COMD3_HUMAN - dbPTM
COMD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COMD3_HUMAN
UniProt AC Q9UBI1
Protein Name COMM domain-containing protein 3
Gene Name COMMD3
Organism Homo sapiens (Human).
Sequence Length 195
Subcellular Localization Cytoplasm . Nucleus .
Protein Description May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. [PubMed: 21778237 May down-regulate activation of NF-kappa-B]
Protein Sequence MELSESVQKGFQMLADPRSFDSNAFTLLLRAAFQSLLDAQADEAVLDHPDLKHIDPVVLKHCHAAAATYILEAGKHRADKSTLSTYLEDCKFDRERIELFCTEYQNNKNSLEILLGSIGRSLPHITDVSWRLEYQIKTNQLHRMYRPAYLVTLSVQNTDSPSYPEISFSCSMEQLQDLVGKLKDASKSLERATQL
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-------MELSESVQ
-------CCHHHHHH
12.03-
1Sulfoxidation-------MELSESVQ
-------CCHHHHHH
12.0328465586
6Phosphorylation--MELSESVQKGFQM
--CCHHHHHHHHHHH
26.8628857561
9UbiquitinationELSESVQKGFQMLAD
CHHHHHHHHHHHHCC
60.58-
52UbiquitinationVLDHPDLKHIDPVVL
HHCCCCCCCCCHHHH
45.9921963094
60UbiquitinationHIDPVVLKHCHAAAA
CCCHHHHHHHHHHHH
32.3529967540
68PhosphorylationHCHAAAATYILEAGK
HHHHHHHHHHHHCCC
13.3320068231
75UbiquitinationTYILEAGKHRADKST
HHHHHCCCCCCCHHH
36.64-
80UbiquitinationAGKHRADKSTLSTYL
CCCCCCCHHHHHHHH
44.3429967540
91UbiquitinationSTYLEDCKFDRERIE
HHHHHHCCCCHHHHH
63.7224816145
108UbiquitinationCTEYQNNKNSLEILL
HHHHHCCCCCHHHHH
56.3021906983
126PhosphorylationGRSLPHITDVSWRLE
HCCCCCCCCCCHHEE
27.58-
137UbiquitinationWRLEYQIKTNQLHRM
HHEEEEEHHCCCHHE
26.3721890473
137MethylationWRLEYQIKTNQLHRM
HHEEEEEHHCCCHHE
26.37-
137MalonylationWRLEYQIKTNQLHRM
HHEEEEEHHCCCHHE
26.3732601280
183UbiquitinationQDLVGKLKDASKSLE
HHHHHHHHHHHHHHH
55.52-
186PhosphorylationVGKLKDASKSLERAT
HHHHHHHHHHHHHHH
32.6722468782
187UbiquitinationGKLKDASKSLERATQ
HHHHHHHHHHHHHHC
61.8629967540
188PhosphorylationKLKDASKSLERATQL
HHHHHHHHHHHHHCC
32.7322468782
193PhosphorylationSKSLERATQL-----
HHHHHHHHCC-----
36.3022468782

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 COMD3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COMD3_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 COMD3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN337_HUMANZNF337physical
16169070
COMD1_HUMANCOMMD1physical
15799966
NFKB1_HUMANNFKB1physical
15799966
COMD8_HUMANCOMMD8physical
22939629
TRAF5_HUMANTRAF5physical
21988832
COMD2_HUMANCOMMD2physical
26186194
CP062_HUMANC16orf62physical
26186194
CCD93_HUMANCCDC93physical
26186194
COMDA_HUMANCOMMD10physical
26186194
COMD4_HUMANCOMMD4physical
26186194
COMD7_HUMANCOMMD7physical
26186194
FA45A_HUMANFAM45Aphysical
26186194
DSCR3_HUMANDSCR3physical
26186194
COMD6_HUMANCOMMD6physical
26186194
CCD22_HUMANCCDC22physical
26186194
COMD5_HUMANCOMMD5physical
26186194
COMD8_HUMANCOMMD8physical
26186194
COMD9_HUMANCOMMD9physical
26186194
COMD1_HUMANCOMMD1physical
26186194
CCD22_HUMANCCDC22physical
26344197
COMDA_HUMANCOMMD10physical
26344197
COMD2_HUMANCOMMD2physical
26344197
COMD6_HUMANCOMMD6physical
26344197
COMD4_HUMANCOMMD4physical
28514442
FA45A_HUMANFAM45Aphysical
28514442
COMD5_HUMANCOMMD5physical
28514442
CCD93_HUMANCCDC93physical
28514442
CP062_HUMANC16orf62physical
28514442
COMD9_HUMANCOMMD9physical
28514442
COMD7_HUMANCOMMD7physical
28514442
DSCR3_HUMANDSCR3physical
28514442
JOS2_HUMANJOSD2physical
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
There are no disease associations of PTM sites.
Regulatory Network of COMD3_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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