ZFAN5_MOUSE - dbPTM
ZFAN5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZFAN5_MOUSE
UniProt AC O88878
Protein Name AN1-type zinc finger protein 5
Gene Name Zfand5
Organism Mus musculus (Mouse).
Sequence Length 213
Subcellular Localization Cytoplasm.
Protein Description Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation..
Protein Sequence MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADAGLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSSSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI
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
44PhosphorylationHLQRQQNSGRMSPMG
HHHHHHHCCCCCCCC
24.3625619855
48PhosphorylationQQNSGRMSPMGTASG
HHHCCCCCCCCCCCC
15.4625521595
52PhosphorylationGRMSPMGTASGSNSP
CCCCCCCCCCCCCCC
16.0527087446
54PhosphorylationMSPMGTASGSNSPTS
CCCCCCCCCCCCCCC
42.4623684622
56PhosphorylationPMGTASGSNSPTSDS
CCCCCCCCCCCCCCC
31.4727087446
58PhosphorylationGTASGSNSPTSDSAS
CCCCCCCCCCCCCHH
31.1125521595
60PhosphorylationASGSNSPTSDSASVQ
CCCCCCCCCCCHHHH
45.0125619855
61PhosphorylationSGSNSPTSDSASVQR
CCCCCCCCCCHHHHH
32.7125619855
63PhosphorylationSNSPTSDSASVQRAD
CCCCCCCCHHHHHHH
23.3925619855
65PhosphorylationSPTSDSASVQRADAG
CCCCCCHHHHHHHHC
23.8025619855
82PhosphorylationNCEGAAGSTSEKSRN
CCCCCCCCCCHHHCC
24.8422802335
86UbiquitinationAAGSTSEKSRNVPVA
CCCCCCHHHCCCCEE
55.2522790023
102PhosphorylationLPVTQQMTEMSISRE
EECCHHHHHCCCCCC
24.9721454597
105PhosphorylationTQQMTEMSISREDKI
CHHHHHCCCCCCCCC
15.9221454597
107PhosphorylationQMTEMSISREDKITT
HHHHCCCCCCCCCCC
23.4721454597
113PhosphorylationISREDKITTPKTEVS
CCCCCCCCCCCCCCC
42.6726643407
114PhosphorylationSREDKITTPKTEVSE
CCCCCCCCCCCCCCC
26.6826643407
117PhosphorylationDKITTPKTEVSEPVV
CCCCCCCCCCCCCEE
42.7126643407
120PhosphorylationTTPKTEVSEPVVTQP
CCCCCCCCCCEECCC
29.9226643407
128PhosphorylationEPVVTQPSPSVSQPS
CCEECCCCCCCCCCC
21.7125338131
188PhosphorylationSDKHNCPYDYKAEAA
CCCCCCCCCHHHHHH
33.8229514104
209AcetylationNPVVVAEKIQRI---
CCEEEEEECCCC---
34.1123806337

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 ZFAN5_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZFAN5_MOUSE !!

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 ZFAN5_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNFA_MOUSETnfphysical
22665488

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZFAN5_MOUSE

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Related Literatures of Post-Translational Modification

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