dbPTM

DHB4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DHB4_HUMAN
UniProt AC	P51659
Protein Name	Peroxisomal multifunctional enzyme type 2
Gene Name	HSD17B4
Organism	Homo sapiens (Human).
Sequence Length	736
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..
Protein Sequence	MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLSKIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKDLKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKVAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNIGAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MGSPLRFDGR -----CCCCCEECCE	21.33	23401153
15	Phosphorylation	DGRVVLVTGAGAGLG CCEEEEEECCCCCHH	19.70	20068231
46	2-Hydroxyisobutyrylation	NDLGGDFKGVGKGSL ECCCCCCCCCCCCHH	58.38	-
46	Acetylation	NDLGGDFKGVGKGSL ECCCCCCCCCCCCHH	58.38	23954790
46	Malonylation	NDLGGDFKGVGKGSL ECCCCCCCCCCCCHH	58.38	26320211
46	Succinylation	NDLGGDFKGVGKGSL ECCCCCCCCCCCCHH	58.38	-
46	Succinylation	NDLGGDFKGVGKGSL ECCCCCCCCCCCCHH	58.38	23954790
46	Ubiquitination	NDLGGDFKGVGKGSL ECCCCCCCCCCCCHH	58.38	-
50	2-Hydroxyisobutyrylation	GDFKGVGKGSLAADK CCCCCCCCCHHHHHH	42.81	-
50	Ubiquitination	GDFKGVGKGSLAADK CCCCCCCCCHHHHHH	42.81	-
52	Phosphorylation	FKGVGKGSLAADKVV CCCCCCCHHHHHHHH	20.51	24275569
57	2-Hydroxyisobutyrylation	KGSLAADKVVEEIRR CCHHHHHHHHHHHHH	43.37	-
57	Acetylation	KGSLAADKVVEEIRR CCHHHHHHHHHHHHH	43.37	23954790
57	Malonylation	KGSLAADKVVEEIRR CCHHHHHHHHHHHHH	43.37	26320211
57	Succinylation	KGSLAADKVVEEIRR CCHHHHHHHHHHHHH	43.37	-
57	Succinylation	KGSLAADKVVEEIRR CCHHHHHHHHHHHHH	43.37	-
57	Ubiquitination	KGSLAADKVVEEIRR CCHHHHHHHHHHHHH	43.37	-
68	Malonylation	EIRRRGGKAVANYDS HHHHCCCEEECCCCC	42.38	26320211
68	Succinylation	EIRRRGGKAVANYDS HHHHCCCEEECCCCC	42.38	-
68	Succinylation	EIRRRGGKAVANYDS HHHHCCCEEECCCCC	42.38	-
68	Ubiquitination	EIRRRGGKAVANYDS HHHHCCCEEECCCCC	42.38	-
73	Phosphorylation	GGKAVANYDSVEEGE CCEEECCCCCHHHCH	10.39	20071362
75	Phosphorylation	KAVANYDSVEEGEKV EEECCCCCHHHCHHH	22.52	25072903
81	2-Hydroxyisobutyrylation	DSVEEGEKVVKTALD CCHHHCHHHHHHHHH	64.28	-
81	Acetylation	DSVEEGEKVVKTALD CCHHHCHHHHHHHHH	64.28	23954790
81	Ubiquitination	DSVEEGEKVVKTALD CCHHHCHHHHHHHHH	64.28	-
84	Succinylation	EEGEKVVKTALDAFG HHCHHHHHHHHHHCC	30.94	-
84	Succinylation	EEGEKVVKTALDAFG HHCHHHHHHHHHHCC	30.94	-
112	Phosphorylation	DRSFARISDEDWDII CCCEEECCCCCCCEE	29.42	-
139	Acetylation	RAAWEHMKKQKYGRI HHHHHHHHHHCCCEE	54.69	23749302
139	Succinylation	RAAWEHMKKQKYGRI HHHHHHHHHHCCCEE	54.69	23954790
143	Phosphorylation	EHMKKQKYGRIIMTS HHHHHHCCCEEEEEC	14.78	-
149	Phosphorylation	KYGRIIMTSSASGIY CCCEEEEECCCCCCC	14.77	-
150	Phosphorylation	YGRIIMTSSASGIYG CCEEEEECCCCCCCC	13.41	-
151	Phosphorylation	GRIIMTSSASGIYGN CEEEEECCCCCCCCC	19.79	-
153	Phosphorylation	IIMTSSASGIYGNFG EEEECCCCCCCCCCC	27.89	28348404
156	Phosphorylation	TSSASGIYGNFGQAN ECCCCCCCCCCCCHH	15.00	-
184	Ubiquitination	SLAIEGRKSNIHCNT HHHHCCCCCCCCCCC	59.73	-
185	Phosphorylation	LAIEGRKSNIHCNTI HHHCCCCCCCCCCCC	39.39	-
189	Glutathionylation	GRKSNIHCNTIAPNA CCCCCCCCCCCCCCC	4.21	22555962
265	Phosphorylation	RQKNHPMTPEAVKAN HCCCCCCCHHHHHCC	23.56	25159151
270	Acetylation	PMTPEAVKANWKKIC CCCHHHHHCCHHHHC	42.95	25953088
270	Ubiquitination	PMTPEAVKANWKKIC CCCHHHHHCCHHHHC	42.95	-
275	Succinylation	AVKANWKKICDFENA HHHCCHHHHCCCCCC	39.93	-
275	Succinylation	AVKANWKKICDFENA HHHCCHHHHCCCCCC	39.93	-
275	Ubiquitination	AVKANWKKICDFENA HHHCCHHHHCCCCCC	39.93	-
277	Glutathionylation	KANWKKICDFENASK HCCHHHHCCCCCCCC	7.23	22555962
283	Phosphorylation	ICDFENASKPQSIQE HCCCCCCCCCCHHHH	57.35	30624053
287	Phosphorylation	ENASKPQSIQESTGS CCCCCCCHHHHHHCC	34.46	28450419
290	Phosphorylation	SKPQSIQESTGSIIE CCCCHHHHHHCCHHH	48.90	27251275
291	Phosphorylation	KPQSIQESTGSIIEV CCCHHHHHHCCHHHH	22.99	28450419
292	Phosphorylation	PQSIQESTGSIIEVL CCHHHHHHCCHHHHH	33.91	28450419
294	Phosphorylation	SIQESTGSIIEVLSK HHHHHHCCHHHHHHC	22.08	25159151
300	Phosphorylation	GSIIEVLSKIDSEGG CCHHHHHHCCCCCCC	32.51	28450419
301	Acetylation	SIIEVLSKIDSEGGV CHHHHHHCCCCCCCC	46.50	26051181
304	Phosphorylation	EVLSKIDSEGGVSAN HHHHCCCCCCCCCCC	41.43	29255136
309	Phosphorylation	IDSEGGVSANHTSRA CCCCCCCCCCCCCCC	26.99	29255136
313	Phosphorylation	GGVSANHTSRATSTA CCCCCCCCCCCCCCC	21.51	29255136
314	Phosphorylation	GVSANHTSRATSTAT CCCCCCCCCCCCCCC	16.62	29255136
317	Phosphorylation	ANHTSRATSTATSGF CCCCCCCCCCCCCCC	26.04	29255136
318	Phosphorylation	NHTSRATSTATSGFA CCCCCCCCCCCCCCC	18.30	29255136
319	Phosphorylation	HTSRATSTATSGFAG CCCCCCCCCCCCCCH	29.60	30266825
321	Phosphorylation	SRATSTATSGFAGAI CCCCCCCCCCCCHHH	29.48	30266825
322	Phosphorylation	RATSTATSGFAGAIG CCCCCCCCCCCHHHC	29.47	30266825
325	Phosphorylation	STATSGFAGAIGQKL CCCCCCCCHHHCCCC	15.27	27251275
336	Phosphorylation	GQKLPPFSYAYTELE CCCCCCCCCCHHHHH	18.02	24275569
343	Phosphorylation	SYAYTELEAIMYALG CCCHHHHHHHHHHHC	29.89	27251275
347	Phosphorylation	TELEAIMYALGVGAS HHHHHHHHHHCCCCC	7.80	27251275
356	Succinylation	LGVGASIKDPKDLKF HCCCCCCCCHHHCCE	66.53	-
356	Succinylation	LGVGASIKDPKDLKF HCCCCCCCCHHHCCE	66.53	-
368	Phosphorylation	LKFIYEGSSDFSCLP CCEEEECCCCCCCCC	18.13	28348404
369	Phosphorylation	KFIYEGSSDFSCLPT CEEEECCCCCCCCCC	54.23	28348404
398	Phosphorylation	LAEIPGLSINFAKVL CCCCCCEEEEEEEEC	22.77	28348404
410	Phosphorylation	KVLHGEQYLELYKPL EECCCHHHHHHHCCC	9.61	29496907
414	Phosphorylation	GEQYLELYKPLPRAG CHHHHHHHCCCCCCC	10.94	29496907
415	Acetylation	EQYLELYKPLPRAGK HHHHHHHCCCCCCCC	53.34	23954790
415	Succinylation	EQYLELYKPLPRAGK HHHHHHHCCCCCCCC	53.34	23954790
415	Ubiquitination	EQYLELYKPLPRAGK HHHHHHHCCCCCCCC	53.34	-
424	2-Hydroxyisobutyrylation	LPRAGKLKCEAVVAD CCCCCCCCCEEEEEE	33.25	-
424	Acetylation	LPRAGKLKCEAVVAD CCCCCCCCCEEEEEE	33.25	26051181
424	Malonylation	LPRAGKLKCEAVVAD CCCCCCCCCEEEEEE	33.25	26320211
424	Succinylation	LPRAGKLKCEAVVAD CCCCCCCCCEEEEEE	33.25	-
424	Succinylation	LPRAGKLKCEAVVAD CCCCCCCCCEEEEEE	33.25	-
424	Ubiquitination	LPRAGKLKCEAVVAD CCCCCCCCCEEEEEE	33.25	-
446	Phosphorylation	VVIIMDVYSYSEKEL EEEEEECCCCCCCEE	9.53	22817900
448	Phosphorylation	IIMDVYSYSEKELIC EEEECCCCCCCEEEE	11.80	22817900
475	Phosphorylation	GFGGKRTSDKVKVAV CCCCCCCCCCEEEEE	39.19	28258704
496	Phosphorylation	PDAVLTDTTSLNQAA CCCEEECCCCCCHHH	17.04	28258704
497	Phosphorylation	DAVLTDTTSLNQAAL CCEEECCCCCCHHHH	33.74	28258704
565	Acetylation	AIKARFAKPVYPGQT HHHHHCCCCCCCCCE	32.10	19608861
565	Malonylation	AIKARFAKPVYPGQT HHHHHCCCCCCCCCE	32.10	26320211
565	Ubiquitination	AIKARFAKPVYPGQT HHHHHCCCCCCCCCE	32.10	19608861
579	Acetylation	TLQTEMWKEGNRIHF EEEEEHHHCCCEEEE	55.20	23954790
579	Malonylation	TLQTEMWKEGNRIHF EEEEEHHHCCCEEEE	55.20	32601280
579	Succinylation	TLQTEMWKEGNRIHF EEEEEHHHCCCEEEE	55.20	-
579	Succinylation	TLQTEMWKEGNRIHF EEEEEHHHCCCEEEE	55.20	23954790
599	Phosphorylation	ETGDIVISNAYVDLA ECCCEEEEEEEEEEC	12.43	29978859
602	Phosphorylation	DIVISNAYVDLAPTS CEEEEEEEEEECCCC	9.96	30576142
608	Phosphorylation	AYVDLAPTSGTSAKT EEEEECCCCCCCCCC	33.89	28450419
609	Phosphorylation	YVDLAPTSGTSAKTP EEEECCCCCCCCCCC	38.73	28450419
611	Phosphorylation	DLAPTSGTSAKTPSE EECCCCCCCCCCCCC	25.86	28450419
612	Phosphorylation	LAPTSGTSAKTPSEG ECCCCCCCCCCCCCC	31.15	28450419
614	Acetylation	PTSGTSAKTPSEGGK CCCCCCCCCCCCCCC	61.81	25953088
615	Phosphorylation	TSGTSAKTPSEGGKL CCCCCCCCCCCCCCE	31.59	28450419
617	Phosphorylation	GTSAKTPSEGGKLQS CCCCCCCCCCCCEEE	54.85	27422710
621	Acetylation	KTPSEGGKLQSTFVF CCCCCCCCEEEEEEH	54.96	25953088
624	Phosphorylation	SEGGKLQSTFVFEEI CCCCCEEEEEEHHHH	33.96	26074081
625	Phosphorylation	EGGKLQSTFVFEEIG CCCCEEEEEEHHHHH	15.74	26074081
636	Acetylation	EEIGRRLKDIGPEVV HHHHHHHHHHCHHHH	45.55	23749302
636	Malonylation	EEIGRRLKDIGPEVV HHHHHHHHHHCHHHH	45.55	26320211
636	Ubiquitination	EEIGRRLKDIGPEVV HHHHHHHHHHCHHHH	45.55	-
637	Phosphorylation	EIGRRLKDIGPEVVK HHHHHHHHHCHHHHH	56.52	27251275
644	2-Hydroxyisobutyrylation	DIGPEVVKKVNAVFE HHCHHHHHHHCEEEE	57.06	-
644	Acetylation	DIGPEVVKKVNAVFE HHCHHHHHHHCEEEE	57.06	23749302
644	Malonylation	DIGPEVVKKVNAVFE HHCHHHHHHHCEEEE	57.06	26320211
644	Succinylation	DIGPEVVKKVNAVFE HHCHHHHHHHCEEEE	57.06	23954790
645	Malonylation	IGPEVVKKVNAVFEW HCHHHHHHHCEEEEE	29.16	32601280
655	Phosphorylation	AVFEWHITKGGNIGA EEEEEEECCCCCCCC	15.68	-
663	Acetylation	KGGNIGAKWTIDLKS CCCCCCCEEEEECCC	39.39	25953088
663	Succinylation	KGGNIGAKWTIDLKS CCCCCCCEEEEECCC	39.39	-
663	Succinylation	KGGNIGAKWTIDLKS CCCCCCCEEEEECCC	39.39	-
669	2-Hydroxyisobutyrylation	AKWTIDLKSGSGKVY CEEEEECCCCCCEEE	49.36	-
669	Acetylation	AKWTIDLKSGSGKVY CEEEEECCCCCCEEE	49.36	19608861
674	Acetylation	DLKSGSGKVYQGPAK ECCCCCCEEEECCCC	39.19	25953088
674	Ubiquitination	DLKSGSGKVYQGPAK ECCCCCCEEEECCCC	39.19	-
676	Phosphorylation	KSGSGKVYQGPAKGA CCCCCEEEECCCCCC	15.96	29496907
707	2-Hydroxyisobutyrylation	LGKLDPQKAFFSGRL HCCCCHHHHHHCCCC	53.18	-
707	Acetylation	LGKLDPQKAFFSGRL HCCCCHHHHHHCCCC	53.18	19608861
707	Malonylation	LGKLDPQKAFFSGRL HCCCCHHHHHHCCCC	53.18	26320211
707	Succinylation	LGKLDPQKAFFSGRL HCCCCHHHHHHCCCC	53.18	27452117
707	Ubiquitination	LGKLDPQKAFFSGRL HCCCCHHHHHHCCCC	53.18	19608861
711	Phosphorylation	DPQKAFFSGRLKARG CHHHHHHCCCCHHHC	19.29	24719451
725	Acetylation	GNIMLSQKLQMILKD CCCHHHHHHHHHHHH	36.99	25953088
725	Succinylation	GNIMLSQKLQMILKD CCCHHHHHHHHHHHH	36.99	-
725	Succinylation	GNIMLSQKLQMILKD CCCHHHHHHHHHHHH	36.99	-
731	Acetylation	QKLQMILKDYAKL-- HHHHHHHHHHHCC--	37.46	25953088
731	Malonylation	QKLQMILKDYAKL-- HHHHHHHHHHHCC--	37.46	26320211
731	Succinylation	QKLQMILKDYAKL-- HHHHHHHHHHHCC--	37.46	23954790
731	Ubiquitination	QKLQMILKDYAKL-- HHHHHHHHHHHCC--	37.46	-
733	Phosphorylation	LQMILKDYAKL---- HHHHHHHHHCC----	12.21	24641631

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DHB4_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 DHB4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THIK_HUMAN	ACAA1	physical	22939629
NLTP_HUMAN	SCP2	physical	22939629
GRHPR_HUMAN	GRHPR	physical	22939629
SSBP_HUMAN	SSBP1	physical	22939629
FIS1_HUMAN	FIS1	physical	22939629
RACK1_HUMAN	GNB2L1	physical	22939629
VAMP2_HUMAN	VAMP2	physical	22939629
MK08_HUMAN	MAPK8	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
261515	D-bifunctional protein deficiency (DBPD)
233400	Perrault syndrome 1 (PRLTS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DHB4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-565; LYS-669 AND LYS-707,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-265; THR-292;SER-294; SER-304; SER-309; THR-317; SER-318 AND THR-608, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, AND MASSSPECTROMETRY.	18691976 [Abstract]