UniProt ID | ATLA1_MOUSE | |
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UniProt AC | Q8BH66 | |
Protein Name | Atlastin-1 | |
Gene Name | Atl1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 558 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . Golgi apparatus membrane Multi-pass membrane protein . Cell projection, axon . Localizes to endoplasmic reticulum tubular network. |
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Protein Description | GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development.. | |
Protein Sequence | MAKSRRDRNSWGGFSEKSSDWSSEEEEPVRKAGPVQVLIVKDDHSFELDEAALNRILLSQAVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMYNQESVDWVGDYNEPLTGFSWRGGSERETTGIQIWSEVFLINKLDGKKVAVLLMDTQGTFDSQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTEYGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNFDGKLKEIDDEFIKNLKILIPWLLSPERLDIKEINGNKITCRGLLEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVATAKDTYNKKMEEVCGGDKPFLAPNDLQSKHLQLKEESVKLFRGVKKMGGEEFSRRYLQQLESEIDELYIQYIKHNDSKNIFHAARTPATLFVVIFITYVIAGVTGFIGLDIIASLCNMIMGLTLITLCTWAYIRYSGEYRELGAVIDQVAAALWDQGSTNEALYKLYSAAATHRHLCHQAFPAPKSEPTQQPEKKKI | |
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 |
---|---|---|---|---|---|
10 | Phosphorylation | KSRRDRNSWGGFSEK CCCCCCCCCCCCCCC | 28.17 | 25521595 | |
15 | Phosphorylation | RNSWGGFSEKSSDWS CCCCCCCCCCCCCCC | 47.60 | 25521595 | |
18 | Phosphorylation | WGGFSEKSSDWSSEE CCCCCCCCCCCCCCC | 29.49 | 25521595 | |
19 | Phosphorylation | GGFSEKSSDWSSEEE CCCCCCCCCCCCCCC | 54.92 | 25521595 | |
22 | Phosphorylation | SEKSSDWSSEEEEPV CCCCCCCCCCCCCCC | 32.63 | 25521595 | |
23 | Phosphorylation | EKSSDWSSEEEEPVR CCCCCCCCCCCCCCH | 44.78 | 25521595 | |
31 | Ubiquitination | EEEEPVRKAGPVQVL CCCCCCHHCCCEEEE | 58.91 | 27667366 | |
364 | Ubiquitination | LAAVATAKDTYNKKM HHHHHHHHHHCHHHH | 46.37 | 22790023 | |
395 | Acetylation | QSKHLQLKEESVKLF HHCCHHHHHHHHHHH | 46.61 | - | |
395 | Ubiquitination | QSKHLQLKEESVKLF HHCCHHHHHHHHHHH | 46.61 | 22790023 |
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 ATLA1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of ATLA1_MOUSE !! |
* 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 ATLA1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ATLA1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-23, AND MASSSPECTROMETRY. | |
"Proteomic analysis of in vivo phosphorylated synaptic proteins."; Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.; J. Biol. Chem. 280:5972-5982(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22 AND SER-23,AND MASS SPECTROMETRY. |