ATD3B_HUMAN - dbPTM
ATD3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATD3B_HUMAN
UniProt AC Q5T9A4
Protein Name ATPase family AAA domain-containing protein 3B
Gene Name ATAD3B
Organism Homo sapiens (Human).
Sequence Length 648
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein . Has been found to co-purify with nucleoids (PubMed:22453275). Since it does not face the mitochondrial matrix, the association with nucleoids could be mediated by ATAD3A.
Protein Description May play a role in a mitochondrial network organization typical for stem cells, characterized by reduced mitochondrial metabolism, low mtDNA copies and fragmentated mitochondrial network. may act by suppressing ATAD3A function, interfering with ATAD3A interaction with matrix nucleoid complexes..
Protein Sequence MSWLFGVNKGPKGEGAGPPPPLPPAQPGAEGGGDRGLGDRPAPKDKWSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQDVLEGVVLSPSLEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDLPQQEERERLVRLHFDNCVLKPATEGKRRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQATAYASKDGVLTEAMMDACVQDAVQQYRQKMRWLKAEGPGRGVEHPLSGVQGETLTSWSLATDPSYPCLAGPCTFRICSWMGTGLCPGPLSPRMSCGGGRPFCPPGHPLL
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
2Phosphorylation------MSWLFGVNK
------CCCCCCCCC		32.2728348404
2Acetylation------MSWLFGVNK
------CCCCCCCCC		32.2722223895
9MethylationSWLFGVNKGPKGEGA
CCCCCCCCCCCCCCC		74.34-
17 (in isoform 2)Ubiquitination-46.2121906983
46AcetylationDRPAPKDKWSNFDPT
CCCCCCCCCCCCCHH		59.6623954790
46MalonylationDRPAPKDKWSNFDPT
CCCCCCCCCCCCCHH		59.6626320211
46UbiquitinationDRPAPKDKWSNFDPT
CCCCCCCCCCCCCHH		59.6629967540
58UbiquitinationDPTGLERAAKAAREL
CHHHHHHHHHHHHHH		12.1632015554
89 (in isoform 3)Ubiquitination-62.5321906983
89UbiquitinationEQTLQLEQQSKLKEY
HHHHHHHHHHHHHHH		62.5332015554
942-HydroxyisobutyrylationLEQQSKLKEYEAAVE
HHHHHHHHHHHHHHH		63.08-
94UbiquitinationLEQQSKLKEYEAAVE
HHHHHHHHHHHHHHH		63.0829967540
94AcetylationLEQQSKLKEYEAAVE
HHHHHHHHHHHHHHH		63.0826051181
96PhosphorylationQQSKLKEYEAAVEQL
HHHHHHHHHHHHHHH		14.8528152594
100UbiquitinationLKEYEAAVEQLKSEQ
HHHHHHHHHHHHHHH		6.5832015554
104UbiquitinationEAAVEQLKSEQIRAQ
HHHHHHHHHHHHHHH		52.2032015554
104AcetylationEAAVEQLKSEQIRAQ
HHHHHHHHHHHHHHH		52.2026051181
112UbiquitinationSEQIRAQAEERRKTL
HHHHHHHHHHHHHHH		21.4524816145
118PhosphorylationQAEERRKTLSEETRQ
HHHHHHHHHCHHHHH		33.4329449344
120PhosphorylationEERRKTLSEETRQHQ
HHHHHHHCHHHHHHH		38.3225159151
123PhosphorylationRKTLSEETRQHQARA
HHHHCHHHHHHHHHH		31.4225072903
132PhosphorylationQHQARAQYQDKLARQ
HHHHHHHHHHHHHHH		20.0729496907
135 (in isoform 1)Ubiquitination-28.6421906983
135UbiquitinationARAQYQDKLARQRYE
HHHHHHHHHHHHHHH		28.6432015554
1352-HydroxyisobutyrylationARAQYQDKLARQRYE
HHHHHHHHHHHHHHH		28.64-
135AcetylationARAQYQDKLARQRYE
HHHHHHHHHHHHHHH		28.6423749302
135MalonylationARAQYQDKLARQRYE
HHHHHHHHHHHHHHH		28.6426320211
146AcetylationQRYEDQLKQQQLLNE
HHHHHHHHHHHHHCH		40.1926051181
146UbiquitinationQRYEDQLKQQQLLNE
HHHHHHHHHHHHHCH		40.1932015554
158UbiquitinationLNEENLRKQEESVQK
HCHHHHHHHHHHHHH		66.2924816145
190UbiquitinationKNEMLRVETEARARA
HCCCHHHHHHHHHHH		34.2022817900
195UbiquitinationRVETEARARAKAERE
HHHHHHHHHHHHHHH		23.8822817900
206UbiquitinationAERENADIIREQIRL
HHHHHHHHHHHHHHH		2.7324816145
226UbiquitinationRQTVLESIRTAGTLF
HHHHHHHHHHHHHHH		3.1121890473
263PhosphorylationLLAVGVYSAKNATAV
HEEEEEECCCCCHHH		30.29-
281MalonylationFIEARLGKPSLVRET
HHHHHCCCHHHHCCH		35.7026320211
281SuccinylationFIEARLGKPSLVRET
HHHHHCCCHHHHCCH		35.7023954790
283PhosphorylationEARLGKPSLVRETSR
HHHCCCHHHHCCHHC		42.8721406692
288PhosphorylationKPSLVRETSRITVLE
CHHHHCCHHCCHHHH		16.85-
289PhosphorylationPSLVRETSRITVLEA
HHHHCCHHCCHHHHH		19.55-
292PhosphorylationVRETSRITVLEALRH
HCCHHCCHHHHHHHC		20.2320860994
312UbiquitinationRRLLSRPQDVLEGVV
HHHHCCCHHHHHCCC		52.9422817900
317UbiquitinationRPQDVLEGVVLSPSL
CCHHHHHCCCCCCCH		15.6322817900
321PhosphorylationVLEGVVLSPSLEARV
HHHCCCCCCCHHHHH		10.7927050516
323PhosphorylationEGVVLSPSLEARVRD
HCCCCCCCHHHHHHH		35.1527050516
335PhosphorylationVRDIAIATRNTKKNR
HHHHHHHCCCCCCCC		20.5220068231
337UbiquitinationDIAIATRNTKKNRGL
HHHHHCCCCCCCCCC		52.4724816145
338PhosphorylationIAIATRNTKKNRGLY
HHHHCCCCCCCCCCE		39.8520068231
345PhosphorylationTKKNRGLYRHILLYG
CCCCCCCEEEEEEEC		11.7227811184
348UbiquitinationNRGLYRHILLYGPPG
CCCCEEEEEEECCCC		1.7821890473
351PhosphorylationLYRHILLYGPPGTGK
CEEEEEEECCCCCCH		24.9227811184
356PhosphorylationLLYGPPGTGKTLFAK
EEECCCCCCHHHHHH		41.0827811184
358UbiquitinationYGPPGTGKTLFAKKL
ECCCCCCHHHHHHHH		41.7222817900
363UbiquitinationTGKTLFAKKLALHSG
CCHHHHHHHHHHCCC		40.7722817900
364MalonylationGKTLFAKKLALHSGM
CHHHHHHHHHHCCCC		35.2526320211
373PhosphorylationALHSGMDYAIMTGGD
HHCCCCCEEEECCCC		6.80-
377PhosphorylationGMDYAIMTGGDVAPM
CCCEEEECCCCCCCC		31.7223401153
381AcetylationAIMTGGDVAPMGREG
EEECCCCCCCCCCCC		7.9219608861
390PhosphorylationPMGREGVTAMHKLFD
CCCCCCCHHHHHHHH		29.1723401153
394UbiquitinationEGVTAMHKLFDWANT
CCCHHHHHHHHHHCC		37.4521890473
406UbiquitinationANTSRRGLLLFMDEA
HCCCCCEEEEECCHH		3.4022817900
411UbiquitinationRGLLLFMDEADAFLR
CEEEEECCHHHHHHH		40.3722817900
422PhosphorylationAFLRKRATEEISKDL
HHHHHHCHHHHHHHH		37.8820860994
426PhosphorylationKRATEEISKDLRATL
HHCHHHHHHHHHHHH		24.3220860994
4272-HydroxyisobutyrylationRATEEISKDLRATLN
HCHHHHHHHHHHHHH		67.45-
427AcetylationRATEEISKDLRATLN
HCHHHHHHHHHHHHH		67.4519608861
427MalonylationRATEEISKDLRATLN
HCHHHHHHHHHHHHH		67.4526320211
432PhosphorylationISKDLRATLNAFLYH
HHHHHHHHHHHHHHH		17.7028509920
438PhosphorylationATLNAFLYHMGQHSN
HHHHHHHHHCHHCCC		5.3628509920
442UbiquitinationAFLYHMGQHSNKFML
HHHHHCHHCCCCEEE		29.3021890473
459UbiquitinationASNLPEQFDCAINSR
CCCCHHHCCCHHHCC		8.7524816145
495AcetylationHFDNCVLKPATEGKR
HHCCCEECCCCCCCH		16.5326822725
505UbiquitinationTEGKRRLKLAQFDYG
CCCCHHHEEECCCCC		39.7124816145
516PhosphorylationFDYGRKCSEVARLTE
CCCCCCHHHHHHHCC		37.83-
553UbiquitinationDGVLTEAMMDACVQD
CCCCHHHHHHHHHHH		1.7124816145
629PhosphorylationGLCPGPLSPRMSCGG
CCCCCCCCCCCCCCC		17.3721815630
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 ATD3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATD3B_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 ATD3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF2B_HUMANEIF2S2physical
26344197
SPB1_HUMANFTSJ3physical
26344197
PHB2_HUMANPHB2physical
26344197
RPN1_HUMANRPN1physical
26344197
SRP68_HUMANSRP68physical
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 ATD3B_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-135 AND LYS-427, AND MASSSPECTROMETRY.

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