STAM2_MOUSE - dbPTM
STAM2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAM2_MOUSE
UniProt AC O88811
Protein Name Signal transducing adapter molecule 2
Gene Name Stam2
Organism Mus musculus (Mouse).
Sequence Length 523
Subcellular Localization Cytoplasm . Early endosome membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity)..
Protein Sequence MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDRVGSTPSGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRSVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGVTFPSAGSQTVAAAAKNGTSLNKNKEDEDIAKAIELSLQEQKQQYTETKALYPPAESQLNNKAARRVRALYDFEAVEDNELTFKHGELITVLDDSDANWWQGENHRGTGLFPSNFVTTDLSTEVETATVDKLNVIDDDVEEIKKSEPEPVYIDEGKMDRALQILQSIDPKESKPDSQDLLDLEDVCQQMGPMIDEKLEEIDRKHSELSELNVKVLEALDLYNKLVNEAPVYSVYSKLHPAHYPPAAAGVPVQTYPVQSHGGNYLGHGIHQVSVAQNYNLGPDPMGSLRSLPPNMNSVTAHTVQPPYLSTGQDTVSNPSYMNQSSRLQAAAGTAAYTQPVGMSTDVSSFQNTASGLPQLAGFPVAVPAPVAAQPQASYHQQPLL
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
134UbiquitinationSLISATIKSMKEEGV
HHHHHHHHHHHHHCC
39.8922790023
156UbiquitinationQTVAAAAKNGTSLNK
HHHHHHHHCCCCCCC
51.7022790023
182UbiquitinationELSLQEQKQQYTETK
HHHHHHHHHHHHHHH
38.3222790023
185PhosphorylationLQEQKQQYTETKALY
HHHHHHHHHHHHCCC
12.2129514104
189UbiquitinationKQQYTETKALYPPAE
HHHHHHHHCCCCCHH
30.1122790023
192PhosphorylationYTETKALYPPAESQL
HHHHHCCCCCHHHHH
16.4226026062
202UbiquitinationAESQLNNKAARRVRA
HHHHHCHHHHHHHHH
42.2022790023
284UbiquitinationDDVEEIKKSEPEPVY
CCHHHHHHCCCCCEE
66.7622790023
285PhosphorylationDVEEIKKSEPEPVYI
CHHHHHHCCCCCEEE
54.0725338131
343UbiquitinationKLEEIDRKHSELSEL
HHHHHHHHCHHHHHH
47.97-
363UbiquitinationEALDLYNKLVNEAPV
HHHHHHHHHHCCCCC
40.01-
371PhosphorylationLVNEAPVYSVYSKLH
HHCCCCCHHHCCCCC
7.4326032504
372PhosphorylationVNEAPVYSVYSKLHP
HCCCCCHHHCCCCCC
18.1425367039
374PhosphorylationEAPVYSVYSKLHPAH
CCCCHHHCCCCCCCC
8.3120116462
375PhosphorylationAPVYSVYSKLHPAHY
CCCHHHCCCCCCCCC
26.9522817900

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 STAM2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAM2_MOUSE !!

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 STAM2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
12972556
GBG12_MOUSEGng12physical
20697350
HGS_MOUSEHgsphysical
20697350
ALDOA_MOUSEAldoaphysical
20697350
CRK_MOUSECrkphysical
20697350
UBC_MOUSEUbcphysical
16432517

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STAM2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374, AND MASSSPECTROMETRY.

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