AL4A1_HUMAN - dbPTM
AL4A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AL4A1_HUMAN
UniProt AC P30038
Protein Name Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Gene Name ALDH4A1
Organism Homo sapiens (Human).
Sequence Length 563
Subcellular Localization Mitochondrion matrix.
Protein Description Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes..
Protein Sequence MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGRMEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWSYAYMQ
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
27PhosphorylationAGLRWKHTSSLKVAN
CCCCCEECCCCEECC		19.1125852190
28PhosphorylationGLRWKHTSSLKVANE
CCCCEECCCCEECCC		33.1325852190
29PhosphorylationLRWKHTSSLKVANEP
CCCEECCCCEECCCC		33.1125852190
31SuccinylationWKHTSSLKVANEPVL
CEECCCCEECCCCEE		41.05-
31SuccinylationWKHTSSLKVANEPVL
CEECCCCEECCCCEE		41.05-
41PhosphorylationNEPVLAFTQGSPERD
CCCEEEECCCCHHHH		26.8130108239
44PhosphorylationVLAFTQGSPERDALQ
EEEECCCCHHHHHHH		17.4829255136
52AcetylationPERDALQKALKDLKG
HHHHHHHHHHHHHCC		57.44-
93AcetylationNHGHKVAKFCYADKS
CCCCHHHHHHHCCHH		38.6725825284
93SuccinylationNHGHKVAKFCYADKS
CCCCHHHHHHHCCHH		38.67-
93MalonylationNHGHKVAKFCYADKS
CCCCHHHHHHHCCHH		38.6732601280
93SuccinylationNHGHKVAKFCYADKS
CCCCHHHHHHHCCHH		38.6727452117
96PhosphorylationHKVAKFCYADKSLLN
CHHHHHHHCCHHHHH		22.4422322641
99MalonylationAKFCYADKSLLNKAI
HHHHHCCHHHHHHHH		34.5332601280
99SuccinylationAKFCYADKSLLNKAI
HHHHHCCHHHHHHHH		34.53-
99AcetylationAKFCYADKSLLNKAI
HHHHHCCHHHHHHHH		34.5325953088
99SuccinylationAKFCYADKSLLNKAI
HHHHHCCHHHHHHHH		34.53-
100PhosphorylationKFCYADKSLLNKAIE
HHHHCCHHHHHHHHH		38.3424719451
104AcetylationADKSLLNKAIEAALA
CCHHHHHHHHHHHHH		51.1927178108
114AcetylationEAALAARKEWDLKPI
HHHHHHHHHCCCCCC		59.43-
114SuccinylationEAALAARKEWDLKPI
HHHHHHHHHCCCCCC		59.43-
114SuccinylationEAALAARKEWDLKPI
HHHHHHHHHCCCCCC		59.43-
119AcetylationARKEWDLKPIADRAQ
HHHHCCCCCCCHHHH		31.7227178108
119SuccinylationARKEWDLKPIADRAQ
HHHHCCCCCCCHHHH		31.7223954790
130AcetylationDRAQIFLKAADMLSG
HHHHHHHHHHHHHCC		30.6827178108
130SuccinylationDRAQIFLKAADMLSG
HHHHHHHHHHHHHCC		30.68-
130SuccinylationDRAQIFLKAADMLSG
HHHHHHHHHHHHHCC		30.68-
153MethylationKTMVGQGKTVIQAEI
HHHCCCCCCEEEHHH		31.56-
175SuccinylationDFFRFNAKYAVELEG
HHHHCCCEEEEEECC		34.54-
175AcetylationDFFRFNAKYAVELEG
HHHHCCCEEEEEECC		34.5425038526
175SuccinylationDFFRFNAKYAVELEG
HHHHCCCEEEEEECC		34.54-
304MethylationQVAQNLDRFHTFPRL
HHHHHHHHHCCCHHH		28.54-
318AcetylationLAGECGGKNFHFVHR
HCHHCCCCCEEEEEC		41.55-
326PhosphorylationNFHFVHRSADVESVV
CEEEEECCCCHHHHH		17.5946162053
331PhosphorylationHRSADVESVVSGTLR
ECCCCHHHHHHCCCC		27.8946162059
336PhosphorylationVESVVSGTLRSAFEY
HHHHHHCCCCHHHHH		16.1146162065
347SuccinylationAFEYGGQKCSACSRL
HHHHCCEECCCCCEE		33.17-
347SuccinylationAFEYGGQKCSACSRL
HHHHCCEECCCCCEE		33.17-
365AcetylationHSLWPQIKGRLLEEH
HHHHHHHHHHHHHHH		32.5025038526
376AcetylationLEEHSRIKVGDPAED
HHHHCCCCCCCCHHH		38.77-
395SuccinylationFSAVIDAKSFARIKK
HHHHHCHHHHHHHHH		42.21-
395SuccinylationFSAVIDAKSFARIKK
HHHHHCHHHHHHHHH		42.21-
402AcetylationKSFARIKKWLEHARS
HHHHHHHHHHHHHHC		55.4227178108
402MalonylationKSFARIKKWLEHARS
HHHHHHHHHHHHHHC		55.4226320211
409PhosphorylationKWLEHARSSPSLTIL
HHHHHHHCCCCEEEE		47.5928857561
410PhosphorylationWLEHARSSPSLTILA
HHHHHHCCCCEEEEE		16.9828857561
412PhosphorylationEHARSSPSLTILAGG
HHHHCCCCEEEEECC		39.8428348404
435UbiquitinationFVEPCIVESKDPQEP
EEEEEEEECCCCCCC		31.9621890473
444UbiquitinationKDPQEPIMKEEIFGP
CCCCCCCHHHHHCCC		6.99-
462AcetylationVYVYPDDKYKETLQL
EEECCCCHHHHHEEE		66.6520167786
495MethylationDVVQEATKVLRNAAG
HHHHHHHHHHHHHCC		46.44-
495UbiquitinationDVVQEATKVLRNAAG
HHHHHHHHHHHHHCC		46.4421890473
495"N6,N6-dimethyllysine"DVVQEATKVLRNAAG
HHHHHHHHHHHHHCC		46.44-
498MethylationQEATKVLRNAAGNFY
HHHHHHHHHHCCCEE		33.46-
505PhosphorylationRNAAGNFYINDKSTG
HHHCCCEEECCCCCC		11.6526074081
509SuccinylationGNFYINDKSTGSIVG
CCEEECCCCCCCEEE		45.49-
509SuccinylationGNFYINDKSTGSIVG
CCEEECCCCCCCEEE		45.49-
509AcetylationGNFYINDKSTGSIVG
CCEEECCCCCCCEEE		45.49-
510PhosphorylationNFYINDKSTGSIVGQ
CEEECCCCCCCEEEC		40.6426074081
511PhosphorylationFYINDKSTGSIVGQQ
EEECCCCCCCEEECC		40.4626074081
513PhosphorylationINDKSTGSIVGQQPF
ECCCCCCCEEECCCC		17.7526074081
528PhosphorylationGGARASGTNDKPGGP
CCCCCCCCCCCCCCC		37.4446162071
531AcetylationRASGTNDKPGGPHYI
CCCCCCCCCCCCEEE		47.86-
542PhosphorylationPHYILRWTSPQVIKE
CEEEEEECCHHHHHH		24.8928348404
543PhosphorylationHYILRWTSPQVIKET
EEEEEECCHHHHHHC		13.3328348404
552AcetylationQVIKETHKPLGDWSY
HHHHHCCCCCCCCCH		49.7325038526
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 AL4A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AL4A1_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 AL4A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ARGI1_HUMANARG1physical
21988832
AL4A1_HUMANALDH4A1physical
24502590
SAHH_HUMANAHCYphysical
26344197
ENOA_HUMANENO1physical
26344197
ENOB_HUMANENO3physical
26344197
ESTD_HUMANESDphysical
26344197
AATC_HUMANGOT1physical
26344197
PGM2_HUMANPGM2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
239510Hyperprolinemia 2 (HYRPRO2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AL4A1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND MASSSPECTROMETRY.

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