Reviewed, UniProtKB/Swiss-Prot P61978 (HNRPK_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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, 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 ANKRD28. Interacts with HCV core protein. Interacts with ASFV p30 protein.
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.14
Sequence similarities	Contains 3 KH domains.
Mass spectrometry	Molecular mass is 50976.25 Da from positions 1 - 463 (P61978-1). Determined by MALDI. Ref.10

Ontologies

Keywords
Biological process	Host-virus interaction mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome signal transduction Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Traceable author statement. Source: ProtInc heterogeneous nuclear ribonucleoprotein complex Ref.2 Traceable author statement. Source: ProtInc nucleoplasm Ref.1 Traceable author statement. Source: ProtInc spliceosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Ref.2 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HCK	P08631	1	EBI-304185,EBI-346340
QKI	Q96PU8	1	EBI-304185,EBI-945792
TOB1	P50616	1	EBI-304185,EBI-723281

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 463

463

Heterogeneous nuclear ribonucleoprotein K

PRO_0000050096

Regions

Domain

42 – 104

63

KH 1

Repeat

54 – 76

23

1-1

Repeat

59 – 62

4

3-1

Domain

144 – 209

66

KH 2

Repeat

245 – 250

6

2-1

Repeat

257 – 260

4

3-2

Repeat

267 – 270

4

3-3

Repeat

295 – 298

4

3-4

Repeat

324 – 329

6

2-2

Domain

387 – 451

65

KH 3

Repeat

399 – 421

23

1-2

Repeat

404 – 407

4

3-5

Region

35 – 197

163

Interaction with ASFV p30

Region

54 – 421

368

2 X 22 AA approximate repeats

Region

59 – 407

349

5 X 4 AA repeats of G-X-G-G

Region

209 – 337

129

Interaction with ZIK1 By similarity

Region

236 – 273

38

RNA-binding RGG-box

Region

245 – 329

85

2 X 6 AA approximate repeats

Compositional bias

289 – 294

6

Poly-Pro

Compositional bias

310 – 315

6

Poly-Pro

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.7

Modified residue

3

1

Phosphothreonine Ref.15

Modified residue

36

1

Phosphoserine Ref.16

Modified residue

116

1

Phosphoserine Ref.15 Ref.19 Ref.23

Modified residue

214

1

Phosphoserine Ref.18

Modified residue

216

1

Phosphoserine Ref.16 Ref.23 Ref.18 Ref.17 Ref.20 Ref.22

Modified residue

284

1

Phosphoserine Ref.15 Ref.16 Ref.19 Ref.23 Ref.17 Ref.22 Ref.12 Ref.13

Modified residue

296

1

Omega-N-methylated arginine Ref.14

Modified residue

299

1

Omega-N-methylated arginine Ref.14

Modified residue

379

1

Phosphoserine Ref.18 Ref.17

Natural variations

Alternative sequence

111 – 134

24

Missing in isoform 3.

VSP_021669

Alternative sequence

459 – 463

5

SGKFF → ADVEGF in isoform 2 and isoform 3.

VSP_002822

Experimental info

Sequence conflict

32

1

A → D in CAA51267. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

463

Helix Strand Turn

Details...

Beta strand

388 – 395

8

Turn

396 – 398

3

Helix

399 – 402

4

Helix

405 – 407

3

Helix

408 – 417

10

Beta strand

420 – 423

4

Beta strand

430 – 439

10

Helix

441 – 459

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: 0F70EE169B2A064A	FASTA	463	50,976
	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
	Isoform 2 [UniParc] [UniParc]. Checksum: 0B4EC22FE4534A06	FASTA	464	51,028
	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 LQNSVKQYAD VEGF
	Isoform 3. Checksum: C98A78A7462BF776	FASTA	440	48,562
	10 20 30 40 50 60 METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK 70 80 90 100 110 120 GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE YQHYKGSDFD 130 140 150 160 170 180 CELRLLIHQS LAGGIIGVKG AKIKELRENT QTTIKLFQEC CPHSTDRVVL IGGKPDRVVE 190 200 210 220 230 240 CIKIILDLIS ESPIKGRAQP YDPNFYDETY DYGGFTMMFD DRRGRPVGFP MRGRGGFDRM 250 260 270 280 290 300 PPGRGGRPMP PSRRDYDDMS PRRGPPPPPP GRGGRGGSRA RNLPLPPPPP PRGGDLMAYD 310 320 330 340 350 360 RRGRPGDRYD GMVGFSADET WDSAIDTWSP SEWQMAYEPQ GGSGYDYSYA GGRGSYGDLG 370 380 390 400 410 420 GPIITTQVTI PKDLAGSIIG KGGQRIKQIR HESGASIKID EPLEGSEDRI ITITGTQDQI 430 440 QNAQYLLQNS VKQYADVEGF

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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 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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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

EMBLGenBankDDBJ

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.

IPI

IPI00216049.
IPI00216746.
IPI00807545.

PIR

S43363.

RefSeq

NP_002131.2.
NP_112552.1.
NP_112553.1.

UniGene

Hs.522257

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P61978. 28 interactions.

PTM databases

PhosphoSite

P61978.

2-D gel databases

SWISS-2DPAGE

P61978.

Proteomic databases

PRIDE

P61978.

Genome annotation databases

Ensembl

ENSG00000165119. Homo sapiens. [Contig view]

GeneID

3190.

KEGG

hsa:3190.

Organism-specific databases

GeneCards

GC09M085775.

H-InvDB

HIX0008131.

HGNC

HGNC:5044. HNRNPK.

HPA

CAB004435.
CAB016225.
HPA007644.

MIM

600712. gene.

PharmGKB

PA29368.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P61978.

OMA

P61978. XGLQLPS.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P61978.

Bgee

P61978.

CleanEx

HS_HNRNPK.

GermOnline

ENSG00000165119. Homo sapiens.

Family and domain databases

InterPro

IPR004087. KH.
IPR004088. KH_type_1.
IPR018111. KH_type_1_subgr.
IPR012987. ROK_N.
[Graphical view]

Pfam

PF00013. KH_1. 3 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]

SMART

SM00322. KH. 3 hits.
[Graphical view]

PROSITE

PS50084. KH_TYPE_1. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

12686.

PMAP-CutDB

P61978.

SOURCE

Search...

Entry information

Entry name

HNRPK_HUMAN

Accession

Primary (citable) accession number: P61978
Secondary accession number(s): Q07244 , Q15671, Q59F98, Q5T6W4, Q60577, Q922Y7, Q96J62

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)