CAR14_HUMAN - dbPTM
CAR14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAR14_HUMAN
UniProt AC Q9BXL6
Protein Name Caspase recruitment domain-containing protein 14
Gene Name CARD14
Organism Homo sapiens (Human).
Sequence Length 1004
Subcellular Localization Isoform 1: Cytoplasm .
Isoform 2: Cytoplasm .
Isoform 3: Cytoplasm .
Protein Description Acts as a scaffolding protein that can activate the inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase signaling pathways. Forms a signaling complex with BCL10 and MALT1, and activates MALT1 proteolytic activity and inflammatory gene expression. MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and p38/JNK MAP kinases. [PubMed: 11278692]
Protein Sequence MGELCRRDSALTALDEETLWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPDVYTLVTGLQPDVDFSNFSGLMETSKLTECLAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQEARTREPCPREKQRLVRMHAICPRDDSDCSLVSSTESQLLSDLSATSSRELVDSFRSSSPAPPSQQSLYKRVAEDFGEEPWSFSSCLEIPEGDPGALPGAKAGDPHLDYELLDTADLPQLESSLQPVSPGRLDVSESGVLMRRRPARRILSQVTMLAFQGDALLEQISVIGGNLTGIFIHRVTPGSAADQMALRPGTQIVMVDYEASEPLFKAVLEDTTLEEAVGLLRRVDGFCCLSVKVNTDGYKRLLQDLEAKVATSGDSFYIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQGCGCWHAHRVNSYTMKDTAAHGTIPNYSRAQQQLIALIQDMTQQCTVTRKPSSGGPQKLVRIVSMDKAKASPLRLSFDRGQLDPSRMEGSSTCFWAESCLTLVPYTLVRPHRPARPRPVLLVPRAVGKILSEKLCLLQGFKKCLAEYLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIHVSVNEKMAKKLKKGLQRLGTSEEQLLEAARQEEGDLDRAPCLYSSLAPDGWSDLDGLLSCVRQAIADEQKKVVWTEQSPR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
9PhosphorylationGELCRRDSALTALDE
CCCCCCCCCCHHCCH		24.3020873877
12PhosphorylationCRRDSALTALDEETL
CCCCCCCHHCCHHHH		25.5427251275
18PhosphorylationLTALDEETLWEMMES
CHHCCHHHHHHHHHH		34.8120873877
60PhosphorylationDEEEVLHSPRLTNSA
CHHHHHCCCCHHCHH		13.9325159151
185PhosphorylationSRMKREVSAHFHEVL
HHHHHHHHHHHHHHH		15.9828348404
227PhosphorylationRSLQEELYLLKQELQ
HHHHHHHHHHHHHHH		17.1722817900
240PhosphorylationLQRANMVSSCELELQ
HHHCCCCCCHHHHHH		20.6422468782
241PhosphorylationQRANMVSSCELELQE
HHCCCCCCHHHHHHH		10.5322468782
250PhosphorylationELELQEQSLRTASDQ
HHHHHHHHHHHHCCC		21.0427251275
253PhosphorylationLQEQSLRTASDQESG
HHHHHHHHHCCCCCC		35.4924732914
255PhosphorylationEQSLRTASDQESGDE
HHHHHHHCCCCCCHH		38.9323663014
259PhosphorylationRTASDQESGDEELNR
HHHCCCCCCHHHHHH		46.0030278072
276PhosphorylationEENEKLRSLTFSLAE
HHHHHHHHHHHHHHH		42.0420873877
278PhosphorylationNEKLRSLTFSLAEKD
HHHHHHHHHHHHHHH		16.6620873877
280PhosphorylationKLRSLTFSLAEKDIL
HHHHHHHHHHHHHHH		22.7920873877
290PhosphorylationEKDILEQSLDEARGS
HHHHHHHHHHHHHCC		28.5423663014
297PhosphorylationSLDEARGSRQELVER
HHHHHHCCHHHHHHH		25.8220873877
307PhosphorylationELVERIHSLRERAVA
HHHHHHHHHHHHHHH		27.1024719451
470PhosphorylationSSRELVDSFRSSSPA
CCHHHHHHHHHCCCC		18.3223663014
473PhosphorylationELVDSFRSSSPAPPS
HHHHHHHHCCCCCCC		32.9123663014
474PhosphorylationLVDSFRSSSPAPPSQ
HHHHHHHCCCCCCCH		35.7623663014
475PhosphorylationVDSFRSSSPAPPSQQ
HHHHHHCCCCCCCHH		26.7430278072
480PhosphorylationSSSPAPPSQQSLYKR
HCCCCCCCHHHHHHH		39.5323663014
483PhosphorylationPAPPSQQSLYKRVAE
CCCCCHHHHHHHHHH		26.4823663014
485PhosphorylationPPSQQSLYKRVAEDF
CCCHHHHHHHHHHHH		11.2923663014
486UbiquitinationPSQQSLYKRVAEDFG
CCHHHHHHHHHHHHC		45.77-
498PhosphorylationDFGEEPWSFSSCLEI
HHCCCCCCCCCCEEC		26.4320873877
500PhosphorylationGEEPWSFSSCLEIPE
CCCCCCCCCCEECCC		18.0225627689
501PhosphorylationEEPWSFSSCLEIPEG
CCCCCCCCCEECCCC		22.2520873877
525PhosphorylationAGDPHLDYELLDTAD
CCCCCCCHHHCCCCC		18.1627642862
539PhosphorylationDLPQLESSLQPVSPG
CCCHHHHHCCCCCCC		22.9628387310
544PhosphorylationESSLQPVSPGRLDVS
HHHCCCCCCCCCCCC		28.4611356195
653PhosphorylationVDGFCCLSVKVNTDG
CCCEEEEEEEECCHH		13.1329083192
658PhosphorylationCLSVKVNTDGYKRLL
EEEEEECCHHHHHHH		33.5129083192
763PhosphorylationCTVTRKPSSGGPQKL
CCEEECCCCCCCCEE		44.6529396449
764PhosphorylationTVTRKPSSGGPQKLV
CEEECCCCCCCCEEE		57.1929396449
775PhosphorylationQKLVRIVSMDKAKAS
CEEEEEEECCHHCCC		20.9224719451
782PhosphorylationSMDKAKASPLRLSFD
ECCHHCCCCCEEEEC		24.6226425664
787PhosphorylationKASPLRLSFDRGQLD
CCCCCEEEECCCCCC		20.7620873877
796PhosphorylationDRGQLDPSRMEGSST
CCCCCCHHHCCCCCC		43.8827499020
842PhosphorylationRAVGKILSEKLCLLQ
CHHHHHHHHHHHHHH		35.8424719451
944PhosphorylationKGLQRLGTSEEQLLE
HHHHHHCCCHHHHHH		37.2428348404
945PhosphorylationGLQRLGTSEEQLLEA
HHHHHCCCHHHHHHH		37.0228348404
1002PhosphorylationKVVWTEQSPR-----
CEEECCCCCC-----		19.1925159151
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 CAR14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAR14_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 CAR14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCL10_HUMANBCL10physical
11278692
RBX2_HUMANRNF7physical
29194363
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
602723Psoriasis 2 (PSORS2)
173200Pityriasis rubra pilaris (PRP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAR14_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND MASSSPECTROMETRY.

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