AZI2_HUMAN - dbPTM
AZI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AZI2_HUMAN
UniProt AC Q9H6S1
Protein Name 5-azacytidine-induced protein 2
Gene Name AZI2
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization Cytoplasm .
Protein Description Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1..
Protein Sequence MDALVEDDICILNHEKAHKRDTVTPVSIYSGDESVASHFALVTAYEDIKKRLKDSEKENSLLKKRIRFLEEKLIARFEEETSSVGREQVNKAYHAYREVCIDRDNLKSKLDKMNKDNSESLKVLNEQLQSKEVELLQLRTEVETQQVMRNLNPPSSNWEVEKLSCDLKIHGLEQELELMRKECSDLKIELQKAKQTDPYQEDNLKSRDLQKLSISSDNMQHAYWELKREMSNLHLVTQVQAELLRKLKTSTAIKKACAPVGCSEDLGRDSTKLHLMNFTATYTRHPPLLPNGKALCHTTSSPLPGDVKVLSEKAILQSWTDNERSIPNDGTCFQEHSSYGRNSLEDNSWVFPSPPKSSETAFGETKTKTLPLPNLPPLHYLDQHNQNCLYKN
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
19UbiquitinationLNHEKAHKRDTVTPV
CCCHHHCCCCCCCCE		57.7529967540
24PhosphorylationAHKRDTVTPVSIYSG
HCCCCCCCCEEEECC		21.7719060867
50UbiquitinationTAYEDIKKRLKDSEK
HHHHHHHHHCCCHHH		64.4029967540
60PhosphorylationKDSEKENSLLKKRIR
CCHHHHHHHHHHHHH		35.8524719451
63UbiquitinationEKENSLLKKRIRFLE
HHHHHHHHHHHHHHH		45.3524816145
66UbiquitinationNSLLKKRIRFLEEKL
HHHHHHHHHHHHHHH		5.1224816145
80UbiquitinationLIARFEEETSSVGRE
HHHHHHHHHCCCCHH		46.9529967540
81PhosphorylationIARFEEETSSVGREQ
HHHHHHHHCCCCHHH		29.5828857561
82PhosphorylationARFEEETSSVGREQV
HHHHHHHCCCCHHHH		26.7218691976
83PhosphorylationRFEEETSSVGREQVN
HHHHHHCCCCHHHHH		35.6928857561
91UbiquitinationVGREQVNKAYHAYRE
CCHHHHHHHHHHHHH		52.0129967540
93UbiquitinationREQVNKAYHAYREVC
HHHHHHHHHHHHHHH		6.6522817900
118PhosphorylationDKMNKDNSESLKVLN
HHHCCCCHHHHHHHH		38.4030619164
120PhosphorylationMNKDNSESLKVLNEQ
HCCCCHHHHHHHHHH		33.0528857561
122UbiquitinationKDNSESLKVLNEQLQ
CCCHHHHHHHHHHHH		54.6929967540
130PhosphorylationVLNEQLQSKEVELLQ
HHHHHHHHCHHHHHH		39.1027499020
131UbiquitinationLNEQLQSKEVELLQL
HHHHHHHCHHHHHHH		53.4729967540
140PhosphorylationVELLQLRTEVETQQV
HHHHHHHHHHHHHHH		53.64-
143UbiquitinationLQLRTEVETQQVMRN
HHHHHHHHHHHHHHH		34.3729967540
144PhosphorylationQLRTEVETQQVMRNL
HHHHHHHHHHHHHHC		29.49-
148SulfoxidationEVETQQVMRNLNPPS
HHHHHHHHHHCCCCC		1.7221406390
155PhosphorylationMRNLNPPSSNWEVEK
HHHCCCCCCCCCCEE		37.2428348404
156PhosphorylationRNLNPPSSNWEVEKL
HHCCCCCCCCCCEEH		52.3028348404
162UbiquitinationSSNWEVEKLSCDLKI
CCCCCCEEHHHCEEE		51.3729967540
164PhosphorylationNWEVEKLSCDLKIHG
CCCCEEHHHCEEECC		19.36-
181UbiquitinationQELELMRKECSDLKI
HHHHHHHHHHHHHHH		49.4629967540
192UbiquitinationDLKIELQKAKQTDPY
HHHHHHHHHHCCCCC		70.9029967540
194UbiquitinationKIELQKAKQTDPYQE
HHHHHHHHCCCCCCC		61.85-
196UbiquitinationELQKAKQTDPYQEDN
HHHHHHCCCCCCCCC		37.9322817900
201UbiquitinationKQTDPYQEDNLKSRD
HCCCCCCCCCCCCCC		42.9222817900
205 (in isoform 1)Ubiquitination-50.1021906983
205UbiquitinationPYQEDNLKSRDLQKL
CCCCCCCCCCCHHHH		50.1021906983
205 (in isoform 3)Ubiquitination-50.1021906983
208UbiquitinationEDNLKSRDLQKLSIS
CCCCCCCCHHHHCCC		61.6222817900
213PhosphorylationSRDLQKLSISSDNMQ
CCCHHHHCCCCCHHH		27.7124275569
244UbiquitinationTQVQAELLRKLKTST
HHHHHHHHHHHCCCH		3.2329967540
249PhosphorylationELLRKLKTSTAIKKA
HHHHHHCCCHHHHHH		41.57-
250PhosphorylationLLRKLKTSTAIKKAC
HHHHHCCCHHHHHHC		17.79-
251PhosphorylationLRKLKTSTAIKKACA
HHHHCCCHHHHHHCC		37.32-
255UbiquitinationKTSTAIKKACAPVGC
CCCHHHHHHCCCCCC		42.4529967540
263PhosphorylationACAPVGCSEDLGRDS
HCCCCCCCCHHCCCC		28.37-
270PhosphorylationSEDLGRDSTKLHLMN
CCHHCCCCCEEEEEE		26.5327251275
293UbiquitinationPPLLPNGKALCHTTS
CCCCCCCCEECCCCC		44.8429967540
298PhosphorylationNGKALCHTTSSPLPG
CCCEECCCCCCCCCC		27.6328450419
299PhosphorylationGKALCHTTSSPLPGD
CCEECCCCCCCCCCC		11.9825159151
300PhosphorylationKALCHTTSSPLPGDV
CEECCCCCCCCCCCC		30.9825159151
301PhosphorylationALCHTTSSPLPGDVK
EECCCCCCCCCCCCE		28.5025159151
308UbiquitinationSPLPGDVKVLSEKAI
CCCCCCCEEECHHHH		42.0522817900
311PhosphorylationPGDVKVLSEKAILQS
CCCCEEECHHHHHHH		39.7928634298
311UbiquitinationPGDVKVLSEKAILQS
CCCCEEECHHHHHHH		39.7922817900
313UbiquitinationDVKVLSEKAILQSWT
CCEEECHHHHHHHCC		37.0322817900
313 (in isoform 1)Ubiquitination-37.0321906983
316UbiquitinationVLSEKAILQSWTDNE
EECHHHHHHHCCCCC		3.8422817900
318PhosphorylationSEKAILQSWTDNERS
CHHHHHHHCCCCCCC		28.6223927012
320PhosphorylationKAILQSWTDNERSIP
HHHHHHCCCCCCCCC		33.9128450419
325PhosphorylationSWTDNERSIPNDGTC
HCCCCCCCCCCCCCC		35.9027251275
331PhosphorylationRSIPNDGTCFQEHSS
CCCCCCCCCCCCCCC		17.0128348404
337PhosphorylationGTCFQEHSSYGRNSL
CCCCCCCCCCCCCCC		25.2228348404
338PhosphorylationTCFQEHSSYGRNSLE
CCCCCCCCCCCCCCC		33.2527251275
339PhosphorylationCFQEHSSYGRNSLED
CCCCCCCCCCCCCCC		24.1028348404
343PhosphorylationHSSYGRNSLEDNSWV
CCCCCCCCCCCCCEE		31.6025850435
348PhosphorylationRNSLEDNSWVFPSPP
CCCCCCCCEECCCCC		36.6230266825
353PhosphorylationDNSWVFPSPPKSSET
CCCEECCCCCCCCCC		42.2330266825
356UbiquitinationWVFPSPPKSSETAFG
EECCCCCCCCCCCCC		70.7429967540
357PhosphorylationVFPSPPKSSETAFGE
ECCCCCCCCCCCCCC		38.9025159151
358PhosphorylationFPSPPKSSETAFGET
CCCCCCCCCCCCCCC		45.1326852163
360PhosphorylationSPPKSSETAFGETKT
CCCCCCCCCCCCCCC		29.2726852163
365PhosphorylationSETAFGETKTKTLPL
CCCCCCCCCCEEECC		44.3826852163
366UbiquitinationETAFGETKTKTLPLP
CCCCCCCCCEEECCC		43.66-
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 AZI2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AZI2_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 AZI2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIB1_HUMANMIB1physical
21903422
APBA3_HUMANAPBA3physical
21903422
CACO2_HUMANCALCOCO2physical
21903422
IKKE_HUMANIKBKEphysical
21903422
PAPD1_HUMANMTPAPphysical
21903422
N4BP1_HUMANN4BP1physical
21903422
RNF31_HUMANRNF31physical
21903422
TBK1_HUMANTBK1physical
21903422
TRAF3_HUMANTRAF3physical
21903422
TXLNA_HUMANTXLNAphysical
21903422
TXLNG_HUMANTXLNGphysical
21903422
TBK1_HUMANTBK1physical
14560022
IKKE_HUMANIKBKEphysical
17568778
TBK1_HUMANTBK1physical
17568778
TBKB1_HUMANTBKBP1physical
17568778
AZI2_HUMANAZI2physical
17568778
TRI38_HUMANTRIM38physical
22539786
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 AZI2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; THR-81; SER-82;THR-299; SER-300; SER-318; SER-348; SER-353 AND SER-357, AND MASSSPECTROMETRY.

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