HERC5_HUMAN - dbPTM
HERC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HERC5_HUMAN
UniProt AC Q9UII4
Protein Name E3 ISG15--protein ligase HERC5
Gene Name HERC5
Organism Homo sapiens (Human).
Sequence Length 1024
Subcellular Localization Cytoplasm, perinuclear region . Associated with the polyribosomes, probably via the 60S subunit.
Protein Description Major E3 ligase for ISG15 conjugation. Acts as a positive regulator of innate antiviral response in cells induced by interferon. Functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner. Catalyzes ISGylation of IRF3 which results in sustained activation, it attenuates IRF3-PIN1 interaction, which antagonizes IRF3 ubiquitination and degradation, and boosts the antiviral response. Catalyzes ISGylation of influenza A viral NS1 which attenuates virulence; ISGylated NS1 fails to form homodimers and thus to interact with its RNA targets. Catalyzes ISGylation of papillomavirus type 16 L1 protein which results in dominant-negative effect on virus infectivity. Physically associated with polyribosomes, broadly modifies newly synthesized proteins in a cotranslational manner. In an interferon-stimulated cell, newly translated viral proteins are primary targets of ISG15..
Protein Sequence MERRSRRKSRRNGRSTAGKAAATQPAKSPGAQLWLFPSAAGLHRALLRRVEVTRQLCCSPGRLAVLERGGAGVQVHQLLAGSGGARTPKCIKLGKNMKIHSVDQGAEHMLILSSDGKPFEYDNYSMKHLRFESILQEKKIIQITCGDYHSLALSKGGELFAWGQNLHGQLGVGRKFPSTTTPQIVEHLAGVPLAQISAGEAHSMALSMSGNIYSWGKNECGQLGLGHTESKDDPSLIEGLDNQKVEFVACGGSHSALLTQDGLLFTFGAGKHGQLGHNSTQNELRPCLVAELVGYRVTQIACGRWHTLAYVSDLGKVFSFGSGKDGQLGNGGTRDQLMPLPVKVSSSEELKLESHTSEKELIMIAGGNQSILLWIKKENSYVNLKRTIPTLNEGTVKRWIADVETKRWQSTKREIQEIFSSPACLTGSFLRKRRTTEMMPVYLDLNKARNIFKELTQKDWITNMITTCLKDNLLKRLPFHSPPQEALEIFFLLPECPMMHISNNWESLVVPFAKVVCKMSDQSSLVLEEYWATLQESTFSKLVQMFKTAVICQLDYWDESAEENGNVQALLEMLKKLHRVNQVKCQLPESIFQVDELLHRLNFFVEVCRRYLWKMTVDASENVQCCVIFSHFPFIFNNLSKIKLLHTDTLLKIESKKHKAYLRSAAIEEERESEFALRPTFDLTVRRNHLIEDVLNQLSQFENEDLRKELWVSFSGEIGYDLGGVKKEFFYCLFAEMIQPEYGMFMYPEGASCMWFPVKPKFEKKRYFFFGVLCGLSLFNCNVANLPFPLALFKKLLDQMPSLEDLKELSPDLGKNLQTLLDDEGDNFEEVFYIHFNVHWDRNDTNLIPNGSSITVNQTNKRDYVSKYINYIFNDSVKAVYEEFRRGFYKMCDEDIIKLFHPEELKDVIVGNTDYDWKTFEKNARYEPGYNSSHPTIVMFWKAFHKLTLEEKKKFLVFLTGTDRLQMKDLNNMKITFCCPESWNERDPIRALTCFSVLFLPKYSTMETVEEALQEAINNNRGFG
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
19UbiquitinationNGRSTAGKAAATQPA
CCCCCCHHHHCCCCC		32.18-
27UbiquitinationAAATQPAKSPGAQLW
HHCCCCCCCCCCEEE		64.9621890473
27UbiquitinationAAATQPAKSPGAQLW
HHCCCCCCCCCCEEE		64.9621890473
27UbiquitinationAAATQPAKSPGAQLW
HHCCCCCCCCCCEEE		64.9621890473
28PhosphorylationAATQPAKSPGAQLWL
HCCCCCCCCCCEEEE		30.5822777824
117UbiquitinationLILSSDGKPFEYDNY
EEECCCCCCCCCCCC		52.07-
127UbiquitinationEYDNYSMKHLRFESI
CCCCCCCHHHHHHHH		33.28-
138UbiquitinationFESILQEKKIIQITC
HHHHHCCCCEEEEEC		35.99-
231UbiquitinationGLGHTESKDDPSLIE
CCCCCCCCCCHHHCC		60.98-
324UbiquitinationVFSFGSGKDGQLGNG
EEEECCCCCCCCCCC		61.45-
357O-linked_GlycosylationLKLESHTSEKELIMI
EECCCCCCCCEEEEE		41.0530379171
370PhosphorylationMIAGGNQSILLWIKK
EEECCCEEEEEEEEE		21.14-
377UbiquitinationSILLWIKKENSYVNL
EEEEEEEECCCCEEE		53.66-
385UbiquitinationENSYVNLKRTIPTLN
CCCCEEEEEEECCCC		42.14-
397UbiquitinationTLNEGTVKRWIADVE
CCCCCHHHHHHHHHH		41.68-
406UbiquitinationWIADVETKRWQSTKR
HHHHHHHHHHHHCHH		37.83-
447UbiquitinationPVYLDLNKARNIFKE
EEEECHHHHHHHHHH		56.89-
453UbiquitinationNKARNIFKELTQKDW
HHHHHHHHHHHHHHH		48.28-
458UbiquitinationIFKELTQKDWITNMI
HHHHHHHHHHHHHHH		50.20-
502PhosphorylationECPMMHISNNWESLV
CCCCCEECCCHHHHH		14.9426657352
541SumoylationLQESTFSKLVQMFKT
HHHHHHHHHHHHHHH		48.78-
643UbiquitinationFNNLSKIKLLHTDTL
HCCCCCCEEEECCCE		49.05-
652UbiquitinationLHTDTLLKIESKKHK
EECCCEEHHCCHHHH		47.76-
661PhosphorylationESKKHKAYLRSAAIE
CCHHHHHHHHHHHHH		13.8822210691
673PhosphorylationAIEEERESEFALRPT
HHHHHHHHHCCCCCC		44.2122210691
684PhosphorylationLRPTFDLTVRRNHLI
CCCCEECCHHCCHHH		17.5122210691
795UbiquitinationFPLALFKKLLDQMPS
CCHHHHHHHHHCCCC		47.12-
802PhosphorylationKLLDQMPSLEDLKEL
HHHHCCCCHHHHHHH		38.7622210691
807UbiquitinationMPSLEDLKELSPDLG
CCCHHHHHHHCCCHH		69.77-
810PhosphorylationLEDLKELSPDLGKNL
HHHHHHHCCCHHHHH		19.9122496350
867UbiquitinationNKRDYVSKYINYIFN
CCHHHHHHHHHHHCC		39.85-
868PhosphorylationKRDYVSKYINYIFND
CHHHHHHHHHHHCCH		6.2118452278
871PhosphorylationYVSKYINYIFNDSVK
HHHHHHHHHCCHHHH		9.4218452278
890UbiquitinationEFRRGFYKMCDEDII
HHHHHHHHHCCHHHH		30.69-
898UbiquitinationMCDEDIIKLFHPEEL
HCCHHHHHHCCHHHH		45.49-
906UbiquitinationLFHPEELKDVIVGNT
HCCHHHHCCEEECCC		53.91-
918UbiquitinationGNTDYDWKTFEKNAR
CCCCCCHHHHHHHCC		40.20-
946UbiquitinationMFWKAFHKLTLEEKK
HHHHHHHHCCHHHHH		36.39-
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 HERC5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HERC5_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 HERC5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNA2_HUMANCCNA2physical
10581175
CCNE1_HUMANCCNE1physical
10581175
CCNB1_HUMANCCNB1physical
10581175
CCND1_HUMANCCND1physical
10581175
CDN1A_HUMANCDKN1Aphysical
10581175
NDKB_HUMANNME2physical
18535780
ERCC2_HUMANERCC2physical
16884686
STK38_HUMANSTK38physical
16884686
PITX2_HUMANPITX2physical
16884686
HERC5_HUMANHERC5physical
15331633
IRF3_HUMANIRF3physical
20308324
ISG15_HUMANISG15physical
16815975
HSP7C_HUMANHSPA8physical
16815975
TRXR1_HUMANTXNRD1physical
16815975
UB2D1_HUMANUBE2D1physical
15331633
SMAD4_HUMANSMAD4physical
12202226
ISG15_HUMANISG15physical
24693865
UB2L6_HUMANUBE2L6physical
20308324
P53_HUMANTP53physical
25071020
BECN1_HUMANBECN1physical
25906440
VIRF1_HHV8PvIRF-1physical
26355087
CTNB1_HUMANCTNNB1physical
28744352
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 HERC5_HUMAN

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Related Literatures of Post-Translational Modification

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