ATLA1_HUMAN - dbPTM
ATLA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATLA1_HUMAN
UniProt AC Q8WXF7
Protein Name Atlastin-1
Gene Name ATL1
Organism Homo sapiens (Human).
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 (PubMed:27619977).
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. [PubMed: 27619977 May also regulate Golgi biogenesis. May regulate axonal development.]
Protein Sequence MAKNRRDRNSWGGFSEKTYEWSSEEEEPVKKAGPVQVLIVKDDHSFELDETALNRILLSEAVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMYNQESVDWVGDYNEPLTGFSWRGGSERETTGIQIWSEIFLINKPDGKKVAVLLMDTQGTFDSQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTEYGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNFDGKLKEIDDEFIKNLKILIPWLLSPESLDIKEINGNKITCRGLVEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVATAKDTYNKKMEEICGGDKPFLAPNDLQTKHLQLKEESVKLFRGVKKMGGEEFSRRYLQQLESEIDELYIQYIKHNDSKNIFHAARTPATLFVVIFITYVIAGVTGFIGLDIIASLCNMIMGLTLITLCTWAYIRYSGEYRELGAVIDQVAAALWDQGSTNEALYKLYSAAATHRHLYHQAFPTPKSESTEQSEKKKM
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
10PhosphorylationKNRRDRNSWGGFSEK
CCCCCCCCCCCCCCC
28.1723401153
15PhosphorylationRNSWGGFSEKTYEWS
CCCCCCCCCCCCCCC
41.2723927012
18PhosphorylationWGGFSEKTYEWSSEE
CCCCCCCCCCCCCCC
23.7123090842
19PhosphorylationGGFSEKTYEWSSEEE
CCCCCCCCCCCCCCC
26.8623090842
22PhosphorylationSEKTYEWSSEEEEPV
CCCCCCCCCCCCCCC
18.8725159151
23PhosphorylationEKTYEWSSEEEEPVK
CCCCCCCCCCCCCCC
50.5325159151
45PhosphorylationLIVKDDHSFELDETA
EEEECCCCCCCCHHH
27.66-
59PhosphorylationALNRILLSEAVRDKE
HHHHHHHHHHHCCCC
21.7723909892
71PhosphorylationDKEVVAVSVAGAFRK
CCCEEEEEEEHHHHC
9.12-
287UbiquitinationPNFDGKLKEIDDEFI
CCCCCCCCCCCHHHH
56.99-
334UbiquitinationEYFKAYIKIYQGEEL
HHHHHHHHHHCCCCC
23.7621890473
334UbiquitinationEYFKAYIKIYQGEEL
HHHHHHHHHHCCCCC
23.7621890473
346PhosphorylationEELPHPKSMLQATAE
CCCCCCHHHHHHHHH
29.2222210691
351PhosphorylationPKSMLQATAEANNLA
CHHHHHHHHHHHCHH
16.4522210691
362PhosphorylationNNLAAVATAKDTYNK
HCHHHHHHHHHHCHH
27.8630622161
395AcetylationQTKHLQLKEESVKLF
CCCCHHHHHHHHHHH
46.61-
400UbiquitinationQLKEESVKLFRGVKK
HHHHHHHHHHHHHHH
51.71-
414PhosphorylationKMGGEEFSRRYLQQL
HHCHHHHHHHHHHHH
21.09-
429PhosphorylationESEIDELYIQYIKHN
HHHHHHHHHHHHHHC
5.50-
432PhosphorylationIDELYIQYIKHNDSK
HHHHHHHHHHHCCCC
11.46-
520 (in isoform 2)Phosphorylation-43.8526503514
544PhosphorylationLYHQAFPTPKSESTE
HHHCCCCCCCCCCCC
36.5728555341

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATLA1_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 ATLA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEY1_YEASTSEY1genetic
22508509
YOP1_YEASTYOP1genetic
22508509

Drug and Disease Associations
Kegg Disease
H00266 Hereditary spastic paraplegia (SPG)
OMIM Disease
182600Spastic paraplegia 3, autosomal dominant (SPG3)
613708Neuropathy, hereditary sensory, 1D (HSN1D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATLA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-23, AND MASSSPECTROMETRY.

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