STAM2_HUMAN - dbPTM
STAM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAM2_HUMAN
UniProt AC O75886
Protein Name Signal transducing adapter molecule 2
Gene Name STAM2
Organism Homo sapiens (Human).
Sequence Length 525
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 MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDKVGSTPNGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRAVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGITFPPAGSQTVSAAAKNGTSSNKNKEDEDIAKAIELSLQEQKQQHTETKSLYPSSEIQLNNKVARKVRALYDFEAVEDNELTFKHGEIIIVLDDSDANWWKGENHRGIGLFPSNFVTTNLNIETEAAAVDKLNVIDDDVEEIKKSEPEPVYIDEDKMDRALQVLQSIDPTDSKPDSQDLLDLEDICQQMGPMIDEKLEEIDRKHSELSELNVKVLEALELYNKLVNEAPVYSVYSKLHPPAHYPPASSGVPMQTYPVQSHGGNYMGQSIHQVTVAQSYSLGPDQIGPLRSLPPNVNSSVTAQPAQTSYLSTGQDTVSNPTYMNQNSNLQSATGTTAYTQQMGMSVDMSSYQNTTSNLPQLAGFPVTVPAHPVAQQHTNYHQQPLL
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
20PhosphorylationVEKATNEYNTTEDWS
HHHHHHCCCCCCCHH		21.6327642862
30SulfoxidationTEDWSLIMDICDKVG
CCCHHHHHHHHHHHC		3.2630846556
57UbiquitinationIMKRVNHKVPHVALQ
HHHHCCCCCHHHHHH		52.86-
100UbiquitinationVRAVIKNKAHPKVCE
HHHHHHCCCCHHHHH		42.9721853274
104UbiquitinationIKNKAHPKVCEKLKS
HHCCCCHHHHHHHHH		50.0433845483
122 (in isoform 1)Ubiquitination-76.3621890473
122UbiquitinationEWSEEFQKDPQFSLI
HHHHHHHHCCCHHHH		76.3621906983
122 (in isoform 2)Ubiquitination-76.3621890473
127PhosphorylationFQKDPQFSLISATIK
HHHCCCHHHHHHHHH		21.3927251275
134UbiquitinationSLISATIKSMKEEGI
HHHHHHHHHHHHHCC		39.8923000965
134 (in isoform 1)Ubiquitination-39.8921890473
134 (in isoform 2)Ubiquitination-39.8921890473
137UbiquitinationSATIKSMKEEGITFP
HHHHHHHHHHCCCCC		60.7623000965
156UbiquitinationQTVSAAAKNGTSSNK
HHHHHHHHCCCCCCC		51.7021906983
156 (in isoform 1)Ubiquitination-51.7021890473
156 (in isoform 2)Ubiquitination-51.7021890473
159PhosphorylationSAAAKNGTSSNKNKE
HHHHHCCCCCCCCHH		38.07-
160PhosphorylationAAAKNGTSSNKNKED
HHHHCCCCCCCCHHH		33.06-
161PhosphorylationAAKNGTSSNKNKEDE
HHHCCCCCCCCHHHH		52.22-
163UbiquitinationKNGTSSNKNKEDEDI
HCCCCCCCCHHHHHH		71.9322817900
165 (in isoform 1)Ubiquitination-69.0621890473
165 (in isoform 2)Ubiquitination-69.0621890473
165UbiquitinationGTSSNKNKEDEDIAK
CCCCCCCHHHHHHHH		69.0621906983
172UbiquitinationKEDEDIAKAIELSLQ
HHHHHHHHHHHHHHH		50.6729967540
177PhosphorylationIAKAIELSLQEQKQQ
HHHHHHHHHHHHHHH		18.4028555341
182UbiquitinationELSLQEQKQQHTETK
HHHHHHHHHHHCCCC		51.6921906983
182 (in isoform 1)Ubiquitination-51.6921890473
182 (in isoform 2)Ubiquitination-51.6921890473
189UbiquitinationKQQHTETKSLYPSSE
HHHHCCCCCCCCCCH		32.0323000965
189 (in isoform 2)Ubiquitination-32.0321890473
189 (in isoform 1)Ubiquitination-32.0321890473
190PhosphorylationQQHTETKSLYPSSEI
HHHCCCCCCCCCCHH		40.3228152594
192PhosphorylationHTETKSLYPSSEIQL
HCCCCCCCCCCHHHH		14.2527273156
194PhosphorylationETKSLYPSSEIQLNN
CCCCCCCCCHHHHCH		27.3522210691
195PhosphorylationTKSLYPSSEIQLNNK
CCCCCCCCHHHHCHH		33.9322210691
202UbiquitinationSEIQLNNKVARKVRA
CHHHHCHHHHHHHHH		35.8823000965
202 (in isoform 2)Ubiquitination-35.8821890473
202 (in isoform 1)Ubiquitination-35.8821890473
206UbiquitinationLNNKVARKVRALYDF
HCHHHHHHHHHHHCE		26.7423000965
283 (in isoform 1)Ubiquitination-54.2321890473
283 (in isoform 2)Ubiquitination-54.2321890473
283UbiquitinationDDDVEEIKKSEPEPV
CCCHHHHHHCCCCCE		54.2321906983
284UbiquitinationDDVEEIKKSEPEPVY
CCHHHHHHCCCCCEE		66.7633845483
285PhosphorylationDVEEIKKSEPEPVYI
CHHHHHHCCCCCEEC		54.0728796482
291PhosphorylationKSEPEPVYIDEDKMD
HCCCCCEECCHHHHH		17.2328796482
296UbiquitinationPVYIDEDKMDRALQV
CEECCHHHHHHHHHH		40.4229967540
343UbiquitinationKLEEIDRKHSELSEL
HHHHHHHHCHHHHHH		47.9730230243
345PhosphorylationEEIDRKHSELSELNV
HHHHHHCHHHHHHHH		43.1828348404
353UbiquitinationELSELNVKVLEALEL
HHHHHHHHHHHHHHH		39.78-
361PhosphorylationVLEALELYNKLVNEA
HHHHHHHHHHHHHCC		10.8123532336
363 (in isoform 1)Ubiquitination-40.0121890473
363UbiquitinationEALELYNKLVNEAPV
HHHHHHHHHHHCCCH		40.0122817900
371PhosphorylationLVNEAPVYSVYSKLH
HHHCCCHHCHHHCCC		7.4321945579
372PhosphorylationVNEAPVYSVYSKLHP
HHCCCHHCHHHCCCC		18.1421945579
374PhosphorylationEAPVYSVYSKLHPPA
CCCHHCHHHCCCCCC		8.3121945579
375PhosphorylationAPVYSVYSKLHPPAH
CCHHCHHHCCCCCCC		26.9521945579
375O-linked_GlycosylationAPVYSVYSKLHPPAH
CCHHCHHHCCCCCCC		26.9531373491
418PhosphorylationQVTVAQSYSLGPDQI
EEEEEEEECCCCCCC		8.8825884760
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
291YPhosphorylationKinaseFYNP06241
PSP
371YPhosphorylationKinaseFYNP06241
PSP
374YPhosphorylationKinaseFYNP06241
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAM2_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 STAM2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMBL2_HUMANL3MBTL2physical
16189514
STABP_HUMANSTAMBPphysical
16189514
UBP8_HUMANUSP8physical
13129930
UBP8_HUMANUSP8physical
10982817
HGS_HUMANHGSphysical
12551915
EPS15_HUMANEPS15physical
12551915
JAK2_HUMANJAK2physical
10899310
JAK3_HUMANJAK3physical
10899310
TYK2_HUMANTYK2physical
10899310
JAK1_HUMANJAK1physical
10899310
CBX5_HUMANCBX5physical
15882967
UBC_HUMANUBCphysical
21121635
ITCH_HUMANITCHphysical
22275353
UBC_HUMANUBCphysical
22841719
HGS_HUMANHGSphysical
13679051
HGS_HUMANHGSphysical
20504764
PTN23_HUMANPTPN23physical
23477725
KIF15_HUMANKIF15physical
22863883
SF3A3_HUMANSF3A3physical
22863883
TERA_HUMANVCPphysical
22863883
PKHB2_HUMANPLEKHB2physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
KLH42_HUMANKLHL42physical
25416956
ARRD3_HUMANARRDC3physical
25416956
SH24A_HUMANSH2D4Aphysical
25416956
COG7_HUMANCOG7physical
26344197
ASPP2_HUMANTP53BP2physical
26344197
TS101_HUMANTSG101physical
26344197
F1892_HUMANFAM189A2physical
21516116
UBC_HUMANUBCphysical
26601948
STABP_HUMANSTAMBPphysical
27725184
UBC_HUMANUBCphysical
27725184
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 STAM2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192; TYR-371 ANDTYR-374, AND MASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192 AND TYR-291, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-371 AND TYR-374, ANDMASS SPECTROMETRY.

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