RAB14_HUMAN
ID RAB14_HUMAN Reviewed; 215 AA.
AC P61106; B3KR31; P35287; Q5JVD4; Q6Q7K5; Q969L0; Q9UI11;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Ras-related protein Rab-14;
GN Name=RAB14;
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], AND VARIANT THR-4.
RC TISSUE=Liver;
RA Proikas-Cezanne T., Jenkins J.R.;
RT "Human Rab14 cloning and intracellular localization to the
RT biosynthetic/secretory trafficking pathway.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-4.
RA Ren Y.;
RT "Cloning and characterization of human small GTPase Rab14.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang Y.-P., Wang L., Cheng J.;
RT "Screening and identification of HCV F protein-binding protein 1.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala, and Placenta;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-4.
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [12]
RP PROTEIN SEQUENCE OF 2-24; 36-59; 62-72; 83-95; 97-132 AND 141-171, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (FEB-2006) to UniProtKB.
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=16962593; DOI=10.1016/j.febslet.2006.08.053;
RA Proikas-Cezanne T., Gaugel A., Frickey T., Nordheim A.;
RT "Rab14 is part of the early endosomal clathrin-coated TGN microdomain.";
RL FEBS Lett. 580:5241-5246(2006).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
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 [16]
RP 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 [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22595670; DOI=10.1016/j.devcel.2012.04.010;
RA Linford A., Yoshimura S., Nunes Bastos R., Langemeyer L., Gerondopoulos A.,
RA Rigden D.J., Barr F.A.;
RT "Rab14 and its exchange factor FAM116 link endocytic recycling and adherens
RT junction stability in migrating cells.";
RL Dev. Cell 22:952-966(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP IDENTIFICATION BY 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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-175 IN COMPLEX WITH GDP, AND
RP INTERACTION WITH ZFYVE20.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-181 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB14.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in membrane trafficking between the Golgi complex
CC and endosomes during early embryonic development. Regulates the Golgi
CC to endosome transport of FGFR-containing vesicles during early
CC development, a key process for developing basement membrane and
CC epiblast and primitive endoderm lineages during early postimplantation
CC development. May act by modulating the kinesin KIF16B-cargo association
CC to endosomes (By similarity). Regulates, together with its guanine
CC nucleotide exchange factor DENND6A, the specific endocytic transport of
CC ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion. {ECO:0000250,
CC ECO:0000269|PubMed:22595670}.
CC -!- SUBUNIT: Interacts with KIF16B (By similarity). Interacts with ZFYVE20.
CC {ECO:0000250, ECO:0000269|PubMed:16034420, ECO:0000269|Ref.22}.
CC -!- INTERACTION:
CC P61106; O00471: EXOC5; NbExp=6; IntAct=EBI-1056404, EBI-949824;
CC P61106; Q8NEG0: FAM71C; NbExp=3; IntAct=EBI-1056404, EBI-752049;
CC P61106; Q01968: OCRL; NbExp=3; IntAct=EBI-1056404, EBI-6148898;
CC P61106; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-1056404, EBI-747389;
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:22595670}.
CC Early endosome membrane {ECO:0000269|PubMed:16962593}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16962593}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:16962593}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:21255211}. Note=Recruited to recycling endosomes by
CC DENND6A (PubMed:22595670). Recruited to phagosomes containing S.aureus
CC or M.tuberculosis (PubMed:21255211). {ECO:0000269|PubMed:21255211,
CC ECO:0000269|PubMed:22595670}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF152463; AAF00150.1; -; mRNA.
DR EMBL; AF203689; AAF19400.1; -; mRNA.
DR EMBL; AY553875; AAS64573.1; -; mRNA.
DR EMBL; AF112206; AAF17194.1; -; mRNA.
DR EMBL; AL162081; CAB82414.1; -; mRNA.
DR EMBL; AK023524; BAB14598.1; -; mRNA.
DR EMBL; AK090889; BAG52243.1; -; mRNA.
DR EMBL; AF498949; AAM21097.1; -; mRNA.
DR EMBL; AL137068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR457394; CAG33675.1; -; mRNA.
DR EMBL; CH471090; EAW87487.1; -; Genomic_DNA.
DR EMBL; BC006081; AAH06081.1; -; mRNA.
DR CCDS; CCDS6827.1; -.
DR RefSeq; NP_057406.2; NM_016322.3.
DR PDB; 1Z0F; X-ray; 2.15 A; A=2-175.
DR PDB; 4D0G; X-ray; 2.50 A; A=8-180.
DR PDB; 4DRZ; X-ray; 2.30 A; A=1-177.
DR PDBsum; 1Z0F; -.
DR PDBsum; 4D0G; -.
DR PDBsum; 4DRZ; -.
DR AlphaFoldDB; P61106; -.
DR SMR; P61106; -.
DR BioGRID; 119605; 188.
DR DIP; DIP-42491N; -.
DR IntAct; P61106; 47.
DR MINT; P61106; -.
DR STRING; 9606.ENSP00000362946; -.
DR GlyGen; P61106; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61106; -.
DR MetOSite; P61106; -.
DR PhosphoSitePlus; P61106; -.
DR SwissPalm; P61106; -.
DR BioMuta; RAB14; -.
DR DMDM; 85700392; -.
DR EPD; P61106; -.
DR jPOST; P61106; -.
DR MassIVE; P61106; -.
DR MaxQB; P61106; -.
DR PaxDb; P61106; -.
DR PeptideAtlas; P61106; -.
DR PRIDE; P61106; -.
DR ProteomicsDB; 57265; -.
DR Antibodypedia; 15967; 173 antibodies from 31 providers.
DR DNASU; 51552; -.
DR Ensembl; ENST00000373840.9; ENSP00000362946.4; ENSG00000119396.11.
DR GeneID; 51552; -.
DR KEGG; hsa:51552; -.
DR MANE-Select; ENST00000373840.9; ENSP00000362946.4; NM_016322.4; NP_057406.2.
DR UCSC; uc004blc.4; human.
DR CTD; 51552; -.
DR DisGeNET; 51552; -.
DR GeneCards; RAB14; -.
DR HGNC; HGNC:16524; RAB14.
DR HPA; ENSG00000119396; Low tissue specificity.
DR MIM; 612673; gene.
DR neXtProt; NX_P61106; -.
DR OpenTargets; ENSG00000119396; -.
DR PharmGKB; PA34104; -.
DR VEuPathDB; HostDB:ENSG00000119396; -.
DR eggNOG; KOG0097; Eukaryota.
DR GeneTree; ENSGT00940000155178; -.
DR InParanoid; P61106; -.
DR OMA; TRRITYN; -.
DR OrthoDB; 1146851at2759; -.
DR PhylomeDB; P61106; -.
DR TreeFam; TF300032; -.
DR PathwayCommons; P61106; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P61106; -.
DR SIGNOR; P61106; -.
DR BioGRID-ORCS; 51552; 50 hits in 1055 CRISPR screens.
DR ChiTaRS; RAB14; human.
DR EvolutionaryTrace; P61106; -.
DR GeneWiki; RAB14; -.
DR GenomeRNAi; 51552; -.
DR Pharos; P61106; Tbio.
DR PRO; PR:P61106; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P61106; protein.
DR Bgee; ENSG00000119396; Expressed in nipple and 211 other tissues.
DR ExpressionAtlas; P61106; baseline and differential.
DR Genevisible; P61106; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IEA:InterPro.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR GO; GO:0032456; P:endocytic recycling; IDA:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; NAS:UniProtKB.
DR GO; GO:0090387; P:phagolysosome assembly involved in apoptotic cell clearance; IBA:GO_Central.
DR GO; GO:0090382; P:phagosome maturation; ISS:FlyBase.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
DR CDD; cd04122; Rab14; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030702; Rab14.
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; Acetylation; Cytoplasmic vesicle; Direct protein sequencing;
KW Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..215
FT /note="Ras-related protein Rab-14"
FT /id="PRO_0000121185"
FT REGION 188..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 215
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 4
FT /note="A -> T"
FT /evidence="ECO:0000269|Ref.1, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.7"
FT /id="VAR_012986"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:1Z0F"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:1Z0F"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1Z0F"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:1Z0F"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1Z0F"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:1Z0F"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1Z0F"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:1Z0F"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1Z0F"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1Z0F"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1Z0F"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:1Z0F"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1Z0F"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1Z0F"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:1Z0F"
SQ SEQUENCE 215 AA; 23897 MW; BC8A8B98FB9944AC CRC64;
MATAPYNYSY IFKYIIIGDM GVGKSCLLHQ FTEKKFMADC PHTIGVEFGT RIIEVSGQKI
KLQIWDTAGQ ERFRAVTRSY YRGAAGALMV YDITRRSTYN HLSSWLTDAR NLTNPNTVII
LIGNKADLEA QRDVTYEEAK QFAEENGLLF LEASAKTGEN VEDAFLEAAK KIYQNIQDGS
LDLNAAESGV QHKPSAPQGG RLTSEPQPQR EGCGC
