dbPTM

FUMH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FUMH_HUMAN
UniProt AC	P07954
Protein Name	Fumarate hydratase, mitochondrial
Gene Name	FH
Organism	Homo sapiens (Human).
Sequence Length	510
Subcellular Localization	Isoform Mitochondrial: Mitochondrion. Isoform Cytoplasmic: Cytoplasm.
Protein Description	Also acts as a tumor suppressor..
Protein Sequence	MYRALRLLARSRPLVRAPAAALASAPGLGGAAVPSFWPPNAARMASQNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYGLDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3 (in isoform 2)	Phosphorylation	-	26.33	25159151
46	Phosphorylation	PNAARMASQNSFRIE CCHHHHHHCCCEEEE	22.13	25627689
51 (in isoform 2)	Ubiquitination	-	22.20	21890473
54	Nitration	QNSFRIEYDTFGELK CCCEEEEEECCCCEE	20.22	-
54	Phosphorylation	QNSFRIEYDTFGELK CCCEEEEEECCCCEE	20.22	25884760
56	Phosphorylation	SFRIEYDTFGELKVP CEEEEEECCCCEECC	32.41	28152594
61	Acetylation	YDTFGELKVPNDKYY EECCCCEECCCCCCC	51.88	23954790
61	Malonylation	YDTFGELKVPNDKYY EECCCCEECCCCCCC	51.88	26320211
61	Succinylation	YDTFGELKVPNDKYY EECCCCEECCCCCCC	51.88	-
61	Succinylation	YDTFGELKVPNDKYY EECCCCEECCCCCCC	51.88	27452117
61	Ubiquitination	YDTFGELKVPNDKYY EECCCCEECCCCCCC	51.88	-
66	2-Hydroxyisobutyrylation	ELKVPNDKYYGAQTV CEECCCCCCCCCCCC	47.19	-
66	Acetylation	ELKVPNDKYYGAQTV CEECCCCCCCCCCCC	47.19	19608861
66	Malonylation	ELKVPNDKYYGAQTV CEECCCCCCCCCCCC	47.19	26320211
66	Succinylation	ELKVPNDKYYGAQTV CEECCCCCCCCCCCC	47.19	-
66	Succinylation	ELKVPNDKYYGAQTV CEECCCCCCCCCCCC	47.19	27452117
66	Ubiquitination	ELKVPNDKYYGAQTV CEECCCCCCCCCCCC	47.19	19608861
67	Phosphorylation	LKVPNDKYYGAQTVR EECCCCCCCCCCCCC	15.25	25884760
68	Phosphorylation	KVPNDKYYGAQTVRS ECCCCCCCCCCCCCC	16.24	25884760
72	Phosphorylation	DKYYGAQTVRSTMNF CCCCCCCCCCCCCCE	19.83	25954137
75	O-linked_Glycosylation	YGAQTVRSTMNFKIG CCCCCCCCCCCEEEC	27.89	28628081
75	Phosphorylation	YGAQTVRSTMNFKIG CCCCCCCCCCCEEEC	27.89	-
76	Phosphorylation	GAQTVRSTMNFKIGG CCCCCCCCCCEEECC	12.93	25954137
80	2-Hydroxyisobutyrylation	VRSTMNFKIGGVTER CCCCCCEEECCCCCC	35.12	-
80	Acetylation	VRSTMNFKIGGVTER CCCCCCEEECCCCCC	35.12	19608861
80	Malonylation	VRSTMNFKIGGVTER CCCCCCEEECCCCCC	35.12	26320211
80	Succinylation	VRSTMNFKIGGVTER CCCCCCEEECCCCCC	35.12	-
80	Succinylation	VRSTMNFKIGGVTER CCCCCCEEECCCCCC	35.12	27452117
85	Phosphorylation	NFKIGGVTERMPTPV CEEECCCCCCCCCHH	22.58	26437602
90	Phosphorylation	GVTERMPTPVIKAFG CCCCCCCCHHHHHHH	22.35	25159151
94	Ubiquitination	RMPTPVIKAFGILKR CCCCHHHHHHHHHHH	37.59	21890473
94	Acetylation	RMPTPVIKAFGILKR CCCCHHHHHHHHHHH	37.59	19608861
94	Ubiquitination	RMPTPVIKAFGILKR CCCCHHHHHHHHHHH	37.59	19608861
94 (in isoform 1)	Ubiquitination	-	37.59	21890473
100	2-Hydroxyisobutyrylation	IKAFGILKRAAAEVN HHHHHHHHHHHHHHH	37.76	-
100	Methylation	IKAFGILKRAAAEVN HHHHHHHHHHHHHHH	37.76	-
100	Ubiquitination	IKAFGILKRAAAEVN HHHHHHHHHHHHHHH	37.76	-
110	Phosphorylation	AAEVNQDYGLDPKIA HHHHHHHCCCCHHHH	15.15	28152594
115	Acetylation	QDYGLDPKIANAIMK HHCCCCHHHHHHHHH	54.86	23954790
115	Succinylation	QDYGLDPKIANAIMK HHCCCCHHHHHHHHH	54.86	-
115	Succinylation	QDYGLDPKIANAIMK HHCCCCHHHHHHHHH	54.86	27452117
115	Ubiquitination	QDYGLDPKIANAIMK HHCCCCHHHHHHHHH	54.86	-
122	Acetylation	KIANAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	23954790
122	Malonylation	KIANAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	26320211
122	Succinylation	KIANAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	-
122	Succinylation	KIANAIMKAADEVAE HHHHHHHHHHHHHHC	34.02	27452117
131	Acetylation	ADEVAEGKLNDHFPL HHHHHCCCCCCCCCE	35.31	25038526
164	Sulfoxidation	ISNRAIEMLGGELGS HCHHHHHHHCCCCCC	3.26	21406390
171	Phosphorylation	MLGGELGSKIPVHPN HHCCCCCCCCCCCCC	39.78	20068231
172	2-Hydroxyisobutyrylation	LGGELGSKIPVHPND HCCCCCCCCCCCCCC	49.59	-
172	Acetylation	LGGELGSKIPVHPND HCCCCCCCCCCCCCC	49.59	20167786
172	Malonylation	LGGELGSKIPVHPND HCCCCCCCCCCCCCC	49.59	26320211
172	Ubiquitination	LGGELGSKIPVHPND HCCCCCCCCCCCCCC	49.59	-
213	Acetylation	VLLPGLQKLHDALDA HHHHHHHHHHHHHHH	53.48	-
221	2-Hydroxyisobutyrylation	LHDALDAKSKEFAQI HHHHHHHCCHHHHHH	62.82	-
221	Succinylation	LHDALDAKSKEFAQI HHHHHHHCCHHHHHH	62.82	23954790
221	Ubiquitination	LHDALDAKSKEFAQI HHHHHHHCCHHHHHH	62.82	-
223	2-Hydroxyisobutyrylation	DALDAKSKEFAQIIK HHHHHCCHHHHHHHH	57.03	-
223	Acetylation	DALDAKSKEFAQIIK HHHHHCCHHHHHHHH	57.03	26051181
223	Malonylation	DALDAKSKEFAQIIK HHHHHCCHHHHHHHH	57.03	26320211
223	Succinylation	DALDAKSKEFAQIIK HHHHHCCHHHHHHHH	57.03	-
223	Succinylation	DALDAKSKEFAQIIK HHHHHCCHHHHHHHH	57.03	-
223	Ubiquitination	DALDAKSKEFAQIIK HHHHHCCHHHHHHHH	57.03	-
230	2-Hydroxyisobutyrylation	KEFAQIIKIGRTHTQ HHHHHHHHHCCCCCC	40.51	-
230	Ubiquitination	KEFAQIIKIGRTHTQ HHHHHHHHHCCCCCC	40.51	-
236	Phosphorylation	IKIGRTHTQDAVPLT HHHCCCCCCCCCCCC	27.77	26237645
249	Phosphorylation	LTLGQEFSGYVQQVK CCCCCCCHHHHHHHH	28.58	28152594
251	Phosphorylation	LGQEFSGYVQQVKYA CCCCCHHHHHHHHHH	8.22	28152594
256	Acetylation	SGYVQQVKYAMTRIK HHHHHHHHHHHHHHH	23.97	19608861
263	2-Hydroxyisobutyrylation	KYAMTRIKAAMPRIY HHHHHHHHHHHHHHH	27.14	-
263	Malonylation	KYAMTRIKAAMPRIY HHHHHHHHHHHHHHH	27.14	26320211
270	Nitration	KAAMPRIYELAAGGT HHHHHHHHHHHCCCC	13.23	-
270	Phosphorylation	KAAMPRIYELAAGGT HHHHHHHHHHHCCCC	13.23	28152594
277	Phosphorylation	YELAAGGTAVGTGLN HHHHCCCCEECCCCH	19.77	20068231
281	Phosphorylation	AGGTAVGTGLNTRIG CCCCEECCCCHHHCC	31.71	20068231
285	Phosphorylation	AVGTGLNTRIGFAEK EECCCCHHHCCHHHH	28.80	20068231
292	Acetylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	19608861
292	Malonylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	26320211
292	Succinylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	-
292	Succinylation	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	23954790
292	Ubiquitination	TRIGFAEKVAAKVAA HHCCHHHHHHHHHHH	33.47	19608861
296	Acetylation	FAEKVAAKVAALTGL HHHHHHHHHHHHHCC	23.75	27178108
301	Phosphorylation	AAKVAALTGLPFVTA HHHHHHHHCCCCCCC	31.76	19413330
330	Phosphorylation	ELSGAMNTTACSLMK HHCCCCCHHHHHHHH	11.59	24719451
334	Phosphorylation	AMNTTACSLMKIAND CCCHHHHHHHHHHHH	29.09	24719451
343	Methylation	MKIANDIRFLGSGPR HHHHHHCHHCCCCCC	24.49	-
351	Phosphorylation	FLGSGPRSGLGELIL HCCCCCCCCCCCEEC	41.31	27050516
365	Phosphorylation	LPENEPGSSIMPGKV CCCCCCCCCCCCCCC	27.66	25850435
366	Phosphorylation	PENEPGSSIMPGKVN CCCCCCCCCCCCCCC	28.90	25850435
368	Sulfoxidation	NEPGSSIMPGKVNPT CCCCCCCCCCCCCHH	3.75	21406390
465	Phosphorylation	ALNPHIGYDKAAKIA HCCCCCCHHHHHHHH	17.42	21253578
467	Acetylation	NPHIGYDKAAKIAKT CCCCCHHHHHHHHHH	41.58	23954790
467	Succinylation	NPHIGYDKAAKIAKT CCCCCHHHHHHHHHH	41.58	-
467	Succinylation	NPHIGYDKAAKIAKT CCCCCHHHHHHHHHH	41.58	-
470	Acetylation	IGYDKAAKIAKTAHK CCHHHHHHHHHHHHH	48.32	2401403
473	Acetylation	DKAAKIAKTAHKNGS HHHHHHHHHHHHCCC	50.12	2401405
473	Succinylation	DKAAKIAKTAHKNGS HHHHHHHHHHHHCCC	50.12	-
473	Succinylation	DKAAKIAKTAHKNGS HHHHHHHHHHHHCCC	50.12	-
477	Acetylation	KIAKTAHKNGSTLKE HHHHHHHHCCCCHHH	61.61	26051181
485	Phosphorylation	NGSTLKETAIELGYL CCCCHHHHHHHHHCC	31.20	26356563
491	Phosphorylation	ETAIELGYLTAEQFD HHHHHHHCCCHHHHH	17.32	22115753
493	Phosphorylation	AIELGYLTAEQFDEW HHHHHCCCHHHHHHC	21.47	26356563
502	Acetylation	EQFDEWVKPKDMLGP HHHHHCCCHHHHCCC	47.63	-
502	Ubiquitination	EQFDEWVKPKDMLGP HHHHHCCCHHHHCCC	47.63	-
504	Acetylation	FDEWVKPKDMLGPK- HHHCCCHHHHCCCC-	50.48	26822725

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
46	S	Phosphorylation	Kinase	PAK4	O96013	PSP
75	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
90	T	Phosphorylation	Kinase	P38A	Q16539	PSP
236	T	Phosphorylation	Kinase	DNAPK	P78527	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
236	T	Phosphorylation		26237645
[Isoform Cytoplasmic]: Phosphorylation at Thr-236 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SERC_HUMAN	PSAT1	physical	22939629
HEM6_HUMAN	CPOX	physical	22939629
PGM1_HUMAN	PGM1	physical	22939629
THIC_HUMAN	ACAT2	physical	22863883
SAHH_HUMAN	AHCY	physical	22863883
ASB6_HUMAN	ASB6	physical	22863883
PUR9_HUMAN	ATIC	physical	22863883
CALD1_HUMAN	CALD1	physical	22863883
DHX15_HUMAN	DHX15	physical	22863883
EZRI_HUMAN	EZR	physical	22863883
H2AV_HUMAN	H2AFV	physical	22863883
MOES_HUMAN	MSN	physical	22863883
MTRR_HUMAN	MTRR	physical	22863883
NSF1C_HUMAN	NSFL1C	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PAPS1_HUMAN	PAPSS1	physical	22863883
PTMA_HUMAN	PTMA	physical	22863883
PYGL_HUMAN	PYGL	physical	22863883
UBA1_HUMAN	UBA1	physical	22863883
XPP1_HUMAN	XPNPEP1	physical	22863883
PIM1_HUMAN	PIM1	physical	25416956
ANX11_HUMAN	ANXA11	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
CK054_HUMAN	C11orf54	physical	26344197
QSPP_HUMAN	C9orf64	physical	26344197
CAB39_HUMAN	CAB39	physical	26344197
CBR1_HUMAN	CBR1	physical	26344197
CRIP1_HUMAN	CRIP1	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
FAH2A_HUMAN	FAHD2A	physical	26344197
GLOD4_HUMAN	GLOD4	physical	26344197
GNPI1_HUMAN	GNPDA1	physical	26344197
GNPI2_HUMAN	GNPDA2	physical	26344197
GNA1_HUMAN	GNPNAT1	physical	26344197
AATC_HUMAN	GOT1	physical	26344197
GPDA_HUMAN	GPD1	physical	26344197
GPD1L_HUMAN	GPD1L	physical	26344197
HIBCH_HUMAN	HIBCH	physical	26344197
KYNU_HUMAN	KYNU	physical	26344197
SIAS_HUMAN	NANS	physical	26344197
NDUV1_HUMAN	NDUFV1	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
PSMD5_HUMAN	PSMD5	physical	26344197
PTGR1_HUMAN	PTGR1	physical	26344197
UBE2N_HUMAN	UBE2N	physical	26344197
WDFY1_HUMAN	WDFY1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606812	Fumarase deficiency (FMRD)
150800	Hereditary leiomyomatosis and renal cell cancer (HLRCC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FUMH_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-66; LYS-80; LYS-94; LYS-256AND LYS-292, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-491, AND MASSSPECTROMETRY.	18083107 [Abstract]

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