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P61978 (HNRPK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Alternative name(s):
Transformation up-regulated nuclear protein
Short name=TUNP
Gene names
Name:HNRNPK
Synonyms:HNRPK
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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.

Subunit structure

Interacts with RBM42 and ZIK1 By similarity. Identified in the spliceosome C complex. Interacts with ANKRD28. Interacts with HCV core protein. Interacts with ASFV p30 protein. Interacts with DDX1. Ref.9 Ref.10 Ref.14 Ref.22

Subcellular location

Cytoplasm. Nucleus › nucleoplasm. Note: In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear. Ref.1

Post-translational modification

Arg-296 and Arg-299 are dimethylated, probably to asymmetric dimethylarginine. Ref.15

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
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
RNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processinterspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear 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. Source: BHF-UCL

positive regulation of receptor-mediated endocytosis

Inferred from mutant phenotype. Source: BHF-UCL

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

Inferred from mutant phenotype. Source: BHF-UCL

regulation of low-density lipoprotein particle clearance

Inferred from mutant phenotype. Source: BHF-UCL

signal transduction

Traceable author statement. Source: ProtInc

   Cellular componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Traceable author statement. Source: ProtInc

heterogeneous nuclear ribonucleoprotein complex

Traceable author statement. Source: ProtInc

nuclear chromatin

Inferred from direct assay. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular functionRNA binding

Traceable author statement. Source: ProtInc

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

Inferred from mutant phenotype. 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. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.10. Source: UniProtKB

single-stranded DNA binding

Traceable author statement. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

QKIQ96PU83EBI-304185,EBI-945792
TP63Q9H3D42EBI-304185,EBI-2337775

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.27
Modified residue31Phosphothreonine Ref.16
Modified residue361Phosphoserine Ref.17
Modified residue1161Phosphoserine Ref.16 Ref.20 Ref.25
Modified residue2141Phosphoserine Ref.19
Modified residue2161Phosphoserine Ref.17 Ref.18 Ref.19 Ref.21 Ref.24 Ref.25 Ref.27 Ref.28
Modified residue2841Phosphoserine Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.25 Ref.27
Modified residue2961Omega-N-methylated arginine Ref.15
Modified residue2991Omega-N-methylated arginine Ref.15
Modified residue3791Phosphoserine Ref.18 Ref.19
Modified residue3801Phosphotyrosine Ref.28
Cross-link422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.26

Natural variations

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

Experimental info

Sequence conflict321A → D in CAA51267. Ref.2

Secondary structure

1 .............. 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: 1729596] [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: 8107114] [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: 15164053] [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: 15489334] [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, 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, 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: 9651361] [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: 12183465] [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: 11840567] [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: 11991638] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[13]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma.
[14]"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: 16564677] [Abstract]
Cited for: INTERACTION WITH ANKRD28, PHOSPHORYLATION AT SER-284.
[15]"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
Ong S.E., Mittler G., Mann M.
Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract]
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-296 AND ARG-299, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[16]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-116 AND SER-284, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-216 AND SER-284, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[18]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-284 AND SER-379, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[19]"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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-216 AND SER-379, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[20]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-284, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[21]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[22]"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: 18775702] [Abstract]
Cited for: INTERACTION WITH ASFV PROTEIN P30.
[23]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, MASS SPECTROMETRY.
Tissue: T-cell.
[24]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-284, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[25]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-216 AND SER-284, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[26]"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells."
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.
Proteomics 8:2885-2896(2008) [PubMed: 18655026] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[27]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-284, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[28]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND TYR-380, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[29]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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: 10369774] [Abstract]
Cited for: STRUCTURE BY NMR OF 375-463.
[31]"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: 12093748] [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.
IPIIPI00216049.
IPI00216746.
IPI00807545.
PIRS43363.
RefSeqNP_002131.2. NM_002140.3.
NP_112552.1. NM_031262.2.
NP_112553.1. NM_031263.2.
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 40-215, 385-463.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31805N.
IntActP61978. 43 interactions.
MINTMINT-225422.
STRINGP61978.

PTM databases

PhosphoSiteP61978.

Polymorphism databases

DMDM48429103.

2D gel databases

SWISS-2DPAGEP61978.

Proteomic databases

PRIDEP61978.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351839; ENSP00000317788; ENSG00000165119.
ENST00000360384; ENSP00000353552; ENSG00000165119.
ENST00000376264; ENSP00000365440; ENSG00000165119.
GeneID3190.
KEGGhsa:3190.
UCSCuc004ang.2. human.
uc004anh.2. human.

Organism-specific databases

CTD3190.
GeneCardsGC09M086582.
H-InvDBHIX0008131.
HIX0200444.
HGNCHGNC:5044. HNRNPK.
HPACAB004435.
CAB016225.
HPA007644.
MIM600712. gene.
neXtProtNX_P61978.
PharmGKBPA162391350.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07231.
GeneTreeENSGT00550000074311.
HOVERGENHBG051916.
OMAXGLQLPS.
OrthoDBEOG49KFRD.
PhylomeDBP61978.

Enzyme and pathway databases

ReactomeREACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP61978.
BgeeP61978.
CleanExHS_HNRNPK.
GenevestigatorP61978.
GermOnlineENSG00000165119. Homo sapiens.

Family and domain databases

InterProIPR004087. KH.
IPR004088. KH_type_1.
IPR018111. KH_type_1_subgr.
IPR012987. ROK_N.
[Graphical view]
KOK12886.
PfamPF00013. KH_1. 3 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]
SMARTSM00322. KH. 3 hits.
[Graphical view]
PROSITEPS50084. KH_TYPE_1. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio12686.
PMAP-CutDBP61978.
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: January 25, 2012
This is version 113 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

Recent format changes

Overview of recent format changes

Human chromosome 9

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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