BDH2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BDH2_HUMAN
• UniProt AC: Q9BUT1
• Protein Name: 3-hydroxybutyrate dehydrogenase type 2
• Gene Name: BDH2
• Organism: Homo sapiens (Human).
• Sequence Length: 245
• Subcellular Localization: Cytoplasm .
• Protein Description: Dehydrogenase that mediates the formation of 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin and associates with LCN2, thereby playing a key role in iron homeostasis and transport. Also acts as a 3-hydroxybutyrate dehydrogenase (By similarity)..
• Protein Sequence: MGRLDGKVIILTAAAQGIGQAAALAFAREGAKVIATDINESKLQELEKYPGIQTRVLDVTKKKQIDQFANEVERLDVLFNVAGFVHHGTVLDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSVKGVVNRCVYSTTKAAVIGLTKSVAADFIQQGIRCNCVCPGTVDTPSLQERIQARGNPEEARNDFLKRQKTGRFATAEEIAMLCVYLASDESAYVTGNPVIIDGGWSL

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
32	Ubiquitination	AFAREGAKVIATDIN HHHHCCCEEEEEECC	45.06	30230243
41	Phosphorylation	IATDINESKLQELEK EEEECCHHHHHHHHH	33.89	28857561
42	Ubiquitination	ATDINESKLQELEKY EEECCHHHHHHHHHC	48.27	23000965
42	Sumoylation	ATDINESKLQELEKY EEECCHHHHHHHHHC	48.27	-
48	Acetylation	SKLQELEKYPGIQTR HHHHHHHHCCCCCEE	70.17	19608861
48 (in isoform 2)	Ubiquitination	-	70.17	21890473
48 (in isoform 1)	Ubiquitination	-	70.17	21890473
48	Ubiquitination	SKLQELEKYPGIQTR HHHHHHHHCCCCCEE	70.17	21890473
48	Ubiquitination	SKLQELEKYPGIQTR HHHHHHHHCCCCCEE	70.17	21890473
48	Ubiquitination	SKLQELEKYPGIQTR HHHHHHHHCCCCCEE	70.17	23000965
61	Acetylation	TRVLDVTKKKQIDQF EEEEECCCHHHHHHH	58.80	25953088
61	2-Hydroxyisobutyrylation	TRVLDVTKKKQIDQF EEEEECCCHHHHHHH	58.80	-
62	Ubiquitination	RVLDVTKKKQIDQFA EEEECCCHHHHHHHH	40.31	29967540
63	Ubiquitination	VLDVTKKKQIDQFAN EEECCCHHHHHHHHH	54.78	24816145
63	Acetylation	VLDVTKKKQIDQFAN EEECCCHHHHHHHHH	54.78	23954790
101	Phosphorylation	EEKDWDFSMNLNVRS CCCCCCCCCCCCHHH	12.32	29116813
124	Ubiquitination	LPKMLAQKSGNIINM HHHHHHHHCCCEEEH	55.51	29967540
124	Acetylation	LPKMLAQKSGNIINM HHHHHHHHCCCEEEH	55.51	7675547
125	Phosphorylation	PKMLAQKSGNIINMS HHHHHHHCCCEEEHH	25.62	21406692
132	Phosphorylation	SGNIINMSSVASSVK CCCEEEHHHHHHHHH	19.71	21406692
133	Phosphorylation	GNIINMSSVASSVKG CCEEEHHHHHHHHHH	15.78	21406692
136	Phosphorylation	INMSSVASSVKGVVN EEHHHHHHHHHHHHH	33.24	21406692
137	Phosphorylation	NMSSVASSVKGVVNR EHHHHHHHHHHHHHH	20.36	21406692
139	Acetylation	SSVASSVKGVVNRCV HHHHHHHHHHHHHHH	48.19	7675557
139	Ubiquitination	SSVASSVKGVVNRCV HHHHHHHHHHHHHHH	48.19	32015554
151	Acetylation	RCVYSTTKAAVIGLT HHHHHHHHHHHHHCC	34.14	88291
159 (in isoform 1)	Ubiquitination	-	48.23	21890473
159	Ubiquitination	AAVIGLTKSVAADFI HHHHHCCHHHHHHHH	48.23	21890473
159	Ubiquitination	AAVIGLTKSVAADFI HHHHHCCHHHHHHHH	48.23	21890473
159	Ubiquitination	AAVIGLTKSVAADFI HHHHHCCHHHHHHHH	48.23	22053931
166	Ubiquitination	KSVAADFIQQGIRCN HHHHHHHHHCCCCCC	2.84	27667366
173	Ubiquitination	IQQGIRCNCVCPGTV HHCCCCCCEECCCCC	16.06	21890473
182	Phosphorylation	VCPGTVDTPSLQERI ECCCCCCCHHHHHHH	15.50	28857561
184	Phosphorylation	PGTVDTPSLQERIQA CCCCCCHHHHHHHHH	44.79	28857561
204	Ubiquitination	EARNDFLKRQKTGRF HHHHHHHHHHHCCCC	53.42	27667366
218	Ubiquitination	FATAEEIAMLCVYLA CCCHHHHHHHHHHHH	6.54	27667366

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BDH2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BDH2_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 BDH2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BDH2_HUMAN	BDH2	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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"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-48, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASSSPECTROMETRY.
PubMed: 18187866