ID RAB34_HUMAN Reviewed; 259 AA. AC Q9BZG1; B4E3A0; E9PEJ9; Q5BJE6; Q8NCJ8; Q96AR4; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 198. DE RecName: Full=Ras-related protein Rab-34; DE AltName: Full=Ras-related protein Rab-39; DE AltName: Full=Ras-related protein Rah; GN Name=RAB34; Synonyms=RAB39, RAH; 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] (ISOFORM 1). RA Hong W.; RT "Human Rab39 coding region (cDNA)."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Skeletal muscle; RA Stanchi F., Lanfranchi G.; RT "Full-length sequencing of 100 cDNA clones from human adult skeletal RT muscle."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Embryo, Mammary gland, and Uterus; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Pancreas; 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 INTERACTION WITH RILP. RX PubMed=14668488; DOI=10.1091/mbc.e03-06-0413; RA Wang T., Wong K.K., Hong W.; RT "A unique region of RILP distinguishes it from its related proteins in its RT regulation of lysosomal morphology and interaction with Rab7 and Rab34."; RL Mol. Biol. Cell 15:815-826(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-244, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x; RA Seto S., Tsujimura K., Koide Y.; RT "Rab GTPases regulating phagosome maturation are differentially recruited RT to mycobacterial phagosomes."; RL Traffic 12:407-420(2011). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [15] RP FUNCTION, AND INTERACTION WITH RILP. RX PubMed=27113757; DOI=10.15252/embr.201541382; RA Starling G.P., Yip Y.Y., Sanger A., Morton P.E., Eden E.R., Dodding M.P.; RT "Folliculin directs the formation of a Rab34-RILP complex to control the RT nutrient-dependent dynamic distribution of lysosomes."; RL EMBO Rep. 17:823-841(2016). RN [16] RP VARIANTS VAL-202; HIS-211 AND LYS-218, INVOLVEMENT IN OROFACIODIGITAL RP SYNDROME, CHARACTERIZATION OF VARIANTS VAL-202 AND HIS-211, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=37384395; DOI=10.1093/hmg/ddad109; RA Bruel A.L., Ganga A.K., Noskova L., Valenzuela I., Martinovic J., RA Duffourd Y., Zikanova M., Majer F., Kmoch S., Mohler M., Sun J., RA Sweeney L.K., Martinez-Gil N., Thauvin-Robinet C., Breslow D.K.; RT "Pathogenic RAB34 variants impair primary cilium assembly and cause a novel RT oral-facial-digital syndrome."; RL Hum. Mol. Genet. 32:2822-2831(2023). CC -!- FUNCTION: Transport protein involved in the redistribution of lysosomes CC to the peri-Golgi region (PubMed:27113757). Plays a role in the CC maturation of phagosomes that engulf pathogens, such as S.aureus and CC M.tuberculosis (PubMed:21255211). Plays a role in the fusion of CC phagosomes with lysosomes (PubMed:21255211). Involved in ciliogenesis CC (PubMed:37384395). Acts also as a positive regulator of hedgehog CC signaling and regulates ciliary function (By similarity). CC {ECO:0000250|UniProtKB:Q64008, ECO:0000269|PubMed:21255211, CC ECO:0000269|PubMed:27113757, ECO:0000269|PubMed:37384395}. CC -!- SUBUNIT: Interacts with RILP. {ECO:0000269|PubMed:14668488, CC ECO:0000269|PubMed:27113757}. CC -!- INTERACTION: CC Q9BZG1; P35219: CA8; NbExp=3; IntAct=EBI-2856739, EBI-718700; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q64008}. Golgi CC apparatus {ECO:0000250|UniProtKB:Q64008}. Cytoplasmic vesicle, CC phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome CC membrane {ECO:0000269|PubMed:21255211}; Lipid-anchor CC {ECO:0000269|PubMed:21255211}; Cytoplasmic side CC {ECO:0000269|PubMed:21255211}. Cell projection, cilium CC {ECO:0000250|UniProtKB:Q64008}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome, centriole {ECO:0000269|PubMed:37384395}. CC Note=Recruited to phagosomes containing S.aureus or M.tuberculosis CC (PubMed:21255211). {ECO:0000269|PubMed:21255211}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9BZG1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZG1-2; Sequence=VSP_010142; CC Name=NARR; CC IsoId=P0DI83-1; Sequence=External; CC Name=4; CC IsoId=Q9BZG1-4; Sequence=VSP_044734; CC -!- DISEASE: Note=RAB34 variants have been found in individuals affected by CC a ciliopathy with features of orofaciodigital syndrome. Patients show CC bilateral cleft lip/palate, lobulated tongue, abnormal frenulum, and CC bilateral polydactyly or polysyndactyly of the feet and hands. CC Additional clinical features are Y-shaped metacarpal bones, short femur CC and/or humerus, cardiac defects, anal atresia, and cerebral CC malformations including agenesis of the corpus callosum and cerebellar CC hypoplasia. {ECO:0000269|PubMed:37384395}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {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; AF322067; AAK09397.1; -; mRNA. DR EMBL; AJ277106; CAC81760.1; -; mRNA. DR EMBL; BT006702; AAP35348.1; -; mRNA. DR EMBL; AK027312; BAB55034.1; -; mRNA. DR EMBL; AK074689; BAC11141.1; -; mRNA. DR EMBL; AK304633; BAG65412.1; -; mRNA. DR EMBL; AC010761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC016841; AAH16841.1; -; mRNA. DR EMBL; BC091510; AAH91510.1; -; mRNA. DR CCDS; CCDS11240.1; -. [Q9BZG1-1] DR CCDS; CCDS45636.1; -. [Q9BZG1-2] DR CCDS; CCDS58536.1; -. [Q9BZG1-4] DR RefSeq; NP_001138414.1; NM_001144942.1. [Q9BZG1-2] DR RefSeq; NP_001243205.1; NM_001256276.1. [Q9BZG1-4] DR RefSeq; NP_001243206.1; NM_001256277.1. [Q9BZG1-1] DR RefSeq; NP_001243207.1; NM_001256278.1. DR RefSeq; NP_114140.4; NM_031934.5. [Q9BZG1-1] DR AlphaFoldDB; Q9BZG1; -. DR SMR; Q9BZG1; -. DR BioGRID; 123784; 67. DR IntAct; Q9BZG1; 30. DR MINT; Q9BZG1; -. DR STRING; 9606.ENSP00000413156; -. DR iPTMnet; Q9BZG1; -. DR PhosphoSitePlus; Q9BZG1; -. DR BioMuta; RAB34; -. DR DMDM; 20139693; -. DR EPD; Q9BZG1; -. DR jPOST; Q9BZG1; -. DR MassIVE; Q9BZG1; -. DR MaxQB; Q9BZG1; -. DR PaxDb; 9606-ENSP00000413156; -. DR PeptideAtlas; Q9BZG1; -. DR ProteomicsDB; 19907; -. DR ProteomicsDB; 79837; -. [Q9BZG1-1] DR ProteomicsDB; 79838; -. [Q9BZG1-2] DR Pumba; Q9BZG1; -. DR Antibodypedia; 14281; 145 antibodies from 26 providers. DR DNASU; 83871; -. DR Ensembl; ENST00000301043.10; ENSP00000301043.6; ENSG00000109113.20. [Q9BZG1-1] DR Ensembl; ENST00000395245.9; ENSP00000378666.3; ENSG00000109113.20. [Q9BZG1-1] DR Ensembl; ENST00000415040.6; ENSP00000410279.2; ENSG00000109113.20. [Q9BZG1-4] DR Ensembl; ENST00000436730.7; ENSP00000404180.3; ENSG00000109113.20. [Q9BZG1-1] DR Ensembl; ENST00000450529.5; ENSP00000391048.1; ENSG00000109113.20. [Q9BZG1-2] DR GeneID; 83871; -. DR KEGG; hsa:83871; -. DR MANE-Select; ENST00000395245.9; ENSP00000378666.3; NM_031934.6; NP_114140.4. DR UCSC; uc002hce.3; human. [Q9BZG1-1] DR AGR; HGNC:16519; -. DR CTD; 83871; -. DR DisGeNET; 83871; -. DR GeneCards; RAB34; -. DR HGNC; HGNC:16519; RAB34. DR HPA; ENSG00000109113; Low tissue specificity. DR MIM; 610917; gene. DR neXtProt; NX_Q9BZG1; -. DR OpenTargets; ENSG00000109113; -. DR PharmGKB; PA34126; -. DR VEuPathDB; HostDB:ENSG00000109113; -. DR eggNOG; KOG0094; Eukaryota. DR GeneTree; ENSGT00940000159645; -. DR InParanoid; Q9BZG1; -. DR OMA; LIRRTCE; -. DR OrthoDB; 3669528at2759; -. DR PhylomeDB; Q9BZG1; -. DR PathwayCommons; Q9BZG1; -. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR SignaLink; Q9BZG1; -. DR BioGRID-ORCS; 83871; 28 hits in 1157 CRISPR screens. DR ChiTaRS; RAB34; human. DR GeneWiki; RAB34; -. DR GenomeRNAi; 83871; -. DR Pharos; Q9BZG1; Tbio. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9BZG1; Protein. DR Bgee; ENSG00000109113; Expressed in descending thoracic aorta and 176 other cell types or tissues. DR ExpressionAtlas; Q9BZG1; baseline and differential. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB. DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB. DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031982; C:vesicle; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB. DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB. DR GO; GO:0032418; P:lysosome localization; IDA:UniProtKB. DR GO; GO:0090382; P:phagosome maturation; IMP:UniProtKB. DR GO; GO:0090385; P:phagosome-lysosome fusion; IMP:UniProtKB. DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB. DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB. DR CDD; cd04108; Rab36_Rab34; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR PANTHER; PTHR47977:SF8; RAS-RELATED PROTEIN RAB-34; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. DR Genevisible; Q9BZG1; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell projection; KW Cilium biogenesis/degradation; Cytoplasm; Cytoplasmic vesicle; KW Cytoskeleton; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..259 FT /note="Ras-related protein Rab-34" FT /id="PRO_0000121243" FT MOTIF 81..89 FT /note="Effector region" FT /evidence="ECO:0000250" FT BINDING 59..66 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 107..111 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 166..169 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT LIPID 257 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000255" FT LIPID 258 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000255" FT VAR_SEQ 51..72 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044734" FT VAR_SEQ 164..171 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_010142" FT VARIANT 197 FT /note="V -> L (in dbSNP:rs12125)" FT /id="VAR_015097" FT VARIANT 202 FT /note="G -> V (found in a patient with orofaciodigital FT syndrome; uncertain significance; due to a nucleotide FT substitution that also affects splicing; patient cells FT contain both normally spliced transcripts with variant FT V-202 and aberrant transcripts; severely decreased function FT in ciliogenesis; does not fully rescue cilia formation when FT expressed in RAB34-null retinal epithelium cells; no effect FT on localization to centrioles)" FT /evidence="ECO:0000269|PubMed:37384395" FT /id="VAR_088676" FT VARIANT 211 FT /note="R -> H (found in a patient with orofaciodigital FT syndrome; uncertain significance; severely decreased FT function in ciliogenesis; does not fully rescue cilia FT formation when expressed in RAB34-null rethinal epithelium FT cells; no effect on localization to centrioles)" FT /evidence="ECO:0000269|PubMed:37384395" FT /id="VAR_088677" FT VARIANT 218 FT /note="E -> K (found in a patient with orofaciodigital FT syndrome; uncertain significance)" FT /evidence="ECO:0000269|PubMed:37384395" FT /id="VAR_088678" FT CONFLICT 10 FT /note="D -> Y (in Ref. 4; BAG65412)" FT /evidence="ECO:0000305" FT CONFLICT 55 FT /note="V -> I (in Ref. 4; BAC11141)" FT /evidence="ECO:0000305" SQ SEQUENCE 259 AA; 29044 MW; 6D38A6F090F9802D CRC64; MNILAPVRRD RVLAELPQCL RKEAALHGHK DFHPRVTCAC QEHRTGTVGF KISKVIVVGD LSVGKTCLIN RFCKDTFDKN YKATIGVDFE MERFEVLGIP FSLQLWDTAG QERFKCIAST YYRGAQAIII VFNLNDVASL EHTKQWLADA LKENDPSSVL LFLVGSKKDL STPAQYALME KDALQVAQEM KAEYWAVSSL TGENVREFFF RVAALTFEAN VLAELEKSGA RRIGDVVRIN SDDSNLYLTA SKKKPTCCP //