dbPTM

FUMH_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FUMH_MOUSE
UniProt AC	P97807
Protein Name	Fumarate hydratase, mitochondrial
Gene Name	Fh
Organism	Mus musculus (Mouse).
Sequence Length	507
Subcellular Localization	Isoform Mitochondrial: Mitochondrion. Isoform Cytoplasmic: Cytoplasm.
Protein Description
Protein Sequence	MYRALRLLARSRRLLRVPSAGAAVSGEATTLPRCAPNVARMASQNSFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIQAFGILKRAAAEVNQEYGLDPKIASAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3 (in isoform 2)	Phosphorylation	-	26.33	27818261
11	Phosphorylation	ALRLLARSRRLLRVP HHHHHHHHHHHHCCC	19.02	23882026
23 (in isoform 2)	Acetylation	-	8.62	-
25	Phosphorylation	PSAGAAVSGEATTLP CCCCCCCCCCCCCCC	26.62	29899451
37 (in isoform 2)	Acetylation	-	22.89	-
43	Phosphorylation	PNVARMASQNSFRVE HHHHHHHHCCCEEEE	22.13	29176673
46	Phosphorylation	ARMASQNSFRVEFDT HHHHHCCCEEEEECC	13.54	28059163
58	Acetylation	FDTFGELKVPTDKYY ECCCCCEECCCCCCC	41.70	23576753
58	Glutarylation	FDTFGELKVPTDKYY ECCCCCEECCCCCCC	41.70	24703693
58	Malonylation	FDTFGELKVPTDKYY ECCCCCEECCCCCCC	41.70	26320211
58	Succinylation	FDTFGELKVPTDKYY ECCCCCEECCCCCCC	41.70	-
58	Succinylation	FDTFGELKVPTDKYY ECCCCCEECCCCCCC	41.70	23806337
58	Ubiquitination	FDTFGELKVPTDKYY ECCCCCEECCCCCCC	41.70	-
63	Acetylation	ELKVPTDKYYGAQTV CEECCCCCCCCCCCC	42.73	23806337
63	Glutarylation	ELKVPTDKYYGAQTV CEECCCCCCCCCCCC	42.73	24703693
63	Malonylation	ELKVPTDKYYGAQTV CEECCCCCCCCCCCC	42.73	26320211
63	Succinylation	ELKVPTDKYYGAQTV CEECCCCCCCCCCCC	42.73	-
63	Succinylation	ELKVPTDKYYGAQTV CEECCCCCCCCCCCC	42.73	23806337
63	Ubiquitination	ELKVPTDKYYGAQTV CEECCCCCCCCCCCC	42.73	27667366
69	Phosphorylation	DKYYGAQTVRSTMNF CCCCCCCCCCCCCCE	19.83	24759943
73	Phosphorylation	GAQTVRSTMNFKIGG CCCCCCCCCCEEECC	12.93	24759943
77	Acetylation	VRSTMNFKIGGATER CCCCCCEEECCCCCC	35.12	23576753
77	Glutarylation	VRSTMNFKIGGATER CCCCCCEEECCCCCC	35.12	24703693
77	Malonylation	VRSTMNFKIGGATER CCCCCCEEECCCCCC	35.12	26320211
77	Succinylation	VRSTMNFKIGGATER CCCCCCEEECCCCCC	35.12	-
77	Succinylation	VRSTMNFKIGGATER CCCCCCEEECCCCCC	35.12	23806337
77	Ubiquitination	VRSTMNFKIGGATER CCCCCCEEECCCCCC	35.12	27667366
82	Phosphorylation	NFKIGGATERMPIPV CEEECCCCCCCCCHH	27.65	22817900
97	Acetylation	IQAFGILKRAAAEVN HHHHHHHHHHHHHHH	37.76	22826441
97	Ubiquitination	IQAFGILKRAAAEVN HHHHHHHHHHHHHHH	37.76	22790023
112	Acetylation	QEYGLDPKIASAIMK HHHCCCHHHHHHHHH	51.04	23576753
112	Glutarylation	QEYGLDPKIASAIMK HHHCCCHHHHHHHHH	51.04	24703693
112	Malonylation	QEYGLDPKIASAIMK HHHCCCHHHHHHHHH	51.04	26320211
112	Succinylation	QEYGLDPKIASAIMK HHHCCCHHHHHHHHH	51.04	-
112	Succinylation	QEYGLDPKIASAIMK HHHCCCHHHHHHHHH	51.04	23806337
112	Ubiquitination	QEYGLDPKIASAIMK HHHCCCHHHHHHHHH	51.04	-
115	Phosphorylation	GLDPKIASAIMKAAD CCCHHHHHHHHHHHH	23.08	22817900
119	Acetylation	KIASAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	23576753
119	Glutarylation	KIASAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	24703693
119	Malonylation	KIASAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	26320211
119	Succinylation	KIASAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	-
119	Succinylation	KIASAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	23806337
119	Ubiquitination	KIASAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	-
128	Acetylation	ADEVAEGKLNDHFPL HHHHHCCCCCCCCCE	35.31	22733758
169	Acetylation	LGGELGSKKPVHPND CCCCCCCCCCCCCCC	60.33	23954790
170	Acetylation	GGELGSKKPVHPNDH CCCCCCCCCCCCCCC	54.70	24062335
170	Glutarylation	GGELGSKKPVHPNDH CCCCCCCCCCCCCCC	54.70	24703693
170 (in isoform 2)	Acetylation	-	54.70	-
180	Succinylation	HPNDHVNKSQSSNDT CCCCCCCCCCCCCCC	49.10	24315375
180 (in isoform 2)	Acetylation	-	49.10	-
202	Acetylation	AAAVEVHKVLLPGLQ HHHHHHHHHHHHHHH	39.49	24062335
210	Acetylation	VLLPGLQKLHDALSA HHHHHHHHHHHHHHH	53.48	23576753
210	Succinylation	VLLPGLQKLHDALSA HHHHHHHHHHHHHHH	53.48	23806337
220	Acetylation	DALSAKSKEFAQVIK HHHHHCCHHHHHHHH	57.03	23576753
220	Glutarylation	DALSAKSKEFAQVIK HHHHHCCHHHHHHHH	57.03	24703693
220	Malonylation	DALSAKSKEFAQVIK HHHHHCCHHHHHHHH	57.03	26320211
220	Succinylation	DALSAKSKEFAQVIK HHHHHCCHHHHHHHH	57.03	-
220	Succinylation	DALSAKSKEFAQVIK HHHHHCCHHHHHHHH	57.03	23806337
220	Ubiquitination	DALSAKSKEFAQVIK HHHHHCCHHHHHHHH	57.03	27667366
220 (in isoform 2)	Acetylation	-	57.03	-
227	Acetylation	KEFAQVIKIGRTHTQ HHHHHHHHCCCCCCC	40.01	22826441
233	Phosphorylation	IKIGRTHTQDAVPLT HHCCCCCCCCCEECC	27.77	-
249 (in isoform 2)	Acetylation	-	3.51	-
260	Acetylation	QYAMVRIKAAMPRIY HHHHHHHHHHCHHHH	21.38	24062335
260	Malonylation	QYAMVRIKAAMPRIY HHHHHHHHHHCHHHH	21.38	26320211
260	Succinylation	QYAMVRIKAAMPRIY HHHHHHHHHHCHHHH	21.38	26388266
260	Ubiquitination	QYAMVRIKAAMPRIY HHHHHHHHHHCHHHH	21.38	27667366
278	Phosphorylation	AGGTAVGTGLNTRIG CCCCEECCCCHHHCC	31.71	25890499
289	Acetylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	23576753
289	Glutarylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	24703693
289	Malonylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	26320211
289	Succinylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	-
289	Succinylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	23806337
289	Ubiquitination	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	-
293	Acetylation	FAEKVAAKVAALTGL HHHHHHHHHHHHHCC	23.75	22826441
330	S-nitrosocysteine	GAMNTAACSLMKIAN HHHHHHHHHHHHHHH	2.73	-
330	S-nitrosylation	GAMNTAACSLMKIAN HHHHHHHHHHHHHHH	2.73	21278135
362	Phosphorylation	LPENEPGSSIMPGKV CCCCCCCCCCCCCCC	27.66	23737553
363	Phosphorylation	PENEPGSSIMPGKVN CCCCCCCCCCCCCCC	28.90	20495213
424 (in isoform 2)	Acetylation	-	24.04	-
427 (in isoform 2)	Acetylation	-	10.49	-
430 (in isoform 2)	Acetylation	-	19.88	-
434 (in isoform 2)	Acetylation	-	5.96	-
462	Phosphorylation	ALNPHIGYDKAAKIA HCCCCCCHHHHHHHH	17.42	-
464	Acetylation	NPHIGYDKAAKIAKT CCCCCHHHHHHHHHH	41.58	23864654
464	Succinylation	NPHIGYDKAAKIAKT CCCCCHHHHHHHHHH	41.58	-
464	Succinylation	NPHIGYDKAAKIAKT CCCCCHHHHHHHHHH	41.58	23806337
467	Acetylation	IGYDKAAKIAKTAHK CCHHHHHHHHHHHHH	48.32	23201123
467	Succinylation	IGYDKAAKIAKTAHK CCHHHHHHHHHHHHH	48.32	26388266
470	Acetylation	DKAAKIAKTAHKNGS HHHHHHHHHHHHCCC	50.12	23806337
470	Succinylation	DKAAKIAKTAHKNGS HHHHHHHHHHHHCCC	50.12	-
470	Succinylation	DKAAKIAKTAHKNGS HHHHHHHHHHHHCCC	50.12	23806337
474	Acetylation	KIAKTAHKNGSTLKE HHHHHHHHCCCCHHH	61.61	23864654
482	Phosphorylation	NGSTLKETAIELGYL CCCCHHHHHHHHHCC	31.20	23984901
488	Phosphorylation	ETAIELGYLTAEQFD HHHHHHHCCCHHHHH	17.32	23984901
490	Phosphorylation	AIELGYLTAEQFDEW HHHHHCCCHHHHHHC	21.47	17242355
499	Acetylation	EQFDEWVKPKDMLGP HHHHHCCCHHHHCCC	47.63	23576753
501	Acetylation	FDEWVKPKDMLGPK- HHHCCCHHHHCCCC-	50.48	23954790
501	Succinylation	FDEWVKPKDMLGPK- HHHCCCHHHHCCCC-	50.48	26388266
507	Acetylation	PKDMLGPK------- HHHHCCCC-------	71.78	23864654
507	Succinylation	PKDMLGPK------- HHHHCCCC-------	71.78	26388266

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 FUMH_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
233	T	Phosphorylation		-
[Isoform Cytoplasmic]: Phosphorylation at Thr-233 by PRKDC in response to DNA damage promotes translocation to the nucleus and recruitment to DNA double-strand breaks (DSBs).

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 FUMH_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
XPO1_MOUSE	Xpo1	physical	18782761

Drug and Disease Associations

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

Regulatory Network of FUMH_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-63; LYS-112 AND LYS-474, ANDMASS SPECTROMETRY.	16916647 [Abstract]

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