ANCHR_MOUSE
ID ANCHR_MOUSE Reviewed; 389 AA.
AC Q9DAZ9; A2AV55; Q8VCV7;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Abscission/NoCut checkpoint regulator;
DE Short=ANCHR;
DE AltName: Full=Zinc finger FYVE domain-containing protein 19;
GN Name=Zfyve19; Synonyms=Anchr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-157.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-64; GLN-91;
RP GLY-94; LEU-164 AND ALA-229.
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP STRUCTURE BY NMR OF 1-75 AND 336-389.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the FYVE domain and the B-box domain of the zinc
RT finger FYVE domain-containing protein 19 from Mus musculus.";
RL Submitted (JUN-2006) to the PDB data bank.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via MIM1-B) with VPS4A; interaction takes place at
CC the midbody ring following cytokinesis checkpoint activation.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q96K21}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q96K21}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q96K21}. 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:0000250|UniProtKB:Q96K21}.
CC -!- DOMAIN: The FYVE-type zinc finger mediates binding to
CC phosphatidylinositol-3-phosphate (PtdIns(3)P). {ECO:0000250}.
CC -!- DOMAIN: The MIM1-B motif mediates interaction with VPS4A.
CC {ECO:0000250}.
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DR EMBL; AK005386; BAB23993.1; -; mRNA.
DR EMBL; AL772264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018420; AAH18420.1; -; mRNA.
DR CCDS; CCDS16595.1; -.
DR RefSeq; NP_082330.2; NM_028054.3.
DR PDB; 1WFK; NMR; -; A=1-75.
DR PDB; 2D8V; NMR; -; A=336-389.
DR PDBsum; 1WFK; -.
DR PDBsum; 2D8V; -.
DR AlphaFoldDB; Q9DAZ9; -.
DR BMRB; Q9DAZ9; -.
DR SMR; Q9DAZ9; -.
DR BioGRID; 215091; 2.
DR STRING; 10090.ENSMUSP00000087636; -.
DR iPTMnet; Q9DAZ9; -.
DR PhosphoSitePlus; Q9DAZ9; -.
DR EPD; Q9DAZ9; -.
DR jPOST; Q9DAZ9; -.
DR MaxQB; Q9DAZ9; -.
DR PaxDb; Q9DAZ9; -.
DR PeptideAtlas; Q9DAZ9; -.
DR PRIDE; Q9DAZ9; -.
DR ProteomicsDB; 296408; -.
DR Antibodypedia; 23171; 205 antibodies from 30 providers.
DR Ensembl; ENSMUST00000090174; ENSMUSP00000087636; ENSMUSG00000068580.
DR GeneID; 72008; -.
DR KEGG; mmu:72008; -.
DR UCSC; uc008lti.2; mouse.
DR CTD; 84936; -.
DR MGI; MGI:1919258; Zfyve19.
DR VEuPathDB; HostDB:ENSMUSG00000068580; -.
DR eggNOG; KOG1818; Eukaryota.
DR GeneTree; ENSGT00390000016108; -.
DR HOGENOM; CLU_043234_2_0_1; -.
DR InParanoid; Q9DAZ9; -.
DR OMA; CDGELFC; -.
DR OrthoDB; 1355078at2759; -.
DR PhylomeDB; Q9DAZ9; -.
DR TreeFam; TF317652; -.
DR BioGRID-ORCS; 72008; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Zfyve19; mouse.
DR EvolutionaryTrace; Q9DAZ9; -.
DR PRO; PR:Q9DAZ9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DAZ9; protein.
DR Bgee; ENSMUSG00000068580; Expressed in crypt of Lieberkuhn of small intestine and 259 other tissues.
DR ExpressionAtlas; Q9DAZ9; baseline and differential.
DR Genevisible; Q9DAZ9; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS: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; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0009838; P:abscission; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS: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 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Lipid-binding; Metal-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..389
FT /note="Abscission/NoCut checkpoint regulator"
FT /id="PRO_0000098719"
FT ZN_FING 1..58
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 158..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..261
FT /evidence="ECO:0000255"
FT MOTIF 99..112
FT /note="MIM1-A"
FT MOTIF 252..265
FT /note="MIM1-B"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96K21"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96K21"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96K21"
FT VARIANT 64
FT /note="N -> S (in strain: FVB/N)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 91
FT /note="H -> Q (in strain: FVB/N)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 94
FT /note="S -> G (in strain: FVB/N)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 157
FT /note="P -> T (in strain: C57BL/6)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT VARIANT 164
FT /note="P -> L (in strain: FVB/N)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 229
FT /note="E -> A (in strain: FVB/N)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:1WFK"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1WFK"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1WFK"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1WFK"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1WFK"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1WFK"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1WFK"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1WFK"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1WFK"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:1WFK"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1WFK"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:2D8V"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:2D8V"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:2D8V"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:2D8V"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:2D8V"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:2D8V"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2D8V"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2D8V"
SQ SEQUENCE 389 AA; 43272 MW; 13AA752764AB17A1 CRC64;
MESRCYGCAV KFTLFKKEYG CKNCGRAFCN GCLSFSALVP RAGNTQQKVC KQCHTILTRG
SSDNASKWSP PQNYKKRVAA LEAKKKSSTS HSQSLTHKDQ AIAERLARLR QENKPKSVPS
QAEIEARLAA LKDEVQGPIP STQEMEDRLA ALQGRVPPSH TVRPAHQAPD TRTQAQQTQD
LLTQLTAEVA IDENCQPRAS ASLQNDLNKG AARSQRTNSQ GQASQSLEEE KYKLLAEAAV
ELQEENTRQE RILALAKRLA VLKGQDPSRV TLQDYHLPDS DEDEETAIQR VMQQLTEEAA
LDEASGFNIP EKPAPGSRAQ PCKAEMEGPQ AEEEELPWCC ICNEDATLRC AGCDGDLYCA
RCFREGHDNF DLKEHQTSPY HPRRPCQEH
