ATIF1_HUMAN - dbPTM
ATIF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATIF1_HUMAN
UniProt AC Q9UII2
Protein Name ATPase inhibitor, mitochondrial
Gene Name ATPIF1
Organism Homo sapiens (Human).
Sequence Length 106
Subcellular Localization Mitochondrion .
Protein Description Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme..
Protein Sequence MAVTALAARTWLGVWGVRTMQARGFGSDQSENVDRGAGSIREAGGAFGKREQAEEERYFRAQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLKHDD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
27PhosphorylationMQARGFGSDQSENVD
HHHCCCCCCCCCCCC
30.16-
39PhosphorylationNVDRGAGSIREAGGA
CCCCCCHHHHHCCCC
20.2423401153
41MethylationDRGAGSIREAGGAFG
CCCCHHHHHCCCCCC
29.43-
49AcetylationEAGGAFGKREQAEEE
HCCCCCCCHHHHHHH
46.4325953088
49SuccinylationEAGGAFGKREQAEEE
HCCCCCCCHHHHHHH
46.4323954790
49UbiquitinationEAGGAFGKREQAEEE
HCCCCCCCHHHHHHH
46.4324816145
49SumoylationEAGGAFGKREQAEEE
HCCCCCCCHHHHHHH
46.43-
57MethylationREQAEEERYFRAQSR
HHHHHHHHHHHHHCH
38.89-
58PhosphorylationEQAEEERYFRAQSRE
HHHHHHHHHHHHCHH
10.7423917254
63PhosphorylationERYFRAQSREQLAAL
HHHHHHHCHHHHHHH
36.4825159151
71AcetylationREQLAALKKHHEEEI
HHHHHHHHHHHHHHH
45.3827178108
71MalonylationREQLAALKKHHEEEI
HHHHHHHHHHHHHHH
45.3826320211
72AcetylationEQLAALKKHHEEEIV
HHHHHHHHHHHHHHH
51.5525825284
82AcetylationEEEIVHHKKEIERLQ
HHHHHHCHHHHHHHH
36.9023954790
82SuccinylationEEEIVHHKKEIERLQ
HHHHHHCHHHHHHHH
36.9023954790
822-HydroxyisobutyrylationEEEIVHHKKEIERLQ
HHHHHHCHHHHHHHH
36.90-
83AcetylationEEIVHHKKEIERLQK
HHHHHCHHHHHHHHH
60.617406683
90SuccinylationKEIERLQKEIERHKQ
HHHHHHHHHHHHHHH
66.3123954790
90UbiquitinationKEIERLQKEIERHKQ
HHHHHHHHHHHHHHH
66.31-
90MalonylationKEIERLQKEIERHKQ
HHHHHHHHHHHHHHH
66.3126320211
90AcetylationKEIERLQKEIERHKQ
HHHHHHHHHHHHHHH
66.3123749302
103SuccinylationKQKIKMLKHDD----
HHHHHHHCCCC----
41.30-
103UbiquitinationKQKIKMLKHDD----
HHHHHHHCCCC----
41.3024816145
103SuccinylationKQKIKMLKHDD----
HHHHHHHCCCC----
41.30-
103AcetylationKQKIKMLKHDD----
HHHHHHHCCCC----
41.3027178108

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
39SPhosphorylationKinasePRKACAP17612
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATIF1_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 ATIF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
16169070
CATA_HUMANCATphysical
26344197
LYAG_HUMANGAAphysical
26344197
RNT2_HUMANRNASET2physical
26344197
UCRI_HUMANUQCRFS1physical
26344197

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 ATIF1_HUMAN

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Related Literatures of Post-Translational Modification

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