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Protein

AN1-type zinc finger protein 5

Gene

ZFAND5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

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

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, ZNF216
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:13008. ZFAND5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37587.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213AN1-type zinc finger protein 5PRO_0000066557Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO76080.
MaxQBiO76080.
PaxDbiO76080.
PeptideAtlasiO76080.
PRIDEiO76080.
TopDownProteomicsiO76080.

PTM databases

iPTMnetiO76080.
PhosphoSiteiO76080.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle. Expressed in fetal cochlea. Also expressed in infant brain, fetal heart, pancreatic islet, melanocyte, pineal gland, placenta, corneal stroma, and parathyroid tumor. Weakly expressed or undetectable in adult brain, heart, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocytes. Expressed in rhabdomyosarcoma RD cells (at protein level).2 Publications

Gene expression databases

BgeeiO76080.
CleanExiHS_ZFAND5.
ExpressionAtlasiO76080. baseline and differential.
GenevisibleiO76080. HS.

Organism-specific databases

HPAiHPA018129.

Interactioni

Subunit structurei

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). Homooligomer and/or heterooligomer. Interacts (via A20-type domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type domain).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
UBCP0CG483EBI-8028844,EBI-3390054

Protein-protein interaction databases

BioGridi113546. 13 interactions.
IntActiO76080. 6 interactions.
MINTiMINT-1958864.
STRINGi9606.ENSP00000237937.

Structurei

3D structure databases

ProteinModelPortaliO76080.
SMRiO76080. Positions 1-60, 140-196.
ModBaseiSearch...
MobiDBiSearch...

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 (By similarity).By similarity

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.
InParanoidiO76080.
OMAiSLNNCES.
OrthoDBiEOG7TTQ9W.
PhylomeDBiO76080.
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.

O76080-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQETNQTPG PMLCSTGCGF YGNPRTNGMC SVCYKEHLQR QQNSGRMSPM
60 70 80 90 100
GTASGSNSPT SDSASVQRAD TSLNNCEGAA GSTSEKSRNV PVAALPVTQQ
110 120 130 140 150
MTEMSISRED KITTPKTEVS EPVVTQPSPS VSQPSTSQSE EKAPELPKPK
160 170 180 190 200
KNRCFMCRKK VGLTGFDCRC GNLFCGLHRY SDKHNCPYDY KAEAAAKIRK
210
ENPVVVAEKI QRI
Length:213
Mass (Da):23,132
Last modified:November 1, 1998 - v1
Checksum:iE477504B1BA77753
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062072 Genomic DNA. Translation: AAC61801.1.
AF062346 mRNA. Translation: AAC42601.1.
AF062347 mRNA. Translation: AAC42602.1.
AK290849 mRNA. Translation: BAF83538.1.
AL135924 Genomic DNA. Translation: CAD13440.1.
CH471089 Genomic DNA. Translation: EAW62533.1.
BC011018 mRNA. Translation: AAH11018.1.
BC027707 mRNA. Translation: AAH27707.1.
BC073131 mRNA. Translation: AAH73131.1.
CCDSiCCDS6642.1.
RefSeqiNP_001095890.1. NM_001102420.2.
NP_001095891.1. NM_001102421.2.
NP_001265172.1. NM_001278243.1.
NP_001265173.1. NM_001278244.1.
NP_001265174.1. NM_001278245.1.
NP_005998.1. NM_006007.3.
UniGeneiHs.406096.

Genome annotation databases

EnsembliENST00000237937; ENSP00000237937; ENSG00000107372.
ENST00000343431; ENSP00000350586; ENSG00000107372.
ENST00000376960; ENSP00000366159; ENSG00000107372.
ENST00000376962; ENSP00000366161; ENSG00000107372.
GeneIDi7763.
KEGGihsa:7763.
UCSCiuc004aix.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062072 Genomic DNA. Translation: AAC61801.1.
AF062346 mRNA. Translation: AAC42601.1.
AF062347 mRNA. Translation: AAC42602.1.
AK290849 mRNA. Translation: BAF83538.1.
AL135924 Genomic DNA. Translation: CAD13440.1.
CH471089 Genomic DNA. Translation: EAW62533.1.
BC011018 mRNA. Translation: AAH11018.1.
BC027707 mRNA. Translation: AAH27707.1.
BC073131 mRNA. Translation: AAH73131.1.
CCDSiCCDS6642.1.
RefSeqiNP_001095890.1. NM_001102420.2.
NP_001095891.1. NM_001102421.2.
NP_001265172.1. NM_001278243.1.
NP_001265173.1. NM_001278244.1.
NP_001265174.1. NM_001278245.1.
NP_005998.1. NM_006007.3.
UniGeneiHs.406096.

3D structure databases

ProteinModelPortaliO76080.
SMRiO76080. Positions 1-60, 140-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113546. 13 interactions.
IntActiO76080. 6 interactions.
MINTiMINT-1958864.
STRINGi9606.ENSP00000237937.

PTM databases

iPTMnetiO76080.
PhosphoSiteiO76080.

Proteomic databases

EPDiO76080.
MaxQBiO76080.
PaxDbiO76080.
PeptideAtlasiO76080.
PRIDEiO76080.
TopDownProteomicsiO76080.

Protocols and materials databases

DNASUi7763.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237937; ENSP00000237937; ENSG00000107372.
ENST00000343431; ENSP00000350586; ENSG00000107372.
ENST00000376960; ENSP00000366159; ENSG00000107372.
ENST00000376962; ENSP00000366161; ENSG00000107372.
GeneIDi7763.
KEGGihsa:7763.
UCSCiuc004aix.3. human.

Organism-specific databases

CTDi7763.
GeneCardsiZFAND5.
HGNCiHGNC:13008. ZFAND5.
HPAiHPA018129.
MIMi604761. gene.
neXtProtiNX_O76080.
PharmGKBiPA37587.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3173. Eukaryota.
ENOG4111UWC. LUCA.
GeneTreeiENSGT00510000046525.
HOGENOMiHOG000238229.
HOVERGENiHBG053349.
InParanoidiO76080.
OMAiSLNNCES.
OrthoDBiEOG7TTQ9W.
PhylomeDBiO76080.
TreeFamiTF313612.

Miscellaneous databases

ChiTaRSiZFAND5. human.
GenomeRNAii7763.
PROiO76080.
SOURCEiSearch...

Gene expression databases

BgeeiO76080.
CleanExiHS_ZFAND5.
ExpressionAtlasiO76080. baseline and differential.
GenevisibleiO76080. HS.

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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Eye, Lung and Skin.
  6. "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, INTERACTION WITH IKBKG; RIPK1 AND TRAF6, FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiZFAN5_HUMAN
AccessioniPrimary (citable) accession number: O76080
Secondary accession number(s): A8K484
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.