COX1_HUMAN - dbPTM
COX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COX1_HUMAN
UniProt AC P00395
Protein Name Cytochrome c oxidase subunit 1
Gene Name MT-CO1
Organism Homo sapiens (Human).
Sequence Length 513
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. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B..
Protein Sequence MFADRWLFSTNHKDIGTLYLLFGAWAGVLGTALSLLIRAELGQPGNLLGNDHIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASAMVEAGAGTGWTVYPPLAGNYSHPGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGSNMKWSAAVLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFSGYTLDQTYAKIHFTIMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAYTTWNILSSVGSFISLTAVMLMIFMIWEAFASKRKVLMVEEPSMNLEWLYGCPPPYHTFEEPVYMKS
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
17PhosphorylationTNHKDIGTLYLLFGA
CCCCCHHHHHHHHHH
16.74-
19PhosphorylationHKDIGTLYLLFGAWA
CCCHHHHHHHHHHHH
10.95-
31PhosphorylationAWAGVLGTALSLLIR
HHHHHHHHHHHHHHH
21.92-
34PhosphorylationGVLGTALSLLIRAEL
HHHHHHHHHHHHHHH
20.75-
279PhosphorylationGMVWAMMSIGFLGFI
HHHHHHHHHHHHHHH
13.3830257219
316PhosphorylationTMIIAIPTGVKVFSW
EEEEEECCCCHHHHH
48.7929514088
330PhosphorylationWLATLHGSNMKWSAA
HHHHHCCCCCHHHHH
24.01-
409PhosphorylationGYTLDQTYAKIHFTI
CCCCCHHHHCCEEEE
10.5625332170
415PhosphorylationTYAKIHFTIMFIGVN
HHHCCEEEEEEEEEC
9.4325332170
434PhosphorylationPQHFLGLSGMPRRYS
CHHHHCCCCCCCCCC
31.1125332170
455O-linked_GlycosylationTTWNILSSVGSFISL
HHHHHHHHHHHHHHH
27.3528510447
489PhosphorylationVLMVEEPSMNLEWLY
EEEEECCCCCCHHHH
24.4725262027
496PhosphorylationSMNLEWLYGCPPPYH
CCCCHHHHCCCCCCC
20.1125262027
502PhosphorylationLYGCPPPYHTFEEPV
HHCCCCCCCCCCCCC
21.1825262027
504PhosphorylationGCPPPYHTFEEPVYM
CCCCCCCCCCCCCCC
27.2225262027
510PhosphorylationHTFEEPVYMKS----
CCCCCCCCCCC----
15.0025262027

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 COX1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COX1_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 COX1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRDX4_HUMANPRDX4physical
21988832
COX2_HUMANCOX2physical
22252130
NDUB8_HUMANNDUFB8physical
22252130
COX41_HUMANCOX4I1physical
22252130

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COX1_HUMAN

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Related Literatures of Post-Translational Modification

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