SSDH_HUMAN - dbPTM
SSDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSDH_HUMAN
UniProt AC P51649
Protein Name Succinate-semialdehyde dehydrogenase, mitochondrial
Gene Name ALDH5A1
Organism Homo sapiens (Human).
Sequence Length 535
Subcellular Localization Mitochondrion.
Protein Description Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA)..
Protein Sequence MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
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-----MATCIWLRSC
-----CCEEEEECCC		11.8329083192
4S-palmitoylation----MATCIWLRSCG
----CCEEEEECCCC		1.2029575903
35PhosphorylationAGGLVPASGPAPGPA
CCCCCCCCCCCCCHH		38.9680535861
55PhosphorylationAGRLAGLSAALLRTD
HHHHHHHHHHHHCCC		15.58113634609
61PhosphorylationLSAALLRTDSFVGGR
HHHHHHCCCCCCCCC		35.6446162095
63PhosphorylationAALLRTDSFVGGRWL
HHHHCCCCCCCCCEE		22.6326074081
83PhosphorylationFPVQDPASGAALGMV
CCCCCCCCCHHHHHE		34.0646162077
121PhosphorylationEVSAKERSSLLRKWY
HCCHHHHHHHHHHHH		26.8221964256
122PhosphorylationVSAKERSSLLRKWYN
CCHHHHHHHHHHHHH		37.3323927012
126AcetylationERSSLLRKWYNLMIQ
HHHHHHHHHHHHHCC		54.7419608861
126SuccinylationERSSLLRKWYNLMIQ
HHHHHHHHHHHHHCC		54.74-
126SuccinylationERSSLLRKWYNLMIQ
HHHHHHHHHHHHHCC		54.74-
126MalonylationERSSLLRKWYNLMIQ
HHHHHHHHHHHHHCC		54.7426320211
128PhosphorylationSSLLRKWYNLMIQNK
HHHHHHHHHHHCCCH		11.06142047
135SuccinylationYNLMIQNKDDLARII
HHHHCCCHHHHHHHH		35.92-
135SuccinylationYNLMIQNKDDLARII
HHHHCCCHHHHHHHH		35.92-
135AcetylationYNLMIQNKDDLARII
HHHHCCCHHHHHHHH		35.9223954790
148UbiquitinationIITAESGKPLKEAHG
HHHCCCCCCHHHHHH		57.36-
175PhosphorylationSEEARRVYGDIIHTP
CHHHHHHHCCCCCCC		13.797301537
181PhosphorylationVYGDIIHTPAKDRRA
HHCCCCCCCHHCCCE		17.9618847512
184SuccinylationDIIHTPAKDRRALVL
CCCCCCHHCCCEEEE		53.63-
184SuccinylationDIIHTPAKDRRALVL
CCCCCCHHCCCEEEE		53.63-
214AcetylationPSAMITRKVGAALAA
CHHHHHHHHHHHHHC		36.057825119
265SuccinylationPCSRKNAKEVGEAIC
CCCCCCHHHHHHHHH		63.43-
265AcetylationPCSRKNAKEVGEAIC
CCCCCCHHHHHHHHH		63.43-
265SuccinylationPCSRKNAKEVGEAIC
CCCCCCHHHHHHHHH		63.4323954790
265UbiquitinationPCSRKNAKEVGEAIC
CCCCCCHHHHHHHHH		63.43-
273PhosphorylationEVGEAICTDPLVSKI
HHHHHHHCCCCCCEE		34.2420068231
278PhosphorylationICTDPLVSKISFTGS
HHCCCCCCEEEEECC		31.7720068231
279UbiquitinationCTDPLVSKISFTGST
HCCCCCCEEEEECCC		34.58-
285PhosphorylationSKISFTGSTTTGKIL
CEEEEECCCCCCHHH		21.3728857561
286PhosphorylationKISFTGSTTTGKILL
EEEEECCCCCCHHHH		29.7128857561
287PhosphorylationISFTGSTTTGKILLH
EEEECCCCCCHHHHH		34.9428857561
288PhosphorylationSFTGSTTTGKILLHH
EEECCCCCCHHHHHH		36.2428857561
301UbiquitinationHHAANSVKRVSMELG
HHHHHHCHHHHHHHC		47.07-
358AcetylationGIHDAFVKAFAEAMK
CHHHHHHHHHHHHHH		31.1919608861
365AcetylationKAFAEAMKKNLRVGN
HHHHHHHHHCCCCCC		45.6225953088
365SuccinylationKAFAEAMKKNLRVGN
HHHHHHHHHCCCCCC		45.6223954790
371AcetylationMKKNLRVGNGFEEGT
HHHCCCCCCCCCCCC		23.3119608861
378PhosphorylationGNGFEEGTTQGPLIN
CCCCCCCCCCCCCCC		21.1646162083
379PhosphorylationNGFEEGTTQGPLINE
CCCCCCCCCCCCCCH		42.2446162089
387AcetylationQGPLINEKAVEKVEK
CCCCCCHHHHHHHHH		53.9323236377
387UbiquitinationQGPLINEKAVEKVEK
CCCCCCHHHHHHHHH		53.93-
394AcetylationKAVEKVEKQVNDAVS
HHHHHHHHHHHHHHH		63.6325953088
402SuccinylationQVNDAVSKGATVVTG
HHHHHHHCCCEEEEC		46.06-
402SuccinylationQVNDAVSKGATVVTG
HHHHHHHCCCEEEEC		46.06-
4112-HydroxyisobutyrylationATVVTGGKRHQLGKN
CEEEECCCCCCCCCC		48.31-
411AcetylationATVVTGGKRHQLGKN
CEEEECCCCCCCCCC		48.31-
498PhosphorylationGVNEGLISSVECPFG
EECCCCEEEEECCCC		33.1168997293
499PhosphorylationVNEGLISSVECPFGG
ECCCCEEEEECCCCC		18.2314702039
524PhosphorylationSKYGIDEYLELKYVC
CCCCHHHHHEEEEEE		11.17110746295
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
181TPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSDH_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 SSDH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOM40_HUMANTOMM40physical
22939629
TIAR_HUMANTIAL1physical
22939629
VDAC1_HUMANVDAC1physical
22939629
MAGAB_HUMANMAGEA11physical
24722188
MTND_HUMANADI1physical
26344197
AL1B1_HUMANALDH1B1physical
26344197
ARF5_HUMANARF5physical
26344197
FUMH_HUMANFHphysical
26344197
SC31A_HUMANSEC31Aphysical
26344197
SC31B_HUMANSEC31Bphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
271980Succinic semialdehyde dehydrogenase deficiency (SSADHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SSDH_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-126 AND LYS-358, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory