AMGO1_HUMAN - dbPTM
AMGO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMGO1_HUMAN
UniProt AC Q86WK6
Protein Name Amphoterin-induced protein 1
Gene Name AMIGO1 {ECO:0000312|HGNC:HGNC:20824}
Organism Homo sapiens (Human).
Sequence Length 493
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Perikaryon . Cell projection, dendrite . Cell projection, axon . Colocalizes with KCNB1 at high-density somatodendritic clusters on the surface of hippocampal and cortical neurons. Associated with
Protein Description Promotes growth and fasciculation of neurites from cultured hippocampal neurons. May be involved in fasciculation as well as myelination of developing neural axons. May have a role in regeneration as well as neural plasticity in the adult nervous system. May mediate homophilic as well as heterophilic cell-cell interaction and contribute to signal transduction through its intracellular domain. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1..
Protein Sequence MHPHRDPRGLWLLLPSLSLLLFEVARAGRAVVSCPAACLCASNILSCSKQQLPNVPHSLPSYTALLDLSHNNLSRLRAEWTPTRLTQLHSLLLSHNHLNFISSEAFSPVPNLRYLDLSSNQLRTLDEFLFSDLQVLEVLLLYNNHIMAVDRCAFDDMAQLQKLYLSQNQISRFPLELVKEGAKLPKLTLLDLSSNKLKNLPLPDLQKLPAWIKNGLYLHNNPLNCDCELYQLFSHWQYRQLSSVMDFQEDLYCMNSKKLHNVFNLSFLNCGEYKERAWEAHLGDTLIIKCDTKQQGMTKVWVTPSNERVLDEVTNGTVSVSKDGSLLFQQVQVEDGGVYTCYAMGETFNETLSVELKVHNFTLHGHHDTLNTAYTTLVGCILSVVLVLIYLYLTPCRCWCRGVEKPSSHQGDSLSSSMLSTTPNHDPMAGGDKDDGFDRRVAFLEPAGPGQGQNGKLKPGNTLPVPEATGKGQRRMSDPESVSSVFSDTPIVV
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
72N-linked_GlycosylationLLDLSHNNLSRLRAE
HEECCCCCHHHHHCC
33.69UniProtKB CARBOHYD
242PhosphorylationHWQYRQLSSVMDFQE
HHHHHHHHHHCCHHH
16.7322210691
256PhosphorylationEDLYCMNSKKLHNVF
HHHHHCCCHHHHCEE
12.3222210691
264N-linked_GlycosylationKKLHNVFNLSFLNCG
HHHHCEECCEEECCH
30.41UniProtKB CARBOHYD
315N-linked_GlycosylationRVLDEVTNGTVSVSK
CEEEECCCCEEEECC
49.68UniProtKB CARBOHYD
349N-linked_GlycosylationYAMGETFNETLSVEL
EEECCCCCCEEEEEE
49.08UniProtKB CARBOHYD
360N-linked_GlycosylationSVELKVHNFTLHGHH
EEEEEEEEEEEECCH
34.29UniProtKB CARBOHYD
462PhosphorylationGKLKPGNTLPVPEAT
CCCCCCCCCCCCCCC
38.0524719451
469PhosphorylationTLPVPEATGKGQRRM
CCCCCCCCCCCCCCC
37.4524719451
471UbiquitinationPVPEATGKGQRRMSD
CCCCCCCCCCCCCCC
47.7329967540
477PhosphorylationGKGQRRMSDPESVSS
CCCCCCCCCHHHHHH
48.4822617229
481PhosphorylationRRMSDPESVSSVFSD
CCCCCHHHHHHHHCC
32.4625850435
483PhosphorylationMSDPESVSSVFSDTP
CCCHHHHHHHHCCCC
30.0227732954
484PhosphorylationSDPESVSSVFSDTPI
CCHHHHHHHHCCCCC
25.6546162891

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 AMGO1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMGO1_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 AMGO1_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 AMGO1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND MASSSPECTROMETRY.

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