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

loading...

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.

TOP