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Q3UH66 (WNK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase WNK2

EC=2.7.11.1
Alternative name(s):
Protein kinase lysine-deficient 2
Protein kinase with no lysine 2
Gene names
Name:Wnk2
Synonyms:Kiaa1760
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2149 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 SLC12A2, SCNN1A, SCNN1B, SCNN1D and SGK1 and inhibits SLC12A5. Negatively regulates the EGF-induced activation of the ERK/MAPK-pathway and the downstream cell cycle progression. Affects MAPK3/MAPK1 activity by modulating the activity of MAP2K1 and this modulation depends on phosphorylation of MAP2K1 by PAK1. WNK2 acts by interfering with the activity of PAK1 by controlling the balance of the activity of upstream regulators of PAK1 activity, RHOA and RAC1, which display reciprocal activity. Ref.5

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activation requires autophosphorylation of Ser-356. Phosphorylation of Ser-352 also promotes increased activity By similarity.

Subunit structure

Forms a complex with the phosphorylated form of STK39 in the brain.

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity.

Tissue specificity

Brain and heart. Ref.5

Post-translational modification

Autophosphorylated By similarity. Ref.5

Sequence similarities

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

Contains 1 protein kinase domain.

Caution

Cys-224 is present instead of the conserved Lys which is expected to be an active site residue. Lys-207 appears to fulfill the required catalytic function.

Sequence caution

The sequence AAH46464.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH55795.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE20646.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein phosphorylation

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3UH66-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q3UH66-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1921-2004: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q3UH66-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1935-1935: R → AHASTPP
     2019-2025: SLYDSPG → R
Note: No experimental confirmation available.
Isoform 4 (identifier: Q3UH66-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1935-1935: R → AHASTPP
     1971-2024: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q3UH66-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1935-1935: R → AHASTPP
     2019-2025: SLYDSPG → R
     2142-2149: DPESEKPD → GTVHSSLSGP...STPGPRLHIT
Note: No experimental confirmation available.
Isoform 6 (identifier: Q3UH66-6)

The sequence of this isoform differs from the canonical sequence as follows:
     731-742: Missing.
     971-1068: Missing.
     1935-1935: R → AHASTPP
     1971-2024: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q3UH66-7)

The sequence of this isoform differs from the canonical sequence as follows:
     971-1068: Missing.
     1592-1593: AE → E
     1935-1935: R → AHASTPP
     2019-2025: SLYDSPG → R
     2142-2149: DPESEKPD → EACALPTPPCKFLSRPSSGQPTEGRSISGGFHDTCPGGERGDENSLTPSG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21492149Serine/threonine-protein kinase WNK2
PRO_0000278774

Regions

Domain195 – 453259Protein kinase
Nucleotide binding201 – 2099ATP By similarity
Compositional bias172 – 1776Poly-Glu
Compositional bias645 – 1080436Pro-rich
Compositional bias1430 – 149667Pro-rich
Compositional bias1594 – 15974Poly-Ser

Sites

Active site3231Proton acceptor By similarity
Binding site2071ATP By similarity

Amino acid modifications

Modified residue451Phosphoserine By similarity
Modified residue3521Phosphoserine; by autocatalysis By similarity
Modified residue3561Phosphoserine; by autocatalysis By similarity
Modified residue5601Phosphoserine By similarity
Modified residue10981Phosphoserine By similarity
Modified residue12101Phosphoserine By similarity
Modified residue15071Phosphoserine By similarity
Modified residue15661Phosphoserine Ref.5
Modified residue15941Phosphoserine By similarity
Modified residue17251Phosphoserine By similarity
Modified residue17261Phosphoserine By similarity
Modified residue17701Phosphoserine Ref.5
Modified residue17971Phosphoserine Ref.5
Modified residue19621Phosphoserine By similarity

Natural variations

Alternative sequence731 – 74212Missing in isoform 6.
VSP_023366
Alternative sequence971 – 106898Missing in isoform 6 and isoform 7.
VSP_023367
Alternative sequence1592 – 15932AE → E in isoform 7.
VSP_023368
Alternative sequence1921 – 200484Missing in isoform 2.
VSP_023369
Alternative sequence19351R → AHASTPP in isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7.
VSP_023370
Alternative sequence1971 – 202454Missing in isoform 4 and isoform 6.
VSP_023371
Alternative sequence2019 – 20257SLYDSPG → R in isoform 3, isoform 5 and isoform 7.
VSP_023372
Alternative sequence2142 – 21498DPESEKPD → GTVHSSLSGPPCTLPLCQYG GLLPDPVSWGPWVASGNPEG SWGSQSPTQVPVFPVFLRPP VISTPGPRLHIT in isoform 5.
VSP_023373
Alternative sequence2142 – 21498DPESEKPD → EACALPTPPCKFLSRPSSGQ PTEGRSISGGFHDTCPGGER GDENSLTPSG in isoform 7.
VSP_023374

Experimental info

Sequence conflict761 – 79434PYLAP…QVPPQ → RRYLWPIFCSPQGWGTRPWT RPVHACLQGLLARE in BAC98249. Ref.4

Sequences

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

Last modified February 20, 2007. Version 2.
Checksum: A4BBF1D391FE9BEC

FASTA2,149227,527
        10         20         30         40         50         60 
MDGDGGRRDA PGALMEAGRG TGSAGMAEPR ARAARLGPQR FLRRSVVESD QEEPPGLEAA 

        70         80         90        100        110        120 
ETPSAQPPQP LQRRVLLLCK TRRLIAERAR GRPAAPAPAA PAAPPGSPSV PSDPGPERAG 

       130        140        150        160        170        180 
TQEPSPDPTT ASAAATQVPD GGPRQEEAPA PTQEDAGTTE AKPEPGRARK DEPEEEEDDE 

       190        200        210        220        230        240 
DDLKAVATSL DGRFLKFDIE LGRGSFKTVY KGLDTETWVE VAWCELQDRK LTKLERQRFK 

       250        260        270        280        290        300 
EEAEMLKGLQ HPNIVRFYDF WESSAKGKRC IVLVTELMTS GTLKTYLKRF KVMKPKVLRS 

       310        320        330        340        350        360 
WCRQILKGLL FLHTRTPPII HRDLKCDNIF ITGPTGSVKI GDLGLATLKR ASFAKSVIGT 

       370        380        390        400        410        420 
PEFMAPEMYE EHYDESVDVY AFGMCMLEMA TSEYPYSECQ NAAQIYRKVT CGIKPASFEK 

       430        440        450        460        470        480 
VHDPEIKEII GECICKNKEE RYEIKDLLSH AFFAEDTGVR VELAEEDHGR KSTIALRLWV 

       490        500        510        520        530        540 
EDPKKLKGKP KDNGAIEFTF DLEKETPDEV AQEMIDSGFF HESDVKIVAK SIRDRVALIQ 

       550        560        570        580        590        600 
WRRERIWPAL QSQEPKDSGS PDKARGLPAP LQVQVTYHAQ SGQPGQPEPE EPEADQHLLP 

       610        620        630        640        650        660 
PTLPASVTSL ASDSTFDSGQ GSTVYSDSQS SQQSMVLSSL VDTAPTPASC VCSPPVSEGP 

       670        680        690        700        710        720 
GLTHSLPTLG AFQQPATVPG LSVGPVPPPA RPPLLQQHFP ESSMSFTPVL PPPSTPVPTG 

       730        740        750        760        770        780 
PSQPAPPVQQ PLPMAQPPTL PQVLAPQPMG TVQPVPSHLP PYLAPTSQVV APAQLKPLQM 

       790        800        810        820        830        840 
PQPPLQPLAQ VPPQMPQMPV VPPITPLTGL DGLPQTLTDL PAANVAPVPP PQYFSPAVIL 

       850        860        870        880        890        900 
PSLTTPLPTS PALPMQAVKL PHPPGTPLAV PCQTIVPNAP AAIPLLAVAP QGVAALSIHP 

       910        920        930        940        950        960 
AVAQIPAQPV YPAAFPQMVP GDIPPSPHHT VQSLRATPPQ LASPVPPQPV QPSVIHLPEQ 

       970        980        990       1000       1010       1020 
AAPTAASGTQ VLLGHPPSYT ADVAAPVSAV SLPPAVLSPP LPDTLLPTVP DLLPKVPSSL 

      1030       1040       1050       1060       1070       1080 
APTVVAASQS APAQTSSLLL PTNPPLPTGP AVAGPCPAVQ LMVEVAQEEQ VSQDKPPGPP 

      1090       1100       1110       1120       1130       1140 
QSSESFGGSD VTSGRDLSDS CEGTFGGGRL EGRTARKHHR RSTRARSRQE RASRPRLTIL 

      1150       1160       1170       1180       1190       1200 
NVCNTGDKMV ECQLETHNHK MVTFKFDLDG DAPDEIATYM VEHDFILPAE RETFIEQMKD 

      1210       1220       1230       1240       1250       1260 
VMDKAEDMLS EDTDADHGSD TGTSPPHLGT CGLATGEENR QSQANAPVYQ QNVLHTGKRW 

      1270       1280       1290       1300       1310       1320 
FIICPVAEHP ATDTSESSPP LPLSSLQPEA SQDPAPYPDQ LSLTDKPSFP AAQQLLSQAG 

      1330       1340       1350       1360       1370       1380 
SSNPPGGASA PLAPSSPPVT TVIPAAPATS TVPESAAGTA MQAGGPGTHQ GPASVHETLQ 

      1390       1400       1410       1420       1430       1440 
PLAETRSAQC TAQPLSTGQG PCTPALEASR CSTGLGEPIS TREVSTQGEP LPASVPEPSP 

      1450       1460       1470       1480       1490       1500 
PTGATQSVPG QPPPPLPITV GAISLAAPQL PSPPLGPTAP PPPPSALESD GEGPPPRVGF 

      1510       1520       1530       1540       1550       1560 
VDNTIKSLDE KLRTLLYQEH VPTSSASAGT PMEASDRDFT LEPLRGDLPS ALSDKTPSLT 

      1570       1580       1590       1600       1610       1620 
QQTQPSLEKS ETAPAGWALA QREQGASSPM TAESSSSNTL GCDSDAGQVA SDSSTAPSVP 

      1630       1640       1650       1660       1670       1680 
QDASGSSVPT HMDPKDQNSS VPREALAAPM QSGPGSFTVG SPAQLRGARD SGSPHKRPGQ 

      1690       1700       1710       1720       1730       1740 
QDNSSPAKTV GRFSVVSTQD EWTLASPHSL RYSAPPDVYL DEIPSSPEVK LAVRRVQTAS 

      1750       1760       1770       1780       1790       1800 
SIEVGVEEPA SSDSGDERPR RRSQVQKQSS LPGTGGVASD FVKKATAFLH RSSRAGSLGP 

      1810       1820       1830       1840       1850       1860 
ETPSRAGVKV PTISITSFHS QSSYISSDND SEFEDADIKK ELRSLREKHL KEISELQSQQ 

      1870       1880       1890       1900       1910       1920 
KQEIEALYRR LGKPLPPNVG FFHTAPPMGR RRKTSKSKLK AGKLLNPLVQ QLKVVASSTG 

      1930       1940       1950       1960       1970       1980 
HLSDSSRGPP TKDPRGTKAV QTQQPCSVRA SLSTDICSGL ASDGGGARGQ GWTVYHPTSE 

      1990       2000       2010       2020       2030       2040 
RGAYKSSSKP RARFLSGPVS VSIWSALKRL CLGKEHSSSL YDSPGSSTSS LAPGPEPGPQ 

      2050       2060       2070       2080       2090       2100 
PTLHVQAQVN NSNNKKGTFT DDLHKLVDEW TTKTVGAAQV KPTLNQLKQT QKLHDMEASG 

      2110       2120       2130       2140 
DARATSVPRA AVGASCLAPA PGPLSTTATP GATPALPVPI PDPESEKPD 

« Hide

Isoform 2 [UniParc].

Checksum: CF4AE4A4DC664F90
Show »

FASTA2,065218,728
Isoform 3 [UniParc].

Checksum: 98AD382CFD4CFE45
Show »

FASTA2,149227,469
Isoform 4 [UniParc].

Checksum: 953172919B0CBF8D
Show »

FASTA2,101222,082
Isoform 5 [UniParc].

Checksum: 0BE7B0D8B10819E2
Show »

FASTA2,213234,069
Isoform 6 [UniParc].

Checksum: 1177FFA99C62BFD0
Show »

FASTA1,991211,147
Isoform 7 [UniParc].

Checksum: 581DA7240F2E5FE5
Show »

FASTA2,092221,908

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1506-2149 (ISOFORM 5).
Strain: C57BL/6J.
Tissue: Retina.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-2149 (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 801-2149 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1513-2149 (ISOFORM 4).
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Salivary gland.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 761-2149 (ISOFORM 7).
Tissue: Brain.
[5]"WNK2 is a novel regulator of essential neuronal cation-chloride cotransporters."
Rinehart J., Vazquez N., Kahle K.T., Hodson C.A., Ring A.M., Gulcicek E.E., Louvi A., Bobadilla N.A., Gamba G., Lifton R.P.
J. Biol. Chem. 286:30171-30180(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1566; SER-1770 AND SER-1797, INTERACTION WITH STK39.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CAAA01187366 Genomic DNA. No translation available.
AC140284 Genomic DNA. No translation available.
AK044381 mRNA. Translation: BAE20646.1. Different initiation.
AK147550 mRNA. Translation: BAE27991.1.
BC046464 mRNA. Translation: AAH46464.1. Different initiation.
BC055795 mRNA. Translation: AAH55795.1. Different initiation.
BC060187 mRNA. Translation: AAH60187.1.
AK129439 mRNA. Translation: BAC98249.1.
RefSeqNP_001277240.1. NM_001290311.1.
NP_001277242.1. NM_001290313.1.
NP_083637.2. NM_029361.4.
UniGeneMm.342723.

3D structure databases

ProteinModelPortalQ3UH66.
SMRQ3UH66. Positions 184-545.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3UH66.

Proteomic databases

MaxQBQ3UH66.
PaxDbQ3UH66.
PRIDEQ3UH66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000160087; ENSMUSP00000124614; ENSMUSG00000037989.
GeneID75607.
KEGGmmu:75607.

Organism-specific databases

CTD65268.
MGIMGI:1922857. Wnk2.
RougeSearch...

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074385.
HOGENOMHOG000139922.
HOVERGENHBG050345.
KOK08867.
OrthoDBEOG7KDF8Z.
PhylomeDBQ3UH66.

Gene expression databases

ArrayExpressQ3UH66.
BgeeQ3UH66.
CleanExMM_WNK2.
GenevestigatorQ3UH66.

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

ChiTaRSWNK2. mouse.
NextBio343494.
PROQ3UH66.
SOURCESearch...

Entry information

Entry nameWNK2_MOUSE
AccessionPrimary (citable) accession number: Q3UH66
Secondary accession number(s): Q3V387 expand/collapse secondary AC list , Q6PAN9, Q6ZPI6, Q7TNS1, Q811F2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot