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 ---------------------------------------------------------------------------
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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 Genevisible; Q7Z7G8; HS.
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.
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; AAP41102/AAP41103/AAP41104/
FT AAP41105 and 3; BAC03664)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="D -> N (in Ref. 1; AAP41102/AAP41103/AAP41104/
FT 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
//
