TMM70_HUMAN - dbPTM
TMM70_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMM70_HUMAN
UniProt AC Q9BUB7
Protein Name Transmembrane protein 70, mitochondrial
Gene Name TMEM70
Organism Homo sapiens (Human).
Sequence Length 260
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Involved in biogenesis of mitochondrial ATP synthase..
Protein Sequence MLFLALGSPWAVELPLCGRRTALCAAAALRGPRASVSRASSSSGPSGPVAGWSTGPSGAARLLRRPGRAQIPVYWEGYVRFLNTPSDKSEDGRLIYTGNMARAVFGVKCFSYSTSLIGLTFLPYIFTQNNAISESVPLPIQIIFYGIMGSFTVITPVLLHFITKGYVIRLYHEATTDTYKAITYNAMLAETSTVFHQNDVKIPDAKHVFTTFYAKTKSLLVNPVLFPNREDYIHLMGYDKEEFILYMEETSEEKRHKDDK
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
21PhosphorylationLPLCGRRTALCAAAA
CCCCCHHHHHHHHHH
23.7122210691
35PhosphorylationALRGPRASVSRASSS
HHHCCCEEECCCCCC
23.16-
37PhosphorylationRGPRASVSRASSSSG
HCCCEEECCCCCCCC
21.4528857561
74PhosphorylationGRAQIPVYWEGYVRF
CCCCCCEEEEEEEEE
7.7427642862
84PhosphorylationGYVRFLNTPSDKSED
EEEEEECCCCCCCCC
26.73-
86PhosphorylationVRFLNTPSDKSEDGR
EEEECCCCCCCCCCC
56.48-
88UbiquitinationFLNTPSDKSEDGRLI
EECCCCCCCCCCCEE
61.1421906983
88 (in isoform 1)Ubiquitination-61.1421890473
89PhosphorylationLNTPSDKSEDGRLIY
ECCCCCCCCCCCEEE
46.0024719451
96PhosphorylationSEDGRLIYTGNMARA
CCCCCEEECCCHHHH
17.1229496907
102 (in isoform 2)Ubiquitination-22.1021890473
118 (in isoform 2)Ubiquitination-24.7721890473
171PhosphorylationKGYVIRLYHEATTDT
CCCEEEEEEECCCCH
6.43-
179PhosphorylationHEATTDTYKAITYNA
EECCCCHHHHHHHHH
10.96-
184PhosphorylationDTYKAITYNAMLAET
CHHHHHHHHHHHHCC
8.53-
201UbiquitinationVFHQNDVKIPDAKHV
EECCCCCCCCCHHHE
51.9221906983
201 (in isoform 1)Ubiquitination-51.9221890473
206UbiquitinationDVKIPDAKHVFTTFY
CCCCCCHHHEEEEEE
47.9122817900
206MalonylationDVKIPDAKHVFTTFY
CCCCCCHHHEEEEEE
47.9130639696
213PhosphorylationKHVFTTFYAKTKSLL
HHEEEEEEECCHHHE
12.7029496907
215UbiquitinationVFTTFYAKTKSLLVN
EEEEEEECCHHHEEE
45.1422817900
217UbiquitinationTTFYAKTKSLLVNPV
EEEEECCHHHEEECE
38.1027667366
217 (in isoform 1)Ubiquitination-38.1021890473

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 TMM70_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMM70_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 TMM70_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACS2L_HUMANACSS1physical
28514442
CHDH_HUMANCHDHphysical
28514442
MIPEP_HUMANMIPEPphysical
28514442
SYNM_HUMANNARS2physical
28514442
ZMY19_HUMANZMYND19physical
28514442
MCCA_HUMANMCCC1physical
28514442
COQ6_HUMANCOQ6physical
28514442
CPSM_HUMANCPS1physical
28514442
CPT2_HUMANCPT2physical
28514442
DHRS4_HUMANDHRS4physical
28514442
IF2M_HUMANMTIF2physical
28514442
ACTBL_HUMANACTBL2physical
28514442
ADRO_HUMANFDXRphysical
28514442
ACSF3_HUMANACSF3physical
28514442
MAEA_HUMANMAEAphysical
28514442
TOP3A_HUMANTOP3Aphysical
28514442

Drug and Disease Associations
Kegg Disease
H00473 Mitochondrial respiratory chain deficiencies (MRCD), including: Mitochondrial complex I deficiency (
OMIM Disease
614052Mitochondrial complex V deficiency, nuclear 2 (MC5DN2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TMM70_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP