ZFAN1_HUMAN
ID ZFAN1_HUMAN Reviewed; 268 AA.
AC Q8TCF1; E5RIG0; E5RJ99; Q658R7; Q6IA32; Q6PGQ6; Q9H810;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=AN1-type zinc finger protein 1 {ECO:0000305};
DE AltName: Full=Zinc finger AN1-type-containing protein 1 {ECO:0000305};
GN Name=ZFAND1 {ECO:0000312|HGNC:HGNC:25858};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Colon;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 72-268 (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, INTERACTION WITH 26S PROTEASOME, INTERACTION WITH PSMA1; PSMC4;
RP PSMD1 AND VCP, SUBCELLULAR LOCATION, AND REGION UBIQUITIN-LIKE DOMAIN.
RX PubMed=29804830; DOI=10.1016/j.molcel.2018.04.021;
RA Turakhiya A., Meyer S.R., Marincola G., Boehm S., Vanselow J.T.,
RA Schlosser A., Hofmann K., Buchberger A.;
RT "ZFAND1 recruits p97 and the 26S proteasome to promote the clearance of
RT arsenite-induced stress granules.";
RL Mol. Cell 70:906-919(2018).
CC -!- FUNCTION: Plays a role in the regulation of cytoplasmic stress granules
CC (SGs) turnover. SGs are dynamic and transient cytoplasmic
CC ribonucleoprotein assemblies important for cellular protein homeostasis
CC when protein production is suspended after acute exogenous stress
CC (PubMed:29804830). Associates with SGs and is involved in the efficient
CC and specific arsenite-induced clearance process of SGs through the
CC recruitment of the ubiquitin-selective ATPase VCP and the 26S
CC proteasome (PubMed:29804830). This process requires both complexes for
CC efficient degradation of damaged ubiquitinated SG proteins during
CC recovery from arsenite stress, and hence avoiding aberrant cytoplasmic
CC SGs degradation via autophagy (PubMed:29804830).
CC {ECO:0000269|PubMed:29804830}.
CC -!- SUBUNIT: Associates with the 26S proteasome; this association occurs
CC upon exposure to arsenite and is reduced in the presence of ATP
CC (PubMed:29804830). Interacts (via AN1-type 1 and 2 zinc fingers) with
CC PSMD1; this interaction is increased upon arsenite treatment and occurs
CC in an ATP-independent manner (PubMed:29804830). Interacts with PSMC4
CC (PubMed:29804830). Interacts with PSMA1 (PubMed:29804830). Interacts
CC (via its ubiquitin-like region) with VCP; this interaction occurs in an
CC arsenite-dependent manner and is necessary for the recruitment of the
CC ubiquitin-selective ATPase VCP to stress granules (SGs)
CC (PubMed:29804830). {ECO:0000269|PubMed:29804830}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:29804830}. Note=Colocalizes with TIA1, G3BP1, VCP
CC and 26S proteasome in cytoplasmic stress granules (SGs) in response to
CC arsenite-induced stress treatment in a VCP-independent manner
CC (PubMed:29804830). Not localized in SGs in response to other
CC heat- oxidative- or osmotic-induced stress treatments. Colocalizes with
CC VCP in cytoplasmic speckles (PubMed:29804830).
CC {ECO:0000269|PubMed:29804830}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TCF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCF1-2; Sequence=VSP_014988;
CC Name=3;
CC IsoId=Q8TCF1-3; Sequence=VSP_046404;
CC Name=4;
CC IsoId=Q8TCF1-4; Sequence=VSP_054080, VSP_054081;
CC -!- DOMAIN: The ubiquitin-like region is necessary for its localization to
CC stress granules (SGs) in a VCP-independent manner (PubMed:29804830).
CC The AN1-type 1 and 2 zinc finger domains are necessary for the
CC recruitment of the 26S proteasome to SGs (PubMed:29804830). Both the
CC AN1-type 1 and 2 zinc finger domains and the ubiquitin-like region are
CC necessary for efficient SGs clearance upon specific arsenite-induced
CC responses (PubMed:29804830). {ECO:0000269|PubMed:29804830}.
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DR EMBL; AK024069; BAB14813.1; -; mRNA.
DR EMBL; CR457323; CAG33604.1; -; mRNA.
DR EMBL; AK225195; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC132219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022251; AAH22251.1; -; mRNA.
DR EMBL; BC056877; AAH56877.1; -; mRNA.
DR EMBL; AL833030; CAH56344.1; -; mRNA.
DR CCDS; CCDS55250.1; -. [Q8TCF1-4]
DR CCDS; CCDS55251.1; -. [Q8TCF1-3]
DR CCDS; CCDS6232.1; -. [Q8TCF1-1]
DR RefSeq; NP_001164267.1; NM_001170796.1. [Q8TCF1-3]
DR RefSeq; NP_001164268.1; NM_001170797.1. [Q8TCF1-4]
DR RefSeq; NP_078975.2; NM_024699.2. [Q8TCF1-1]
DR AlphaFoldDB; Q8TCF1; -.
DR SMR; Q8TCF1; -.
DR BioGRID; 122863; 13.
DR IntAct; Q8TCF1; 3.
DR MINT; Q8TCF1; -.
DR STRING; 9606.ENSP00000220669; -.
DR iPTMnet; Q8TCF1; -.
DR PhosphoSitePlus; Q8TCF1; -.
DR BioMuta; ZFAND1; -.
DR DMDM; 73622102; -.
DR EPD; Q8TCF1; -.
DR jPOST; Q8TCF1; -.
DR MassIVE; Q8TCF1; -.
DR MaxQB; Q8TCF1; -.
DR PaxDb; Q8TCF1; -.
DR PeptideAtlas; Q8TCF1; -.
DR PRIDE; Q8TCF1; -.
DR ProteomicsDB; 16275; -.
DR ProteomicsDB; 16535; -.
DR ProteomicsDB; 74130; -. [Q8TCF1-1]
DR ProteomicsDB; 74131; -. [Q8TCF1-2]
DR Antibodypedia; 12557; 25 antibodies from 11 providers.
DR DNASU; 79752; -.
DR Ensembl; ENST00000220669.10; ENSP00000220669.5; ENSG00000104231.11. [Q8TCF1-1]
DR Ensembl; ENST00000519523.5; ENSP00000429167.1; ENSG00000104231.11. [Q8TCF1-4]
DR Ensembl; ENST00000521287.5; ENSP00000428139.1; ENSG00000104231.11. [Q8TCF1-2]
DR Ensembl; ENST00000522520.5; ENSP00000429999.1; ENSG00000104231.11. [Q8TCF1-2]
DR Ensembl; ENST00000523096.5; ENSP00000430736.1; ENSG00000104231.11. [Q8TCF1-3]
DR GeneID; 79752; -.
DR KEGG; hsa:79752; -.
DR MANE-Select; ENST00000220669.10; ENSP00000220669.5; NM_024699.3; NP_078975.2.
DR UCSC; uc003ycj.3; human. [Q8TCF1-1]
DR CTD; 79752; -.
DR DisGeNET; 79752; -.
DR GeneCards; ZFAND1; -.
DR HGNC; HGNC:25858; ZFAND1.
DR HPA; ENSG00000104231; Low tissue specificity.
DR neXtProt; NX_Q8TCF1; -.
DR OpenTargets; ENSG00000104231; -.
DR PharmGKB; PA142670532; -.
DR VEuPathDB; HostDB:ENSG00000104231; -.
DR eggNOG; KOG3183; Eukaryota.
DR GeneTree; ENSGT00730000111180; -.
DR HOGENOM; CLU_052358_0_0_1; -.
DR InParanoid; Q8TCF1; -.
DR OMA; EAIGAHC; -.
DR OrthoDB; 1422113at2759; -.
DR PhylomeDB; Q8TCF1; -.
DR TreeFam; TF314219; -.
DR PathwayCommons; Q8TCF1; -.
DR SignaLink; Q8TCF1; -.
DR BioGRID-ORCS; 79752; 20 hits in 1074 CRISPR screens.
DR ChiTaRS; ZFAND1; human.
DR GenomeRNAi; 79752; -.
DR Pharos; Q8TCF1; Tbio.
DR PRO; PR:Q8TCF1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8TCF1; protein.
DR Bgee; ENSG00000104231; Expressed in body of pancreas and 197 other tissues.
DR ExpressionAtlas; Q8TCF1; baseline and differential.
DR Genevisible; Q8TCF1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1903843; P:cellular response to arsenite ion; IMP:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0035617; P:stress granule disassembly; IMP:UniProtKB.
DR Gene3D; 4.10.1110.10; -; 2.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF01428; zf-AN1; 2.
DR SMART; SM00154; ZnF_AN1; 2.
DR SUPFAM; SSF118310; SSF118310; 2.
DR PROSITE; PS51039; ZF_AN1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..268
FT /note="AN1-type zinc finger protein 1"
FT /id="PRO_0000066580"
FT ZN_FING 4..52
FT /note="AN1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT ZN_FING 58..106
FT /note="AN1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 160..260
FT /note="ubiquitin-like"
FT /evidence="ECO:0000303|PubMed:29804830"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014988"
FT VAR_SEQ 160..166
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_046404"
FT VAR_SEQ 213..227
FT /note="KLRLCHITSGEALPL -> VTSHYNNISILIKVL (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054080"
FT VAR_SEQ 228..268
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054081"
FT CONFLICT 182
FT /note="F -> L (in Ref. 1; BAB14813)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> T (in Ref. 6; CAH56344)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="E -> D (in Ref. 2; CAG33604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 30787 MW; EE554E5D7455F111 CRC64;
MAELDIGQHC QVEHCRQRDF LPFVCDDCSG IFCLEHRSRE SHGCPEVTVI NERLKTDQHT
SYPCSFKDCA ERELVAVICP YCEKNFCLRH RHQSDHECEK LEIPKPRMAA TQKLVKDIID
SKTGETASKR WKGAKNSETA AKVALMKLKM HADGDKSLPQ TERIYFQVFL PKGSKEKSKP
MFFCHRWSIG KAIDFAASLA RLKNDNNKFT AKKLRLCHIT SGEALPLDHT LETWIAKEDC
PLYNGGNIIL EYLNDEEQFC KNVESYLE
