ANCHR_HUMAN
ID ANCHR_HUMAN Reviewed; 471 AA.
AC Q96K21; B3KVB2; C9JNF4; H3BUF9; Q86WC2; Q8WU96;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Abscission/NoCut checkpoint regulator;
DE Short=ANCHR;
DE AltName: Full=MLL partner containing FYVE domain;
DE AltName: Full=Zinc finger FYVE domain-containing protein 19;
GN Name=ZFYVE19; Synonyms=ANCHR, MPFYVE;
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 2), CHROMOSOMAL TRANSLOCATION WITH
RP KMT2A/MLL1, AND TISSUE SPECIFICITY.
RX PubMed=12618766; DOI=10.1038/sj.onc.1206273;
RA Chinwalla V., Chien A., Odero M., Neilly M.B., Zeleznik-Le N.J.,
RA Rowley J.D.;
RT "A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene
RT MPFYVE on chromosome 15.";
RL Oncogene 22:1400-1410(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 19-471 (ISOFORM 1), AND VARIANT ALA-376.
RC TISSUE=Ovary, and Synovium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-471 (ISOFORM 3), AND VARIANT
RP ALA-376.
RC TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-286 (ISOFORM 3), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-243; SER-354 AND SER-463, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-293; SER-354 AND
RP SER-463, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, 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).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A, AND MUTAGENESIS OF
RP ARG-101.
RX PubMed=24814515; DOI=10.1038/ncb2959;
RA Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K.,
RA Andersen J.S., Raiborg C., Stenmark H.;
RT "ANCHR mediates Aurora-B-dependent abscission checkpoint control through
RT retention of VPS4.";
RL Nat. Cell Biol. 16:550-560(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-207, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-207, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Key regulator of abscission step in cytokinesis: part of the
CC cytokinesis checkpoint, a process required to delay abscission to
CC prevent both premature resolution of intercellular chromosome bridges
CC and accumulation of DNA damage. Together with CHMP4C, required to
CC retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody
CC ring until abscission checkpoint signaling is terminated at late
CC cytokinesis. Deactivation of AURKB results in dephosphorylation of
CC CHMP4C followed by its dissociation from ZFYVE19/ANCHR and VPS4 and
CC subsequent abscission. {ECO:0000269|PubMed:24814515}.
CC -!- SUBUNIT: Interacts (via MIM1-B) with VPS4A; interaction takes place at
CC the midbody ring following cytokinesis checkpoint activation.
CC {ECO:0000269|PubMed:24814515}.
CC -!- INTERACTION:
CC Q96K21; Q92870-2: APBB2; NbExp=3; IntAct=EBI-6448240, EBI-21535880;
CC Q96K21; Q7Z479: CAPN7; NbExp=3; IntAct=EBI-6448240, EBI-10213454;
CC Q96K21; Q9C005: DPY30; NbExp=3; IntAct=EBI-6448240, EBI-744973;
CC Q96K21; P04792: HSPB1; NbExp=3; IntAct=EBI-6448240, EBI-352682;
CC Q96K21; P42858: HTT; NbExp=21; IntAct=EBI-6448240, EBI-466029;
CC Q96K21; Q8WV92: MITD1; NbExp=6; IntAct=EBI-6448240, EBI-2691489;
CC Q96K21; O75351: VPS4B; NbExp=7; IntAct=EBI-6448240, EBI-2514459;
CC Q96K21-1; Q9UN37: VPS4A; NbExp=3; IntAct=EBI-16106990, EBI-1171942;
CC Q96K21-3; O15169: AXIN1; NbExp=3; IntAct=EBI-10187928, EBI-710484;
CC Q96K21-3; Q7Z479: CAPN7; NbExp=3; IntAct=EBI-10187928, EBI-10213454;
CC Q96K21-3; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-10187928, EBI-10175300;
CC Q96K21-3; Q8WV92: MITD1; NbExp=3; IntAct=EBI-10187928, EBI-2691489;
CC Q96K21-3; O75351: VPS4B; NbExp=3; IntAct=EBI-10187928, EBI-2514459;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:24814515}. Cleavage furrow
CC {ECO:0000269|PubMed:24814515}. Midbody, Midbody ring
CC {ECO:0000269|PubMed:24814515}. Note=Localizes mainly on centrosomes in
CC interphase and early mitosis. Localizes at the cleavage furrow and
CC midbody ring in late mitosis and cytokinesis.
CC {ECO:0000269|PubMed:24814515}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96K21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96K21-2; Sequence=VSP_013791;
CC Name=3;
CC IsoId=Q96K21-3; Sequence=VSP_013792;
CC Name=4;
CC IsoId=Q96K21-4; Sequence=VSP_046008;
CC -!- TISSUE SPECIFICITY: Detected in brain, heart, skeletal muscle, kidney
CC and liver. {ECO:0000269|PubMed:12618766}.
CC -!- DOMAIN: The FYVE-type zinc finger mediates binding to
CC phosphatidylinositol-3-phosphate (PtdIns(3)P).
CC {ECO:0000269|PubMed:24814515}.
CC -!- DOMAIN: The MIM1-B motif mediates interaction with VPS4A.
CC {ECO:0000269|PubMed:24814515}.
CC -!- DISEASE: Note=A chromosomal aberration involving ZFYVE19 is associated
CC with acute myeloblastic leukemia (AML). Translocation t(11;15)(q23;q14)
CC with KMT2A/MLL1 (PubMed:12618766). {ECO:0000269|PubMed:12618766}.
CC -!- CAUTION: Phosphorylated in vitro at Ser-22 by AURKB; however,
CC phosphorylation at this site could not be confirmed in vivo.
CC {ECO:0000305|PubMed:24814515}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21092.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO73862.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB55338.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF445414; AAO73862.1; ALT_FRAME; mRNA.
DR EMBL; AK027746; BAB55338.1; ALT_INIT; mRNA.
DR EMBL; AK122779; BAG53724.1; -; mRNA.
DR EMBL; AC012476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92451.1; -; Genomic_DNA.
DR EMBL; BC021092; AAH21092.1; ALT_INIT; mRNA.
DR CCDS; CCDS42025.1; -. [Q96K21-1]
DR CCDS; CCDS58353.1; -. [Q96K21-2]
DR CCDS; CCDS58354.1; -. [Q96K21-3]
DR CCDS; CCDS58355.1; -. [Q96K21-4]
DR RefSeq; NP_001070736.1; NM_001077268.1. [Q96K21-1]
DR RefSeq; NP_001245349.1; NM_001258420.1. [Q96K21-3]
DR RefSeq; NP_001245350.1; NM_001258421.1. [Q96K21-4]
DR RefSeq; NP_116239.3; NM_032850.4. [Q96K21-2]
DR AlphaFoldDB; Q96K21; -.
DR SMR; Q96K21; -.
DR BioGRID; 124370; 50.
DR DIP; DIP-60854N; -.
DR IntAct; Q96K21; 12.
DR STRING; 9606.ENSP00000347498; -.
DR GlyGen; Q96K21; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; Q96K21; -.
DR MetOSite; Q96K21; -.
DR PhosphoSitePlus; Q96K21; -.
DR BioMuta; ZFYVE19; -.
DR DMDM; 296453076; -.
DR EPD; Q96K21; -.
DR jPOST; Q96K21; -.
DR MassIVE; Q96K21; -.
DR MaxQB; Q96K21; -.
DR PaxDb; Q96K21; -.
DR PeptideAtlas; Q96K21; -.
DR PRIDE; Q96K21; -.
DR ProteomicsDB; 42921; -.
DR ProteomicsDB; 77031; -. [Q96K21-1]
DR ProteomicsDB; 77032; -. [Q96K21-2]
DR ProteomicsDB; 77033; -. [Q96K21-3]
DR Antibodypedia; 23171; 205 antibodies from 30 providers.
DR DNASU; 84936; -.
DR Ensembl; ENST00000299173.14; ENSP00000299173.10; ENSG00000166140.17. [Q96K21-3]
DR Ensembl; ENST00000336455.9; ENSP00000337824.5; ENSG00000166140.17. [Q96K21-2]
DR Ensembl; ENST00000355341.8; ENSP00000347498.4; ENSG00000166140.17. [Q96K21-1]
DR Ensembl; ENST00000564258.5; ENSP00000457617.1; ENSG00000166140.17. [Q96K21-4]
DR GeneID; 84936; -.
DR KEGG; hsa:84936; -.
DR MANE-Select; ENST00000355341.8; ENSP00000347498.4; NM_001077268.2; NP_001070736.1.
DR UCSC; uc001zmt.2; human. [Q96K21-1]
DR CTD; 84936; -.
DR DisGeNET; 84936; -.
DR GeneCards; ZFYVE19; -.
DR HGNC; HGNC:20758; ZFYVE19.
DR HPA; ENSG00000166140; Low tissue specificity.
DR MIM; 619635; gene.
DR neXtProt; NX_Q96K21; -.
DR OpenTargets; ENSG00000166140; -.
DR PharmGKB; PA134906967; -.
DR VEuPathDB; HostDB:ENSG00000166140; -.
DR eggNOG; KOG1818; Eukaryota.
DR GeneTree; ENSGT00390000016108; -.
DR HOGENOM; CLU_043234_1_0_1; -.
DR InParanoid; Q96K21; -.
DR OMA; CDGELFC; -.
DR OrthoDB; 1355078at2759; -.
DR PhylomeDB; Q96K21; -.
DR TreeFam; TF317652; -.
DR PathwayCommons; Q96K21; -.
DR SignaLink; Q96K21; -.
DR BioGRID-ORCS; 84936; 16 hits in 1082 CRISPR screens.
DR ChiTaRS; ZFYVE19; human.
DR GeneWiki; ZFYVE19; -.
DR GenomeRNAi; 84936; -.
DR Pharos; Q96K21; Tbio.
DR PRO; PR:Q96K21; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96K21; protein.
DR Bgee; ENSG00000166140; Expressed in lower esophagus mucosa and 139 other tissues.
DR ExpressionAtlas; Q96K21; baseline and differential.
DR Genevisible; Q96K21; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0009838; P:abscission; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; IMP:UniProtKB.
DR CDD; cd19817; Bbox1_ANCHR-like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044553; Bbox1_ANCHR.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromosomal rearrangement;
KW Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Lipid-binding;
KW Metal-binding; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..471
FT /note="Abscission/NoCut checkpoint regulator"
FT /id="PRO_0000098718"
FT ZN_FING 74..133
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 311..375
FT /evidence="ECO:0000255"
FT MOTIF 174..187
FT /note="MIM1-A"
FT MOTIF 326..339
FT /note="MIM1-B"
FT COMPBIAS 278..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT SITE 145..146
FT /note="Breakpoint for translocation to form KMT2A/MLL1-
FT ZFYVE19"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..175
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046008"
FT VAR_SEQ 1..93
FT /note="MNYDSQQPPLPPLPYAGCRRASGFPALGRGGTVPVGVWGGAGQGREGRSWGE
FT GPRGPGLGRRDLSSADPAVLGATMESRCYGCAVKFTLFKKE -> MPAVAEALGQEGPP
FT DLSRSAFLATVLTSLSAAFSSMPSSAYSLPFSRSLELDYHTSSCFRGTMVKADCPVPIT
FT DLPDSSGKLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12618766"
FT /id="VSP_013791"
FT VAR_SEQ 276..343
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013792"
FT VARIANT 210
FT /note="R -> H (in dbSNP:rs34819163)"
FT /id="VAR_057494"
FT VARIANT 376
FT /note="S -> A (in dbSNP:rs690347)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060474"
FT VARIANT 398
FT /note="R -> C (in dbSNP:rs72735636)"
FT /id="VAR_060475"
FT MUTAGEN 101
FT /note="R->A: Abolishes binding to phosphatidylinositol-3-
FT phosphate (PtdIns(3)P) without affecting localization to
FT the midbody."
FT /evidence="ECO:0000269|PubMed:24814515"
FT CONFLICT 104
FT /note="C -> R (in Ref. 5; AAH21092)"
FT /evidence="ECO:0000305"
FT MOD_RES Q96K21-3:286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
SQ SEQUENCE 471 AA; 51546 MW; 0F07D2DDFD19864D CRC64;
MNYDSQQPPL PPLPYAGCRR ASGFPALGRG GTVPVGVWGG AGQGREGRSW GEGPRGPGLG
RRDLSSADPA VLGATMESRC YGCAVKFTLF KKEYGCKNCG RAFCSGCLSF SAAVPRTGNT
QQKVCKQCHE VLTRGSSANA SKWSPPQNYK KRVAALEAKQ KPSTSQSQGL TRQDQMIAER
LARLRQENKP KLVPSQAEIE ARLAALKDER QGSIPSTQEM EARLAALQGR VLPSQTPQPA
HHTPDTRTQA QQTQDLLTQL AAEVAIDESW KGGGPAASLQ NDLNQGGPGS TNSKRQANWS
LEEEKSRLLA EAALELREEN TRQERILALA KRLAMLRGQD PERVTLQDYR LPDSDDDEDE
ETAIQRVLQQ LTEEASLDEA SGFNIPAEQA SRPWTQPRGA EPEAQDVDPR PEAEEEELPW
CCICNEDATL RCAGCDGDLF CARCFREGHD AFELKEHQTS AYSPPRAGQE H
