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Q9BYP7

- WNK3_HUMAN

UniProt

Q9BYP7 - WNK3_HUMAN

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Protein

Serine/threonine-protein kinase WNK3

Gene

WNK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
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 PubMed:19470686, isoform 1 inhibits the activity of SLC12A3.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activation requires autophosphorylation of Ser-308. Phosphorylation of Ser-304 also promotes increased activity (By similarity). Kinase activity is inhibited by WNK4.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei159 – 1591ATPBy similarityPROSITE-ProRule annotation
Active sitei275 – 2751Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi153 – 1619ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. chloride channel inhibitor activity Source: UniProt
  3. protein kinase activity Source: BHF-UCL
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. intracellular signal transduction Source: UniProtKB
  2. negative regulation of apoptotic process Source: UniProtKB
  3. positive regulation of calcium ion transport Source: UniProtKB
  4. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  5. positive regulation of ion transmembrane transporter activity Source: BHF-UCL
  6. positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  7. positive regulation of rubidium ion transmembrane transporter activity Source: UniProtKB
  8. positive regulation of rubidium ion transport Source: UniProtKB
  9. positive regulation of sodium ion transmembrane transporter activity Source: UniProtKB
  10. positive regulation of sodium ion transport Source: BHF-UCL
  11. protein autophosphorylation Source: BHF-UCL
  12. protein phosphorylation Source: UniProtKB
  13. regulation of ion homeostasis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_160189. Stimuli-sensing channels.
SignaLinkiQ9BYP7.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:WNK3
Synonyms:KIAA1566, PRKWNK3
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:14543. WNK3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. adherens junction Source: BHF-UCL
  2. cytoplasm Source: UniProtKB
  3. tight junction Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi294 – 2941D → A: Catalytically inactive form. Inhibits sodium-coupled chloride cotransporters and activates potassium-coupled chloride cotransporters. 2 Publications

Organism-specific databases

PharmGKBiPA33784.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18001800Serine/threonine-protein kinase WNK3PRO_0000086823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621Phosphoserine1 Publication
Modified residuei304 – 3041Phosphoserine; by autocatalysisBy similarity
Modified residuei308 – 3081Phosphoserine; by autocatalysisBy similarity

Post-translational modificationi

Ubiquitinated by the BCR(KLHL2) complex, leading to its degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9BYP7.
PaxDbiQ9BYP7.
PRIDEiQ9BYP7.

PTM databases

PhosphoSiteiQ9BYP7.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiQ9BYP7.
CleanExiHS_WNK3.
ExpressionAtlasiQ9BYP7. baseline and differential.
GenevestigatoriQ9BYP7.

Organism-specific databases

HPAiHPA031652.

Interactioni

Subunit structurei

Interacts with WNK1 and WNK4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP3P425742EBI-1182602,EBI-524064

Protein-protein interaction databases

BioGridi122422. 8 interactions.
IntActiQ9BYP7. 2 interactions.
STRINGi9606.ENSP00000346667.

Structurei

3D structure databases

ProteinModelPortaliQ9BYP7.
SMRiQ9BYP7. Positions 136-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 405259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WNK subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074385.
HOGENOMiHOG000049042.
HOVERGENiHBG050346.
InParanoidiQ9BYP7.
KOiK08867.
OMAiERRDSQC.
PhylomeDBiQ9BYP7.
TreeFamiTF315363.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR024678. Kinase_OSR1/WNK_CCT.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF12202. OSR1_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BYP7) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATDSGDPAS TEDSEKPDGI SFENRVPQVA ATLTVEARLK EKNSTFSASG
60 70 80 90 100
ETVERKRFFR KSVEMTEDDK VAESSPKDER IKAAMNIPRV DKLPSNVLRG
110 120 130 140 150
GQEVKYEQCS KSTSEISKDC FKEKNEKEME EEAEMKAVAT SPSGRFLKFD
160 170 180 190 200
IELGRGAFKT VYKGLDTETW VEVAWCELQD RKLTKAEQQR FKEEAEMLKG
210 220 230 240 250
LQHPNIVRFY DSWESILKGK KCIVLVTELM TSGTLKTYLK RFKVMKPKVL
260 270 280 290 300
RSWCRQILKG LQFLHTRTPP IIHRDLKCDN IFITGPTGSV KIGDLGLATL
310 320 330 340 350
MRTSFAKSVI GTPEFMAPEM YEEHYDESVD VYAFGMCMLE MATSEYPYSE
360 370 380 390 400
CQNAAQIYRK VTSGIKPASF NKVTDPEVKE IIEGCIRQNK SERLSIRDLL
410 420 430 440 450
NHAFFAEDTG LRVELAEEDD CSNSSLALRL WVEDPKKLKG KHKDNEAIEF
460 470 480 490 500
SFNLETDTPE EVAYEMVKSG FFHESDSKAV AKSIRDRVTP IKKTREKKPA
510 520 530 540 550
GCLEERRDSQ CKSMGNVFPQ PQNTTLPLAP AQQTGAECEE TEVDQHVRQQ
560 570 580 590 600
LLQRKPQQHC SSVTGDNLSE AGAASVIHSD TSSQPSVAYS SNQTMGSQMV
610 620 630 640 650
SNIPQAEVNV PGQIYSSQQL VGHYQQVSGL QKHSKLTQPQ ILPLVQGQST
660 670 680 690 700
VLPVHVLGPT VVSQPQVSPL TVQKVPQIKP VSQPVGAEQQ AALLKPDLVR
710 720 730 740 750
SLNQDVATTK ENVSSPDNPS GNGKQDRIKQ RRASCPRPEK GTKFQLTVLQ
760 770 780 790 800
VSTSGDNMVE CQLETHNNKM VTFKFDVDGD APEDIADYMV EDNFVLESEK
810 820 830 840 850
EKFVEELRAI VGQAQEILHV HFATERATGV DSITVDSNSS QTGSSEQVQI
860 870 880 890 900
NSTSTQTSNE SAPQSSPVGR WRFCINQTIR NRETQSPPSL QHSMSAVPGR
910 920 930 940 950
HPLPSPKNTS NKEISRDTLL TIENNPCHRA LFTSKSEHKD VVDGKISECA
960 970 980 990 1000
SVETKQPAIL YQVEDNRQIM APVTNSSSYS TTSVRAVPAE CEGLTKQASI
1010 1020 1030 1040 1050
FIPVYPCHQT ASQADALMSH PGESTQTSGN SLTTLAFDQK PQTLSVQQPA
1060 1070 1080 1090 1100
MDAEFISQEG ETTVNTEASS PKTVIPTQTP GLEPTTLQPT TVLESDGERP
1110 1120 1130 1140 1150
PKLEFADNRI KTLDEKLRNL LYQEHSISSI YPESQKDTQS IDSPFSSSAE
1160 1170 1180 1190 1200
DTLSCPVTEV IAISHCGIKD SPVQSPNFQQ TGSKLLSNVA ASQPANISVF
1210 1220 1230 1240 1250
KRDLNVITSV PSELCLHEMS SDASLPGDPE AYPAAVSSGG AIHLQTGGGY
1260 1270 1280 1290 1300
FGLSFTCPSL KNPISKKSWT RKLKSWAYRL RQSTSFFKRS KVRQVETEEM
1310 1320 1330 1340 1350
RSAIAPDPIP LTRESTADTR ALNRCKAMSG SFQRGRFQVI TIPQQQSAKM
1360 1370 1380 1390 1400
TSFGIEHISV FSETNHSSEE AFIKTAKSQL VEIEPATQNP KTSFSYEKLQ
1410 1420 1430 1440 1450
ALQETCKENK GVPKQGDNFL SFSAACETDV SSVTPEKEFE ETSATGSSMQ
1460 1470 1480 1490 1500
SGSELLLKER EILTAGKQPS SDSEFSASLA GSGKSVAKTG PESNQCLPHH
1510 1520 1530 1540 1550
EEQAYAQTQS SLFYSPSSPM SSDDESEIED EDLKVELQRL REKHIQEVVN
1560 1570 1580 1590 1600
LQTQQNKELQ ELYERLRSIK DSKTQSTEIP LPPASPRRPR SFKSKLRSRP
1610 1620 1630 1640 1650
QSLTHVDNGI VATGKSCLIN ELENPLCVES NAASCQQSPA SKKGMFTDDL
1660 1670 1680 1690 1700
HKLVDDWTKE AVGNSLIKPS LNQLKQSQHK LETENWNKVS ENTPSTMGYT
1710 1720 1730 1740 1750
STWISSLSQI RGAVPTSLPQ GLSLPSFPGP LSSYGMPHVC QYNAVAGAGY
1760 1770 1780 1790 1800
PVQWVGISGT TQQSVVIPAQ SGGPFQPGMN MQAFPTSSVQ NPATIPPGPK
Length:1,800
Mass (Da):198,416
Last modified:October 19, 2011 - v3
Checksum:i1766D6AC8C7DE864
GO
Isoform 2 (identifier: Q9BYP7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1614-1624: GKSCLINELEN → D

Note: No experimental confirmation available.

Show »
Length:1,790
Mass (Da):197,329
Checksum:iF49E2D171D308FE3
GO
Isoform 3 (identifier: Q9BYP7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1248-1294: Missing.
     1614-1624: GKSCLINELEN → D

Show »
Length:1,743
Mass (Da):191,789
Checksum:i7B06CC8C7E8E4D67
GO
Isoform 4 (identifier: Q9BYP7-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,753
Mass (Da):192,875
Checksum:iD08B93F28F01E049
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101S → N in AAL99253. (PubMed:15194194)Curated
Sequence conflicti431 – 4322WV → RD in BAB13392. (PubMed:10997877)Curated
Sequence conflicti1211 – 12111P → S in BAB13392. (PubMed:10997877)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti704 – 7041Q → H.1 Publication
Corresponds to variant rs56077971 [ dbSNP | Ensembl ].
VAR_041323
Natural varianti854 – 8541S → C in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_041324
Natural varianti998 – 9981A → T.1 Publication
Corresponds to variant rs56404148 [ dbSNP | Ensembl ].
VAR_041325
Natural varianti1169 – 11691K → E.1 Publication
Corresponds to variant rs55903619 [ dbSNP | Ensembl ].
VAR_041326
Natural varianti1375 – 13751T → I.1 Publication
Corresponds to variant rs55879434 [ dbSNP | Ensembl ].
VAR_041327
Natural varianti1533 – 15331L → F in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_041328
Natural varianti1634 – 16341S → P in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
VAR_041329

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1248 – 129447Missing in isoform 3 and isoform 4. 2 PublicationsVSP_041932Add
BLAST
Alternative sequencei1614 – 162411GKSCLINELEN → D in isoform 3 and isoform 2. 2 PublicationsVSP_041933Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14357.1. [Q9BYP7-1]
CCDS35302.1. [Q9BYP7-3]
RefSeqiNP_001002838.1. NM_001002838.3. [Q9BYP7-3]
NP_065973.2. NM_020922.4. [Q9BYP7-1]
XP_006724656.1. XM_006724593.1. [Q9BYP7-3]
XP_006724657.1. XM_006724594.1. [Q9BYP7-3]
UniGeneiHs.92423.

Genome annotation databases

GeneIDi65267.
KEGGihsa:65267.
UCSCiuc004dtc.2. human. [Q9BYP7-1]
uc004dtd.2. human. [Q9BYP7-3]

Polymorphism databases

DMDMi353526307.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14357.1. [Q9BYP7-1 ]
CCDS35302.1. [Q9BYP7-3 ]
RefSeqi NP_001002838.1. NM_001002838.3. [Q9BYP7-3 ]
NP_065973.2. NM_020922.4. [Q9BYP7-1 ]
XP_006724656.1. XM_006724593.1. [Q9BYP7-3 ]
XP_006724657.1. XM_006724594.1. [Q9BYP7-3 ]
UniGenei Hs.92423.

3D structure databases

ProteinModelPortali Q9BYP7.
SMRi Q9BYP7. Positions 136-498.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122422. 8 interactions.
IntActi Q9BYP7. 2 interactions.
STRINGi 9606.ENSP00000346667.

Chemistry

ChEMBLi CHEMBL6055.
GuidetoPHARMACOLOGYi 2282.

PTM databases

PhosphoSitei Q9BYP7.

Polymorphism databases

DMDMi 353526307.

Proteomic databases

MaxQBi Q9BYP7.
PaxDbi Q9BYP7.
PRIDEi Q9BYP7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 65267.
KEGGi hsa:65267.
UCSCi uc004dtc.2. human. [Q9BYP7-1 ]
uc004dtd.2. human. [Q9BYP7-3 ]

Organism-specific databases

CTDi 65267.
GeneCardsi GC0XM054235.
HGNCi HGNC:14543. WNK3.
HPAi HPA031652.
MIMi 300358. gene.
neXtProti NX_Q9BYP7.
PharmGKBi PA33784.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074385.
HOGENOMi HOG000049042.
HOVERGENi HBG050346.
InParanoidi Q9BYP7.
KOi K08867.
OMAi ERRDSQC.
PhylomeDBi Q9BYP7.
TreeFami TF315363.

Enzyme and pathway databases

Reactomei REACT_160189. Stimuli-sensing channels.
SignaLinki Q9BYP7.

Miscellaneous databases

GeneWikii WNK3.
GenomeRNAii 65267.
NextBioi 67402.
PROi Q9BYP7.
SOURCEi Search...

Gene expression databases

Bgeei Q9BYP7.
CleanExi HS_WNK3.
ExpressionAtlasi Q9BYP7. baseline and differential.
Genevestigatori Q9BYP7.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR024678. Kinase_OSR1/WNK_CCT.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF12202. OSR1_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: Brain1 Publication.
  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.
    , 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: Brain1 Publication.
  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. 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. Cited for: UBIQUITINATION BY KLHL2.
  18. "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.
    , 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.

Entry informationi

Entry nameiWNK3_HUMAN
AccessioniPrimary (citable) accession number: Q9BYP7
Secondary accession number(s): B1AKG2
, Q5JRC1, Q6JP76, Q8TCX6, Q9HCK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: October 19, 2011
Last modified: October 29, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3