| UniProt ID | PCP_HUMAN | |
|---|---|---|
| UniProt AC | P42785 | |
| Protein Name | Lysosomal Pro-X carboxypeptidase | |
| Gene Name | PRCP | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 496 | |
| Subcellular Localization | Lysosome. | |
| Protein Description | Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.. | |
| Protein Sequence | MGRRALLLLLLSFLAPWATIALRPALRALGSLHLPTNPTSLPAVAKNYSVLYFQQKVDHFGFNTVKTFNQRYLVADKYWKKNGGSILFYTGNEGDIIWFCNNTGFMWDVAEELKAMLVFAEHRYYGESLPFGDNSFKDSRHLNFLTSEQALADFAELIKHLKRTIPGAENQPVIAIGGSYGGMLAAWFRMKYPHMVVGALAASAPIWQFEDLVPCGVFMKIVTTDFRKSGPHCSESIHRSWDAINRLSNTGSGLQWLTGALHLCSPLTSQDIQHLKDWISETWVNLAMVDYPYASNFLQPLPAWPIKVVCQYLKNPNVSDSLLLQNIFQALNVYYNYSGQVKCLNISETATSSLGTLGWSYQACTEVVMPFCTNGVDDMFEPHSWNLKELSDDCFQQWGVRPRPSWITTMYGGKNISSHTNIVFSNGELDPWSGGGVTKDITDTLVAVTISEGAHHLDLRTKNALDPMSVLLARSLEVRHMKNWIRDFYDSAGKQH | |
| 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 |
|---|---|---|---|---|---|
| 39 | O-linked_Glycosylation | LHLPTNPTSLPAVAK CCCCCCCCCHHHHHC | 44.99 | 55829669 | |
| 47 | N-linked_Glycosylation | SLPAVAKNYSVLYFQ CHHHHHCCCEEEEEE | 25.28 | UniProtKB CARBOHYD | |
| 47 | N-linked_Glycosylation | SLPAVAKNYSVLYFQ CHHHHHCCCEEEEEE | 25.28 | 20068230 | |
| 66 | Ubiquitination | HFGFNTVKTFNQRYL CCCCCCCCCCCCCEE | 45.41 | - | |
| 77 | Ubiquitination | QRYLVADKYWKKNGG CCEEEEEEEEEECCC | 43.18 | 21890473 | |
| 77 | Ubiquitination | QRYLVADKYWKKNGG CCEEEEEEEEEECCC | 43.18 | 21890473 | |
| 98 | Ubiquitination | GNEGDIIWFCNNTGF CCCCCEEEEECCCCC | 7.65 | 21890473 | |
| 98 | Ubiquitination | GNEGDIIWFCNNTGF CCCCCEEEEECCCCC | 7.65 | 21890473 | |
| 101 | N-linked_Glycosylation | GDIIWFCNNTGFMWD CCEEEEECCCCCCHH | 39.36 | 20540760 | |
| 116 | Sulfoxidation | VAEELKAMLVFAEHR HHHHHHHHHHHHHHC | 2.91 | 30846556 | |
| 137 | Ubiquitination | PFGDNSFKDSRHLNF CCCCCCCCCHHHHHC | 55.40 | 21890473 | |
| 164 | Phosphorylation | LIKHLKRTIPGAENQ HHHHHHHHCCCCCCC | 29.91 | 24719451 | |
| 185 | Phosphorylation | GSYGGMLAAWFRMKY CCHHHHHHHHHHCCC | 8.18 | 24719451 | |
| 317 | N-linked_Glycosylation | CQYLKNPNVSDSLLL HHHHCCCCCCHHHHH | 56.15 | 20540760 | |
| 336 | N-linked_Glycosylation | QALNVYYNYSGQVKC HHHCHHCCCCCCEEE | 13.55 | 20540760 | |
| 345 | N-linked_Glycosylation | SGQVKCLNISETATS CCCEEEEEEECCCCC | 45.25 | 20540760 | |
| 415 | N-linked_Glycosylation | TTMYGGKNISSHTNI EEEECCEECCCCCEE | 42.52 | 20540760 | |
| 462 | Ubiquitination | HHLDLRTKNALDPMS CCCCCCCCCCCCHHH | 33.51 | 21890473 | |
| 469 | Phosphorylation | KNALDPMSVLLARSL CCCCCHHHHHHHHHH | 18.27 | - |
| 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 PCP_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PCP_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 PCP_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| VDR_HUMAN | VDR | physical | 21988832 | |
| ISOC1_HUMAN | ISOC1 | physical | 22863883 | |
| NCDN_HUMAN | NCDN | physical | 22863883 | |
| NUCKS_HUMAN | NUCKS1 | physical | 22863883 | |
| PDIA4_HUMAN | PDIA4 | physical | 22863883 | |
| IPP2_HUMAN | PPP1R2 | physical | 22863883 | |
| PLPHP_HUMAN | PROSC | physical | 22863883 | |
| STK24_HUMAN | STK24 | physical | 22863883 |
| 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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| N-linked Glycosylation | |
| Reference | PubMed |
| "Structural definition and substrate specificity of the S28 proteasefamily: the crystal structure of human prolylcarboxypeptidase."; Soisson S.M., Patel S.B., Abeywickrema P.D., Byrne N.J., Diehl R.E.,Hall D.L., Ford R.E., Reid J.C., Rickert K.W., Shipman J.M.,Sharma S., Lumb K.J.; BMC Struct. Biol. 10:16-16(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 46-491, SUBUNIT, DISULFIDEBONDS, ACTIVE SITE, AND GLYCOSYLATION AT ASN-101; ASN-317; ASN-336;ASN-345 AND ASN-415. | |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317 AND ASN-415, AND MASSSPECTROMETRY. | |
