ZFP91_HUMAN - dbPTM
ZFP91_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZFP91_HUMAN
UniProt AC Q96JP5
Protein Name E3 ubiquitin-protein ligase ZFP91
Gene Name ZFP91
Organism Homo sapiens (Human).
Sequence Length 570
Subcellular Localization Nucleus .
Protein Description Atypical E3 ubiquitin-protein ligase that mediates 'Lys-63'-linked ubiquitination of MAP3K14/NIK, leading to stabilize and activate MAP3K14/NIK. It thereby acts as an activator of the non-canonical NF-kappa-B2/NFKB2 pathway. May also play an important role in cell proliferation and/or anti-apoptosis..
Protein Sequence MPGETEEPRPPEQQDQEGGEAAKAAPEEPQQRPPEAVAAAPAGTTSSRVLRGGRDRGRAAAAAAAAAVSRRRKAEYPRRRRSSPSARPPDVPGQQPQAAKSPSPVQGKKSPRLLCIEKVTTDKDPKEEKEEEDDSALPQEVSIAASRPSRGWRSSRTSVSRHRDTENTRSSRSKTGSLQLICKSEPNTDQLDYDVGEEHQSPGGISSEEEEEEEEEMLISEEEIPFKDDPRDETYKPHLERETPKPRRKSGKVKEEKEKKEIKVEVEVEVKEEENEIREDEEPPRKRGRRRKDDKSPRLPKRRKKPPIQYVRCEMEGCGTVLAHPRYLQHHIKYQHLLKKKYVCPHPSCGRLFRLQKQLLRHAKHHTDQRDYICEYCARAFKSSHNLAVHRMIHTGEKPLQCEICGFTCRQKASLNWHMKKHDADSFYQFSCNICGKKFEKKDSVVAHKAKSHPEVLIAEALAANAGALITSTDILGTNPESLTQPSDGQGLPLLPEPLGNSTSGECLLLEAEGMSKSYCSGTERVSLMADGKIFVGSGSSGGTEGLVMNSDILGATTEVLIEDSDSAGP
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
5Phosphorylation---MPGETEEPRPPE
---CCCCCCCCCCHH		52.1127135362
44PhosphorylationVAAAPAGTTSSRVLR
HHCCCCCCCCHHHHC		26.1322210691
45PhosphorylationAAAPAGTTSSRVLRG
HCCCCCCCCHHHHCC		24.6422210691
46PhosphorylationAAPAGTTSSRVLRGG
CCCCCCCCHHHHCCC		18.9122210691
47PhosphorylationAPAGTTSSRVLRGGR
CCCCCCCHHHHCCCC		25.0626434776
51MethylationTTSSRVLRGGRDRGR
CCCHHHHCCCCHHHH		42.54115920357
56MethylationVLRGGRDRGRAAAAA
HHCCCCHHHHHHHHH		34.83115920361
58MethylationRGGRDRGRAAAAAAA
CCCCHHHHHHHHHHH		23.19115920365
69PhosphorylationAAAAAAVSRRRKAEY
HHHHHHHHHHHHCCC		18.4926434776
76PhosphorylationSRRRKAEYPRRRRSS
HHHHHCCCCCHHCCC		13.6026657352
82 (in isoform 2)Phosphorylation-44.80-
82PhosphorylationEYPRRRRSSPSARPP
CCCCHHCCCCCCCCC		44.8029255136
83 (in isoform 2)Phosphorylation-22.51-
83PhosphorylationYPRRRRSSPSARPPD
CCCHHCCCCCCCCCC		22.5129255136
85 (in isoform 2)Phosphorylation-38.57-
85PhosphorylationRRRRSSPSARPPDVP
CHHCCCCCCCCCCCC		38.5729255136
101PhosphorylationQQPQAAKSPSPVQGK
CCCCCCCCCCCCCCC		26.3630266825
103PhosphorylationPQAAKSPSPVQGKKS
CCCCCCCCCCCCCCC		44.8125159151
108AcetylationSPSPVQGKKSPRLLC
CCCCCCCCCCCCEEE		32.7425953088
110PhosphorylationSPVQGKKSPRLLCIE
CCCCCCCCCCEEEEE		20.8130576142
120PhosphorylationLLCIEKVTTDKDPKE
EEEEEEEECCCCHHH		40.1026074081
121PhosphorylationLCIEKVTTDKDPKEE
EEEEEEECCCCHHHH		44.0026074081
146PhosphorylationQEVSIAASRPSRGWR
HHHHHHHCCCCCCCC		35.3828555341
149PhosphorylationSIAASRPSRGWRSSR
HHHHCCCCCCCCCCC		42.1725159151
154PhosphorylationRPSRGWRSSRTSVSR
CCCCCCCCCCCCHHH		20.0526434776
155PhosphorylationPSRGWRSSRTSVSRH
CCCCCCCCCCCHHHC		30.8826434776
157PhosphorylationRGWRSSRTSVSRHRD
CCCCCCCCCHHHCCC		35.1126434776
158PhosphorylationGWRSSRTSVSRHRDT
CCCCCCCCHHHCCCC		19.5826434776
160PhosphorylationRSSRTSVSRHRDTEN
CCCCCCHHHCCCCCC		23.3326434776
173PhosphorylationENTRSSRSKTGSLQL
CCCCCCCCCCCCEEE		36.2023312004
174MethylationNTRSSRSKTGSLQLI
CCCCCCCCCCCEEEE		56.6524129315
175PhosphorylationTRSSRSKTGSLQLIC
CCCCCCCCCCEEEEE		33.0029449344
177PhosphorylationSSRSKTGSLQLICKS
CCCCCCCCEEEEECC		20.4121815630
220PhosphorylationEEEEMLISEEEIPFK
HHHHHCCCCCCCCCC		34.6926074081
234PhosphorylationKDDPRDETYKPHLER
CCCCCCCCCHHHHCC		40.9326074081
235PhosphorylationDDPRDETYKPHLERE
CCCCCCCCHHHHCCC		22.0726074081
243PhosphorylationKPHLERETPKPRRKS
HHHHCCCCCCCCCCC		42.7225159151
250PhosphorylationTPKPRRKSGKVKEEK
CCCCCCCCCCCCCHH		41.8726074081
296 (in isoform 2)Phosphorylation-23.42-
296PhosphorylationRRRKDDKSPRLPKRR
CCCCCCCCCCCCCCC		23.4230576142
305UbiquitinationRLPKRRKKPPIQYVR
CCCCCCCCCCCCEEE		54.97-
333 (in isoform 2)Ubiquitination-34.2021890473
333UbiquitinationRYLQHHIKYQHLLKK
HHHHHHHHHHHHHCC		34.2021890473
333 (in isoform 1)Ubiquitination-34.2021890473
333UbiquitinationRYLQHHIKYQHLLKK
HHHHHHHHHHHHHCC		34.2021890473
339UbiquitinationIKYQHLLKKKYVCPH
HHHHHHHCCCCCCCC		54.29-
342PhosphorylationQHLLKKKYVCPHPSC
HHHHCCCCCCCCCCH		19.0328152594
348PhosphorylationKYVCPHPSCGRLFRL
CCCCCCCCHHHHHHH		26.60-
357UbiquitinationGRLFRLQKQLLRHAK
HHHHHHHHHHHHHHH		47.72-
367 (in isoform 2)Phosphorylation-33.28-
367PhosphorylationLRHAKHHTDQRDYIC
HHHHHCCCCCHHHHH		33.2820068231
382UbiquitinationEYCARAFKSSHNLAV
HHHHHHHHHCCCEEE		50.49-
395PhosphorylationAVHRMIHTGEKPLQC
EEEEEECCCCCCEEE		35.7921712546
395 (in isoform 2)Phosphorylation-35.79-
398UbiquitinationRMIHTGEKPLQCEIC
EEECCCCCCEEEEEC		52.99-
414PhosphorylationFTCRQKASLNWHMKK
CEECEECEECEEECC		29.3025159151
426PhosphorylationMKKHDADSFYQFSCN
ECCCCCCCCEEEEEC		27.8126434776
428PhosphorylationKHDADSFYQFSCNIC
CCCCCCCEEEEECCC		16.7626434776
438AcetylationSCNICGKKFEKKDSV
EECCCCCCCCCCCCC		44.0030593537
441AcetylationICGKKFEKKDSVVAH
CCCCCCCCCCCCHHH		66.0830593543
442AcetylationCGKKFEKKDSVVAHK
CCCCCCCCCCCHHHC		48.3030593549
449AcetylationKDSVVAHKAKSHPEV
CCCCHHHCCCCCHHH		48.0130593555
521PhosphorylationGMSKSYCSGTERVSL
CCCCHHCCCCCEEEE		40.2828102081
523PhosphorylationSKSYCSGTERVSLMA
CCHHCCCCCEEEEEE		12.3422210691
527PhosphorylationCSGTERVSLMADGKI
CCCCCEEEEEECCEE		20.7422210691
551PhosphorylationTEGLVMNSDILGATT
CCCEEECCCCCCCEE		14.1322210691
558PhosphorylationSDILGATTEVLIEDS
CCCCCCEEEEEECCC		24.4622210691
565PhosphorylationTEVLIEDSDSAGP--
EEEEECCCCCCCC--		22.2222210691
567PhosphorylationVLIEDSDSAGP----
EEECCCCCCCC----		38.7922210691
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 ZFP91_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZFP91_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 ZFP91_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K14_HUMANMAP3K14physical
20682767
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 ZFP91_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-83, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395, AND MASSSPECTROMETRY.

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