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Q96J92 (WNK4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
Serine/threonine-protein kinase WNK4

EC=2.7.11.1
Alternative name(s):
Protein kinase lysine-deficient 4
Protein kinase with no lysine 4
Gene names
Name:WNK4
Synonyms:PRKWNK4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1243 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D, SGK1, TRPV5 and TRPV6. Regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation which appears to prevent membrane trafficking of SLC12A3. Also inhibits the renal K+ channel, KCNJ1, via a kinase-independent mechanism by which it induces clearance of the protein from the cell surface by clathrin-dependent endocytosis. WNK4 appears to act as a molecular switch that can vary the balance between NaCl reabsorption and K+ secretion to maintain integrated homeostasis. Phosphorylates NEDD4L. Ref.5

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity. UniProtKB Q9H4A3

Enzyme regulation

Activation requires autophosphorylation of Ser-335. Phosphorylation of Ser-331 also promotes increased activity By similarity. UniProtKB Q9JIH7

Subunit structure

Interacts with the C-terminal region of KCNJ1 By similarity. Interacts with WNK1 and WNK3 By similarity. Interacts with KLHL3. Ref.6 Ref.7 Ref.8 Ref.9 UniProtKB Q80UE6

Subcellular location

Cell junctiontight junction By similarity. Note: Present exclusively in intercellular junctions in the distal convoluted tubule and in both the cytoplasm and intercellular junctions in the cortical collecting duct. WNK4 is part of the tight junction complex By similarity.

Tissue specificity

Expressed in kidney, colon and skin. Ref.4

Post-translational modification

Phosphorylated by WNK1 and WNK3 By similarity.

Ubiquitinated by the BCR(KLHL3) complex, leading to its degradation and increased expression of KCNJ1 at the cell surface. Ref.7 Ref.9

Involvement in disease

Pseudohypoaldosteronism 2B (PHA2B) [MIM:614491]: An autosomal dominant disorder characterized by hypertension, hyperkalemia, hyperchloremia, mild hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.6 Ref.7 Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WNK subfamily.

Contains 1 protein kinase domain.

Caution

Cys-203 is present instead of the conserved Lys which is expected to be an active site residue. Lys-186 appears to fulfill the required catalytic function. UniProtKB Q9JIH7

Sequence caution

The sequence BAC04669.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAC48387.1 differs from that shown. Reason: Frameshift at position 4.

Ontologies

Keywords
   Cellular componentCell junction
Tight junction
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchloride transport

Inferred from electronic annotation. Source: Ensembl

distal tubule morphogenesis

Inferred from mutant phenotype Ref.7Ref.9. Source: UniProtKB

intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

ion homeostasis

Inferred from mutant phenotype Ref.7Ref.9. Source: UniProtKB

ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of pancreatic juice secretion

Inferred from electronic annotation. Source: Ensembl

protein localization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cellular process

Inferred from sequence or structural similarity. Source: UniProtKB

renal sodium ion absorption

Inferred from mutant phenotype Ref.7Ref.9. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

tight junction

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

chloride channel inhibitor activity

Inferred from direct assay PubMed 17673510. Source: UniProt

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OXSR1O9574711EBI-766352,EBI-620853

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q96J92-1)

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: Q96J92-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-228: Missing.
     229-264: QHPNIVRFYDSWKSVLRGQVCIVLVTELMTSGTLKT → MRRRQQGAAGGNFPVGGSFPEDVSPHQDSGYAPSPR
     828-1210: Missing.
     1233-1243: GVTFAGDVGRM → EAGQRPGKLWLRATVQLRVWGLELRRKEMMGRNPKLGAAPNP
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96J92-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1145-1165: HLSEVETLQTLQKKEIEDLYS → PFHALRASSGTCQRWKHYRHY
     1166-1243: Missing.
Note: No experimental confirmation available. Incomplete sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12431243Serine/threonine-protein kinase WNK4
PRO_0000086824

Regions

Domain174 – 432259Protein kinase
Nucleotide binding180 – 1889ATP By similarity UniProtKB Q8TDX7

Sites

Active site3021Proton acceptor By similarity UniProtKB Q8TDX7
Binding site1861ATP By similarity UniProtKB Q9JIH7

Amino acid modifications

Modified residue3311Phosphoserine; by autocatalysis By similarity UniProtKB Q9JIH7
Modified residue3351Phosphoserine; by autocatalysis By similarity UniProtKB Q9JIH7
Cross-link157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link450Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link454Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link1010Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link1144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link1157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link1158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Alternative sequence1 – 228228Missing in isoform 2.
VSP_050648
Alternative sequence229 – 26436QHPNI…GTLKT → MRRRQQGAAGGNFPVGGSFP EDVSPHQDSGYAPSPR in isoform 2.
VSP_050649
Alternative sequence828 – 1210383Missing in isoform 2.
VSP_050650
Alternative sequence1145 – 116521HLSEV…EDLYS → PFHALRASSGTCQRWKHYRH Y in isoform 3.
VSP_050652
Alternative sequence1166 – 124378Missing in isoform 3.
VSP_050653
Alternative sequence1233 – 124311GVTFAGDVGRM → EAGQRPGKLWLRATVQLRVW GLELRRKEMMGRNPKLGAAP NP in isoform 2.
VSP_050651
Natural variant4341E → D in an ovarian mucinous carcinoma sample; somatic mutation. Ref.10
VAR_041330
Natural variant5621E → K in PHA2B; impaired interaction with KLHL3. Ref.1 Ref.6 Ref.9
VAR_017588
Natural variant5641D → A in PHA2B; impaired interaction with KLHL3. Ref.1 Ref.7
VAR_017589
Natural variant5651Q → E in PHA2B; impaired interaction with KLHL3. Ref.1 Ref.6 Ref.9
VAR_017590
Natural variant6011A → S.
Corresponds to variant rs55781437 [ dbSNP | Ensembl ].
VAR_061748
Natural variant6771R → W.
Corresponds to variant rs9896991 [ dbSNP | Ensembl ].
VAR_051685
Natural variant8131P → L. Ref.10
VAR_041331
Natural variant9611P → S.
Corresponds to variant rs2290041 [ dbSNP | Ensembl ].
VAR_051686
Natural variant9921P → S in a metastatic melanoma sample; somatic mutation. Ref.10
VAR_041332
Natural variant10131L → P. Ref.10
VAR_041333
Natural variant11851R → C in PHA2B. Ref.1
VAR_017591

Experimental info

Sequence conflict5251R → C in BAC04688. Ref.3

Secondary structure

... 1243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BAC35F0098BA3391

FASTA1,243134,739
        10         20         30         40         50         60 
MLASPATETT VLMSQTEADL ALRPPPPLGT AGQPRLGPPP RRARRFSGKA EPRPRSSRLS 

        70         80         90        100        110        120 
RRSSVDLGLL SSWSLPASPA PDPPDPPDSA GPGPARSPPP SSKEPPEGTW TEGAPVKAAE 

       130        140        150        160        170        180 
DSARPELPDS AVGPGSREPL RVPEAVALER RREQEEKEDM ETQAVATSPD GRYLKFDIEI 

       190        200        210        220        230        240 
GRGSFKTVYR GLDTDTTVEV AWCELQTRKL SRAERQRFSE EVEMLKGLQH PNIVRFYDSW 

       250        260        270        280        290        300 
KSVLRGQVCI VLVTELMTSG TLKTYLRRFR EMKPRVLQRW SRQILRGLHF LHSRVPPILH 

       310        320        330        340        350        360 
RDLKCDNVFI TGPTGSVKIG DLGLATLKRA SFAKSVIGTP EFMAPEMYEE KYDEAVDVYA 

       370        380        390        400        410        420 
FGMCMLEMAT SEYPYSECQN AAQIYRKVTS GRKPNSFHKV KIPEVKEIIE GCIRTDKNER 

       430        440        450        460        470        480 
FTIQDLLAHA FFREERGVHV ELAEEDDGEK PGLKLWLRME DARRGGRPRD NQAIEFLFQL 

       490        500        510        520        530        540 
GRDAAEEVAQ EMVALGLVCE ADYQPVARAV RERVAAIQRK REKLRKAREL EALPPEPGPP 

       550        560        570        580        590        600 
PATVPMAPGP PSVFPPEPEE PEADQHQPFL FRHASYSSTT SDCETDGYLS SSGFLDASDP 

       610        620        630        640        650        660 
ALQPPGGVPS SLAESHLCLP SAFALSIPRS GPGSDFSPGD SYASDAASGL SDVGEGMGQM 

       670        680        690        700        710        720 
RRPPGRNLRR RPRSRLRVTS VSDQNDRVVE CQLQTHNSKM VTFRFDLDGD SPEEIAAAMV 

       730        740        750        760        770        780 
YNEFILPSER DGFLRRIREI IQRVETLLKR DTGPMEAAED TLSPQEEPAP LPALPVPLPD 

       790        800        810        820        830        840 
PSNEELQSST SLEHRSWTAF STSSSSPGTP LSPGNPFSPG TPISPGPIFP ITSPPCHPSP 

       850        860        870        880        890        900 
SPFSPISSQV SSNPSPHPTS SPLPFSSSTP EFPVPLSQCP WSSLPTTSPP TFSPTCSQVT 

       910        920        930        940        950        960 
LSSPFFPPCP STSSFPSTTA APLLSLASAF SLAVMTVAQS LLSPSPGLLS QSPPAPPSPL 

       970        980        990       1000       1010       1020 
PSLPLPPPVA PGGQESPSPH TAEVESEASP PPARPLPGEA RLAPISEEGK PQLVGRFQVT 

      1030       1040       1050       1060       1070       1080 
SSKEPAEPLP LQPTSPTLSG SPKPSTPQLT SESSDTEDSA GGGPETREAL AESDRAAEGL 

      1090       1100       1110       1120       1130       1140 
GAGVEEEGDD GKEPQVGGSP QPLSHPSPVW MNYSYSSLCL SSEESESSGE DEEFWAELQS 

      1150       1160       1170       1180       1190       1200 
LRQKHLSEVE TLQTLQKKEI EDLYSRLGKQ PPPGIVAPAA MLSSRQRRLS KGSFPTSRRN 

      1210       1220       1230       1240 
SLQRSEPPGP GIMRRNSLSG SSTGSQEQRA SKGVTFAGDV GRM 

« Hide

Isoform 2 [UniParc].

Checksum: 6711A9D6CEFD8146
Show »

FASTA66373,370
Isoform 3 [UniParc].

Checksum: 87D926F2D3141A1B
Show »

FASTA1,165126,577

References

« Hide 'large scale' references
[1]"Human hypertension caused by mutations in WNK kinases."
Wilson F.H., Disse-Nicodeme S., Choate K.A., Ishikawa K., Nelson-Williams C., Desitter I., Gunel M., Milford D.V., Lipkin G.W., Achard J.-M., Feely M.P., Dussol B., Berland Y., Unwin R.J., Mayan H., Simon D.B., Farfel Z., Jeunemaitre X., Lifton R.P.
Science 293:1107-1112(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DISEASE, VARIANTS PHA2B LYS-562; ALA-564; GLU-565 AND CYS-1185.
Tissue: Kidney.
[2]Chistiakov D.A.
Thesis (2001), College de France / Paris, France
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Kidney.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-1165 (ISOFORM 3).
Tissue: Kidney.
[4]"WNK kinases, a novel protein kinase subfamily in multi-cellular organisms."
Verissimo F., Jordan P.
Oncogene 20:5562-5569(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 207-418 (ISOFORMS 1/3), TISSUE SPECIFICITY, CHROMOSOMAL LOCATION.
Tissue: Colon.
[5]"Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium channel are regulated by multiple with no lysine (WNK) family members."
Heise C.J., Xu B.E., Deaton S.L., Cha S.K., Cheng C.J., Earnest S., Sengupta S., Juang Y.C., Stippec S., Xu Y., Zhao Y., Huang C.L., Cobb M.H.
J. Biol. Chem. 285:25161-25167(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The CUL3-KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in KLHL3 and WNK4 disrupt interaction."
Ohta A., Schumacher F.R., Mehellou Y., Johnson C., Knebel A., Macartney T.J., Wood N.T., Alessi D.R., Kurz T.
Biochem. J. 451:111-122(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLHL3, CHARACTERIZATION OF VARIANTS PHA2B LYS-562 AND GLU-565.
[7]"Impaired KLHL3-mediated ubiquitination of WNK4 causes human hypertension."
Wakabayashi M., Mori T., Isobe K., Sohara E., Susa K., Araki Y., Chiga M., Kikuchi E., Nomura N., Mori Y., Matsuo H., Murata T., Nomura S., Asano T., Kawaguchi H., Nonoyama S., Rai T., Sasaki S., Uchida S.
Cell Rep. 3:858-868(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH KLHL3, CHARACTERIZATION OF VARIANT PHA2B ALA-564.
[8]"Disease-causing mutations in KLHL3 impair its effect on WNK4 degradation."
Wu G., Peng J.B.
FEBS Lett. 587:1717-1722(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLHL3.
[9]"Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via ubiquitination and degradation of WNK4."
Shibata S., Zhang J., Puthumana J., Stone K.L., Lifton R.P.
Proc. Natl. Acad. Sci. U.S.A. 110:7838-7843(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-157; LYS-175; LYS-186; LYS-226; LYS-241; LYS-328; LYS-387; LYS-393; LYS-450; LYS-454; LYS-1010; LYS-1144; LYS-1157 AND LYS-1158, INTERACTION WITH KLHL3, CHARACTERIZATION OF VARIANTS PHA2B LYS-562 AND GLU-565.
[10]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-434; LEU-813; SER-992 AND PRO-1013.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF390018 mRNA. Translation: AAK91995.1.
AJ316534 mRNA. Translation: CAC48387.1. Frameshift.
AK096003 mRNA. Translation: BAC04669.1. Different initiation.
AK096052 mRNA. Translation: BAC04688.1.
AJ309861 mRNA. Translation: CAC32991.1.
RefSeqNP_115763.2. NM_032387.4.
UniGeneHs.105448.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V3SX-ray1.70C/D1015-1020[»]
4CH9X-ray1.84C/D557-567[»]
4CHBX-ray1.56C/D557-567[»]
ProteinModelPortalQ96J92.
SMRQ96J92. Positions 132-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122421. 12 interactions.
IntActQ96J92. 6 interactions.
MINTMINT-5207492.
STRING9606.ENSP00000246914.

Chemistry

ChEMBLCHEMBL1795196.

PTM databases

PhosphoSiteQ96J92.

Polymorphism databases

DMDM41688789.

Proteomic databases

PaxDbQ96J92.
PRIDEQ96J92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246914; ENSP00000246914; ENSG00000126562. [Q96J92-1]
GeneID65266.
KEGGhsa:65266.
UCSCuc002ibj.3. human. [Q96J92-1]

Organism-specific databases

CTD65266.
GeneCardsGC17P040932.
HGNCHGNC:14544. WNK4.
HPAHPA016500.
MIM601844. gene.
614491. phenotype.
neXtProtNX_Q96J92.
Orphanet88939. Pseudohypoaldosteronism type 2B.
PharmGKBPA134875400.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230962.
HOVERGENHBG050347.
InParanoidQ96J92.
KOK08867.
OMAESHLRLP.
OrthoDBEOG7KDF8Z.
PhylomeDBQ96J92.
TreeFamTF315363.

Enzyme and pathway databases

SignaLinkQ96J92.

Gene expression databases

ArrayExpressQ96J92.
BgeeQ96J92.
CleanExHS_WNK4.
GenevestigatorQ96J92.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR024678. Kinase_OSR1/WNK_CCT.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF12202. OSR1_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWNK4. human.
EvolutionaryTraceQ96J92.
GeneWikiWNK4.
GenomeRNAi65266.
NextBio67398.
PROQ96J92.
SOURCESearch...

Entry information

Entry nameWNK4_HUMAN
AccessionPrimary (citable) accession number: Q96J92
Secondary accession number(s): Q8N8X3 expand/collapse secondary AC list , Q8N8Z2, Q96DT8, Q9BYS5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 125 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM