FZD10_HUMAN - dbPTM
FZD10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FZD10_HUMAN
UniProt AC Q9ULW2
Protein Name Frizzled-10
Gene Name FZD10
Organism Homo sapiens (Human).
Sequence Length 581
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Receptor for Wnt proteins. Functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable)..
Protein Sequence MQRPGPRLWLVLQVMGSCAAISSMDMERPGDGKCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHGHLRFFLCSLYAPMCTEQVSTPIPACRVMCEQARLKCSPIMEQFNFKWPDSLDCRKLPNKNDPNYLCMEAPNNGSDEPTRGSGLFPPLFRPQRPHSAQEHPLKDGGPGRGGCDNPGKFHHVEKSASCAPLCTPGVDVYWSREDKRFAVVWLAIWAVLCFFSSAFTVLTFLIDPARFRYPERPIIFLSMCYCVYSVGYLIRLFAGAESIACDRDSGQLYVIQEGLESTGCTLVFLVLYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEANSSYFHLAAWAIPAVKTILILVMRRVAGDELTGVCYVGSMDVNALTGFVLIPLACYLVIGTSFILSGFVALFHIRRVMKTGGENTDKLEKLMVRIGLFSVLYTVPATCVIACYFYERLNMDYWKILAAQHKCKMNNQTKTLDCLMAASIPAVEIFMVKIFMLLVVGITSGMWIWTSKTLQSWQQVCSRRLKKKSRRKPASVITSGGIYKKAQHPQKTHHGKYEIPAQSPTCV
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
48N-linked_GlycosylationMCKDIGYNMTRMPNL
CCCCCCCCCCCCCCC
21.82UniProtKB CARBOHYD
145PhosphorylationPNKNDPNYLCMEAPN
CCCCCCCCCCEECCC
13.48-
153N-linked_GlycosylationLCMEAPNNGSDEPTR
CCEECCCCCCCCCCC
50.73UniProtKB CARBOHYD
155PhosphorylationMEAPNNGSDEPTRGS
EECCCCCCCCCCCCC
40.71-
159PhosphorylationNNGSDEPTRGSGLFP
CCCCCCCCCCCCCCC
45.69-
176PhosphorylationFRPQRPHSAQEHPLK
CCCCCCCCCCCCCCC
34.0427251275
485N-linked_GlycosylationQHKCKMNNQTKTLDC
HHHHHCCCCCCHHHH
47.61UniProtKB CARBOHYD
527PhosphorylationMWIWTSKTLQSWQQV
CCHHCHHHHHHHHHH
29.7824114839
530PhosphorylationWTSKTLQSWQQVCSR
HCHHHHHHHHHHHHH
29.9324114839
549PhosphorylationKSRRKPASVITSGGI
HHCCCCCEEEECCCH
23.6821945579
552PhosphorylationRKPASVITSGGIYKK
CCCCEEEECCCHHHH
21.1121945579
553PhosphorylationKPASVITSGGIYKKA
CCCEEEECCCHHHHC
24.7321945579
557PhosphorylationVITSGGIYKKAQHPQ
EEECCCHHHHCCCCC
15.0921945579
570UbiquitinationPQKTHHGKYEIPAQS
CCCCCCCCEECCCCC
35.04-
571PhosphorylationQKTHHGKYEIPAQSP
CCCCCCCEECCCCCC
24.5524719451
577PhosphorylationKYEIPAQSPTCV---
CEECCCCCCCCC---
25.0421945579
579PhosphorylationEIPAQSPTCV-----
ECCCCCCCCC-----
31.0224719451

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 FZD10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FZD10_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 FZD10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EVI5_HUMANEVI5physical
28514442
TMED8_HUMANTMED8physical
28514442
GSTCD_HUMANGSTCDphysical
28514442
VPS8_HUMANVPS8physical
28514442
ATRIP_HUMANATRIPphysical
28514442
EVI5L_HUMANEVI5Lphysical
28514442
VEZA_HUMANVEZTphysical
28514442
RINT1_HUMANRINT1physical
28514442
CND1_HUMANNCAPD2physical
28514442
XPO7_HUMANXPO7physical
28514442
XPO4_HUMANXPO4physical
28514442
VPP2_HUMANATP6V0A2physical
28514442
CD032_HUMANC4orf32physical
28514442
TNPO2_HUMANTNPO2physical
28514442
HEAT3_HUMANHEATR3physical
28514442
THADA_HUMANTHADAphysical
28514442
S39A1_HUMANSLC39A1physical
28514442
IPO7_HUMANIPO7physical
28514442
IPO11_HUMANIPO11physical
28514442
CIP2A_HUMANKIAA1524physical
28514442
MYADM_HUMANMYADMphysical
28514442
CND3_HUMANNCAPGphysical
28514442
IPO9_HUMANIPO9physical
28514442
AT2B2_HUMANATP2B2physical
28514442
EI2BG_HUMANEIF2B3physical
28514442
TNPO3_HUMANTNPO3physical
28514442
TSN15_HUMANTSPAN15physical
28514442
EI2BD_HUMANEIF2B4physical
28514442
GLMN_HUMANGLMNphysical
28514442
EBP_HUMANEBPphysical
28514442
YIPF3_HUMANYIPF3physical
28514442
ZW10_HUMANZW10physical
28514442
INT12_HUMANINTS12physical
28514442
BTAF1_HUMANBTAF1physical
28514442
SAAL1_HUMANSAAL1physical
28514442
CAND2_HUMANCAND2physical
28514442
DYM_HUMANDYMphysical
28514442
SMC2_HUMANSMC2physical
28514442
VPP1_HUMANATP6V0A1physical
28514442
CND2_HUMANNCAPHphysical
28514442
NRP1_HUMANNRP1physical
28514442
TBC9B_HUMANTBC1D9Bphysical
28514442
GBB4_HUMANGNB4physical
28514442
GEMI4_HUMANGEMIN4physical
28514442
LEG1_HUMANLGALS1physical
28514442
SETX_HUMANSETXphysical
28514442
CREL1_HUMANCRELD1physical
28514442
EI2BE_HUMANEIF2B5physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FZD10_HUMAN

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Related Literatures of Post-Translational Modification

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