Tag | Content |
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CPLM ID | CPLM-017475 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aminopeptidase O |
Protein Synonyms/Alias | AP-O |
Gene Name | AOPEP |
Gene Synonyms/Alias | C9orf3; ONPEP |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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55 | EDGNRFKKQNSSIEE | ubiquitination | [1] | 169 | AAVPGLEKFTRSPEL | ubiquitination | [1] | 231 | TWSLQIRKTGAQTAT | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart. |
Sequence Annotation | ACT_SITE 480 480 Proton acceptor (By similarity). METAL 479 479 Zinc; catalytic (By similarity). METAL 483 483 Zinc; catalytic (By similarity). METAL 502 502 Zinc; catalytic (By similarity). |
Keyword | Alternative splicing; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 819 AA |
Protein Sequence | MDIQLDPARD DLPLMANTSH ILVKHYVLDL DVDFESQVIE GTIVLFLEDG NRFKKQNSSI 60 EEACQSESNK ACKFGMPEPC HIPVTNARTF SSEMEYNDFA ICSKGEKDTS DKDGNHDNQE 120 HASGISSSKY CCDTGNHGSE DFLLVLDCCD LSVLKVEEVD VAAVPGLEKF TRSPELTVVS 180 EEFRNQIVRE LVTLPANRWR EQLDYYARCS QAPGCGELLF DTDTWSLQIR KTGAQTATDF 240 PHAIRIWYKT KPEGRSVTWT SDQSGRPCVY TVGSPINNRA LFPCQEPPVA MSTWQATVRA 300 AASFVVLMSG ENSAKPTQLW EECSSWYYYV TMPMPASTFT IAVGCWTEMK METWSSNDLA 360 TERPFSPSEA NFRHVGVCSH MEYPCRFQNA SATTQEIIPH RVFAPVCLTG ACQETLLRLI 420 PPCLSAAHSV LGAHPFSRLD VLIVPANFPS LGMASPHIMF LSQSILTGGN HLCGTRLCHE 480 IAHAWFGLAI GARDWTEEWL SEGFATHLED VFWATAQQLA PYEAREQQEL RACLRWRRLQ 540 DEMQCSPEEM QVLRPSKDKT GHTSDSGASV IKHGLNPEKI FMQVHYLKGY FLLRFLAKRL 600 GDETYFSFLR KFVHTFHGQL ILSQDFLQML LENIPEEKRL ELSVENIYQD WLESSGIPKP 660 LQRERRAGAE CGLARQVRAE VTKWIGVNRR PRKRKRREKE EVFEKLLPDQ LVLLLEHLLE 720 QKTLSPRTLQ SLQRTYHLQD QDAEVRHRWC ELIVKHKFTK AYKSVERFLQ EDQAMGVYLY 780 GELMVSEDAR QQQLARRCFE RTKEQMDRSS AQVVAEMLF 819 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004177; F:aminopeptidase activity; IDA:UniProtKB. GO:0008237; F:metallopeptidase activity; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0019370; P:leukotriene biosynthetic process; IEA:InterPro. GO:0006508; P:proteolysis; IDA:UniProtKB. |
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