AMGO2_HUMAN - dbPTM
AMGO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMGO2_HUMAN
UniProt AC Q86SJ2
Protein Name Amphoterin-induced protein 2
Gene Name AMIGO2 {ECO:0000312|EMBL:AAH47595.1}
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Nucleus. Associated with nucleus as well as plasma membrane. Restricted to somata of cerebellar as well as hippocampal neurons (By similarity)..
Protein Description Required for depolarization-dependent survival of cultured cerebellar granule neurons. May mediate homophilic as well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3. May contribute to signal transduction through its intracellular domain. May be required for tumorigenesis of a subset of gastric adenocarcinomas..
Protein Sequence MSLRVHTLPTLLGAVVRPGCRELLCLLMITVTVGPGASGVCPTACICATDIVSCTNKNLSKVPGNLFRLIKRLDLSYNRIGLLDSEWIPVSFAKLNTLILRHNNITSISTGSFSTTPNLKCLDLSSNKLKTVKNAVFQELKVLEVLLLYNNHISYLDPSAFGGLSQLQKLYLSGNFLTQFPMDLYVGRFKLAELMFLDVSYNRIPSMPMHHINLVPGKQLRGIYLHGNPFVCDCSLYSLLVFWYRRHFSSVMDFKNDYTCRLWSDSRHSRQVLLLQDSFMNCSDSIINGSFRALGFIHEAQVGERLMVHCDSKTGNANTDFIWVGPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMNKQRLLNETVDVTINVSNFTVSRSHAHEAFNTAFTTLAACVASIVLVLLYLYLTPCPCKCKTKRQKNMLHQSNAHSSILSPGPASDASADERKAGAGKRVVFLEPLKDTAAGQNGKVRLFPSEAVIAEGILKSTRGKSDSDSVNSVFSDTPFVAST
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
58N-linked_GlycosylationIVSCTNKNLSKVPGN
HHHCCCCCHHCCCCC		52.17UniProtKB CARBOHYD
104N-linked_GlycosylationTLILRHNNITSISTG
EEEHHCCCCCEEECC		32.56UniProtKB CARBOHYD
173PhosphorylationQLQKLYLSGNFLTQF
HHHHHHHCCCHHHCC		20.3822210691
200PhosphorylationELMFLDVSYNRIPSM
HHHCCCCCCCCCCCC		19.1622210691
201PhosphorylationLMFLDVSYNRIPSMP
HHCCCCCCCCCCCCC		14.3322210691
281N-linked_GlycosylationLLQDSFMNCSDSIIN
EEEHHHCCCCHHHHH		21.82UniProtKB CARBOHYD
288N-linked_GlycosylationNCSDSIINGSFRALG
CCCHHHHHCCHHHHC		38.08UniProtKB CARBOHYD
345N-linked_GlycosylationENFYVFHNGSLVIES
CCEEEEECCEEEECC		30.22UniProtKB CARBOHYD
373N-linked_GlycosylationMNKQRLLNETVDVTI
ECHHHHHCCEEEEEE		47.70UniProtKB CARBOHYD
381N-linked_GlycosylationETVDVTINVSNFTVS
CEEEEEEEECCCEEE		23.07UniProtKB CARBOHYD
384N-linked_GlycosylationDVTINVSNFTVSRSH
EEEEEECCCEEECHH		32.12UniProtKB CARBOHYD
432UbiquitinationKCKTKRQKNMLHQSN
CCCCHHHHCCCCCCC		48.64-
438PhosphorylationQKNMLHQSNAHSSIL
HHCCCCCCCCCCCCC		25.8229514088
442PhosphorylationLHQSNAHSSILSPGP
CCCCCCCCCCCCCCC		19.3629514088
443PhosphorylationHQSNAHSSILSPGPA
CCCCCCCCCCCCCCC		20.0663761241
446PhosphorylationNAHSSILSPGPASDA
CCCCCCCCCCCCCCC		26.5829514088
451PhosphorylationILSPGPASDASADER
CCCCCCCCCCCHHHH		36.5223312004
454PhosphorylationPGPASDASADERKAG
CCCCCCCCHHHHHCC		41.0423312004
473UbiquitinationVVFLEPLKDTAAGQN
EEEEEECCCCCCCCC		64.84-
482UbiquitinationTAAGQNGKVRLFPSE
CCCCCCCEEEECCCH		31.56-
488PhosphorylationGKVRLFPSEAVIAEG
CEEEECCCHHHHHHH		30.7429514088
498UbiquitinationVIAEGILKSTRGKSD
HHHHHHHHHCCCCCC		48.11-
504PhosphorylationLKSTRGKSDSDSVNS
HHHCCCCCCHHCHHH		45.2129514088
506PhosphorylationSTRGKSDSDSVNSVF
HCCCCCCHHCHHHHC		38.5930266825
508PhosphorylationRGKSDSDSVNSVFSD
CCCCCHHCHHHHCCC		27.4425849741
511PhosphorylationSDSDSVNSVFSDTPF
CCHHCHHHHCCCCCC		23.5322210691
514PhosphorylationDSVNSVFSDTPFVAS
HCHHHHCCCCCCEEC		38.1229514088
516PhosphorylationVNSVFSDTPFVAST-
HHHHCCCCCCEECC-		19.8929514088
521PhosphorylationSDTPFVAST------
CCCCCEECC------		29.3729514088
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 AMGO2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMGO2_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 AMGO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AMGO1_HUMANAMIGO1physical
12629050
AMGO2_HUMANAMIGO2physical
12629050
AMGO3_HUMANAMIGO3physical
12629050
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 AMGO2_HUMAN

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Related Literatures of Post-Translational Modification

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