KBL_HUMAN - dbPTM
KBL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KBL_HUMAN
UniProt AC O75600
Protein Name 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
Gene Name GCAT
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization Mitochondrion. Nucleus . Translocates to the nucleus upon cold and osmotic stress.
Protein Description
Protein Sequence MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRVDGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
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
45SuccinylationIRGAGTWKSERVITS
CCCCCCEECCEEEEC
42.13-
45SuccinylationIRGAGTWKSERVITS
CCCCCCEECCEEEEC
42.13-
45AcetylationIRGAGTWKSERVITS
CCCCCCEECCEEEEC
42.13-
51PhosphorylationWKSERVITSRQGPHI
EECCEEEECCCCCCE
18.2620068231
52PhosphorylationKSERVITSRQGPHIR
ECCEEEECCCCCCEE
16.1023532336
100PhosphorylationEEFGAGLSSVRFICG
HHHCCCHHHEEEEEC
26.3524719451
101PhosphorylationEFGAGLSSVRFICGT
HHCCCHHHEEEEECC
23.5024275569
113UbiquitinationCGTQSIHKNLEAKIA
ECCHHHHHCHHHHHH
62.65-
118UbiquitinationIHKNLEAKIARFHQR
HHHCHHHHHHHHHHC
27.76-
187SuccinylationDMADLEAKLQEAQKH
CHHHHHHHHHHHHHH
41.13-
187SuccinylationDMADLEAKLQEAQKH
CHHHHHHHHHHHHHH
41.13-
187AcetylationDMADLEAKLQEAQKH
CHHHHHHHHHHHHHH
41.1325953088
187UbiquitinationDMADLEAKLQEAQKH
CHHHHHHHHHHHHHH
41.13-
265N6-(pyridoxal phosphate)lysineIINSTLGKALGGASG
EEECHHHHHHCCCCC
43.48-
265OtherIINSTLGKALGGASG
EEECHHHHHHCCCCC
43.48-
274PhosphorylationLGGASGGYTTGPGPL
HCCCCCCCCCCCCHH
12.49-
292PhosphorylationLRQRARPYLFSNSLP
HHHHCCHHHHCCCCC
18.1522461510
307PhosphorylationPAVVGCASKALDLLM
HHHHHHHHHHHHHHH
23.6522461510
326SuccinylationIVQSMAAKTQRFRSK
HHHHHHHHHHHHHHH
35.34-
326SuccinylationIVQSMAAKTQRFRSK
HHHHHHHHHHHHHHH
35.34-
333UbiquitinationKTQRFRSKMEAAGFT
HHHHHHHHHHHCCEE
36.18-
368SuccinylationRMADDMLKRGIFVIG
HHHHHHHHCCEEEEE
41.77-
368AcetylationRMADDMLKRGIFVIG
HHHHHHHHCCEEEEE
41.772380539
368SuccinylationRMADDMLKRGIFVIG
HHHHHHHHCCEEEEE
41.77-
383SuccinylationFSYPVVPKGKARIRV
ECCCCCCCCEEEEEE
62.53-
383SuccinylationFSYPVVPKGKARIRV
ECCCCCCCCEEEEEE
62.53-
383AcetylationFSYPVVPKGKARIRV
ECCCCCCCCEEEEEE
62.53-
397PhosphorylationVQISAVHSEEDIDRC
EEEEECCCHHHHHHH
35.76-

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 KBL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KBL_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 KBL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDM2_HUMANMDM2physical
21988832
TEAD1_HUMANTEAD1physical
21988832
CLPX_HUMANCLPXphysical
26186194
LONM_HUMANLONP1physical
26186194
MCCA_HUMANMCCC1physical
26186194
EMB_HUMANEMBphysical
26186194
NDUS6_HUMANNDUFS6physical
26186194
EMB_HUMANEMBphysical
28514442
LONM_HUMANLONP1physical
28514442
NDUS6_HUMANNDUFS6physical
28514442
MCCA_HUMANMCCC1physical
28514442

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

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Related Literatures of Post-Translational Modification

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