dbPTM

COMD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COMD1_HUMAN
UniProt AC	Q8N668
Protein Name	COMM domain-containing protein 1
Gene Name	COMMD1
Organism	Homo sapiens (Human).
Sequence Length	190
Subcellular Localization	Nucleus . Cytoplasm . Endosome membrane . Cytoplasmic vesicle . Early endosome . Recycling endosome . Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins.
Protein Description	Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. [PubMed: 21778237 Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity]
Protein Sequence	MAAGELEGGKPLSGLLNALAQDTFHGYPGITEELLRSQLYPEVPPEEFRPFLAKMRGILKSIASADMDFNQLEAFLTAQTKKQGGITSDQAAVISKFWKSHKTKIRESLMNQSRWNSGLRGLSWRVDGKSQSRHSAQIHTPVAIIELELGKYGQESEFLCLEFDEVKVNQILKTLSEVEESISTLISQPN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAGELEGG ------CCCCCCCCC	24.95	19413330
61	Phosphorylation	KMRGILKSIASADMD HHHHHHHHHHCCCCC	21.68	22210691
64	Phosphorylation	GILKSIASADMDFNQ HHHHHHHCCCCCHHH	24.11	22210691
81	Ubiquitination	AFLTAQTKKQGGITS HHHHHHHHHCCCCCH	30.90	32015554
81	Ubiquitination	AFLTAQTKKQGGITS HHHHHHHHHCCCCCH	30.90	-
82	Ubiquitination	FLTAQTKKQGGITSD HHHHHHHHCCCCCHH	58.52	29967540
82	Ubiquitination	FLTAQTKKQGGITSD HHHHHHHHCCCCCHH	58.52	-
82	Malonylation	FLTAQTKKQGGITSD HHHHHHHHCCCCCHH	58.52	32601280
87	Phosphorylation	TKKQGGITSDQAAVI HHHCCCCCHHHHHHH	29.53	21406692
88	Phosphorylation	KKQGGITSDQAAVIS HHCCCCCHHHHHHHH	26.29	21406692
95	Phosphorylation	SDQAAVISKFWKSHK HHHHHHHHHHHHHHH	18.40	21406692
96	Acetylation	DQAAVISKFWKSHKT HHHHHHHHHHHHHHH	44.08	25953088
123	Phosphorylation	NSGLRGLSWRVDGKS CCCCCCCEEEECCCC	18.70	24719451
135	Phosphorylation	GKSQSRHSAQIHTPV CCCCCCCCCEECCCE	22.28	25159151
140	Phosphorylation	RHSAQIHTPVAIIEL CCCCEECCCEEEEEE	22.53	28122231

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
-	K	Ubiquitination	E3 ubiquitin ligase	XIAP	P98170	PMID:14685266
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:20068069

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
63	K	ubiquitylation		20068069
Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked polyubiquitination.

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 COMD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IKBA_HUMAN	NFKBIA	physical	14685242
XIAP_HUMAN	XIAP	physical	18795889
SOCS1_HUMAN	SOCS1	physical	17183367
CUL2_HUMAN	CUL2	physical	17183367
TF65_HUMAN	RELA	physical	17183367
CUL1_HUMAN	CUL1	physical	21778237
CUL2_HUMAN	CUL2	physical	21778237
CUL3_HUMAN	CUL3	physical	21778237
CUL4A_HUMAN	CUL4A	physical	21778237
CUL4B_HUMAN	CUL4B	physical	21778237
CUL5_HUMAN	CUL5	physical	21778237
CUL7_HUMAN	CUL7	physical	21778237
HSP74_HUMAN	HSPA4	physical	19802386
HIF1A_HUMAN	HIF1A	physical	19802386
TF65_HUMAN	RELA	physical	20048074
CLUS_HUMAN	CLU	physical	20068069
IKBA_HUMAN	NFKBIA	physical	20068069
CFTR_HUMAN	CFTR	physical	21483833
SCNND_HUMAN	SCNN1D	physical	21741370
KAT2A_HUMAN	KAT2A	physical	19339690
TF65_HUMAN	RELA	physical	19339690
SGK1_HUMAN	SGK1	physical	20237237
SCNNB_HUMAN	SCNN1B	physical	20237237
AKT1_HUMAN	AKT1	physical	20237237
XIAP_HUMAN	XIAP	physical	14685266
BIRC1_HUMAN	NAIP	physical	14685266
BIRC3_HUMAN	BIRC3	physical	14685266
CDN2A_HUMAN	CDKN2A	physical	18305112
ARF_HUMAN	CDKN2A	physical	18305112
NMRL1_HUMAN	NMRAL1	physical	19433587
SODC_HUMAN	SOD1	physical	20595380
ATP7B_HUMAN	ATP7B	physical	12968035
COMD1_HUMAN	COMMD1	physical	15799966
TF65_HUMAN	RELA	physical	15799966
REL_HUMAN	REL	physical	15799966
RELB_HUMAN	RELB	physical	15799966
NFKB1_HUMAN	NFKB1	physical	15799966
NFKB2_HUMAN	NFKB2	physical	15799966
SCNND_HUMAN	SCNN1D	physical	14645214
SCNNB_HUMAN	SCNN1B	physical	14645214
SCNNG_HUMAN	SCNN1G	physical	14645214
COMD6_HUMAN	COMMD6	physical	16573520
IKBA_HUMAN	NFKBIA	physical	16573520
TF65_HUMAN	RELA	physical	16573520
ATP7B_HUMAN	ATP7B	physical	17919502
CCD22_HUMAN	CCDC22	physical	23563313
COMD6_HUMAN	COMMD6	physical	23563313
CUL2_HUMAN	CUL2	physical	23563313
EP300_HUMAN	EP300	physical	25074812
TF65_HUMAN	RELA	physical	25074812
COMD6_HUMAN	COMMD6	physical	25416956
CP062_HUMAN	C16orf62	physical	25355947
CCD93_HUMAN	CCDC93	physical	25355947
PRKN_HUMAN	PARK2	physical	24691167
IKBA_HUMAN	NFKBIA	physical	25520503
COMD8_HUMAN	COMMD8	physical	28514442
COMDA_HUMAN	COMMD10	physical	28514442
COMD4_HUMAN	COMMD4	physical	28514442
FA45A_HUMAN	FAM45A	physical	28514442
COMD3_HUMAN	COMMD3	physical	28514442
CCD22_HUMAN	CCDC22	physical	28514442
COMD5_HUMAN	COMMD5	physical	28514442
CP062_HUMAN	C16orf62	physical	28514442
CCD93_HUMAN	CCDC93	physical	28514442
COMD7_HUMAN	COMMD7	physical	28514442
COMD9_HUMAN	COMMD9	physical	28514442
COMD2_HUMAN	COMMD2	physical	28514442
DSCR3_HUMAN	DSCR3	physical	28514442
E2F6_HUMAN	E2F6	physical	28514442
TFDP1_HUMAN	TFDP1	physical	28514442
BCR_HUMAN	BCR	physical	28514442
VPS29_HUMAN	VPS29	physical	28514442
VP33B_HUMAN	VPS33B	physical	28514442
S11IP_HUMAN	STK11IP	physical	28514442
TTF2_HUMAN	TTF2	physical	28514442
NFYC_HUMAN	NFYC	physical	28514442
G6PD_HUMAN	G6PD	physical	28514442
ATD3C_HUMAN	ATAD3C	physical	28514442
TBCD4_HUMAN	TBC1D4	physical	28514442
RAD21_HUMAN	RAD21	physical	28514442
F107A_HUMAN	FAM107A	physical	28604741

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 COMD1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]

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