3HIDH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: 3HIDH_HUMAN
• UniProt AC: P31937
• Protein Name: 3-hydroxyisobutyrate dehydrogenase, mitochondrial
• Gene Name: HIBADH
• Organism: Homo sapiens (Human).
• Sequence Length: 336
• Subcellular Localization: Mitochondrion.
• Protein Sequence: MAASLRLLGAASGLRYWSRRLRPAAGSFAAVCSRSVASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVFPDACKEFQDAGEQVVSSPADVAEKADRIITMLPTSINAIEAYSGANGILKKVKKGSLLIDSSTIDPAVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLGCMGSNVVYCGAVGTGQAAKICNNMLLAISMIGTAEAMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSANNYQGGFGTTLMAKDLGLAQDSATSTKSPILLGSLAHQIYRMMCAKGYSKKDFSSVFQFLREEETF

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
4	Phosphorylation	----MAASLRLLGAA ----CHHHHHHHHHH	12.41	20068231
12	Phosphorylation	LRLLGAASGLRYWSR HHHHHHHHHHHHHHH	37.51	24670416
18	Phosphorylation	ASGLRYWSRRLRPAA HHHHHHHHHHHCCCC	9.89	-
60	Acetylation	PMAKNLMKHGYPLII HHHHHHHHCCCCEEE	36.72	25038526
60	Succinylation	PMAKNLMKHGYPLII HHHHHHHHCCCCEEE	36.72	-
60	Succinylation	PMAKNLMKHGYPLII HHHHHHHHCCCCEEE	36.72	-
63	Phosphorylation	KNLMKHGYPLIIYDV HHHHHCCCCEEEEEC	8.45	23898821
76	Succinylation	DVFPDACKEFQDAGE ECCHHHHHHHHHHCC	64.38	-
76	Succinylation	DVFPDACKEFQDAGE ECCHHHHHHHHHHCC	64.38	-
76	Acetylation	DVFPDACKEFQDAGE ECCHHHHHHHHHHCC	64.38	25038526
87	Phosphorylation	DAGEQVVSSPADVAE HHCCHHHCCHHHHHH	31.57	27732954
88	Phosphorylation	AGEQVVSSPADVAEK HCCHHHCCHHHHHHH	16.70	25850435
95	Succinylation	SPADVAEKADRIITM CHHHHHHHHHHHHHH	45.94	-
95	Succinylation	SPADVAEKADRIITM CHHHHHHHHHHHHHH	45.94	-
95	Acetylation	SPADVAEKADRIITM CHHHHHHHHHHHHHH	45.94	25038526
95	Ubiquitination	SPADVAEKADRIITM CHHHHHHHHHHHHHH	45.94	-
105	Phosphorylation	RIITMLPTSINAIEA HHHHHCCCCHHHHHH	37.97	28348404
106	Phosphorylation	IITMLPTSINAIEAY HHHHCCCCHHHHHHH	16.35	28857561
113	Phosphorylation	SINAIEAYSGANGIL CHHHHHHHHCCCCHH	8.54	22210691
114	Phosphorylation	INAIEAYSGANGILK HHHHHHHHCCCCHHH	38.18	22210691
121	Acetylation	SGANGILKKVKKGSL HCCCCHHHHHHCCCE	54.31	2380209
125	Succinylation	GILKKVKKGSLLIDS CHHHHHHCCCEEEEC	57.63	27452117
125	Malonylation	GILKKVKKGSLLIDS CHHHHHHCCCEEEEC	57.63	26320211
127	Phosphorylation	LKKVKKGSLLIDSST HHHHHCCCEEEECCC	28.96	25850435
132	Phosphorylation	KGSLLIDSSTIDPAV CCCEEEECCCCCHHH	23.53	25850435
133	Phosphorylation	GSLLIDSSTIDPAVS CCEEEECCCCCHHHH	26.15	25850435
134	Phosphorylation	SLLIDSSTIDPAVSK CEEEECCCCCHHHHH	33.09	25850435
140	Phosphorylation	STIDPAVSKELAKEV CCCCHHHHHHHHHHH	23.63	-
141	Succinylation	TIDPAVSKELAKEVE CCCHHHHHHHHHHHH	50.58	-
141	Succinylation	TIDPAVSKELAKEVE CCCHHHHHHHHHHHH	50.58	-
141	Acetylation	TIDPAVSKELAKEVE CCCHHHHHHHHHHHH	50.58	25038526
141	Ubiquitination	TIDPAVSKELAKEVE CCCHHHHHHHHHHHH	50.58	-
145	Acetylation	AVSKELAKEVEKMGA HHHHHHHHHHHHCCC	74.95	-
145	Succinylation	AVSKELAKEVEKMGA HHHHHHHHHHHHCCC	74.95	23954790
149	Acetylation	ELAKEVEKMGAVFMD HHHHHHHHCCCEEEE	48.05	-
149	Succinylation	ELAKEVEKMGAVFMD HHHHHHHHCCCEEEE	48.05	-
149	Succinylation	ELAKEVEKMGAVFMD HHHHHHHHCCCEEEE	48.05	-
160	Phosphorylation	VFMDAPVSGGVGAAR EEEECCCCCCCCCCC	28.86	20068231
168	Phosphorylation	GGVGAARSGNLTFMV CCCCCCCCCCEEEEE	27.57	22210691
198	Phosphorylation	CMGSNVVYCGAVGTG CCCCCEEEECCCCHH	4.85	22210691
238	2-Hydroxyisobutyrylation	IRLGLDPKLLAKILN HHCCCCHHHHHHHHC	56.66	-
238	Succinylation	IRLGLDPKLLAKILN HHCCCCHHHHHHHHC	56.66	-
238	Acetylation	IRLGLDPKLLAKILN HHCCCCHHHHHHHHC	56.66	155923
238	Succinylation	IRLGLDPKLLAKILN HHCCCCHHHHHHHHC	56.66	23954790
242	Succinylation	LDPKLLAKILNMSSG CCHHHHHHHHCCCCC	47.93	-
242	Succinylation	LDPKLLAKILNMSSG CCHHHHHHHHCCCCC	47.93	-
242	Acetylation	LDPKLLAKILNMSSG CCHHHHHHHHCCCCC	47.93	25038526
242	Malonylation	LDPKLLAKILNMSSG CCHHHHHHHHCCCCC	47.93	26320211
292	Phosphorylation	DLGLAQDSATSTKSP HHCCCCCCCCCCCCC	22.74	21712546
297	Acetylation	QDSATSTKSPILLGS CCCCCCCCCCHHHHH	54.74	23954790
297	Ubiquitination	QDSATSTKSPILLGS CCCCCCCCCCHHHHH	54.74	-
297	Succinylation	QDSATSTKSPILLGS CCCCCCCCCCHHHHH	54.74	-
297	Succinylation	QDSATSTKSPILLGS CCCCCCCCCCHHHHH	54.74	-
297	Malonylation	QDSATSTKSPILLGS CCCCCCCCCCHHHHH	54.74	26320211
310	Phosphorylation	GSLAHQIYRMMCAKG HHHHHHHHHHHHHCC	5.96	-
321	Ubiquitination	CAKGYSKKDFSSVFQ HHCCCCHHHHHHHHH	59.05	21890473
321	Ubiquitination	CAKGYSKKDFSSVFQ HHCCCCHHHHHHHHH	59.05	21890473
321	Succinylation	CAKGYSKKDFSSVFQ HHCCCCHHHHHHHHH	59.05	21890473
321	Succinylation	CAKGYSKKDFSSVFQ HHCCCCHHHHHHHHH	59.05	-
321	Acetylation	CAKGYSKKDFSSVFQ HHCCCCHHHHHHHHH	59.05	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM63	Q969Q1	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of 3HIDH_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of 3HIDH_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
3HIDH_HUMAN	HIBADH	physical	3335502
AL1B1_HUMAN	ALDH1B1	physical	26344197
MMSA_HUMAN	ALDH6A1	physical	26344197
MDHC_HUMAN	MDH1	physical	26344197
PDXK_HUMAN	PDXK	physical	26344197
SODC_HUMAN	SOD1	physical	26344197

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.