ATAD1_HUMAN - dbPTM
ATAD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATAD1_HUMAN
UniProt AC Q8NBU5
Protein Name ATPase family AAA domain-containing protein 1
Gene Name ATAD1
Organism Homo sapiens (Human).
Sequence Length 361
Subcellular Localization Peroxisome . Cell junction, synapse, postsynaptic cell membrane .
Protein Description ATPase that plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent (By similarity)..
Protein Sequence MVHAEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDPLNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEESHDEDEIRPVQQQDLHRAIEKMKKSKDAAFQNVLTHVCLD
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
7Ubiquitination-MVHAEAFSRPLSRN
-CCCHHHCCCCCCHH		4.8527667366
8PhosphorylationMVHAEAFSRPLSRNE
CCCHHHCCCCCCHHH		39.7821406692
12PhosphorylationEAFSRPLSRNEVVGL
HHCCCCCCHHHHHHH		35.4221406692
25UbiquitinationGLIFRLTIFGAVTYF
HHHHHHHHHCHHHHH		3.3832015554
29UbiquitinationRLTIFGAVTYFTIKW
HHHHHCHHHHHHHHH		4.5729967540
44PhosphorylationMVDAIDPTRKQKVEA
HHHCCCCCHHHHHHH		46.9120068231
46UbiquitinationDAIDPTRKQKVEAQK
HCCCCCHHHHHHHHH		57.8822817900
53"N6,N6-dimethyllysine"KQKVEAQKQAEKLMK
HHHHHHHHHHHHHHH		59.53-
53MethylationKQKVEAQKQAEKLMK
HHHHHHHHHHHHHHH		59.53-
54UbiquitinationQKVEAQKQAEKLMKQ
HHHHHHHHHHHHHHH		42.5521890473
55UbiquitinationKVEAQKQAEKLMKQI
HHHHHHHHHHHHHHH		23.9522817900
56UbiquitinationVEAQKQAEKLMKQIG
HHHHHHHHHHHHHHC		44.2022817900
60UbiquitinationKQAEKLMKQIGVKNV
HHHHHHHHHHCCCCC		49.5629967540
60MethylationKQAEKLMKQIGVKNV
HHHHHHHHHHCCCCC		49.56-
60"N6,N6-dimethyllysine"KQAEKLMKQIGVKNV
HHHHHHHHHHCCCCC		49.56-
65UbiquitinationLMKQIGVKNVKLSEY
HHHHHCCCCCCCCHH		51.3027667366
652-HydroxyisobutyrylationLMKQIGVKNVKLSEY
HHHHHCCCCCCCCHH		51.30-
107UbiquitinationITDLKDTVILPIKKK
HHHCCCCEEEEECHH		6.4122817900
1122-HydroxyisobutyrylationDTVILPIKKKHLFEN
CCEEEEECHHHHHCC		54.55-
112 (in isoform 1)Ubiquitination-54.5521890473
112UbiquitinationDTVILPIKKKHLFEN
CCEEEEECHHHHHCC		54.5522817900
112 (in isoform 2)Ubiquitination-54.5521890473
113UbiquitinationTVILPIKKKHLFENS
CEEEEECHHHHHCCC		46.2622817900
114UbiquitinationVILPIKKKHLFENSR
EEEEECHHHHHCCCC		40.3027667366
114AcetylationVILPIKKKHLFENSR
EEEEECHHHHHCCCC		40.3019608861
127UbiquitinationSRLLQPPKGVLLYGP
CCCCCCCCEEEEECC		69.2329967540
132PhosphorylationPPKGVLLYGPPGCGK
CCCEEEEECCCCCCH		24.35-
137S-nitrosylationLLYGPPGCGKTLIAK
EEECCCCCCHHHHHH		6.6121278135
137S-nitrosocysteineLLYGPPGCGKTLIAK
EEECCCCCCHHHHHH		6.61-
139UbiquitinationYGPPGCGKTLIAKAT
ECCCCCCHHHHHHHH		44.2129967540
144AcetylationCGKTLIAKATAKEAG
CCHHHHHHHHHHHHC		39.0025953088
144UbiquitinationCGKTLIAKATAKEAG
CCHHHHHHHHHHHHC		39.0027667366
146PhosphorylationKTLIAKATAKEAGCR
HHHHHHHHHHHHCCE		37.2419413330
148UbiquitinationLIAKATAKEAGCRFI
HHHHHHHHHHCCEEE		43.6829967540
151UbiquitinationKATAKEAGCRFINLQ
HHHHHHHCCEEEECC		12.2933845483
155UbiquitinationKEAGCRFINLQPSTL
HHHCCEEEECCCCCC		2.3227667366
165UbiquitinationQPSTLTDKWYGESQK
CCCCCCCCCCCHHHH		36.7621906983
165 (in isoform 2)Ubiquitination-36.7621890473
165 (in isoform 1)Ubiquitination-36.7621890473
165AcetylationQPSTLTDKWYGESQK
CCCCCCCCCCCHHHH		36.7626051181
167PhosphorylationSTLTDKWYGESQKLA
CCCCCCCCCHHHHHH		19.4326657352
181UbiquitinationAAAVFSLAIKLQPSI
HHHHHHHHHHHCCEE		8.8221963094
202PhosphorylationDSFLRNRSSSDHEAT
HHHHHCCCCCHHHHH		37.43-
203PhosphorylationSFLRNRSSSDHEATA
HHHHCCCCCHHHHHH		36.2333259812
204PhosphorylationFLRNRSSSDHEATAM
HHHCCCCCHHHHHHH		44.21-
205UbiquitinationLRNRSSSDHEATAMM
HHCCCCCHHHHHHHH		45.6627667366
209PhosphorylationSSSDHEATAMMKAQF
CCCHHHHHHHHHHHH		16.46-
212UbiquitinationDHEATAMMKAQFMSL
HHHHHHHHHHHHHHH		2.7821890473
216UbiquitinationTAMMKAQFMSLWDGL
HHHHHHHHHHHHCCC		4.2522817900
228UbiquitinationDGLDTDHSCQVIVMG
CCCCCCCCCEEEEEC		14.7329967540
240UbiquitinationVMGATNRPQDLDSAI
EECCCCCCCCHHHHH		33.8221890473
242UbiquitinationGATNRPQDLDSAIMR
CCCCCCCCHHHHHHH		55.9421963094
244UbiquitinationTNRPQDLDSAIMRRM
CCCCCCHHHHHHHHC		44.2922817900
263 (in isoform 1)Ubiquitination-49.7921890473
263 (in isoform 2)Ubiquitination-49.7921890473
2632-HydroxyisobutyrylationHINQPALKQREAILK
CCCCHHHHHHHHHHH		49.79-
263UbiquitinationHINQPALKQREAILK
CCCCHHHHHHHHHHH		49.7927667366
270 (in isoform 1)Ubiquitination-27.6321890473
270 (in isoform 2)Ubiquitination-27.6321890473
270UbiquitinationKQREAILKLILKNEN
HHHHHHHHHHHHCCC		27.6321963094
274UbiquitinationAILKLILKNENVDRH
HHHHHHHHCCCCHHH		56.0427667366
274AcetylationAILKLILKNENVDRH
HHHHHHHHCCCCHHH		56.0419829937
274 (in isoform 1)Ubiquitination-56.0421890473
280MethylationLKNENVDRHVDLLEV
HHCCCCHHHCHHHHH		27.70-
292PhosphorylationLEVAQETDGFSGSDL
HHHHHHCCCCCHHHH		56.2233259812
300AcetylationGFSGSDLKEMCRDAA
CCCHHHHHHHHHHHH		48.6826051181
300UbiquitinationGFSGSDLKEMCRDAA
CCCHHHHHHHHHHHH		48.6821963094
303GlutathionylationGSDLKEMCRDAALLC
HHHHHHHHHHHHHHH		3.6022555962
314PhosphorylationALLCVREYVNSTSEE
HHHHHHHHHHCCCCC		8.3829255136
317PhosphorylationCVREYVNSTSEESHD
HHHHHHHCCCCCCCC		24.2223401153
317UbiquitinationCVREYVNSTSEESHD
HHHHHHHCCCCCCCC		24.2229967540
318PhosphorylationVREYVNSTSEESHDE
HHHHHHCCCCCCCCC		34.6529255136
319PhosphorylationREYVNSTSEESHDED
HHHHHCCCCCCCCCC		38.9123401153
322PhosphorylationVNSTSEESHDEDEIR
HHCCCCCCCCCCCCC		31.9929255136
347UbiquitinationIEKMKKSKDAAFQNV
HHHHHHCHHHHHHHH		61.3329967540
359GlutathionylationQNVLTHVCLD-----
HHHHHHHHCC-----		2.4822555962
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 ATAD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATAD1_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 ATAD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOSR1_HUMANGOSR1physical
24843043
TPM2_HUMANTPM2physical
28514442
ANKS6_HUMANANKS6physical
27173435
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.
Regulatory Network of ATAD1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-146, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells.";
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.;
J. Proteome Res. 6:298-305(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory