HGS_MOUSE - dbPTM
HGS_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HGS_MOUSE
UniProt AC Q99LI8
Protein Name Hepatocyte growth factor-regulated tyrosine kinase substrate
Gene Name Hgs
Organism Mus musculus (Mouse).
Sequence Length 775
Subcellular Localization Cytoplasm. Early endosome membrane
Peripheral membrane protein
Cytoplasmic side. Endosome, multivesicular body membrane
Peripheral membrane protein. Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartmen
Protein Description Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (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. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation..
Protein Sequence MGRGSGTFERLLDKATSQLLLETDWESILQICDLIRQGDTQAKYAVNSIKKKVNDKNPHVALYALEVMESVVKNCGQTVHDEVANKQTMEELKELLKRQVEVNVRNKILYLIQAWAHAFRNEPKYKVVQDTYQIMKVEGHVFPEFKESDAMFAAERAPDWVDAEECHRCRVQFGVVTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLNKKAEGKASSTTELPPEYLTSPLSQQSQLPPKRDETALQEEEELQLALALSQSEAEEKERMRQKTTYTAHPKAEPTPLASSAPPAGSLYSSPVNSSAPLAEDIDPELARYLNRNYWEKKQEEARKSPTPSAPVPLTEPAAQPGEGHTAPNSMAEAPLPETDSQPITPCSGPFSEYQNGESEESHEQFLKALQNAVSTFVNRMKSNHMRGRSITNDSAVLSLFQSINTMHPQLLELLNQLDERRLYYEGLQDKLAQIRDARGALSALREEHREKLRRAAEEAERQRQIQLAQKLEIMRQKKQEYLEVQRQLAIQRLQEQEKERQMRLEQQKQTVQMRAQMPAFPLPYAQLQAMPTAGGVLYQPSGPTSFPATFSPAGSVEGSPMHGVYMSQPAPATGPYPSMPGTTADPSMVSAYMYPTGAPGAQAAPQAQAGPTTSPAYSSYQPTPTPGYQSVASQAPQSLPAISQPPQTSNIGYMGSQPMSMGYQPYNMQNLMTALPGQDASLPAQQPYIPGQQPLYQQMAPSTGPPQQQPPVAQPAPTQGPPAQGSEAQLISFD
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
86UbiquitinationVHDEVANKQTMEELK
HHHHHHCHHHHHHHH		37.09-
93UbiquitinationKQTMEELKELLKRQV
HHHHHHHHHHHHHHC		49.98-
126UbiquitinationFRNEPKYKVVQDTYQ
HHCCCCCCEEECHHH		41.89-
131PhosphorylationKYKVVQDTYQIMKVE
CCCEEECHHHHHEEC		10.5522499769
132PhosphorylationYKVVQDTYQIMKVEG
CCEEECHHHHHEECC		12.3422499769
146UbiquitinationGHVFPEFKESDAMFA
CCCCCCCCHHHHCHH		55.43-
207AcetylationIPKFGIEKEVRVCEP
CCCCCCCCEEEECHH		60.64-
216PhosphorylationVRVCEPCYEQLNKKA
EEECHHHHHHHHHHH		19.8825521595
221UbiquitinationPCYEQLNKKAEGKAS
HHHHHHHHHHCCCCC		63.05-
222UbiquitinationCYEQLNKKAEGKASS
HHHHHHHHHCCCCCC		51.07-
228PhosphorylationKKAEGKASSTTELPP
HHHCCCCCCCCCCCH		31.5324925903
229PhosphorylationKAEGKASSTTELPPE
HHCCCCCCCCCCCHH		44.1824925903
230PhosphorylationAEGKASSTTELPPEY
HCCCCCCCCCCCHHH		23.0724925903
231PhosphorylationEGKASSTTELPPEYL
CCCCCCCCCCCHHHH		37.1624925903
237PhosphorylationTTELPPEYLTSPLSQ
CCCCCHHHHCCCHHH		22.5124925903
239PhosphorylationELPPEYLTSPLSQQS
CCCHHHHCCCHHHCC		27.6525521595
240PhosphorylationLPPEYLTSPLSQQSQ
CCHHHHCCCHHHCCC		22.6525521595
243PhosphorylationEYLTSPLSQQSQLPP
HHHCCCHHHCCCCCC		29.5625521595
246PhosphorylationTSPLSQQSQLPPKRD
CCCHHHCCCCCCCCC		26.5024925903
270PhosphorylationLQLALALSQSEAEEK
HHHHHHHCHHHHHHH		26.5029899451
285PhosphorylationERMRQKTTYTAHPKA
HHHHHHCCCCCCCCC		26.3825367039
286PhosphorylationRMRQKTTYTAHPKAE
HHHHHCCCCCCCCCC		13.7325367039
287PhosphorylationMRQKTTYTAHPKAEP
HHHHCCCCCCCCCCC		19.1925367039
295PhosphorylationAHPKAEPTPLASSAP
CCCCCCCCCCCCCCC		23.5725777480
299PhosphorylationAEPTPLASSAPPAGS
CCCCCCCCCCCCCCC		34.4125777480
300PhosphorylationEPTPLASSAPPAGSL
CCCCCCCCCCCCCCC		38.9124453211
306PhosphorylationSSAPPAGSLYSSPVN
CCCCCCCCCCCCCCC		26.6626643407
308PhosphorylationAPPAGSLYSSPVNSS
CCCCCCCCCCCCCCC		14.5926643407
309PhosphorylationPPAGSLYSSPVNSSA
CCCCCCCCCCCCCCC		33.2026643407
310PhosphorylationPAGSLYSSPVNSSAP
CCCCCCCCCCCCCCC		21.2225521595
314PhosphorylationLYSSPVNSSAPLAED
CCCCCCCCCCCCHHC		28.2826643407
315PhosphorylationYSSPVNSSAPLAEDI
CCCCCCCCCCCHHCC		28.8026643407
329PhosphorylationIDPELARYLNRNYWE
CCHHHHHHHHHHHHH		11.6122817900
334PhosphorylationARYLNRNYWEKKQEE
HHHHHHHHHHHHHHH		16.2322817900
345PhosphorylationKQEEARKSPTPSAPV
HHHHHHCCCCCCCCC		28.5820139300
471UbiquitinationYYEGLQDKLAQIRDA
HHHHHHHHHHHHHHH		32.53-
511UbiquitinationRQIQLAQKLEIMRQK
HHHHHHHHHHHHHHH		42.34-
519UbiquitinationLEIMRQKKQEYLEVQ
HHHHHHHHHHHHHHH		39.77-
522PhosphorylationMRQKKQEYLEVQRQL
HHHHHHHHHHHHHHH		12.9829514104
549SuccinylationQMRLEQQKQTVQMRA
HHHHHHHHHHHHHHH		47.8623806337
549SuccinylationQMRLEQQKQTVQMRA
HHHHHHHHHHHHHHH		47.86-
549UbiquitinationQMRLEQQKQTVQMRA
HHHHHHHHHHHHHHH		47.86-
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
-KUbiquitinationE3 ubiquitin ligaseCblP22682
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HGS_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 HGS_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAM2_MOUSEStam2physical
10651905
HGS_MOUSEHgsphysical
16615908
STAM2_MOUSEStam2physical
12972556
UBC_HUMANUBCphysical
12972556
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HGS_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND MASSSPECTROMETRY.
"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-216, AND MASSSPECTROMETRY.
"The UIM domain of Hrs couples receptor sorting to vesicleformation.";
Urbe S., Sachse M., Row P.E., Preisinger C., Barr F.A., Strous G.,Klumperman J., Clague M.J.;
J. Cell Sci. 116:4169-4179(2003).
Cited for: PHOSPHORYLATION AT TYR-329 AND TYR-334, MASS SPECTROMETRY, MUTAGENESISOF LEU-269; SER-270; TYR-329 AND TYR-334, AND SUBCELLULAR LOCATION.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory