SCO1_HUMAN - dbPTM
SCO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCO1_HUMAN
UniProt AC O75880
Protein Name Protein SCO1 homolog, mitochondrial
Gene Name SCO1
Organism Homo sapiens (Human).
Sequence Length 301
Subcellular Localization Mitochondrion . Mitochondrion inner membrane
Single-pass membrane protein .
Protein Description Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT-CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. [PubMed: 15659396]
Protein Sequence MAMLVLVPGRVMRPLGGQLWRFLPRGLEFWGPAEGTARVLLRQFCARQAEAWRASGRPGYCLGTRPLSTARPPPPWSQKGPGDSTRPSKPGPVSWKSLAITFAIGGALLAGMKHVKKEKAEKLEKERQRHIGKPLLGGPFSLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSITTLPDLTPLFISIDPERDTKEAIANYVKEFSPKLVGLTGTREEVDQVARAYRVYYSPGPKDEDEDYIVDHTIIMYLIGPDGEFLDYFGQNKRKGEIAASIATHMRPYRKKS
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
22UbiquitinationLGGQLWRFLPRGLEF
CCHHHHHHCCCCCCC
8.1321890473
60PhosphorylationRASGRPGYCLGTRPL
HHCCCCCCCCCCCCC
6.28-
89UbiquitinationGDSTRPSKPGPVSWK
CCCCCCCCCCCCCHH
57.5922817900
89MalonylationGDSTRPSKPGPVSWK
CCCCCCCCCCCCCHH
57.5926320211
119AcetylationMKHVKKEKAEKLEKE
HHHHHHHHHHHHHHH
71.3930592243
133AcetylationERQRHIGKPLLGGPF
HHHHHCCCCCCCCCC
31.7126051181
133UbiquitinationERQRHIGKPLLGGPF
HHHHHCCCCCCCCCC
31.7122817900
141PhosphorylationPLLGGPFSLTTHTGE
CCCCCCCCCEECCCC
28.1220860994
143PhosphorylationLGGPFSLTTHTGERK
CCCCCCCEECCCCCC
18.4820860994
144PhosphorylationGGPFSLTTHTGERKT
CCCCCCEECCCCCCC
23.8028348404
146PhosphorylationPFSLTTHTGERKTDK
CCCCEECCCCCCCCC
38.3520860994
189PhosphorylationQVVDEIDSITTLPDL
HHHHHHHHCCCCCCC
27.7424275569
191PhosphorylationVDEIDSITTLPDLTP
HHHHHHCCCCCCCCE
26.6524275569
2102-HydroxyisobutyrylationIDPERDTKEAIANYV
ECCCCCHHHHHHHHH
49.81-
210UbiquitinationIDPERDTKEAIANYV
ECCCCCHHHHHHHHH
49.8129901268
216PhosphorylationTKEAIANYVKEFSPK
HHHHHHHHHHHHCHH
12.13-
218UbiquitinationEAIANYVKEFSPKLV
HHHHHHHHHHCHHHH
42.5632015554
221PhosphorylationANYVKEFSPKLVGLT
HHHHHHHCHHHHCCC
23.4024719451
223UbiquitinationYVKEFSPKLVGLTGT
HHHHHCHHHHCCCCC
55.3929967540
2232-HydroxyisobutyrylationYVKEFSPKLVGLTGT
HHHHHCHHHHCCCCC
55.39-
228PhosphorylationSPKLVGLTGTREEVD
CHHHHCCCCCHHHHH
30.4921406692
230PhosphorylationKLVGLTGTREEVDQV
HHHCCCCCHHHHHHH
29.6721406692
246PhosphorylationRAYRVYYSPGPKDED
HHHEEEECCCCCCCC
12.99-
283UbiquitinationYFGQNKRKGEIAASI
HHCCCCCCHHHHHHH
63.61-
289PhosphorylationRKGEIAASIATHMRP
CCHHHHHHHHHHCCC
12.0620068231
292PhosphorylationEIAASIATHMRPYRK
HHHHHHHHHCCCCCC
17.9720068231
297PhosphorylationIATHMRPYRKKS---
HHHHCCCCCCCC---
25.3820068231

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 SCO1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCO1_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 SCO1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SCO1_HUMAN !!

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
There are no disease associations of PTM sites.
Regulatory Network of SCO1_HUMAN

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Related Literatures of Post-Translational Modification

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