STAM1_HUMAN - dbPTM
STAM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAM1_HUMAN
UniProt AC Q92783
Protein Name Signal transducing adapter molecule 1
Gene Name STAM
Organism Homo sapiens (Human).
Sequence Length 540
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..
Protein Sequence MPLFATNPFDQDVEKATSEMNTAEDWGLILDICDKVGQSRTGPKDCLRSIMRRVNHKDPHVAMQALTLLGACVSNCGKIFHLEVCSRDFASEVSNVLNKGHPKVCEKLKALMVEWTDEFKNDPQLSLISAMIKNLKEQGVTFPAIGSQAAEQAKASPALVAKDPGTVANKKEEEDLAKAIELSLKEQRQQSTTLSTLYPSTSSLLTNHQHEGRKVRAIYDFEAAEDNELTFKAGEIITVLDDSDPNWWKGETHQGIGLFPSNFVTADLTAEPEMIKTEKKTVQFSDDVQVETIEPEPEPAFIDEDKMDQLLQMLQSTDPSDDQPDLPELLHLEAMCHQMGPLIDEKLEDIDRKHSELSELNVKVMEALSLYTKLMNEDPMYSMYAKLQNQPYYMQSSGVSGSQVYAGPPPSGAYLVAGNAQMSHLQSYSLPPEQLSSLSQAVVPPSANPALPSQQTQAAYPNTMVSSVQGNTYPSQAPVYSPPPAATAAAATADVTLYQNAGPNMPQVPNYNLTSSTLPQPGGSQQPPQPQQPYSQKALL
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
6Phosphorylation--MPLFATNPFDQDV
--CCCCCCCCCCHHH		35.7725599653
17PhosphorylationDQDVEKATSEMNTAE
CHHHHHHHHHCCCHH		35.9728111955
18PhosphorylationQDVEKATSEMNTAED
HHHHHHHHHCCCHHH		39.4428111955
22PhosphorylationKATSEMNTAEDWGLI
HHHHHCCCHHHHHHH		30.0728111955
39PhosphorylationICDKVGQSRTGPKDC
HHHHHCCCCCCHHHH		26.3628111955
41PhosphorylationDKVGQSRTGPKDCLR
HHHCCCCCCHHHHHH		64.1828111955
91PhosphorylationVCSRDFASEVSNVLN
ECCHHHHHHHHHHHH		38.2321712546
99UbiquitinationEVSNVLNKGHPKVCE
HHHHHHHCCCHHHHH		55.20-
103UbiquitinationVLNKGHPKVCEKLKA
HHHCCCHHHHHHHHH		54.57-
133 (in isoform 1)Ubiquitination-43.0421890473
133 (in isoform 2)Ubiquitination-43.0421890473
133UbiquitinationSLISAMIKNLKEQGV
HHHHHHHHHHHHCCC		43.0421890473
133UbiquitinationSLISAMIKNLKEQGV
HHHHHHHHHHHHCCC		43.0421890473
136UbiquitinationSAMIKNLKEQGVTFP
HHHHHHHHHCCCCCC		58.34-
136 (in isoform 2)Ubiquitination-58.34-
141PhosphorylationNLKEQGVTFPAIGSQ
HHHHCCCCCCCCCHH		30.6323186163
147PhosphorylationVTFPAIGSQAAEQAK
CCCCCCCHHHHHHHH		15.5523403867
154 (in isoform 2)Ubiquitination-49.4421890473
154UbiquitinationSQAAEQAKASPALVA
HHHHHHHHCCCCEEC		49.4421890473
154 (in isoform 1)Ubiquitination-49.4421890473
154UbiquitinationSQAAEQAKASPALVA
HHHHHHHHCCCCEEC		49.4421890473
156PhosphorylationAAEQAKASPALVAKD
HHHHHHCCCCEECCC		15.2525159151
162 (in isoform 1)Ubiquitination-57.9121890473
162 (in isoform 2)Ubiquitination-57.9121890473
162UbiquitinationASPALVAKDPGTVAN
CCCCEECCCCCCCCC		57.9120639865
170 (in isoform 1)Ubiquitination-52.3921890473
170AcetylationDPGTVANKKEEEDLA
CCCCCCCHHHHHHHH		52.3923749302
170 (in isoform 2)Ubiquitination-52.3921890473
170UbiquitinationDPGTVANKKEEEDLA
CCCCCCCHHHHHHHH		52.3921906983
171 (in isoform 2)Ubiquitination-70.8921890473
171 (in isoform 1)Ubiquitination-70.8921890473
171UbiquitinationPGTVANKKEEEDLAK
CCCCCCHHHHHHHHH		70.8921906983
178UbiquitinationKEEEDLAKAIELSLK
HHHHHHHHHHHHHHH		58.14-
183PhosphorylationLAKAIELSLKEQRQQ
HHHHHHHHHHHHHHH		25.3029514088
185 (in isoform 1)Ubiquitination-48.7221890473
185UbiquitinationKAIELSLKEQRQQST
HHHHHHHHHHHHHHC		48.7221890473
185UbiquitinationKAIELSLKEQRQQST
HHHHHHHHHHHHHHC		48.7221890473
185 (in isoform 2)Ubiquitination-48.7221890473
191PhosphorylationLKEQRQQSTTLSTLY
HHHHHHHHCCHHHHC		18.2821945579
192PhosphorylationKEQRQQSTTLSTLYP
HHHHHHHCCHHHHCC		27.6721945579
193PhosphorylationEQRQQSTTLSTLYPS
HHHHHHCCHHHHCCC		24.7721945579
195PhosphorylationRQQSTTLSTLYPSTS
HHHHCCHHHHCCCHH		17.8021945579
196PhosphorylationQQSTTLSTLYPSTSS
HHHCCHHHHCCCHHH		33.1621945579
198PhosphorylationSTTLSTLYPSTSSLL
HCCHHHHCCCHHHHH		8.6721945579
200PhosphorylationTLSTLYPSTSSLLTN
CHHHHCCCHHHHHHC		27.6221945579
201PhosphorylationLSTLYPSTSSLLTNH
HHHHCCCHHHHHHCC		20.1721945579
202PhosphorylationSTLYPSTSSLLTNHQ
HHHCCCHHHHHHCCC		24.2721945579
203PhosphorylationTLYPSTSSLLTNHQH
HHCCCHHHHHHCCCC		27.7321945579
206PhosphorylationPSTSSLLTNHQHEGR
CCHHHHHHCCCCCCC		35.6321945579
276 (in isoform 1)Ubiquitination-49.6921890473
276 (in isoform 2)Ubiquitination-49.6921890473
276UbiquitinationTAEPEMIKTEKKTVQ
CCCHHHCCCCCCEEE		49.692190698
276SumoylationTAEPEMIKTEKKTVQ
CCCHHHCCCCCCEEE		49.6928112733
279 (in isoform 2)Ubiquitination-60.00-
353UbiquitinationKLEDIDRKHSELSEL
HHHHHHHHCHHHHHH		47.97-
353 (in isoform 2)Ubiquitination-47.97-
355PhosphorylationEDIDRKHSELSELNV
HHHHHHCHHHHHHHH		43.1828348404
371PhosphorylationVMEALSLYTKLMNED
HHHHHHHHHHHCCCC		9.84-
372PhosphorylationMEALSLYTKLMNEDP
HHHHHHHHHHCCCCC		24.01-
381PhosphorylationLMNEDPMYSMYAKLQ
HCCCCCCHHHHHHHC		8.8221945579
382PhosphorylationMNEDPMYSMYAKLQN
CCCCCCHHHHHHHCC		10.0821945579
384PhosphorylationEDPMYSMYAKLQNQP
CCCCHHHHHHHCCCC		8.4721945579
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 STAM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAM1_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 STAM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HGS_HUMANHGSphysical
16189514
TIM8A_HUMANTIMM8Aphysical
12745081
STABP_HUMANSTAMBPphysical
10982817
STABP_HUMANSTAMBPphysical
10383417
JAK2_HUMANJAK2physical
9133424
JAK3_HUMANJAK3physical
9133424
STABP_HUMANSTAMBPphysical
17078930
UBC_HUMANUBCphysical
17078930
UBC_HUMANUBCphysical
16771824
ARRB1_HUMANARRB1physical
20505072
HGS_HUMANHGSphysical
20505072
UBP8_HUMANUSP8physical
20736164
CD79B_HUMANCD79Bphysical
17878339
STABP_HUMANSTAMBPphysical
16431367
UBC_HUMANUBCphysical
19111546
ITCH_HUMANITCHphysical
22275353
SC31A_HUMANSEC31Aphysical
19054391
HGS_HUMANHGSphysical
13679051
STAM2_HUMANSTAM2physical
13679051
ZRAB2_HUMANZRANB2physical
22939629
UBP34_HUMANUSP34physical
22939629
UBQL4_HUMANUBQLN4physical
22939629
STMN2_HUMANSTMN2physical
22939629
CHIP_HUMANSTUB1physical
22939629
TBCK_HUMANTBCKphysical
22939629
THADA_HUMANTHADAphysical
22939629
ZPR1_HUMANZPR1physical
22939629
UBQL2_HUMANUBQLN2physical
22939629
TPM2_HUMANTPM2physical
22939629
UNK_HUMANUNKphysical
22939629
UBC_HUMANUBCphysical
23314748
UBC_BOVINUBCphysical
20150893
UBE4B_HUMANUBE4Bphysical
24344129
HGS_HUMANHGSphysical
24344129
CHMP3_MOUSEChmp3physical
16431367
HGS_HUMANHGSphysical
24790097
UBC_HUMANUBCphysical
21187078
GGA1_HUMANGGA1physical
26344197
HGS_HUMANHGSphysical
20736164
UBC_HUMANUBCphysical
26601948
ARRD3_HUMANARRDC3physical
27226565
HGS_HUMANHGSphysical
28514442
TRAF7_HUMANTRAF7physical
28514442
NCEH1_HUMANNCEH1physical
28514442
SNX1_HUMANSNX1physical
28514442
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 STAM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASSSPECTROMETRY.
"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-198 AND TYR-384, 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-198, 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-381, AND MASSSPECTROMETRY.
"Tyrosine phosphorylation mapping of the epidermal growth factorreceptor signaling pathway.";
Steen H., Kuster B., Fernandez M., Pandey A., Mann M.;
J. Biol. Chem. 277:1031-1039(2002).
Cited for: PROTEIN SEQUENCE OF 189-213, INTERACTION WITH HGS, CLEAVAGE OFINITIATOR METHIONINE, PHOSPHORYLATION AT TYR-198, AND MASSSPECTROMETRY.

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