dbPTM

DHB4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DHB4_MOUSE
UniProt AC	P51660
Protein Name	Peroxisomal multifunctional enzyme type 2
Gene Name	Hsd17b4
Organism	Mus musculus (Mouse).
Sequence Length	735
Subcellular Localization	Peroxisome.
Protein Description	Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids (By similarity)..
Protein Sequence	MASPLRFDGRVVLVTGAGGGLGRAYALAFAERGALVIVNDLGGDFKGIGKGSSAADKVVAEIRRKGGKAVANYDSVEAGEKLVKTALDTFGRIDVVVNNAGILRDRSFSRISDEDWDIIHRVHLRGSFQVTRAAWDHMKKQNYGRILMTSSASGIYGNFGQANYSAAKLGILGLCNTLAIEGRKNNIHCNTIAPNAGSRMTETVLPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRKRNQPMTPEAVRDNWEKICDFSNASKPQTIQESTGGIVEVLHKVDSEGISPNRTSHAAPAATSGFVGAVGHKLPSFSSSYTELQSIMYALGVGASVKNPKDLKFVYEGSADFSCLPTFGVIVAQKSMMNGGLAEVPGLSFNFAKALHGEQYLELYKPLPRSGELKCEAVIADILDKGSGVVIVMDVYSYSGKELICYNQFSVFVVGSGGFGGKRTSEKLKAAVAVPNRPPDAVLRDATSLNQAALYRLSGDWNPLHIDPDFASVAGFEKPILHGLCTFGFSARHVLQQFADNDVSRFKAIKVRFAKPVYPGQTLQTEMWKEGNRIHFQTKVHETGDVVISNAYVDLVPASGVSTQTPSEGGELQSALVFGEIGRRLKSVGREVVKKANAVFEWHITKGGTVAAKWTIDLKSGSGEVYQGPAKGSADVTIIISDEDFMEVVFGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASPLRFDG ------CCCCCEECC	21.61	-
3	Phosphorylation	-----MASPLRFDGR -----CCCCCEECCE	24.14	26824392
46	Acetylation	NDLGGDFKGIGKGSS ECCCCCCCCCCCCCC	55.12	23576753
46	Succinylation	NDLGGDFKGIGKGSS ECCCCCCCCCCCCCC	55.12	-
46	Succinylation	NDLGGDFKGIGKGSS ECCCCCCCCCCCCCC	55.12	23806337
46	Ubiquitination	NDLGGDFKGIGKGSS ECCCCCCCCCCCCCC	55.12	-
50	Glutarylation	GDFKGIGKGSSAADK CCCCCCCCCCCHHHH	54.41	24703693
50	Malonylation	GDFKGIGKGSSAADK CCCCCCCCCCCHHHH	54.41	26320211
52	Phosphorylation	FKGIGKGSSAADKVV CCCCCCCCCHHHHHH	21.93	23684622
53	Phosphorylation	KGIGKGSSAADKVVA CCCCCCCCHHHHHHH	35.82	23140645
57	Acetylation	KGSSAADKVVAEIRR CCCCHHHHHHHHHHH	33.60	23864654
57	Glutarylation	KGSSAADKVVAEIRR CCCCHHHHHHHHHHH	33.60	24703693
57	Malonylation	KGSSAADKVVAEIRR CCCCHHHHHHHHHHH	33.60	26320211
57	Succinylation	KGSSAADKVVAEIRR CCCCHHHHHHHHHHH	33.60	-
57	Succinylation	KGSSAADKVVAEIRR CCCCHHHHHHHHHHH	33.60	23806337
57	Ubiquitination	KGSSAADKVVAEIRR CCCCHHHHHHHHHHH	33.60	-
65	Succinylation	VVAEIRRKGGKAVAN HHHHHHHCCCEEECC	63.27	24315375
68	Acetylation	EIRRKGGKAVANYDS HHHHCCCEEECCCCH	48.64	23806337
68	Glutarylation	EIRRKGGKAVANYDS HHHHCCCEEECCCCH	48.64	24703693
68	Malonylation	EIRRKGGKAVANYDS HHHHCCCEEECCCCH	48.64	26320211
68	Succinylation	EIRRKGGKAVANYDS HHHHCCCEEECCCCH	48.64	-
68	Succinylation	EIRRKGGKAVANYDS HHHHCCCEEECCCCH	48.64	23806337
68	Ubiquitination	EIRRKGGKAVANYDS HHHHCCCEEECCCCH	48.64	27667366
73	Phosphorylation	GGKAVANYDSVEAGE CCEEECCCCHHHHHH	10.39	-
75	Phosphorylation	KAVANYDSVEAGEKL EEECCCCHHHHHHHH	16.11	-
81	Acetylation	DSVEAGEKLVKTALD CHHHHHHHHHHHHHH	58.63	23864654
81	Glutarylation	DSVEAGEKLVKTALD CHHHHHHHHHHHHHH	58.63	24703693
81	Ubiquitination	DSVEAGEKLVKTALD CHHHHHHHHHHHHHH	58.63	-
84	Acetylation	EAGEKLVKTALDTFG HHHHHHHHHHHHHCC	38.22	23806337
84	Succinylation	EAGEKLVKTALDTFG HHHHHHHHHHHHHCC	38.22	-
84	Succinylation	EAGEKLVKTALDTFG HHHHHHHHHHHHHCC	38.22	23806337
84	Ubiquitination	EAGEKLVKTALDTFG HHHHHHHHHHHHHCC	38.22	-
107	Phosphorylation	AGILRDRSFSRISDE CCCCCCCCCCCCCCC	31.68	23984901
109	Phosphorylation	ILRDRSFSRISDEDW CCCCCCCCCCCCCCC	29.92	23684622
112	Phosphorylation	DRSFSRISDEDWDII CCCCCCCCCCCCCEE	33.56	23984901
139	Acetylation	RAAWDHMKKQNYGRI HHHHHHHHHCCCCEE	48.03	23864654
139	Succinylation	RAAWDHMKKQNYGRI HHHHHHHHHCCCCEE	48.03	23806337
175	S-nitrosocysteine	KLGILGLCNTLAIEG HHHHHHHHHHHHCCC	3.29	-
175	S-nitrosylation	KLGILGLCNTLAIEG HHHHHHHHHHHHCCC	3.29	21278135
175	S-palmitoylation	KLGILGLCNTLAIEG HHHHHHHHHHHHCCC	3.29	28526873
184	Malonylation	TLAIEGRKNNIHCNT HHHCCCCCCCEECCC	66.26	26320211
184	Ubiquitination	TLAIEGRKNNIHCNT HHHCCCCCCCEECCC	66.26	-
189	S-nitrosocysteine	GRKNNIHCNTIAPNA CCCCCEECCCCCCCC	4.21	-
189	S-nitrosylation	GRKNNIHCNTIAPNA CCCCCEECCCCCCCC	4.21	22178444
189	S-palmitoylation	GRKNNIHCNTIAPNA CCCCCEECCCCCCCC	4.21	26165157
191	Phosphorylation	KNNIHCNTIAPNAGS CCCEECCCCCCCCCC	24.74	23140645
198	Phosphorylation	TIAPNAGSRMTETVL CCCCCCCCCCCCCCC	19.23	25521595
265	Phosphorylation	RKRNQPMTPEAVRDN HHCCCCCCHHHHHHC	25.35	23140645
275	Acetylation	AVRDNWEKICDFSNA HHHHCHHHHCCCCCC	40.00	23806337
275	Succinylation	AVRDNWEKICDFSNA HHHHCHHHHCCCCCC	40.00	-
275	Succinylation	AVRDNWEKICDFSNA HHHHCHHHHCCCCCC	40.00	23806337
277	S-nitrosylation	RDNWEKICDFSNASK HHCHHHHCCCCCCCC	6.82	22178444
277	S-palmitoylation	RDNWEKICDFSNASK HHCHHHHCCCCCCCC	6.82	28526873
280	Phosphorylation	WEKICDFSNASKPQT HHHHCCCCCCCCCCC	20.45	23140645
283	Phosphorylation	ICDFSNASKPQTIQE HCCCCCCCCCCCHHH	49.47	23140645
284	Acetylation	CDFSNASKPQTIQES CCCCCCCCCCCHHHC	38.44	23201123
284	Ubiquitination	CDFSNASKPQTIQES CCCCCCCCCCCHHHC	38.44	22790023
287	Phosphorylation	SNASKPQTIQESTGG CCCCCCCCHHHCCCC	32.91	23140645
291	Phosphorylation	KPQTIQESTGGIVEV CCCCHHHCCCCHHEE	18.90	23140645
292	Phosphorylation	PQTIQESTGGIVEVL CCCHHHCCCCHHEEE	38.38	23140645
304	Phosphorylation	EVLHKVDSEGISPNR EEEEECCCCCCCCCC	40.48	27180971
308	Phosphorylation	KVDSEGISPNRTSHA ECCCCCCCCCCCCCC	27.29	26824392
312	Phosphorylation	EGISPNRTSHAAPAA CCCCCCCCCCCCCCH	31.35	26643407
313	Phosphorylation	GISPNRTSHAAPAAT CCCCCCCCCCCCCHH	14.11	26643407
320	Phosphorylation	SHAAPAATSGFVGAV CCCCCCHHCCCCHHH	31.33	26643407
321	Phosphorylation	HAAPAATSGFVGAVG CCCCCHHCCCCHHHC	26.05	26643407
355	Acetylation	LGVGASVKNPKDLKF HCCCCCCCCHHHCCE	66.10	23806337
355	Succinylation	LGVGASVKNPKDLKF HCCCCCCCCHHHCCE	66.10	-
355	Succinylation	LGVGASVKNPKDLKF HCCCCCCCCHHHCCE	66.10	23806337
397	Phosphorylation	LAEVPGLSFNFAKAL CCCCCCEEHHHHHHH	24.86	23140645
402	Ubiquitination	GLSFNFAKALHGEQY CEEHHHHHHHCCHHH	47.55	22790023
414	Acetylation	EQYLELYKPLPRSGE HHHHHHCCCCCCCCC	53.34	23864654
414	Succinylation	EQYLELYKPLPRSGE HHHHHHCCCCCCCCC	53.34	24315375
414	Ubiquitination	EQYLELYKPLPRSGE HHHHHHCCCCCCCCC	53.34	-
423	Acetylation	LPRSGELKCEAVIAD CCCCCCCCCEEEEEH	26.23	23864654
423	Succinylation	LPRSGELKCEAVIAD CCCCCCCCCEEEEEH	26.23	-
423	Succinylation	LPRSGELKCEAVIAD CCCCCCCCCEEEEEH	26.23	23806337
423	Ubiquitination	LPRSGELKCEAVIAD CCCCCCCCCEEEEEH	26.23	-
476	Acetylation	GGKRTSEKLKAAVAV CCCCCHHHHHHHEEC	55.87	23864654
478	Ubiquitination	KRTSEKLKAAVAVPN CCCHHHHHHHEECCC	45.42	22790023
496	Phosphorylation	DAVLRDATSLNQAAL CHHHCCCCCCCHHHH	37.73	23140645
497	Phosphorylation	AVLRDATSLNQAALY HHHCCCCCCCHHHHH	27.35	23140645
564	Acetylation	AIKVRFAKPVYPGQT EEEEEECCCCCCCCE	32.10	23576753
564	Malonylation	AIKVRFAKPVYPGQT EEEEEECCCCCCCCE	32.10	26320211
564	Ubiquitination	AIKVRFAKPVYPGQT EEEEEECCCCCCCCE	32.10	-
578	Acetylation	TLQTEMWKEGNRIHF EEEEEHHHCCCEEEE	55.20	23864654
578	Succinylation	TLQTEMWKEGNRIHF EEEEEHHHCCCEEEE	55.20	-
578	Succinylation	TLQTEMWKEGNRIHF EEEEEHHHCCCEEEE	55.20	23806337
636	Phosphorylation	EIGRRLKSVGREVVK HHHHHHHHHCHHHHH	34.10	23684622
662	Acetylation	KGGTVAAKWTIDLKS CCCEEEEEEEEECCC	34.82	23806337
662	Succinylation	KGGTVAAKWTIDLKS CCCEEEEEEEEECCC	34.82	-
662	Succinylation	KGGTVAAKWTIDLKS CCCEEEEEEEEECCC	34.82	23806337
668	Acetylation	AKWTIDLKSGSGEVY EEEEEECCCCCCEEE	49.36	23864654
668	Succinylation	AKWTIDLKSGSGEVY EEEEEECCCCCCEEE	49.36	23954790
671	Phosphorylation	TIDLKSGSGEVYQGP EEECCCCCCEEEECC	38.58	23140645
706	Acetylation	FGKLDPQKAFFSGRL HCCCCHHHCHHHCCC	53.18	23576753
706	Succinylation	FGKLDPQKAFFSGRL HCCCCHHHCHHHCCC	53.18	24315375
710	Phosphorylation	DPQKAFFSGRLKARG CHHHCHHHCCCCHHC	19.29	24719451
724	Acetylation	GNIMLSQKLQMILKD CCCHHHHHHHHHHHH	36.99	23806337
724	Succinylation	GNIMLSQKLQMILKD CCCHHHHHHHHHHHH	36.99	-
724	Succinylation	GNIMLSQKLQMILKD CCCHHHHHHHHHHHH	36.99	23806337
730	Acetylation	QKLQMILKDYAKL-- HHHHHHHHHHHCC--	37.46	23806337
730	Succinylation	QKLQMILKDYAKL-- HHHHHHHHHHHCC--	37.46	23806337

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 DHB4_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DHB4_MOUSE !!

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 DHB4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DHB4_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DHB4_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3,AND MASS SPECTROMETRY.	16452087 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-662, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3,AND MASS SPECTROMETRY.	16452087 [Abstract]