ODAM_HUMAN - dbPTM
ODAM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ODAM_HUMAN
UniProt AC A1E959
Protein Name Odontogenic ameloblast-associated protein
Gene Name ODAM
Organism Homo sapiens (Human).
Sequence Length 279
Subcellular Localization Secreted . Cytoplasm . Nucleus .
Protein Description Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface..
Protein Sequence MKIIILLGFLGATLSAPLIPQRLMSASNSNELLLNLNNGQLLPLQLQGPLNSWIPPFSGILQQQQQAQIPGLSQFSLSALDQFAGLLPNQIPLTGEASFAQGAQAGQVDPLQLQTPPQTQPGPSHVMPYVFSFKMPQEQGQMFQYYPVYMVLPWEQPQQTVPRSPQQTRQQQYEEQIPFYAQFGYIPQLAEPAISGGQQQLAFDPQLGTAPEIAVMSTGEEIPYLQKEAINFRHDSAGVFMPSTSPKPSTTNVFTSAVDQTITPELPEEKDKTDSLREP
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
115O-linked_GlycosylationVDPLQLQTPPQTQPG
CCCCCCCCCCCCCCC
45.59UniProtKB CARBOHYD
119O-linked_GlycosylationQLQTPPQTQPGPSHV
CCCCCCCCCCCCCCC
42.37UniProtKB CARBOHYD
132PhosphorylationHVMPYVFSFKMPQEQ
CCCCEEEEEECCHHH
17.5724719451
244O-linked_GlycosylationAGVFMPSTSPKPSTT
CCEECCCCCCCCCCC
43.08UniProtKB CARBOHYD
249O-linked_GlycosylationPSTSPKPSTTNVFTS
CCCCCCCCCCCCCCC
54.73UniProtKB CARBOHYD
250O-linked_GlycosylationSTSPKPSTTNVFTSA
CCCCCCCCCCCCCCC
30.80UniProtKB CARBOHYD
251O-linked_GlycosylationTSPKPSTTNVFTSAV
CCCCCCCCCCCCCCC
33.45UniProtKB CARBOHYD
255O-linked_GlycosylationPSTTNVFTSAVDQTI
CCCCCCCCCCCCCCC
16.11UniProtKB CARBOHYD
255PhosphorylationPSTTNVFTSAVDQTI
CCCCCCCCCCCCCCC
16.11-
256O-linked_GlycosylationSTTNVFTSAVDQTIT
CCCCCCCCCCCCCCC
18.16UniProtKB CARBOHYD
256PhosphorylationSTTNVFTSAVDQTIT
CCCCCCCCCCCCCCC
18.16-
261O-linked_GlycosylationFTSAVDQTITPELPE
CCCCCCCCCCCCCCC
23.50UniProtKB CARBOHYD
263O-linked_GlycosylationSAVDQTITPELPEEK
CCCCCCCCCCCCCCC
17.69UniProtKB CARBOHYD
273O-linked_GlycosylationLPEEKDKTDSLREP-
CCCCCCCCCCCCCC-
40.74UniProtKB CARBOHYD
275O-linked_GlycosylationEEKDKTDSLREP---
CCCCCCCCCCCC---
34.26UniProtKB CARBOHYD

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 ODAM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ODAM_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 ODAM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
FHL2_HUMANFHL2physical
28514442
NISCH_HUMANNISCHphysical
28514442

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

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Related Literatures of Post-Translational Modification

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