AT2L2_HUMAN - dbPTM
AT2L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT2L2_HUMAN
UniProt AC Q8IUZ5
Protein Name 5-phosphohydroxy-L-lysine phospho-lyase
Gene Name PHYKPL
Organism Homo sapiens (Human).
Sequence Length 450
Subcellular Localization Mitochondrion .
Protein Description Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde..
Protein Sequence MAADQRPKADTLALRQRLISSSCRLFFPEDPVKIVRAQGQYMYDEQGAEYIDCISNVAHVGHCHPLVVQAAHEQNQVLNTNSRYLHDNIVDYAQRLSETLPEQLCVFYFLNSGSEANDLALRLARHYTGHQDVVVLDHAYHGHLSSLIDISPYKFRNLDGQKEWVHVAPLPDTYRGPYREDHPNPAMAYANEVKRVVSSAQEKGRKIAAFFAESLPSVGGQIIPPAGYFSQVAEHIRKAGGVFVADEIQVGFGRVGKHFWAFQLQGKDFVPDIVTMGKSIGNGHPVACVAATQPVARAFEATGVEYFNTFGGSPVSCAVGLAVLNVLEKEQLQDHATSVGSFLMQLLGQQKIKHPIVGDVRGVGLFIGVDLIKDEATRTPATEEAAYLVSRLKENYVLLSTDGPGRNILKFKPPMCFSLDNARQVVAKLDAILTDMEEKVRSCETLRLQP
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
8UbiquitinationMAADQRPKADTLALR
CCCCCCCCHHHHHHH
62.17-
11PhosphorylationDQRPKADTLALRQRL
CCCCCHHHHHHHHHH
20.8428857561
20PhosphorylationALRQRLISSSCRLFF
HHHHHHHHHCCCEEC
22.3128857561
21PhosphorylationLRQRLISSSCRLFFP
HHHHHHHHCCCEECC
26.8528857561
22PhosphorylationRQRLISSSCRLFFPE
HHHHHHHCCCEECCC
9.1028857561
33AcetylationFFPEDPVKIVRAQGQ
ECCCCCHHEEEECCC
40.6519608861
33UbiquitinationFFPEDPVKIVRAQGQ
ECCCCCHHEEEECCC
40.65-
121UbiquitinationSEANDLALRLARHYT
CHHHHHHHHHHHHHC
6.3229967540
151PhosphorylationLSSLIDISPYKFRNL
HHHCCCCCCCEEECC
20.5926091039
153PhosphorylationSLIDISPYKFRNLDG
HCCCCCCCEEECCCC
18.9046160631
162UbiquitinationFRNLDGQKEWVHVAP
EECCCCCCCEEEEEC
60.1029967540
278OtherPDIVTMGKSIGNGHP
CCEEEECCCCCCCCC
28.25-
278UbiquitinationPDIVTMGKSIGNGHP
CCEEEECCCCCCCCC
28.25-
278N6-(pyridoxal phosphate)lysinePDIVTMGKSIGNGHP
CCEEEECCCCCCCCC
28.25-
279PhosphorylationDIVTMGKSIGNGHPV
CEEEECCCCCCCCCC
29.9628857561
352UbiquitinationQLLGQQKIKHPIVGD
HHHCCCCCCCCCCCC
4.2729967540
353UbiquitinationLLGQQKIKHPIVGDV
HHCCCCCCCCCCCCC
50.82-
393UbiquitinationAYLVSRLKENYVLLS
HHHHHHHHHCEEEEE
42.6829967540
398UbiquitinationRLKENYVLLSTDGPG
HHHHCEEEEECCCCC
1.8929967540
439UbiquitinationILTDMEEKVRSCETL
HHHCHHHHHHCCHHC
29.6429967540

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 AT2L2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT2L2_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 AT2L2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT2L2_HUMANPHYKPLphysical
16189514
AT2L2_HUMANPHYKPLphysical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AT2L2_HUMAN

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Related Literatures of Post-Translational Modification

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