ID VP13B_HUMAN Reviewed; 4022 AA. AC Q7Z7G8; C9JD30; Q709C6; Q709C7; Q7Z7G4; Q7Z7G5; Q7Z7G6; Q7Z7G7; Q8NB77; AC Q9NWV1; Q9Y4E7; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 2. DT 27-MAR-2024, entry version 160. DE RecName: Full=Intermembrane lipid transfer protein VPS13B {ECO:0000305}; DE AltName: Full=Cohen syndrome protein 1; DE AltName: Full=Vacuolar protein sorting-associated protein 13B; GN Name=VPS13B; Synonyms=CHS1, COH1, KIAA0532; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE SPECIFICITY, RP VARIANT 413-TYR--LEU-415 DEL (ISOFORM 5), AND VARIANT COH1 ARG-2193. RC TISSUE=Lymphoblast; RX PubMed=12730828; DOI=10.1086/375454; RA Kolehmainen J., Black G.C.M., Saarinen A., Chandler K., Clayton-Smith J., RA Traeskelin A.-L., Perveen R., Kivitie-Kallio S., Norio R., Warburg M., RA Fryns J.-P., de la Chapelle A., Lehesjoki A.-E.; RT "Cohen syndrome is caused by mutations in a novel gene, COH1, encoding a RT transmembrane protein with a presumed role in vesicle-mediated sorting and RT intracellular protein transport."; RL Am. J. Hum. Genet. 72:1359-1369(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lymphoblast; RX PubMed=15498460; DOI=10.1016/j.ygeno.2004.04.012; RA Velayos-Baeza A., Vettori A., Copley R.R., Dobson-Stone C., Monaco A.P.; RT "Analysis of the human VPS13 gene family."; RL Genomics 84:536-549(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 518-1522 (ISOFORM 6), AND VARIANT 413-TYR--LEU-415 RP DEL (ISOFORM 5). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2386-4022. RC TISSUE=Brain; RX PubMed=9628581; DOI=10.1093/dnares/5.1.31; RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., RA Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. IX. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:31-39(1998). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414; SER-999; SER-1002; RP SER-1033 AND SER-1815, 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 [8] RP FUNCTION, INTERACTION WITH RAB6A AND RAB6B, AND SUBCELLULAR LOCATION. RX PubMed=25492866; DOI=10.1074/jbc.m114.608174; RA Seifert W., Kuehnisch J., Maritzen T., Lommatzsch S., Hennies H.C., RA Bachmann S., Horn D., Haucke V.; RT "Cohen syndrome-associated protein COH1 physically and functionally RT interacts with the small GTPase RAB6 at the Golgi complex and directs RT neurite outgrowth."; RL J. Biol. Chem. 290:3349-3358(2015). RN [9] RP FUNCTION. RX PubMed=30962439; DOI=10.1038/s41467-019-09617-9; RA Koike S., Jahn R.; RT "SNAREs define targeting specificity of trafficking vesicles by RT combinatorial interaction with tethering factors."; RL Nat. Commun. 10:1608-1608(2019). RN [10] RP FUNCTION. RX PubMed=32375900; DOI=10.1186/s13041-020-00611-7; RA Lee Y.K., Lee S.K., Choi S., Huh Y.H., Kwak J.H., Lee Y.S., Jang D.J., RA Lee J.H., Lee K., Kaang B.K., Lim C.S., Lee J.A.; RT "Autophagy pathway upregulation in a human iPSC-derived neuronal model of RT Cohen syndrome with VPS13B missense mutations."; RL Mol. Brain 13:69-69(2020). RN [11] RP VARIANT COH1 SER-2993. RX PubMed=15141358; DOI=10.1086/422197; RA Kolehmainen J., Wilkinson R., Lehesjoki A.-E., Chandler K., RA Kivitie-Kallio S., Clayton-Smith J., Traeskelin A.-L., Waris L., RA Saarinen A., Khan J., Gross-Tsur V., Traboulsi E.I., Warburg M., RA Fryns J.-P., Norio R., Black G.C.M., Manson F.D.C.; RT "Delineation of Cohen syndrome following a large-scale genotype-phenotype RT screen."; RL Am. J. Hum. Genet. 75:122-127(2004). RN [12] RP VARIANTS COH1 CYS-2341 AND ASP-2645. RX PubMed=15154116; DOI=10.1086/422219; RA Hennies H.C., Rauch A., Seifert W., Schumi C., Moser E., Al-Taji E., RA Tariverdian G., Chrzanowska K.H., Krajewska-Walasek M., Rajab A., RA Giugliani R., Neumann T.E., Eckl K.M., Karbasiyan M., Reis A., Horn D.; RT "Allelic heterogeneity in the COH1 gene explains clinical variability in RT Cohen syndrome."; RL Am. J. Hum. Genet. 75:138-145(2004). RN [13] RP VARIANT COH1 THR-2820. RX PubMed=15211651; DOI=10.1002/ajmg.a.30033; RA Falk M.J., Feiler H.S., Neilson D.E., Maxwell K., Lee J.V., Segall S.K., RA Robin N.H., Wilhelmsen K.C., Traeskelin A.-L., Kolehmainen J., RA Lehesjoki A.-E., Wiznitzer M., Warman M.L.; RT "Cohen syndrome in the Ohio Amish."; RL Am. J. Med. Genet. A 128:23-28(2004). RN [14] RP VARIANTS COH1 1739-GLU--GLN-1744 DEL AND LEU-2773, AND VARIANTS THR-829; RP ILE-866; VAL-1994; CYS-2822 AND ARG-3142. RX PubMed=16648375; DOI=10.1136/jmg.2005.039867; RA Seifert W., Holder-Espinasse M., Spranger S., Hoeltzenbein M., Rossier E., RA Dollfus H., Lacombe D., Verloes A., Chrzanowska K.H., Maegawa G.H.B., RA Chitayat D., Kotzot D., Huhle D., Meinecke P., Albrecht B., Mathijssen I., RA Leheup B., Raile K., Hennies H.C., Horn D.; RT "Mutational spectrum of COH1 and clinical heterogeneity in Cohen RT syndrome."; RL J. Med. Genet. 43:E22-E22(2006). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] VAL-3001. 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). RN [16] RP INVOLVEMENT IN COH1. RX PubMed=19190672; DOI=10.1038/ejhg.2008.273; RA Megarbane A., Slim R., Nuernberg G., Ebermann I., Nuernberg P., Bolz H.J.; RT "A novel VPS13B mutation in two brothers with Cohen syndrome, cutis RT verticis gyrata and sensorineural deafness."; RL Eur. J. Hum. Genet. 17:1076-1079(2009). RN [17] RP VARIANT COH1 LEU-1494 DEL, AND TISSUE SPECIFICITY. RX PubMed=19006247; DOI=10.1002/humu.20886; RA Seifert W., Holder-Espinasse M., Kuehnisch J., Kahrizi K., Tzschach A., RA Garshasbi M., Najmabadi H., Walter Kuss A., Kress W., Laureys G., Loeys B., RA Brilstra E., Mancini G.M.S., Dollfus H., Dahan K., Apse K., Hennies H.C., RA Horn D.; RT "Expanded mutational spectrum in Cohen syndrome, tissue expression, and RT transcript variants of COH1."; RL Hum. Mutat. 30:E404-E420(2009). RN [18] RP INVOLVEMENT IN COH1. RX PubMed=19533689; DOI=10.1002/humu.21065; RA Balikova I., Lehesjoki A.E., de Ravel T.J., Thienpont B., Chandler K.E., RA Clayton-Smith J., Traeskelin A.L., Fryns J.P., Vermeesch J.R.; RT "Deletions in the VPS13B (COH1) gene as a cause of Cohen syndrome."; RL Hum. Mutat. 30:E845-E854(2009). RN [19] RP CHARACTERIZATION OF VARIANT COH1 2839-ARG--PRO-4022 DEL, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=21865173; DOI=10.1074/jbc.m111.267971; RA Seifert W., Kuehnisch J., Maritzen T., Horn D., Haucke V., Hennies H.C.; RT "Cohen syndrome-associated protein, COH1, is a novel, giant Golgi matrix RT protein required for Golgi integrity."; RL J. Biol. Chem. 286:37665-37675(2011). RN [20] RP VARIANT ILE-2481. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). RN [21] RP CHARACTERIZATION OF VARIANTS COH1 146-ARG--PRO-4022 DEL; 336-GLN--PRO-4022 RP DEL; 579-ILE--PRO-4022 DEL; 692-ARG--PRO-4022 DEL; 1143-ARG--PRO-4022 DEL; RP 2548-PHE--PRO-4022 DEL; 2839-ARG--PRO-4022 DEL AND 3627-THR--HIS-3633 RP DELINS ILE. RX PubMed=23188044; DOI=10.1038/ejhg.2012.251; RA El Chehadeh-Djebbar S., Blair E., Holder-Espinasse M., Moncla A., RA Frances A.M., Rio M., Debray F.G., Rump P., Masurel-Paulet A., Gigot N., RA Callier P., Duplomb L., Aral B., Huet F., Thauvin-Robinet C., Faivre L.; RT "Changing facial phenotype in Cohen syndrome: towards clues for an earlier RT diagnosis."; RL Eur. J. Hum. Genet. 21:736-742(2013). RN [22] RP CHARACTERIZATION OF VARIANTS COH1 692-ARG--PRO-4022 DEL; 1143-ARG--PRO-4022 RP DEL; 2548-PHE--PRO-4022 DEL; 2839-ARG--PRO-4022 DEL AND 3627-THR--HIS-3633 RP DELINS ILE, AND FUNCTION. RX PubMed=24334764; DOI=10.1093/hmg/ddt630; RA Duplomb L., Duvet S., Picot D., Jego G., El Chehadeh-Djebbar S., Marle N., RA Gigot N., Aral B., Carmignac V., Thevenon J., Lopez E., Riviere J.B., RA Klein A., Philippe C., Droin N., Blair E., Girodon F., Donadieu J., RA Bellanne-Chantelot C., Delva L., Michalski J.C., Solary E., Faivre L., RA Foulquier F., Thauvin-Robinet C.; RT "Cohen syndrome is associated with major glycosylation defects."; RL Hum. Mol. Genet. 23:2391-2399(2014). RN [23] RP CHARACTERIZATION OF VARIANTS COH1 146-ARG--PRO-4022 DEL; 579-ILE--PRO-4022 RP DEL; 692-ARG--PRO-4022 DEL; 971-ARG--PRO-4022 DEL; 1143-ARG--PRO-4022 DEL; RP 1227-TYR--PRO-4022 DEL AND 3627-THR--HIS-3633 DELINS ILE, AND FUNCTION. RX PubMed=26358774; DOI=10.1093/hmg/ddv366; RA Limoge F., Faivre L., Gautier T., Petit J.M., Gautier E., Masson D., RA Jego G., El Chehadeh-Djebbar S., Marle N., Carmignac V., Deckert V., RA Brindisi M.C., Edery P., Ghoumid J., Blair E., Lagrost L., RA Thauvin-Robinet C., Duplomb L.; RT "Insulin response dysregulation explains abnormal fat storage and increased RT risk of diabetes mellitus type 2 in Cohen Syndrome."; RL Hum. Mol. Genet. 24:6603-6613(2015). RN [24] RP INVOLVEMENT IN COH1. RX PubMed=29149870; DOI=10.1186/s12881-017-0493-5; RA Rejeb I., Jilani H., Elaribi Y., Hizem S., Hila L., Zillahrdt J.L., RA Chelly J., Benjemaa L.; RT "First case report of Cohen syndrome in the Tunisian population caused by RT VPS13B mutations."; RL BMC Med. Genet. 18:134-134(2017). RN [25] RP VARIANT COH1 3282-LYS--PRO-4022 DEL. RX PubMed=31752730; DOI=10.1186/s12881-019-0920-x; RA Zhao S., Luo Z., Xiao Z., Li L., Zhao R., Yang Y., Zhong Y.; RT "Case report: two novel VPS13B mutations in a Chinese family with Cohen RT syndrome and hyperlinear palms."; RL BMC Med. Genet. 20:187-187(2019). RN [26] RP VARIANT COH1 2704-TYR--PRO-4022 DEL. RX PubMed=31580008; DOI=10.1111/aos.14255; RA Nasser F., Kurtenbach A., Biskup S., Weidensee S., Kohl S., Zrenner E.; RT "Ophthalmic features of retinitis pigmentosa in Cohen syndrome caused by RT pathogenic variants in the VPS13B gene."; RL Acta Ophthalmol. 98:e316-e321(2020). RN [27] RP VARIANT COH1 21-LEU--PRO-4022 DEL. RX PubMed=31825161; DOI=10.1002/ajmg.a.61435; RA Koehler K., Schuelke M., Hell A.K., Schittkowski M., Huebner A., RA Brockmann K.; RT "A novel homozygous nonsense mutation of VPS13B associated with previously RT unreported features of Cohen syndrome."; RL Am. J. Med. Genet. A 182:570-575(2020). RN [28] RP INVOLVEMENT IN COH1. RX PubMed=32605629; DOI=10.1186/s12881-020-01075-1; RA Momtazmanesh S., Rayzan E., Shahkarami S., Rohlfs M., Klein C., Rezaei N.; RT "A novel VPS13B mutation in Cohen syndrome: a case report and review of RT literature."; RL BMC Med. Genet. 21:140-140(2020). RN [29] RP INVOLVEMENT IN COH1. RX PubMed=32402540; DOI=10.1016/j.braindev.2020.04.010; RA Hashmi J.A., Fadhli F., Almatrafi A., Afzal S., Ramzan K., Thiele H., RA Nuernberg P., Basit S.; RT "Homozygosity mapping and whole exome sequencing provide exact diagnosis of RT Cohen syndrome in a Saudi family."; RL Brain Dev. 42:587-593(2020). RN [30] RP INVOLVEMENT IN COH1. RX PubMed=32505691; DOI=10.1016/j.ejmg.2020.103973; RA Boschann F., Fischer-Zirnsak B., Wienker T.F., Holtgrewe M., Seelow D., RA Eichhorn B., Doehnert S., Fahsold R., Horn D., Graul-Neumann L.M.; RT "An intronic splice site alteration in combination with a large deletion RT affecting VPS13B (COH1) causes Cohen syndrome."; RL Eur. J. Med. Genet. 63:103973-103973(2020). RN [31] RP VARIANT COH1 413-TYR--LEU-415 DEL (ISOFORM 5), VARIANT COH1 MET-3445, AND RP FUNCTION. RX PubMed=32560273; DOI=10.3390/jcm9061886; RA Lee Y.K., Hwang S.K., Lee S.K., Yang J.E., Kwak J.H., Seo H., Ahn H., RA Lee Y.S., Kim J., Lim C.S., Kaang B.K., Lee J.H., Lee J.A., Lee K.; RT "Cohen Syndrome Patient iPSC-Derived Neurospheres and Forebrain-Like RT Glutamatergic Neurons Reveal Reduced Proliferation of Neural Progenitor RT Cells and Altered Expression of Synapse Genes."; RL J. Clin. Med. 9:1886-1886(2020). RN [32] RP INVOLVEMENT IN COH1. RX PubMed=31444703; DOI=10.1007/s12031-019-01394-w; RA Alipour N., Salehpour S., Tonekaboni S.H., Rostami M., Bahari S., RA Yassaee V., Miryounesi M., Ghafouri-Fard S.; RT "Mutations in the VPS13B Gene in Iranian Patients with Different Phenotypes RT of Cohen Syndrome."; RL J. Mol. Neurosci. 70:21-25(2020). RN [33] RP INVOLVEMENT IN COH1. RX PubMed=32170714; DOI=10.1007/s12031-020-01530-x; RA Kaushik P., Mahajan N., Girimaji S.C., Kumar A.; RT "Whole Exome Sequencing Identifies a Novel Homozygous Duplication Mutation RT in the VPS13B Gene in an Indian Family with Cohen Syndrome."; RL J. Mol. Neurosci. 70:1225-1228(2020). RN [34] RP VARIANT COH1 2067-LEU--PRO-4022 DEL. RX PubMed=34840762; DOI=10.1016/j.amsu.2021.103014; RA Ghzawi A., Hirbawi H., Negida A., Abu-Farsakh H.; RT "A case of a Jordanian male twin with Cohen's syndrome, with genetic RT analysis and muscle biopsy; case report."; RL Ann. Med. 71:103014-103014(2021). RN [35] RP VARIANT COH1 2900-GLU--PRO-4022 DEL. RX PubMed=34484844; DOI=10.1155/2021/3143609; RA Dehghan R., Behnam M., Moafi A., Salehi M.; RT "A Novel Mutation in the VPS13B Gene in a Cohen Syndrome Patient with RT Positive Antiphospholipid Antibodies."; RL Case Rep. Immunol. 2021:3143609-3143609(2021). RN [36] RP INVOLVEMENT IN COH1. RX PubMed=34322253; DOI=10.1002/ccr3.4492; RA Razavi A., Jafarpour H., Khosravi M.R., Abbasi G., Dabbaghzadeh A.; RT "A VPS13B mutation in Cohen syndrome presented with petechiae: An unusual RT presentation."; RL Clin. Case Rep. 9:e04492-e04492(2021). RN [37] RP INVOLVEMENT IN COH1. RX PubMed=33959574; DOI=10.3389/fped.2021.651621; RA Li L., Bu X., Ji Y., Tan P., Liu S.; RT "A Novel Homozygous VPS13B Splice-Site Mutation Causing the Skipping of RT Exon 38 in a Chinese Family With Cohen Syndrome."; RL Front. Pediatr. 9:651621-651621(2021). RN [38] RP INVOLVEMENT IN COH1, AND TISSUE SPECIFICITY. RX PubMed=33025479; DOI=10.1007/s12031-020-01713-6; RA Lou G., Ke Y., Zhang Y., Liangjie G., Shama S.A., Qi N., Qin L., Liao S., RA Zhao Y.; RT "Functional Analysis of a Compound Heterozygous Mutation in the VPS13B Gene RT in a Chinese Pedigree with Cohen Syndrome."; RL J. Mol. Neurosci. 71:943-952(2021). RN [39] RP VARIANT COH1 3457-GLN--PRO-4022 DEL. RX PubMed=34041686; DOI=10.1007/s12031-021-01852-4; RA Karimzadeh M.R., Omidi F., Sahebalzamani A., Saeidi K.; RT "A Novel VPS13B Mutation Identified by Whole-Exome Sequencing in Iranian RT Patients with Cohen Syndrome."; RL J. Mol. Neurosci. 71:2566-2574(2021). RN [40] RP INVOLVEMENT IN COH1. RX PubMed=34898996; DOI=10.2147/pgpm.s327252; RA Hu X., Huang T., Liu Y., Zhang L., Zhu L., Peng X., Zhang S.; RT "Identification of a Novel VPS13B Mutation in a Chinese Patient with Cohen RT Syndrome by Whole-Exome Sequencing."; RL Pharmacogenomics 14:1583-1589(2021). RN [41] RP VARIANTS COH1 336-GLN--PRO-4022 DEL; 579-ILE--PRO-4022 DEL; RP 692-ARG--PRO-4022 DEL; 971-ARG--PRO-4022 DEL; 1143-ARG--PRO-4022 DEL; RP 1227-TYR--PRO-4022 DEL; 1471-ARG--PRO-4022 DEL; PHE-3616 DEL AND RP 3627-THR--HIS-3633 DELINS ILE. RX PubMed=34385517; DOI=10.1038/s41598-021-95743-8; RA Gabrielle P.H., Faivre L., Audo I., Zanlonghi X., Dollfus H., RA Thiadens A.A.H.J., Zeitz C., Mancini G.M.S., Perdomo Y., Mohand-Said S., RA Lize E., Lhussiez V., Nandrot E.F., Acar N., Creuzot-Garcher C., RA Sahel J.A., Ansar M., Thauvin-Robinet C., Duplomb L., Da Costa R.; RT "Cystoid maculopathy is a frequent feature of Cohen syndrome-associated RT retinopathy."; RL Sci. Rep. 11:16412-16412(2021). CC -!- FUNCTION: Mediates the transfer of lipids between membranes at CC organelle contact sites (By similarity). Binds phosphatidylinositol 3- CC phosphate (By similarity). Functions as a tethering factor in the slow CC endocytic recycling pathway, to assist traffic between early and CC recycling endosomes (PubMed:30962439, PubMed:24334764, CC PubMed:32375900). Involved in the transport of proacrosomal vesicles to CC the nuclear dense lamina (NDL) during spermatid development (By CC similarity). Plays a role in the assembly of the Golgi apparatus, CC possibly by mediating trafficking to the Golgi membrane CC (PubMed:21865173). Plays a role in the development of the nervous CC system, and may be required for neuron projection development CC (PubMed:25492866, PubMed:32560273). May also play a role during adipose CC tissue development (PubMed:26358774). Required for maintenance of the CC ocular lens (By similarity). {ECO:0000250|UniProtKB:Q07878, CC ECO:0000250|UniProtKB:Q80TY5, ECO:0000269|PubMed:21865173, CC ECO:0000269|PubMed:24334764, ECO:0000269|PubMed:26358774, CC ECO:0000269|PubMed:30962439, ECO:0000269|PubMed:32375900, CC ECO:0000269|PubMed:32560273, ECO:0000305|PubMed:25492866, CC ECO:0000305|PubMed:32560273}. CC -!- SUBUNIT: Interacts with STX6 (By similarity). Interacts with STX12 (By CC similarity). Interacts with RAB6A isoform 1 (GTP-bound) and isoform 2 CC (GTP-bound) (PubMed:25492866). Interacts with RAB6B (GTP-bound) CC (PubMed:25492866). {ECO:0000250|UniProtKB:Q80TY5, CC ECO:0000269|PubMed:25492866}. CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane CC {ECO:0000250|UniProtKB:Q80TY5}; Peripheral membrane protein CC {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, acrosome CC membrane {ECO:0000250|UniProtKB:Q80TY5}; Peripheral membrane protein CC {ECO:0000305}. Golgi apparatus, cis-Golgi network membrane CC {ECO:0000269|PubMed:21865173, ECO:0000269|PubMed:25492866}; Peripheral CC membrane protein {ECO:0000269|PubMed:21865173}. Endoplasmic reticulum- CC Golgi intermediate compartment membrane {ECO:0000269|PubMed:21865173}; CC Peripheral membrane protein {ECO:0000269|PubMed:21865173}. Golgi CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21865173}; CC Peripheral membrane protein {ECO:0000269|PubMed:21865173}. Early CC endosome membrane {ECO:0000269|PubMed:25492866}; Peripheral membrane CC protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:25492866}; CC Peripheral membrane protein {ECO:0000305}. Note=Localizes to CC proacrosomal and acrosomal vesicles and not the Golgi apparatus during CC acrosome formation. {ECO:0000250|UniProtKB:Q80TY5}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=1A; CC IsoId=Q7Z7G8-1; Sequence=Displayed; CC Name=2; Synonyms=2A; CC IsoId=Q7Z7G8-2; Sequence=VSP_009408; CC Name=3; CC IsoId=Q7Z7G8-3; Sequence=VSP_009409, VSP_009410; CC Name=4; CC IsoId=Q7Z7G8-4; Sequence=VSP_009406, VSP_009407; CC Name=5; CC IsoId=Q7Z7G8-5; Sequence=VSP_009404, VSP_009405; CC Name=6; CC IsoId=Q7Z7G8-6; Sequence=VSP_039837; CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:12730828). There is CC apparent differential expression of different transcripts CC (PubMed:12730828, PubMed:19006247). In fetal brain, lung, liver, and CC kidney, two transcripts of 2 and 5 kb are identified (PubMed:12730828). CC These transcripts are also seen in all adult tissues analyzed CC (PubMed:12730828). A larger transcript (12-14 kb) is expressed in CC prostate, testis, ovary, and colon in the adult (PubMed:12730828). CC Expression is very low in adult brain tissue (PubMed:12730828). CC Expressed in peripheral blood lymphocytes (PubMed:33025479). Isoform 1 CC and isoform 2 are expressed in brain and retina (PubMed:12730828, CC PubMed:19006247). Isoform 2 is expressed ubiquitously (PubMed:12730828, CC PubMed:19006247). {ECO:0000269|PubMed:12730828, CC ECO:0000269|PubMed:19006247, ECO:0000269|PubMed:33025479}. CC -!- DISEASE: Cohen syndrome (COH1) [MIM:216550]: A rare autosomal recessive CC disorder characterized by obesity, hypotonia, intellectual deficit, CC characteristic craniofacial dysmorphism and abnormalities of the hands CC and feet. Characteristic facial features include high-arched or wave- CC shaped eyelids, a short philtrum, thick hair and low hairline. CC {ECO:0000269|PubMed:12730828, ECO:0000269|PubMed:15141358, CC ECO:0000269|PubMed:15154116, ECO:0000269|PubMed:15211651, CC ECO:0000269|PubMed:16648375, ECO:0000269|PubMed:19006247, CC ECO:0000269|PubMed:19190672, ECO:0000269|PubMed:19533689, CC ECO:0000269|PubMed:21865173, ECO:0000269|PubMed:23188044, CC ECO:0000269|PubMed:24334764, ECO:0000269|PubMed:26358774, CC ECO:0000269|PubMed:29149870, ECO:0000269|PubMed:31444703, CC ECO:0000269|PubMed:31580008, ECO:0000269|PubMed:31752730, CC ECO:0000269|PubMed:31825161, ECO:0000269|PubMed:32170714, CC ECO:0000269|PubMed:32402540, ECO:0000269|PubMed:32505691, CC ECO:0000269|PubMed:32560273, ECO:0000269|PubMed:32605629, CC ECO:0000269|PubMed:33025479, ECO:0000269|PubMed:33959574, CC ECO:0000269|PubMed:34041686, ECO:0000269|PubMed:34322253, CC ECO:0000269|PubMed:34385517, ECO:0000269|PubMed:34484844, CC ECO:0000269|PubMed:34840762, ECO:0000269|PubMed:34898996}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC03664.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AY223814; AAP41102.1; -; mRNA. DR EMBL; AY223815; AAP41103.1; -; mRNA. DR EMBL; AY223816; AAP41104.1; -; mRNA. DR EMBL; AY223817; AAP41105.1; -; mRNA. DR EMBL; AY223818; AAP41106.1; -; mRNA. DR EMBL; AJ608772; CAE75584.1; -; mRNA. DR EMBL; AJ608773; CAE75585.1; -; mRNA. DR EMBL; AK091431; BAC03664.1; ALT_INIT; mRNA. DR EMBL; AK000590; BAA91275.1; -; mRNA. DR EMBL; AC018442; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC023933; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026827; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104986; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105195; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105328; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107909; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP004289; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP004290; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB011104; BAA25458.1; -; mRNA. DR CCDS; CCDS47903.1; -. [Q7Z7G8-5] DR CCDS; CCDS6280.1; -. [Q7Z7G8-1] DR CCDS; CCDS6281.1; -. [Q7Z7G8-2] DR PIR; T00070; T00070. DR RefSeq; NP_056058.2; NM_015243.2. [Q7Z7G8-4] DR RefSeq; NP_060360.3; NM_017890.4. [Q7Z7G8-1] DR RefSeq; NP_689777.3; NM_152564.4. [Q7Z7G8-2] DR RefSeq; NP_858047.2; NM_181661.2. [Q7Z7G8-5] DR RefSeq; XP_005250857.1; XM_005250800.3. DR RefSeq; XP_005250858.1; XM_005250801.4. DR RefSeq; XP_011515150.1; XM_011516848.2. DR BioGRID; 127612; 100. DR IntAct; Q7Z7G8; 21. DR STRING; 9606.ENSP00000351346; -. DR TCDB; 1.R.2.1.4; the bridge-like lipid transfer protein (bltp) family. DR CarbonylDB; Q7Z7G8; -. DR GlyGen; Q7Z7G8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7Z7G8; -. DR MetOSite; Q7Z7G8; -. DR PhosphoSitePlus; Q7Z7G8; -. DR BioMuta; VPS13B; -. DR DMDM; 308153515; -. DR EPD; Q7Z7G8; -. DR jPOST; Q7Z7G8; -. DR MassIVE; Q7Z7G8; -. DR MaxQB; Q7Z7G8; -. DR PaxDb; 9606-ENSP00000351346; -. DR PeptideAtlas; Q7Z7G8; -. DR ProteomicsDB; 69541; -. [Q7Z7G8-1] DR ProteomicsDB; 69542; -. [Q7Z7G8-2] DR ProteomicsDB; 69543; -. [Q7Z7G8-3] DR ProteomicsDB; 69544; -. [Q7Z7G8-4] DR ProteomicsDB; 69545; -. [Q7Z7G8-5] DR ProteomicsDB; 69546; -. [Q7Z7G8-6] DR Pumba; Q7Z7G8; -. DR Antibodypedia; 26091; 115 antibodies from 25 providers. DR DNASU; 157680; -. DR Ensembl; ENST00000357162.7; ENSP00000349685.2; ENSG00000132549.20. [Q7Z7G8-2] DR Ensembl; ENST00000358544.7; ENSP00000351346.2; ENSG00000132549.20. [Q7Z7G8-1] DR Ensembl; ENST00000441350.2; ENSP00000398472.2; ENSG00000132549.20. [Q7Z7G8-5] DR Ensembl; ENST00000496144.5; ENSP00000430900.1; ENSG00000132549.20. [Q7Z7G8-3] DR GeneID; 157680; -. DR KEGG; hsa:157680; -. DR MANE-Select; ENST00000357162.7; ENSP00000349685.2; NM_152564.5; NP_689777.3. [Q7Z7G8-2] DR UCSC; uc003yis.4; human. [Q7Z7G8-1] DR AGR; HGNC:2183; -. DR CTD; 157680; -. DR DisGeNET; 157680; -. DR GeneCards; VPS13B; -. DR GeneReviews; VPS13B; -. DR HGNC; HGNC:2183; VPS13B. DR HPA; ENSG00000132549; Low tissue specificity. DR MalaCards; VPS13B; -. DR MIM; 216550; phenotype. DR MIM; 607817; gene. DR neXtProt; NX_Q7Z7G8; -. DR OpenTargets; ENSG00000132549; -. DR Orphanet; 193; Cohen syndrome. DR PharmGKB; PA26699; -. DR VEuPathDB; HostDB:ENSG00000132549; -. DR eggNOG; KOG1809; Eukaryota. DR GeneTree; ENSGT00940000154684; -. DR HOGENOM; CLU_331741_0_0_1; -. DR InParanoid; Q7Z7G8; -. DR OMA; SFYMPRI; -. DR OrthoDB; 4231425at2759; -. DR PhylomeDB; Q7Z7G8; -. DR TreeFam; TF323503; -. DR PathwayCommons; Q7Z7G8; -. DR SignaLink; Q7Z7G8; -. DR SIGNOR; Q7Z7G8; -. DR BioGRID-ORCS; 157680; 11 hits in 1157 CRISPR screens. DR ChiTaRS; VPS13B; human. DR GenomeRNAi; 157680; -. DR Pharos; Q7Z7G8; Tbio. DR PRO; PR:Q7Z7G8; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q7Z7G8; Protein. DR Bgee; ENSG00000132549; Expressed in sural nerve and 210 other cell types or tissues. DR ExpressionAtlas; Q7Z7G8; baseline and differential. DR GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB. DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB. DR GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB. DR GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB. DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0090168; P:Golgi reassembly; IMP:UniProtKB. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0036438; P:maintenance of lens transparency; ISS:UniProtKB. DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB. DR GO; GO:0031175; P:neuron projection development; TAS:UniProtKB. DR GO; GO:0032458; P:slow endocytic recycling; IDA:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB. DR InterPro; IPR026854; VPS13-like_N. DR InterPro; IPR031645; VPS13_DH-like. DR InterPro; IPR009543; VPS13_VAB. DR InterPro; IPR039782; VPS13B. DR PANTHER; PTHR12517:SF0; INTERMEMBRANE LIPID TRANSFER PROTEIN VPS13B; 1. DR PANTHER; PTHR12517; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 13B; 1. DR Pfam; PF12624; Chorein_N; 1. DR Pfam; PF16909; VPS13_DH-like; 1. DR Pfam; PF06650; VPS13_VAB; 1. DR Genevisible; Q7Z7G8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasmic vesicle; Disease variant; Endosome; KW Golgi apparatus; Lipid transport; Lipid-binding; Lysosome; Membrane; KW Obesity; Phosphoprotein; Reference proteome; Transport. FT CHAIN 1..4022 FT /note="Intermembrane lipid transfer protein VPS13B" FT /id="PRO_0000065880" FT DOMAIN 2..102 FT /note="Chorein N-terminal" FT /evidence="ECO:0000255" FT DOMAIN 2631..2716 FT /note="SHR-BD" FT /evidence="ECO:0000255" FT REGION 100..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1247..1314 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1860..1880 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3908..4022 FT /note="Localizes the protein to the Golgi apparatus" FT /evidence="ECO:0000269|PubMed:21865173" FT COMPBIAS 101..125 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1862..1876 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 414 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 999 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1002 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1033 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1815 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 403..415 FT /note="LTEMQVESSYYSP -> VGLFSCCLYLYQL (in isoform 5)" FT /evidence="ECO:0000303|PubMed:12730828, FT ECO:0000303|PubMed:14702039" FT /id="VSP_009404" FT VAR_SEQ 416..4022 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:12730828, FT ECO:0000303|PubMed:14702039" FT /id="VSP_009405" FT VAR_SEQ 839..863 FT /note="GVKSKNPLPTLEGSIQNVELKYCST -> EIGSCYVAQVDLELLASNDPPTS FT TS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12730828" FT /id="VSP_009406" FT VAR_SEQ 864..4022 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12730828" FT /id="VSP_009407" FT VAR_SEQ 977 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039837" FT VAR_SEQ 1386..1433 FT /note="SLGEECWSLGQCGGVFLSCTDKLNRRTLLVRPISKQDPFSNCSGFFPS -> FT RPGEGWQSGHFEGVFLQCKEKSV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12730828, FT ECO:0000303|PubMed:15498460" FT /id="VSP_009408" FT VAR_SEQ 1386..1427 FT /note="SLGEECWSLGQCGGVFLSCTDKLNRRTLLVRPISKQDPFSNC -> RPGEGW FT QSGHFEGVFLQCKEKSVPWGRVLVFGAMWRCLPFLY (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12730828" FT /id="VSP_009409" FT VAR_SEQ 1428..4022 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12730828" FT /id="VSP_009410" FT VARIANT 21..4022 FT /note="Missing (in COH1)" FT /evidence="ECO:0000269|PubMed:31825161" FT /id="VAR_086594" FT VARIANT 146..4022 FT /note="Missing (in COH1; leads to an accumulation of liquid FT droplets and accelerates differentiation of adipose cells; FT response to insulin is abnormal.; dbSNP:rs144539572)" FT /evidence="ECO:0000269|PubMed:23188044, FT ECO:0000269|PubMed:26358774" FT /id="VAR_086595" FT VARIANT 336..4022 FT /note="Missing (in COH1; dbSNP:rs1554625617)" FT /evidence="ECO:0000269|PubMed:23188044, FT ECO:0000269|PubMed:34385517" FT /id="VAR_086596" FT VARIANT 579..4022 FT /note="Missing (in COH1)" FT /evidence="ECO:0000269|PubMed:23188044, FT ECO:0000269|PubMed:26358774, ECO:0000269|PubMed:34385517" FT /id="VAR_086597" FT VARIANT 692..4022 FT /note="Missing (in COH1; glycosylation is defective; FT accelerates differentiation of adipose cells; FT dbSNP:rs180177356)" FT /evidence="ECO:0000269|PubMed:23188044, FT ECO:0000269|PubMed:24334764, ECO:0000269|PubMed:26358774, FT ECO:0000269|PubMed:34385517" FT /id="VAR_086598" FT VARIANT 829 FT /note="A -> T (in dbSNP:rs61753721)" FT /evidence="ECO:0000269|PubMed:16648375" FT /id="VAR_058749" FT VARIANT 866 FT /note="V -> I (in dbSNP:rs150185067)" FT /evidence="ECO:0000269|PubMed:16648375" FT /id="VAR_058750" FT VARIANT 971..4022 FT /note="Missing (in COH1; dbSNP:rs120074152)" FT /evidence="ECO:0000269|PubMed:26358774, FT ECO:0000269|PubMed:34385517" FT /id="VAR_086599" FT VARIANT 1138 FT /note="P -> L (in dbSNP:rs35342235)" FT /id="VAR_057750" FT VARIANT 1143..4022 FT /note="Missing (in COH1; accelerates differentiation of FT adipose cells; response to insulin is abnormal.; FT dbSNP:rs386834080)" FT /evidence="ECO:0000269|PubMed:23188044, FT ECO:0000269|PubMed:24334764, ECO:0000269|PubMed:26358774, FT ECO:0000269|PubMed:34385517" FT /id="VAR_086600" FT VARIANT 1227..4022 FT /note="Missing (in COH1; dbSNP:rs1554814266)" FT /evidence="ECO:0000269|PubMed:26358774, FT ECO:0000269|PubMed:34385517" FT /id="VAR_086601" FT VARIANT 1471..4022 FT /note="Missing (in COH1; dbSNP:rs386834086)" FT /evidence="ECO:0000269|PubMed:34385517" FT /id="VAR_086602" FT VARIANT 1494 FT /note="Missing (in COH1; dbSNP:rs386834088)" FT /evidence="ECO:0000269|PubMed:19006247" FT /id="VAR_058751" FT VARIANT 1739..1744 FT /note="Missing (in COH1)" FT /id="VAR_058752" FT VARIANT 1994 FT /note="I -> V (in dbSNP:rs139640224)" FT /evidence="ECO:0000269|PubMed:16648375" FT /id="VAR_058753" FT VARIANT 2067..4022 FT /note="Missing (in COH1; dbSNP:rs371364257)" FT /evidence="ECO:0000269|PubMed:34840762" FT /id="VAR_086603" FT VARIANT 2193 FT /note="L -> R (in COH1; uncertain significance; FT dbSNP:rs120074149)" FT /evidence="ECO:0000269|PubMed:12730828" FT /id="VAR_017759" FT VARIANT 2341 FT /note="Y -> C (in COH1; dbSNP:rs386834104)" FT /evidence="ECO:0000269|PubMed:15154116" FT /id="VAR_038422" FT VARIANT 2481 FT /note="V -> I (found in a patient with intellectual FT disability and facial dysmorphisms; dbSNP:rs201963516)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069429" FT VARIANT 2548..4022 FT /note="Missing (in COH1; early endosomes are abnormal, FT lysosomes are enlarged and glycosylation is defective)" FT /evidence="ECO:0000269|PubMed:23188044, FT ECO:0000269|PubMed:24334764" FT /id="VAR_086604" FT VARIANT 2584 FT /note="V -> A (in dbSNP:rs7833870)" FT /id="VAR_057751" FT VARIANT 2645 FT /note="G -> D (in COH1; dbSNP:rs120074153)" FT /evidence="ECO:0000269|PubMed:15154116" FT /id="VAR_038423" FT VARIANT 2704..4022 FT /note="Missing (in COH1; dbSNP:rs777019428)" FT /evidence="ECO:0000269|PubMed:31580008" FT /id="VAR_086605" FT VARIANT 2773 FT /note="S -> L (in COH1; dbSNP:rs180177370)" FT /evidence="ECO:0000269|PubMed:16648375" FT /id="VAR_058754" FT VARIANT 2820 FT /note="I -> T (in COH1; dbSNP:rs120074155)" FT /evidence="ECO:0000269|PubMed:15211651" FT /id="VAR_058755" FT VARIANT 2822 FT /note="Y -> C (in dbSNP:rs371325199)" FT /evidence="ECO:0000269|PubMed:16648375" FT /id="VAR_058756" FT VARIANT 2839..4022 FT /note="Missing (in COH1; disrupts protein localization to FT the perinuclear region; Golgi stacks are fragmented, early FT endosomes are abnormal, lysosomes are enlarged and FT glycosylation is defective; leads to an accumulation of FT liquid droplets and accelerates differentiation of adipose FT cells; response to insulin is abnormal.; FT dbSNP:rs386834113)" FT /evidence="ECO:0000269|PubMed:21865173, FT ECO:0000269|PubMed:23188044, ECO:0000269|PubMed:24334764" FT /id="VAR_086606" FT VARIANT 2900..4022 FT /note="Missing (in COH1)" FT /evidence="ECO:0000269|PubMed:34484844" FT /id="VAR_086607" FT VARIANT 2993 FT /note="N -> S (in COH1; dbSNP:rs28940272)" FT /evidence="ECO:0000269|PubMed:15141358" FT /id="VAR_038424" FT VARIANT 3001 FT /note="L -> V (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036325" FT VARIANT 3142 FT /note="S -> R" FT /evidence="ECO:0000269|PubMed:16648375" FT /id="VAR_058757" FT VARIANT 3282..4022 FT /note="Missing (in COH1)" FT /evidence="ECO:0000269|PubMed:31752730" FT /id="VAR_086608" FT VARIANT 3432 FT /note="G -> R (in dbSNP:rs6468694)" FT /id="VAR_057752" FT VARIANT 3445 FT /note="V -> M (in COH1; uncertain significance; FT dbSNP:rs191174682)" FT /evidence="ECO:0000269|PubMed:32560273" FT /id="VAR_086609" FT VARIANT 3457..4022 FT /note="Missing (in COH1)" FT /evidence="ECO:0000269|PubMed:34041686" FT /id="VAR_086610" FT VARIANT 3616 FT /note="Missing (in COH1; dbSNP:rs1554581821)" FT /evidence="ECO:0000269|PubMed:34385517" FT /id="VAR_086611" FT VARIANT 3627..3633 FT /note="TARQLVH -> I (in COH1)" FT /evidence="ECO:0000269|PubMed:23188044, FT ECO:0000269|PubMed:24334764, ECO:0000269|PubMed:26358774, FT ECO:0000269|PubMed:34385517" FT /id="VAR_086612" FT CONFLICT 401 FT /note="F -> S (in Ref. 3; BAA91275)" FT /evidence="ECO:0000305" FT CONFLICT 544 FT /note="M -> V (in Ref. 1; FT AAP41102/AAP41103/AAP41104/AAP41105 and 3; BAC03664)" FT /evidence="ECO:0000305" FT CONFLICT 618 FT /note="D -> N (in Ref. 1; FT AAP41102/AAP41103/AAP41104/AAP41105 and 3; BAC03664)" FT /evidence="ECO:0000305" FT CONFLICT 1387 FT /note="L -> H (in Ref. 1; AAP41102)" FT /evidence="ECO:0000305" FT CONFLICT 1401 FT /note="F -> I (in Ref. 1; AAP41102)" FT /evidence="ECO:0000305" FT CONFLICT 1425 FT /note="S -> R (in Ref. 1; AAP41102)" FT /evidence="ECO:0000305" FT CONFLICT 1673 FT /note="A -> D (in Ref. 1; AAP41102/AAP41103)" FT /evidence="ECO:0000305" FT VARIANT Q7Z7G8-5:413..415 FT /note="Missing (in COH1; dbSNP:rs7460625)" FT /evidence="ECO:0000269|PubMed:32560273" FT /id="VAR_082932" SQ SEQUENCE 4022 AA; 448664 MW; 35B79EE13730AFE3 CRC64; MLESYVTPIL MSYVNRYIKN LKPSDLQLSL WGGDVVLSKL ELKLDVLEQE LKLPFTFLSG HIHELRIHVP WTKLGSEPVV ITINTMECIL KLKDGIQDDH ESCGSNSTNR STAESTKSSI KPRRMQQAAP TDPDLPPGYV QSLIRRVVNN VNIVINNLIL KYVEDDIVLS VNITSAECYT VGELWDRAFM DISATDLVLR KVINFSDCTV CLDKRNASGK IEFYQDPLLY KCSFRTRLHF TYENLNSKMP SVIKIHTLVE SLKLSITDQQ LPMFIRIMQL GIALYYGEIG NFKEGEIEDL TCHNKDMLGN ITGSEDETRI DMQYPAQHKG QELYSQQDEE QPQGWVSWAW SFVPAIVSYD DGEEDFVGND PASTMHQQKA QTLKDPIVSI GFYCTKATVT FKLTEMQVES SYYSPQKVKS KEVLCWEQEG TTVEALMMGE PFFDCQIGFV GCRAMCLKGI MGVKDFEENM NRSETEACFF ICGDNLSTKG FTYLTNSLFD YRSPENNGTR AEFILDSTHH KETYTEIAGM QRFGAFYMDY LYTMENTSGK GSTNQQDFSS GKSEDLGTVQ EKSTKSLVIG PLDFRLDSSA VHRILKMIVC ALEHEYEPYS RLKSDIKDEN ETILNPEEVA LLEEYIPTRH TSVTLLKCTC TISMAEFNLL DHLLPVIMGE KNSSNFMNTT NFQSLRPLPS IRILVDKINL EHSVPMYAEQ LVHVVSSLTQ PSDNLLHYCY VHCYLKIFGF QAGLTSLDCS GSYCLPVPVI PSFSTALYGK LLKLPTCWTK RSQIAITEGI FELPNLTIQA TRAQTLLLQA IYQSWSHLGN VSSSAVIEAL INEIFLSIGV KSKNPLPTLE GSIQNVELKY CSTSLVKCAS GTMGSIKICA KAPVDSGKEK LIPLLQGPSD TKDLHSTKWL NESRKPESLL APDLMAFTIQ VPQYIDYCHN SGAVLLCSIQ GLAVNIDPIL YTWLIYQPQK RTSRHMQQQP VVAVPLVMPV CRRKEDEVSI GSAPLAKQQS YQASEYASSP VKTKTVTESR PLSVPVKAML NISESCRSPE ERMKEFIGIV WNAVKHLTLQ LEVQSCCVFI PNDSLPSPST IVSGDIPGTV RSWYHGQTSM PGTLVLCLPQ IKIISAGHKY MEPLQEIPFV IPRPILEEGD AFPWTISLHN FSIYTLLGKQ VTLCLVEPMG CTSTLAVTSQ KLLATGPDTR HSFVVCLHVD LESLEIKCSN PQVQLFYELT DIMNKVWNKI QKRGNLNLSP TSPETMAGPV PTSPVRSSIG TAPPDTSTCS PSADIGTTTE GDSIQAGEES PFSDSVTLEQ TTSNIGGTSG RVSLWMQWVL PKITIKLFAP DPENKGTEVC MVSELEDLSA SIDVQDVYTK VKCKIESFNI DHYRSSLGEE CWSLGQCGGV FLSCTDKLNR RTLLVRPISK QDPFSNCSGF FPSTTTKLLD GTHQQHGFLS LTYTKAVTKN VRHKLTSRNE RRSFHKLSEG LMDGSPHFLH EILLSAQAFD IVLYFPLLNA IASIFQAKLP KTQKEKRKSP GQPMRTHTLT SRNLPLIYVN TSVIRIFIPK TEEMQPTVEA NQAAKEDTVV LKIGSVAMAP QADNPLGRSV LRKDIYQRAL NLGILRDPGS EIEDRQYQID LQSINIGTAQ WHQLKPEKES VSGGVVTETE RNSQNPALEW NMASSIRRHQ ERRAILTPVL TDFSVRITGA PAVIFTKVVS PENLHTEEIL VCGHSLEVNI TTNLDFFLSV AQVQLLHQLI VANMTGLEPS NKAAEISKQE QKKVDIFDGG MAETSSRYSG AQDSGIGSDS VKIRIVQIEQ HSGASQHRIA RPSRQSSIVK NLNFIPFDIF ITASRISLMT YSCMALSKSK SQEQKNNEKT DKSSLNLPEV DSDVAKPNQA CISTVTAEDL LRSSISFPSG KKIGVLSLES LHASTRSSAR QALGITIVRQ PGRRGTGDLQ LEPFLYFIVS QPSLLLSCHH RKQRVEVSIF DAVLKGVASD YKCIDPGKTL PEALDYCTVW LQTVPGEIDS KSGIPPSFIT LQIKDFLNGP ADVNLDISKP LKANLSFTKL DQINLFLKKI KNAHSLAHSE ETSAMSNTMV NKDDLPVSKY YRGKLSKPKI HGDGVQKISA QENMWRAVSC FQKISVQTTQ IVISMETVPH TSKPCLLASL SNLNGSLSVK ATQKVPGIIL GSSFLLSIND FLLKTSLKER SRILIGPCCA TANLEAKWCK HSGNPGPEQS IPKISIDLRG GLLQVFWGQE HLNCLVLLHE LLNGYLNEEG NFEVQVSEPV PQMSSPVEKN QTFKSEQSSD DLRTGLFQYV QDAESLKLPG VYEVLFYNET EDCPGMMLWR YPEPRVLTLV RITPVPFNTT EDPDISTADL GDVLQVPCSL EYWDELQKVF VAFREFNLSE SKVCELQLPD INLVNDQKKL VSSDLWRIVL NSSQNGADDQ SSASESGSQS TCDPLVTPTA LAACTRVDSC FTPWFVPSLC VSFQFAHLEF HLCHHLDQLG TAAPQYLQPF VSDRNMPSEL EYMIVSFREP HMYLRQWNNG SVCQEIQFLA QADCKLLECR NVTMQSVVKP FSIFGQMAVS SDVVEKLLDC TVIVDSVFVN LGQHVVHSLN TAIQAWQQNK CPEVEELVFS HFVICNDTQE TLRFGQVDTD ENILLASLHS HQYSWRSHKS PQLLHICIEG WGNWRWSEPF SVDHAGTFIR TIQYRGRTAS LIIKVQQLNG VQKQIIICGR QIICSYLSQS IELKVVQHYI GQDGQAVVRE HFDCLTAKQK LPSYILENNE LTELCVKAKG DEDWSRDVCL ESKAPEYSIV IQVPSSNSSI IYVWCTVLTL EPNSQVQQRM IVFSPLFIMR SHLPDPIIIH LEKRSLGLSE TQIIPGKGQE KPLQNIEPDL VHHLTFQARE EYDPSDCAVP ISTSLIKQIA TKVHPGGTVN QILDEFYGPE KSLQPIWPYN KKDSDRNEQL SQWDSPMRVK LSIWKPYVRT LLIELLPWAL LINESKWDLW LFEGEKIVLQ VPAGKIIIPP NFQEAFQIGI YWANTNTVHK SVAIKLVHNL TSPKWKDGGN GEVVTLDEEA FVDTEIRLGA FPGHQKLCQF CISSMVQQGI QIIQIEDKTT IINNTPYQIF YKPQLSVCNP HSGKEYFRVP DSATFSICPG GEQPAMKSSS LPCWDLMPDI SQSVLDASLL QKQIMLGFSP APGADSSQCW SLPAIVRPEF PRQSVAVPLG NFRENGFCTR AIVLTYQEHL GVTYLTLSED PSPRVIIHNR CPVKMLIKEN IKDIPKFEVY CKKIPSECSI HHELYHQISS YPDCKTKDLL PSLLLRVEPL DEVTTEWSDA IDINSQGTQV VFLTGFGYVY VDVVHQCGTV FITVAPEGKA GPILTNTNRA PEKIVTFKMF ITQLSLAVFD DLTHHKASAE LLRLTLDNIF LCVAPGAGPL PGEEPVAALF ELYCVEICCG DLQLDNQLYN KSNFHFAVLV CQGEKAEPIQ CSKMQSLLIS NKELEEYKEK CFIKLCITLN EGKSILCDIN EFSFELKPAR LYVEDTFVYY IKTLFDTYLP NSRLAGHSTH LSGGKQVLPM QVTQHARALV NPVKLRKLVI QPVNLLVSIH ASLKLYIASD HTPLSFSVFE RGPIFTTARQ LVHALAMHYA AGALFRAGWV VGSLDILGSP ASLVRSIGNG VADFFRLPYE GLTRGPGAFV SGVSRGTTSF VKHISKGTLT SITNLATSLA RNMDRLSLDE EHYNRQEEWR RQLPESLGEG LRQGLSRLGI SLLGAIAGIV DQPMQNFQKT SEAQASAGHK AKGVISGVGK GIMGVFTKPI GGAAELVSQT GYGILHGAGL SQLPKQRHQP SDLHADQAPN SHVKYVWKML QSLGRPEVHM ALDVVLVRGS GQEHEGCLLL TSEVLFVVSV SEDTQQQAFP VTEIDCAQDS KQNNLLTVQL KQPRVACDVE VDGVRERLSE QQYNRLVDYI TKTSCHLAPS CSSMQIPCPV VAAEPPPSTV KTYHYLVDPH FAQVFLSKFT MVKNKALRKG FP //