SUCA_RAT - dbPTM
SUCA_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUCA_RAT
UniProt AC P13086
Protein Name Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222}
Gene Name Suclg1 {ECO:0000255|HAMAP-Rule:MF_03222}
Organism Rattus norvegicus (Rat).
Sequence Length 346
Subcellular Localization Mitochondrion .
Protein Description Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits..
Protein Sequence MTAAVVAAAATATMVSGSSGLAAARLLSRTFLLQQNGIRHGSYTASRKNIYIDKNTKVICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGKKHLGLPVFNTVKEAKEKTGATASVIYVPPPFAAAAINEAIDAEIPLVVCITEGIPQQDMVRVKHKLTRQGKTRLIGPNCPGIINPGECKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCIGIGGDPFNGTNFIDCLDVFLKDPATEGIVLIGEIGGHAEENAAEFLKEHNSGPKAKPVVSFIAGITAPPGRRMGHAGAIIAGGKGGAKEKISALQSAGVIVSMSPAQLGTCMYKEFEKRKML
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
11PhosphorylationAVVAAAATATMVSGS
HHHHHHHHHHHHCCC
20.2426022182
48AcetylationGSYTASRKNIYIDKN
CCEECCCCEEEEECC
45.2422902405
48SuccinylationGSYTASRKNIYIDKN
CCEECCCCEEEEECC
45.2426843850
54AcetylationRKNIYIDKNTKVICQ
CCEEEEECCCEEEEC
57.8922902405
54SuccinylationRKNIYIDKNTKVICQ
CCEEEEECCCEEEEC
57.8926843850
57AcetylationIYIDKNTKVICQGFT
EEEECCCEEEECCCC
38.7122902405
57SuccinylationIYIDKNTKVICQGFT
EEEECCCEEEECCCC
38.71-
57SuccinylationIYIDKNTKVICQGFT
EEEECCCEEEECCCC
38.71-
66AcetylationICQGFTGKQGTFHSQ
EECCCCCCCCEECHH
42.3622902405
66SuccinylationICQGFTGKQGTFHSQ
EECCCCCCCCEECHH
42.36-
66SuccinylationICQGFTGKQGTFHSQ
EECCCCCCCCEECHH
42.36-
81AcetylationQALEYGTKLVGGTTP
HHHHHCCEEECCCCC
36.4922902405
86PhosphorylationGTKLVGGTTPGKGGK
CCEEECCCCCCCCCC
24.7228432305
87PhosphorylationTKLVGGTTPGKGGKK
CEEECCCCCCCCCCC
33.0628432305
90AcetylationVGGTTPGKGGKKHLG
ECCCCCCCCCCCCCC
66.7422902405
94AcetylationTPGKGGKKHLGLPVF
CCCCCCCCCCCCCCC
47.54-
103PhosphorylationLGLPVFNTVKEAKEK
CCCCCCCCHHHHHHH
22.8423984901
105AcetylationLPVFNTVKEAKEKTG
CCCCCCHHHHHHHHC
50.3322902405
108AcetylationFNTVKEAKEKTGATA
CCCHHHHHHHHCCEE
61.9222902405
156AcetylationQQDMVRVKHKLTRQG
HHHHHHHHEEHHHCC
25.1822902405
192AcetylationIMPGHIHKKGRIGIV
ECCCCCCCCCCEEEE
57.2122902405
271AcetylationENAAEFLKEHNSGPK
HHHHHHHHHCCCCCC
63.3522902405
278AcetylationKEHNSGPKAKPVVSF
HHCCCCCCCCCCEEE
72.9926302492
338SuccinylationQLGTCMYKEFEKRKM
HHCCHHHHHHHHHHC
29.10-
338SuccinylationQLGTCMYKEFEKRKM
HHCCHHHHHHHHHHC
29.10-
342AcetylationCMYKEFEKRKML---
HHHHHHHHHHCC---
63.7441680817

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 SUCA_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUCA_RAT !!

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 SUCA_RAT !!

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

Oops, there are no PPI records of SUCA_RAT !!

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

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Related Literatures of Post-Translational Modification

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