UniProt ID | AMGO1_HUMAN | |
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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 |
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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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
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 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of AMGO1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of AMGO1_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AMGO1_HUMAN | AMIGO1 | physical | 12629050 | |
AMGO2_HUMAN | AMIGO2 | physical | 12629050 | |
AMGO3_HUMAN | AMIGO3 | physical | 12629050 |
Kegg Disease | ||||||
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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. |
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Phosphorylation | |
Reference | PubMed |
"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. |