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Protein

Serine/threonine-protein kinase WNK1

Gene

Wnk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. Activates SCNN1A, SCNN1B, SCNN1D and SGK1. Controls sodium and chloride ion transport by inhibiting the activity of WNK4, by either phosphorylating the kinase or via an interaction between WNK4 and the autoinhibitory domain of WNK1. WNK4 regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation. WNK1 may also play a role in actin cytoskeletal reorganization. Phosphorylates NEDD4L. Acts as a scaffold to inhibit SLC4A4, SLC26A6 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition (By similarity).By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+1 Publication

Enzyme regulationi

By hypertonicity. Activation requires autophosphorylation of Ser-382. Phosphorylation of Ser-378 also promotes increased activity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei233 – 2331ATPPROSITE-ProRule annotation1 Publication
Active sitei349 – 3491Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi227 – 2359ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • chloride channel inhibitor activity Source: Ensembl
  • magnesium ion binding Source: RGD
  • phosphatase binding Source: UniProtKB
  • potassium channel inhibitor activity Source: RGD
  • protein kinase binding Source: RGD
  • protein serine/threonine kinase activity Source: UniProtKB
  • protein serine/threonine kinase inhibitor activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Protein kinase inhibitor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-2672351. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase WNK1 (EC:2.7.11.1)
Alternative name(s):
Protein kinase lysine-deficient 1
Protein kinase with no lysine 1
Gene namesi
Name:Wnk1
Synonyms:Hsn2, Prkwnk1
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi621141. Wnk1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi233 – 2331K → G: Loss of kinase activity; when associated with K-250. 2 Publications
Mutagenesisi233 – 2331K → M: Loss of kinase activity. 2 Publications
Mutagenesisi250 – 2501C → A: No effect on kinase activity. 2 Publications
Mutagenesisi250 – 2501C → K: Reduced kinase activity. Loss of kinase activity; when associated with G-233. 2 Publications
Mutagenesisi256 – 2561K → M: No effect on kinase activity. 1 Publication
Mutagenesisi259 – 2591K → M: No effect on kinase activity. 1 Publication
Mutagenesisi378 – 3781S → A: Reduced kinase activity. 1 Publication
Mutagenesisi378 – 3781S → D: Increased kinase activity. 1 Publication
Mutagenesisi382 – 3821S → A: Loss of kinase activity. 1 Publication
Mutagenesisi382 – 3821S → D: Loss of kinase activity. 1 Publication
Mutagenesisi524 – 5241F → A: Reduced ability of autoinhibitory domain to regulate kinase activity. 1 Publication
Mutagenesisi526 – 5261F → A: Reduced ability of autoinhibitory domain to regulate kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21262126Serine/threonine-protein kinase WNK1PRO_0000086821Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei172 – 1721PhosphoserineCombined sources
Modified residuei378 – 3781Phosphoserine; by autocatalysis1 Publication
Modified residuei382 – 3821Phosphoserine; by autocatalysis1 Publication
Modified residuei1007 – 10071PhosphoserineBy similarity
Modified residuei1723 – 17231PhosphoserineBy similarity
Modified residuei1755 – 17551PhosphoserineBy similarity
Modified residuei1756 – 17561PhosphoserineBy similarity
Modified residuei1771 – 17711PhosphoserineBy similarity
Modified residuei1773 – 17731PhosphoserineCombined sources
Modified residuei1776 – 17761PhosphoserineCombined sources
Modified residuei1865 – 18651PhosphoserineBy similarity
Modified residuei2014 – 20141PhosphoserineBy similarity
Modified residuei2030 – 20301PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated in vitro by the BCR(KLHL3) complex and in vivo by a BCR(KLHL2) complex, leading to proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9JIH7.
PRIDEiQ9JIH7.

PTM databases

iPTMnetiQ9JIH7.
PhosphoSiteiQ9JIH7.

Expressioni

Gene expression databases

ExpressionAtlasiQ9JIH7. baseline and differential.
GenevisibleiQ9JIH7. RN.

Interactioni

Subunit structurei

Interacts with SYT2. Interacts with KLHL3, WNK3 and WNK4.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Syt2P291019EBI-457953,EBI-458017

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB
  • protein kinase binding Source: RGD

Protein-protein interaction databases

IntActiQ9JIH7. 6 interactions.
STRINGi10116.ENSRNOP00000013355.

Structurei

Secondary structure

1
2126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi211 – 2144Combined sources
Beta strandi218 – 22912Combined sources
Beta strandi231 – 24010Combined sources
Turni241 – 2433Combined sources
Beta strandi246 – 2538Combined sources
Helixi254 – 2563Combined sources
Helixi259 – 27315Combined sources
Beta strandi283 – 2919Combined sources
Beta strandi294 – 3029Combined sources
Helixi309 – 3168Combined sources
Helixi321 – 33919Combined sources
Beta strandi341 – 3433Combined sources
Helixi352 – 3543Combined sources
Beta strandi355 – 3595Combined sources
Beta strandi364 – 3663Combined sources
Helixi371 – 3744Combined sources
Beta strandi379 – 3835Combined sources
Helixi392 – 3965Combined sources
Helixi402 – 41716Combined sources
Turni421 – 4244Combined sources
Helixi428 – 4358Combined sources
Turni436 – 4383Combined sources
Helixi442 – 4465Combined sources
Helixi450 – 45910Combined sources
Helixi464 – 4663Combined sources
Helixi470 – 4745Combined sources
Helixi477 – 4793Combined sources
Beta strandi484 – 4918Combined sources
Beta strandi498 – 50710Combined sources
Beta strandi511 – 5155Combined sources
Beta strandi521 – 5277Combined sources
Turni528 – 5303Combined sources
Helixi533 – 54210Combined sources
Helixi548 – 5503Combined sources
Helixi551 – 56818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LRUNMR-A480-572[»]
3FPQX-ray1.80A/B194-483[»]
4Q2AX-ray3.50A194-480[»]
ProteinModelPortaliQ9JIH7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JIH7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini221 – 479259Protein 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

eggNOGiKOG0584. Eukaryota.
ENOG410XQWZ. LUCA.
GeneTreeiENSGT00800000124049.
HOGENOMiHOG000168221.
HOVERGENiHBG079897.
InParanoidiQ9JIH7.
KOiK08867.
PhylomeDBiQ9JIH7.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR024678. Kinase_OSR1/WNK_CCT.
IPR000719. Prot_kinase_dom.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JIH7-1) [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
MSDGTAEKQS GTPGFLSPPA PVPKNGSSSD SSVGEKLGAA VADSGIGRTE
60 70 80 90 100
EYRRRRHTMD KDSRGAAATT TPTEHRFFRR SVICDSNATA LELPGLPLSI
110 120 130 140 150
PQPSVPAVVP QSAPPEPHRE ETLTATVASQ VSQQPSAAAS PGEQAVVGSA
160 170 180 190 200
TATVPSSTSK DRPVSQPSLV GSKEEPPPSR SGSGSGGASA KEPQEERNQQ
210 220 230 240 250
QDDIEELETK AVGMSNDGRF LKFDIEIGRG SFKTVYKGLD TETTVEVAWC
260 270 280 290 300
ELQDRKLTKS ERQRFKEEAE MLKGLQHPNI VRFYDSWEST VKGKKCIVLV
310 320 330 340 350
TELMTSGTLK TYLKRFKVMK IKVLRSWCRQ ILKGLQFLHT RTPPIIHRDL
360 370 380 390 400
KCDNIFITGP TGSVKIGDLG LATLKRASFA KSVIGTPEFM APEMYEEKYD
410 420 430 440 450
ESVDVYAFGM CMLEMATSEY PYSECQNAAQ IYRRVTSGVK PASFDKVAIP
460 470 480 490 500
EVKEIIEGCI RQNKDERYSI KDLLNHAFFQ EETGVRVELA EEDDGEKIAI
510 520 530 540 550
KLWLRIEDIK KLKGKYKDNE AIEFSFDLER DVPEDVAQEM VESGYVCEGD
560 570 580 590 600
HKTMAKAIKD RVSLIKRKRE QRQLVREEQE KRKQEESSFK QQNEQQASVS
610 620 630 640 650
QAGIQPLSVA STGIPTAPTT SASVSTQVEP EEPEADQHQQ LQYQQPSISV
660 670 680 690 700
LSDGTVDSGQ GSSVFTESRV SSQQTVSYGS QHEQAHSIGT APGHTVSSIQ
710 720 730 740 750
AQSQPHGVYP PSSMAQGQNQ GQPSSSLAGV LSSQPVQHPQ QQGIQPTVPP
760 770 780 790 800
QQAVQYSLPQ AASSSEGTVQ PVSQPQVSAG TQSSTQGVSQ AAPPEQTPIT
810 820 830 840 850
QSQPTQPVPL VSSVDSAHSD VASGMSDGNE NAPSSSGRHE GRTTKRHYRK
860 870 880 890 900
SVRSRSRHEK TSRPKLRILN VSNKGDRVVE CQLETHNRKM VTFKFDLDGD
910 920 930 940 950
NPEEIATIMV NNDFILAIER ESFVAQVREI IEKADEMLSE DVSVEPEGDQ
960 970 980 990 1000
GLESLQGKDD YGFPGSQKLE GEFKQPIAVS SMPQQIGVPT SSLTQVVHSA
1010 1020 1030 1040 1050
GRRFIVSPVP ESRLRESKIF TSEIPDPVAA STSQGPGMNL SHSASSLSLQ
1060 1070 1080 1090 1100
QAFSELKHGQ MTEGPNTAPP NFNHPGPTFS PFLTSIAGVQ TVAASTPSVS
1110 1120 1130 1140 1150
VPITSSPLND ISTSVMQSEG ALPTDKGIGG VTTSTGVVAS GGLTTLSVSE
1160 1170 1180 1190 1200
TPTLSSAVSS STAPAVVTVS TTSQPVQAST SGSIASSTGS FPSGTFSTTT
1210 1220 1230 1240 1250
GTTVSSVAVP NAKPPTVLLQ QVAGNTAGVA IVTSVSTTTP FPAMASQPSL
1260 1270 1280 1290 1300
PLGSSTSAPT LAETVVVSAH SLDKASHSST AGLGLSFCAP SSSSSSGTAV
1310 1320 1330 1340 1350
SSSVSQPGIV HPLVISSAIA STPVLPQPAV PTSTPLLPQV PNIPPLVQPV
1360 1370 1380 1390 1400
ANVPAVQQTL IHSQPQPALL PNQPHTHCPE MDADTQSKAP GIDDIKTLEE
1410 1420 1430 1440 1450
KLRSLFSEHS SSGTQHASVS LETPLVVETV TPGIPTTAVA PSKLMTSTTS
1460 1470 1480 1490 1500
TCLPPTNLPL GTAGMPVMPV GTPGQVSTPG THASAPASTA TGAKPGTTPP
1510 1520 1530 1540 1550
KPSLTKTVVP PVGTELSAGT VPCEQLPPFP GPSLIQTQQP LEDLDAQLRR
1560 1570 1580 1590 1600
TLSPETIPVT PAVGPLSTMS STAVTEAGSQ PQKDGTEVHV TASSSGAGVV
1610 1620 1630 1640 1650
KMGRFQVSVT MDDAQKERKN RSEDTKSVHF ESSTSESSVL SSSSPESTLV
1660 1670 1680 1690 1700
KPEPNGITVS GISLDVPDST HRTPTPEAKS ETGQPTKVGR FQVTTTANKV
1710 1720 1730 1740 1750
GRFSVSRTED KVTELKKEGP VTSPFRDSEQ TVIPAAIPKK EKPELAEPSH
1760 1770 1780 1790 1800
LNGPSSDLEA AFLSRGGEDG SGSPHSPPHL CSKSLPIQTL SQSLSNSFNS
1810 1820 1830 1840 1850
SYMSSDNESD IEDEDLRLEL RRLREKHLKE IQDLQSRQKH EIESLYTKLG
1860 1870 1880 1890 1900
KVPPAVIIPP AAPLSGRRRR PTKSKGSKSS RSSSLGNKSP QLSGNLSGQS
1910 1920 1930 1940 1950
GTSVLNPQQT LHPPGNTPET GHNQLLQPLK PSPSSDNLYS AFTSDGAISV
1960 1970 1980 1990 2000
PSLSAPGQGT SSTNTVGGTV SSQAAQAQPP AMTSSRKGTF TDDLHKLVDN
2010 2020 2030 2040 2050
WARDAMNLSG RRGSKGHMNY EGPGMARKFS APGQLCISMT SNMGGSTPIS
2060 2070 2080 2090 2100
AASATSLGHF TKSMCPPQQY GFPAAPFGTQ WSGTGGPAPQ PLGQFQPVGT
2110 2120
TSLQNFNISN LQKSISNPPG SNLRTT
Length:2,126
Mass (Da):225,112
Last modified:November 30, 2010 - v2
Checksum:i89AC72F9CC8B07DF
GO
Isoform 2 (identifier: Q9JIH7-3) [UniParc]FASTAAdd to basket

Also known as: Brain and spinal cord variant

The sequence of this isoform differs from the canonical sequence as follows:
     714-714: M → MPRRGRSMSV...SSGGSALHPQ

Note: This isoform which includes the HSN2 exon has been identified in human and mouse. The sequence shown here is the result of gene prediction.
Show »
Length:2,625
Mass (Da):278,978
Checksum:i3A08561C46528F28
GO
Isoform 3 (identifier: Q9JIH7-2) [UniParc]FASTAAdd to basket

Also known as: Dorsal root ganglia and sciatic nerve variant, DRG and sciatic nerve variant

The sequence of this isoform differs from the canonical sequence as follows:
     714-714: M → MPQSVAHPCG...SSGGSALHPQ
     782-782: Q → QGFPSRLPPQ...TTSSQQAVLE

Note: This isoform which includes the HSN2 exon has been identified in human and mouse. The sequence shown here is the result of gene prediction.
Show »
Length:2,634
Mass (Da):279,566
Checksum:i16F6B2F0666858C7
GO

Sequence cautioni

The sequence DAA04492.1 differs from that shown. Reason: Erroneous gene model prediction. Includes 3' and 3' intronic sequences.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1179 – 11791S → F in AAF74258 (PubMed:10828064).Curated
Sequence conflicti1950 – 19501V → I in AAF74258 (PubMed:10828064).Curated
Sequence conflicti2120 – 21201G → S in AAF74258 (PubMed:10828064).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei714 – 7141M → MPRRGRSMSVCVPHLSAVPS LSRISPSAPSTPPPVLSAPL CPSLLRSAPEETFAEKLSKA LESVLPMHSASQRKHRRSSL PSLFVTTPQSVAHPCGGTPT YPESQIFFPTIHERPVSFSP PPTCPPKVAISQRRKSTSFL EAQTRHFQPLLRTVGQNHLP PGGSPTNWTPEAIVMLGTTA NRVNRELCEMQVQPVFETTQ IYSDYRPGLVLAEEAHYFIP QETVYLAGVHYQAHAAGQYE GISYNSPVLSSPMKQITEQK PVPGCPASSSVFEFPSGQAF LVGHLQNLRLDSGPSPASPL SSISAPNSTDATHLKFHPVF VPHSAPAVLTHSNENRSNCV FEFHAQTPSSSSGEGGGILP QRVYRNRQVAVDSSQEELSP QSVGLHCHLQPVTEEQRNNH TPELTISVVEPMGQNWPVGS PEYSSDSSQITSSDISDFQS PPPTGGTAAPFGSDVSLPYI RLPQTVLQESPLFFCFPQGT TSQQVLSASYSSGGSALHPQ in isoform 2. CuratedVSP_040279
Alternative sequencei714 – 7141M → MPQSVAHPCGGTPTYPESQI FFPTIHERPVSFSPPPTCPP KVAISQRRKSTSFLEAQTRH FQPLLRTVGQNHLPPGGSPT NWTPEAIVMLGTTANRVNRE LCEMQVQPVFETTQIYSDYR PGLVLAEEAHYFIPQETVYL AGVHYQAHAAGQYEGISYNS PVLSSPMKQITEQKPVPGCP ASSSVFEFPSGQAFLVGHLQ NLRLDSGPSPASPLSSISAP NSTDATHLKFHPVFVPHSAP AVLTHSNENRSNCVFEFHAQ TPSSSSGEGGGILPQRVYRN RQVAVDSSQEELSPQSVGLH CHLQPVTEEQRNNHTPELTI SVVEPMGQNWPVGSPEYSSD SSQITSSDISDFQSPPPTGG TAAPFGSDVSLPYIRLPQTV LQESPLFFCFPQGTTSQQVL SASYSSGGSALHPQ in isoform 3. CuratedVSP_040278
Alternative sequencei782 – 7821Q → QGFPSRLPPQYPGDSNIAPS SNVASVCIHSTVLAPPPMPT EALATQGYFPTVVQPYVEST PLVPMGSVGGQVQVSQPAVS LSQQPPTTSSQQAVLE in isoform 3. CuratedVSP_040280

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF227741 mRNA. Translation: AAF74258.1.
AC106348 Genomic DNA. No translation available.
BK004106 Genomic DNA. Translation: DAA04492.1. Sequence problems.
RefSeqiNP_001002823.2. NM_001002823.2. [Q9JIH7-2]
NP_001186024.1. NM_001199095.1. [Q9JIH7-3]
NP_446246.2. NM_053794.2. [Q9JIH7-1]
UniGeneiRn.27409.

Genome annotation databases

EnsembliENSRNOT00000013355; ENSRNOP00000013355; ENSRNOG00000009956. [Q9JIH7-2]
ENSRNOT00000013621; ENSRNOP00000013622; ENSRNOG00000009956. [Q9JIH7-3]
ENSRNOT00000080788; ENSRNOP00000072173; ENSRNOG00000009956. [Q9JIH7-1]
GeneIDi116477.
KEGGirno:116477.
UCSCiRGD:621141. rat. [Q9JIH7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF227741 mRNA. Translation: AAF74258.1.
AC106348 Genomic DNA. No translation available.
BK004106 Genomic DNA. Translation: DAA04492.1. Sequence problems.
RefSeqiNP_001002823.2. NM_001002823.2. [Q9JIH7-2]
NP_001186024.1. NM_001199095.1. [Q9JIH7-3]
NP_446246.2. NM_053794.2. [Q9JIH7-1]
UniGeneiRn.27409.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LRUNMR-A480-572[»]
3FPQX-ray1.80A/B194-483[»]
4Q2AX-ray3.50A194-480[»]
ProteinModelPortaliQ9JIH7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JIH7. 6 interactions.
STRINGi10116.ENSRNOP00000013355.

PTM databases

iPTMnetiQ9JIH7.
PhosphoSiteiQ9JIH7.

Proteomic databases

PaxDbiQ9JIH7.
PRIDEiQ9JIH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000013355; ENSRNOP00000013355; ENSRNOG00000009956. [Q9JIH7-2]
ENSRNOT00000013621; ENSRNOP00000013622; ENSRNOG00000009956. [Q9JIH7-3]
ENSRNOT00000080788; ENSRNOP00000072173; ENSRNOG00000009956. [Q9JIH7-1]
GeneIDi116477.
KEGGirno:116477.
UCSCiRGD:621141. rat. [Q9JIH7-1]

Organism-specific databases

CTDi65125.
RGDi621141. Wnk1.

Phylogenomic databases

eggNOGiKOG0584. Eukaryota.
ENOG410XQWZ. LUCA.
GeneTreeiENSGT00800000124049.
HOGENOMiHOG000168221.
HOVERGENiHBG079897.
InParanoidiQ9JIH7.
KOiK08867.
PhylomeDBiQ9JIH7.

Enzyme and pathway databases

ReactomeiR-RNO-2672351. Stimuli-sensing channels.

Miscellaneous databases

EvolutionaryTraceiQ9JIH7.
NextBioi619039.
PROiQ9JIH7.

Gene expression databases

ExpressionAtlasiQ9JIH7. baseline and differential.
GenevisibleiQ9JIH7. RN.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR024678. Kinase_OSR1/WNK_CCT.
IPR000719. Prot_kinase_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "WNK1, a novel mammalian serine/threonine protein kinase lacking the catalytic lysine in subdomain II."
    Xu B.-E., English J.M., Wilsbacher J.L., Stippec S., Goldsmith E.J., Cobb M.H.
    J. Biol. Chem. 275:16795-16801(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-233; CYS-250; LYS-256 AND LYS-259.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 312-2126.
    Strain: Brown Norway.
  3. Cited for: IDENTIFICATION OF THE HSN2 EXON.
  4. "Regulation of WNK1 by an autoinhibitory domain and autophosphorylation."
    Xu B.-E., Min X., Stippec S., Lee B.H., Goldsmith E.J., Cobb M.H.
    J. Biol. Chem. 277:48456-48462(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-378 AND SER-382, MUTAGENESIS OF LYS-233; CYS-250; SER-378; SER-382; PHE-524 AND PHE-526.
  5. "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 WNK3 AND WNK4.
  6. "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.
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-172; SER-1773 AND SER-1776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Crystal structure of the kinase domain of WNK1, a kinase that causes a hereditary form of hypertension."
    Min X., Lee B.-H., Cobb M.H., Goldsmith E.J.
    Structure 12:1303-1311(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 194-483 OF MUTANT ALA-382, SUBUNIT.

Entry informationi

Entry nameiWNK1_RAT
AccessioniPrimary (citable) accession number: Q9JIH7
Secondary accession number(s): Q6IFS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: November 30, 2010
Last modified: May 11, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Cys-250 is present instead of the conserved Lys which is expected to be an active site residue. Lys-233 appears to fulfill the required catalytic function.2 Publications
HSN2 was originally thought to be an intronless gene lying within a WNK1 gene intron. It has been shown to be an alternative exon of the WNK1 gene in other mammalian species, including human and mouse. Isoforms bearing this exon (isoform 2 and isoform 3 in this entry) are specifically expressed in the nervous system in these species. system.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.