dbPTM

CAR11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAR11_MOUSE
UniProt AC	Q8CIS0
Protein Name	Caspase recruitment domain-containing protein 11
Gene Name	Card11
Organism	Mus musculus (Mouse).
Sequence Length	1159
Subcellular Localization	Cytoplasm . Membrane raft . Colocalized with DPP4 in membrane rafts.
Protein Description	Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. [PubMed: 12356734]
Protein Sequence	MPGGGPAMDDYMETLKDEEEALWDNVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPELYKLVTGKEPTRRFSTIVVEEGHEGLTHFLMNEVIKLQQQVKAKDLQRCELLAKSRQLEDEKKQLSLIRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPRKEQVLELERENEMLKTKIQELQSIIQAGKRSLPDSDKAILDILEHDRKEALEDRQELVNKIYNLQEEVRQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDNGSLDQSLPRHLPATIISQNLGDTSPRTNGQEADDSSTSEESPEDSKYFLPYHPPRRRMNLKGIQLQRAKSPISMKQASEFQALMRTVKGHEEDFTDGSPSSSRSLPVTSSFSKMQPHRSRSSIMSITAEPPGNDSIVRRCKEDAPHRSTVEEDNDSCGFDALDLDDENHERYSFGPPSIHSSSSSHQSEGLDAYDLEQVNLMLRKFSLERPFRPSVTSGGHVRGTGPLVQHTTLNGDGLITQLTLLGGNARGSFIHSVKPGSLAERAGLREGHQLLLLEGCIRGERQSVPLDACTKEEARWTIQRCSGLITLHYKVNHEGYRKLLKEMEDGLITSGDSFYIRLNLNISSQLDACSMSLKCDDVVHVLDTMYQDRHEWLCARVDPFTDQDLDTGTIPSYSRAQQLLLVKLQRLVHRGNREEADSAHHTLRSLRNTLQPEEMLSTSDPRVSPRLSRASFFFGQLLQFVSRSENKYKRMNSNERVRIISGSPLGSLSRSSLDATKLLTEKHEELDPENELSRNLTLIPYSLVRAFHCERRRPVLFTPTMLAKTLVQKLLNSGGAMEFTICKSDIVTRDEFLRKQKTETIIYSREKNPNTFECIVPANIEAVAAKNKHCLLEAGIGCVRDLIKCKVYPIVLLIRVSEKNIKRFRKLLPRPETEEEFLRVCRLKEKELEALPCLYATVEAEMWSSVEELLRVLKDKIVEEQRKTIWVDEDQL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
116	Phosphorylation	KEPTRRFSTIVVEEG CCCCCCEEEEEEECC	18.53	27600695
221	Dimethylation	EKNMAVMRSRDLQLE HHCHHHHHHHHHHHH	23.18	-
439	Phosphorylation	ESKLRRLSKDNGSLD HHHHHHHHCCCCCCC	35.83	29176673
444	Phosphorylation	RLSKDNGSLDQSLPR HHHCCCCCCCCCCCC	34.72	24704852
448	Phosphorylation	DNGSLDQSLPRHLPA CCCCCCCCCCCCCCC	39.75	29176673
459	Phosphorylation	HLPATIISQNLGDTS CCCCEEHHCCCCCCC	14.79	28285833
465	Phosphorylation	ISQNLGDTSPRTNGQ HHCCCCCCCCCCCCC	38.54	28833060
466	Phosphorylation	SQNLGDTSPRTNGQE HCCCCCCCCCCCCCC	19.68	22942356
512 (in isoform 2)	Phosphorylation	-	26.87	27566939
512	Phosphorylation	IQLQRAKSPISMKQA HHCCCCCCCCCHHHH	26.87	25266776
537	Phosphorylation	KGHEEDFTDGSPSSS CCCHHHCCCCCCCCC	52.34	30635358
540	Phosphorylation	EEDFTDGSPSSSRSL HHHCCCCCCCCCCCC	25.15	24704852
542	Phosphorylation	DFTDGSPSSSRSLPV HCCCCCCCCCCCCCC	42.51	30635358
543	Phosphorylation	FTDGSPSSSRSLPVT CCCCCCCCCCCCCCC	32.91	30635358
544	Phosphorylation	TDGSPSSSRSLPVTS CCCCCCCCCCCCCCC	30.17	30635358
545	Phosphorylation	DGSPSSSRSLPVTSS CCCCCCCCCCCCCCC	44.13	24719451
546	Phosphorylation	GSPSSSRSLPVTSSF CCCCCCCCCCCCCCC	38.69	28833060
550	Phosphorylation	SSRSLPVTSSFSKMQ CCCCCCCCCCCCCCC	19.40	28833060
551	Phosphorylation	SRSLPVTSSFSKMQP CCCCCCCCCCCCCCC	29.62	28833060
552	Phosphorylation	RSLPVTSSFSKMQPH CCCCCCCCCCCCCCC	24.95	28833060
554	Phosphorylation	LPVTSSFSKMQPHRS CCCCCCCCCCCCCCC	29.21	28833060
561	Phosphorylation	SKMQPHRSRSSIMSI CCCCCCCCCCCCEEE	33.22	28285833
563	Phosphorylation	MQPHRSRSSIMSITA CCCCCCCCCCEEEEC	26.01	27600695
564	Phosphorylation	QPHRSRSSIMSITAE CCCCCCCCCEEEECC	22.62	16356855
569	Phosphorylation	RSSIMSITAEPPGND CCCCEEEECCCCCCC	20.05	21454597
598	Phosphorylation	TVEEDNDSCGFDALD CCCCCCCCCCCCCCC	23.53	28833060
620	Phosphorylation	RYSFGPPSIHSSSSS CCCCCCCCCCCCCCC	35.75	-
644	Phosphorylation	DLEQVNLMLRKFSLE CHHHHHHHHHHHCCC	2.61	24719451
649	Phosphorylation	NLMLRKFSLERPFRP HHHHHHHCCCCCCCC	32.15	21183079
657	Phosphorylation	LERPFRPSVTSGGHV CCCCCCCCCCCCCCC	33.50	16356855
884	Phosphorylation	LQPEEMLSTSDPRVS CCHHHHHCCCCCCCC	25.26	30635358
885	Phosphorylation	QPEEMLSTSDPRVSP CHHHHHCCCCCCCCH	32.94	30635358
886	Phosphorylation	PEEMLSTSDPRVSPR HHHHHCCCCCCCCHH	42.09	24719451
891	Phosphorylation	STSDPRVSPRLSRAS CCCCCCCCHHHHHHH	12.94	25266776
928	Phosphorylation	NERVRIISGSPLGSL CCCEEEEECCCCCCC	30.74	29176673
930	Phosphorylation	RVRIISGSPLGSLSR CEEEEECCCCCCCCH	15.34	24704852
937	Methylation	SPLGSLSRSSLDATK CCCCCCCHHHCHHHH	35.24	-
939	Phosphorylation	LGSLSRSSLDATKLL CCCCCHHHCHHHHHH	29.20	25266776
943	Phosphorylation	SRSSLDATKLLTEKH CHHHCHHHHHHHHHH	23.15	25266776
969	Phosphorylation	NLTLIPYSLVRAFHC CCEECCHHHHHHHCC	18.29	28973931
1084	Phosphorylation	IVLLIRVSEKNIKRF EEEEEEECHHHHHHH	32.76	-

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
564	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
564	S	Phosphorylation	Kinase	PRKCB	P68404	Uniprot
564	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
564	S	Phosphorylation	Kinase	PRKCQ	Q02111	Uniprot
649	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
649	S	Phosphorylation	Kinase	PRKCB	P68404	Uniprot
649	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
649	S	Phosphorylation	Kinase	PRKCQ	Q02111	Uniprot
657	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
657	S	Phosphorylation	Kinase	PRKCB	P68404	Uniprot
657	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
657	S	Phosphorylation	Kinase	PRKCQ	Q02111	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
564	S	Phosphorylation	16356855
Phosphorylation at Ser-564, Ser-649 and Ser-657 by PRKCB and PRKCQ leads to a shift from an inactive to an active form that activates the NF-kappa-B signaling.
649	S	Phosphorylation	16356855
Phosphorylation at Ser-564, Ser-649 and Ser-657 by PRKCB and PRKCQ leads to a shift from an inactive to an active form that activates the NF-kappa-B signaling.
657	S	Phosphorylation	16356855
Phosphorylation at Ser-564, Ser-649 and Ser-657 by PRKCB and PRKCQ leads to a shift from an inactive to an active form that activates the NF-kappa-B signaling.

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 CAR11_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
M3K7_MOUSE	Map3k7	physical	16301747
KC1A_HUMAN	CSNK1A1	physical	19118383

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CAR11_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of the CARMA1 linker controls NF-kappaB activation."; Sommer K., Guo B., Pomerantz J.L., Bandaranayake A.D.,Moreno-Garcia M.E., Ovechkina Y.L., Rawlings D.J.; Immunity 23:561-574(2005). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-564; SER-649 AND SER-657.	16356855 [Abstract]

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