Publications
Modified residuei380 – 3801Phosphotyrosine1 Publication
Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

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.1 Publication
Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination.2 Publications
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP61978.
PaxDbiP61978.
PRIDEiP61978.

2D gel databases

SWISS-2DPAGEP61978.

PTM databases

PhosphoSiteiP61978.

Miscellaneous databases

PMAP-CutDBP61978.

Expressioni

Inductioni

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.1 Publication

Gene expression databases

ArrayExpressiP61978.
BgeeiP61978.
CleanExiHS_HNRNPK.
GenevestigatoriP61978.

Organism-specific databases

HPAiCAB004435.
CAB016225.
HPA007644.
HPA044105.

Interactioni

Subunit structurei

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/TP53.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P298469EBI-304185,EBI-8847394From a different organism.
AURKAO149652EBI-304185,EBI-448680
C'204LQ8V1E75EBI-304185,EBI-8068745From a different organism.
MDM2Q009872EBI-304185,EBI-389668
PRMT1Q998733EBI-304185,EBI-78738
QKIQ96PU83EBI-304185,EBI-945792
RBMXP381593EBI-304185,EBI-743526
SRCP129316EBI-304185,EBI-621482
TP53P046372EBI-304185,EBI-366083
TP63Q9H3D42EBI-304185,EBI-2337775

Protein-protein interaction databases

BioGridi109431. 198 interactions.
DIPiDIP-31805N.
IntActiP61978. 99 interactions.
MINTiMINT-225422.
STRINGi9606.ENSP00000365439.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi381 – 3844
Beta strandi388 – 3958
Turni396 – 3983
Helixi399 – 4024
Helixi405 – 4073
Helixi408 – 41710
Beta strandi420 – 4234
Beta strandi430 – 43910
Helixi441 – 45919

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J5KNMR-A379-463[»]
1KHMNMR-A379-463[»]
1ZZIX-ray1.80A/B385-463[»]
1ZZJX-ray2.30A/B/C385-463[»]
1ZZKX-ray0.95A385-463[»]
ProteinModelPortaliP61978.
SMRiP61978. Positions 45-216, 385-463.

Miscellaneous databases

EvolutionaryTraceiP61978.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 276276Necessary for interaction with DDX1Add
BLAST
Regioni35 – 197163Interaction with ASFV p30Add
BLAST
Regioni54 – 4213682 X 22 AA approximate repeatsAdd
BLAST
Regioni59 – 4073495 X 4 AA repeats of G-X-G-GAdd
BLAST
Regioni209 – 337129Interaction with ZIK1 By 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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG285495.
HOVERGENiHBG051916.
KOiK12886.
OMAiKALRTDX.
OrthoDBiEOG7CZK81.
PhylomeDBiP61978.
TreeFamiTF316335.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61978-1) [UniParc]FASTAAdd to Basket

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.

« Hide

METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ    50
SKNAGAVIGK GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI 100
LKKIIPTLEE GLQLPSPTAT SQLPLESDAV ECLNYQHYKG SDFDCELRLL 150
IHQSLAGGII GVKGAKIKEL RENTQTTIKL FQECCPHSTD RVVLIGGKPD 200
RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT MMFDDRRGRP 250
VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG 300
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID 350
TWSPSEWQMA YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG 400
SIIGKGGQRI KQIRHESGAS IKIDEPLEGS EDRIITITGT QDQIQNAQYL 450
LQNSVKQYSG KFF 463
Length:463
Mass (Da):50,976
Last modified:June 7, 2004 - v1
Checksum:i0F70EE169B2A064A
GO
Isoform 2 (identifier: P61978-2) [UniParc] [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     459-463: SGKFF → ADVEGF

Show »
Length:464
Mass (Da):51,028
Checksum:i0B4EC22FE4534A06
GO
Isoform 3 (identifier: P61978-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-134: Missing.
     459-463: SGKFF → ADVEGF

Note: No experimental confirmation available.

Show »
Length:440
Mass (Da):48,562
Checksum:iC98A78A7462BF776
GO

Sequence cautioni

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

Mass spectrometryi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei111 – 13424Missing in isoform 3. VSP_021669Add
BLAST
Alternative sequencei459 – 4635SGKFF → ADVEGF in isoform 2 and isoform 3. VSP_002822

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321A → D in CAA51267. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6667.1.
CCDS6668.1. [P61978-2]
PIRiS43363.
RefSeqiNP_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]
UniGeneiHs.522257.

Genome annotation databases

EnsembliENST00000351839; ENSP00000317788; ENSG00000165119. [P61978-1]
ENST00000360384; ENSP00000353552; ENSG00000165119. [P61978-1]
ENST00000376263; ENSP00000365439; ENSG00000165119. [P61978-2]
ENST00000376264; ENSP00000365440; ENSG00000165119. [P61978-1]
ENST00000376281; ENSP00000365458; ENSG00000165119. [P61978-2]
GeneIDi3190.
KEGGihsa:3190.
UCSCiuc004ang.4. human.
uc004anh.4. human. [P61978-3]

Polymorphism databases

DMDMi48429103.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6667.1.
CCDS6668.1. [P61978-2 ]
PIRi S43363.
RefSeqi NP_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 ]
UniGenei Hs.522257.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J5K NMR - A 379-463 [» ]
1KHM NMR - A 379-463 [» ]
1ZZI X-ray 1.80 A/B 385-463 [» ]
1ZZJ X-ray 2.30 A/B/C 385-463 [» ]
1ZZK X-ray 0.95 A 385-463 [» ]
ProteinModelPortali P61978.
SMRi P61978. Positions 45-216, 385-463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109431. 198 interactions.
DIPi DIP-31805N.
IntActi P61978. 99 interactions.
MINTi MINT-225422.
STRINGi 9606.ENSP00000365439.

PTM databases

PhosphoSitei P61978.

Polymorphism databases

DMDMi 48429103.

2D gel databases

SWISS-2DPAGE P61978.

Proteomic databases

MaxQBi P61978.
PaxDbi P61978.
PRIDEi P61978.

Protocols and materials databases

DNASUi 3190.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000351839 ; ENSP00000317788 ; ENSG00000165119 . [P61978-1 ]
ENST00000360384 ; ENSP00000353552 ; ENSG00000165119 . [P61978-1 ]
ENST00000376263 ; ENSP00000365439 ; ENSG00000165119 . [P61978-2 ]
ENST00000376264 ; ENSP00000365440 ; ENSG00000165119 . [P61978-1 ]
ENST00000376281 ; ENSP00000365458 ; ENSG00000165119 . [P61978-2 ]
GeneIDi 3190.
KEGGi hsa:3190.
UCSCi uc004ang.4. human.
uc004anh.4. human. [P61978-3 ]

Organism-specific databases

CTDi 3190.
GeneCardsi GC09M086582.
HGNCi HGNC:5044. HNRNPK.
HPAi CAB004435.
CAB016225.
HPA007644.
HPA044105.
MIMi 600712. gene.
neXtProti NX_P61978.
PharmGKBi PA162391350.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285495.
HOVERGENi HBG051916.
KOi K12886.
OMAi KALRTDX.
OrthoDBi EOG7CZK81.
PhylomeDBi P61978.
TreeFami TF316335.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi HNRNPK. human.
EvolutionaryTracei P61978.
GeneWikii HNRPK.
GenomeRNAii 3190.
NextBioi 12686.
PMAP-CutDB P61978.
PROi P61978.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61978.
Bgeei P61978.
CleanExi HS_HNRNPK.
Genevestigatori P61978.

Family and domain databases

Gene3Di 3.30.1370.10. 3 hits.
InterProi IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012987. ROK_N.
[Graphical view ]
Pfami PF00013. KH_1. 3 hits.
PF08067. ROKNT. 1 hit.
[Graphical view ]
SMARTi SM00322. KH. 3 hits.
[Graphical view ]
SUPFAMi SSF54791. SSF54791. 3 hits.
PROSITEi PS50084. KH_TYPE_1. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiHNRPK_HUMAN
AccessioniPrimary (citable) accession number: P61978
Secondary accession number(s): Q07244
, Q15671, Q59F98, Q5T6W4, Q60577, Q922Y7, Q96J62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: September 3, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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