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Protein

AN1-type zinc finger protein 5

Gene

Zfand5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri8 – 4235A20-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri151 – 19444AN1-typePROSITE-ProRule annotationAdd
BLAST

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
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1278334. Zfand5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213AN1-type zinc finger protein 5PRO_0000066558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei209 – 2091N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO88878.
MaxQBiO88878.
PaxDbiO88878.
PRIDEiO88878.

PTM databases

iPTMnetiO88878.
PhosphoSiteiO88878.

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

BgeeiO88878.
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. 1 interaction.
STRINGi10090.ENSMUSP00000025659.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi155 – 1573Combined sources
Helixi162 – 1643Combined sources
Beta strandi176 – 1783Combined sources
Turni181 – 1855Combined sources
Helixi190 – 1923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFLNMR-A134-194[»]
ProteinModelPortaliO88878.
SMRiO88878. Positions 1-60, 140-196.
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

Sequence similaritiesi

Contains 1 A20-type zinc finger.PROSITE-ProRule annotation
Contains 1 AN1-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri8 – 4235A20-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri151 – 19444AN1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3173. Eukaryota.
ENOG4111UWC. LUCA.
GeneTreeiENSGT00510000046525.
HOGENOMiHOG000238229.
HOVERGENiHBG053349.
InParanoidiO88878.
OMAiSLNNCES.
OrthoDBiEOG7TTQ9W.
PhylomeDBiO88878.
TreeFamiTF313612.

Family and domain databases

Gene3Di4.10.1110.10. 1 hit.
InterProiIPR002653. Znf_A20.
IPR000058. Znf_AN1.
[Graphical view]
PfamiPF01754. zf-A20. 1 hit.
PF01428. zf-AN1. 1 hit.
[Graphical view]
SMARTiSM00259. ZnF_A20. 1 hit.
SM00154. ZnF_AN1. 1 hit.
[Graphical view]
PROSITEiPS51036. ZF_A20. 1 hit.
PS51039. ZF_AN1. 1 hit.
[Graphical view]

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_006527058.2.
UniGeneiMm.292405.
Mm.379919.

Genome annotation databases

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

Cross-referencesi

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_006527058.2.
UniGeneiMm.292405.
Mm.379919.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFLNMR-A134-194[»]
ProteinModelPortaliO88878.
SMRiO88878. Positions 1-60, 140-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204649. 1 interaction.
STRINGi10090.ENSMUSP00000025659.

PTM databases

iPTMnetiO88878.
PhosphoSiteiO88878.

Proteomic databases

EPDiO88878.
MaxQBiO88878.
PaxDbiO88878.
PRIDEiO88878.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7763.
MGIiMGI:1278334. Zfand5.

Phylogenomic databases

eggNOGiKOG3173. Eukaryota.
ENOG4111UWC. LUCA.
GeneTreeiENSGT00510000046525.
HOGENOMiHOG000238229.
HOVERGENiHBG053349.
InParanoidiO88878.
OMAiSLNNCES.
OrthoDBiEOG7TTQ9W.
PhylomeDBiO88878.
TreeFamiTF313612.

Miscellaneous databases

ChiTaRSiZfand5. mouse.
EvolutionaryTraceiO88878.
NextBioi303111.
PROiO88878.
SOURCEiSearch...

Gene expression databases

BgeeiO88878.
CleanExiMM_ZFAND5.
ExpressionAtlasiO88878. baseline and differential.
GenevisibleiO88878. MM.

Family and domain databases

Gene3Di4.10.1110.10. 1 hit.
InterProiIPR002653. Znf_A20.
IPR000058. Znf_AN1.
[Graphical view]
PfamiPF01754. zf-A20. 1 hit.
PF01428. zf-AN1. 1 hit.
[Graphical view]
SMARTiSM00259. ZnF_A20. 1 hit.
SM00154. ZnF_AN1. 1 hit.
[Graphical view]
PROSITEiPS51036. ZF_A20. 1 hit.
PS51039. ZF_AN1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and mutation analysis of a cochlear-expressed, zinc finger protein gene at the DFNB7/11 and dn hearing-loss loci on human chromosome 9q and mouse chromosome 19."
    Scott D.A., Greinwald J.H. Jr., Marietta J.R., Drury S., Swiderski R.E., Vinas A., DeAngelis M.M., Carmi R., Ramesh A., Kraft M.L., Elbedour K., Skworak A.B., Friedman R.A., Srikumari Srisailapathy C.R., Verhoeven K., Van Camp G., Lovett M., Deininger P.L.
    , Batzer M.A., Morton C.C., Keats B.J., Smith R.J.H., Sheffield V.C.
    Gene 215:461-469(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: 129.
    Tissue: Mammary gland.
  4. "ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation."
    Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z., Shu H.-B.
    J. Biol. Chem. 279:16847-16853(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "A RANKL-inducible gene Znf216 in osteoclast differentiation."
    Hishiya A., Ikeda K., Watanabe K.
    J. Recept. Signal Transduct. 25:199-216(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, FUNCTION.
  6. "A novel ubiquitin-binding protein ZNF216 functioning in muscle atrophy."
    Hishiya A., Iemura S., Natsume T., Takayama S., Ikeda K., Watanabe K.
    EMBO J. 25:554-564(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, UBIQUITIN-BINDING, DOMAIN A20-TYPE ZINC-FINGER, FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "Solution structure of the ZF-AN1 domain from mouse zinc finger protein 216."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 132-194.

Entry informationi

Entry nameiZFAN5_MOUSE
AccessioniPrimary (citable) accession number: O88878
Secondary accession number(s): Q3B7K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1998
Last modified: March 16, 2016
This is version 119 of the entry and version 1 of the sequence. [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
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.