dbPTM

CARD9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CARD9_HUMAN
UniProt AC	Q9H257
Protein Name	Caspase recruitment domain-containing protein 9
Gene Name	CARD9
Organism	Homo sapiens (Human).
Sequence Length	536
Subcellular Localization	Cytoplasm .
Protein Description	Adapter protein that plays a key role in innate immune response to a number of intracellular pathogens, such as C.albicans and L.monocytogenes. Is at the crossroads of ITAM-tyrosine kinase and the Toll-like receptors (TLR) and NOD2 signaling pathways. Probably controls various innate immune response pathways depending on the intracellular pathogen. In response to L.monocytogenes infection, acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B. Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B (By similarity). Controls CLEC7A (dectin-1)-mediated myeloid cell activation induced by the yeast cell wall component zymosan, leading to cytokine production and innate anti-fungal immunity: acts by regulating BCL10-MALT1-mediated NF-kappa-B activation pathway. Activates NF-kappa-B via BCL10. In response to the hyphal form of C.albicans, mediates CLEC6A (dectin-2)-induced I-kappa-B kinase ubiquitination, leading to NF-kappa-B activation via interaction with BCL10. In response to fungal infection, may be required for the development and subsequent differentiation of interleukin 17-producing T helper (TH-17) cells..
Protein Sequence	MSDYENDDECWSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYKKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECEAGSRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWELQQEKALLQARVQELEASVQEGKLDRSSPYIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEAQLLAVEGRLRRQQLETLVLSSDLEDGSPRRSQELSLPQDLEDTQLSDKGCLAGGGSPKQPFAALHQEQVLRNPHDAGLSSGEPPEKERRRLKESFENYRRKRALRKMQKGWRQGEEDRENTTGSDNTDTEGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDYENDDE ------CCCCCCCHH	49.23	28270605
38	Sumoylation	TPYLRQCKVLNPDDE CHHHHCCCCCCCCCH	41.22	-
76	Phosphorylation	QRTGHKGYVAFLESL HHHCCCCHHHHHHHH	8.07	-
86	Phosphorylation	FLESLELYYPQLYKK HHHHHHHHHHHHHHH	12.06	-
95	Phosphorylation	PQLYKKVTGKEPARV HHHHHHHHCCCCHHH	51.95	22265677
125	Ubiquitination	LLMTEVMKLQKKVQD HHHHHHHHHHHHHHH	53.60	-
134	Phosphorylation	QKKVQDLTALLSSKD HHHHHHHHHHHCCCH	24.45	24670416
152	Phosphorylation	KELRVKDSLLRKHQE HHHHHHHHHHHHHHH	24.48	28857561
178	S-nitrosylation	GSRELKRCKEENYDL HHHHHHHHHHHCHHH	6.59	24105792
231	Phosphorylation	CKVERKHTLKLRHAM CCCCHHHHHHHHHHH	28.73	22265677
267	Phosphorylation	RVQELEASVQEGKLD HHHHHHHHHHCCCCC	18.24	28450419
276	Phosphorylation	QEGKLDRSSPYIQVL HCCCCCCCCCCHHHH	35.02	28450419
277	Phosphorylation	EGKLDRSSPYIQVLE CCCCCCCCCCHHHHH	23.71	28450419
279	Phosphorylation	KLDRSSPYIQVLEED CCCCCCCCHHHHHHH	13.11	23186163
300	Phosphorylation	DHQEQANTIFSLRKD HHHHHHHHHHHHHHH	26.81	22468782
303	Phosphorylation	EQANTIFSLRKDLRQ HHHHHHHHHHHHHHH	24.34	22468782
339	Phosphorylation	LRKDSKMYKDRIEAI HHCCCHHHHHHHHHH	17.30	-
420	Phosphorylation	LRRQQLETLVLSSDL HHHHHHHHHHHCCCC	30.66	25841592
424	Phosphorylation	QLETLVLSSDLEDGS HHHHHHHCCCCCCCC	17.83	28450419
425	Phosphorylation	LETLVLSSDLEDGSP HHHHHHCCCCCCCCC	41.89	22617229
431	Phosphorylation	SSDLEDGSPRRSQEL CCCCCCCCCCCHHCC	27.79	28450419
435	Phosphorylation	EDGSPRRSQELSLPQ CCCCCCCHHCCCCCC	29.32	27251275
439	Phosphorylation	PRRSQELSLPQDLED CCCHHCCCCCCCCCC	36.93	23312004
447	Phosphorylation	LPQDLEDTQLSDKGC CCCCCCCCCCCCCCC	23.26	28348404
450	Phosphorylation	DLEDTQLSDKGCLAG CCCCCCCCCCCCCCC	27.71	22617229
460	Phosphorylation	GCLAGGGSPKQPFAA CCCCCCCCCCCHHHH	32.00	22617229
483	Phosphorylation	NPHDAGLSSGEPPEK CHHHCCCCCCCCCHH	35.07	23186163
484	Phosphorylation	PHDAGLSSGEPPEKE HHHCCCCCCCCCHHH	52.82	23186163
498	Phosphorylation	ERRRLKESFENYRRK HHHHHHHHHHHHHHH	35.95	28450419
502	Phosphorylation	LKESFENYRRKRALR HHHHHHHHHHHHHHH	12.47	30177828
531	Phosphorylation	NTTGSDNTDTEGS-- CCCCCCCCCCCCC--	49.65	17936701
533	Phosphorylation	TGSDNTDTEGS---- CCCCCCCCCCC----	39.96	17936701

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
231	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
531	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
531	T	Phosphorylation	Kinase	CK2	-	Uniprot
533	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
533	T	Phosphorylation	Kinase	CK2	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM62	Q9BVG3	PMID:26488816

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
531	T	Phosphorylation	-
Phosphorylated at Thr-531 and Thr-533 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B.
533	T	Phosphorylation	-
Phosphorylated at Thr-531 and Thr-533 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B.

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 CARD9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCL10_HUMAN	BCL10	physical	11053425
CARD9_HUMAN	CARD9	physical	11053425
VHL_HUMAN	VHL	physical	17936701
CARD9_HUMAN	CARD9	physical	25416956
ZN655_HUMAN	ZNF655	physical	25416956
LENG1_HUMAN	LENG1	physical	25416956
HMBX1_HUMAN	HMBOX1	physical	25416956
F124B_HUMAN	FAM124B	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
F161A_HUMAN	FAM161A	physical	25416956
ZCHC7_HUMAN	ZCCHC7	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
ZN587_HUMAN	ZNF587	physical	25416956
CA094_HUMAN	C1orf94	physical	25416956
PNMA5_HUMAN	PNMA5	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
ZN572_HUMAN	ZNF572	physical	25416956
C19L2_HUMAN	CWF19L2	physical	25416956
ZN417_HUMAN	ZNF417	physical	25416956
C2CD6_HUMAN	ALS2CR11	physical	25416956
TEANC_HUMAN	TCEANC	physical	25416956
PPR18_HUMAN	PPP1R18	physical	25416956
RTP5_HUMAN	RTP5	physical	25416956
CE57L_HUMAN	CEP57L1	physical	25416956
TRI42_HUMAN	TRIM42	physical	25416956
IHO1_HUMAN	CCDC36	physical	25416956
KR101_HUMAN	KRTAP10-1	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
EDC3_HUMAN	EDC3	physical	26186194
CK5P2_HUMAN	CDK5RAP2	physical	26186194
NFRKB_HUMAN	NFRKB	physical	26186194
CP135_HUMAN	CEP135	physical	26186194
TRI62_HUMAN	TRIM62	physical	26488816
CP135_HUMAN	CEP135	physical	28514442
NFRKB_HUMAN	NFRKB	physical	28514442
CK5P2_HUMAN	CDK5RAP2	physical	28514442
EDC3_HUMAN	EDC3	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
212050	Candidiasis, familial, 2 (CANDF2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CARD9_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-460, AND MASSSPECTROMETRY.	18088087 [Abstract]

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