UniProt ID | ABCBA_HUMAN | |
---|---|---|
UniProt AC | Q9NRK6 | |
Protein Name | ATP-binding cassette sub-family B member 10, mitochondrial | |
Gene Name | ABCB10 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 738 | |
Subcellular Localization |
Mitochondrion inner membrane Multi-pass membrane protein. |
|
Protein Description | May mediate critical mitochondrial transport functions related to heme biosynthesis.. | |
Protein Sequence | MRGPPAWPLRLLEPPSPAEPGRLLPVACVWAAASRVPGSLSPFTGLRPARLWGAGPALLWGVGAARRWRSGCRGGGPGASRGVLGLARLLGLWARGPGSCRCGAFAGPGAPRLPRARFPGGPAAAAWAGDEAWRRGPAAPPGDKGRLRPAAAGLPEARKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNEGVILNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQSFISA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
16 | Phosphorylation | LRLLEPPSPAEPGRL CCCCCCCCCCCCCCC | 47.67 | 26074081 | |
80 | Phosphorylation | RGGGPGASRGVLGLA CCCCCCHHHHHHHHH | 35.17 | 50558515 | |
86 | Ubiquitination | ASRGVLGLARLLGLW HHHHHHHHHHHHCHH | 1.88 | 24816145 | |
159 | Ubiquitination | AGLPEARKLLGLAYP CCCHHHHHHHCCCCH | 55.93 | 21890473 | |
207 | Phosphorylation | YTNPTVDYSDNLTRL ECCCCCCCCCHHHHH | 17.37 | 46156643 | |
208 | Phosphorylation | TNPTVDYSDNLTRLC CCCCCCCCCHHHHHH | 18.63 | 46156631 | |
212 | Phosphorylation | VDYSDNLTRLCLGLS CCCCCHHHHHHHHHH | 28.05 | 46156637 | |
219 | Phosphorylation | TRLCLGLSAVFLCGA HHHHHHHHHHHHHHH | 22.16 | 22210691 | |
254 | Phosphorylation | LRTSLFSSILRQEVA HHHHHHHHHHHHHHH | 20.50 | 24719451 | |
265 | Ubiquitination | QEVAFFDKTRTGELI HHHHHCCCCCHHHHH | 34.45 | 24816145 | |
265 | Acetylation | QEVAFFDKTRTGELI HHHHHCCCCCHHHHH | 34.45 | 19608861 | |
341 | Malonylation | RYLRKLTKVTQDSLA HHHHHHCCCCHHHHH | 54.44 | 26320211 | |
351 | Phosphorylation | QDSLAQATQLAEERI HHHHHHHHHHHHHHH | 16.43 | 26657352 | |
351 | O-linked_Glycosylation | QDSLAQATQLAEERI HHHHHHHHHHHHHHH | 16.43 | 29351928 | |
363 | Phosphorylation | ERIGNVRTVRAFGKE HHHCCHHHHHHCCCC | 15.29 | 63650289 | |
369 | Ubiquitination | RTVRAFGKEMTEIEK HHHHHCCCCHHHHHH | 37.55 | - | |
377 | Phosphorylation | EMTEIEKYASKVDHV CHHHHHHHHHHHHHH | 11.87 | 22468782 | |
380 | Malonylation | EIEKYASKVDHVMQL HHHHHHHHHHHHHHH | 43.44 | 26320211 | |
380 | Ubiquitination | EIEKYASKVDHVMQL HHHHHHHHHHHHHHH | 43.44 | - | |
385 | Sulfoxidation | ASKVDHVMQLARKEA HHHHHHHHHHHHHHH | 2.13 | 21406390 | |
486 | Ubiquitination | EGVILNEKSFQGALE CCCCCCCCCCCCCEE | 56.34 | - | |
661 | Phosphorylation | ILLLDEATSALDAEN EEEECCCCCCCHHCC | 16.69 | 24275569 | |
700 | Sulfoxidation | STIKNANMVAVLDQG HHCCCCCEEEEEECC | 1.58 | 21406390 | |
732 | Ubiquitination | IYRKLMNKQSFISA- HHHHHHCCHHHHCC- | 33.10 | - |
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 ABCBA_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ABCBA_HUMAN !! |
* 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 ABCBA_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NDUA2_HUMAN | NDUFA2 | physical | 22939629 | |
NDUBB_HUMAN | NDUFB11 | physical | 22939629 | |
ECSIT_HUMAN | ECSIT | physical | 22939629 | |
LTOR2_HUMAN | LAMTOR2 | physical | 22939629 | |
BAK_HUMAN | BAK1 | physical | 22939629 |
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. |
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Acetylation | |
Reference | PubMed |
"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-265, AND MASS SPECTROMETRY. |