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 07-OCT-2020, entry version 144. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 Antibodypedia; 23171; 189 antibodies. 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 eggNOG; KOG1818; Eukaryota. DR GeneTree; ENSGT00390000016108; -. DR HOGENOM; CLU_043234_2_0_1; -. DR InParanoid; Q9DAZ9; -. DR OMA; FKKECGC; -. DR OrthoDB; 1355078at2759; -. DR TreeFam; TF317652; -. DR BioGRID-ORCS; 72008; 0 hits in 18 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 adult mammalian kidney and 302 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; ISS:UniProtKB. DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB. DR Gene3D; 3.30.40.10; -; 1. 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; Polymorphism; Reference proteome; Ubl conjugation; Zinc; KW 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 COILED 226..261 FT /evidence="ECO:0000255" FT MOTIF 99..112 FT /note="MIM1-A" FT MOTIF 252..265 FT /note="MIM1-B" FT COMPBIAS 332..335 FT /note="Poly-Glu" FT COMPBIAS 339..362 FT /note="Cys-rich" 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:0000244|PubMed:17242355, FT ECO:0000244|PubMed:19131326, ECO:0000244|PubMed:19144319, FT ECO:0000244|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:0000244|PDB:1WFK" FT STRAND 14..16 FT /evidence="ECO:0000244|PDB:1WFK" FT STRAND 18..20 FT /evidence="ECO:0000244|PDB:1WFK" FT STRAND 22..24 FT /evidence="ECO:0000244|PDB:1WFK" FT STRAND 27..29 FT /evidence="ECO:0000244|PDB:1WFK" FT TURN 30..32 FT /evidence="ECO:0000244|PDB:1WFK" FT STRAND 35..39 FT /evidence="ECO:0000244|PDB:1WFK" FT TURN 40..43 FT /evidence="ECO:0000244|PDB:1WFK" FT STRAND 44..49 FT /evidence="ECO:0000244|PDB:1WFK" FT HELIX 51..59 FT /evidence="ECO:0000244|PDB:1WFK" FT STRAND 66..68 FT /evidence="ECO:0000244|PDB:1WFK" FT TURN 340..342 FT /evidence="ECO:0000244|PDB:2D8V" FT STRAND 348..350 FT /evidence="ECO:0000244|PDB:2D8V" FT TURN 351..354 FT /evidence="ECO:0000244|PDB:2D8V" FT STRAND 355..358 FT /evidence="ECO:0000244|PDB:2D8V" FT HELIX 362..366 FT /evidence="ECO:0000244|PDB:2D8V" FT TURN 367..369 FT /evidence="ECO:0000244|PDB:2D8V" FT TURN 372..374 FT /evidence="ECO:0000244|PDB:2D8V" FT STRAND 383..386 FT /evidence="ECO:0000244|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 //