| UniProt ID | CLPP_HUMAN | |
|---|---|---|
| UniProt AC | Q16740 | |
| Protein Name | ATP-dependent Clp protease proteolytic subunit, mitochondrial | |
| Gene Name | CLPP | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 277 | |
| Subcellular Localization | Mitochondrion matrix . | |
| Protein Description | Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates.. | |
| Protein Sequence | MWPGILVGGARVASCRYPALGPRLAAHFPAQRPPQRTLQNGLALQRCLHATATRALPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLVQKEPVEAAPAAEPVPAST | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 73 | Phosphorylation | TGRGERAYDIYSRLL CCCCCHHHHHHHHHH | 14.75 | 29496907 | |
| 77 | Phosphorylation | ERAYDIYSRLLRERI CHHHHHHHHHHHCCE | 19.45 | 24719451 | |
| 169 | Phosphorylation | GTPGMRHSLPNSRIM CCCCCCCCCCCCCEE | 34.85 | 20068231 | |
| 173 | Phosphorylation | MRHSLPNSRIMIHQP CCCCCCCCCEEEECC | 22.65 | 20068231 | |
| 176 | Sulfoxidation | SLPNSRIMIHQPSGG CCCCCCEEEECCCCC | 1.86 | 21406390 | |
| 181 | Phosphorylation | RIMIHQPSGGARGQA CEEEECCCCCCCCCH | 43.20 | 27251275 | |
| 189 | Phosphorylation | GGARGQATDIAIQAE CCCCCCHHHHHHHHH | 21.76 | 27251275 | |
| 199 | Sulfoxidation | AIQAEEIMKLKKQLY HHHHHHHHHHHHHHH | 4.74 | 21406390 | |
| 200 | Succinylation | IQAEEIMKLKKQLYN HHHHHHHHHHHHHHH | 63.92 | - | |
| 200 | Succinylation | IQAEEIMKLKKQLYN HHHHHHHHHHHHHHH | 63.92 | - | |
| 202 | Ubiquitination | AEEIMKLKKQLYNIY HHHHHHHHHHHHHHH | 32.71 | - | |
| 203 | Ubiquitination | EEIMKLKKQLYNIYA HHHHHHHHHHHHHHH | 56.84 | 29967540 | |
| 203 | Succinylation | EEIMKLKKQLYNIYA HHHHHHHHHHHHHHH | 56.84 | 27452117 | |
| 203 | Malonylation | EEIMKLKKQLYNIYA HHHHHHHHHHHHHHH | 56.84 | 26320211 | |
| 211 | Ubiquitination | QLYNIYAKHTKQSLQ HHHHHHHHHCHHHHH | 34.53 | 22817900 | |
| 211 | Acetylation | QLYNIYAKHTKQSLQ HHHHHHHHHCHHHHH | 34.53 | 19608861 | |
| 211 | Succinylation | QLYNIYAKHTKQSLQ HHHHHHHHHCHHHHH | 34.53 | 23954790 | |
| 214 | Ubiquitination | NIYAKHTKQSLQVIE HHHHHHCHHHHHHHH | 37.29 | 21963094 | |
| 214 | Acetylation | NIYAKHTKQSLQVIE HHHHHHCHHHHHHHH | 37.29 | 25038526 | |
| 230 | Sulfoxidation | AMERDRYMSPMEAQE HHHHCCCCCHHHHHH | 3.64 | 21406390 | |
| 231 | Phosphorylation | MERDRYMSPMEAQEF HHHCCCCCHHHHHHH | 16.50 | 28348404 | |
| 276 | Phosphorylation | AAEPVPAST------ CCCCCCCCC------ | 28.69 | 23401153 | |
| 277 | Phosphorylation | AEPVPAST------- CCCCCCCC------- | 44.74 | 30108239 |
| 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 CLPP_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLPP_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 CLPP_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CLPP_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 614129 | Perrault syndrome 3 (PRLTS3) | |||||
| 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-211, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277, AND MASSSPECTROMETRY. | |
