HOIL1_HUMAN - dbPTM
HOIL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HOIL1_HUMAN
UniProt AC Q9BYM8
Protein Name RanBP-type and C3HC4-type zinc finger-containing protein 1
Gene Name RBCK1
Organism Homo sapiens (Human).
Sequence Length 510
Subcellular Localization
Protein Description E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types..
Protein Sequence MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDIRLWVSVEDAQMHTVTIWLTVRPDMTVASLKDMVFLDYGFPPVLQQWVIGQRLARDQETLHSHGVRQNGDSAYLYLLSARNTSLNPQELQRERQLRMLEDLGFKDLTLQPRGPLEPGPPKPGVPQEPGRGQPDAVPEPPPVGWQCPGCTFINKPTRPGCEMCCRARPEAYQVPASYQPDEEERARLAGEEEALRQYQQRKQQQQEGNYLQHVQLDQRSLVLNTEPAECPVCYSVLAPGEAVVLRECLHTFCRECLQGTIRNSQEAEVSCPFIDNTYSCSGKLLEREIKALLTPEDYQRFLDLGISIAENRSAFSYHCKTPDCKGWCFFEDDVNEFTCPVCFHVNCLLCKAIHEQMNCKEYQEDLALRAQNDVAARQTTEMLKVMLQQGEAMRCPQCQIVVQKKDGCDWIRCTVCHTEICWVTKGPRWGPGGPGDTSGGCRCRVNGIPCHPSCQNCH
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
1Acetylation-------MDEKTKKA
-------CCHHHHHH		15.7622814378
14PhosphorylationKAEEMALSLTRAVAG
HHHHHHHHHHHHHHC		20.3924670416
16PhosphorylationEEMALSLTRAVAGGD
HHHHHHHHHHHHCCC		17.1327251275
29UbiquitinationGDEQVAMKCAIWLAE
CCHHHHHHHHHHHHH		15.69-
42PhosphorylationAEQRVPLSVQLKPEV
HHCCCCEEEEECCCC		11.1823403867
50PhosphorylationVQLKPEVSPTQDIRL
EEECCCCCCCCCEEE		22.1429255136
52PhosphorylationLKPEVSPTQDIRLWV
ECCCCCCCCCEEEEE		31.2229255136
116 (in isoform 4)Ubiquitination-25.6721890473
116 (in isoform 3)Ubiquitination-25.6721890473
132 (in isoform 4)Ubiquitination-23.6921890473
132 (in isoform 3)Ubiquitination-23.6921890473
132PhosphorylationSAYLYLLSARNTSLN
CEEEEHHHHCCCCCC		23.6924719451
136PhosphorylationYLLSARNTSLNPQEL
EHHHHCCCCCCHHHH		29.1028348404
137PhosphorylationLLSARNTSLNPQELQ
HHHHCCCCCCHHHHH		29.6928857561
158UbiquitinationMLEDLGFKDLTLQPR
HHHHCCCCCCCCCCC		50.4521890473
158 (in isoform 1)Ubiquitination-50.4521890473
174 (in isoform 1)Ubiquitination-58.5021890473
174UbiquitinationPLEPGPPKPGVPQEP
CCCCCCCCCCCCCCC		58.5021890473
212 (in isoform 3)Ubiquitination-19.4121890473
224PhosphorylationCRARPEAYQVPASYQ
CCCCCCHHCCCCCCC		14.3728796482
229PhosphorylationEAYQVPASYQPDEEE
CHHCCCCCCCCCHHH		20.4528857561
250PhosphorylationEEEALRQYQQRKQQQ
HHHHHHHHHHHHHHH		10.5228152594
254 (in isoform 1)Ubiquitination-48.3921890473
254UbiquitinationLRQYQQRKQQQQEGN
HHHHHHHHHHHHHCC		48.3921890473
262PhosphorylationQQQQEGNYLQHVQLD
HHHHHCCCCHHHEEC		20.7028796482
272PhosphorylationHVQLDQRSLVLNTEP
HHEECCCEEEECCCC		19.7326657352
277PhosphorylationQRSLVLNTEPAECPV
CCEEEECCCCCCCCC		38.9030108239
286PhosphorylationPAECPVCYSVLAPGE
CCCCCCEEEEECCCC		11.3127080861
288PhosphorylationECPVCYSVLAPGEAV
CCCCEEEEECCCCCH		1.8215951569
300 (in isoform 3)Ubiquitination-2.4621890473
316PhosphorylationLQGTIRNSQEAEVSC
HHHHHCCCCCEEEEC		21.3921945579
322PhosphorylationNSQEAEVSCPFIDNT
CCCCEEEECCCCCCC		13.9421945579
329PhosphorylationSCPFIDNTYSCSGKL
ECCCCCCCCCCCHHH		17.0521945579
330PhosphorylationCPFIDNTYSCSGKLL
CCCCCCCCCCCHHHH		17.5921945579
331PhosphorylationPFIDNTYSCSGKLLE
CCCCCCCCCCHHHHH		10.3621945579
333PhosphorylationIDNTYSCSGKLLERE
CCCCCCCCHHHHHHH		32.7821945579
335UbiquitinationNTYSCSGKLLEREIK
CCCCCCHHHHHHHHH		33.34-
342UbiquitinationKLLEREIKALLTPED
HHHHHHHHHHCCHHH		28.382189047
342 (in isoform 1)Ubiquitination-28.3821890473
346PhosphorylationREIKALLTPEDYQRF
HHHHHHCCHHHHHHH		26.0228857561
350PhosphorylationALLTPEDYQRFLDLG
HHCCHHHHHHHHHHC		10.4228152594
359PhosphorylationRFLDLGISIAENRSA
HHHHHCCCEECCCCC		17.5923532336
368PhosphorylationAENRSAFSYHCKTPD
ECCCCCEECCCCCCC		17.4327251275
409SulfoxidationCKAIHEQMNCKEYQE
HHHHHHHHCCHHHHH		6.0630846556
412UbiquitinationIHEQMNCKEYQEDLA
HHHHHCCHHHHHHHH		55.22-
436UbiquitinationRQTTEMLKVMLQQGE
HHHHHHHHHHHHCCC		25.04-
490PhosphorylationPGGPGDTSGGCRCRV
CCCCCCCCCCCEEEE		37.62-
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
-KUbiquitinationE3 ubiquitin ligaseRBCK1Q9BYM8
PMID:18303026
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HOIL1_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 HOIL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
18303026
HOIL1_HUMANRBCK1physical
18303026
BACH1_HUMANBACH1physical
17682061
UB2D3_HUMANUBE2D3physical
17682061
SOCS6_MOUSESocs6physical
16643902
IREB2_HUMANIREB2physical
12629548
TRI25_HUMANTRIM25physical
21292167
UBC_HUMANUBCphysical
19796170
HOIL1_HUMANRBCK1physical
16083853
KPCB_HUMANPRKCBphysical
17121852
TAB2_HUMANTAB2physical
17449468
TAB3_HUMANTAB3physical
17449468
M3K7_HUMANMAP3K7physical
17449468
TRAF6_HUMANTRAF6physical
17449468
RIPK1_HUMANRIPK1physical
17449468
IREB2_HUMANIREB2physical
17822790
UBC_HUMANUBCphysical
22139374
NR2C2_HUMANNR2C2physical
17449468
PML_HUMANPMLphysical
15833741
ESR1_HUMANESR1physical
23042805
KPCB_HUMANPRKCBphysical
23042805
UB2L3_HUMANUBE2L3physical
18303026
UB2D3_HUMANUBE2D3physical
12629548
UB2D3_HUMANUBE2D3physical
21292167
A4_HUMANAPPphysical
21832049
NR1I2_HUMANNR1I2physical
23160820
RNF31_HUMANRNF31physical
17006537
MKRN2_HUMANMKRN2physical
22493164
TRIML_HUMANTRIML1physical
22493164
UHRF2_HUMANUHRF2physical
22493164
PCGF2_HUMANPCGF2physical
22493164
RN181_HUMANRNF181physical
22493164
TRI65_HUMANTRIM65physical
22493164
FKBPL_HUMANFKBPLphysical
23912458
HS90A_HUMANHSP90AA1physical
23912458
ESR1_HUMANESR1physical
23912458
SHRPN_HUMANSHARPINphysical
21455180
RNF31_HUMANRNF31physical
21455180
KPCA_HUMANPRKCAphysical
25118570
HOIL1_HUMANRBCK1physical
25416956
NDUF3_HUMANNDUFAF3physical
25416956
TSSK3_HUMANTSSK3physical
25416956
SYCE1_HUMANSYCE1physical
25416956
NEMO_HUMANIKBKGphysical
19675569
UBC_HUMANUBCphysical
17006537
UB2D3_HUMANUBE2D3physical
17006537
UB2D1_HUMANUBE2D1physical
17006537
UB2D2_HUMANUBE2D2physical
17006537
UB2L3_HUMANUBE2L3physical
17006537
UBC_HUMANUBCphysical
23986494
RNF31_HUMANRNF31physical
26577923
RNF31_HUMANRNF31physical
26525107
NEMO_HUMANIKBKGphysical
27893701
TRAF1_HUMANTRAF1physical
27893701
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615895Polyglucosan body myopathy 1 with or without immunodeficiency (PGBM1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HOIL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, AND MASSSPECTROMETRY.

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