ID   ZFY26_HUMAN             Reviewed;        2539 AA.
AC   Q68DK2; B1B5Y3; B4E2U3; O15035; Q68DT9; Q6AW90; Q6ZR50; Q7Z3A4; Q7Z3I1;
AC   Q8N4W7; Q96H43;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2023, sequence version 4.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Zinc finger FYVE domain-containing protein 26;
DE   AltName: Full=FYVE domain-containing centrosomal protein;
DE            Short=FYVE-CENT;
DE   AltName: Full=Spastizin;
GN   Name=ZFYVE26; Synonyms=KIAA0321;
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), AND VARIANTS TYR-1457
RP   AND SER-1891.
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP   SER-1891.
RC   TISSUE=Trachea;
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 MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP   LEU-1103; TYR-1457 AND SER-1891.
RC   TISSUE=Cervix, Endometrial adenocarcinoma, and Fetal kidney;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2057-2539, AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 2155-2539 (ISOFORM 5).
RC   TISSUE=Brain, and Ovary;
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   [7]
RP   INVOLVEMENT IN SPG15, AND TISSUE SPECIFICITY.
RX   PubMed=18394578; DOI=10.1016/j.ajhg.2008.03.004;
RA   Hanein S., Martin E., Boukhris A., Byrne P., Goizet C., Hamri A.,
RA   Benomar A., Lossos A., Denora P., Fernandez J., Elleuch N., Forlani S.,
RA   Durr A., Feki I., Hutchinson M., Santorelli F.M., Mhiri C., Brice A.,
RA   Stevanin G.;
RT   "Identification of the SPG15 gene, encoding spastizin, as a frequent cause
RT   of complicated autosomal-recessive spastic paraplegia, including Kjellin
RT   syndrome.";
RL   Am. J. Hum. Genet. 82:992-1002(2008).
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   INVOLVEMENT IN SPG15.
RX   PubMed=19084844; DOI=10.1016/j.jns.2008.09.039;
RA   Denora P.S., Muglia M., Casali C., Truchetto J., Silvestri G., Messina D.,
RA   Boukrhis A., Magariello A., Modoni A., Masciullo M., Malandrini A.,
RA   Morelli M., de Leva M.F., Villanova M., Giugni E., Citrigno L., Rizza T.,
RA   Federico A., Pierallini A., Quattrone A., Filla A., Brice A., Stevanin G.,
RA   Santorelli F.M.;
RT   "Spastic paraplegia with thinning of the corpus callosum and white matter
RT   abnormalities: further mutations and relative frequency in ZFYVE26/SPG15 in
RT   the Italian population.";
RL   J. Neurol. Sci. 277:22-25(2009).
RN   [10]
RP   INVOLVEMENT IN SPG15.
RX   PubMed=19805727; DOI=10.1212/wnl.0b013e3181bacf59;
RA   Goizet C., Boukhris A., Maltete D., Guyant-Marechal L., Truchetto J.,
RA   Mundwiller E., Hanein S., Jonveaux P., Roelens F., Loureiro J., Godet E.,
RA   Forlani S., Melki J., Auer-Grumbach M., Fernandez J.C., Martin-Hardy P.,
RA   Sibon I., Sole G., Orignac I., Mhiri C., Coutinho P., Durr A., Brice A.,
RA   Stevanin G.;
RT   "SPG15 is the second most common cause of hereditary spastic paraplegia
RT   with thin corpus callosum.";
RL   Neurology 73:1111-1119(2009).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL 3-PHOSPHATE-BINDING,
RP   DOMAIN FYVE-TYPE ZINC-FINGER, INTERACTION WITH TTC19 AND KIF13A, AND
RP   MUTAGENESIS OF ARG-1836.
RX   PubMed=20208530; DOI=10.1038/ncb2036;
RA   Sagona A.P., Nezis I.P., Pedersen N.M., Liestol K., Poulton J.,
RA   Rusten T.E., Skotheim R.I., Raiborg C., Stenmark H.;
RT   "PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of
RT   FYVE-CENT to the midbody.";
RL   Nat. Cell Biol. 12:362-371(2010).
RN   [12]
RP   POSSIBLE FUNCTION, AND INTERACTION WITH AP5Z1; AP5B1; AP5S1 AND SPG11.
RX   PubMed=20613862; DOI=10.1371/journal.pbio.1000408;
RA   Slabicki M., Theis M., Krastev D.B., Samsonov S., Mundwiller E.,
RA   Junqueira M., Paszkowski-Rogacz M., Teyra J., Heninger A.K., Poser I.,
RA   Prieur F., Truchetto J., Confavreux C., Marelli C., Durr A.,
RA   Camdessanche J.P., Brice A., Shevchenko A., Pisabarro M.T., Stevanin G.,
RA   Buchholz F.;
RT   "A genome-scale DNA repair RNAi screen identifies SPG48 as a novel gene
RT   associated with hereditary spastic paraplegia.";
RL   PLoS Biol. 8:E1000408-E1000408(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-619; SER-703;
RP   SER-800 AND SER-1764, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [14]
RP   IDENTIFICATION BY 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   [15]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLU-1164 AND GLN-1945.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Phosphatidylinositol 3-phosphate-binding protein required for
CC       the abcission step in cytokinesis: recruited to the midbody during
CC       cytokinesis and acts as a regulator of abcission. May also be required
CC       for efficient homologous recombination DNA double-strand break repair.
CC       {ECO:0000269|PubMed:20208530}.
CC   -!- SUBUNIT: Interacts with AP5Z1, AP5B1, AP5S1 and SPG11. Interacts with
CC       TTC19 and KIF13A. {ECO:0000269|PubMed:20208530,
CC       ECO:0000269|PubMed:20613862}.
CC   -!- INTERACTION:
CC       Q68DK2-5; P13196: ALAS1; NbExp=3; IntAct=EBI-8656416, EBI-3905054;
CC       Q68DK2-5; Q8WXK1: ASB15; NbExp=3; IntAct=EBI-8656416, EBI-12809012;
CC       Q68DK2-5; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-8656416, EBI-11524851;
CC       Q68DK2-5; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-8656416, EBI-11977221;
CC       Q68DK2-5; Q9C0F1: CEP44; NbExp=6; IntAct=EBI-8656416, EBI-744115;
CC       Q68DK2-5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-8656416, EBI-618309;
CC       Q68DK2-5; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-8656416, EBI-473189;
CC       Q68DK2-5; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-8656416, EBI-2549423;
CC       Q68DK2-5; P07910: HNRNPC; NbExp=3; IntAct=EBI-8656416, EBI-357966;
CC       Q68DK2-5; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-8656416, EBI-10961706;
CC       Q68DK2-5; P19012: KRT15; NbExp=3; IntAct=EBI-8656416, EBI-739566;
CC       Q68DK2-5; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-8656416, EBI-3044087;
CC       Q68DK2-5; O76011: KRT34; NbExp=3; IntAct=EBI-8656416, EBI-1047093;
CC       Q68DK2-5; Q6A162: KRT40; NbExp=6; IntAct=EBI-8656416, EBI-10171697;
CC       Q68DK2-5; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-8656416, EBI-10172290;
CC       Q68DK2-5; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-8656416, EBI-10172052;
CC       Q68DK2-5; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-8656416, EBI-716006;
CC       Q68DK2-5; Q99750: MDFI; NbExp=7; IntAct=EBI-8656416, EBI-724076;
CC       Q68DK2-5; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-8656416, EBI-742388;
CC       Q68DK2-5; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-8656416, EBI-302345;
CC       Q68DK2-5; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-8656416, EBI-10171633;
CC       Q68DK2-5; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-8656416, EBI-710402;
CC       Q68DK2-5; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-8656416, EBI-11320284;
CC       Q68DK2-5; O75478: TADA2A; NbExp=3; IntAct=EBI-8656416, EBI-742268;
CC       Q68DK2-5; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-8656416, EBI-11955057;
CC       Q68DK2-5; P48775: TDO2; NbExp=6; IntAct=EBI-8656416, EBI-743494;
CC       Q68DK2-5; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-8656416, EBI-1105213;
CC       Q68DK2-5; Q13077: TRAF1; NbExp=3; IntAct=EBI-8656416, EBI-359224;
CC       Q68DK2-5; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-8656416, EBI-9090990;
CC       Q68DK2-5; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-8656416, EBI-739895;
CC       Q68DK2-5; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-8656416, EBI-14096082;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:20208530}. Midbody
CC       {ECO:0000269|PubMed:20208530}. Note=Localizes to the centrosome during
CC       all stages of the cell cycle. Recruited to the midbody during
CC       cytokinesis by KIF13A.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q68DK2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q68DK2-2; Sequence=VSP_030339;
CC       Name=4;
CC         IsoId=Q68DK2-4; Sequence=VSP_041049, VSP_041050;
CC       Name=3;
CC         IsoId=Q68DK2-3; Sequence=VSP_030338, VSP_030340, VSP_030341;
CC       Name=5;
CC         IsoId=Q68DK2-5; Sequence=VSP_058963, VSP_058964;
CC   -!- TISSUE SPECIFICITY: Strongest expression in the adrenal gland, bone
CC       marrow, adult brain, fetal brain, lung, placenta, prostate, skeletal
CC       muscle, testis, thymus, and retina. Intermediate levels are detected in
CC       other structures, including the spinal cord.
CC       {ECO:0000269|PubMed:18394578}.
CC   -!- DOMAIN: The FYVE-type zinc finger mediates binding to
CC       phosphatidylinositol 3-phosphate and recruitment to the midbody during
CC       cytokinesis. {ECO:0000269|PubMed:20208530}.
CC   -!- DISEASE: Spastic paraplegia 15, autosomal recessive (SPG15)
CC       [MIM:270700]: A form of spastic paraplegia, a neurodegenerative
CC       disorder characterized by a slow, gradual, progressive weakness and
CC       spasticity of the lower limbs. Rate of progression and the severity of
CC       symptoms are quite variable. Initial symptoms may include difficulty
CC       with balance, weakness and stiffness in the legs, muscle spasms, and
CC       dragging the toes when walking. In some forms of the disorder, bladder
CC       symptoms (such as incontinence) may appear, or the weakness and
CC       stiffness may spread to other parts of the body. SPG15 is a complex
CC       form associated with additional neurological symptoms such as cognitive
CC       deterioration or intellectual disability, axonal neuropathy, mild
CC       cerebellar signs, and, less frequently, a central hearing deficit,
CC       decreased visual acuity, or retinal degeneration.
CC       {ECO:0000269|PubMed:18394578, ECO:0000269|PubMed:19084844,
CC       ECO:0000269|PubMed:19805727}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG11658.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD97882.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB002319; BAA20779.1; -; mRNA.
DR   EMBL; AB425197; BAG11658.1; ALT_INIT; mRNA.
DR   EMBL; AK304428; BAG65255.1; -; mRNA.
DR   EMBL; AK128496; BAC87467.1; -; mRNA.
DR   EMBL; BX537886; CAD97882.1; ALT_SEQ; mRNA.
DR   EMBL; BX538025; CAD97971.1; -; mRNA.
DR   EMBL; BX648683; CAH10379.1; -; mRNA.
DR   EMBL; CR749276; CAH18131.1; -; mRNA.
DR   EMBL; CR749365; CAH18218.1; -; mRNA.
DR   EMBL; AL049779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL121595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471061; EAW80954.1; -; Genomic_DNA.
DR   EMBL; BC008927; AAH08927.2; -; mRNA.
DR   EMBL; BC033235; AAH33235.2; -; mRNA.
DR   CCDS; CCDS9788.1; -. [Q68DK2-1]
DR   RefSeq; NP_056161.2; NM_015346.3. [Q68DK2-1]
DR   AlphaFoldDB; Q68DK2; -.
DR   BioGRID; 117050; 53.
DR   CORUM; Q68DK2; -.
DR   IntAct; Q68DK2; 42.
DR   MINT; Q68DK2; -.
DR   STRING; 9606.ENSP00000251119; -.
DR   iPTMnet; Q68DK2; -.
DR   PhosphoSitePlus; Q68DK2; -.
DR   BioMuta; ZFYVE26; -.
DR   DMDM; 296453077; -.
DR   EPD; Q68DK2; -.
DR   jPOST; Q68DK2; -.
DR   MassIVE; Q68DK2; -.
DR   MaxQB; Q68DK2; -.
DR   PaxDb; 9606-ENSP00000251119; -.
DR   PeptideAtlas; Q68DK2; -.
DR   ProteomicsDB; 66082; -. [Q68DK2-1]
DR   ProteomicsDB; 66083; -. [Q68DK2-2]
DR   ProteomicsDB; 66084; -. [Q68DK2-3]
DR   ProteomicsDB; 66085; -. [Q68DK2-4]
DR   ProteomicsDB; 76701; -.
DR   Pumba; Q68DK2; -.
DR   Antibodypedia; 24903; 95 antibodies from 26 providers.
DR   DNASU; 23503; -.
DR   Ensembl; ENST00000347230.9; ENSP00000251119.5; ENSG00000072121.17. [Q68DK2-1]
DR   GeneID; 23503; -.
DR   KEGG; hsa:23503; -.
DR   MANE-Select; ENST00000347230.9; ENSP00000251119.5; NM_015346.4; NP_056161.2.
DR   UCSC; uc001xka.2; human. [Q68DK2-1]
DR   UCSC; uc001xkb.4; human.
DR   AGR; HGNC:20761; -.
DR   CTD; 23503; -.
DR   DisGeNET; 23503; -.
DR   GeneCards; ZFYVE26; -.
DR   GeneReviews; ZFYVE26; -.
DR   HGNC; HGNC:20761; ZFYVE26.
DR   HPA; ENSG00000072121; Low tissue specificity.
DR   MalaCards; ZFYVE26; -.
DR   MIM; 270700; phenotype.
DR   MIM; 612012; gene.
DR   neXtProt; NX_Q68DK2; -.
DR   OpenTargets; ENSG00000072121; -.
DR   Orphanet; 100996; Autosomal recessive spastic paraplegia type 15.
DR   PharmGKB; PA134904455; -.
DR   VEuPathDB; HostDB:ENSG00000072121; -.
DR   eggNOG; KOG1811; Eukaryota.
DR   GeneTree; ENSGT00920000149143; -.
DR   HOGENOM; CLU_228199_0_0_1; -.
DR   InParanoid; Q68DK2; -.
DR   OrthoDB; 2945465at2759; -.
DR   PhylomeDB; Q68DK2; -.
DR   TreeFam; TF324517; -.
DR   PathwayCommons; Q68DK2; -.
DR   SignaLink; Q68DK2; -.
DR   SIGNOR; Q68DK2; -.
DR   BioGRID-ORCS; 23503; 16 hits in 1159 CRISPR screens.
DR   ChiTaRS; ZFYVE26; human.
DR   GenomeRNAi; 23503; -.
DR   Pharos; Q68DK2; Tbio.
DR   PRO; PR:Q68DK2; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q68DK2; Protein.
DR   Bgee; ENSG00000072121; Expressed in sural nerve and 203 other cell types or tissues.
DR   ExpressionAtlas; Q68DK2; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0005770; C:late endosome; IDA:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
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:0019901; F:protein kinase binding; IDA:MGI.
DR   GO; GO:1905037; P:autophagosome organization; IDA:MGI.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR   GO; GO:0007040; P:lysosome organization; IDA:MGI.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR   GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR   CDD; cd15724; FYVE_ZFY26; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR028730; ZFYVE26.
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   PANTHER; PTHR46591; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 26; 1.
DR   PANTHER; PTHR46591:SF1; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 26; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   Genevisible; Q68DK2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; DNA damage; DNA repair; Hereditary spastic paraplegia;
KW   Lipid-binding; Metal-binding; Neurodegeneration; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..2539
FT                   /note="Zinc finger FYVE domain-containing protein 26"
FT                   /id="PRO_0000314612"
FT   ZN_FING         1812..1872
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          594..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1267..1296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1754..1808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          868..895
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        706..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..757
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1268..1296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1818
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1821
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1835
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1838
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1843
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1846
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1864
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1867
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         615
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D4A8G9"
FT   MOD_RES         619
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         703
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         800
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1742
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT   MOD_RES         1764
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1780
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT   MOD_RES         1782
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT   VAR_SEQ         1..1809
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030338"
FT   VAR_SEQ         203..223
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_030339"
FT   VAR_SEQ         778..791
FT                   /note="DGRDRGSNPSLEST -> GNLKSSFPCTRQVV (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041049"
FT   VAR_SEQ         792..2539
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041050"
FT   VAR_SEQ         1810..1828
FT                   /note="VPDETESICMVCCREHFTM -> MAISPSLLPLSSPPDGIPQ (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030340"
FT   VAR_SEQ         2473..2539
FT                   /note="VRAYLICCKLRSAYLIAVKQEHSRATALVQQVQQAAKSSGDAVVQDICAQWL
FT                   LTSHPRGAHGPGSRK -> IVPILAALRDRVHTEERGRSPSTLC (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030341"
FT   VAR_SEQ         2474..2481
FT                   /note="RAYLICCK -> SGIVSKRW (in isoform 5)"
FT                   /id="VSP_058963"
FT   VAR_SEQ         2482..2539
FT                   /note="Missing (in isoform 5)"
FT                   /id="VSP_058964"
FT   VARIANT         429
FT                   /note="K -> E (in dbSNP:rs34059852)"
FT                   /id="VAR_037987"
FT   VARIANT         898
FT                   /note="T -> S (in dbSNP:rs17192170)"
FT                   /id="VAR_037988"
FT   VARIANT         951
FT                   /note="T -> M (in dbSNP:rs35471427)"
FT                   /id="VAR_037989"
FT   VARIANT         1071
FT                   /note="S -> N (in dbSNP:rs7156206)"
FT                   /id="VAR_037990"
FT   VARIANT         1103
FT                   /note="P -> L (in dbSNP:rs3742885)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_037991"
FT   VARIANT         1122
FT                   /note="A -> V (in dbSNP:rs3742884)"
FT                   /id="VAR_037992"
FT   VARIANT         1164
FT                   /note="A -> E (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_037993"
FT   VARIANT         1457
FT                   /note="C -> Y (in dbSNP:rs2235967)"
FT                   /evidence="ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|PubMed:9205841"
FT                   /id="VAR_037994"
FT   VARIANT         1891
FT                   /note="N -> S (in dbSNP:rs3742883)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:9205841"
FT                   /id="VAR_037995"
FT   VARIANT         1945
FT                   /note="R -> Q (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs200595749)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_037996"
FT   VARIANT         2411
FT                   /note="R -> H (in dbSNP:rs34373049)"
FT                   /id="VAR_037997"
FT   MUTAGEN         1836
FT                   /note="R->A: Abolishes phosphatidylinositol
FT                   3-phosphate-binding and localization to the midbody."
FT                   /evidence="ECO:0000269|PubMed:20208530"
FT   CONFLICT        243
FT                   /note="L -> P (in Ref. 3; CAD97882)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        556
FT                   /note="L -> P (in Ref. 1; BAG11658)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        586
FT                   /note="S -> P (in Ref. 3; CAH18131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        629
FT                   /note="K -> E (in Ref. 3; CAH18131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        946
FT                   /note="D -> G (in Ref. 3; CAH18218)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1040
FT                   /note="S -> T (in Ref. 1; BAG11658)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1115
FT                   /note="A -> T (in Ref. 3; CAH18131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1320
FT                   /note="C -> S (in Ref. 3; CAH18218)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1358
FT                   /note="R -> H (in Ref. 3; CAH18131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1556
FT                   /note="E -> V (in Ref. 3; CAH18131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1597
FT                   /note="A -> T (in Ref. 3; CAH10379)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1615
FT                   /note="E -> K (in Ref. 3; CAH10379)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1670
FT                   /note="S -> N (in Ref. 3; CAH18218)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1727
FT                   /note="K -> R (in Ref. 3; CAH10379)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1774
FT                   /note="G -> D (in Ref. 3; CAD97882)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2246
FT                   /note="Q -> L (in Ref. 3; CAH18131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2288
FT                   /note="K -> R (in Ref. 3; CAD97882)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2434
FT                   /note="M -> L (in Ref. 6; AAH33235)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2539 AA;  284603 MW;  85484EB6BACC8566 CRC64;
     MNHPFGKEEA ASQKQLFGFF CECLRRGEWE LAQACVPQLQ EGQGDIPKRV EDILQALVVC
     PNLLRCGQDI NPQRVAWVWL LVLEKWLARE KKLLPVVFRR KLEFLLLSED LQGDIPENIL
     EELYETLTQG AVGHVPDGNP RRESWTPRLS SEAVSVLWDL LRQSPQPAQA LLELLLEEDD
     GTGLCHWPLQ NALVDLIRKA LRALQGPDSV PPGVVDAIYG ALRTLRCPAE PLGVELHLLC
     EELLEACRTE GSPLREERLL SCLLHKASRG LLSLYGHTYA EKVTEKPPRA TASGKVSPDH
     LDPERAMLAL FSNPNPAEAW KVAYFYCLSN NKHFLEQILV TALTLLKEED FPNLGCLLDR
     EFRPLSCLLV LLGWTHCQSL ESAKRLLQTL HRTQGPGCDE LLRDACDGLW AHLEVLEWCI
     QQSSNPIPKR DLLYHLHGGD SHSVLYTLHH LTNLPALREE DVLKLLQKVP AKDPQQEPDA
     VDAPVPEHLS QCQNLTLYQG FCAMKYAIYA LCVNSHQHSQ CQDCKDSLSE DLASATEPAN
     DSLSSPGAAN LFSTYLARCQ QYLCSIPDSL CLELLENIFS LLLITSADLH PEPHLPEDYA
     EDDDIEGKSP SGLRSPSESP QHIAHPERKS ERGSLGVPKT LAYTMPSHVK AEPKDSYPGP
     HRHSFLDLKH FTSGISGFLA DEFAIGAFLR LLQEQLDEIS SRSPPEKPKQ ESQSCSGSRD
     GLQSRLHRLS KVVSEAQWRH KVVTSNHRSE EQPSRRYQPA TRHPSLRRGR RTRRSQADGR
     DRGSNPSLES TSSELSTSTS EGSLSAMSGR NELHSRLHPH PQSSLIPMMF SPPESLLASC
     ILRGNFAEAH QVLFTFNLKS SPSSGELMFM ERYQEVIQEL AQVEHKIENQ NSDAGSSTIR
     RTGSGRSTLQ AIGSAAAAGM VFYSISDVTD KLLNTSGDPI PMLQEDFWIS TALVEPTAPL
     REVLEDLSPP AMAAFDLACS QCQLWKTCKQ LLETAERRLN SSLERRGRRI DHVLLNADGI
     RGFPVVLQQI SKSLNYLLMS ASQTKSESVE EKGGGPPRCS ITELLQMCWP SLSEDCVASH
     TTLSQQLDQV LQSLREALEL PEPRTPPLSS LVEQAAQKAP EAEAHPVQIQ TQLLQKNLGK
     QTPSGSRQMD YLGTFFSYCS TLAAVLLQSL SSEPDHVEVK VGNPFVLLQQ SSSQLVSHLL
     FERQVPPERL AALLAQENLS LSVPQVIVSC CCEPLALCSS RQSQQTSSLL TRLGTLAQLH
     ASHCLDDLPL STPSSPRTTE NPTLERKPYS SPRDSSLPAL TSSALAFLKS RSKLLATVAC
     LGASPRLKVS KPSLSWKELR GRREVPLAAE QVARECERLL EQFPLFEAFL LAAWEPLRGS
     LQQGQSLAVN LCGWASLSTV LLGLHSPIAL DVLSEAFEES LVARDWSRAL QLTEVYGRDV
     DDLSSIKDAV LSCAVACDKE GWQYLFPVKD ASLRSRLALQ FVDRWPLESC LEILAYCISD
     TAVQEGLKCE LQRKLAELQV YQKILGLQSP PVWCDWQTLR SCCVEDPSTV MNMILEAQEY
     ELCEEWGCLY PIPREHLISL HQKHLLHLLE RRDHDKALQL LRRIPDPTMC LEVTEQSLDQ
     HTSLATSHFL ANYLTTHFYG QLTAVRHREI QALYVGSKIL LTLPEQHRAS YSHLSSNPLF
     MLEQLLMNMK VDWATVAVQT LQQLLVGQEI GFTMDEVDSL LSRYAEKALD FPYPQREKRS
     DSVIHLQEIV HQAADPETLP RSPSAEFSPA APPGISSIHS PSLRERSFPP TQPSQEFVPP
     ATPPARHQWV PDETESICMV CCREHFTMFN RRHHCRRCGR LVCSSCSTKK MVVEGCRENP
     ARVCDQCYSY CNKDVPEEPS EKPEALDSSK NESPPYSFVV RVPKADEVEW ILDLKEEENE
     LVRSEFYYEQ APSASLCIAI LNLHRDSIAC GHQLIEHCCR LSKGLTNPEV DAGLLTDIMK
     QLLFSAKMMF VKAGQSQDLA LCDSYISKVD VLNILVAAAY RHVPSLDQIL QPAAVTRLRN
     QLLEAEYYQL GVEVSTKTGL DTTGAWHAWG MACLKAGNLT AAREKFSRCL KPPFDLNQLN
     HGSRLVQDVV EYLESTVRPF VSLQDDDYFA TLRELEATLR TQSLSLAVIP EGKIMNNTYY
     QECLFYLHNY STNLAIISFY VRHSCLREAL LHLLNKESPP EVFIEGIFQP SYKSGKLHTL
     ENLLESIDPT LESWGKYLIA ACQHLQKKNY YHILYELQQF MKDQVRAAMT CIRFFSHKAK
     SYTELGEKLS WLLKAKDHLK IYLQETSRSS GRKKTTFFRK KMTAADVSRH MNTLQLQMEV
     TRFLHRCESA GTSQITTLPL PTLFGNNHMK MDVACKVMLG GKNVEDGFGI AFRVLQDFQL
     DAAMTYCRAA RQLVEKEKYS EIQQLLKCVS ESGMAAKSDG DTILLNCLEA FKRIPPQELE
     GLIQAIHNDD NKVRAYLICC KLRSAYLIAV KQEHSRATAL VQQVQQAAKS SGDAVVQDIC
     AQWLLTSHPR GAHGPGSRK
//