dbPTM

CISD3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CISD3_HUMAN
UniProt AC	P0C7P0
Protein Name	CDGSH iron-sulfur domain-containing protein 3, mitochondrial
Gene Name	CISD3
Organism	Homo sapiens (Human).
Sequence Length	127
Subcellular Localization	Mitochondrion .
Protein Description	Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function..
Protein Sequence	MRGAGAILRPAARGARDLNPRRDISSWLAQWFPRTPARSVVALKTPIKVELVAGKTYRWCVCGRSKKQPFCDGSHFFQRTGLSPLKFKAQETRMVALCTCKATQRPPYCDGTHRSERVQKAEVGSPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	Acetylation	VALKTPIKVELVAGK EEECCCEEEEEECCC	30.75	23749302
48	Malonylation	VALKTPIKVELVAGK EEECCCEEEEEECCC	30.75	26320211
48	Succinylation	VALKTPIKVELVAGK EEECCCEEEEEECCC	30.75	23954790
55	Acetylation	KVELVAGKTYRWCVC EEEEECCCCEEEEEE	32.42	19608861
55	Succinylation	KVELVAGKTYRWCVC EEEEECCCCEEEEEE	32.42	-
55	Succinylation	KVELVAGKTYRWCVC EEEEECCCCEEEEEE	32.42	23954790
80	Phosphorylation	GSHFFQRTGLSPLKF CCCCCHHCCCCCCCC	31.52	30266825
83	Phosphorylation	FFQRTGLSPLKFKAQ CCHHCCCCCCCCCCC	29.54	30266825
86	Acetylation	RTGLSPLKFKAQETR HCCCCCCCCCCCCCE	48.48	25953088
88	Ubiquitination	GLSPLKFKAQETRMV CCCCCCCCCCCCEEE	47.80	24816145
88	2-Hydroxyisobutyrylation	GLSPLKFKAQETRMV CCCCCCCCCCCCEEE	47.80	-
125	Phosphorylation	VQKAEVGSPL----- HHHCCCCCCC-----	28.36	26503514

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 CISD3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CISD3_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 CISD3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CISD3_HUMAN	CISD3	physical	27499296
MIPEP_HUMAN	MIPEP	physical	27499296
ERAL1_HUMAN	ERAL1	physical	27499296
AFG32_HUMAN	AFG3L2	physical	27499296
CLPX_HUMAN	CLPX	physical	27499296
GRSF1_HUMAN	GRSF1	physical	27499296
SCO2_HUMAN	SCO2	physical	27499296
CLPB_HUMAN	CLPB	physical	27499296
MPPA_HUMAN	PMPCA	physical	27499296
MPPB_HUMAN	PMPCB	physical	27499296
MRRP1_HUMAN	TRMT10C	physical	27499296
RPOM_HUMAN	POLRMT	physical	27499296
CHCH2_HUMAN	CHCHD2	physical	27499296
STML2_HUMAN	STOML2	physical	27499296
CX6A1_HUMAN	COX6A1	physical	27499296
MTEF3_HUMAN	MTERF3	physical	27499296
TOM5_HUMAN	TOMM5	physical	27499296
IDE_HUMAN	IDE	physical	27499296
PREP_HUMAN	PITRM1	physical	27499296
TIM44_HUMAN	TIMM44	physical	27499296
SYYM_HUMAN	YARS2	physical	27499296
MTX1_HUMAN	MTX1	physical	27499296
ATP5H_HUMAN	ATP5H	physical	27499296
GLSK_HUMAN	GLS	physical	27499296
PDIP2_HUMAN	POLDIP2	physical	27499296
ODBA_HUMAN	BCKDHA	physical	27499296
NDUA2_HUMAN	NDUFA2	physical	27499296
DHX30_HUMAN	DHX30	physical	27499296
UCRI_HUMAN	UQCRFS1	physical	27499296
NT5D2_HUMAN	NT5DC2	physical	27499296
SYTM_HUMAN	TARS2	physical	27499296
NDUA5_HUMAN	NDUFA5	physical	27499296
ATP5E_HUMAN	ATP5E	physical	27499296
TIM50_HUMAN	TIMM50	physical	27499296
ATPO_HUMAN	ATP5O	physical	27499296
GLRX5_HUMAN	GLRX5	physical	27499296
QCR7_HUMAN	UQCRB	physical	27499296
NDUS2_HUMAN	NDUFS2	physical	27499296
ECH1_HUMAN	ECH1	physical	27499296
COX6C_HUMAN	COX6C	physical	27499296
TXTP_HUMAN	SLC25A1	physical	27499296
AT5F1_HUMAN	ATP5F1	physical	27499296
NDUS3_HUMAN	NDUFS3	physical	27499296
DHC24_HUMAN	DHCR24	physical	27499296
MOT1_HUMAN	SLC16A1	physical	27499296
NDUS1_HUMAN	NDUFS1	physical	27499296
RM22_HUMAN	MRPL22	physical	27499296
SYSM_HUMAN	SARS2	physical	27499296
NIPS1_HUMAN	NIPSNAP1	physical	27499296
NDUC2_HUMAN	NDUFC2	physical	27499296
MAVS_HUMAN	MAVS	physical	27499296
RT10_HUMAN	MRPS10	physical	27499296
RT33_HUMAN	MRPS33	physical	27499296
C1QBP_HUMAN	C1QBP	physical	27499296
ABHDA_HUMAN	ABHD10	physical	27499296
NRDC_HUMAN	NRD1	physical	27499296
ATPG_HUMAN	ATP5C1	physical	27499296
MMAD_HUMAN	MMADHC	physical	27499296
NDUA8_HUMAN	NDUFA8	physical	27499296
MIA40_HUMAN	CHCHD4	physical	27499296
ODP2_HUMAN	DLAT	physical	27499296
CX7A2_HUMAN	COX7A2	physical	27499296
ATP5J_HUMAN	ATP5J	physical	27499296
SCO1_HUMAN	SCO1	physical	27499296
COASY_HUMAN	COASY	physical	27499296
SPART_HUMAN	SPG20	physical	27499296
QCR2_HUMAN	UQCRC2	physical	27499296
COX5A_HUMAN	COX5A	physical	27499296
GSTK1_HUMAN	GSTK1	physical	27499296
TBRG4_HUMAN	TBRG4	physical	27499296

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.

Regulatory Network of CISD3_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-55, AND MASS SPECTROMETRY.	19608861 [Abstract]