WNK3_HUMAN - dbPTM
WNK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WNK3_HUMAN
UniProt AC Q9BYP7
Protein Name Serine/threonine-protein kinase WNK3 {ECO:0000305}
Gene Name WNK3 {ECO:0000312|HGNC:HGNC:14543}
Organism Homo sapiens (Human).
Sequence Length 1800
Subcellular Localization Cytoplasm .
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. [PubMed: 16275913]
Protein Sequence MATDSGDPASTEDSEKPDGISFENRVPQVAATLTVEARLKEKNSTFSASGETVERKRFFRKSVEMTEDDKVAESSPKDERIKAAMNIPRVDKLPSNVLRGGQEVKYEQCSKSTSEISKDCFKEKNEKEMEEEAEMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLMRTSFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIRDLLNHAFFAEDTGLRVELAEEDDCSNSSLALRLWVEDPKKLKGKHKDNEAIEFSFNLETDTPEEVAYEMVKSGFFHESDSKAVAKSIRDRVTPIKKTREKKPAGCLEERRDSQCKSMGNVFPQPQNTTLPLAPAQQTGAECEETEVDQHVRQQLLQRKPQQHCSSVTGDNLSEAGAASVIHSDTSSQPSVAYSSNQTMGSQMVSNIPQAEVNVPGQIYSSQQLVGHYQQVSGLQKHSKLTQPQILPLVQGQSTVLPVHVLGPTVVSQPQVSPLTVQKVPQIKPVSQPVGAEQQAALLKPDLVRSLNQDVATTKENVSSPDNPSGNGKQDRIKQRRASCPRPEKGTKFQLTVLQVSTSGDNMVECQLETHNNKMVTFKFDVDGDAPEDIADYMVEDNFVLESEKEKFVEELRAIVGQAQEILHVHFATERATGVDSITVDSNSSQTGSSEQVQINSTSTQTSNESAPQSSPVGRWRFCINQTIRNRETQSPPSLQHSMSAVPGRHPLPSPKNTSNKEISRDTLLTIENNPCHRALFTSKSEHKDVVDGKISECASVETKQPAILYQVEDNRQIMAPVTNSSSYSTTSVRAVPAECEGLTKQASIFIPVYPCHQTASQADALMSHPGESTQTSGNSLTTLAFDQKPQTLSVQQPAMDAEFISQEGETTVNTEASSPKTVIPTQTPGLEPTTLQPTTVLESDGERPPKLEFADNRIKTLDEKLRNLLYQEHSISSIYPESQKDTQSIDSPFSSSAEDTLSCPVTEVIAISHCGIKDSPVQSPNFQQTGSKLLSNVAASQPANISVFKRDLNVITSVPSELCLHEMSSDASLPGDPEAYPAAVSSGGAIHLQTGGGYFGLSFTCPSLKNPISKKSWTRKLKSWAYRLRQSTSFFKRSKVRQVETEEMRSAIAPDPIPLTRESTADTRALNRCKAMSGSFQRGRFQVITIPQQQSAKMTSFGIEHISVFSETNHSSEEAFIKTAKSQLVEIEPATQNPKTSFSYEKLQALQETCKENKGVPKQGDNFLSFSAACETDVSSVTPEKEFEETSATGSSMQSGSELLLKEREILTAGKQPSSDSEFSASLAGSGKSVAKTGPESNQCLPHHEEQAYAQTQSSLFYSPSSPMSSDDESEIEDEDLKVELQRLREKHIQEVVNLQTQQNKELQELYERLRSIKDSKTQSTEIPLPPASPRRPRSFKSKLRSRPQSLTHVDNGIVATGKSCLINELENPLCVESNAASCQQSPASKKGMFTDDLHKLVDDWTKEAVGNSLIKPSLNQLKQSQHKLETENWNKVSENTPSTMGYTSTWISSLSQIRGAVPTSLPQGLSLPSFPGPLSSYGMPHVCQYNAVAGAGYPVQWVGISGTTQQSVVIPAQSGGPFQPGMNMQAFPTSSVQNPATIPPGPK
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
3Phosphorylation-----MATDSGDPAS
-----CCCCCCCCCC
42.4229507054
5Phosphorylation---MATDSGDPASTE
---CCCCCCCCCCCC
40.5229507054
10PhosphorylationTDSGDPASTEDSEKP
CCCCCCCCCCCCCCC
37.4029507054
11PhosphorylationDSGDPASTEDSEKPD
CCCCCCCCCCCCCCC
46.0129507054
14PhosphorylationDPASTEDSEKPDGIS
CCCCCCCCCCCCCCC
41.0929507054
44PhosphorylationARLKEKNSTFSASGE
EHHHHCCCCCCCCCC
41.7328509920
45PhosphorylationRLKEKNSTFSASGET
HHHHCCCCCCCCCCC
30.8828509920
47PhosphorylationKEKNSTFSASGETVE
HHCCCCCCCCCCCHH
22.9328857561
49PhosphorylationKNSTFSASGETVERK
CCCCCCCCCCCHHHH
35.6424114839
52PhosphorylationTFSASGETVERKRFF
CCCCCCCCHHHHHHH
31.0628509920
62PhosphorylationRKRFFRKSVEMTEDD
HHHHHHHCCCCCCCC
21.0329978859
66PhosphorylationFRKSVEMTEDDKVAE
HHHCCCCCCCCHHHC
23.8224719451
77AcetylationKVAESSPKDERIKAA
HHHCCCCHHHHHHHH
74.3319413330
140PhosphorylationAEMKAVATSPSGRFL
HHHHHHEECCCCCEE
34.2722210691
141PhosphorylationEMKAVATSPSGRFLK
HHHHHEECCCCCEEE
13.82-
143PhosphorylationKAVATSPSGRFLKFD
HHHEECCCCCEEEEE
42.2222210691
215PhosphorylationRFYDSWESILKGKKC
HHHHHHHHHHCCCCE
27.2824719451
227PhosphorylationKKCIVLVTELMTSGT
CCEEEEEEECCCCCH
21.1730387612
232PhosphorylationLVTELMTSGTLKTYL
EEEECCCCCHHHHHH
18.8024719451
234PhosphorylationTELMTSGTLKTYLKR
EECCCCCHHHHHHHH
25.5024719451
238PhosphorylationTSGTLKTYLKRFKVM
CCCHHHHHHHHHCCC
14.5130387612
252PhosphorylationMKPKVLRSWCRQILK
CCHHHHHHHHHHHHH
26.7722964224
299PhosphorylationIGDLGLATLMRTSFA
ECHHHHHHHHHHHHH
26.5722199227
303PhosphorylationGLATLMRTSFAKSVI
HHHHHHHHHHHHHHC
17.7729514088
304PhosphorylationLATLMRTSFAKSVIG
HHHHHHHHHHHHHCC
16.9124719451
308PhosphorylationMRTSFAKSVIGTPEF
HHHHHHHHHCCCCHH
18.61-
343PhosphorylationMCMLEMATSEYPYSE
HHHHHHHCCCCCHHH
22.3026552605
344PhosphorylationCMLEMATSEYPYSEC
HHHHHHCCCCCHHHH
26.1226552605
346PhosphorylationLEMATSEYPYSECQN
HHHHCCCCCHHHHHC
13.7726552605
348PhosphorylationMATSEYPYSECQNAA
HHCCCCCHHHHHCHH
19.0526552605
349PhosphorylationATSEYPYSECQNAAQ
HCCCCCHHHHHCHHH
27.6526552605
358PhosphorylationCQNAAQIYRKVTSGI
HHCHHHHHHHHHCCC
7.7226552605
362PhosphorylationAQIYRKVTSGIKPAS
HHHHHHHHCCCCCCC
25.0323909892
363PhosphorylationQIYRKVTSGIKPASF
HHHHHHHCCCCCCCC
41.3223909892
439AcetylationVEDPKKLKGKHKDNE
HCCHHHHCCCCCCCC
74.8420167786
443AcetylationKKLKGKHKDNEAIEF
HHHCCCCCCCCCEEE
66.7820167786
468AcetylationEVAYEMVKSGFFHES
HHHHHHHHCCCCCHH
43.4820167786
475PhosphorylationKSGFFHESDSKAVAK
HCCCCCHHHCHHHHH
38.32-
489PhosphorylationKSIRDRVTPIKKTRE
HHHHHHCCCCHHCCC
21.8624719451
509PhosphorylationCLEERRDSQCKSMGN
CCHHHHHHCCCCCCC
35.35-
525PhosphorylationFPQPQNTTLPLAPAQ
CCCCCCCCCCCCCCH
33.65-
682PhosphorylationVPQIKPVSQPVGAEQ
CCCCCCCCCCCCHHH
36.9827251275
701PhosphorylationLKPDLVRSLNQDVAT
HCHHHHHHCCCCCCC
24.9627251275
709O-linked_GlycosylationLNQDVATTKENVSSP
CCCCCCCCCCCCCCC
26.9921740066
714PhosphorylationATTKENVSSPDNPSG
CCCCCCCCCCCCCCC
47.9722199227
715PhosphorylationTTKENVSSPDNPSGN
CCCCCCCCCCCCCCC
31.8022199227
734PhosphorylationRIKQRRASCPRPEKG
HHHHHHHCCCCCCCC
23.8918187866
865PhosphorylationSNESAPQSSPVGRWR
CCCCCCCCCCCCCEE
35.2324275569
893PhosphorylationSPPSLQHSMSAVPGR
CCCCHHHHCCCCCCC
11.0624114839
895PhosphorylationPSLQHSMSAVPGRHP
CCHHHHCCCCCCCCC
29.1824114839
905PhosphorylationPGRHPLPSPKNTSNK
CCCCCCCCCCCCCCC
57.0724719451
921PhosphorylationISRDTLLTIENNPCH
CCCCCEEEECCCHHH
29.3822985185
974O-linked_GlycosylationRQIMAPVTNSSSYST
CEEEEEECCCCCCCC
28.4621740066
1070PhosphorylationTVNTEASSPKTVIPT
EEECCCCCCCEECCC
37.15-
1085PhosphorylationQTPGLEPTTLQPTTV
CCCCCCCCCCCCCEE
30.6630266825
1086PhosphorylationTPGLEPTTLQPTTVL
CCCCCCCCCCCCEEE
33.8330266825
1090PhosphorylationEPTTLQPTTVLESDG
CCCCCCCCEEEECCC
19.3130266825
1091PhosphorylationPTTLQPTTVLESDGE
CCCCCCCEEEECCCC
29.7630266825
1095PhosphorylationQPTTVLESDGERPPK
CCCEEEECCCCCCCC
46.9130266825
1122PhosphorylationEKLRNLLYQEHSISS
HHHHHHHHHHHCHHH
18.2829978859
1192PhosphorylationLLSNVAASQPANISV
HHHHHHHCCCCCEEE
27.2729396449
1198PhosphorylationASQPANISVFKRDLN
HCCCCCEEEEECCCC
22.7029396449
12882-HydroxyisobutyrylationRQSTSFFKRSKVRQV
HHCCCHHHHHCCEEE
54.47-
1302PhosphorylationVETEEMRSAIAPDPI
ECCHHHHHHCCCCCC
23.7922210691
1312O-linked_GlycosylationAPDPIPLTRESTADT
CCCCCCCCCCCCCCH
27.3421740066
1315PhosphorylationPIPLTRESTADTRAL
CCCCCCCCCCCHHHH
26.13-
1316PhosphorylationIPLTRESTADTRALN
CCCCCCCCCCHHHHH
24.6522210691
1329PhosphorylationLNRCKAMSGSFQRGR
HHHHHHHCCCCCCCC
35.8227732954
1331PhosphorylationRCKAMSGSFQRGRFQ
HHHHHCCCCCCCCEE
15.7630377224
1334MethylationAMSGSFQRGRFQVIT
HHCCCCCCCCEEEEE
35.92115920085
1341PhosphorylationRGRFQVITIPQQQSA
CCCEEEEEECHHHCC
27.96-
1393PhosphorylationATQNPKTSFSYEKLQ
CCCCCCCCCCHHHHH
20.5127732954
1395PhosphorylationQNPKTSFSYEKLQAL
CCCCCCCCHHHHHHH
31.9527732954
1396PhosphorylationNPKTSFSYEKLQALQ
CCCCCCCHHHHHHHH
18.3127732954
1470PhosphorylationLTAGKQPSSDSEFSA
HHCCCCCCCCCCHHH
44.2630266825
1471PhosphorylationTAGKQPSSDSEFSAS
HCCCCCCCCCCHHHH
52.4130266825
1473PhosphorylationGKQPSSDSEFSASLA
CCCCCCCCCHHHHHC
42.3530266825
1476PhosphorylationPSSDSEFSASLAGSG
CCCCCCHHHHHCCCC
16.9427251275
1538PhosphorylationEDLKVELQRLREKHI
HHHHHHHHHHHHHHH
28.9332142685
1576PhosphorylationIKDSKTQSTEIPLPP
HCCCCCCCCCCCCCC
32.9924275569
1577PhosphorylationKDSKTQSTEIPLPPA
CCCCCCCCCCCCCCC
28.2822210691
1585PhosphorylationEIPLPPASPRRPRSF
CCCCCCCCCCCCCCH
25.3930266825
1598PhosphorylationSFKSKLRSRPQSLTH
CHHHHHHCCCCCCCC
59.7629978859
1602PhosphorylationKLRSRPQSLTHVDNG
HHHCCCCCCCCCCCC
37.6129978859
1604PhosphorylationRSRPQSLTHVDNGIV
HCCCCCCCCCCCCEE
25.7129978859
1638PhosphorylationNAASCQQSPASKKGM
CCHHCCCCCCHHCCC
9.1421613606
1641PhosphorylationSCQQSPASKKGMFTD
HCCCCCCHHCCCCCH
37.98-
1647PhosphorylationASKKGMFTDDLHKLV
CHHCCCCCHHHHHHH
21.5122985185
1652AcetylationMFTDDLHKLVDDWTK
CCCHHHHHHHCHHHH
58.4612654585
1665PhosphorylationTKEAVGNSLIKPSLN
HHHHHHCCCCCCCHH
26.0824719451
1670PhosphorylationGNSLIKPSLNQLKQS
HCCCCCCCHHHHHHH
34.6429978859
1677PhosphorylationSLNQLKQSQHKLETE
CHHHHHHHHHHHHCC
32.4429978859

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
-KUbiquitinationE3 ubiquitin ligaseKLHL2O95198
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WNK3_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 WNK3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NED4L_HUMANNEDD4Lphysical
24920754

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 WNK3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1471, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734, AND MASSSPECTROMETRY.

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