COX41_HUMAN - dbPTM
COX41_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COX41_HUMAN
UniProt AC P13073
Protein Name Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
Gene Name COX4I1
Organism Homo sapiens (Human).
Sequence Length 169
Subcellular Localization Mitochondrion inner membrane.
Protein Description This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport..
Protein Sequence MLATRVFSLVGKRAISTSVCVRAHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRGSNEWKTVVGGAMFFIGFTALVIMWQKHYVYGPLPQSFDKEWVAKQTKRMLDMKVNPIQGLASKWDYEKNEWKK
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
12MethylationRVFSLVGKRAISTSV
HHHHHHCCCCCCCHH		31.04-
12AcetylationRVFSLVGKRAISTSV
HHHHHHCCCCCCCHH		31.0425953088
26PhosphorylationVCVRAHESVVKSEDF
HHHHHCCHHCCCCCC		23.4921406692
29UbiquitinationRAHESVVKSEDFSLP
HHCCHHCCCCCCCCC		46.0721890473
29AcetylationRAHESVVKSEDFSLP
HHCCHHCCCCCCCCC		46.0725038526
29SuccinylationRAHESVVKSEDFSLP
HHCCHHCCCCCCCCC		46.0721890473
29SuccinylationRAHESVVKSEDFSLP
HHCCHHCCCCCCCCC		46.07-
29UbiquitinationRAHESVVKSEDFSLP
HHCCHHCCCCCCCCC		46.0721890473
30PhosphorylationAHESVVKSEDFSLPA
HCCHHCCCCCCCCCC		30.6825159151
34PhosphorylationVVKSEDFSLPAYMDR
HCCCCCCCCCCCCCC		45.8523312004
38NitrationEDFSLPAYMDRRDHP
CCCCCCCCCCCCCCC		9.52-
38PhosphorylationEDFSLPAYMDRRDHP
CCCCCCCCCCCCCCC		9.52-
53UbiquitinationLPEVAHVKHLSASQK
CCCCHHHHHHCHHHH		29.0321890473
53MalonylationLPEVAHVKHLSASQK
CCCCHHHHHHCHHHH		29.0326320211
53UbiquitinationLPEVAHVKHLSASQK
CCCCHHHHHHCHHHH		29.0321890473
53AcetylationLPEVAHVKHLSASQK
CCCCHHHHHHCHHHH		29.0319608861
532-HydroxyisobutyrylationLPEVAHVKHLSASQK
CCCCHHHHHHCHHHH		29.03-
56PhosphorylationVAHVKHLSASQKALK
CHHHHHHCHHHHHHH		26.1224719451
58PhosphorylationHVKHLSASQKALKEK
HHHHHCHHHHHHHHH		28.9225849741
60SuccinylationKHLSASQKALKEKEK
HHHCHHHHHHHHHHH		53.87-
60SuccinylationKHLSASQKALKEKEK
HHHCHHHHHHHHHHH		53.8727452117
60UbiquitinationKHLSASQKALKEKEK
HHHCHHHHHHHHHHH		53.8719608861
60MalonylationKHLSASQKALKEKEK
HHHCHHHHHHHHHHH		53.8726320211
60AcetylationKHLSASQKALKEKEK
HHHCHHHHHHHHHHH		53.8719608861
63MethylationSASQKALKEKEKASW
CHHHHHHHHHHHCCH		72.15-
67SuccinylationKALKEKEKASWSSLS
HHHHHHHHCCHHHCC		59.8123954790
67MalonylationKALKEKEKASWSSLS
HHHHHHHHCCHHHCC		59.8126320211
67AcetylationKALKEKEKASWSSLS
HHHHHHHHCCHHHCC		59.8125953088
67UbiquitinationKALKEKEKASWSSLS
HHHHHHHHCCHHHCC		59.81-
69PhosphorylationLKEKEKASWSSLSMD
HHHHHHCCHHHCCHH		38.2621406692
71PhosphorylationEKEKASWSSLSMDEK
HHHHCCHHHCCHHHC		20.9321406692
72PhosphorylationKEKASWSSLSMDEKV
HHHCCHHHCCHHHCH		20.4321406692
74PhosphorylationKASWSSLSMDEKVEL
HCCHHHCCHHHCHHE		26.5721406692
872-HydroxyisobutyrylationELYRIKFKESFAEMN
HEEEEEEHHHHHHHC		47.66-
87AcetylationELYRIKFKESFAEMN
HEEEEEEHHHHHHHC		47.6623954790
87UbiquitinationELYRIKFKESFAEMN
HEEEEEEHHHHHHHC		47.66-
87SuccinylationELYRIKFKESFAEMN
HEEEEEEHHHHHHHC		47.6623954790
87MalonylationELYRIKFKESFAEMN
HEEEEEEHHHHHHHC		47.6626320211
89PhosphorylationYRIKFKESFAEMNRG
EEEEEHHHHHHHCCC		30.2820068231
93SulfoxidationFKESFAEMNRGSNEW
EHHHHHHHCCCCCHH		3.5721406390
124PhosphorylationVIMWQKHYVYGPLPQ
HHHHHHHCCCCCCCC		11.47-
126PhosphorylationMWQKHYVYGPLPQSF
HHHHHCCCCCCCCCC		13.0828064214
132PhosphorylationVYGPLPQSFDKEWVA
CCCCCCCCCCHHHHH		33.2125159151
1352-HydroxyisobutyrylationPLPQSFDKEWVAKQT
CCCCCCCHHHHHHHH		52.01-
135AcetylationPLPQSFDKEWVAKQT
CCCCCCCHHHHHHHH		52.0125825284
135UbiquitinationPLPQSFDKEWVAKQT
CCCCCCCHHHHHHHH		52.0121890473
135UbiquitinationPLPQSFDKEWVAKQT
CCCCCCCHHHHHHHH		52.0121890473
140UbiquitinationFDKEWVAKQTKRMLD
CCHHHHHHHHHHHHH		49.21-
149UbiquitinationTKRMLDMKVNPIQGL
HHHHHHCCCCCCHHH		38.2321890473
1492-HydroxyisobutyrylationTKRMLDMKVNPIQGL
HHHHHHCCCCCCHHH		38.23-
149UbiquitinationTKRMLDMKVNPIQGL
HHHHHHCCCCCCHHH		38.2321906983
158PhosphorylationNPIQGLASKWDYEKN
CCCHHHHHHHCHHCC		39.0420068231
159UbiquitinationPIQGLASKWDYEKNE
CCHHHHHHHCHHCCC		38.1821890473
159AcetylationPIQGLASKWDYEKNE
CCHHHHHHHCHHCCC		38.1827452117
1592-HydroxyisobutyrylationPIQGLASKWDYEKNE
CCHHHHHHHCHHCCC		38.18-
159UbiquitinationPIQGLASKWDYEKNE
CCHHHHHHHCHHCCC		38.1821890473
164UbiquitinationASKWDYEKNEWKK--
HHHHCHHCCCCCC--		54.6721906983
164AcetylationASKWDYEKNEWKK--
HHHHCHHCCCCCC--		54.6725825284
164UbiquitinationASKWDYEKNEWKK--
HHHHCHHCCCCCC--		54.6721890473
168AcetylationDYEKNEWKK------
CHHCCCCCC------		42.2911794739
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 COX41_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COX41_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 COX41_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SDCB1_HUMANSDCBPphysical
25416956
ECHM_HUMANECHS1physical
26186194
ODB2_HUMANDBTphysical
26186194
FMC1_HUMANC7orf55physical
26186194
GCSP_HUMANGLDCphysical
26186194
ALDOA_HUMANALDOAphysical
26344197
BAP29_HUMANBCAP29physical
26344197
BAP31_HUMANBCAP31physical
26344197
CISD2_HUMANCISD2physical
26344197
COX5A_HUMANCOX5Aphysical
26344197
OST48_HUMANDDOSTphysical
26344197
NDUA2_HUMANNDUFA2physical
26344197
NDUS4_HUMANNDUFS4physical
26344197
PHB_HUMANPHBphysical
26344197
SSRG_HUMANSSR3physical
26344197
SSRD_HUMANSSR4physical
26344197
TPM1_HUMANTPM1physical
26344197
TPM2_HUMANTPM2physical
26344197
TPM3_HUMANTPM3physical
26344197
TPM4_HUMANTPM4physical
26344197
QCR7_HUMANUQCRBphysical
26344197
VDAC1_HUMANVDAC1physical
26344197
VDAC2_HUMANVDAC2physical
26344197
FMC1_HUMANC7orf55physical
28514442
ODB2_HUMANDBTphysical
28514442
COR1A_HUMANCORO1Aphysical
28514442
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
DB02659Cholic Acid
Regulatory Network of COX41_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-53 AND LYS-60, AND MASSSPECTROMETRY.

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