COMD6_HUMAN - dbPTM
COMD6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COMD6_HUMAN
UniProt AC Q7Z4G1
Protein Name COMM domain-containing protein 6
Gene Name COMMD6
Organism Homo sapiens (Human).
Sequence Length 85
Subcellular Localization Nucleus . Cytoplasm .
Protein Description May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. [PubMed: 21778237 Down-regulates activation of NF-kappa-B. Inhibits TNF-induced NFKB1 activation.]
Protein Sequence MEASSEPPLDAKSDVTNQLVDFQWKLGMAVSSDTCRSLKYPYVAVMLKVADHSGQVKTKCFEMTIPQFQNFYRQFKEIAAVIETV
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
1Acetylation-------MEASSEPP
-------CCCCCCCC
9.7819413330
12UbiquitinationSEPPLDAKSDVTNQL
CCCCCCCCCHHHHHH
47.0223000965
28SulfoxidationDFQWKLGMAVSSDTC
HHHHHHCCCCCCHHH
4.8921406390
31PhosphorylationWKLGMAVSSDTCRSL
HHHCCCCCCHHHHHC
16.9827251275
32 (in isoform 2)Phosphorylation-30.2727251275
32PhosphorylationKLGMAVSSDTCRSLK
HHCCCCCCHHHHHCC
30.2727251275
39AcetylationSDTCRSLKYPYVAVM
CHHHHHCCCCEEEEE
45.4820167786
39UbiquitinationSDTCRSLKYPYVAVM
CHHHHHCCCCEEEEE
45.4823000965
39 (in isoform 2)Ubiquitination-45.4821890473
39 (in isoform 1)Ubiquitination-45.4821890473
48AcetylationPYVAVMLKVADHSGQ
CEEEEEEEECCCCCC
19.7920167786
57AcetylationADHSGQVKTKCFEMT
CCCCCCEEEEEEEEE
34.0925953088
72PhosphorylationIPQFQNFYRQFKEIA
HHHHHHHHHHHHHHH
15.8530257219
79UbiquitinationYRQFKEIAAVIETV-
HHHHHHHHHHEECC-
9.2121890473

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 COMD6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COMD6_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 COMD6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COMD1_HUMANCOMMD1physical
15799966
TF65_HUMANRELAphysical
15799966
NFKB1_HUMANNFKB1physical
15799966
COMD1_HUMANCOMMD1physical
16573520
COMD6_HUMANCOMMD6physical
16573520
TF65_HUMANRELAphysical
16573520
CCD22_HUMANCCDC22physical
23563313
COMD1_HUMANCOMMD1physical
23563313
COMDA_HUMANCOMMD10physical
23563313
COMD1_HUMANCOMMD1physical
28514442
COMDA_HUMANCOMMD10physical
28514442
FA45A_HUMANFAM45Aphysical
28514442
COMD2_HUMANCOMMD2physical
28514442
COMD4_HUMANCOMMD4physical
28514442
COMD8_HUMANCOMMD8physical
28514442
CCD22_HUMANCCDC22physical
28514442
COMD3_HUMANCOMMD3physical
28514442
CCD93_HUMANCCDC93physical
28514442
CP062_HUMANC16orf62physical
28514442
COMD5_HUMANCOMMD5physical
28514442
COMD9_HUMANCOMMD9physical
28514442
DSCR3_HUMANDSCR3physical
28514442
COMD7_HUMANCOMMD7physical
28514442
E2F6_HUMANE2F6physical
28514442
VPS29_HUMANVPS29physical
28514442
TFDP1_HUMANTFDP1physical
28514442
VP33B_HUMANVPS33Bphysical
28514442
MFAP3_HUMANMFAP3physical
28514442
EMB_HUMANEMBphysical
28514442
TM2D3_HUMANTM2D3physical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COMD6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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