dbPTM

COMD4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COMD4_HUMAN
UniProt AC	Q9H0A8
Protein Name	COMM domain-containing protein 4
Gene Name	COMMD4
Organism	Homo sapiens (Human).
Sequence Length	199
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. [PubMed: 21778237 Down-regulates activation of NF-kappa-B.]
Protein Sequence	MRFRFCGDLDCPDWVLAEISTLAKMSSVKLRLLCSQVLKELLGQGIDYEKILKLTADAKFESGDVKATVAVLSFILSSAAKHSVDGESLSSELQQLGLPKEHAASLCRCYEEKQSPLQKHLRVCSLRMNRLAGVGWRVDYTLSSSLLQSVEEPMVHLRLEVAAAPGTPAQPVAMSLSADKFQVLLAELKQAQTLMSSLG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
27	Phosphorylation	STLAKMSSVKLRLLC HHHHHHCHHHHHHHH	21.55	23532336
29	Ubiquitination	LAKMSSVKLRLLCSQ HHHHCHHHHHHHHHH	29.82	-
29	Acetylation	LAKMSSVKLRLLCSQ HHHHCHHHHHHHHHH	29.82	25953088
29	Malonylation	LAKMSSVKLRLLCSQ HHHHCHHHHHHHHHH	29.82	26320211
39	Ubiquitination	LLCSQVLKELLGQGI HHHHHHHHHHHCCCC	47.67	-
50	Sumoylation	GQGIDYEKILKLTAD CCCCCHHHHHHHHCC	47.30	-
50	2-Hydroxyisobutyrylation	GQGIDYEKILKLTAD CCCCCHHHHHHHHCC	47.30	-
50	Sumoylation	GQGIDYEKILKLTAD CCCCCHHHHHHHHCC	47.30	-
50 (in isoform 1)	Ubiquitination	-	47.30	21890473
50 (in isoform 2)	Ubiquitination	-	47.30	21890473
50	Ubiquitination	GQGIDYEKILKLTAD CCCCCHHHHHHHHCC	47.30	21890473
53 (in isoform 1)	Ubiquitination	-	47.46	21890473
53 (in isoform 2)	Ubiquitination	-	47.46	21890473
53	Ubiquitination	IDYEKILKLTADAKF CCHHHHHHHHCCCCC	47.46	21906983
53	Acetylation	IDYEKILKLTADAKF CCHHHHHHHHCCCCC	47.46	25953088
59 (in isoform 1)	Ubiquitination	-	50.65	21890473
59	Ubiquitination	LKLTADAKFESGDVK HHHHCCCCCCCCCHH	50.65	21906983
59 (in isoform 2)	Ubiquitination	-	50.65	21890473
59	Ubiquitination	LKLTADAKFESGDVK HHHHCCCCCCCCCHH	50.65	21890473
100	Ubiquitination	LQQLGLPKEHAASLC HHHCCCCHHHHHHHH	68.15	-
110	Phosphorylation	AASLCRCYEEKQSPL HHHHHHHHHHHCCHH	14.05	27251275
113	Ubiquitination	LCRCYEEKQSPLQKH HHHHHHHHCCHHHHH	44.10	-
113	Acetylation	LCRCYEEKQSPLQKH HHHHHHHHCCHHHHH	44.10	23749302
115	Phosphorylation	RCYEEKQSPLQKHLR HHHHHHCCHHHHHHH	38.35	25159151
119	Ubiquitination	EKQSPLQKHLRVCSL HHCCHHHHHHHHHHH	52.90	-
125	Phosphorylation	QKHLRVCSLRMNRLA HHHHHHHHHHHHHHC	19.02	28258704
130	Methylation	VCSLRMNRLAGVGWR HHHHHHHHHCCCCCE	19.30	-
167	Phosphorylation	EVAAAPGTPAQPVAM EEECCCCCCCCCEEE	17.87	28555341
180	Ubiquitination	AMSLSADKFQVLLAE EEECCHHHHHHHHHH	37.10	22053931
180 (in isoform 1)	Ubiquitination	-	37.10	21890473
189	Ubiquitination	QVLLAELKQAQTLMS HHHHHHHHHHHHHHH	34.78	-

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 COMD4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of COMD4_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 COMD4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COMD1_HUMAN	COMMD1	physical	15799966
TF65_HUMAN	RELA	physical	15799966
RELB_HUMAN	RELB	physical	15799966
NFKB1_HUMAN	NFKB1	physical	15799966
COMD6_HUMAN	COMMD6	physical	22939629
COMD2_HUMAN	COMMD2	physical	26186194
CP062_HUMAN	C16orf62	physical	26186194
CCD93_HUMAN	CCDC93	physical	26186194
COMDA_HUMAN	COMMD10	physical	26186194
PRPK_HUMAN	TP53RK	physical	26186194
EXOS4_HUMAN	EXOSC4	physical	26186194
COMD7_HUMAN	COMMD7	physical	26186194
FA45A_HUMAN	FAM45A	physical	26186194
EXOS2_HUMAN	EXOSC2	physical	26186194
COMD6_HUMAN	COMMD6	physical	26186194
CCD22_HUMAN	CCDC22	physical	26186194
COMD5_HUMAN	COMMD5	physical	26186194
COMD8_HUMAN	COMMD8	physical	26186194
COMD9_HUMAN	COMMD9	physical	26186194
DSCR3_HUMAN	DSCR3	physical	26186194
TFDP1_HUMAN	TFDP1	physical	26186194
COMD1_HUMAN	COMMD1	physical	26186194
RHG17_HUMAN	ARHGAP17	physical	26344197
GDIR1_HUMAN	ARHGDIA	physical	26344197
VATD_HUMAN	ATP6V1D	physical	26344197
COMD1_HUMAN	COMMD1	physical	26344197
COMD5_HUMAN	COMMD5	physical	26344197
DDX6_HUMAN	DDX6	physical	26344197
MCMBP_HUMAN	MCMBP	physical	26344197
PEPL1_HUMAN	NPEPL1	physical	26344197
PFD4_HUMAN	PFDN4	physical	26344197
PFKAM_HUMAN	PFKM	physical	26344197
PFKAP_HUMAN	PFKP	physical	26344197
ST1A1_HUMAN	SULT1A1	physical	26344197
TIPRL_HUMAN	TIPRL	physical	26344197
TRI25_HUMAN	TRIM25	physical	26344197
UCHL5_HUMAN	UCHL5	physical	26344197
FA45A_HUMAN	FAM45A	physical	28514442
COMD9_HUMAN	COMMD9	physical	28514442
COMD5_HUMAN	COMMD5	physical	28514442
CCD93_HUMAN	CCDC93	physical	28514442
COMD7_HUMAN	COMMD7	physical	28514442
DSCR3_HUMAN	DSCR3	physical	28514442
CP062_HUMAN	C16orf62	physical	28514442
TFDP1_HUMAN	TFDP1	physical	28514442
EXOS2_HUMAN	EXOSC2	physical	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 COMD4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASSSPECTROMETRY.	18691976 [Abstract]