AL9A1_HUMAN - dbPTM
AL9A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AL9A1_HUMAN
UniProt AC P49189
Protein Name 4-trimethylaminobutyraldehyde dehydrogenase
Gene Name ALDH9A1
Organism Homo sapiens (Human).
Sequence Length 494
Subcellular Localization Cytoplasm.
Protein Description Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction..
Protein Sequence MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVCVEMGDVESAF
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
2Acetylation------MSTGTFVVS
------CCCCEEEEC
35.2322223895
2Phosphorylation------MSTGTFVVS
------CCCCEEEEC
35.2320068231
3Phosphorylation-----MSTGTFVVSQ
-----CCCCEEEECC
38.6520068231
5Phosphorylation---MSTGTFVVSQPL
---CCCCEEEECCCC
17.2220068231
9PhosphorylationSTGTFVVSQPLNYRG
CCCEEEECCCCCCCC
22.3020068231
11PhosphorylationGTFVVSQPLNYRGGA
CEEEECCCCCCCCCC
18.3118669648
14PhosphorylationVVSQPLNYRGGARVE
EECCCCCCCCCCEEC
20.5124043423
15MethylationVSQPLNYRGGARVEP
ECCCCCCCCCCEECC
35.68-
20PhosphorylationNYRGGARVEPADASG
CCCCCCEECCCCCCC
11.6527251275
26AcetylationRVEPADASGTEKAFE
EECCCCCCCCCCCCC
46.9620068231
26PhosphorylationRVEPADASGTEKAFE
EECCCCCCCCCCCCC
46.9620068231
28PhosphorylationEPADASGTEKAFEPA
CCCCCCCCCCCCCCC
31.6426437602
30AcetylationADASGTEKAFEPATG
CCCCCCCCCCCCCCC
59.2123954790
30MalonylationADASGTEKAFEPATG
CCCCCCCCCCCCCCC
59.2126320211
30SuccinylationADASGTEKAFEPATG
CCCCCCCCCCCCCCC
59.21-
30SuccinylationADASGTEKAFEPATG
CCCCCCCCCCCCCCC
59.2121890473
30UbiquitinationADASGTEKAFEPATG
CCCCCCCCCCCCCCC
59.2121890473
31UbiquitinationDASGTEKAFEPATGR
CCCCCCCCCCCCCCC
14.0624816145
33PhosphorylationSGTEKAFEPATGRVI
CCCCCCCCCCCCCEE
38.6020068231
42PhosphorylationATGRVIATFTCSGEK
CCCCEEEEEEECCCE
14.3526437602
44PhosphorylationGRVIATFTCSGEKEV
CCEEEEEEECCCEEH
11.0421406692
45GlutathionylationRVIATFTCSGEKEVN
CEEEEEEECCCEEHH
4.2622555962
46PhosphorylationVIATFTCSGEKEVNL
EEEEEEECCCEEHHH
47.1021406692
49AcetylationTFTCSGEKEVNLAVQ
EEEECCCEEHHHHHH
71.1826051181
49UbiquitinationTFTCSGEKEVNLAVQ
EEEECCCEEHHHHHH
71.18-
54UbiquitinationGEKEVNLAVQNAKAA
CCEEHHHHHHHHHHH
8.8121890473
54UbiquitinationGEKEVNLAVQNAKAA
CCEEHHHHHHHHHHH
8.8121890473
54UbiquitinationGEKEVNLAVQNAKAA
CCEEHHHHHHHHHHH
8.8127667366
59AcetylationNLAVQNAKAAFKIWS
HHHHHHHHHHHHHHH
48.0427452117
59SuccinylationNLAVQNAKAAFKIWS
HHHHHHHHHHHHHHH
48.04-
59SuccinylationNLAVQNAKAAFKIWS
HHHHHHHHHHHHHHH
48.04-
59UbiquitinationNLAVQNAKAAFKIWS
HHHHHHHHHHHHHHH
48.04-
63AcetylationQNAKAAFKIWSQKSG
HHHHHHHHHHHCCCH
38.2425953088
66PhosphorylationKAAFKIWSQKSGMER
HHHHHHHHCCCHHHH
31.0730576142
68AcetylationAFKIWSQKSGMERCR
HHHHHHCCCHHHHHH
43.3825953088
68UbiquitinationAFKIWSQKSGMERCR
HHHHHHCCCHHHHHH
43.3821890473
83UbiquitinationILLEAARIIREREDE
HHHHHHHHHHHCCCC
2.7429967540
87UbiquitinationAARIIREREDEIATM
HHHHHHHCCCCCEEE
46.9823000965
92UbiquitinationREREDEIATMECINN
HHCCCCCEEEEEHHC
9.99-
92NeddylationREREDEIATMECINN
HHCCCCCEEEEEHHC
9.9932015554
92UbiquitinationREREDEIATMECINN
HHCCCCCEEEEEHHC
9.9923000965
93PhosphorylationEREDEIATMECINNG
HCCCCCEEEEEHHCC
21.1124114839
94SulfoxidationREDEIATMECINNGK
CCCCCEEEEEHHCCC
2.6730846556
101AcetylationMECINNGKSIFEARL
EEEHHCCCCCEEEEE
42.3726051181
113PhosphorylationARLDIDISWQCLEYY
EEECCCCCHHHHHHH
13.8223663014
119PhosphorylationISWQCLEYYAGLAAS
CCHHHHHHHHHHHHH
5.9023663014
120PhosphorylationSWQCLEYYAGLAASM
CHHHHHHHHHHHHHH
5.7023663014
125UbiquitinationEYYAGLAASMAGEHI
HHHHHHHHHHCCCCC
12.6024816145
126PhosphorylationYYAGLAASMAGEHIQ
HHHHHHHHHCCCCCC
11.9823663014
138PhosphorylationHIQLPGGSFGYTRRE
CCCCCCCCCCCCCCC
22.7823663014
141PhosphorylationLPGGSFGYTRREPLG
CCCCCCCCCCCCCCC
8.6123663014
142PhosphorylationPGGSFGYTRREPLGV
CCCCCCCCCCCCCCE
24.5123663014
164PhosphorylationNYPFQIASWKSAPAL
CCCEEEECCCCCCEE
36.3424719451
169UbiquitinationIASWKSAPALACGNA
EECCCCCCEEECCCE
34.59-
176UbiquitinationPALACGNAMVFKPSP
CEEECCCEEEECCCC
4.84-
179UbiquitinationACGNAMVFKPSPFTP
ECCCEEEECCCCCCC
6.55-
228UbiquitinationQHPDVAKVSFTGSVP
CCCCEEEEEEECCCC
4.03-
228UbiquitinationQHPDVAKVSFTGSVP
CCCCEEEEEEECCCC
4.0323000965
229PhosphorylationHPDVAKVSFTGSVPT
CCCEEEEEEECCCCC
19.1820068231
231PhosphorylationDVAKVSFTGSVPTGM
CEEEEEEECCCCCCC
22.5028857561
233AcetylationAKVSFTGSVPTGMKI
EEEEEECCCCCCCCC
23.13-
233UbiquitinationAKVSFTGSVPTGMKI
EEEEEECCCCCCCCC
23.13-
233PhosphorylationAKVSFTGSVPTGMKI
EEEEEECCCCCCCCC
23.1320068231
233UbiquitinationAKVSFTGSVPTGMKI
EEEEEECCCCCCCCC
23.1321890473
236PhosphorylationSFTGSVPTGMKIMEM
EEECCCCCCCCCEEE
47.9926437602
238SulfoxidationTGSVPTGMKIMEMSA
ECCCCCCCCCEEECC
2.6821406390
239AcetylationGSVPTGMKIMEMSAK
CCCCCCCCCEEECCC
40.0025038526
239UbiquitinationGSVPTGMKIMEMSAK
CCCCCCCCCEEECCC
40.00-
240AcetylationSVPTGMKIMEMSAKG
CCCCCCCCEEECCCC
1.78-
240UbiquitinationSVPTGMKIMEMSAKG
CCCCCCCCEEECCCC
1.78-
240UbiquitinationSVPTGMKIMEMSAKG
CCCCCCCCEEECCCC
1.7822817900
246UbiquitinationKIMEMSAKGIKPVTL
CCEEECCCCCCCEEE
54.59-
246AcetylationKIMEMSAKGIKPVTL
CCEEECCCCCCCEEE
54.5926051181
246UbiquitinationKIMEMSAKGIKPVTL
CCEEECCCCCCCEEE
54.5930230243
249UbiquitinationEMSAKGIKPVTLELG
EECCCCCCCEEEECC
41.95-
253PhosphorylationKGIKPVTLELGGKSP
CCCCCEEEECCCCCC
5.3520068231
257PhosphorylationPVTLELGGKSPLIIF
CEEEECCCCCCEEEE
39.6324719451
263UbiquitinationGGKSPLIIFSDCDMN
CCCCCEEEEECCCCC
3.4029967540
267GlutathionylationPLIIFSDCDMNNAVK
CEEEEECCCCCHHHH
5.3222555962
269SulfoxidationIIFSDCDMNNAVKGA
EEEECCCCCHHHHHH
5.3930846556
270UbiquitinationIFSDCDMNNAVKGAL
EEECCCCCHHHHHHH
21.7629967540
273UbiquitinationDCDMNNAVKGALMAN
CCCCCHHHHHHHHHH
6.8029967540
274AcetylationCDMNNAVKGALMANF
CCCCHHHHHHHHHHC
35.74-
274UbiquitinationCDMNNAVKGALMANF
CCCCHHHHHHHHHHC
35.74-
274UbiquitinationCDMNNAVKGALMANF
CCCCHHHHHHHHHHC
35.7420639865
277UbiquitinationNNAVKGALMANFLTQ
CHHHHHHHHHHCCCC
4.5520639865
282UbiquitinationGALMANFLTQGQVCC
HHHHHHCCCCCCCCC
3.3329967540
298AcetylationGTRVFVQKEILDKFT
CEEEEEEHHHHHHHH
41.2319608861
298UbiquitinationGTRVFVQKEILDKFT
CEEEEEEHHHHHHHH
41.2327667366
303AcetylationVQKEILDKFTEEVVK
EEHHHHHHHHHHHHH
51.2223954790
303SuccinylationVQKEILDKFTEEVVK
EEHHHHHHHHHHHHH
51.22-
303SuccinylationVQKEILDKFTEEVVK
EEHHHHHHHHHHHHH
51.2221890473
303UbiquitinationVQKEILDKFTEEVVK
EEHHHHHHHHHHHHH
51.2221890473
310AcetylationKFTEEVVKQTQRIKI
HHHHHHHHHHCCCCC
53.4525038526
310MalonylationKFTEEVVKQTQRIKI
HHHHHHHHHHCCCCC
53.4526320211
310UbiquitinationKFTEEVVKQTQRIKI
HHHHHHHHHHCCCCC
53.45-
316MalonylationVKQTQRIKIGDPLLE
HHHHCCCCCCCCCCC
42.7126320211
316UbiquitinationVKQTQRIKIGDPLLE
HHHHCCCCCCCCCCC
42.71-
322AcetylationIKIGDPLLEDTRMGP
CCCCCCCCCCCCCCC
7.3319608861
322UbiquitinationIKIGDPLLEDTRMGP
CCCCCCCCCCCCCCC
7.3323000965
327UbiquitinationPLLEDTRMGPLINRP
CCCCCCCCCCCCCCH
7.6221890473
327UbiquitinationPLLEDTRMGPLINRP
CCCCCCCCCCCCCCH
7.6221890473
327UbiquitinationPLLEDTRMGPLINRP
CCCCCCCCCCCCCCH
7.6221890473
334UbiquitinationMGPLINRPHLERVLG
CCCCCCCHHHHHHHH
31.7422817900
340UbiquitinationRPHLERVLGFVKVAK
CHHHHHHHHHHHHHH
5.7330230243
344AcetylationERVLGFVKVAKEQGA
HHHHHHHHHHHHCCC
33.9323236377
344UbiquitinationERVLGFVKVAKEQGA
HHHHHHHHHHHHCCC
33.9320639865
347UbiquitinationLGFVKVAKEQGAKVL
HHHHHHHHHCCCEEE
54.262063986
352AcetylationVAKEQGAKVLCGGDI
HHHHCCCEEEECCCE
42.4326051181
355GlutathionylationEQGAKVLCGGDIYVP
HCCCEEEECCCEECC
6.8322555962
360PhosphorylationVLCGGDIYVPEDPKL
EEECCCEECCCCCCC
18.077442915
366AcetylationIYVPEDPKLKDGYYM
EECCCCCCCCCCEEE
79.2026051181
368UbiquitinationVPEDPKLKDGYYMRP
CCCCCCCCCCEEECC
56.0620639865
371UbiquitinationDPKLKDGYYMRPCVL
CCCCCCCEEECCEEE
12.2920639865
376UbiquitinationDGYYMRPCVLTNCRD
CCEEECCEEEECCCC
2.5029967540
390UbiquitinationDDMTCVKEEIFGPVM
CCCHHHHHHHHHCCE
35.6129967540
392UbiquitinationMTCVKEEIFGPVMSI
CHHHHHHHHHCCEEE
5.1927667366
416PhosphorylationLERANDTTFGLAAGV
HHHCCCCCCCCEEEE
20.6924076635
442PhosphorylationVAELQAGTCFINNYN
HHHHHCCCEEEECCC
13.7822468782
451PhosphorylationFINNYNVSPVELPFG
EEECCCCCCEECCCC
21.4222468782
460PhosphorylationVELPFGGYKKSGFGR
EECCCCCCCCCCCCC
18.6722468782
461AcetylationELPFGGYKKSGFGRE
ECCCCCCCCCCCCCC
43.68155651
462AcetylationLPFGGYKKSGFGREN
CCCCCCCCCCCCCCC
47.5324430995
473PhosphorylationGRENGRVTIEYYSQL
CCCCCEEEEEEECCC
13.5126356563
476PhosphorylationNGRVTIEYYSQLKTV
CCEEEEEEECCCCEE
12.4528102081
477PhosphorylationGRVTIEYYSQLKTVC
CEEEEEEECCCCEEE
4.1628152594
478PhosphorylationRVTIEYYSQLKTVCV
EEEEEEECCCCEEEE
28.3028152594
482PhosphorylationEYYSQLKTVCVEMGD
EEECCCCEEEEECCC
27.9429083192
484GlutathionylationYSQLKTVCVEMGDVE
ECCCCEEEEECCCHH
2.3122555962
487SulfoxidationLKTVCVEMGDVESAF
CCEEEEECCCHHHCC
2.5030846556
492PhosphorylationVEMGDVESAF-----
EECCCHHHCC-----
34.5229083192
497PhosphorylationVESAF----------
HHHCC----------
20068231
500PhosphorylationAF-------------
CC-------------
-

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 AL9A1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AL9A1_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 AL9A1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THIC_HUMANACAT2physical
22863883
CPIN1_HUMANCIAPIN1physical
22863883

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AL9A1_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-298, AND MASS SPECTROMETRY.

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