TYOBP_HUMAN - dbPTM
TYOBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TYOBP_HUMAN
UniProt AC O43914
Protein Name TYRO protein tyrosine kinase-binding protein
Gene Name TYROBP
Organism Homo sapiens (Human).
Sequence Length 113
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin..
Protein Sequence MGGLEPCSRLLLLPLLLAVSGLRPVQAQAQSDCSCSTVSPGVLAGIVMGDLVLTVLIALAVYFLGRLVPRGRGAAEAATRKQRITETESPYQELQGQRSDVYSDLNTQRPYYK
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
85PhosphorylationATRKQRITETESPYQ
HHHHHHHHCCCCHHH
38.7627486199
87PhosphorylationRKQRITETESPYQEL
HHHHHHCCCCHHHHH
32.8723532336
89PhosphorylationQRITETESPYQELQG
HHHHCCCCHHHHHCC
36.0128450419
91PhosphorylationITETESPYQELQGQR
HHCCCCHHHHHCCCC
24.7321082442
99PhosphorylationQELQGQRSDVYSDLN
HHHCCCCCHHHHHHC
24.4428176486
102PhosphorylationQGQRSDVYSDLNTQR
CCCCCHHHHHHCCCC
11.0625587033
103PhosphorylationGQRSDVYSDLNTQRP
CCCCHHHHHHCCCCC
35.1628176486
107PhosphorylationDVYSDLNTQRPYYK-
HHHHHHCCCCCCCC-
33.0024719451
111PhosphorylationDLNTQRPYYK-----
HHCCCCCCCC-----
26.5225587033
112PhosphorylationLNTQRPYYK------
HCCCCCCCC------
16.9525587033

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
91YPhosphorylationKinaseSYKP43405
GPS
91YPhosphorylationKinaseSYKQ15046
PhosphoELM
102YPhosphorylationKinaseSYKP43405
GPS
102YPhosphorylationKinaseSYKQ15046
PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TYOBP_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 TYOBP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIRB1_HUMANSIRPB1physical
10940905
SIRBL_HUMANSIRPB1physical
10940905

Drug and Disease Associations
Kegg Disease
H00438 Polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL); Nasu-Hakola di
OMIM Disease
221770Polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TYOBP_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91, AND MASSSPECTROMETRY.

TOP