SPYA_HUMAN - dbPTM
SPYA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPYA_HUMAN
UniProt AC P21549
Protein Name Serine--pyruvate aminotransferase
Gene Name AGXT
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization Peroxisome . Mitochondrion . Predominantly localized in the peroxisomes. Mitochondrial mistargeting occurs in variant proteins Arg-41, Arg-47, Ile-152, Arg-170 and Thr-244 associated with the disease HP1.
Protein Description
Protein Sequence MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCNATRENVDRVTEALRAALQHCPKKKL
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
3Phosphorylation-----MASHKLLVTP
-----CCCCCEEECC
21.6128258704
9PhosphorylationASHKLLVTPPKALLK
CCCCEEECCCHHHCC
33.5721902226
48PhosphorylationGGLQMIGSMSKDMYQ
HCCEEECCCCHHHHH
14.6821406692
50PhosphorylationLQMIGSMSKDMYQIM
CEEECCCCHHHHHHH
27.4821406692
81PhosphorylationLTLVISGSGHCALEA
EEEEECCCCCHHHHH
20.6969009055
194PhosphorylationSLGGTPLYMDRQGID
HCCCCCCEECCCCCE
9.737103239
205PhosphorylationQGIDILYSGSQKALN
CCCEEEEECCCCHHC
28.6425072903
207PhosphorylationIDILYSGSQKALNAP
CEEEEECCCCHHCCC
23.6725072903
209OtherILYSGSQKALNAPPG
EEEECCCCHHCCCCC
57.44-
209N6-(pyridoxal phosphate)lysineILYSGSQKALNAPPG
EEEECCCCHHCCCCC
57.44-
225SuccinylationSLISFSDKAKKKMYS
CEEECCHHHHHHHHC
61.99-
225AcetylationSLISFSDKAKKKMYS
CEEECCHHHHHHHHC
61.99-
225SuccinylationSLISFSDKAKKKMYS
CEEECCHHHHHHHHC
61.99-
228TrimethylationSFSDKAKKKMYSRKT
ECCHHHHHHHHCCCC
47.86-
228MethylationSFSDKAKKKMYSRKT
ECCHHHHHHHHCCCC
47.8623644510
231PhosphorylationDKAKKKMYSRKTKPF
HHHHHHHHCCCCCCE
17.7610409595
234AcetylationKKKMYSRKTKPFSFY
HHHHHCCCCCCEEEE
55.76-
235PhosphorylationKKMYSRKTKPFSFYL
HHHHCCCCCCEEEEE
42.7223898821
239PhosphorylationSRKTKPFSFYLDIKW
CCCCCCEEEEEEHHH
22.8523898821
241PhosphorylationKTKPFSFYLDIKWLA
CCCCEEEEEEHHHHH
11.4123898821
260PhosphorylationCDDQPRMYHHTIPVI
CCCCCCCCCCCCCEE
7.5421253578
271PhosphorylationIPVISLYSLRESLAL
CCEEEHHCHHHHHHH
26.6624719451
275PhosphorylationSLYSLRESLALIAEQ
EHHCHHHHHHHHHHH
16.7120873877
287PhosphorylationAEQGLENSWRQHREA
HHHCHHHHHHHHHHH
17.7920873877
297PhosphorylationQHREAAAYLHGRLQA
HHHHHHHHHHHHHHH
8.4321253578
312AcetylationLGLQLFVKDPALRLP
HCCCEEECCCCCCCC
51.14-
354PhosphorylationIMGGLGPSTGKVLRI
EECCCCCCCCCEEEE
48.2524275569
389AcetylationAALQHCPKKKL----
HHHHHCCCCCC----
68.8624885217

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 SPYA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPYA_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 SPYA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPYA_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
259900Hyperoxaluria primary 1 (HP1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00145Glycine
DB00160L-Alanine
DB00133L-Serine
Regulatory Network of SPYA_HUMAN

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Related Literatures of Post-Translational Modification

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