ADPPT_HUMAN - dbPTM
ADPPT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADPPT_HUMAN
UniProt AC Q9NRN7
Protein Name L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
Gene Name AASDHPPT
Organism Homo sapiens (Human).
Sequence Length 309
Subcellular Localization Cytoplasm .
Protein Description Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN..
Protein Sequence MVFPAKRFCLVPSMEGVRWAFSCGTWLPSRAEWLLAVRSIQPEEKERIGQFVFARDAKAAMAGRLMIRKLVAEKLNIPWNHIRLQRTAKGKPVLAKDSSNPYPNFNFNISHQGDYAVLAAEPELQVGIDIMKTSFPGRGSIPEFFHIMKRKFTNKEWETIRSFKDEWTQLDMFYRNWALKESFIKAIGVGLGFELQRLEFDLSPLNLDIGQVYKETRLFLDGEEEKEWAFEESKIDEHHFVAVALRKPDGSRHQDVPSQDDSKPTQRQFTILNFNDLMSSAVPMTPEDPSFWDCFCFTEEIPIRNGTKS
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
45UbiquitinationRSIQPEEKERIGQFV
HHCCHHHHHHHHHEE
51.10-
45UbiquitinationRSIQPEEKERIGQFV
HHCCHHHHHHHHHEE
51.1024816145
58AcetylationFVFARDAKAAMAGRL
EEHHHHHHHHHHHHH
40.7512436925
58UbiquitinationFVFARDAKAAMAGRL
EEHHHHHHHHHHHHH
40.7527667366
58UbiquitinationFVFARDAKAAMAGRL
EEHHHHHHHHHHHHH
40.75-
74UbiquitinationIRKLVAEKLNIPWNH
HHHHHHHHCCCCCHH
36.7829967540
74UbiquitinationIRKLVAEKLNIPWNH
HHHHHHHHCCCCCHH
36.78-
89UbiquitinationIRLQRTAKGKPVLAK
HEEEEECCCCCCEEC
67.8429967540
89AcetylationIRLQRTAKGKPVLAK
HEEEEECCCCCCEEC
67.8411924561
149UbiquitinationPEFFHIMKRKFTNKE
HHHHHHHHHHCCCCC
52.4021890473
149UbiquitinationPEFFHIMKRKFTNKE
HHHHHHHHHHCCCCC
52.4021906983
149AcetylationPEFFHIMKRKFTNKE
HHHHHHHHHHCCCCC
52.4023749302
151AcetylationFFHIMKRKFTNKEWE
HHHHHHHHCCCCCCH
51.5323749302
151MalonylationFFHIMKRKFTNKEWE
HHHHHHHHCCCCCCH
51.5326320211
151UbiquitinationFFHIMKRKFTNKEWE
HHHHHHHHCCCCCCH
51.5322817900
155UbiquitinationMKRKFTNKEWETIRS
HHHHCCCCCCHHHHH
62.2327667366
161MethylationNKEWETIRSFKDEWT
CCCCHHHHHHHHHHH
43.38-
164UbiquitinationWETIRSFKDEWTQLD
CHHHHHHHHHHHHHH
56.8621890473
164AcetylationWETIRSFKDEWTQLD
CHHHHHHHHHHHHHH
56.8626051181
164UbiquitinationWETIRSFKDEWTQLD
CHHHHHHHHHHHHHH
56.8621906983
168PhosphorylationRSFKDEWTQLDMFYR
HHHHHHHHHHHHHHH
19.7320068231
174PhosphorylationWTQLDMFYRNWALKE
HHHHHHHHHCHHHHH
9.0820068231
180UbiquitinationFYRNWALKESFIKAI
HHHCHHHHHHHHHHH
43.4923503661
182PhosphorylationRNWALKESFIKAIGV
HCHHHHHHHHHHHCC
30.5924719451
185UbiquitinationALKESFIKAIGVGLG
HHHHHHHHHHCCCCC
31.7623503661
214UbiquitinationLDIGQVYKETRLFLD
CCHHHHHEEEEEEEC
54.4721906983
226UbiquitinationFLDGEEEKEWAFEES
EECCHHHHHHCCCHH
62.9329967540
233PhosphorylationKEWAFEESKIDEHHF
HHHCCCHHCCCCCCE
27.9320068231
251PhosphorylationALRKPDGSRHQDVPS
EEECCCCCCCCCCCC
33.6928555341
258PhosphorylationSRHQDVPSQDDSKPT
CCCCCCCCCCCCCCC
46.2017525332
262PhosphorylationDVPSQDDSKPTQRQF
CCCCCCCCCCCCCEE
49.1528450419
263UbiquitinationVPSQDDSKPTQRQFT
CCCCCCCCCCCCEEE
60.1127667366
265PhosphorylationSQDDSKPTQRQFTIL
CCCCCCCCCCEEEEE
39.8723312004

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 ADPPT_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADPPT_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 ADPPT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHD1_HUMANEHD1physical
22863883
EHD4_HUMANEHD4physical
22863883
HNRH1_HUMANHNRNPH1physical
22863883
NOL3_HUMANNOL3physical
22863883
PLCG1_HUMANPLCG1physical
22863883
NIPA_HUMANZC3HC1physical
22863883
STIL_HUMANSTILphysical
26186194
POTEI_HUMANPOTEIphysical
26186194
UBP22_HUMANUSP22physical
26186194
TPPC4_HUMANTRAPPC4physical
26344197
UBP22_HUMANUSP22physical
28514442
POTEI_HUMANPOTEIphysical
28514442

Drug and Disease Associations
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.
Regulatory Network of ADPPT_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASSSPECTROMETRY.

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