RB39B_HUMAN
ID RB39B_HUMAN Reviewed; 213 AA.
AC Q96DA2; Q5JT79; Q8NEX3;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ras-related protein Rab-39B;
GN Name=RAB39B;
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].
RC TISSUE=Fetal brain;
RX PubMed=12438742; DOI=10.1159/000064047;
RA Cheng H., Ma Y., Ni X., Jiang M., Guo L., Ying K., Xie Y., Mao Y.;
RT "Isolation and characterization of a human novel RAB (RAB39B) gene.";
RL Cytogenet. Genome Res. 97:72-75(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN XLID72.
RX PubMed=20159109; DOI=10.1016/j.ajhg.2010.01.011;
RA Giannandrea M., Bianchi V., Mignogna M.L., Sirri A., Carrabino S.,
RA D'Elia E., Vecellio M., Russo S., Cogliati F., Larizza L., Ropers H.H.,
RA Tzschach A., Kalscheuer V., Oehl-Jaschkowitz B., Skinner C., Schwartz C.E.,
RA Gecz J., Van Esch H., Raynaud M., Chelly J., de Brouwer A.P., Toniolo D.,
RA D'Adamo P.;
RT "Mutations in the small GTPase gene RAB39B are responsible for X-linked
RT mental retardation associated with autism, epilepsy, and macrocephaly.";
RL Am. J. Hum. Genet. 86:185-195(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=24349490; DOI=10.1371/journal.pone.0083324;
RA Seto S., Sugaya K., Tsujimura K., Nagata T., Horii T., Koide Y.;
RT "Rab39a interacts with phosphatidylinositol 3-kinase and negatively
RT regulates autophagy induced by lipopolysaccharide stimulation in
RT macrophages.";
RL PLoS ONE 8:E83324-E83324(2013).
RN [7]
RP INTERACTION WITH PICK1.
RX PubMed=25784538; DOI=10.1038/ncomms7504;
RA Mignogna M.L., Giannandrea M., Gurgone A., Fanelli F., Raimondi F.,
RA Mapelli L., Bassani S., Fang H., Van Anken E., Alessio M., Passafaro M.,
RA Gatti S., Esteban J.A., Huganir R., D'Adamo P.;
RT "The intellectual disability protein RAB39B selectively regulates GluA2
RT trafficking to determine synaptic AMPAR composition.";
RL Nat. Commun. 6:6504-6504(2015).
RN [8]
RP INVOLVEMENT IN WSMN, VARIANT WSMN LYS-168, AND CHARACTERIZATION OF VARIANT
RP WSMN LYS-168.
RX PubMed=25434005; DOI=10.1016/j.ajhg.2014.10.015;
RA Wilson G.R., Sim J.C., McLean C., Giannandrea M., Galea C.A., Riseley J.R.,
RA Stephenson S.E., Fitzpatrick E., Haas S.A., Pope K., Hogan K.J.,
RA Gregg R.G., Bromhead C.J., Wargowski D.S., Lawrence C.H., James P.A.,
RA Churchyard A., Gao Y., Phelan D.G., Gillies G., Salce N., Stanford L.,
RA Marsh A.P., Mignogna M.L., Hayflick S.J., Leventer R.J., Delatycki M.B.,
RA Mellick G.D., Kalscheuer V.M., D'Adamo P., Bahlo M., Amor D.J.,
RA Lockhart P.J.;
RT "Mutations in RAB39B cause X-linked intellectual disability and early-onset
RT Parkinson disease with alpha-synuclein pathology.";
RL Am. J. Hum. Genet. 95:729-735(2014).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF SER-22 AND GLN-68.
RX PubMed=27103069; DOI=10.15252/embj.201593350;
RA Sellier C., Campanari M.L., Julie Corbier C., Gaucherot A.,
RA Kolb-Cheynel I., Oulad-Abdelghani M., Ruffenach F., Page A., Ciura S.,
RA Kabashi E., Charlet-Berguerand N.;
RT "Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to
RT induce motor neuron dysfunction and cell death.";
RL EMBO J. 35:1276-1297(2016).
RN [10]
RP DISCUSSION ON INVOLVEMENT IN WSMN.
RX PubMed=27459931; DOI=10.1016/j.neurobiolaging.2016.03.021;
RA Hodges K., Brewer S.S., Labbe C., Soto-Ortolaza A.I., Walton R.L.,
RA Strongosky A.J., Uitti R.J., van Gerpen J.A., Ertekin-Taner N.,
RA Kantarci K., Lowe V.J., Parisi J.E., Savica R., Graff-Radford J.,
RA Jones D.T., Knopman D.S., Petersen R.C., Murray M.E., Graff-Radford N.R.,
RA Ferman T.J., Dickson D.W., Wszolek Z.K., Boeve B.F., Ross O.A.,
RA Lorenzo-Betancor O.;
RT "RAB39B gene mutations are not a common cause of Parkinson's disease or
RT dementia with Lewy bodies.";
RL Neurobiol. Aging 45:107-108(2016).
RN [11]
RP DISCUSSION ON INVOLVEMENT IN WSMN.
RX PubMed=26739247; DOI=10.1016/j.parkreldis.2015.12.014;
RA Loechte T., Brueggemann N., Vollstedt E.J., Krause P., Domingo A.,
RA Rosales R., Lee L.V., Hopfner F., Westenberger A., Kuehn A., Klein C.,
RA Lohmann K.;
RT "RAB39B mutations are a rare finding in Parkinson disease patients.";
RL Parkinsonism Relat. Disord. 23:116-117(2016).
RN [12]
RP VARIANT WSMN ARG-192, AND SUBCELLULAR LOCATION.
RX PubMed=26399558; DOI=10.1186/s13024-015-0045-4;
RA Mata I.F., Jang Y., Kim C.H., Hanna D.S., Dorschner M.O., Samii A.,
RA Agarwal P., Roberts J.W., Klepitskaya O., Shprecher D.R., Chung K.A.,
RA Factor S.A., Espay A.J., Revilla F.J., Higgins D.S., Litvan I.,
RA Leverenz J.B., Yearout D., Inca-Martinez M., Martinez E., Thompson T.R.,
RA Cholerton B.A., Hu S.C., Edwards K.L., Kim K.S., Zabetian C.P.;
RT "The RAB39B p.G192R mutation causes X-linked dominant Parkinson's
RT disease.";
RL Mol. Neurodegener. 10:50-50(2015).
RN [13]
RP VARIANT WSMN 186-TRP--CYS-213 DEL.
RX PubMed=27066548; DOI=10.1212/nxg.0000000000000009;
RG French Parkinson's Disease Genetics Study Group (PDG) and the International Parkinson's Disease Genomics Consortium (IPDGC);
RA Lesage S., Bras J., Cormier-Dequaire F., Condroyer C., Nicolas A.,
RA Darwent L., Guerreiro R., Majounie E., Federoff M., Heutink P., Wood N.W.,
RA Gasser T., Hardy J., Tison F., Singleton A., Brice A.;
RT "Loss-of-function mutations in RAB39B are associated with typical early-
RT onset Parkinson disease.";
RL Neurol. Genet. 1:E9-E9(2015).
CC -!- FUNCTION: Small GTPases Rab involved in autophagy (PubMed:27103069).
CC The small GTPases Rab are key regulators of intracellular membrane
CC trafficking, from the formation of transport vesicles to their fusion
CC with membranes. Rabs cycle between an inactive GDP-bound form and an
CC active GTP-bound form that is able to recruit to membranes different
CC sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion (PubMed:27103069). May
CC regulate the homeostasis of SNCA/alpha-synuclein. Together with PICK1
CC proposed to ensure selectively GRIA2 exit from the endoplasmic
CC reticulum to the Golgi and to regulate AMPAR compostion at the post-
CC synapses and thus synaptic transmission (By similarity).
CC {ECO:0000250|UniProtKB:Q8BHC1, ECO:0000269|PubMed:27103069}.
CC -!- SUBUNIT: Interacts (in GTP-bound form) with PICK1 (via PDZ domain); a
CC PICK1 homodimer may allow simultaneous association of RAB39B and GRIA2
CC to PICK1 which is involved in GRIA2 trafficking. Interacts with isoform
CC c of RASSF1; the interaction is strong (By similarity). Interacts with
CC isoform a of RASSF1; the interaction is weak (By similarity). Interacts
CC with the DLG4/PSD-95 (By similarity). {ECO:0000250|UniProtKB:Q8BHC1,
CC ECO:0000269|PubMed:25784538}.
CC -!- INTERACTION:
CC Q96DA2; Q08379: GOLGA2; NbExp=4; IntAct=EBI-9089467, EBI-618309;
CC Q96DA2; Q96T51: RUFY1; NbExp=4; IntAct=EBI-9089467, EBI-3941207;
CC Q96DA2; O14972: VPS26C; NbExp=3; IntAct=EBI-9089467, EBI-7207091;
CC Q96DA2; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-9089467, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle
CC membrane {ECO:0000269|PubMed:26399558}; Lipid-anchor {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Golgi apparatus
CC {ECO:0000269|PubMed:20159109, ECO:0000269|PubMed:24349490}.
CC Note=Partial colocalization with markers that cycle from the cell
CC surface to the trans-Golgi network. {ECO:0000250|UniProtKB:Q8BHC1}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain.
CC {ECO:0000269|PubMed:20159109}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 72 (XLID72)
CC [MIM:300271]: A disorder characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC Intellectual deficiency is the only primary symptom of non-syndromic X-
CC linked forms, while syndromic forms present with associated physical,
CC neurological and/or psychiatric manifestations. XLID72 patients can
CC manifest autism spectrum disorder, seizures and macrocephaly as
CC additional features. {ECO:0000269|PubMed:20159109}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Waisman syndrome (WSMN) [MIM:311510]: A neurologic disorder
CC characterized by delayed psychomotor development, intellectual
CC disability, and early-onset Parkinson disease.
CC {ECO:0000269|PubMed:25434005, ECO:0000269|PubMed:26399558,
CC ECO:0000269|PubMed:27066548}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Its association with
CC Parkinson disease is however unclear (PubMed:26739247,
CC PubMed:27459931). According to a number of studies, variations
CC affecting this gene are not a frequent cause of Parkinson disease,
CC suggesting that RAB39B does not play a major role in Parkinson disease
CC etiology (PubMed:26739247, PubMed:27459931).
CC {ECO:0000269|PubMed:26739247, ECO:0000269|PubMed:27459931}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY052478; AAL12244.1; -; mRNA.
DR EMBL; AL834460; CAD39120.1; -; mRNA.
DR EMBL; AL356738; CAI41468.1; -; Genomic_DNA.
DR EMBL; BC009714; AAH09714.1; -; mRNA.
DR CCDS; CCDS14766.1; -.
DR RefSeq; NP_741995.1; NM_171998.3.
DR PDB; 6S5F; X-ray; 1.70 A; A=1-207.
DR PDBsum; 6S5F; -.
DR AlphaFoldDB; Q96DA2; -.
DR SMR; Q96DA2; -.
DR BioGRID; 125507; 50.
DR IntAct; Q96DA2; 25.
DR MINT; Q96DA2; -.
DR STRING; 9606.ENSP00000358466; -.
DR iPTMnet; Q96DA2; -.
DR PhosphoSitePlus; Q96DA2; -.
DR BioMuta; RAB39B; -.
DR DMDM; 27734447; -.
DR EPD; Q96DA2; -.
DR jPOST; Q96DA2; -.
DR MassIVE; Q96DA2; -.
DR MaxQB; Q96DA2; -.
DR PaxDb; Q96DA2; -.
DR PeptideAtlas; Q96DA2; -.
DR PRIDE; Q96DA2; -.
DR ProteomicsDB; 76264; -.
DR Antibodypedia; 350; 193 antibodies from 28 providers.
DR DNASU; 116442; -.
DR Ensembl; ENST00000369454.4; ENSP00000358466.3; ENSG00000155961.5.
DR GeneID; 116442; -.
DR KEGG; hsa:116442; -.
DR MANE-Select; ENST00000369454.4; ENSP00000358466.3; NM_171998.4; NP_741995.1.
DR UCSC; uc004fne.5; human.
DR CTD; 116442; -.
DR DisGeNET; 116442; -.
DR GeneCards; RAB39B; -.
DR GeneReviews; RAB39B; -.
DR HGNC; HGNC:16499; RAB39B.
DR HPA; ENSG00000155961; Tissue enhanced (brain, retina).
DR MalaCards; RAB39B; -.
DR MIM; 300271; phenotype.
DR MIM; 300774; gene.
DR MIM; 311510; phenotype.
DR neXtProt; NX_Q96DA2; -.
DR OpenTargets; ENSG00000155961; -.
DR Orphanet; 2379; Early-onset parkinsonism-intellectual disability syndrome.
DR Orphanet; 106; NON RARE IN EUROPE: Autism.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA34131; -.
DR VEuPathDB; HostDB:ENSG00000155961; -.
DR eggNOG; KOG0091; Eukaryota.
DR GeneTree; ENSGT00940000158132; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q96DA2; -.
DR OMA; XSITRAY; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q96DA2; -.
DR TreeFam; TF300032; -.
DR PathwayCommons; Q96DA2; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q96DA2; -.
DR SIGNOR; Q96DA2; -.
DR BioGRID-ORCS; 116442; 12 hits in 695 CRISPR screens.
DR GeneWiki; RAB39B; -.
DR GenomeRNAi; 116442; -.
DR Pharos; Q96DA2; Tbio.
DR PRO; PR:Q96DA2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96DA2; protein.
DR Bgee; ENSG00000155961; Expressed in endothelial cell and 121 other tissues.
DR Genevisible; Q96DA2; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd04111; Rab39; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041818; Rab39.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autism spectrum disorder; Autophagy; Cell membrane;
KW Cytoplasmic vesicle; Disease variant; Golgi apparatus; GTP-binding;
KW Intellectual disability; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Parkinson disease; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..213
FT /note="Ras-related protein Rab-39B"
FT /id="PRO_0000121255"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHC1"
FT MOD_RES 213
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 168
FT /note="T -> K (in WSMN; loss of function mutation;
FT expression of the mutation in neuroblastoma cells results
FT in low levels of the mutant protein; dbSNP:rs587777874)"
FT /evidence="ECO:0000269|PubMed:25434005"
FT /id="VAR_073264"
FT VARIANT 186..213
FT /note="Missing (in WSMN)"
FT /evidence="ECO:0000269|PubMed:27066548"
FT /id="VAR_078514"
FT VARIANT 192
FT /note="G -> R (in WSMN; impaired localization to
FT cytoplasmic vesicles; dbSNP:rs864309527)"
FT /evidence="ECO:0000269|PubMed:26399558"
FT /id="VAR_078515"
FT MUTAGEN 22
FT /note="S->N: Dominant negative mutant."
FT /evidence="ECO:0000269|PubMed:27103069"
FT MUTAGEN 68
FT /note="Q->L: Constitutively active mutant locked in the
FT active GTP-bound form."
FT /evidence="ECO:0000269|PubMed:27103069"
FT CONFLICT 57
FT /note="R -> T (in Ref. 1; AAL12244)"
FT /evidence="ECO:0000305"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:6S5F"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:6S5F"
FT STRAND 42..53
FT /evidence="ECO:0007829|PDB:6S5F"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:6S5F"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6S5F"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:6S5F"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6S5F"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:6S5F"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:6S5F"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6S5F"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6S5F"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6S5F"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:6S5F"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6S5F"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:6S5F"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:6S5F"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6S5F"
SQ SEQUENCE 213 AA; 24622 MW; 2B2C5B35C61FA88E CRC64;
MEAIWLYQFR LIVIGDSTVG KSCLIRRFTE GRFAQVSDPT VGVDFFSRLV EIEPGKRIKL
QIWDTAGQER FRSITRAYYR NSVGGLLLFD ITNRRSFQNV HEWLEETKVH VQPYQIVFVL
VGHKCDLDTQ RQVTRHEAEK LAAAYGMKYI ETSARDAINV EKAFTDLTRD IYELVKRGEI
TIQEGWEGVK SGFVPNVVHS SEEVVKSERR CLC
