dbPTM

AL1A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AL1A1_HUMAN
UniProt AC	P00352
Protein Name	Retinal dehydrogenase 1 {ECO:0000305}
Gene Name	ALDH1A1 {ECO:0000312\|HGNC:HGNC:402}
Organism	Homo sapiens (Human).
Sequence Length	501
Subcellular Localization	Cytoplasm, cytosol .
Protein Description	Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo. [PubMed: 19296407]
Protein Sequence	MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSSGTPDL ------CCCCCCCCC	32.96	6723659
2	Acetylation	------MSSSGTPDL ------CCCCCCCCC	32.96	6723659
3	Phosphorylation	-----MSSSGTPDLP -----CCCCCCCCCC	31.33	29116813
4	Phosphorylation	----MSSSGTPDLPV ----CCCCCCCCCCC	39.10	29116813
6	Phosphorylation	--MSSSGTPDLPVLL --CCCCCCCCCCCEE	18.64	23401153
14	Phosphorylation	PDLPVLLTDLKIQYT CCCCCEEEEEEEEEE	34.81	23401153
20	Phosphorylation	LTDLKIQYTKIFINN EEEEEEEEEEEEECC	17.30	23401153
21	Phosphorylation	TDLKIQYTKIFINNE EEEEEEEEEEEECCC	10.99	23401153
22	Acetylation	DLKIQYTKIFINNEW EEEEEEEEEEECCCE	30.59	25825284
45	Phosphorylation	FPVFNPATEEELCQV CCCCCCCCHHHHHCC	45.23	28258704
65	Acetylation	EDVDKAVKAARQAFQ HHHHHHHHHHHHHHH	40.98	129459
68	Dimethylation	DKAVKAARQAFQIGS HHHHHHHHHHHHCCC	32.97	-
75	Phosphorylation	RQAFQIGSPWRTMDA HHHHHCCCCCCCCCH	23.95	27422710
79	Phosphorylation	QIGSPWRTMDASERG HCCCCCCCCCHHHHH	18.61	22210691
80	Sulfoxidation	IGSPWRTMDASERGR CCCCCCCCCHHHHHH	2.80	30846556
85	Dimethylation	RTMDASERGRLLYKL CCCCHHHHHHHHHHH	32.79	-
91	Acetylation	ERGRLLYKLADLIER HHHHHHHHHHHHHHH	36.85	19608861
105	Phosphorylation	RDRLLLATMESMNGG HHHHHHHHHHHHCCC	22.80	46161923
108	Phosphorylation	LLLATMESMNGGKLY HHHHHHHHHCCCEEC	13.51	20071362
119	Phosphorylation	GKLYSNAYLNDLAGC CEECCCHHHHHHHHH	15.41	21253578
128	Ubiquitination	NDLAGCIKTLRYCAG HHHHHHHHHHHHHHC	45.65	19608861
128	Acetylation	NDLAGCIKTLRYCAG HHHHHHHHHHHHHHC	45.65	19608861
139	Ubiquitination	YCAGWADKIQGRTIP HHHCHHHHCCCEEEE	29.22	-
139	Acetylation	YCAGWADKIQGRTIP HHHCHHHHCCCEEEE	29.22	25825284
144	Phosphorylation	ADKIQGRTIPIDGNF HHHCCCEEEEECCCE	37.62	101661369
154	Phosphorylation	IDGNFFTYTRHEPIG ECCCEEEEECCCCCC	9.16	21253578
207	Phosphorylation	LTALHVASLIKEAGF CHHHHHHHHHHHHCC	29.55	24719451
237	Sulfoxidation	GAAISSHMDIDKVAF HHHHHHCCCCCEEEE	5.37	30846556
252	Acetylation	TGSTEVGKLIKEAAG ECCHHHHHHHHHHCC	52.82	19608861
267	Phosphorylation	KSNLKRVTLELGGKS CCCCCEEEEECCCCC	20.67	22617229
314	Phosphorylation	SRIFVEESIYDEFVR EEEEEEHHHHHHHHH	16.97	27422710
316	Phosphorylation	IFVEESIYDEFVRRS EEEEHHHHHHHHHHH	20.78	80588799
330	Phosphorylation	SVERAKKYILGNPLT HHHHHHHHHCCCCCC	10.73	23312004
337	Phosphorylation	YILGNPLTPGVTQGP HHCCCCCCCCCCCCC	21.18	30206219
341	Phosphorylation	NPLTPGVTQGPQIDK CCCCCCCCCCCCCCH	33.45	26699800
353	Acetylation	IDKEQYDKILDLIES CCHHHHHHHHHHHHH	39.99	19608861
360	Phosphorylation	KILDLIESGKKEGAK HHHHHHHHCCCCCCE	49.25	20068231
362	Acetylation	LDLIESGKKEGAKLE HHHHHHCCCCCCEEE	57.86	15617161
367	Acetylation	SGKKEGAKLECGGGP HCCCCCCEEEECCCC	56.53	19608861
394	Sulfoxidation	FSNVTDEMRIAKEEI ECCCCHHHHHHHHHH	4.12	30846556
398	Ubiquitination	TDEMRIAKEEIFGPV CHHHHHHHHHHHCHH	54.21	-
409	Sulfoxidation	FGPVQQIMKFKSLDD HCHHHHHHHHCCHHH	3.47	30846556
410	Acetylation	GPVQQIMKFKSLDDV CHHHHHHHHCCHHHH	51.79	19608861
412	Acetylation	VQQIMKFKSLDDVIK HHHHHHHCCHHHHHH	44.59	25825284
412	Ubiquitination	VQQIMKFKSLDDVIK HHHHHHHCCHHHHHH	44.59	-
413	Phosphorylation	QQIMKFKSLDDVIKR HHHHHHCCHHHHHHH	39.91	26657352
419	Acetylation	KSLDDVIKRANNTFY CCHHHHHHHHHCCEE	45.35	19608861
424	Phosphorylation	VIKRANNTFYGLSAG HHHHHHCCEECCCEE	20.31	24881967
426	Phosphorylation	KRANNTFYGLSAGVF HHHHCCEECCCEEEE	18.34	75283
429	Phosphorylation	NNTFYGLSAGVFTKD HCCEECCCEEEECCC	20.72	46161917
435	Acetylation	LSAGVFTKDIDKAIT CCEEEECCCHHHHHC	41.02	19608861
435	Ubiquitination	LSAGVFTKDIDKAIT CCEEEECCCHHHHHC	41.02	19608861
442	Phosphorylation	KDIDKAITISSALQA CCHHHHHCHHHHHHC	21.48	126141601
481	Phosphorylation	NGRELGEYGFHEYTE CCCCCCCCCCEECEE	24.24	26657352
486	Phosphorylation	GEYGFHEYTEVKTVT CCCCCEECEEEEEEE	10.30	8236723
490	Ubiquitination	FHEYTEVKTVTVKIS CEECEEEEEEEEEEE	30.92	-
491	Phosphorylation	HEYTEVKTVTVKISQ EECEEEEEEEEEEEE	26.95	26437602
493	Phosphorylation	YTEVKTVTVKISQKN CEEEEEEEEEEEECC	22.70	126141599
495	Ubiquitination	EVKTVTVKISQKNS- EEEEEEEEEEECCC-	27.55	19608861
495	Acetylation	EVKTVTVKISQKNS- EEEEEEEEEEECCC-	27.55	19608861
497	Phosphorylation	KTVTVKISQKNS--- EEEEEEEEECCC---	29.41	26437602

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
267	T	Phosphorylation	Kinase	AURA	O14965	PSP
442	T	Phosphorylation	Kinase	AURA	O14965	PSP
493	T	Phosphorylation	Kinase	AURA	O14965	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AL1A1_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 AL1A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AL1A1_HUMAN	ALDH1A1	physical	16189514
ALDH2_HUMAN	ALDH2	physical	21988832
POTE1_HUMAN	POT1	physical	21988832
NUPR1_HUMAN	NUPR1	physical	21988832
AL1A1_HUMAN	ALDH1A1	physical	25416956

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
DB00755	Tretinoin
DB00162	Vitamin A

Regulatory Network of AL1A1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Aldehyde dehydrogenase from human liver. Primary structure of thecytoplasmic isoenzyme."; Hempel J., von Bahr-Lindstroem H., Joernvall H.; Eur. J. Biochem. 141:21-35(1984). Cited for: PROTEIN SEQUENCE OF 2-501, AND ACETYLATION AT SER-2.	6723659 [Abstract]
"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-91; LYS-128; LYS-252;LYS-353; LYS-367; LYS-410; LYS-419; LYS-435 AND LYS-495, AND MASSSPECTROMETRY.	19608861 [Abstract]