AMPO_HUMAN - dbPTM
AMPO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPO_HUMAN
UniProt AC Q8N6M6
Protein Name Aminopeptidase O
Gene Name AOPEP
Organism Homo sapiens (Human).
Sequence Length 819
Subcellular Localization Cytoplasm .
Protein 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..
Protein Sequence MDIQLDPARDDLPLMANTSHILVKHYVLDLDVDFESQVIEGTIVLFLEDGNRFKKQNSSIEEACQSESNKACKFGMPEPCHIPVTNARTFSSEMEYNDFAICSKGEKDTSDKDGNHDNQEHASGISSSKYCCDTGNHGSEDFLLVLDCCDLSVLKVEEVDVAAVPGLEKFTRSPELTVVSEEFRNQIVRELVTLPANRWREQLDYYARCSQAPGCGELLFDTDTWSLQIRKTGAQTATDFPHAIRIWYKTKPEGRSVTWTSDQSGRPCVYTVGSPINNRALFPCQEPPVAMSTWQATVRAAASFVVLMSGENSAKPTQLWEECSSWYYYVTMPMPASTFTIAVGCWTEMKMETWSSNDLATERPFSPSEANFRHVGVCSHMEYPCRFQNASATTQEIIPHRVFAPVCLTGACQETLLRLIPPCLSAAHSVLGAHPFSRLDVLIVPANFPSLGMASPHIMFLSQSILTGGNHLCGTRLCHEIAHAWFGLAIGARDWTEEWLSEGFATHLEDVFWATAQQLAPYEAREQQELRACLRWRRLQDEMQCSPEEMQVLRPSKDKTGHTSDSGASVIKHGLNPEKIFMQVHYLKGYFLLRFLAKRLGDETYFSFLRKFVHTFHGQLILSQDFLQMLLENIPEEKRLELSVENIYQDWLESSGIPKPLQRERRAGAECGLARQVRAEVTKWIGVNRRPRKRKRREKEEVFEKLLPDQLVLLLEHLLEQKTLSPRTLQSLQRTYHLQDQDAEVRHRWCELIVKHKFTKAYKSVERFLQEDQAMGVYLYGELMVSEDARQQQLARRCFERTKEQMDRSSAQVVAEMLF
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
36PhosphorylationDLDVDFESQVIEGTI
EECCCCCCCEEEEEE
29.73-
55UbiquitinationEDGNRFKKQNSSIEE
ECCCHHHHCCCCHHH
52.58-
58PhosphorylationNRFKKQNSSIEEACQ
CHHHHCCCCHHHHHH
30.14-
59PhosphorylationRFKKQNSSIEEACQS
HHHHCCCCHHHHHHC
41.38-
89PhosphorylationIPVTNARTFSSEMEY
CCCCCCCCCCCCCCC
26.0129052541
91PhosphorylationVTNARTFSSEMEYND
CCCCCCCCCCCCCCC
25.4429052541
92PhosphorylationTNARTFSSEMEYNDF
CCCCCCCCCCCCCCE
36.4529052541
96PhosphorylationTFSSEMEYNDFAICS
CCCCCCCCCCEEEEE
20.7929052541
103PhosphorylationYNDFAICSKGEKDTS
CCCEEEEECCCCCCC
37.2729052541
123PhosphorylationHDNQEHASGISSSKY
CCCCHHHCCCCCCCE
38.27-
126PhosphorylationQEHASGISSSKYCCD
CHHHCCCCCCCEECC
31.89-
127PhosphorylationEHASGISSSKYCCDT
HHHCCCCCCCEECCC
29.00-
128PhosphorylationHASGISSSKYCCDTG
HHCCCCCCCEECCCC
22.36-
169UbiquitinationAAVPGLEKFTRSPEL
EECCCHHHHCCCCCC
58.01-
193PhosphorylationQIVRELVTLPANRWR
HHHHHHHCCCCHHHH
39.3820860994
231UbiquitinationTWSLQIRKTGAQTAT
CEEEEEHHHCCCCCC
53.60-
232PhosphorylationWSLQIRKTGAQTATD
EEEEEHHHCCCCCCC
28.0924719451
250PhosphorylationAIRIWYKTKPEGRSV
EEEEEEECCCCCCCC
35.8124719451
256PhosphorylationKTKPEGRSVTWTSDQ
ECCCCCCCCEEECCC
34.4529083192
258PhosphorylationKPEGRSVTWTSDQSG
CCCCCCCEEECCCCC
25.0329083192
261PhosphorylationGRSVTWTSDQSGRPC
CCCCEEECCCCCCCE
25.80-
473UbiquitinationLTGGNHLCGTRLCHE
HCCCCCCCCHHHHHH
3.9929967540
572UbiquitinationDSGASVIKHGLNPEK
CCCCCHHHCCCCHHH
29.4829967540
586PhosphorylationKIFMQVHYLKGYFLL
HHHHHHHHHHHHHHH
15.97-
605PhosphorylationKRLGDETYFSFLRKF
HHHCCHHHHHHHHHH
8.65-

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 AMPO_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMPO_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 AMPO_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUN2_HUMANSUN2physical
22632968
LRC40_HUMANLRRC40physical
28514442
ZDH17_HUMANZDHHC17physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
SUZ12_HUMANSUZ12physical
28514442
TBB3_HUMANTUBB3physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMPO_HUMAN

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Related Literatures of Post-Translational Modification

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