AMGO3_HUMAN - dbPTM
AMGO3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMGO3_HUMAN
UniProt AC Q86WK7
Protein Name Amphoterin-induced protein 3
Gene Name AMIGO3 {ECO:0000312|EMBL:AAO48944.1}
Organism Homo sapiens (Human).
Sequence Length 504
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description May mediate heterophilic cell-cell interaction. May contribute to signal transduction through its intracellular domain (By similarity)..
Protein Sequence MTWLVLLGTLLCMLRVGLGTPDSEGFPPRALHNCPYKCICAADLLSCTGLGLQDVPAELPAATADLDLSHNALQRLRPGWLAPLFQLRALHLDHNELDALGRGVFVNASGLRLLDLSSNTLRALGRHDLDGLGALEKLLLFNNRLVHLDEHAFHGLRALSHLYLGCNELASFSFDHLHGLSATHLLTLDLSSNRLGHISVPELAALPAFLKNGLYLHNNPLPCDCRLYHLLQRWHQRGLSAVRDFAREYVCLAFKVPASRVRFFQHSRVFENCSSAPALGLERPEEHLYALVGRSLRLYCNTSVPAMRIAWVSPQQELLRAPGSRDGSIAVLADGSLAIGNVQEQHAGLFVCLATGPRLHHNQTHEYNVSVHFPRPEPEAFNTGFTTLLGCAVGLVLVLLYLFAPPCRCCRRACRCRRWPQTPSPLQELSAQSSVLSTTPPDAPSRKASVHKHVVFLEPGRRGLNGRVQLAVAEEFDLYNPGGLQLKAGSESASSIGSEGPMTT
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
20PhosphorylationMLRVGLGTPDSEGFP
HHHHCCCCCCCCCCC
29.0323663014
23PhosphorylationVGLGTPDSEGFPPRA
HCCCCCCCCCCCHHH
40.6023663014
107N-linked_GlycosylationLGRGVFVNASGLRLL
HCCCEEECCCCCEEE
19.54UniProtKB CARBOHYD
117PhosphorylationGLRLLDLSSNTLRAL
CCEEEECCHHHHHHC
22.6227732954
118PhosphorylationLRLLDLSSNTLRALG
CEEEECCHHHHHHCC
40.9227732954
120PhosphorylationLLDLSSNTLRALGRH
EEECCHHHHHHCCCC
21.4027732954
137AcetylationDGLGALEKLLLFNNR
CHHHHHHHHHHCCCE
45.337695407
272N-linked_GlycosylationQHSRVFENCSSAPAL
ECCHHCCCCCCCCCC
21.36UniProtKB CARBOHYD
295PhosphorylationLYALVGRSLRLYCNT
HHHHHHCHHHHHHCC
16.3524719451
301N-linked_GlycosylationRSLRLYCNTSVPAMR
CHHHHHHCCCCCCCE
23.10UniProtKB CARBOHYD
324PhosphorylationELLRAPGSRDGSIAV
HHHCCCCCCCCCEEE
26.5824719451
362N-linked_GlycosylationTGPRLHHNQTHEYNV
CCCCCCCCCCEEEEE
37.38UniProtKB CARBOHYD
368N-linked_GlycosylationHNQTHEYNVSVHFPR
CCCCEEEEEEEECCC
19.32UniProtKB CARBOHYD
449PhosphorylationDAPSRKASVHKHVVF
CCCCCCCEECEEEEE
27.9924719451
490PhosphorylationGLQLKAGSESASSIG
CCEEECCCCCCCCCC
32.9868698503
492PhosphorylationQLKAGSESASSIGSE
EEECCCCCCCCCCCC
34.8468698509
494PhosphorylationKAGSESASSIGSEGP
ECCCCCCCCCCCCCC
31.5968698515

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 AMGO3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMGO3_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 AMGO3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AMGO1_HUMANAMIGO1physical
12629050
AMGO2_HUMANAMIGO2physical
12629050
AMGO3_HUMANAMIGO3physical
12629050
TM268_HUMANC9orf91physical
28514442
GOLP3_HUMANGOLPH3physical
28514442
C1QL4_HUMANC1QL4physical
28514442
FBX2_HUMANFBXO2physical
28514442
SE1L1_HUMANSEL1Lphysical
28514442
UFSP2_HUMANUFSP2physical
28514442
CALX_HUMANCANXphysical
28514442
S22AI_HUMANSLC22A18physical
28514442
OMA1_HUMANOMA1physical
28514442
ZDH17_HUMANZDHHC17physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMGO3_HUMAN

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Related Literatures of Post-Translational Modification

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