Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

AN1-type zinc finger protein 5

Gene

Zfand5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri8 – 42A20-typePROSITE-ProRule annotationAdd BLAST35
Zinc fingeri151 – 194AN1-typePROSITE-ProRule annotationAdd BLAST44

GO - Molecular functioni

GO - Biological processi

  • face development Source: MGI
  • fibroblast migration Source: MGI
  • in utero embryonic development Source: MGI
  • platelet-derived growth factor receptor signaling pathway Source: MGI
  • respiratory system process Source: MGI
  • skeletal system morphogenesis Source: MGI
  • smooth muscle tissue development Source: MGI
  • vasculature development Source: MGI

Keywordsi

Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
AN1-type zinc finger protein 5
Alternative name(s):
Zinc finger A20 domain-containing protein 2
Zinc finger protein 216
Gene namesi
Name:Zfand5
Synonyms:Za20d2, Zfp216, Znf216
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi

Organism-specific databases

MGIiMGI:1278334 Zfand5

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Resistance to muscle atrophy accompanied by abnormal accumulation of polyubiquitinated proteins in skeletal muscle.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000665581 – 213AN1-type zinc finger protein 5Add BLAST213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48PhosphoserineCombined sources1
Modified residuei58PhosphoserineCombined sources1
Modified residuei209N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO88878
MaxQBiO88878
PaxDbiO88878
PeptideAtlasiO88878
PRIDEiO88878

PTM databases

iPTMnetiO88878
PhosphoSitePlusiO88878

Expressioni

Tissue specificityi

Expressed in brain, muscle, eye, and heart, lower expression in lung, kidney, and spleen, and very low expression in liver. Expressed in myoblast C2C12 cells (at protein level).2 Publications

Inductioni

Up-regulated after TNFSF11 stimulation. Expression also induced by other cytokines such as TNF and IL1B. No significant inhibitory effect on the NF-kappa-B pathway is observed. Expression is increased in both denervation- and fasting-induced muscle atrophy.1 Publication

Gene expression databases

BgeeiENSMUSG00000024750
CleanExiMM_ZFAND5
ExpressionAtlasiO88878 baseline and differential
GenevisibleiO88878 MM

Interactioni

Subunit structurei

Homooligomer and/or heterooligomer. Interacts (via A20-type domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type domain) (By similarity). Interacts with ubiquitin and polyubiquitinated proteins. Identified in a heterotrimeric complex with ubiquitin and SQSTM1, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule (By similarity).By similarity

Protein-protein interaction databases

BioGridi204649, 2 interactors
STRINGi10090.ENSMUSP00000025659

Structurei

Secondary structure

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi155 – 157Combined sources3
Helixi162 – 164Combined sources3
Beta strandi176 – 178Combined sources3
Turni181 – 185Combined sources5
Helixi190 – 192Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WFLNMR-A134-194[»]
ProteinModelPortaliO88878
SMRiO88878
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88878

Family & Domainsi

Domaini

The A20-type zinc finger directly binds polyubiquitin chains and associates with the 26S proteasome. The zinc-finger A20-type domain is essential for inhibition of NF-kappa-B activation.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri8 – 42A20-typePROSITE-ProRule annotationAdd BLAST35
Zinc fingeri151 – 194AN1-typePROSITE-ProRule annotationAdd BLAST44

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3173 Eukaryota
ENOG4111UWC LUCA
GeneTreeiENSGT00510000046525
HOGENOMiHOG000238229
HOVERGENiHBG053349
InParanoidiO88878
OMAiTEGLCSK
OrthoDBiEOG091G0M53
PhylomeDBiO88878
TreeFamiTF313612

Family and domain databases

Gene3Di4.10.1110.10, 1 hit
InterProiView protein in InterPro
IPR035896 AN1-like_Znf
IPR002653 Znf_A20
IPR000058 Znf_AN1
PfamiView protein in Pfam
PF01754 zf-A20, 1 hit
PF01428 zf-AN1, 1 hit
SMARTiView protein in SMART
SM00259 ZnF_A20, 1 hit
SM00154 ZnF_AN1, 1 hit
SUPFAMiSSF118310 SSF118310, 1 hit
PROSITEiView protein in PROSITE
PS51036 ZF_A20, 1 hit
PS51039 ZF_AN1, 1 hit

Sequencei

Sequence statusi: Complete.

O88878-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQETNQTPG PMLCSTGCGF YGNPRTNGMC SVCYKEHLQR QQNSGRMSPM
60 70 80 90 100
GTASGSNSPT SDSASVQRAD AGLNNCEGAA GSTSEKSRNV PVAALPVTQQ
110 120 130 140 150
MTEMSISRED KITTPKTEVS EPVVTQPSPS VSQPSSSQSE EKAPELPKPK
160 170 180 190 200
KNRCFMCRKK VGLTGFDCRC GNLFCGLHRY SDKHNCPYDY KAEAAAKIRK
210
ENPVVVAEKI QRI
Length:213
Mass (Da):23,058
Last modified:November 1, 1998 - v1
Checksum:i65B3B001DA6B8F59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062071 mRNA Translation: AAC42600.1
AK076397 mRNA Translation: BAC36321.1
BC107566 mRNA Translation: AAI07567.1
BC119124 mRNA Translation: AAI19125.1
BC119126 mRNA Translation: AAI19127.1
CCDSiCCDS29697.1
RefSeqiNP_033577.1, NM_009551.5
XP_006527121.1, XM_006527058.3
UniGeneiMm.292405
Mm.379919

Genome annotation databases

EnsembliENSMUST00000025659; ENSMUSP00000025659; ENSMUSG00000024750
GeneIDi22682
KEGGimmu:22682
UCSCiuc008gyw.2 mouse

Similar proteinsi

Entry informationi

Entry nameiZFAN5_MOUSE
AccessioniPrimary (citable) accession number: O88878
Secondary accession number(s): Q3B7K8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1998
Last modified: March 28, 2018
This is version 132 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health