WNK2_HUMAN - dbPTM
WNK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WNK2_HUMAN
UniProt AC Q9Y3S1
Protein Name Serine/threonine-protein kinase WNK2 {ECO:0000305}
Gene Name WNK2 {ECO:0000312|HGNC:HGNC:14542}
Organism Homo sapiens (Human).
Sequence Length 2297
Subcellular Localization Cytoplasm . Cell membrane .
Protein Description 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..
Protein Sequence MDGDGGRRDVPGTLMEPGRGAGPAGMAEPRAKAARPGPQRFLRRSVVESDQEEPPGLEAAEAPGPQPPQPLQRRVLLLCKTRRLIAERARGRPAAPAPAALVAQPGAPGAPADAGPEPVGTQEPGPDPIAAAVETAPAPDGGPREEAAATVRKEDEGAAEAKPEPGRTRRDEPEEEEDDEDDLKAVATSLDGRFLKFDIELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKLERQRFKEEAEMLKGLQHPNIVRFYDFWESSAKGKRCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPASFEKVHDPEIKEIIGECICKNKEERYEIKDLLSHAFFAEDTGVRVELAEEDHGRKSTIALRLWVEDPKKLKGKPKDNGAIEFTFDLEKETPDEVAQEMIESGFFHESDVKIVAKSIRDRVALIQWRRERIWPALQPKEQQDVGSPDKARGPPVPLQVQVTYHAQAGQPGPPEPEEPEADQHLLPPTLPTSATSLASDSTFDSGQGSTVYSDSQSSQQSVMLGSLADAAPSPAQCVCSPPVSEGPVLPQSLPSLGAYQQPTAAPGLPVGSVPAPACPPSLQQHFPDPAMSFAPVLPPPSTPMPTGPGQPAPPGQQPPPLAQPTPLPQVLAPQPVVPLQPVPPHLPPYLAPASQVGAPAQLKPLQMPQAPLQPLAQVPPQMPPIPVVPPITPLAGIDGLPPALPDLPTATVPPVPPPQYFSPAVILPSLAAPLPPASPALPLQAVKLPHPPGAPLAMPCRTIVPNAPATIPLLAVAPPGVAALSIHSAVAQLPGQPVYPAAFPQMAPTDVPPSPHHTVQNMRATPPQPALPPQPTLPPQPVLPPQPTLPPQPVLPPQPTRPPQPVLPPQPMLPPQPVLPPQPALPVRPEPLQPHLPEQAAPAATPGSQILLGHPAPYAVDVAAQVPTVPVPPAAVLSPPLPEVLLPAAPELLPQFPSSLATVSASVQSVPTQTATLLPPANPPLPGGPGIASPCPTVQLTVEPVQEEQASQDKPPGLPQSCESYGGSDVTSGKELSDSCEGAFGGGRLEGRAARKHHRRSTRARSRQERASRPRLTILNVCNTGDKMVECQLETHNHKMVTFKFDLDGDAPDEIATYMVEHDFILQAERETFIEQMKDVMDKAEDMLSEDTDADRGSDPGTSPPHLSTCGLGTGEESRQSQANAPVYQQNVLHTGKRWFIICPVAEHPAPEAPESSPPLPLSSLPPEASQGPCRGLTLPCLPWRRAACGAVFLSLFSAESAQSKQPPDSAPYKDQLSSKEQPSFLASQQLLSQAGPSNPPGAPPAPLAPSSPPVTALPQDGAAPATSTMPEPASGTASQAGGPGTPQGLTSELETSQPLAETHEAPLAVQPLVVGLAPCTPAPEAASTRDASAPREPLPPPAPEPSPHSGTPQPALGQPAPLLPAAVGAVSLATSQLPSPPLGPTVPPQPPSALESDGEGPPPRVGFVDSTIKSLDEKLRTLLYQEHVPTSSASAGTPVEVGDRDFTLEPLRGDQPRSEVCGGDLALPPVPKEAVSGRVQLPQPLVEKSELAPTRGAVMEQGTSSSMTAESSPRSMLGYDRDGRQVASDSHVVPSVPQDVPAFVRPARVEPTDRDGGEAGESSAEPPPSDMGTVGGQASHPQTLGARALGSPRKRPEQQDVSSPAKTVGRFSVVSTQDEWTLASPHSLRYSAPPDVYLDEAPSSPDVKLAVRRAQTASSIEVGVGEPVSSDSGDEGPRARPPVQKQASLPVSGSVAGDFVKKATAFLQRPSRAGSLGPETPSRVGMKVPTISVTSFHSQSSYISSDNDSELEDADIKKELQSLREKHLKEISELQSQQKQEIEALYRRLGKPLPPNVGFFHTAPPTGRRRKTSKSKLKAGKLLNPLVRQLKVVASSTGHLADSSRGPPAKDPAQASVGLTADSTGLSGKAVQTQQPCSVRASLSSDICSGLASDGGGARGQGWTVYHPTSERVTYKSSSKPRARFLSGPVSVSIWSALKRLCLGKEHSSRSSTSSLAPGPEPGPQPALHVQAQVNNSNNKKGTFTDDLHKLVDEWTSKTVGAAQLKPTLNQLKQTQKLQDMEAQAGWAAPGEARAMTAPRAGVGMPRLPPAPGPLSTTVIPGAAPTLSVPTPDGALGTARRNQVWFGLRVPPTACCGHSTQPRGGQRVGSKTASFAASDPVRS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
13PhosphorylationGRRDVPGTLMEPGRG
CCCCCCCCCCCCCCC		19.50-
19MethylationGTLMEPGRGAGPAGM
CCCCCCCCCCCCCCC		42.3716226709
30MethylationPAGMAEPRAKAARPG
CCCCCCHHHHHCCCC		39.98-
45PhosphorylationPQRFLRRSVVESDQE
HHHHHHHHHHCCCCC		24.8721955146
49PhosphorylationLRRSVVESDQEEPPG
HHHHHHCCCCCCCCC		32.7430175587
210PhosphorylationRGSFKTVYKGLDTET
CCCEEEEECCCCHHH		12.45-
232PhosphorylationELQDRKLTKLERQRF
HHHHHCCHHHHHHHH		36.30-
275PhosphorylationKRCIVLVTELMTSGT
CCEEEEEEECCCCCH		21.1730387612
280PhosphorylationLVTELMTSGTLKTYL
EEEECCCCCHHHHHH		18.8024719451
282PhosphorylationTELMTSGTLKTYLKR
EECCCCCHHHHHHHH		25.5024719451
286PhosphorylationTSGTLKTYLKRFKVM
CCCHHHHHHHHHCCC		14.5130387612
300PhosphorylationMKPKVLRSWCRQILK
CCHHHHHHHHHHHHH		26.7722964224
347PhosphorylationIGDLGLATLKRASFA
ECHHHHHHHHHHHHH		37.5421406692
349UbiquitinationDLGLATLKRASFAKS
HHHHHHHHHHHHHHH		41.38-
352PhosphorylationLATLKRASFAKSVIG
HHHHHHHHHHHHHHC		29.7517081983
356PhosphorylationKRASFAKSVIGTPEF
HHHHHHHHHHCCCCH		18.6125850435
391PhosphorylationMCMLEMATSEYPYSE
HHHHHHHHCCCCHHH		22.3026552605
392PhosphorylationCMLEMATSEYPYSEC
HHHHHHHCCCCHHHH		26.1226552605
394PhosphorylationLEMATSEYPYSECQN
HHHHHCCCCHHHHCC		13.7726552605
396PhosphorylationMATSEYPYSECQNAA
HHHCCCCHHHHCCHH		19.0526552605
397PhosphorylationATSEYPYSECQNAAQ
HHCCCCHHHHCCHHH		27.6526552605
406PhosphorylationCQNAAQIYRKVTCGI
HCCHHHHHHHHCCCC		7.7226552605
442PhosphorylationCKNKEERYEIKDLLS
HCCHHHHHHHHHHHH		25.8622817900
473PhosphorylationEDHGRKSTIALRLWV
CCCCCCCEEEEEEEE		17.1924719451
560PhosphorylationKEQQDVGSPDKARGP
HHHCCCCCCCCCCCC		29.7625159151
1150PhosphorylationVTSGKELSDSCEGAF
CCCCCHHHHCCCCCC		28.6819664994
1152PhosphorylationSGKELSDSCEGAFGG
CCCHHHHCCCCCCCC		15.6428985074
1175PhosphorylationRKHHRRSTRARSRQE
HHHHHHHHHHHHHHH		26.91-
1262PhosphorylationDKAEDMLSEDTDADR
HHHHHHHCCCCCCCC		27.1326471730
1265PhosphorylationEDMLSEDTDADRGSD
HHHHCCCCCCCCCCC		29.0927251275
1271PhosphorylationDTDADRGSDPGTSPP
CCCCCCCCCCCCCCC		41.3428348404
1275PhosphorylationDRGSDPGTSPPHLST
CCCCCCCCCCCCCCC		43.3728985074
1276PhosphorylationRGSDPGTSPPHLSTC
CCCCCCCCCCCCCCC		42.2024076635
1281PhosphorylationGTSPPHLSTCGLGTG
CCCCCCCCCCCCCCC		20.7223312004
1282PhosphorylationTSPPHLSTCGLGTGE
CCCCCCCCCCCCCCH		19.5623312004
1287PhosphorylationLSTCGLGTGEESRQS
CCCCCCCCCHHHHHH		46.6023312004
1329 (in isoform 2)Phosphorylation-47.2728348404
1330 (in isoform 2)Phosphorylation-28.9528348404
1588PhosphorylationFVDSTIKSLDEKLRT
CCHHHHHHHHHHHHH		36.8823312004
1595PhosphorylationSLDEKLRTLLYQEHV
HHHHHHHHHHHHHCC		31.3929978859
1598PhosphorylationEKLRTLLYQEHVPTS
HHHHHHHHHHCCCCC		18.2429978859
1604O-linked_GlycosylationLYQEHVPTSSASAGT
HHHHCCCCCCCCCCC		33.9432574038
1604PhosphorylationLYQEHVPTSSASAGT
HHHHCCCCCCCCCCC		33.9429978859
1605PhosphorylationYQEHVPTSSASAGTP
HHHCCCCCCCCCCCC		20.1729978859
1606PhosphorylationQEHVPTSSASAGTPV
HHCCCCCCCCCCCCE		28.8128348404
1608PhosphorylationHVPTSSASAGTPVEV
CCCCCCCCCCCCEEE		29.2228348404
1611PhosphorylationTSSASAGTPVEVGDR
CCCCCCCCCEEECCC		24.7128348404
1631DimethylationPLRGDQPRSEVCGGD
CCCCCCCCHHCCCCC		39.55-
1631MethylationPLRGDQPRSEVCGGD
CCCCCCCCHHCCCCC		39.5552720005
1677PhosphorylationGAVMEQGTSSSMTAE
CCHHCCCCCCCCCCC		25.7329978859
1678PhosphorylationAVMEQGTSSSMTAES
CHHCCCCCCCCCCCC		27.5224719451
1679PhosphorylationVMEQGTSSSMTAESS
HHCCCCCCCCCCCCC		24.7829978859
1680PhosphorylationMEQGTSSSMTAESSP
HCCCCCCCCCCCCCC		21.6629978859
1682PhosphorylationQGTSSSMTAESSPRS
CCCCCCCCCCCCCCH		29.2629978859
1685PhosphorylationSSSMTAESSPRSMLG
CCCCCCCCCCCHHCC		43.0827251275
1686PhosphorylationSSMTAESSPRSMLGY
CCCCCCCCCCHHCCC		18.8121815630
1689PhosphorylationTAESSPRSMLGYDRD
CCCCCCCHHCCCCCC		23.03-
1693PhosphorylationSPRSMLGYDRDGRQV
CCCHHCCCCCCCCEE		12.12-
1736PhosphorylationDGGEAGESSAEPPPS
CCCCCCCCCCCCCCC		33.6521733846
1765PhosphorylationLGARALGSPRKRPEQ
HCHHHCCCCCCCHHH		23.5223909892
1776PhosphorylationRPEQQDVSSPAKTVG
CHHHCCCCCCCEEEE		38.6023312004
1777PhosphorylationPEQQDVSSPAKTVGR
HHHCCCCCCCEEEEE		28.8229496963
1798PhosphorylationQDEWTLASPHSLRYS
CCCEEECCCCCCCCC		26.6825159151
1801PhosphorylationWTLASPHSLRYSAPP
EEECCCCCCCCCCCC		20.2327251275
1804PhosphorylationASPHSLRYSAPPDVY
CCCCCCCCCCCCCEE		17.9326657352
1805PhosphorylationSPHSLRYSAPPDVYL
CCCCCCCCCCCCEEC		28.0627732954
1811PhosphorylationYSAPPDVYLDEAPSS
CCCCCCEECCCCCCC		18.8030175587
1817PhosphorylationVYLDEAPSSPDVKLA
EECCCCCCCCCHHHH		62.6425159151
1818PhosphorylationYLDEAPSSPDVKLAV
ECCCCCCCCCHHHHH		24.8625159151
1830PhosphorylationLAVRRAQTASSIEVG
HHHHHHHCCCCEEEE		27.7622468782
1832PhosphorylationVRRAQTASSIEVGVG
HHHHHCCCCEEEECC		34.9222468782
1843PhosphorylationVGVGEPVSSDSGDEG
EECCCCCCCCCCCCC		38.8627732954
1844PhosphorylationGVGEPVSSDSGDEGP
ECCCCCCCCCCCCCC		35.7127732954
1846PhosphorylationGEPVSSDSGDEGPRA
CCCCCCCCCCCCCCC		50.5227732954
1862PhosphorylationPPVQKQASLPVSGSV
CCCCCCCCCCCCCCH		30.6130266825
1866PhosphorylationKQASLPVSGSVAGDF
CCCCCCCCCCHHHHH		24.3430266825
1868PhosphorylationASLPVSGSVAGDFVK
CCCCCCCCHHHHHHH		10.9930266825
1885PhosphorylationTAFLQRPSRAGSLGP
HHHHHCCCCCCCCCC		36.6328555341
1889PhosphorylationQRPSRAGSLGPETPS
HCCCCCCCCCCCCCC		29.2125159151
1894PhosphorylationAGSLGPETPSRVGMK
CCCCCCCCCCCCCCC		29.6921815630
1896PhosphorylationSLGPETPSRVGMKVP
CCCCCCCCCCCCCCC		47.2020068231
1906PhosphorylationGMKVPTISVTSFHSQ
CCCCCEEEEEEECCC		23.0930177828
1908PhosphorylationKVPTISVTSFHSQSS
CCCEEEEEEECCCCC		20.9130177828
1909PhosphorylationVPTISVTSFHSQSSY
CCEEEEEEECCCCCC		20.8530177828
1912PhosphorylationISVTSFHSQSSYISS
EEEEEECCCCCCCCC		29.7330177828
1914PhosphorylationVTSFHSQSSYISSDN
EEEECCCCCCCCCCC		28.2930177828
1915PhosphorylationTSFHSQSSYISSDND
EEECCCCCCCCCCCC		20.8830177828
1916PhosphorylationSFHSQSSYISSDNDS
EECCCCCCCCCCCCH		15.2930177828
1918PhosphorylationHSQSSYISSDNDSEL
CCCCCCCCCCCCHHH		24.3330177828
1919PhosphorylationSQSSYISSDNDSELE
CCCCCCCCCCCHHHC		30.7630177828
1923PhosphorylationYISSDNDSELEDADI
CCCCCCCHHHCHHHH		50.7830177828
1936PhosphorylationDIKKELQSLREKHLK
HHHHHHHHHHHHHHH		41.8621406692
2009PhosphorylationRQLKVVASSTGHLAD
HHHHHHHHCCCCCCC		19.4727732954
2010PhosphorylationQLKVVASSTGHLADS
HHHHHHHCCCCCCCC		28.7727732954
2011PhosphorylationLKVVASSTGHLADSS
HHHHHHCCCCCCCCC		26.5627732954
2056O-linked_GlycosylationQPCSVRASLSSDICS
CCCCCEEECCCCHHH		20.4432574038
2056PhosphorylationQPCSVRASLSSDICS
CCCCCEEECCCCHHH		20.44-
2063PhosphorylationSLSSDICSGLASDGG
ECCCCHHHCCCCCCC		36.8629116813
2067PhosphorylationDICSGLASDGGGARG
CHHHCCCCCCCCCCC		41.6611280764
2078PhosphorylationGARGQGWTVYHPTSE
CCCCCCCEEECCCCC		20.29-
2091PhosphorylationSERVTYKSSSKPRAR
CCCEEECCCCCCCHH		29.4527251275
2101PhosphorylationKPRARFLSGPVSVSI
CCCHHHCCCCCHHHH		38.0424719451
2110PhosphorylationPVSVSIWSALKRLCL
CCHHHHHHHHHHHHC		23.2727251275
2128PhosphorylationHSSRSSTSSLAPGPE
CCCCCCCCCCCCCCC		25.88-
2129PhosphorylationSSRSSTSSLAPGPEP
CCCCCCCCCCCCCCC		28.74-
2155UbiquitinationVNNSNNKKGTFTDDL
ECCCCCCCEECCHHH		66.36-
2157PhosphorylationNSNNKKGTFTDDLHK
CCCCCCEECCHHHHH		32.0425159151
2159PhosphorylationNNKKGTFTDDLHKLV
CCCCEECCHHHHHHH		28.5728450419
2170PhosphorylationHKLVDEWTSKTVGAA
HHHHHHHHHCCCCHH		20.4922210691
2171PhosphorylationKLVDEWTSKTVGAAQ
HHHHHHHHCCCCHHH		27.6622210691
2173PhosphorylationVDEWTSKTVGAAQLK
HHHHHHCCCCHHHHH		24.76-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of WNK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WNK2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of WNK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGK1_HUMANSGK1physical
20525693
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WNK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"WNK2 is a novel regulator of essential neuronal cation-chloridecotransporters.";
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).
Cited for: FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-45; SER-560;SER-1150; SER-1262; SER-1588; SER-1685; SER-1736; SER-1817; SER-1818;SER-1862 AND SER-2067.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1817 AND SER-1818, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-1817; SER-1818;SER-1862 AND SER-1889, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1817 AND SER-1818, ANDMASS SPECTROMETRY.

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