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 Genevisible; Q68DK2; HS.
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.
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 3-phosphate-
FT 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
//
