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Q9BYP7 (WNK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase WNK3

EC=2.7.11.1
Alternative name(s):
Protein kinase lysine-deficient 3
Protein kinase with no lysine 3
Gene names
Name:WNK3
Synonyms:KIAA1566, PRKWNK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1800 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. Phosphorylates WNK4. Regulates the phosphorylation of SLC12A1 and SLC12A2. Increases Ca2+ influx mediated by TRPV5 and TRPV6 by enhancing their membrane expression level via a kinase-dependent pathway. Inhibits the activity of KCNJ1 by decreasing its expression at the cell membrane in a non-catalytic manner. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

Isoform 1, isoform 2, isoform 3 and isoform 4 stimulate the activity of SLC12A1, SLC12A2 and SLC12A3 and inhibit the activity of SLC12A4, SLC12A5, SLC12A6 and SLC12A7. According to Ref.13, isoform 1 inhibits the activity of SLC12A3. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB Q9H4A3

Cofactor

Magnesium By similarity. UniProtKB Q9H4A3

Enzyme regulation

Activation requires autophosphorylation of Ser-308. Phosphorylation of Ser-304 also promotes increased activity By similarity. Kinase activity is inhibited by WNK4. Ref.10 UniProtKB Q9JIH7

Subunit structure

Interacts with WNK1 and WNK4. Ref.10

Subcellular location

Cytoplasm Ref.9.

Tissue specificity

Expressed in brain, lung, kidney, liver and pancreas, and in fetal tissues including placenta, fetal brain, lung and kidney. Very low levels of expression were also detected in fetal heart, thymus, liver and spleen. Isoform 1 is brain-specific. Isoform 3 is kidney-specific. Ref.1 Ref.3 Ref.6

Sequence similarities

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

Contains 1 protein kinase domain.

Caution

Cys-176 is present instead of the conserved Lys which is expected to be an active site residue. Lys-159 appears to fulfill the required catalytic function. UniProtKB Q9JIH7

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of calcium ion transport

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of establishment of protein localization to plasma membrane

Inferred from direct assay Ref.6. Source: BHF-UCL

positive regulation of ion transmembrane transporter activity

Inferred from direct assay Ref.6. Source: BHF-UCL

positive regulation of peptidyl-threonine phosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of rubidium ion transmembrane transporter activity

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of rubidium ion transport

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of sodium ion transmembrane transporter activity

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of sodium ion transport

Inferred from direct assay Ref.6. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay Ref.6. Source: BHF-UCL

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of ion homeostasis

Inferred from mutant phenotype Ref.15. Source: UniProtKB

   Cellular_componentadherens junction

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

tight junction

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

chloride channel inhibitor activity

Inferred from direct assay PubMed 17673510. Source: UniProt

protein kinase activity

Inferred from direct assay Ref.6. Source: BHF-UCL

protein serine/threonine kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CASP3P425742EBI-1182602,EBI-524064

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BYP7-1)

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: Q9BYP7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1614-1624: GKSCLINELEN → D
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9BYP7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1248-1294: Missing.
     1614-1624: GKSCLINELEN → D
Isoform 4 (identifier: Q9BYP7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1248-1294: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18001800Serine/threonine-protein kinase WNK3
PRO_0000086823

Regions

Domain147 – 405259Protein kinase
Nucleotide binding153 – 1619ATP By similarity UniProtKB Q8TDX7

Sites

Active site2751Proton acceptor By similarity UniProtKB Q8TDX7
Binding site1591ATP By similarity UniProtKB Q9JIH7

Amino acid modifications

Modified residue621Phosphoserine Ref.16
Modified residue3041Phosphoserine; by autocatalysis By similarity UniProtKB Q9JIH7
Modified residue3081Phosphoserine; by autocatalysis By similarity UniProtKB Q9JIH7

Natural variations

Alternative sequence1248 – 129447Missing in isoform 3 and isoform 4.
VSP_041932
Alternative sequence1614 – 162411GKSCLINELEN → D in isoform 3 and isoform 2.
VSP_041933
Natural variant7041Q → H. Ref.17
Corresponds to variant rs56077971 [ dbSNP | Ensembl ].
VAR_041323
Natural variant8541S → C in a lung squamous cell carcinoma sample; somatic mutation. Ref.17
VAR_041324
Natural variant9981A → T. Ref.17
Corresponds to variant rs56404148 [ dbSNP | Ensembl ].
VAR_041325
Natural variant11691K → E. Ref.17
Corresponds to variant rs55903619 [ dbSNP | Ensembl ].
VAR_041326
Natural variant13751T → I. Ref.17
Corresponds to variant rs55879434 [ dbSNP | Ensembl ].
VAR_041327
Natural variant15331L → F in a lung large cell carcinoma sample; somatic mutation. Ref.17
VAR_041328
Natural variant16341S → P in a renal clear cell carcinoma sample; somatic mutation. Ref.17
VAR_041329

Experimental info

Mutagenesis2941D → A: Catalytically inactive form. Inhibits sodium-coupled chloride cotransporters and activates potassium-coupled chloride cotransporters. Ref.6 Ref.15
Sequence conflict101S → N in AAL99253. Ref.3
Sequence conflict431 – 4322WV → RD in BAB13392. Ref.5
Sequence conflict12111P → S in BAB13392. Ref.5

Sequences

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

Last modified October 19, 2011. Version 3.
Checksum: 1766D6AC8C7DE864

FASTA1,800198,416
        10         20         30         40         50         60 
MATDSGDPAS TEDSEKPDGI SFENRVPQVA ATLTVEARLK EKNSTFSASG ETVERKRFFR 

        70         80         90        100        110        120 
KSVEMTEDDK VAESSPKDER IKAAMNIPRV DKLPSNVLRG GQEVKYEQCS KSTSEISKDC 

       130        140        150        160        170        180 
FKEKNEKEME EEAEMKAVAT SPSGRFLKFD IELGRGAFKT VYKGLDTETW VEVAWCELQD 

       190        200        210        220        230        240 
RKLTKAEQQR FKEEAEMLKG LQHPNIVRFY DSWESILKGK KCIVLVTELM TSGTLKTYLK 

       250        260        270        280        290        300 
RFKVMKPKVL RSWCRQILKG LQFLHTRTPP IIHRDLKCDN IFITGPTGSV KIGDLGLATL 

       310        320        330        340        350        360 
MRTSFAKSVI GTPEFMAPEM YEEHYDESVD VYAFGMCMLE MATSEYPYSE CQNAAQIYRK 

       370        380        390        400        410        420 
VTSGIKPASF NKVTDPEVKE IIEGCIRQNK SERLSIRDLL NHAFFAEDTG LRVELAEEDD 

       430        440        450        460        470        480 
CSNSSLALRL WVEDPKKLKG KHKDNEAIEF SFNLETDTPE EVAYEMVKSG FFHESDSKAV 

       490        500        510        520        530        540 
AKSIRDRVTP IKKTREKKPA GCLEERRDSQ CKSMGNVFPQ PQNTTLPLAP AQQTGAECEE 

       550        560        570        580        590        600 
TEVDQHVRQQ LLQRKPQQHC SSVTGDNLSE AGAASVIHSD TSSQPSVAYS SNQTMGSQMV 

       610        620        630        640        650        660 
SNIPQAEVNV PGQIYSSQQL VGHYQQVSGL QKHSKLTQPQ ILPLVQGQST VLPVHVLGPT 

       670        680        690        700        710        720 
VVSQPQVSPL TVQKVPQIKP VSQPVGAEQQ AALLKPDLVR SLNQDVATTK ENVSSPDNPS 

       730        740        750        760        770        780 
GNGKQDRIKQ RRASCPRPEK GTKFQLTVLQ VSTSGDNMVE CQLETHNNKM VTFKFDVDGD 

       790        800        810        820        830        840 
APEDIADYMV EDNFVLESEK EKFVEELRAI VGQAQEILHV HFATERATGV DSITVDSNSS 

       850        860        870        880        890        900 
QTGSSEQVQI NSTSTQTSNE SAPQSSPVGR WRFCINQTIR NRETQSPPSL QHSMSAVPGR 

       910        920        930        940        950        960 
HPLPSPKNTS NKEISRDTLL TIENNPCHRA LFTSKSEHKD VVDGKISECA SVETKQPAIL 

       970        980        990       1000       1010       1020 
YQVEDNRQIM APVTNSSSYS TTSVRAVPAE CEGLTKQASI FIPVYPCHQT ASQADALMSH 

      1030       1040       1050       1060       1070       1080 
PGESTQTSGN SLTTLAFDQK PQTLSVQQPA MDAEFISQEG ETTVNTEASS PKTVIPTQTP 

      1090       1100       1110       1120       1130       1140 
GLEPTTLQPT TVLESDGERP PKLEFADNRI KTLDEKLRNL LYQEHSISSI YPESQKDTQS 

      1150       1160       1170       1180       1190       1200 
IDSPFSSSAE DTLSCPVTEV IAISHCGIKD SPVQSPNFQQ TGSKLLSNVA ASQPANISVF 

      1210       1220       1230       1240       1250       1260 
KRDLNVITSV PSELCLHEMS SDASLPGDPE AYPAAVSSGG AIHLQTGGGY FGLSFTCPSL 

      1270       1280       1290       1300       1310       1320 
KNPISKKSWT RKLKSWAYRL RQSTSFFKRS KVRQVETEEM RSAIAPDPIP LTRESTADTR 

      1330       1340       1350       1360       1370       1380 
ALNRCKAMSG SFQRGRFQVI TIPQQQSAKM TSFGIEHISV FSETNHSSEE AFIKTAKSQL 

      1390       1400       1410       1420       1430       1440 
VEIEPATQNP KTSFSYEKLQ ALQETCKENK GVPKQGDNFL SFSAACETDV SSVTPEKEFE 

      1450       1460       1470       1480       1490       1500 
ETSATGSSMQ SGSELLLKER EILTAGKQPS SDSEFSASLA GSGKSVAKTG PESNQCLPHH 

      1510       1520       1530       1540       1550       1560 
EEQAYAQTQS SLFYSPSSPM SSDDESEIED EDLKVELQRL REKHIQEVVN LQTQQNKELQ 

      1570       1580       1590       1600       1610       1620 
ELYERLRSIK DSKTQSTEIP LPPASPRRPR SFKSKLRSRP QSLTHVDNGI VATGKSCLIN 

      1630       1640       1650       1660       1670       1680 
ELENPLCVES NAASCQQSPA SKKGMFTDDL HKLVDDWTKE AVGNSLIKPS LNQLKQSQHK 

      1690       1700       1710       1720       1730       1740 
LETENWNKVS ENTPSTMGYT STWISSLSQI RGAVPTSLPQ GLSLPSFPGP LSSYGMPHVC 

      1750       1760       1770       1780       1790       1800 
QYNAVAGAGY PVQWVGISGT TQQSVVIPAQ SGGPFQPGMN MQAFPTSSVQ NPATIPPGPK 

« Hide

Isoform 2 [UniParc].

Checksum: F49E2D171D308FE3
Show »

FASTA1,790197,329
Isoform 3 [UniParc].

Checksum: 7B06CC8C7E8E4D67
Show »

FASTA1,743191,789
Isoform 4 [UniParc].

Checksum: D08B93F28F01E049
Show »

FASTA1,753192,875

References

« Hide 'large scale' references
[1]"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] (ISOFORM 3), TISSUE SPECIFICITY, CHROMOSOMAL LOCATION.
Tissue: Brain.
[2]Jordan P.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]"Cloning, genomic organization, alternative splicing and expression analysis of the human gene WNK3 (PRKWNK3)."
Holden S., Cox J., Raymond F.L.
Gene 335:109-119(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 431-1800 (ISOFORM 3).
Tissue: Brain.
[6]"WNK3 kinase is a positive regulator of NKCC2 and NCC, renal cation-Cl- cotransporters required for normal blood pressure homeostasis."
Rinehart J., Kahle K.T., de Los Heros P., Vazquez N., Meade P., Wilson F.H., Hebert S.C., Gimenez I., Gamba G., Lifton R.P.
Proc. Natl. Acad. Sci. U.S.A. 102:16777-16782(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-294, TISSUE SPECIFICITY.
[7]"WNK3 modulates transport of Cl- in and out of cells: implications for control of cell volume and neuronal excitability."
Kahle K.T., Rinehart J., de Los Heros P., Louvi A., Meade P., Vazquez N., Hebert S.C., Gamba G., Gimenez I., Lifton R.P.
Proc. Natl. Acad. Sci. U.S.A. 102:16783-16788(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"WNK3, a kinase related to genes mutated in hereditary hypertension with hyperkalaemia, regulates the K+ channel ROMK1 (Kir1.1)."
Leng Q., Kahle K.T., Rinehart J., MacGregor G.G., Wilson F.H., Canessa C.M., Lifton R.P., Hebert S.C.
J. Physiol. (Lond.) 571:275-286(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Protein kinase WNK3 increases cell survival in a caspase-3-dependent pathway."
Verissimo F., Silva E., Morris J.D., Pepperkok R., Jordan P.
Oncogene 25:4172-4182(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"The thiazide-sensitive Na-Cl cotransporter is regulated by a WNK kinase signaling complex."
Yang C.L., Zhu X., Ellison D.H.
J. Clin. Invest. 117:3403-3411(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH WNK1 AND WNK4, ENZYME REGULATION.
[11]"WNK3 positively regulates epithelial calcium channels TRPV5 and TRPV6 via a kinase-dependent pathway."
Zhang W., Na T., Peng J.B.
Am. J. Physiol. 295:F1472-F1484(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Renal and brain isoforms of WNK3 have opposite effects on NCCT expression."
Glover M., Zuber A.M., O'Shaughnessy K.M.
J. Am. Soc. Nephrol. 20:1314-1322(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE SPLICING.
[14]"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.
[15]"Similar Effects of all WNK3 Variants upon SLC12 Cotransporters."
Cruz-Rangel S., Melo Z., Vazquez N., Meade P., Bobadilla N.A., Pasantes-Morales H., Gamba G., Mercado A.
Am. J. Physiol. 301:C601-C608(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 4), MUTAGENESIS OF ASP-294.
[16]"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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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] HIS-704; CYS-854; THR-998; GLU-1169; ILE-1375; PHE-1533 AND PRO-1634.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ409088 mRNA. Translation: CAC32455.2.
AY082340 mRNA. Translation: AAL99253.1.
AY352048 mRNA. Translation: AAR89465.1.
AL591766, AL049793, Z84469 Genomic DNA. Translation: CAI40707.1.
Z84469, AL049793, AL591766 Genomic DNA. Translation: CAI42732.1.
AL049793, AL591766, Z84469 Genomic DNA. Translation: CAI43128.1.
AL591766, AL049793, Z84469 Genomic DNA. Translation: CAI40708.1.
Z84469, AL049793, AL591766 Genomic DNA. Translation: CAI42733.1.
AL049793, AL591766, Z84469 Genomic DNA. Translation: CAI43129.1.
AB046786 mRNA. Translation: BAB13392.1.
RefSeqNP_001002838.1. NM_001002838.3.
NP_065973.2. NM_020922.4.
UniGeneHs.92423.

3D structure databases

ProteinModelPortalQ9BYP7.
SMRQ9BYP7. Positions 136-498.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122422. 4 interactions.
IntActQ9BYP7. 2 interactions.
STRING9606.ENSP00000346667.

Chemistry

ChEMBLCHEMBL6055.
GuidetoPHARMACOLOGY2282.

PTM databases

PhosphoSiteQ9BYP7.

Polymorphism databases

DMDM353526307.

Proteomic databases

PaxDbQ9BYP7.
PRIDEQ9BYP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354646; ENSP00000346667; ENSG00000196632. [Q9BYP7-1]
ENST00000375159; ENSP00000364301; ENSG00000196632. [Q9BYP7-1]
ENST00000375169; ENSP00000364312; ENSG00000196632. [Q9BYP7-3]
ENST00000594373; ENSP00000471368; ENSG00000269511. [Q9BYP7-1]
ENST00000598300; ENSP00000472115; ENSG00000269511. [Q9BYP7-1]
ENST00000599955; ENSP00000471833; ENSG00000269511. [Q9BYP7-3]
GeneID65267.
KEGGhsa:65267.
UCSCuc004dtc.2. human. [Q9BYP7-1]
uc004dtd.2. human. [Q9BYP7-3]

Organism-specific databases

CTD65267.
GeneCardsGC0XM054235.
HGNCHGNC:14543. WNK3.
HPAHPA031652.
MIM300358. gene.
neXtProtNX_Q9BYP7.
PharmGKBPA33784.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000049042.
HOVERGENHBG050346.
KOK08867.
OMAERRDSQC.
PhylomeDBQ9BYP7.
TreeFamTF315363.

Enzyme and pathway databases

SignaLinkQ9BYP7.

Gene expression databases

ArrayExpressQ9BYP7.
BgeeQ9BYP7.
CleanExHS_WNK3.
GenevestigatorQ9BYP7.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR024678. Kinase_OSR1/WNK_CCT.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF12202. OSR1_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiWNK3.
GenomeRNAi65267.
NextBio67402.
PROQ9BYP7.
SOURCESearch...

Entry information

Entry nameWNK3_HUMAN
AccessionPrimary (citable) accession number: Q9BYP7
Secondary accession number(s): B1AKG2 expand/collapse secondary AC list , Q5JRC1, Q6JP76, Q8TCX6, Q9HCK6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: October 19, 2011
Last modified: April 16, 2014
This is version 122 of the entry and version 3 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

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 X

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