TOM34_HUMAN - dbPTM
TOM34_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOM34_HUMAN
UniProt AC Q15785
Protein Name Mitochondrial import receptor subunit TOM34
Gene Name TOMM34
Organism Homo sapiens (Human).
Sequence Length 309
Subcellular Localization Cytoplasm . Mitochondrion outer membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state..
Protein Sequence MAPKFPDSVEELRAAGNESFRNGQYAEASALYGRALRVLQAQGSSDPEEESVLYSNRAACHLKDGNCRDCIKDCTSALALVPFSIKPLLRRASAYEALEKYPMAYVDYKTVLQIDDNVTSAVEGINRMTRALMDSLGPEWRLKLPSIPLVPVSAQKRWNSLPSENHKEMAKSKSKETTATKNRVPSAGDVEKARVLKEEGNELVKKGNHKKAIEKYSESLLCSNLESATYSNRALCYLVLKQYTEAVKDCTEALKLDGKNVKAFYRRAQAHKALKDYKSSFADISNLLQIEPRNGPAQKLRQEVKQNLH
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
4Ubiquitination----MAPKFPDSVEE
----CCCCCCCCHHH		61.0524816145
8PhosphorylationMAPKFPDSVEELRAA
CCCCCCCCHHHHHHH		31.5030622161
19PhosphorylationLRAAGNESFRNGQYA
HHHHCCHHHHCCCHH		33.2427362937
25PhosphorylationESFRNGQYAEASALY
HHHHCCCHHHHHHHH		14.0627642862
32PhosphorylationYAEASALYGRALRVL
HHHHHHHHHHHHHHH		12.3227642862
44PhosphorylationRVLQAQGSSDPEEES
HHHHHCCCCCHHHHH		21.3521815630
45PhosphorylationVLQAQGSSDPEEESV
HHHHCCCCCHHHHHH		65.1020873877
51PhosphorylationSSDPEEESVLYSNRA
CCCHHHHHHHHCCCE		22.2428796482
54PhosphorylationPEEESVLYSNRAACH
HHHHHHHHCCCEEEE		11.1828796482
55PhosphorylationEEESVLYSNRAACHL
HHHHHHHCCCEEEEC		18.7128796482
63AcetylationNRAACHLKDGNCRDC
CCEEEECCCCCHHHH		39.6723749302
72UbiquitinationGNCRDCIKDCTSALA
CCHHHHHHHCCHHHH		53.75-
75PhosphorylationRDCIKDCTSALALVP
HHHHHHCCHHHHHCC		27.4520068231
76PhosphorylationDCIKDCTSALALVPF
HHHHHCCHHHHHCCC		27.8420068231
84PhosphorylationALALVPFSIKPLLRR
HHHHCCCCHHHHHHH		24.5120068231
86UbiquitinationALVPFSIKPLLRRAS
HHCCCCHHHHHHHHH		28.5432015554
93PhosphorylationKPLLRRASAYEALEK
HHHHHHHHHHHHHHH		29.5827273156
95PhosphorylationLLRRASAYEALEKYP
HHHHHHHHHHHHHCC		10.1528796482
100AcetylationSAYEALEKYPMAYVD
HHHHHHHHCCCEEEC		56.3525038526
105PhosphorylationLEKYPMAYVDYKTVL
HHHCCCEEECEEEEE		6.3924719451
108PhosphorylationYPMAYVDYKTVLQID
CCCEEECEEEEEEEC		9.8724719451
120PhosphorylationQIDDNVTSAVEGINR
EECCCHHHHHHHHHH		26.4924719451
133SulfoxidationNRMTRALMDSLGPEW
HHHHHHHHHHHCCCH		2.9930846556
143UbiquitinationLGPEWRLKLPSIPLV
HCCCHHCCCCCCCEE		50.18-
146PhosphorylationEWRLKLPSIPLVPVS
CHHCCCCCCCEEECC		47.4720068231
153PhosphorylationSIPLVPVSAQKRWNS
CCCEEECCCHHHHHC		20.9321815630
1562-HydroxyisobutyrylationLVPVSAQKRWNSLPS
EEECCCHHHHHCCCC		60.13-
156AcetylationLVPVSAQKRWNSLPS
EEECCCHHHHHCCCC		60.1325953088
160PhosphorylationSAQKRWNSLPSENHK
CCHHHHHCCCCHHHH		34.4023403867
163PhosphorylationKRWNSLPSENHKEMA
HHHHCCCCHHHHHHH		57.2227794612
170UbiquitinationSENHKEMAKSKSKET
CHHHHHHHHHHCCCC		17.6723000965
173UbiquitinationHKEMAKSKSKETTAT
HHHHHHHHCCCCCCC		65.9123000965
176UbiquitinationMAKSKSKETTATKNR
HHHHHCCCCCCCCCC		59.4923000965
186PhosphorylationATKNRVPSAGDVEKA
CCCCCCCCCCHHHHH		41.8629255136
192UbiquitinationPSAGDVEKARVLKEE
CCCCHHHHHHHHHHH		41.1429967540
197SumoylationVEKARVLKEEGNELV
HHHHHHHHHHHHHHH		51.3528112733
197UbiquitinationVEKARVLKEEGNELV
HHHHHHHHHHHHHHH		51.3524816145
197SumoylationVEKARVLKEEGNELV
HHHHHHHHHHHHHHH		51.35-
197MalonylationVEKARVLKEEGNELV
HHHHHHHHHHHHHHH		51.3532601280
229PhosphorylationCSNLESATYSNRALC
CCCCCCCCCCHHHHH		36.4428796482
230PhosphorylationSNLESATYSNRALCY
CCCCCCCCCHHHHHH		12.0328796482
231PhosphorylationNLESATYSNRALCYL
CCCCCCCCHHHHHHH		18.5828796482
237PhosphorylationYSNRALCYLVLKQYT
CCHHHHHHHHHHHHH		10.7427642862
244PhosphorylationYLVLKQYTEAVKDCT
HHHHHHHHHHHHHHH		18.2522817900
246UbiquitinationVLKQYTEAVKDCTEA
HHHHHHHHHHHHHHH		13.0823000965
249UbiquitinationQYTEAVKDCTEALKL
HHHHHHHHHHHHHCC		37.6623000965
252UbiquitinationEAVKDCTEALKLDGK
HHHHHHHHHHCCCCC		59.3323000965
255AcetylationKDCTEALKLDGKNVK
HHHHHHHCCCCCCHH		52.1326051181
259AcetylationEALKLDGKNVKAFYR
HHHCCCCCCHHHHHH		59.2312656531
272UbiquitinationYRRAQAHKALKDYKS
HHHHHHHHHHHHHHH		59.4323000965
273UbiquitinationRRAQAHKALKDYKSS
HHHHHHHHHHHHHHH		15.2424816145
275UbiquitinationAQAHKALKDYKSSFA
HHHHHHHHHHHHHHH		64.9623000965
277PhosphorylationAHKALKDYKSSFADI
HHHHHHHHHHHHHHH		15.9325693802
278UbiquitinationHKALKDYKSSFADIS
HHHHHHHHHHHHHHH		50.1623000965
279PhosphorylationKALKDYKSSFADISN
HHHHHHHHHHHHHHH		25.1829496907
280PhosphorylationALKDYKSSFADISNL
HHHHHHHHHHHHHHH		21.9430622161
285PhosphorylationKSSFADISNLLQIEP
HHHHHHHHHHHCCCC		23.2121712546
293MethylationNLLQIEPRNGPAQKL
HHHCCCCCCCHHHHH		48.20115918717
299UbiquitinationPRNGPAQKLRQEVKQ
CCCCHHHHHHHHHHH		47.9824816145
305SumoylationQKLRQEVKQNLH---
HHHHHHHHHHCC---		32.49-
305SumoylationQKLRQEVKQNLH---
HHHHHHHHHHCC---		32.49-
305UbiquitinationQKLRQEVKQNLH---
HHHHHHHHHHCC---		32.4929967540
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 TOM34_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOM34_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 TOM34_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
11913976
VATD_HUMANATP6V1Dphysical
11913976
AAPK1_HUMANPRKAA1physical
11913976
DMAP1_HUMANDMAP1physical
11913976
WDR12_HUMANWDR12physical
22939629
ZFAN5_HUMANZFAND5physical
22939629
ZYX_HUMANZYXphysical
22939629
DNJC7_HUMANDNAJC7physical
26344197
FUS_HUMANFUSphysical
26344197
HNRPD_HUMANHNRNPDphysical
26344197
SYTC_HUMANTARSphysical
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 TOM34_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.

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