INAVA_HUMAN - dbPTM
INAVA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INAVA_HUMAN
UniProt AC Q3KP66
Protein Name Innate immunity activator protein {ECO:0000312|HGNC:HGNC:25599}
Gene Name INAVA {ECO:0000312|HGNC:HGNC:25599}
Organism Homo sapiens (Human).
Sequence Length 663
Subcellular Localization Nucleus . Cytoplasm . Translocates to the nucleus upon NOD2 stimulation.
Protein Description Expressed in peripheral macrophages and intestinal myeloid-derived cells, is required for optimal PRR (pattern recognition receptor)-induced signaling, cytokine secretion, and bacterial clearance. Upon stimulation of a broad range of PRRs (pattern recognition receptor) such as NOD2 or TLR2, TLR3, TLR4, TLR5, TLR7 and TLR9, associates with YWHAQ/14-3-3T, which in turn leads to the recruitment and activation of MAP kinases and NF-kappa-B signaling complexes that amplifies PRR-induced downstream signals and cytokine secretion. [PubMed: 28436939 In the intestine, regulates adherens junction stability by regulating the degradation of CYTH1 and CYTH2, probably acting as substrate cofactor for SCF E3 ubiquitin-protein ligase complexes. Stabilizes adherens junctions by limiting CYTH1-dependent ARF6 activation]
Protein Sequence MLQMPKLNEIPPGRAGRREARGEGRWPGQTGPEAARLEWRAQGQAGGARAPWDSWGSSRLPTQPGPGWSRCPPSLLCALSFQKSTMESKDEVSDTDSGIILQSGPDSPVSPMKELTHAVHKQQRALEARLEACLEELRRLCLREAELTGTLPAEYPLKPGEKAPKVRRRIGAAYKLDDWALHREDPLSSLERQLALQLQITEAARRLCLEENLSRQARRQRKHSMLQEEKKLQELQRCLVERRRNSEPPPAAALPLGRELSASDDSSLSDGLLLEEEESQVPKPPPESPAPPSRPLPPQTLEGLQPTGPEAGSPERAPVQNSPWKETSLDHPYEKPRKSSEPWSESSSPATTPQDGPSASSLWLLEPASYHVVPIRGVPGQWQGRTSAPATPEIQGRRGQSQSLRVDSFRAGPEGRGRSAFPRRRPTHYTVTVPDSCFPATKPPLPHAACHSCSEDSGSDVSSISHPTSPGSSSPDISFLQPLSPPKTHRHRGAWVPAGSRELVAHHPKLLLPPGYFPAGRYVVVAESPLPPGEWELRRAAPGPAYEEEGTPLRYQRLVPSRSRIVRTPSLKDSPAGRGLSKAAVSEELKWWHERARLRSTRPHSLDRQGAFRVRSLPLGREGFGRALGPRAQVPTVCVLRRSPDGAPVQVFVPEKGEIISQV
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
36UbiquitinationQTGPEAARLEWRAQG
CCCHHHHHHHHHHCC		33845483
85PhosphorylationALSFQKSTMESKDEV
HHHCCCCCCCCCCCC		24719451
88PhosphorylationFQKSTMESKDEVSDT
CCCCCCCCCCCCCCC		24719451
93PhosphorylationMESKDEVSDTDSGII
CCCCCCCCCCCCCEE		28348404
95PhosphorylationSKDEVSDTDSGIILQ
CCCCCCCCCCCEEEE		28348404
97PhosphorylationDEVSDTDSGIILQSG
CCCCCCCCCEEEECC		28348404
103PhosphorylationDSGIILQSGPDSPVS
CCCEEEECCCCCCCC		26657352
107PhosphorylationILQSGPDSPVSPMKE
EEECCCCCCCCCHHH		26657352
116PhosphorylationVSPMKELTHAVHKQQ
CCCHHHHHHHHHHHH		-
121PhosphorylationELTHAVHKQQRALEA
HHHHHHHHHHHHHHH		27251275
188PhosphorylationLHREDPLSSLERQLA
HCCCCCCHHHHHHHH		24719451
224PhosphorylationARRQRKHSMLQEEKK
HHHHHHHHHHHHHHH		28102081
238PhosphorylationKLQELQRCLVERRRN
HHHHHHHHHHHHHHC		27251275
246PhosphorylationLVERRRNSEPPPAAA
HHHHHHCCCCCCCCC		26657352
260PhosphorylationALPLGRELSASDDSS
CCCCCCCCCCCCCCC		27251275
307PhosphorylationTLEGLQPTGPEAGSP
HHCCCCCCCCCCCCC		25850435
313PhosphorylationPTGPEAGSPERAPVQ
CCCCCCCCCCCCCCC		25850435
327PhosphorylationQNSPWKETSLDHPYE
CCCCCCCCCCCCCCC		21945579
328PhosphorylationNSPWKETSLDHPYEK
CCCCCCCCCCCCCCC		21945579
333PhosphorylationETSLDHPYEKPRKSS
CCCCCCCCCCCCCCC		21945579
339PhosphorylationPYEKPRKSSEPWSES
CCCCCCCCCCCCCCC		23090842
340PhosphorylationYEKPRKSSEPWSESS
CCCCCCCCCCCCCCC		23090842
344PhosphorylationRKSSEPWSESSSPAT
CCCCCCCCCCCCCCC		23090842
346PhosphorylationSSEPWSESSSPATTP
CCCCCCCCCCCCCCC		23090842
347PhosphorylationSEPWSESSSPATTPQ
CCCCCCCCCCCCCCC		23090842
348PhosphorylationEPWSESSSPATTPQD
CCCCCCCCCCCCCCC		23090842
351PhosphorylationSESSSPATTPQDGPS
CCCCCCCCCCCCCCC		23090842
352PhosphorylationESSSPATTPQDGPSA
CCCCCCCCCCCCCCC		23090842
369PhosphorylationLWLLEPASYHVVPIR
EEEECCCEEEEEECC		-
370PhosphorylationWLLEPASYHVVPIRG
EEECCCEEEEEECCC		22817900
384PhosphorylationGVPGQWQGRTSAPAT
CCCCCCCCCCCCCCC		-
386PhosphorylationPGQWQGRTSAPATPE
CCCCCCCCCCCCCHH		25850435
387PhosphorylationGQWQGRTSAPATPEI
CCCCCCCCCCCCHHC		29496963
391PhosphorylationGRTSAPATPEIQGRR
CCCCCCCCHHCCCCC		28985074
401PhosphorylationIQGRRGQSQSLRVDS
CCCCCCCCCCCCCEE		28102081
403PhosphorylationGRRGQSQSLRVDSFR
CCCCCCCCCCCEEEC		28348404
405PhosphorylationRGQSQSLRVDSFRAG
CCCCCCCCCEEECCC		-
408PhosphorylationSQSLRVDSFRAGPEG
CCCCCCEEECCCCCC		26670566
422PhosphorylationGRGRSAFPRRRPTHY
CCCCCCCCCCCCCEE		-
484PhosphorylationISFLQPLSPPKTHRH
CCCCCCCCCCCCCCC		24719451
497UbiquitinationRHRGAWVPAGSRELV
CCCCCEECCCCHHHH		33845483
516PhosphorylationKLLLPPGYFPAGRYV
CCCCCCCCCCCCCEE		27642862
546PhosphorylationRAAPGPAYEEEGTPL
ECCCCCCCCCCCCCC		27642862
551PhosphorylationPAYEEEGTPLRYQRL
CCCCCCCCCCCEEEE		-
555PhosphorylationEEGTPLRYQRLVPSR
CCCCCCCEEEECCCC		-
563PhosphorylationQRLVPSRSRIVRTPS
EEECCCCCCEEECCC		-
568PhosphorylationSRSRIVRTPSLKDSP
CCCCEEECCCCCCCC		28102081
570PhosphorylationSRIVRTPSLKDSPAG
CCEEECCCCCCCCCC		25106551
574PhosphorylationRTPSLKDSPAGRGLS
ECCCCCCCCCCCCCC		27794612
578MethylationLKDSPAGRGLSKAAV
CCCCCCCCCCCHHHH		-
581O-linked_GlycosylationSPAGRGLSKAAVSEE
CCCCCCCCHHHHHHH		30379171
584PhosphorylationGRGLSKAAVSEELKW
CCCCCHHHHHHHHHH		-
586PhosphorylationGLSKAAVSEELKWWH
CCCHHHHHHHHHHHH		28348404
592MethylationVSEELKWWHERARLR
HHHHHHHHHHHHHHH		-
600PhosphorylationHERARLRSTRPHSLD
HHHHHHHCCCCCCCC		23312004
601PhosphorylationERARLRSTRPHSLDR
HHHHHHCCCCCCCCC		23312004
605PhosphorylationLRSTRPHSLDRQGAF
HHCCCCCCCCCCCCE		29743597
616PhosphorylationQGAFRVRSLPLGREG
CCCEEEEECCCCCCC		25106551
619PhosphorylationFRVRSLPLGREGFGR
EEEEECCCCCCCCHH		27251275
630PhosphorylationGFGRALGPRAQVPTV
CCHHHCCCCCCCCEE		27251275
636PhosphorylationGPRAQVPTVCVLRRS
CCCCCCCEEEEEEEC		28102081
643PhosphorylationTVCVLRRSPDGAPVQ
EEEEEEECCCCCCEE		28355574
657PhosphorylationQVFVPEKGEIISQV-
EEEECCCCCEEECC-		27251275
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 INAVA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INAVA_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 INAVA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYH2_HUMANCYTH2physical
28514442
CACO2_HUMANCALCOCO2physical
28514442
CYH1_HUMANCYTH1physical
28514442
CYH3_HUMANCYTH3physical
28514442
P2R3B_HUMANPPP2R3Bphysical
28514442
TX1B3_HUMANTAX1BP3physical
28514442
DCTN5_HUMANDCTN5physical
28514442
CRTAP_HUMANCRTAPphysical
28514442
DCTN6_HUMANDCTN6physical
28514442
CE170_HUMANCEP170physical
28514442
SGF29_HUMANCCDC101physical
28514442
P3H1_HUMANP3H1physical
28514442
ARP10_HUMANACTR10physical
28514442
ARHG7_HUMANARHGEF7physical
28514442
DCTN1_HUMANDCTN1physical
28514442
DCTN2_HUMANDCTN2physical
28514442
DCAF8_HUMANDCAF8physical
28514442
SMCA1_HUMANSMARCA1physical
28514442
GRN_HUMANGRNphysical
28514442
DCTN3_HUMANDCTN3physical
28514442
TRI27_HUMANTRIM27physical
28514442
ACTZ_HUMANACTR1Aphysical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INAVA_HUMAN

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Related Literatures of Post-Translational Modification

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