TXTP_HUMAN - dbPTM
TXTP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TXTP_HUMAN
UniProt AC P53007
Protein Name Tricarboxylate transport protein, mitochondrial
Gene Name SLC25A1
Organism Homo sapiens (Human).
Sequence Length 311
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein.
Protein Description Involved in citrate-H(+)/malate exchange. Important for the bioenergetics of hepatic cells as it provides a carbon source for fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic pathway..
Protein Sequence MPAPRAPRALAAAAPASGKAKLTHPGKAILAGGLAGGIEICITFPTEYVKTQLQLDERSHPPRYRGIGDCVRQTVRSHGVLGLYRGLSSLLYGSIPKAAVRFGMFEFLSNHMRDAQGRLDSTRGLLCGLGAGVAEAVVVVCPMETIKVKFIHDQTSPNPKYRGFFHGVREIVREQGLKGTYQGLTATVLKQGSNQAIRFFVMTSLRNWYRGDNPNKPMNPLITGVFGAIAGAASVFGNTPLDVIKTRMQGLEAHKYRNTWDCGLQILKKEGLKAFYKGTVPRLGRVCLDVAIVFVIYDEVVKLLNKVWKTD
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
17PhosphorylationLAAAAPASGKAKLTH
HHHHCCCCCCCCCCC		39.5029396449
19UbiquitinationAAAPASGKAKLTHPG
HHCCCCCCCCCCCCC		39.59-
21AcetylationAPASGKAKLTHPGKA
CCCCCCCCCCCCCCC		58.3625953088
21UbiquitinationAPASGKAKLTHPGKA
CCCCCCCCCCCCCCC		58.36-
48PhosphorylationCITFPTEYVKTQLQL
EEECCHHHHHHHHHH		15.1026074081
51PhosphorylationFPTEYVKTQLQLDER
CCHHHHHHHHHHCCC		25.1926074081
65MethylationRSHPPRYRGIGDCVR
CCCCCCCCCHHHHHH		31.37115917061
70S-nitrosylationRYRGIGDCVRQTVRS
CCCCHHHHHHHHHHH		1.9824105792
74PhosphorylationIGDCVRQTVRSHGVL
HHHHHHHHHHHCCHH		13.8127080861
88PhosphorylationLGLYRGLSSLLYGSI
HHHHHHHHHHHHCCC		23.0528152594
89PhosphorylationGLYRGLSSLLYGSIP
HHHHHHHHHHHCCCC		27.6928152594
92PhosphorylationRGLSSLLYGSIPKAA
HHHHHHHHCCCCHHH		17.7028152594
94PhosphorylationLSSLLYGSIPKAAVR
HHHHHHCCCCHHHHH		23.3528152594
97AcetylationLLYGSIPKAAVRFGM
HHHCCCCHHHHHHHH		47.5119608861
97UbiquitinationLLYGSIPKAAVRFGM
HHHCCCCHHHHHHHH		47.5121890473
121PhosphorylationDAQGRLDSTRGLLCG
HHCCCCCCCHHHHHH		25.2922210691
122PhosphorylationAQGRLDSTRGLLCGL
HCCCCCCCHHHHHHC		28.5522210691
149AcetylationPMETIKVKFIHDQTS
CCCEEEEEEECCCCC		33.3325825284
149UbiquitinationPMETIKVKFIHDQTS
CCCEEEEEEECCCCC		33.33-
155PhosphorylationVKFIHDQTSPNPKYR
EEEECCCCCCCHHHC		52.8130266825
156PhosphorylationKFIHDQTSPNPKYRG
EEECCCCCCCHHHCC		19.6330266825
1602-HydroxyisobutyrylationDQTSPNPKYRGFFHG
CCCCCCHHHCCHHHH		54.97-
160AcetylationDQTSPNPKYRGFFHG
CCCCCCHHHCCHHHH		54.9719608861
160UbiquitinationDQTSPNPKYRGFFHG
CCCCCCHHHCCHHHH		54.9721890473
178MethylationIVREQGLKGTYQGLT
HHHHCCCCCEECCEE		56.912418839
178MalonylationIVREQGLKGTYQGLT
HHHHCCCCCEECCEE		56.9126320211
178UbiquitinationIVREQGLKGTYQGLT
HHHHCCCCCEECCEE		56.9121890473
187PhosphorylationTYQGLTATVLKQGSN
EECCEEEEEECCCCC		22.5727080861
190UbiquitinationGLTATVLKQGSNQAI
CEEEEEECCCCCHHH		48.5621890473
190MalonylationGLTATVLKQGSNQAI
CEEEEEECCCCCHHH		48.5626320211
204PhosphorylationIRFFVMTSLRNWYRG
HHHHHHHHHHHHHCC		13.7722210691
255AcetylationMQGLEAHKYRNTWDC
HCHHHHHHCCCCHHH		53.6125825284
255MalonylationMQGLEAHKYRNTWDC
HCHHHHHHCCCCHHH		53.6126320211
255UbiquitinationMQGLEAHKYRNTWDC
HCHHHHHHCCCCHHH		53.6119608861
2552-HydroxyisobutyrylationMQGLEAHKYRNTWDC
HCHHHHHHCCCCHHH		53.61-
256PhosphorylationQGLEAHKYRNTWDCG
CHHHHHHCCCCHHHH		10.1420068231
2682-HydroxyisobutyrylationDCGLQILKKEGLKAF
HHHCHHHHHHCCHHH		50.86-
268MalonylationDCGLQILKKEGLKAF
HHHCHHHHHHCCHHH		50.8626320211
268AcetylationDCGLQILKKEGLKAF
HHHCHHHHHHCCHHH		50.8625038526
276PhosphorylationKEGLKAFYKGTVPRL
HHCCHHHHCCCCCCH		17.2322817900
277MalonylationEGLKAFYKGTVPRLG
HCCHHHHCCCCCCHH		41.4726320211
277AcetylationEGLKAFYKGTVPRLG
HCCHHHHCCCCCCHH		41.4725825284
277SuccinylationEGLKAFYKGTVPRLG
HCCHHHHCCCCCCHH		41.4723954790
297PhosphorylationVAIVFVIYDEVVKLL
EEHHHHHHHHHHHHH		10.7619835603
306UbiquitinationEVVKLLNKVWKTD--
HHHHHHHHHHCCC--		49.82-
306AcetylationEVVKLLNKVWKTD--
HHHHHHHHHHCCC--		49.8225825284
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 TXTP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TXTP_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 TXTP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIC60_HUMANIMMTphysical
26344197
RL9_HUMANRPL9physical
26344197
RS26_HUMANRPS26physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
Drug and Disease Associations
Kegg Disease
OMIM Disease
615182Combined D-2- and L-2-hydroxyglutaric aciduria (D2L2AD)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TXTP_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-97; LYS-160 AND LYS-255, ANDMASS SPECTROMETRY.

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