COX2_HUMAN - dbPTM
COX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COX2_HUMAN
UniProt AC P00403
Protein Name Cytochrome c oxidase subunit 2
Gene Name MT-CO2
Organism Homo sapiens (Human).
Sequence Length 227
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein.
Protein Description Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1..
Protein Sequence MAHAAQVGLQDATSPIMEELITFHDHALMIIFLICFLVLYALFLTLTTKLTNTNISDAQEMETVWTILPAIILVLIALPSLRILYMTDEVNDPSLTIKSIGHQWYWTYEYTDYGGLIFNSYMLPPLFLEPGDLRLLDVDNRVVLPIEAPIRMMITSQDVLHSWAVPTLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEMGPVFTL
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
61SulfoxidationNISDAQEMETVWTIL
CCCCHHHHHHHHHHH
3.3028183972
80PhosphorylationLVLIALPSLRILYMT
HHHHHHCCCCHHHCC
31.0024719451
82MethylationLIALPSLRILYMTDE
HHHHCCCCHHHCCCC
22.62-
86SulfoxidationPSLRILYMTDEVNDP
CCCCHHHCCCCCCCC
3.2328183972
94PhosphorylationTDEVNDPSLTIKSIG
CCCCCCCCEEEEECC
40.7924719451
171UbiquitinationAVPTLGLKTDAIPGR
CCCCCCCCCCCCCCC
42.4321890473
182PhosphorylationIPGRLNQTTFTATRP
CCCCCCCCEEEEECC
23.8621406692
183PhosphorylationPGRLNQTTFTATRPG
CCCCCCCEEEEECCC
14.8221406692
185PhosphorylationRLNQTTFTATRPGVY
CCCCCEEEEECCCEE
25.6521406692
187PhosphorylationNQTTFTATRPGVYYG
CCCEEEEECCCEEEE
34.0521406692
196S-nitrosocysteinePGVYYGQCSEICGAN
CCEEEEEHHHHCCCC
3.24-
196S-nitrosylationPGVYYGQCSEICGAN
CCEEEEEHHHHCCCC
3.2422178444
200S-nitrosocysteineYGQCSEICGANHSFM
EEEHHHHCCCCCCCH
3.55-
200S-nitrosylationYGQCSEICGANHSFM
EEEHHHHCCCCCCCH
3.5522178444

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 COX2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COX2_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 COX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSA1_HUMANPSMA1physical
21988832
RIDA_HUMANHRSP12physical
21988832
BAP31_HUMANBCAP31physical
15254227
COX41_HUMANCOX4I1physical
26344197
OST48_HUMANDDOSTphysical
26344197
MAGT1_HUMANMAGT1physical
26344197
PHB_HUMANPHBphysical
26344197
SSRA_HUMANSSR1physical
26344197
SSRD_HUMANSSR4physical
26344197
QCR2_HUMANUQCRC2physical
26344197
VDAC1_HUMANVDAC1physical
26344197
VDAC2_HUMANVDAC2physical
26344197
VDAC3_HUMANVDAC3physical
26344197
STOM_HUMANSTOMphysical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
220110Mitochondrial complex IV deficiency (MT-C4D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB02659Cholic Acid
Regulatory Network of COX2_HUMAN

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Related Literatures of Post-Translational Modification

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