AASS_HUMAN - dbPTM
AASS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AASS_HUMAN
UniProt AC Q9UDR5
Protein Name Alpha-aminoadipic semialdehyde synthase, mitochondrial
Gene Name AASS
Organism Homo sapiens (Human).
Sequence Length 926
Subcellular Localization Mitochondrion.
Protein Description Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively..
Protein Sequence MLQVHRTGLGRLGVSLSKGLHHKAVLAVRREDVNAWERRAPLAPKHIKGITNLGYKVLIQPSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSRKTYAFFSHTIKAQEANMGLLDEILKQEIRLIDYEKMVDHRGVRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQAIFNELPCEYVEPHELKEVSQTGDLRKVYGTVLSRHHHLVRKTDAVYDPAEYDKHPERYISRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLAPGKFSPAGVEGCPALPHKLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFGDMLYPYVEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLRESRERAQSLSMGTRRKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSMDICKQEEKLGFLVAKQDLVISLLPYVLHPLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGELGLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSNNPLRYKFSWSPVGVLMNVMQSATYLLDGKVVNVAGGISFLDAVTSMDFFPGLNLEGYPNRDSTKYAEIYGISSAHTLLRGTLRYKGYMKALNGFVKLGLINREALPAFRPEANPLTWKQLLCDLVGISPSSEHDVLKEAVLKKLGGDNTQLEAAEWLGLLGDEQVPQAESILDALSKHLVMKLSYGPEEKDMIVMRDSFGIRHPSGHLEHKTIDLVAYGDINGFSAMAKTVGLPTAMAAKMLLDGEIGAKGLMGPFSKEIYGPILERIKAEGIIYTTQSTIKP
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
48AcetylationPLAPKHIKGITNLGY
CCCCHHHCCCCCCCC		43.94-
48MalonylationPLAPKHIKGITNLGY
CCCCHHHCCCCCCCC		43.9426320211
51PhosphorylationPKHIKGITNLGYKVL
CHHHCCCCCCCCEEE		32.8121406692
55PhosphorylationKGITNLGYKVLIQPS
CCCCCCCCEEEECCC		10.9021406692
56AcetylationGITNLGYKVLIQPSN
CCCCCCCEEEECCCC		28.85-
93SuccinylationACLILGVKRPPEEKL
HHHHHCCCCCHHHHH		58.34-
93AcetylationACLILGVKRPPEEKL
HHHHHCCCCCHHHHH		58.34-
93SuccinylationACLILGVKRPPEEKL
HHHHHCCCCCHHHHH		58.34-
128AcetylationGLLDEILKQEIRLID
CHHHHHHHHHHHHCC		52.09-
138SuccinylationIRLIDYEKMVDHRGV
HHHCCHHHCCCCCCE		37.69-
138AcetylationIRLIDYEKMVDHRGV
HHHCCHHHCCCCCCE		37.6925953088
138SuccinylationIRLIDYEKMVDHRGV
HHHCCHHHCCCCCCE		37.69-
203PhosphorylationQAVRDAGYEISLGLM
HHHHHCCCEEEEECC		16.2921406692
206PhosphorylationRDAGYEISLGLMPKS
HHCCCEEEEECCCCC		12.4021406692
212AcetylationISLGLMPKSIGPLTF
EEEECCCCCCCCEEE		40.5119812187
229AcetylationTGTGNVSKGAQAIFN
ECCCCCCHHHHHHHH		54.7219812195
249AcetylationYVEPHELKEVSQTGD
CCCHHHHEEEHHCCC		53.7525038526
261PhosphorylationTGDLRKVYGTVLSRH
CCCHHHHHHHHHHHC		15.3221406692
263PhosphorylationDLRKVYGTVLSRHHH
CHHHHHHHHHHHCHH		10.6921406692
266PhosphorylationKVYGTVLSRHHHLVR
HHHHHHHHHCHHHHC		25.8221406692
274SuccinylationRHHHLVRKTDAVYDP
HCHHHHCCCCCCCCH		43.19-
274SuccinylationRHHHLVRKTDAVYDP
HCHHHHCCCCCCCCH		43.19-
286SuccinylationYDPAEYDKHPERYIS
CCHHHHCCCHHHHHH		61.22-
286SuccinylationYDPAEYDKHPERYIS
CCHHHHCCCHHHHHH		61.22-
286AcetylationYDPAEYDKHPERYIS
CCHHHHCCCHHHHHH		61.2225038526
286MalonylationYDPAEYDKHPERYIS
CCHHHHCCCHHHHHH		61.2226320211
333SuccinylationQSLLAPGKFSPAGVE
HHHHCCCCCCCCCCC		41.43-
333SuccinylationQSLLAPGKFSPAGVE
HHHHCCCCCCCCCCC		41.43-
458AcetylationSNGTLPDKYKYIQTL
CCCCCCHHHHHHHHH		41.5225038526
458SuccinylationSNGTLPDKYKYIQTL
CCCCCCHHHHHHHHH		41.52-
458SuccinylationSNGTLPDKYKYIQTL
CCCCCCHHHHHHHHH		41.52-
461PhosphorylationTLPDKYKYIQTLRES
CCCHHHHHHHHHHHH		8.658228037
474PhosphorylationESRERAQSLSMGTRR
HHHHHHHHCCCCCCC		22.7922147821
479PhosphorylationAQSLSMGTRRKVLVL
HHHCCCCCCCEEEEE		20.7522147829
488PhosphorylationRKVLVLGSGYISEPV
CEEEEECCCCCCHHH		25.0222817901
492PhosphorylationVLGSGYISEPVLEYL
EECCCCCCHHHHHHH		27.6222817901
513SulfoxidationEITVGSDMKNQIEQL
EEEECCCHHHHHHHH		4.7421406390
522AcetylationNQIEQLGKKYNINPV
HHHHHHHHHCCCCCC		61.7525953088
523SuccinylationQIEQLGKKYNINPVS
HHHHHHHHCCCCCCC		41.55-
523AcetylationQIEQLGKKYNINPVS
HHHHHHHHCCCCCCC		41.55-
523SuccinylationQIEQLGKKYNINPVS
HHHHHHHHCCCCCCC		41.55-
524PhosphorylationIEQLGKKYNINPVSM
HHHHHHHCCCCCCCH		25.4321406692
530PhosphorylationKYNINPVSMDICKQE
HCCCCCCCHHHHHHH		16.4021406692
535SuccinylationPVSMDICKQEEKLGF
CCCHHHHHHHHHHCC		62.16-
535SuccinylationPVSMDICKQEEKLGF
CCCHHHHHHHHHHCC		62.16-
535AcetylationPVSMDICKQEEKLGF
CCCHHHHHHHHHHCC		62.1625038526
539UbiquitinationDICKQEEKLGFLVAK
HHHHHHHHHCCEEEC		53.8321890473
539AcetylationDICKQEEKLGFLVAK
HHHHHHHHHCCEEEC		53.8325038526
556PhosphorylationLVISLLPYVLHPLVA
HHHHHHHHHHHHHHH		18.6620562403
575PhosphorylationTNKVNMVTASYITPA
CCCCCCHHHHHHHHH		10.1020363803
577PhosphorylationKVNMVTASYITPALK
CCCCHHHHHHHHHHH		14.0120363803
578PhosphorylationVNMVTASYITPALKE
CCCHHHHHHHHHHHH		13.3220363803
580PhosphorylationMVTASYITPALKELE
CHHHHHHHHHHHHHH		8.3525072903
584SuccinylationSYITPALKELEKSVE
HHHHHHHHHHHHHHH		63.46-
584AcetylationSYITPALKELEKSVE
HHHHHHHHHHHHHHH		63.46-
584SuccinylationSYITPALKELEKSVE
HHHHHHHHHHHHHHH		63.46-
700PhosphorylationPGLNLEGYPNRDSTK
CCCCCCCCCCCCCCC		6.4850558297
707AcetylationYPNRDSTKYAEIYGI
CCCCCCCCCCEEECC		46.5519608861
730PhosphorylationGTLRYKGYMKALNGF
HCHHHHHHHHHHCCH		7.416866079
732SuccinylationLRYKGYMKALNGFVK
HHHHHHHHHHCCHHE		41.04-
732SuccinylationLRYKGYMKALNGFVK
HHHHHHHHHHCCHHE		41.04-
739AcetylationKALNGFVKLGLINRE
HHHCCHHEECCCCHH		34.28-
761SuccinylationEANPLTWKQLLCDLV
CCCCCCHHHHHHHHH		26.32-
761SuccinylationEANPLTWKQLLCDLV
CCCCCCHHHHHHHHH		26.32-
761AcetylationEANPLTWKQLLCDLV
CCCCCCHHHHHHHHH		26.32-
780AcetylationSSEHDVLKEAVLKKL
CCHHHHHHHHHHHHH		43.40-
873PhosphorylationGFSAMAKTVGLPTAM
HHHHHHHHCCCCHHH		15.4021406692
878PhosphorylationAKTVGLPTAMAAKML
HHHCCCCHHHHHHHH		33.8237816849
893UbiquitinationLDGEIGAKGLMGPFS
HCCCCCCCCCCCCCC		47.5721890473
904PhosphorylationGPFSKEIYGPILERI
CCCCHHCHHHHHHHH		20.2423403867
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 AASS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AASS_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 AASS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACADM_HUMANACADMphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
238700Hyperlysinemia, 1 (HYPLYS1)
6160342,4-dienoyl-CoA reductase deficiency (DECRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AASS_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-707, AND MASS SPECTROMETRY.

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