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
72	N-linked_Glycosylation	LLDLSHNNLSRLRAE HEECCCCCHHHHHCC	33.69	UniProtKB CARBOHYD
242	Phosphorylation	HWQYRQLSSVMDFQE HHHHHHHHHHCCHHH	16.73	22210691
256	Phosphorylation	EDLYCMNSKKLHNVF HHHHHCCCHHHHCEE	12.32	22210691
264	N-linked_Glycosylation	KKLHNVFNLSFLNCG HHHHCEECCEEECCH	30.41	UniProtKB CARBOHYD
315	N-linked_Glycosylation	RVLDEVTNGTVSVSK CEEEECCCCEEEECC	49.68	UniProtKB CARBOHYD
349	N-linked_Glycosylation	YAMGETFNETLSVEL EEECCCCCCEEEEEE	49.08	UniProtKB CARBOHYD
360	N-linked_Glycosylation	SVELKVHNFTLHGHH EEEEEEEEEEEECCH	34.29	UniProtKB CARBOHYD
462	Phosphorylation	GKLKPGNTLPVPEAT CCCCCCCCCCCCCCC	38.05	24719451
469	Phosphorylation	TLPVPEATGKGQRRM CCCCCCCCCCCCCCC	37.45	24719451
471	Ubiquitination	PVPEATGKGQRRMSD CCCCCCCCCCCCCCC	47.73	29967540
477	Phosphorylation	GKGQRRMSDPESVSS CCCCCCCCCHHHHHH	48.48	22617229
481	Phosphorylation	RRMSDPESVSSVFSD CCCCCHHHHHHHHCC	32.46	25850435
483	Phosphorylation	MSDPESVSSVFSDTP CCCHHHHHHHHCCCC	30.02	27732954
484	Phosphorylation	SDPESVSSVFSDTPI CCHHHHHHHHCCCCC	25.65	46162891

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AMGO1_HUMAN !!

Functions of PTM Sites

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.

Oops, there are no SNP-PTM records of AMGO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AMGO1_HUMAN	AMIGO1	physical	12629050
AMGO2_HUMAN	AMIGO2	physical	12629050
AMGO3_HUMAN	AMIGO3	physical	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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.
PubMed: 18669648