SUCB2_HUMAN - dbPTM
SUCB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUCB2_HUMAN
UniProt AC Q96I99
Protein Name Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221}
Gene Name SUCLG2 {ECO:0000255|HAMAP-Rule:MF_03221}
Organism Homo sapiens (Human).
Sequence Length 432
Subcellular Localization Mitochondrion .
Protein Description GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit..
Protein Sequence MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLEDAAKKAVASVAKK
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-----MASPVAAQAG
-----CCCHHHHHHH		20.71-
47MalonylationLQEYQSKKLMSDNGV
HHHHHHHHHHHCCCC		55.4526320211
73AcetylationNEALEAAKRLNAKEI
HHHHHHHHHCCHHHH		65.5519608861
73SuccinylationNEALEAAKRLNAKEI
HHHHHHHHHCCHHHH		65.5523954790
73MalonylationNEALEAAKRLNAKEI
HHHHHHHHHCCHHHH		65.5526320211
78SuccinylationAAKRLNAKEIVLKAQ
HHHHCCHHHHHHHHH		47.07-
78SuccinylationAAKRLNAKEIVLKAQ
HHHHCCHHHHHHHHH		47.07-
78MalonylationAAKRLNAKEIVLKAQ
HHHHCCHHHHHHHHH		47.0726320211
93MalonylationILAGGRGKGVFNSGL
HHHCCCCCCCCCCCC		51.0126320211
101MalonylationGVFNSGLKGGVHLTK
CCCCCCCCCCEECCC		58.0826320211
101SuccinylationGVFNSGLKGGVHLTK
CCCCCCCCCCEECCC		58.0823954790
108AcetylationKGGVHLTKDPNVVGQ
CCCEECCCCCCHHHH		77.0226051181
108MalonylationKGGVHLTKDPNVVGQ
CCCEECCCCCCHHHH		77.0226320211
118UbiquitinationNVVGQLAKQMIGYNL
CHHHHHHHHHHCCCC		49.3322817900
118UbiquitinationNVVGQLAKQMIGYNL
CHHHHHHHHHHCCCC		49.3321890473
132SumoylationLATKQTPKEGVKVNK
CCCCCCCCCCCCCCE		71.18-
132SumoylationLATKQTPKEGVKVNK
CCCCCCCCCCCCCCE		71.18-
132AcetylationLATKQTPKEGVKVNK
CCCCCCCCCCCCCCE		71.18-
139AcetylationKEGVKVNKVMVAEAL
CCCCCCCEEEEEEHH		34.3926822725
149PhosphorylationVAEALDISRETYLAI
EEEHHHCCHHHHHHH		24.5921406692
152PhosphorylationALDISRETYLAILMD
HHHCCHHHHHHHHHC		23.7922210691
153PhosphorylationLDISRETYLAILMDR
HHCCHHHHHHHHHCC		6.8620068231
161PhosphorylationLAILMDRSCNGPVLV
HHHHHCCCCCCCEEE		13.99-
183PhosphorylationDIEEVAASNPELIFK
CHHHHHHHCHHHEEH		43.0822210691
200AcetylationIDIFEGIKDSQAQRM
HHHHCCCCHHHHHHH		63.28-
200UbiquitinationIDIFEGIKDSQAQRM
HHHHCCCCHHHHHHH		63.2829967540
207SulfoxidationKDSQAQRMAENLGFV
CHHHHHHHHHHCCCC		3.4928183972
218MethylationLGFVGPLKSQAADQI
CCCCCCCHHHHHHHH		43.5966694157
218AcetylationLGFVGPLKSQAADQI
CCCCCCCHHHHHHHH		43.5925953088
218MalonylationLGFVGPLKSQAADQI
CCCCCCCHHHHHHHH		43.5926320211
219PhosphorylationGFVGPLKSQAADQIT
CCCCCCHHHHHHHHH		32.5028102081
226PhosphorylationSQAADQITKLYNLFL
HHHHHHHHHHHHHHH		14.9028102081
227AcetylationQAADQITKLYNLFLK
HHHHHHHHHHHHHHC		51.0719608861
229PhosphorylationADQITKLYNLFLKID
HHHHHHHHHHHHCCC		16.0428152594
255GlutathionylationTPEGQVVCFDAKINF
CCCCCEEEEECEECC		2.4122555962
271AcetylationDNAEFRQKDIFAMDD
CCHHHHHHCEEEECC		48.8423236377
271SuccinylationDNAEFRQKDIFAMDD
CCHHHHHHCEEEECC		48.8427452117
271MalonylationDNAEFRQKDIFAMDD
CCHHHHHHCEEEECC		48.8426320211
279AcetylationDIFAMDDKSENEPIE
CEEEECCCCCCCCCC		56.2425038526
280PhosphorylationIFAMDDKSENEPIEN
EEEECCCCCCCCCCC		53.2828857561
291AcetylationPIENEAAKYDLKYIG
CCCCHHHHCCCEEEC		46.4719608861
338AcetylationLDLGGGVKEAQVYQA
ECCCCCCHHHHHHHH		51.0823954790
338SuccinylationLDLGGGVKEAQVYQA
ECCCCCCHHHHHHHH		51.08-
338MalonylationLDLGGGVKEAQVYQA
ECCCCCCHHHHHHHH		51.0826320211
338SuccinylationLDLGGGVKEAQVYQA
ECCCCCCHHHHHHHH		51.0827452117
343PhosphorylationGVKEAQVYQAFKLLT
CCHHHHHHHHHHHHC		5.09-
347AcetylationAQVYQAFKLLTADPK
HHHHHHHHHHCCCCC		45.6725953088
386UbiquitinationACRELELKVPLVVRL
HHHHHCCCCCEEEEE		32.2224816145
386AcetylationACRELELKVPLVVRL
HHHHHCCCCCEEEEE		32.22-
403AcetylationTNVQEAQKILNNSGL
CCHHHHHHHHHCCCC		57.0923236377
423SuccinylationIDLEDAAKKAVASVA
CCHHHHHHHHHHHHH		42.8823954790
423AcetylationIDLEDAAKKAVASVA
CCHHHHHHHHHHHHH		42.8825953088
424AcetylationDLEDAAKKAVASVAK
CHHHHHHHHHHHHHC		43.282391015
431AcetylationKAVASVAKK------
HHHHHHHCC------		57.782401413
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 SUCB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUCB2_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 SUCB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OZF_HUMANZNF146physical
26186194
DJC12_HUMANDNAJC12physical
26186194
GLT11_HUMANGALNT11physical
26186194
ACADM_HUMANACADMphysical
26344197
VATA_HUMANATP6V1Aphysical
26344197
TCPG_HUMANCCT3physical
26344197
TCPZ_HUMANCCT6Aphysical
26344197
CATD_HUMANCTSDphysical
26344197
ENPL_HUMANHSP90B1physical
26344197
IDH3A_HUMANIDH3Aphysical
26344197
LDHA_HUMANLDHAphysical
26344197
LDH6A_HUMANLDHAL6Aphysical
26344197
RPN1_HUMANRPN1physical
26344197
SUCA_HUMANSUCLG1physical
26344197
SUCA_HUMANSUCLG1physical
28514442
GLT11_HUMANGALNT11physical
28514442
OZF_HUMANZNF146physical
28514442
DJC12_HUMANDNAJC12physical
28514442
ORNT1_HUMANSLC25A15physical
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
DB00139Succinic acid
Regulatory Network of SUCB2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-227; LYS-291 ANDLYS-338, AND MASS SPECTROMETRY.

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