MEMO1_HUMAN - dbPTM
MEMO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEMO1_HUMAN
UniProt AC Q9Y316
Protein Name Protein MEMO1
Gene Name MEMO1
Organism Homo sapiens (Human).
Sequence Length 297
Subcellular Localization
Protein Description May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration..
Protein Sequence MSNRVVCREASHAGSWYTASGPQLNAQLEGWLSQVQSTKRPARAIIAPHAGYTYCGSCAAHAYKQVDPSITRRIFILGPSHHVPLSRCALSSVDIYRTPLYDLRIDQKIYGELWKTGMFERMSLQTDEDEHSIEMHLPYTAKAMESHKDEFTIIPVLVGALSESKEQEFGKLFSKYLADPSNLFVVSSDFCHWGQRFRYSYYDESQGEIYRSIEHLDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQKNGMNMSFSFLNYAQSSQCRNWQDSSVSYAAGALTVH
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
37PhosphorylationGWLSQVQSTKRPARA
HHHHHHHCCCCCCCE		36.72-
38PhosphorylationWLSQVQSTKRPARAI
HHHHHHCCCCCCCEE		17.62-
52PhosphorylationIIAPHAGYTYCGSCA
EECCCCCCCCCHHHH		8.7028152594
53PhosphorylationIAPHAGYTYCGSCAA
ECCCCCCCCCHHHHH		16.0628152594
54PhosphorylationAPHAGYTYCGSCAAH
CCCCCCCCCHHHHHH		6.0728152594
64AcetylationSCAAHAYKQVDPSIT
HHHHHHHHHCCHHHC		44.6326051181
69PhosphorylationAYKQVDPSITRRIFI
HHHHCCHHHCEEEEE		31.9326437602
71PhosphorylationKQVDPSITRRIFILG
HHCCHHHCEEEEEEC		20.4521406692
80PhosphorylationRIFILGPSHHVPLSR
EEEEECCCCCCCHHH		25.15-
86PhosphorylationPSHHVPLSRCALSSV
CCCCCCHHHHCCCCC		21.1726437602
92UbiquitinationLSRCALSSVDIYRTP
HHHHCCCCCEEECCC		25.3421890473
108UbiquitinationYDLRIDQKIYGELWK
CCCCCCHHHHHHHHH		33.8621890473
110PhosphorylationLRIDQKIYGELWKTG
CCCCHHHHHHHHHCC		16.1626074081
111UbiquitinationRIDQKIYGELWKTGM
CCCHHHHHHHHHCCC		27.30-
115UbiquitinationKIYGELWKTGMFERM
HHHHHHHHCCCCEEE		48.0721890473
116PhosphorylationIYGELWKTGMFERMS
HHHHHHHCCCCEEEE		23.4626074081
118UbiquitinationGELWKTGMFERMSLQ
HHHHHCCCCEEEECC		3.6921890473
123PhosphorylationTGMFERMSLQTDEDE
CCCCEEEECCCCCCC		24.4426074081
126PhosphorylationFERMSLQTDEDEHSI
CEEEECCCCCCCCEE		46.8026074081
148UbiquitinationAKAMESHKDEFTIIP
HHHHHHCCCCCCHHH		69.132190698
151UbiquitinationMESHKDEFTIIPVLV
HHHCCCCCCHHHHHH		9.48-
165UbiquitinationVGALSESKEQEFGKL
HHHCCCCHHHHHHHH		60.40-
171UbiquitinationSKEQEFGKLFSKYLA
CHHHHHHHHHHHHHC		52.24-
174PhosphorylationQEFGKLFSKYLADPS
HHHHHHHHHHHCCHH		30.7224719451
178UbiquitinationKLFSKYLADPSNLFV
HHHHHHHCCHHHEEE		24.47-
199PhosphorylationHWGQRFRYSYYDESQ
CCCCCCCCEEECCCC		9.7920068231
200PhosphorylationWGQRFRYSYYDESQG
CCCCCCCEEECCCCC		16.9820068231
201PhosphorylationGQRFRYSYYDESQGE
CCCCCCEEECCCCCE		13.1520068231
202PhosphorylationQRFRYSYYDESQGEI
CCCCCEEECCCCCEE		13.8020068231
205PhosphorylationRYSYYDESQGEIYRS
CCEEECCCCCEEECC		40.3625348954
210PhosphorylationDESQGEIYRSIEHLD
CCCCCEEECCHHHHH		8.2621082442
212PhosphorylationSQGEIYRSIEHLDKM
CCCEEECCHHHHHHH		18.5028064214
231PhosphorylationIEQLDPVSFSNYLKK
HHHCCCCCHHHHHHH		28.4824719451
238UbiquitinationSFSNYLKKYHNTICG
CHHHHHHHHCCCCCC		49.50-
295PhosphorylationSYAAGALTVH-----
HHHCCCCCCC-----		18.92-
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 MEMO1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MEMO1_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 MEMO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LZTS2_HUMANLZTS2physical
25416956
LNX1_HUMANLNX1physical
25416956
RBM45_HUMANRBM45physical
25416956
UBE3D_HUMANUBE3Dphysical
26186194
RENT1_HUMANUPF1physical
26186194
ANFY1_HUMANANKFY1physical
26186194
DICER_HUMANDICER1physical
26186194
KTU_HUMANDNAAF2physical
26186194
HMBX1_HUMANHMBOX1physical
26186194
WDR54_HUMANWDR54physical
26186194
TRBP2_HUMANTARBP2physical
26186194
COF2_HUMANCFL2physical
26344197
TACC1_HUMANTACC1physical
21516116
HMBX1_HUMANHMBOX1physical
28514442
KTU_HUMANDNAAF2physical
28514442
UBE3D_HUMANUBE3Dphysical
28514442
WDR54_HUMANWDR54physical
28514442
RENT1_HUMANUPF1physical
28514442
COPRS_HUMANCOPRSphysical
28514442
TRBP2_HUMANTARBP2physical
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 MEMO1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-210, AND MASSSPECTROMETRY.

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