dbPTM

CCD22_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCD22_HUMAN
UniProt AC	O60826
Protein Name	Coiled-coil domain-containing protein 22
Gene Name	CCDC22
Organism	Homo sapiens (Human).
Sequence Length	627
Subcellular Localization	Endosome .
Protein Description	Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. [PubMed: 23563313 Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes]
Protein Sequence	MEEADRILIHSLRQAGTAVPPDVQTLRAFTTELVVEAVVRCLRVINPAVGSGLSPLLPLAMSARFRLAMSLAQACMDLGYPLELGYQNFLYPSEPDLRDLLLFLAERLPTDASEDADQPAGDSAILLRAIGSQIRDQLALPWVPPHLRTPKLQHLQGSALQKPFHASRLVVPELSSRGEPREFQASPLLLPVPTQVPQPVGRVASLLEHHALQLCQQTGRDRPGDEDWVHRTSRLPPQEDTRAQRQRLQKQLTEHLRQSWGLLGAPIQARDLGELLQAWGAGAKTGAPKGSRFTHSEKFTFHLEPQAQATQVSDVPATSRRPEQVTWAAQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAEREQALRLKSRAVELLPDGTANLAKLQLVVENSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETELGKKTLSNLEKIREDYRALRQENAGLLGRVREA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	ADRILIHSLRQAGTA HHHHHHHHHHHCCCC	20.46	24719451
30	Phosphorylation	VQTLRAFTTELVVEA HHHHHHHCHHHHHHH	20.55	24719451
31	Phosphorylation	QTLRAFTTELVVEAV HHHHHHCHHHHHHHH	22.37	28348404
51	Phosphorylation	VINPAVGSGLSPLLP HHCCCCCCCCCCHHH	29.93	24719451
54	Phosphorylation	PAVGSGLSPLLPLAM CCCCCCCCCHHHHHH	19.61	23403867
70	Phosphorylation	ARFRLAMSLAQACMD HHHHHHHHHHHHHHH	18.23	-
162	Ubiquitination	LQGSALQKPFHASRL HCCCCCCCCCCHHHE	50.96	21890473
250	Ubiquitination	AQRQRLQKQLTEHLR HHHHHHHHHHHHHHH	52.44	-
253	Phosphorylation	QRLQKQLTEHLRQSW HHHHHHHHHHHHHHH	20.90	24719451
259	Phosphorylation	LTEHLRQSWGLLGAP HHHHHHHHHHCCCCC	19.37	28348404
284	Ubiquitination	QAWGAGAKTGAPKGS HHHCCCCCCCCCCCC	46.72	21890473
298	Ubiquitination	SRFTHSEKFTFHLEP CCCCCCCEEEEEECC	53.36	-
347	Phosphorylation	QLEGVNRSIEEVEAD HHHHHHHHHHHHHHH	29.19	29978859
373	Ubiquitination	ESECRHSKLSTAERE HHHHHCCCCCHHHHH	40.09	-
375	Phosphorylation	ECRHSKLSTAEREQA HHHCCCCCHHHHHHH	29.34	24719451
386	Ubiquitination	REQALRLKSRAVELL HHHHHHHHHHHHHHC	31.31	-
402	Ubiquitination	DGTANLAKLQLVVEN CCCCCHHHHHHEEEC	39.67	-
410	Phosphorylation	LQLVVENSAQRVIHL HHHEEECCHHHHHHH	16.57	23092983
423	Acetylation	HLAGQWEKHRVPLLA HHHHCHHHHCCHHHH	33.48	25953088
423	Ubiquitination	HLAGQWEKHRVPLLA HHHHCHHHHCCHHHH	33.48	-
474	Phosphorylation	ARRKEEVYKQLMSEL HHHHHHHHHHHHHHH	9.04	-
508	2-Hydroxyisobutyrylation	VGNIRKQKEEITKIL HHHHHHCHHHHHHHH	61.42	-
513	Ubiquitination	KQKEEITKILSDTKE HCHHHHHHHHHCHHH	47.51	-
519	Ubiquitination	TKILSDTKELQKEIN HHHHHCHHHHHHHHH	62.51	-
523	Ubiquitination	SDTKELQKEINSLSG HCHHHHHHHHHHHCC	73.51	-
527	Phosphorylation	ELQKEINSLSGKLDR HHHHHHHHHCCCCCH	29.58	-
527	O-linked_Glycosylation	ELQKEINSLSGKLDR HHHHHHHHHCCCCCH	29.58	29351928
529	Phosphorylation	QKEINSLSGKLDRTF HHHHHHHCCCCCHHE	33.43	-
529	O-linked_Glycosylation	QKEINSLSGKLDRTF HHHHHHHCCCCCHHE	33.43	29351928
531	Acetylation	EINSLSGKLDRTFAV HHHHHCCCCCHHEEC	43.78	25953088
531	Ubiquitination	EINSLSGKLDRTFAV HHHHHCCCCCHHEEC	43.78	-
545	Ubiquitination	VTDELVFKDAKKDDA CCCHHHCCCCCCCHH	49.66	-
597	Ubiquitination	QIETELGKKTLSNLE HHHHHHHHHHHHHHH	56.03	-
598	Ubiquitination	IETELGKKTLSNLEK HHHHHHHHHHHHHHH	53.55	-
599	Phosphorylation	ETELGKKTLSNLEKI HHHHHHHHHHHHHHH	38.61	-
601	Phosphorylation	ELGKKTLSNLEKIRE HHHHHHHHHHHHHHH	44.60	-
605	Ubiquitination	KTLSNLEKIREDYRA HHHHHHHHHHHHHHH	50.67	-

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 CCD22_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CCD22_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 CCD22_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COMD1_HUMAN	COMMD1	physical	23563313
CUL1_HUMAN	CUL1	physical	23563313
CUL2_HUMAN	CUL2	physical	23563313
CUL3_HUMAN	CUL3	physical	23563313
BL1S6_HUMAN	BLOC1S6	physical	21988832
USBP1_HUMAN	USHBP1	physical	25416956
CCD93_HUMAN	CCDC93	physical	25355947
CP062_HUMAN	C16orf62	physical	25355947
RHG01_HUMAN	ARHGAP1	physical	26344197
CN166_HUMAN	C14orf166	physical	26344197
COMD2_HUMAN	COMMD2	physical	26344197
DSCR3_HUMAN	DSCR3	physical	26344197
NDRG1_HUMAN	NDRG1	physical	26344197
PUR4_HUMAN	PFAS	physical	26344197
PSMG1_HUMAN	PSMG1	physical	26344197
PSMG2_HUMAN	PSMG2	physical	26344197
RPR1A_HUMAN	RPRD1A	physical	26344197
TRI25_HUMAN	TRIM25	physical	26344197
SYWC_HUMAN	WARS	physical	26344197
XPO7_HUMAN	XPO7	physical	26344197
ARAF_HUMAN	ARAF	physical	26496610
DECR_HUMAN	DECR1	physical	26496610
GMDS_HUMAN	GMDS	physical	26496610
PGBM_HUMAN	HSPG2	physical	26496610
FADS1_HUMAN	FADS1	physical	26496610
OAS3_HUMAN	OAS3	physical	26496610
UBC12_HUMAN	UBE2M	physical	26496610
MFHA1_HUMAN	MFHAS1	physical	26496610
VINEX_HUMAN	SORBS3	physical	26496610
SAP18_HUMAN	SAP18	physical	26496610
DSCR3_HUMAN	DSCR3	physical	26496610
BAZ1A_HUMAN	BAZ1A	physical	26496610
HPS5_HUMAN	HPS5	physical	26496610
COMD3_HUMAN	COMMD3	physical	26496610
FA32A_HUMAN	FAM32A	physical	26496610
COMD5_HUMAN	COMMD5	physical	26496610
COMD9_HUMAN	COMMD9	physical	26496610
COMD2_HUMAN	COMMD2	physical	26496610
COMDA_HUMAN	COMMD10	physical	26496610
VPS29_HUMAN	VPS29	physical	26496610
CCD93_HUMAN	CCDC93	physical	26496610
COMD4_HUMAN	COMMD4	physical	26496610
COMD8_HUMAN	COMMD8	physical	26496610
PLXA3_HUMAN	PLXNA3	physical	26496610
CP062_HUMAN	C16orf62	physical	26496610
TOE1_HUMAN	TOE1	physical	26496610
COMD7_HUMAN	COMMD7	physical	26496610
COMD1_HUMAN	COMMD1	physical	26496610
COMD6_HUMAN	COMMD6	physical	26496610
FA45A_HUMAN	FAM45A	physical	26496610
ARG33_HUMAN	ARHGEF33	physical	26496610
FA45A_HUMAN	FAM45A	physical	28514442
COMD3_HUMAN	COMMD3	physical	28514442
MTMR2_HUMAN	MTMR2	physical	28514442
COMD4_HUMAN	COMMD4	physical	28514442
VP33B_HUMAN	VPS33B	physical	28514442
SPE39_HUMAN	VIPAS39	physical	28514442
COMD5_HUMAN	COMMD5	physical	28514442
COMD9_HUMAN	COMMD9	physical	28514442
COMD7_HUMAN	COMMD7	physical	28514442
CP062_HUMAN	C16orf62	physical	28514442
CCD93_HUMAN	CCDC93	physical	28514442
PSPC1_HUMAN	PSPC1	physical	28514442
POTEI_HUMAN	POTEI	physical	28514442
ABI2_HUMAN	ABI2	physical	28514442
ABI1_HUMAN	ABI1	physical	28514442
SPAG5_HUMAN	SPAG5	physical	28514442
NONO_HUMAN	NONO	physical	28514442
ZWINT_HUMAN	ZWINT	physical	28514442
BIRC6_HUMAN	BIRC6	physical	28514442
CYFP2_HUMAN	CYFIP2	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 CCD22_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND MASSSPECTROMETRY.	18088087 [Abstract]