ATD3A_HUMAN - dbPTM
ATD3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATD3A_HUMAN
UniProt AC Q9NVI7
Protein Name ATPase family AAA domain-containing protein 3A {ECO:0000312|HGNC:HGNC:25567}
Gene Name ATAD3A {ECO:0000312|HGNC:HGNC:25567}
Organism Homo sapiens (Human).
Sequence Length 634
Subcellular Localization Mitochondrion inner membrane
Single-pass membrane protein . Mitochondrion matrix, mitochondrion nucleoid . In the mitochondrial inner membrane, enriched in sites with the potential to form contacts with the outer membrane (PubMed:20349121, PubMed:2
Protein Description Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important role in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis..
Protein Sequence MSWLFGINKGPKGEGAGPPPPLPPAQPGAEGGGDRGLGDRPAPKDKWSNFDPTGLERAAKAARELEHSRYAKDALNLAQMQEQTLQLEQQSKLKMRLEALSLLHTLVWAWSLCRAGAVQTQERLSGSASPEQVPAGECCALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVEAEARARAKAERENADIIREQIRLKAAEHRQTVLESIRTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVYSAKNATLVAGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQDALEGVVLSPSLEARVRDIAIATRNTKKNRSLYRNILMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLYRTGQHSNKFMLVLASNQPEQFDWAINDRINEMVHFDLPGQEERERLVRMYFDKYVLKPATEGKQRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQATAYASEDGVLTEAMMDTRVQDAVQQHQQKMCWLKAEGPGRGDEPSPS
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
2Acetylation------MSWLFGINK
------CCCCCCCCC		32.27-
2Phosphorylation------MSWLFGINK
------CCCCCCCCC		32.2723186163
9MethylationSWLFGINKGPKGEGA
CCCCCCCCCCCCCCC		74.74-
25UbiquitinationPPPPLPPAQPGAEGG
CCCCCCCCCCCCCCC		26.6832015554
46AcetylationDRPAPKDKWSNFDPT
CCCCCCCCCCCCCHH		59.66-
46UbiquitinationDRPAPKDKWSNFDPT
CCCCCCCCCCCCCHH		59.6629967540
46 (in isoform 2)Malonylation-59.6626320211
56AcetylationNFDPTGLERAAKAAR
CCCHHHHHHHHHHHH		41.4319608861
56UbiquitinationNFDPTGLERAAKAAR
CCCHHHHHHHHHHHH		41.4332015554
67UbiquitinationKAARELEHSRYAKDA
HHHHHHHHHHHHHHH		30.1532015554
72AcetylationLEHSRYAKDALNLAQ
HHHHHHHHHHHHHHH		34.3026051181
72UbiquitinationLEHSRYAKDALNLAQ
HHHHHHHHHHHHHHH		34.30-
79UbiquitinationKDALNLAQMQEQTLQ
HHHHHHHHHHHHHHH		36.9424816145
84PhosphorylationLAQMQEQTLQLEQQS
HHHHHHHHHHHHHHH		18.7321406692
91PhosphorylationTLQLEQQSKLKMRLE
HHHHHHHHHHHHHHH		39.3821406692
92UbiquitinationLQLEQQSKLKMRLEA
HHHHHHHHHHHHHHH		48.0332015554
94UbiquitinationLEQQSKLKMRLEALS
HHHHHHHHHHHHHHH		26.2229967540
104UbiquitinationLEALSLLHTLVWAWS
HHHHHHHHHHHHHHH		23.5832015554
135AcetylationASPEQVPAGECCALQ
CCCCCCCCCCCCHHH		27.7919608861
135UbiquitinationASPEQVPAGECCALQ
CCCCCCCCCCCCHHH		27.7932015554
135 (in isoform 2)Malonylation-27.7926320211
135 (in isoform 2)Ubiquitination-27.7921890473
144PhosphorylationECCALQEYEAAVEQL
CCCHHHHHHHHHHHH		9.63-
146UbiquitinationCALQEYEAAVEQLKS
CHHHHHHHHHHHHHH		18.8632015554
152UbiquitinationEAAVEQLKSEQIRAQ
HHHHHHHHHHHHHHH		52.2032015554
158UbiquitinationLKSEQIRAQAEERRK
HHHHHHHHHHHHHHH		17.9824816145
166PhosphorylationQAEERRKTLSEETRQ
HHHHHHHHHCHHHHH		33.4329449344
168PhosphorylationEERRKTLSEETRQHQ
HHHHHHHCHHHHHHH		38.3225159151
171PhosphorylationRKTLSEETRQHQARA
HHHHCHHHHHHHHHH		31.4225072903
180PhosphorylationQHQARAQYQDKLARQ
HHHHHHHHHHHHHHH		20.0729496907
183AcetylationARAQYQDKLARQRYE
HHHHHHHHHHHHHHH		28.6419608861
183UbiquitinationARAQYQDKLARQRYE
HHHHHHHHHHHHHHH		28.6432015554
183 (in isoform 1)Ubiquitination-28.6421890473
194AcetylationQRYEDQLKQQQLLNE
HHHHHHHHHHHHHCH		40.197406673
194UbiquitinationQRYEDQLKQQQLLNE
HHHHHHHHHHHHHCH		40.1932015554
206UbiquitinationLNEENLRKQEESVQK
HCHHHHHHHHHHHHH		66.2924816145
262UbiquitinationIREQIRLKAAEHRQT
HHHHHHHHHHHHHHH		35.38-
269PhosphorylationKAAEHRQTVLESIRT
HHHHHHHHHHHHHHH		27.3229214152
279UbiquitinationESIRTAGTLFGEGFR
HHHHHHHHHHCCCHH		19.2221890473
279UbiquitinationESIRTAGTLFGEGFR
HHHHHHHHHHCCCHH		19.2221890473
281 (in isoform 2)Malonylation-9.3326320211
284UbiquitinationAGTLFGEGFRAFVTD
HHHHHCCCHHHEECC		20.0922817900
290PhosphorylationEGFRAFVTDWDKVTA
CCHHHEECCHHHHHH		25.56-
296PhosphorylationVTDWDKVTATVAGLT
ECCHHHHHHHHHHHH		23.5023312004
298PhosphorylationDWDKVTATVAGLTLL
CHHHHHHHHHHHHHH		11.0923312004
303PhosphorylationTATVAGLTLLAVGVY
HHHHHHHHHHHHHHH		20.8623312004
310PhosphorylationTLLAVGVYSAKNATL
HHHHHHHHCCCCCEE		9.2923312004
311PhosphorylationLLAVGVYSAKNATLV
HHHHHHHCCCCCEEE		30.2923312004
315UbiquitinationGVYSAKNATLVAGRF
HHHCCCCCEEEEHHH		11.1221890473
315UbiquitinationGVYSAKNATLVAGRF
HHHCCCCCEEEEHHH		11.1221890473
316PhosphorylationVYSAKNATLVAGRFI
HHCCCCCEEEEHHHH		31.0323312004
331PhosphorylationEARLGKPSLVRETSR
HHHCCCCHHHCHHHC		42.8721406692
336PhosphorylationKPSLVRETSRITVLE
CCHHHCHHHCCHHHH		16.85-
337PhosphorylationPSLVRETSRITVLEA
CHHHCHHHCCHHHHH		19.55-
340PhosphorylationVRETSRITVLEALRH
HCHHHCCHHHHHHHC		20.2320860994
345UbiquitinationRITVLEALRHPIQVS
CCHHHHHHHCHHHHH		3.6424816145
357PhosphorylationQVSRRLLSRPQDALE
HHHHHHHCCCHHHHC		46.6523312004
358UbiquitinationVSRRLLSRPQDALEG
HHHHHHCCCHHHHCC		32.6321890473
358 (in isoform 2)Ubiquitination-32.6321890473
363UbiquitinationLSRPQDALEGVVLSP
HCCCHHHHCCCCCCH		8.7222817900
364 (in isoform 2)Malonylation-52.2226320211
369PhosphorylationALEGVVLSPSLEARV
HHCCCCCCHHHHHHH		10.7930266825
371PhosphorylationEGVVLSPSLEARVRD
CCCCCCHHHHHHHHH		35.1530266825
383PhosphorylationVRDIAIATRNTKKNR
HHHHHHHCCCCCCCH		20.52-
394UbiquitinationKKNRSLYRNILMYGP
CCCHHHHHHHHHCCC		29.0721890473
394 (in isoform 2)Ubiquitination-29.0721890473
404PhosphorylationLMYGPPGTGKTLFAK
HHCCCCCCCHHHHHH		41.0823186163
406UbiquitinationYGPPGTGKTLFAKKL
CCCCCCCHHHHHHHH		41.7221890473
406 (in isoform 1)Ubiquitination-41.7221890473
411UbiquitinationTGKTLFAKKLALHSG
CCHHHHHHHHHHCCC		40.7722817900
412AcetylationGKTLFAKKLALHSGM
CHHHHHHHHHHCCCC		35.2519608861
416AcetylationFAKKLALHSGMDYAI
HHHHHHHCCCCCEEE		19.3919608861
421PhosphorylationALHSGMDYAIMTGGD
HHCCCCCEEEECCCC		6.80-
422UbiquitinationLHSGMDYAIMTGGDV
HCCCCCEEEECCCCC		4.8429967540
424UbiquitinationSGMDYAIMTGGDVAP
CCCCEEEECCCCCCC		1.8524816145
424 (in isoform 2)Malonylation-1.8526320211
425PhosphorylationGMDYAIMTGGDVAPM
CCCEEEECCCCCCCC		31.7223401153
426UbiquitinationMDYAIMTGGDVAPMG
CCEEEECCCCCCCCC		16.9624816145
438PhosphorylationPMGREGVTAMHKLFD
CCCCCCCHHHHHHHH		29.1723401153
442UbiquitinationEGVTAMHKLFDWANT
CCCHHHHHHHHHHCC		37.4521890473
442 (in isoform 1)Ubiquitination-37.4521890473
450PhosphorylationLFDWANTSRRGLLLF
HHHHHCCCCCCEEEE		21.5629116813
472UbiquitinationLRKRATEKISEDLRA
HHHHHHHHHCHHHHH		47.3724816145
474PhosphorylationKRATEKISEDLRATL
HHHHHHHCHHHHHHH		35.8023186163
489UbiquitinationNAFLYRTGQHSNKFM
HHHHHHCCCCCCCEE		17.7622817900
491AcetylationFLYRTGQHSNKFMLV
HHHHCCCCCCCEEEE		34.3819608861
491 (in isoform 2)Malonylation-34.3826320211
494UbiquitinationRTGQHSNKFMLVLAS
HCCCCCCCEEEEEEC		34.8521890473
494AcetylationRTGQHSNKFMLVLAS
HCCCCCCCEEEEEEC		34.8526051181
494UbiquitinationRTGQHSNKFMLVLAS
HCCCCCCCEEEEEEC		34.8521890473
495AcetylationTGQHSNKFMLVLASN
CCCCCCCEEEEEECC		5.5319608861
495 (in isoform 2)Malonylation-5.5326320211
501UbiquitinationKFMLVLASNQPEQFD
CEEEEEECCCHHHCC		31.6629967540
505UbiquitinationVLASNQPEQFDWAIN
EEECCCHHHCCCHHH		54.8624816145
518SulfoxidationINDRINEMVHFDLPG
HHHHHHHHCCCCCCC		2.1621406390
536PhosphorylationRERLVRMYFDKYVLK
HHHHHHHHHHHHCCC		9.6922817900
539AcetylationLVRMYFDKYVLKPAT
HHHHHHHHHCCCCCC		27.6219608861
539MalonylationLVRMYFDKYVLKPAT
HHHHHHHHHCCCCCC		27.6226320211
539SuccinylationLVRMYFDKYVLKPAT
HHHHHHHHHCCCCCC		27.6227452117
540PhosphorylationVRMYFDKYVLKPATE
HHHHHHHHCCCCCCC		16.9222817900
543AcetylationYFDKYVLKPATEGKQ
HHHHHCCCCCCCCCH		23.6719608861
549AcetylationLKPATEGKQRLKLAQ
CCCCCCCCHHHEEEC		26.4725953088
549UbiquitinationLKPATEGKQRLKLAQ
CCCCCCCCHHHEEEC		26.4729967540
553UbiquitinationTEGKQRLKLAQFDYG
CCCCHHHEEECCCCC		43.9224816145
564PhosphorylationFDYGRKCSEVARLTE
CCCCCCHHHHHHHCC		37.83-
568UbiquitinationRKCSEVARLTEGMSG
CCHHHHHHHCCCCCH		47.5222817900
573UbiquitinationVARLTEGMSGREIAQ
HHHHCCCCCHHHHHH		2.9021890473
573 (in isoform 2)Ubiquitination-2.9021890473
592PhosphorylationWQATAYASEDGVLTE
HHHHHHHCCCCCCHH		24.4428387310
598PhosphorylationASEDGVLTEAMMDTR
HCCCCCCHHHHHHHH		21.2028387310
604PhosphorylationLTEAMMDTRVQDAVQ
CHHHHHHHHHHHHHH		18.1628387310
616AcetylationAVQQHQQKMCWLKAE
HHHHHHHHCHHHHCC		29.4726822725
616UbiquitinationAVQQHQQKMCWLKAE
HHHHHHHHCHHHHCC		29.4722817900
621AcetylationQQKMCWLKAEGPGRG
HHHCHHHHCCCCCCC		21.6426051181
621UbiquitinationQQKMCWLKAEGPGRG
HHHCHHHHCCCCCCC		21.6422817900
621 (in isoform 1)Ubiquitination-21.6421890473
632PhosphorylationPGRGDEPSPS-----
CCCCCCCCCC-----		35.4128857561
634PhosphorylationRGDEPSPS-------
CCCCCCCC-------		58.1328857561
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 ATD3A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATD3A_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 ATD3A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPB_HUMANCOPB1physical
26344197
NDUB8_HUMANNDUFB8physical
26344197
NDUS4_HUMANNDUFS4physical
26344197
PHB2_HUMANPHB2physical
26344197
RPN1_HUMANRPN1physical
26344197
SSRA_HUMANSSR1physical
26344197
TERA_HUMANVCPphysical
26344197
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 ATD3A_HUMAN

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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-539, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND MASSSPECTROMETRY.

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