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Reviewed, UniProtKB/Swiss-Prot P61978 (HNRPK_HUMAN)

Last modified September 23, 2008. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 ZIK1 By similarity. Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRNPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Interacts with HCV core protein. Interacts with ANKRD28.

Subcellular location

Cytoplasm. Nucleusnucleoplasm.

Post-translational modification

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

Sequence similarities

Contains 3 KH domains.

Mass spectrometry

Molecular weight is 50976.25 Da from positions 1 - 463 (P61978-1). Determined by MALDI. Ref.10

Binary interactions

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
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 463463Heterogeneous nuclear ribonucleoprotein K

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
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
Modified residue31Phosphothreonine
Modified residue361Phosphoserine
Modified residue1161Phosphoserine
Modified residue2141Phosphoserine
Modified residue2161Phosphoserine
Modified residue2841Phosphoserine
Modified residue2961Omega-N-methylated arginine
Modified residue2991Omega-N-methylated arginine
Modified residue3791Phosphoserine

Natural variations

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

Experimental info

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].

Checksum: 0B4EC22FE4534A06
Show »

46451,028
Isoform 3 [UniParc].

Checksum: C98A78A7462BF776
Show »

44048,562

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.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 149-163, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[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]"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.
[11]"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 SPICEOSOMAL C COMPLEX.
[12]"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.
[13]"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.
[14]"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.
[15]"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: Epithelium.
[16]"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: Epithelium.
[17]"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: Epithelium.
[18]"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: Epithelium.
[19]"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.
[20]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calci