ATLA1_MOUSE - dbPTM
ATLA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATLA1_MOUSE
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.
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationKSRRDRNSWGGFSEK
CCCCCCCCCCCCCCC
28.1725521595
15PhosphorylationRNSWGGFSEKSSDWS
CCCCCCCCCCCCCCC
47.6025521595
18PhosphorylationWGGFSEKSSDWSSEE
CCCCCCCCCCCCCCC
29.4925521595
19PhosphorylationGGFSEKSSDWSSEEE
CCCCCCCCCCCCCCC
54.9225521595
22PhosphorylationSEKSSDWSSEEEEPV
CCCCCCCCCCCCCCC
32.6325521595
23PhosphorylationEKSSDWSSEEEEPVR
CCCCCCCCCCCCCCH
44.7825521595
31UbiquitinationEEEEPVRKAGPVQVL
CCCCCCHHCCCEEEE
58.9127667366
364UbiquitinationLAAVATAKDTYNKKM
HHHHHHHHHHCHHHH
46.3722790023
395AcetylationQSKHLQLKEESVKLF
HHCCHHHHHHHHHHH
46.61-
395UbiquitinationQSKHLQLKEESVKLF
HHCCHHHHHHHHHHH
46.6122790023

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 ATLA1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATLA1_MOUSE !!

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 ATLA1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ATLA1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATLA1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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