NKD2_HUMAN - dbPTM
NKD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NKD2_HUMAN
UniProt AC Q969F2
Protein Name Protein naked cuticle homolog 2
Gene Name NKD2
Organism Homo sapiens (Human).
Sequence Length 451
Subcellular Localization Cell membrane . Cytoplasm . Cytoplasmic vesicle .
Protein Description Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity (By similarity). Required for processing of TGFA and for targeting of TGFA to the basolateral membrane of polarized epithelial cells..
Protein Sequence MGKLQSKHAAAARKRRESPEGDSFVASAYASGRKGAEEAERRARDKQELPNGDPKEGPFREDQCPLQVALPAEKAEGREHPGQLLSADDGERAANREGPRGPGGQRLNIDALQCDVSVEEDDRQEWTFTLYDFDNCGKVTREDMSSLMHTIYEVVDASVNHSSGSSKTLRVKLTVSPEPSSKRKEGPPAGQDREPTRCRMEGELAEEPRVADRRLSAHVRRPSTDPQPCSERGPYCVDENTERRNHYLDLAGIENYTSRFGPGSPPVQAKQEPQGRASHLQARSRSQEPDTHAVHHRRSQVLVEHVVPASEPAARALDTQPRPKGPEKQFLKSPKGSGKPPGVPASSKSGKAFSYYLPAVLPPQAPQDGHHLPQPPPPPYGHKRYRQKGREGHSPLKAPHAQPATVEHEVVRDLPPTPAGEGYAVPVIQRHEHHHHHEHHHHHHHHHFHPS
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
2Myristoylation------MGKLQSKHA
------CCHHHHHHH		39.1115064403
2N-myristoyl glycine------MGKLQSKHA
------CCHHHHHHH		39.11-
18PhosphorylationAARKRRESPEGDSFV
HHHHHHCCCCCCHHH		26.8323312004
23PhosphorylationRESPEGDSFVASAYA
HCCCCCCHHHHHHHH		32.2623312004
27PhosphorylationEGDSFVASAYASGRK
CCCHHHHHHHHHCCC		19.2625003641
29PhosphorylationDSFVASAYASGRKGA
CHHHHHHHHHCCCCH		9.9827642862
31PhosphorylationFVASAYASGRKGAEE
HHHHHHHHCCCCHHH		26.84-
74UbiquitinationQVALPAEKAEGREHP
EEEEEHHHHCCCCCC		54.57-
86PhosphorylationEHPGQLLSADDGERA
CCCCCEEECCCCCHH		37.9428555341
117PhosphorylationDALQCDVSVEEDDRQ
EEEECCEEECCCCCC		15.5726471730
127PhosphorylationEDDRQEWTFTLYDFD
CCCCCEEEEEEEECC		13.1429978859
129PhosphorylationDRQEWTFTLYDFDNC
CCCEEEEEEEECCCC		19.6229978859
131PhosphorylationQEWTFTLYDFDNCGK
CEEEEEEEECCCCCC		16.1129978859
145PhosphorylationKVTREDMSSLMHTIY
CCCHHHHHHHHHHHH		32.4222210691
146PhosphorylationVTREDMSSLMHTIYE
CCHHHHHHHHHHHHH		24.0722210691
152PhosphorylationSSLMHTIYEVVDASV
HHHHHHHHHHHHHHC		12.1122210691
174PhosphorylationKTLRVKLTVSPEPSS
CEEEEEEEECCCCCC		17.1430576142
176PhosphorylationLRVKLTVSPEPSSKR
EEEEEEECCCCCCCC		20.5030576142
180PhosphorylationLTVSPEPSSKRKEGP
EEECCCCCCCCCCCC		46.9928450419
181PhosphorylationTVSPEPSSKRKEGPP
EECCCCCCCCCCCCC		47.3926074081
216PhosphorylationRVADRRLSAHVRRPS
CHHCCCHHHHCCCCC		17.9527422710
223PhosphorylationSAHVRRPSTDPQPCS
HHHCCCCCCCCCCCC		43.5628450419
224PhosphorylationAHVRRPSTDPQPCSE
HHCCCCCCCCCCCCC		55.1530576142
230PhosphorylationSTDPQPCSERGPYCV
CCCCCCCCCCCCCCC		36.6923312004
235PhosphorylationPCSERGPYCVDENTE
CCCCCCCCCCCCCCC		14.1323312004
241PhosphorylationPYCVDENTERRNHYL
CCCCCCCCCCCCCCC		28.9023312004
247PhosphorylationNTERRNHYLDLAGIE
CCCCCCCCCCHHCCC		12.8823312004
256PhosphorylationDLAGIENYTSRFGPG
CHHCCCCCHHCCCCC		8.0325884760
257PhosphorylationLAGIENYTSRFGPGS
HHCCCCCHHCCCCCC		25.6327642862
264PhosphorylationTSRFGPGSPPVQAKQ
HHCCCCCCCCCCCCC		29.2127499020
284PhosphorylationASHLQARSRSQEPDT
HHHHHHHHHCCCCCC		39.0229449344
286PhosphorylationHLQARSRSQEPDTHA
HHHHHHHCCCCCCHH		39.8930576142
291PhosphorylationSRSQEPDTHAVHHRR
HHCCCCCCHHHCCCC		23.5823312004
299PhosphorylationHAVHHRRSQVLVEHV
HHHCCCCHHEEEEEE		25.2921712546
333PhosphorylationPEKQFLKSPKGSGKP
CHHHHCCCCCCCCCC		33.7124719451
394PhosphorylationQKGREGHSPLKAPHA
HCCCCCCCCCCCCCC		42.6628122231
405PhosphorylationAPHAQPATVEHEVVR
CCCCCCCEEEEEEEC		32.8629214152
423PhosphorylationPTPAGEGYAVPVIQR
CCCCCCCCEEEEEEC		10.5027642862
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
223SPhosphorylationKinasePKACAP17612
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF25Q96BH1
PMID:18757723
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NKD2_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 NKD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RNF25_HUMANRNF25physical
18757723
DVL1_HUMANDVL1physical
20177058
CADH1_HUMANCDH1physical
20177058
CAV1_HUMANCAV1physical
20177058
ZN363_HUMANRCHY1physical
21988832
VDR_HUMANVDRphysical
21988832
1433E_HUMANYWHAEphysical
26186194
1433Z_HUMANYWHAZphysical
26186194
ARMT1_HUMANC6orf211physical
26186194
PLSI_HUMANPLS1physical
26186194
UB2D2_HUMANUBE2D2physical
26186194
UB2E3_HUMANUBE2E3physical
26186194
1433Z_HUMANYWHAZphysical
28514442
UB2D2_HUMANUBE2D2physical
28514442
1433G_HUMANYWHAGphysical
28514442
1433E_HUMANYWHAEphysical
28514442
1433B_HUMANYWHABphysical
28514442
ARMT1_HUMANC6orf211physical
28514442
PLSI_HUMANPLS1physical
28514442
PMVK_HUMANPMVKphysical
28514442
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 NKD2_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Myristoylated Naked2 escorts transforming growth factor alpha to thebasolateral plasma membrane of polarized epithelial cells.";
Li C., Franklin J.L., Graves-Deal R., Jerome W.G., Cao Z.,Coffey R.J.;
Proc. Natl. Acad. Sci. U.S.A. 101:5571-5576(2004).
Cited for: FUNCTION, INTERACTION WITH TGFA, SUBCELLULAR LOCATION, MYRISTOYLATION,AND MUTAGENESIS OF GLY-2.

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