ZFAN6_HUMAN
ID ZFAN6_HUMAN Reviewed; 208 AA.
AC Q6FIF0; D3DW92; D3DW94; O95792; Q9BQF7; Q9GZY3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=AN1-type zinc finger protein 6;
DE AltName: Full=Associated with PRK1 protein;
DE AltName: Full=Zinc finger A20 domain-containing protein 3;
GN Name=ZFAND6; Synonyms=AWP1, ZA20D3; ORFNames=HT032;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=11054541; DOI=10.1016/s0378-1119(00)00365-6;
RA Duan W., Sun B., Li T.W., Tan B.J., Lee M.K., Teo T.S.;
RT "Cloning and characterization of AWP1, a novel protein that associates with
RT serine/threonine kinase PRK1 in vivo.";
RL Gene 256:113-121(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Wu J., Liu T., Zhang J., Mao M., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y.,
RA Wang Z., Chen S., Chen Z.;
RT "A novel human gene expressed in acute promyelocytic leukemia cell line
RT NB4.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP FUNCTION, AND INTERACTION WITH POLYUBIQUITIN.
RX PubMed=19285159; DOI=10.1016/j.bbapap.2009.02.013;
RA Fenner B.J., Scannell M., Prehn J.H.;
RT "Identification of polyubiquitin binding proteins involved in NF-kappaB
RT signaling using protein arrays.";
RL Biochim. Biophys. Acta 1794:1010-1016(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH TRAF2.
RX PubMed=21810480; DOI=10.1016/j.biocel.2011.07.010;
RA Chang E.J., Ha J., Kang S.S., Lee Z.H., Kim H.H.;
RT "AWP1 binds to tumor necrosis factor receptor-associated factor 2 (TRAF2)
RT and is involved in TRAF2-mediated nuclear factor-kappaB signaling.";
RL Int. J. Biochem. Cell Biol. 43:1612-1620(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in regulation of TNF-alpha induced NF-kappa-B
CC activation and apoptosis. Involved in modulation of 'Lys-48'-linked
CC polyubiquitination status of TRAF2 and decreases association of TRAF2
CC with RIPK1. Required for PTS1 target sequence-dependent protein import
CC into peroxisomes and PEX5 stability; may cooperate with PEX6. In vitro
CC involved in PEX5 export from the cytosol to peroxisomes (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:19285159,
CC ECO:0000269|PubMed:21810480}.
CC -!- SUBUNIT: Interacts with PKN1 (By similarity). Interacts with TRAF2.
CC Interacts with mono- and polyubiquitin. Interacts with PEX6. Interacts
CC with PEX5 (Cys-linked ubiquitinated) (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6FIF0; P54725: RAD23A; NbExp=3; IntAct=EBI-724630, EBI-746453;
CC Q6FIF0; Q12933: TRAF2; NbExp=7; IntAct=EBI-724630, EBI-355744;
CC Q6FIF0; O00463: TRAF5; NbExp=3; IntAct=EBI-724630, EBI-523498;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6FIF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6FIF0-2; Sequence=VSP_019652;
CC -!- TISSUE SPECIFICITY: Widely expressed with high level in heart, skeletal
CC muscle, liver, kidney and placenta. {ECO:0000269|PubMed:11054541}.
CC -!- DOMAIN: The A20-type zinc finger domain mediates regulation of NF-
CC kappa-B activity.
CC -!- DOMAIN: The AN1-type zinc finger domain mediates association with
CC TRAF2.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17528.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ251095; CAC14876.1; -; mRNA.
DR EMBL; AF061739; AAD17528.1; ALT_FRAME; mRNA.
DR EMBL; AF261138; AAG44674.1; -; mRNA.
DR EMBL; AL136598; CAB66533.1; -; mRNA.
DR EMBL; CR533476; CAG38507.1; -; mRNA.
DR EMBL; CH471136; EAW99122.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99123.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99124.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99125.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99127.1; -; Genomic_DNA.
DR EMBL; BC005283; AAH05283.1; -; mRNA.
DR CCDS; CCDS10313.1; -. [Q6FIF0-1]
DR CCDS; CCDS58395.1; -. [Q6FIF0-2]
DR RefSeq; NP_001229840.1; NM_001242911.1. [Q6FIF0-1]
DR RefSeq; NP_001229841.1; NM_001242912.1. [Q6FIF0-1]
DR RefSeq; NP_001229842.1; NM_001242913.1. [Q6FIF0-1]
DR RefSeq; NP_001229843.1; NM_001242914.1. [Q6FIF0-1]
DR RefSeq; NP_001229844.1; NM_001242915.1. [Q6FIF0-1]
DR RefSeq; NP_001229845.1; NM_001242916.1. [Q6FIF0-1]
DR RefSeq; NP_001229846.1; NM_001242917.1. [Q6FIF0-2]
DR RefSeq; NP_061879.2; NM_019006.3. [Q6FIF0-1]
DR RefSeq; XP_011519986.1; XM_011521684.2. [Q6FIF0-1]
DR AlphaFoldDB; Q6FIF0; -.
DR SMR; Q6FIF0; -.
DR BioGRID; 119975; 16.
DR IntAct; Q6FIF0; 6.
DR STRING; 9606.ENSP00000261749; -.
DR iPTMnet; Q6FIF0; -.
DR PhosphoSitePlus; Q6FIF0; -.
DR BioMuta; ZFAND6; -.
DR DMDM; 110288083; -.
DR EPD; Q6FIF0; -.
DR jPOST; Q6FIF0; -.
DR MassIVE; Q6FIF0; -.
DR MaxQB; Q6FIF0; -.
DR PaxDb; Q6FIF0; -.
DR PeptideAtlas; Q6FIF0; -.
DR PRIDE; Q6FIF0; -.
DR ProteomicsDB; 66298; -. [Q6FIF0-1]
DR ProteomicsDB; 66299; -. [Q6FIF0-2]
DR TopDownProteomics; Q6FIF0-1; -. [Q6FIF0-1]
DR Antibodypedia; 15226; 107 antibodies from 19 providers.
DR CPTC; Q6FIF0; 3 antibodies.
DR DNASU; 54469; -.
DR Ensembl; ENST00000261749.11; ENSP00000261749.6; ENSG00000086666.19. [Q6FIF0-1]
DR Ensembl; ENST00000558087.5; ENSP00000453888.1; ENSG00000086666.19. [Q6FIF0-1]
DR Ensembl; ENST00000558494.5; ENSP00000454137.1; ENSG00000086666.19. [Q6FIF0-1]
DR Ensembl; ENST00000559157.5; ENSP00000454152.1; ENSG00000086666.19. [Q6FIF0-2]
DR Ensembl; ENST00000559775.5; ENSP00000453709.1; ENSG00000086666.19. [Q6FIF0-1]
DR Ensembl; ENST00000559835.5; ENSP00000453291.1; ENSG00000086666.19. [Q6FIF0-1]
DR Ensembl; ENST00000561060.5; ENSP00000452735.1; ENSG00000086666.19. [Q6FIF0-1]
DR Ensembl; ENST00000613266.4; ENSP00000479071.1; ENSG00000086666.19. [Q6FIF0-1]
DR Ensembl; ENST00000616533.4; ENSP00000478129.1; ENSG00000086666.19. [Q6FIF0-1]
DR Ensembl; ENST00000618205.4; ENSP00000484971.1; ENSG00000086666.19. [Q6FIF0-1]
DR GeneID; 54469; -.
DR KEGG; hsa:54469; -.
DR MANE-Select; ENST00000261749.11; ENSP00000261749.6; NM_019006.4; NP_061879.2.
DR UCSC; uc002bfe.2; human. [Q6FIF0-1]
DR CTD; 54469; -.
DR DisGeNET; 54469; -.
DR GeneCards; ZFAND6; -.
DR HGNC; HGNC:30164; ZFAND6.
DR HPA; ENSG00000086666; Low tissue specificity.
DR MIM; 610183; gene.
DR neXtProt; NX_Q6FIF0; -.
DR OpenTargets; ENSG00000086666; -.
DR PharmGKB; PA134883256; -.
DR VEuPathDB; HostDB:ENSG00000086666; -.
DR eggNOG; KOG3173; Eukaryota.
DR GeneTree; ENSGT00940000160833; -.
DR HOGENOM; CLU_057016_1_0_1; -.
DR InParanoid; Q6FIF0; -.
DR OMA; DTTKCFS; -.
DR OrthoDB; 1551371at2759; -.
DR PhylomeDB; Q6FIF0; -.
DR TreeFam; TF313612; -.
DR PathwayCommons; Q6FIF0; -.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; Q6FIF0; -.
DR BioGRID-ORCS; 54469; 17 hits in 1081 CRISPR screens.
DR ChiTaRS; ZFAND6; human.
DR GenomeRNAi; 54469; -.
DR Pharos; Q6FIF0; Tbio.
DR PRO; PR:Q6FIF0; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6FIF0; protein.
DR Bgee; ENSG00000086666; Expressed in right testis and 104 other tissues.
DR ExpressionAtlas; Q6FIF0; baseline and differential.
DR Genevisible; Q6FIF0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISS:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR Gene3D; 4.10.1110.10; -; 1.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR002653; Znf_A20.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF01754; zf-A20; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; SSF118310; 1.
DR PROSITE; PS51036; ZF_A20; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Cytoplasm; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..208
FT /note="AN1-type zinc finger protein 6"
FT /id="PRO_0000245235"
FT ZN_FING 8..42
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT ZN_FING 143..189
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 41..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCH6"
FT VAR_SEQ 52..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019652"
FT CONFLICT 138
FT /note="S -> P (in Ref. 3; CAB66533 and 5; CAG38507)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="E -> D (in Ref. 2; AAD17528)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="H -> L (in Ref. 3; CAB66533 and 5; CAG38507)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="N -> D (in Ref. 5; CAG38507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 22555 MW; 28B443F2E6D84493 CRC64;
MAQETNHSQV PMLCSTGCGF YGNPRTNGMC SVCYKEHLQR QNSSNGRISP PATSVSSLSE
SLPVQCTDGS VPEAQSALDS TSSSMQPSPV SNQSLLSESV ASSQLDSTSV DKAVPETEDV
QASVSDTAQQ PSEEQSKSLE KPKQKKNRCF MCRKKVGLTG FECRCGNVYC GVHRYSDVHN
CSYNYKADAA EKIRKENPVV VGEKIQKI
