ADT4_HUMAN - dbPTM
ADT4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADT4_HUMAN
UniProt AC Q9H0C2
Protein Name ADP/ATP translocase 4
Gene Name SLC25A31
Organism Homo sapiens (Human).
Sequence Length 315
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein. Cell projection, cilium, flagellum. In sperm flagellum this protein is located in the fibrous sheath, a non-mitochondrial region.
Protein Description Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May serve to mediate energy generating and energy consuming processes in the distal flagellum, possibly as a nucleotide shuttle between flagellar glycolysis, protein phosphorylation and mechanisms of motility..
Protein Sequence MHREPAKKKAEKRLFDASSFGKDLLAGGVAAAVSKTAVAPIERVKLLLQVQASSKQISPEARYKGMVDCLVRIPREQGFFSFWRGNLANVIRYFPTQALNFAFKDKYKQLFMSGVNKEKQFWRWFLANLASGGAAGATSLCVVYPLDFARTRLGVDIGKGPEERQFKGLGDCIMKIAKSDGIAGLYQGFGVSVQGIIVYRASYFGAYDTVKGLLPKPKKTPFLVSFFIAQVVTTCSGILSYPFDTVRRRMMMQSGEAKRQYKGTLDCFVKIYQHEGISSFFRGAFSNVLRGTGGALVLVLYDKIKEFFHIDIGGR
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
18PhosphorylationEKRLFDASSFGKDLL
HHHHHCHHHHCHHHH
28.2220068231
19PhosphorylationKRLFDASSFGKDLLA
HHHHCHHHHCHHHHH
39.4720068231
34PhosphorylationGGVAAAVSKTAVAPI
HHHHHHCCCCCCCCH
21.4020068231
36PhosphorylationVAAAVSKTAVAPIER
HHHHCCCCCCCCHHH
20.8920860994
45UbiquitinationVAPIERVKLLLQVQA
CCCHHHHHHHHHHHC
39.3722817900
53PhosphorylationLLLQVQASSKQISPE
HHHHHHCCCCCCCHH
22.4530622161
54PhosphorylationLLQVQASSKQISPEA
HHHHHCCCCCCCHHH
31.4330622161
58PhosphorylationQASSKQISPEARYKG
HCCCCCCCHHHHHCC
17.7521659604
63PhosphorylationQISPEARYKGMVDCL
CCCHHHHHCCHHHEE
20.95-
93PhosphorylationNLANVIRYFPTQALN
CHHHHHHHCHHHHHH
11.6424927040
96PhosphorylationNVIRYFPTQALNFAF
HHHHHCHHHHHHHHC
19.3021712546
104AcetylationQALNFAFKDKYKQLF
HHHHHHCHHHHHHHH
50.296570043
104UbiquitinationQALNFAFKDKYKQLF
HHHHHHCHHHHHHHH
50.2922817900
106AcetylationLNFAFKDKYKQLFMS
HHHHCHHHHHHHHHH
55.747617841
106UbiquitinationLNFAFKDKYKQLFMS
HHHHCHHHHHHHHHH
55.7422817900
108UbiquitinationFAFKDKYKQLFMSGV
HHCHHHHHHHHHHCC
46.3922817900
113PhosphorylationKYKQLFMSGVNKEKQ
HHHHHHHHCCCHHHH
32.0520068231
117UbiquitinationLFMSGVNKEKQFWRW
HHHHCCCHHHHHHHH
64.97-
218AcetylationKGLLPKPKKTPFLVS
HCCCCCCCCCCHHHH
75.3419824391
219AcetylationGLLPKPKKTPFLVSF
CCCCCCCCCCHHHHH
70.7019824399
220PhosphorylationLLPKPKKTPFLVSFF
CCCCCCCCCHHHHHH
25.9622210691
261PhosphorylationSGEAKRQYKGTLDCF
CCHHHHHHCCCHHHE
18.54-
264PhosphorylationAKRQYKGTLDCFVKI
HHHHHCCCHHHEEEH
18.44-
270AcetylationGTLDCFVKIYQHEGI
CCHHHEEEHHHCCCH
18.5525038526
279PhosphorylationYQHEGISSFFRGAFS
HHCCCHHHHHHHHHH
26.8724719451
303AcetylationLVLVLYDKIKEFFHI
EEEEEHHHHHHHHCC
41.9625038526

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 ADT4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADT4_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 ADT4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ADT4_HUMAN !!

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 ADT4_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-104, AND MASS SPECTROMETRY.

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