Full text data of RAB14
RAB14
[Confidence: high (present in two of the MS resources)]
Ras-related protein Rab-14
Ras-related protein Rab-14
hRBCD
IPI00291928
IPI00291928 Ras-related protein Rab-14 Ras-related protein Rab-14 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a cytoplasmic and membrane associated n/a expected molecular weight found in band ~ 17 kDa
IPI00291928 Ras-related protein Rab-14 Ras-related protein Rab-14 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a cytoplasmic and membrane associated n/a expected molecular weight found in band ~ 17 kDa
UniProt
P61106
ID RAB14_HUMAN Reviewed; 215 AA.
AC P61106; B3KR31; P35287; Q5JVD4; Q6Q7K5; Q969L0; Q9UI11;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Ras-related protein Rab-14;
GN Name=RAB14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT sequenced by 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND 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
RT microdomain.";
RL FEBS Lett. 580:5241-5246(2006).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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
RT recruited 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.,
RA Gerondopoulos A., Rigden D.J., Barr F.A.;
RT "Rab14 and its exchange factor FAM116 link endocytic recycling and
RT adherens junction stability in migrating cells.";
RL Dev. Cell 22:952-966(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-175 IN COMPLEX WITH GDP,
RP AND 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-
RT 5.";
RL Nature 436:415-419(2005).
RN [19]
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
CC complex and endosomes during early embryonic development.
CC Regulates the Golgi to endosome transport of FGFR-containing
CC vesicles during early development, a key process for developing
CC basement membrane and epiblast and primitive endoderm lineages
CC during early postimplantation development. May act by modulating
CC the kinesin KIF16B-cargo association to endosomes (By similarity).
CC Regulates, together with its guanine nucleotide exchange factor
CC DENND6A, the specific endocytic transport of ADAM10, N-
CC cadherin/CDH2 shedding and cell-cell adhesion.
CC -!- SUBUNIT: Interacts with KIF16B (By similarity). Interacts with
CC ZFYVE20.
CC -!- INTERACTION:
CC Q01968:OCRL; NbExp=3; IntAct=EBI-1056404, EBI-6148898;
CC -!- SUBCELLULAR LOCATION: Recycling endosome. Early endosome membrane;
CC Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-
CC anchor; Cytoplasmic side (By similarity). Golgi apparatus, trans-
CC Golgi network membrane; Lipid-anchor; Cytoplasmic side.
CC Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome
CC membrane; Lipid-anchor; Cytoplasmic side (By similarity).
CC Note=Recruited to recycling endosomes by DENND6A. Recruited to
CC phagosomes containing S.aureus or M.tuberculosis.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI12361.1; Type=Erroneous gene model prediction;
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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; CAD20124.1; -; Genomic_DNA.
DR EMBL; AL137068; CAI12361.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CR457394; CAG33675.1; -; mRNA.
DR EMBL; CH471090; EAW87487.1; -; Genomic_DNA.
DR EMBL; BC006081; AAH06081.1; -; mRNA.
DR RefSeq; NP_057406.2; NM_016322.3.
DR UniGene; Hs.371563; -.
DR PDB; 1Z0F; X-ray; 2.15 A; A=2-175.
DR PDB; 4DRZ; X-ray; 2.30 A; A=1-181.
DR PDBsum; 1Z0F; -.
DR PDBsum; 4DRZ; -.
DR ProteinModelPortal; P61106; -.
DR SMR; P61106; 7-173.
DR IntAct; P61106; 10.
DR MINT; MINT-2882831; -.
DR STRING; 9606.ENSP00000362946; -.
DR PhosphoSite; P61106; -.
DR DMDM; 85700392; -.
DR PaxDb; P61106; -.
DR PeptideAtlas; P61106; -.
DR PRIDE; P61106; -.
DR DNASU; 51552; -.
DR Ensembl; ENST00000373840; ENSP00000362946; ENSG00000119396.
DR GeneID; 51552; -.
DR KEGG; hsa:51552; -.
DR UCSC; uc004blc.3; human.
DR CTD; 51552; -.
DR GeneCards; GC09M123940; -.
DR HGNC; HGNC:16524; RAB14.
DR HPA; HPA026419; -.
DR MIM; 612673; gene.
DR neXtProt; NX_P61106; -.
DR PharmGKB; PA34104; -.
DR eggNOG; COG1100; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P61106; -.
DR KO; K07881; -.
DR OMA; ASCPHTI; -.
DR OrthoDB; EOG7QK0CV; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR SignaLink; P61106; -.
DR ChiTaRS; RAB14; human.
DR EvolutionaryTrace; P61106; -.
DR GeneWiki; RAB14; -.
DR GenomeRNAi; 51552; -.
DR NextBio; 55334; -.
DR PRO; PR:P61106; -.
DR Bgee; P61106; -.
DR CleanEx; HS_RAB14; -.
DR Genevestigator; P61106; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA: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:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
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:0009790; P:embryo development; ISS:UniProtKB.
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:0007269; P:neurotransmitter secretion; NAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; IDA:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; NAS:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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; Complete proteome; Cytoplasmic vesicle;
KW Direct protein sequencing; Endosome; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Polymorphism;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Ras-related protein Rab-14.
FT /FTId=PRO_0000121185.
FT NP_BIND 18 26 GTP.
FT NP_BIND 66 70 GTP.
FT NP_BIND 124 127 GTP.
FT NP_BIND 154 156 GTP.
FT MOTIF 40 48 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 215 215 Cysteine methyl ester (By similarity).
FT LIPID 213 213 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 215 215 S-geranylgeranyl cysteine (By
FT similarity).
FT VARIANT 4 4 A -> T.
FT /FTId=VAR_012986.
FT STRAND 9 17
FT HELIX 24 33
FT STRAND 48 55
FT STRAND 58 66
FT HELIX 70 72
FT HELIX 75 82
FT STRAND 85 92
FT HELIX 96 100
FT HELIX 102 112
FT STRAND 118 124
FT HELIX 129 131
FT HELIX 136 145
FT STRAND 149 152
FT TURN 155 157
FT HELIX 161 172
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
//
ID RAB14_HUMAN Reviewed; 215 AA.
AC P61106; B3KR31; P35287; Q5JVD4; Q6Q7K5; Q969L0; Q9UI11;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Ras-related protein Rab-14;
GN Name=RAB14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT sequenced by 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND 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
RT microdomain.";
RL FEBS Lett. 580:5241-5246(2006).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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
RT recruited 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.,
RA Gerondopoulos A., Rigden D.J., Barr F.A.;
RT "Rab14 and its exchange factor FAM116 link endocytic recycling and
RT adherens junction stability in migrating cells.";
RL Dev. Cell 22:952-966(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-175 IN COMPLEX WITH GDP,
RP AND 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-
RT 5.";
RL Nature 436:415-419(2005).
RN [19]
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
CC complex and endosomes during early embryonic development.
CC Regulates the Golgi to endosome transport of FGFR-containing
CC vesicles during early development, a key process for developing
CC basement membrane and epiblast and primitive endoderm lineages
CC during early postimplantation development. May act by modulating
CC the kinesin KIF16B-cargo association to endosomes (By similarity).
CC Regulates, together with its guanine nucleotide exchange factor
CC DENND6A, the specific endocytic transport of ADAM10, N-
CC cadherin/CDH2 shedding and cell-cell adhesion.
CC -!- SUBUNIT: Interacts with KIF16B (By similarity). Interacts with
CC ZFYVE20.
CC -!- INTERACTION:
CC Q01968:OCRL; NbExp=3; IntAct=EBI-1056404, EBI-6148898;
CC -!- SUBCELLULAR LOCATION: Recycling endosome. Early endosome membrane;
CC Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-
CC anchor; Cytoplasmic side (By similarity). Golgi apparatus, trans-
CC Golgi network membrane; Lipid-anchor; Cytoplasmic side.
CC Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome
CC membrane; Lipid-anchor; Cytoplasmic side (By similarity).
CC Note=Recruited to recycling endosomes by DENND6A. Recruited to
CC phagosomes containing S.aureus or M.tuberculosis.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI12361.1; Type=Erroneous gene model prediction;
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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; CAD20124.1; -; Genomic_DNA.
DR EMBL; AL137068; CAI12361.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CR457394; CAG33675.1; -; mRNA.
DR EMBL; CH471090; EAW87487.1; -; Genomic_DNA.
DR EMBL; BC006081; AAH06081.1; -; mRNA.
DR RefSeq; NP_057406.2; NM_016322.3.
DR UniGene; Hs.371563; -.
DR PDB; 1Z0F; X-ray; 2.15 A; A=2-175.
DR PDB; 4DRZ; X-ray; 2.30 A; A=1-181.
DR PDBsum; 1Z0F; -.
DR PDBsum; 4DRZ; -.
DR ProteinModelPortal; P61106; -.
DR SMR; P61106; 7-173.
DR IntAct; P61106; 10.
DR MINT; MINT-2882831; -.
DR STRING; 9606.ENSP00000362946; -.
DR PhosphoSite; P61106; -.
DR DMDM; 85700392; -.
DR PaxDb; P61106; -.
DR PeptideAtlas; P61106; -.
DR PRIDE; P61106; -.
DR DNASU; 51552; -.
DR Ensembl; ENST00000373840; ENSP00000362946; ENSG00000119396.
DR GeneID; 51552; -.
DR KEGG; hsa:51552; -.
DR UCSC; uc004blc.3; human.
DR CTD; 51552; -.
DR GeneCards; GC09M123940; -.
DR HGNC; HGNC:16524; RAB14.
DR HPA; HPA026419; -.
DR MIM; 612673; gene.
DR neXtProt; NX_P61106; -.
DR PharmGKB; PA34104; -.
DR eggNOG; COG1100; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P61106; -.
DR KO; K07881; -.
DR OMA; ASCPHTI; -.
DR OrthoDB; EOG7QK0CV; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR SignaLink; P61106; -.
DR ChiTaRS; RAB14; human.
DR EvolutionaryTrace; P61106; -.
DR GeneWiki; RAB14; -.
DR GenomeRNAi; 51552; -.
DR NextBio; 55334; -.
DR PRO; PR:P61106; -.
DR Bgee; P61106; -.
DR CleanEx; HS_RAB14; -.
DR Genevestigator; P61106; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA: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:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
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:0009790; P:embryo development; ISS:UniProtKB.
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:0007269; P:neurotransmitter secretion; NAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; IDA:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; NAS:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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; Complete proteome; Cytoplasmic vesicle;
KW Direct protein sequencing; Endosome; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Polymorphism;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Ras-related protein Rab-14.
FT /FTId=PRO_0000121185.
FT NP_BIND 18 26 GTP.
FT NP_BIND 66 70 GTP.
FT NP_BIND 124 127 GTP.
FT NP_BIND 154 156 GTP.
FT MOTIF 40 48 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 215 215 Cysteine methyl ester (By similarity).
FT LIPID 213 213 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 215 215 S-geranylgeranyl cysteine (By
FT similarity).
FT VARIANT 4 4 A -> T.
FT /FTId=VAR_012986.
FT STRAND 9 17
FT HELIX 24 33
FT STRAND 48 55
FT STRAND 58 66
FT HELIX 70 72
FT HELIX 75 82
FT STRAND 85 92
FT HELIX 96 100
FT HELIX 102 112
FT STRAND 118 124
FT HELIX 129 131
FT HELIX 136 145
FT STRAND 149 152
FT TURN 155 157
FT HELIX 161 172
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
//
MIM
612673
*RECORD*
*FIELD* NO
612673
*FIELD* TI
*612673 RAS-ASSOCIATED PROTEIN RAB14; RAB14
*FIELD* TX
DESCRIPTION
RAB14 belongs to the large RAB family of low molecular mass GTPases that
read moreare involved in intracellular membrane trafficking. These proteins act
as molecular switches that flip between an inactive GDP-bound state and
an active GTP-bound state in which they recruit downstream effector
proteins onto membranes (Junutula et al., 2004).
CLONING
By searching databases using rat Rab14, Junutula et al. (2004)
identified human and mouse RAB14. The mouse and human proteins contain
215 amino acids and are identical to the rat protein except for the
fourth residue, which is threonine in rat and alanine in mouse and
human. RAB14 is most closely related to the Golgi membrane protein RAB2
(179509) and the endosomal protein RAB4 (179511). PCR analysis of human
tissues detected ubiquitous RAB14 expression, with high levels in brain,
heart, kidney, placenta, lung, pancreas, spleen, and testis, and lower
levels in muscle, thymus, intestine, colon, and leukocytes. Western blot
analysis detected Rab14 at an apparent molecular mass of 24 kD in most
rat tissues examined and at 28 kD in heart. Immunohistochemical analysis
of several cell lines, including HeLa cells, revealed endogenous RAB14
in small puncta throughout the cell and in perinuclear structures. RAB14
staining partially overlapped with markers for early and recycling
endosomes, cis-Golgi, and trans-Golgi network. Immunogold labeling of
normal rat kidney cells revealed membrane-bound Rab14 associated with
multiple membrane and vesicular structures. Most Rab14 was associated
with small tubulo-vesicular structures throughout the cytoplasm, with
Golgi stack and associated vesicles, and with endoplasmic reticulum. A
minor fraction was associated with endosomal vacuoles and the plasma
membrane.
GENE FUNCTION
Junutula et al. (2004) found that overexpression of rat Rab14 with a
mutation predicted to result in a GTP-bound conformation (gln70 to leu)
shifted the distribution of Rab14 toward early endosome-associated
vesicles. In contrast, overexpression of RAB14 with mutations predicted
to result in nucleotide-free and GDP-bound conformations (asn124 to ile
and ser25 to asn, respectively) induced a shift toward the Golgi region.
Overexpression of these mutants caused a similar, but less pronounced,
redistribution of transferrin receptor (TFRC; 190010), but transferrin
(TF; 190000) uptake and receptor recycling were unaffected. Junutula et
al. (2004) concluded that RAB14 is involved in the
biosynthetic/recycling pathway between the Golgi and endosomal
compartments.
In muscle and fat cells, insulin (INS; 176730) stimulation activates a
signaling cascade that causes intracellular vesicles containing glucose
transporter-4 (GLUT4, or SLC2A4; 138190) to translocate to and fuse with
the plasma membrane. Using mass spectrometry, Larance et al. (2005)
identified Rab10 (612672), Rab11 (see RAB11A; 605570), and Rab14 on
Glut4 vesicles from cultured mouse adipocytes. These vesicles also
contained the RAB GTPase-activating protein (GAP) As160 (TBC1D4;
612465), suggesting that the RAB proteins may be AS160 substrates.
Miinea et al. (2005) found that the purified recombinant GAP domain of
human AS160 showed GAP activity with RAB2A, RAB8A (165040), RAB10, and
RAB14, but not with 14 other RABs. Immunoblot analysis showed that these
RABs associated with Glut4-positive vesicles in mouse adipocytes. Miinea
et al. (2005) concluded that AK160 functions as a RAB GAP and that RABs
may participate in GLUT4 translocation.
MAPPING
Hartz (2009) mapped the RAB14 gene to chromosome 9q33.2 based on an
alignment of the RAB14 sequence (GENBANK GenBank AF152463) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 3/18/2009.
2. Junutula, J. R.; De Maziere, A. M.; Peden, A. A.; Ervin, K. E.;
Advani, R. J.; van Dijk, S. M.; Klumperman, J.; Scheller, R. H.:
Rab14 is involved in membrane trafficking between the Golgi complex
and endosomes. Molec. Biol. Cell 15: 2218-2229, 2004.
3. Larance, M.; Ramm, G.; Stockli, J.; van Dam, E. M.; Winata, S.;
Wasinger, V.; Simpson, F.; Graham, M.; Junutula, J. R.; Guilhaus,
M.; James, D. E.: Characterization of the role of the Rab GTPase-activating
protein AS160 in insulin-regulated GLUT4 trafficking. J. Biol. Chem. 280:
37803-37813, 2005.
4. Miinea, C. P.; Sano, H.; Kane, S.; Sano, E.; Fukuda, M.; Peranen,
J.; Lane, W. S.; Lienhard, G. E.: AS160, the Akt substrate regulating
GLUT4 translocation, has a functional Rab GTPase-activating protein
domain. Biochem. J. 391: 87-93, 2005.
*FIELD* CD
Patricia A. Hartz: 3/18/2009
*FIELD* ED
mgross: 03/18/2009
*RECORD*
*FIELD* NO
612673
*FIELD* TI
*612673 RAS-ASSOCIATED PROTEIN RAB14; RAB14
*FIELD* TX
DESCRIPTION
RAB14 belongs to the large RAB family of low molecular mass GTPases that
read moreare involved in intracellular membrane trafficking. These proteins act
as molecular switches that flip between an inactive GDP-bound state and
an active GTP-bound state in which they recruit downstream effector
proteins onto membranes (Junutula et al., 2004).
CLONING
By searching databases using rat Rab14, Junutula et al. (2004)
identified human and mouse RAB14. The mouse and human proteins contain
215 amino acids and are identical to the rat protein except for the
fourth residue, which is threonine in rat and alanine in mouse and
human. RAB14 is most closely related to the Golgi membrane protein RAB2
(179509) and the endosomal protein RAB4 (179511). PCR analysis of human
tissues detected ubiquitous RAB14 expression, with high levels in brain,
heart, kidney, placenta, lung, pancreas, spleen, and testis, and lower
levels in muscle, thymus, intestine, colon, and leukocytes. Western blot
analysis detected Rab14 at an apparent molecular mass of 24 kD in most
rat tissues examined and at 28 kD in heart. Immunohistochemical analysis
of several cell lines, including HeLa cells, revealed endogenous RAB14
in small puncta throughout the cell and in perinuclear structures. RAB14
staining partially overlapped with markers for early and recycling
endosomes, cis-Golgi, and trans-Golgi network. Immunogold labeling of
normal rat kidney cells revealed membrane-bound Rab14 associated with
multiple membrane and vesicular structures. Most Rab14 was associated
with small tubulo-vesicular structures throughout the cytoplasm, with
Golgi stack and associated vesicles, and with endoplasmic reticulum. A
minor fraction was associated with endosomal vacuoles and the plasma
membrane.
GENE FUNCTION
Junutula et al. (2004) found that overexpression of rat Rab14 with a
mutation predicted to result in a GTP-bound conformation (gln70 to leu)
shifted the distribution of Rab14 toward early endosome-associated
vesicles. In contrast, overexpression of RAB14 with mutations predicted
to result in nucleotide-free and GDP-bound conformations (asn124 to ile
and ser25 to asn, respectively) induced a shift toward the Golgi region.
Overexpression of these mutants caused a similar, but less pronounced,
redistribution of transferrin receptor (TFRC; 190010), but transferrin
(TF; 190000) uptake and receptor recycling were unaffected. Junutula et
al. (2004) concluded that RAB14 is involved in the
biosynthetic/recycling pathway between the Golgi and endosomal
compartments.
In muscle and fat cells, insulin (INS; 176730) stimulation activates a
signaling cascade that causes intracellular vesicles containing glucose
transporter-4 (GLUT4, or SLC2A4; 138190) to translocate to and fuse with
the plasma membrane. Using mass spectrometry, Larance et al. (2005)
identified Rab10 (612672), Rab11 (see RAB11A; 605570), and Rab14 on
Glut4 vesicles from cultured mouse adipocytes. These vesicles also
contained the RAB GTPase-activating protein (GAP) As160 (TBC1D4;
612465), suggesting that the RAB proteins may be AS160 substrates.
Miinea et al. (2005) found that the purified recombinant GAP domain of
human AS160 showed GAP activity with RAB2A, RAB8A (165040), RAB10, and
RAB14, but not with 14 other RABs. Immunoblot analysis showed that these
RABs associated with Glut4-positive vesicles in mouse adipocytes. Miinea
et al. (2005) concluded that AK160 functions as a RAB GAP and that RABs
may participate in GLUT4 translocation.
MAPPING
Hartz (2009) mapped the RAB14 gene to chromosome 9q33.2 based on an
alignment of the RAB14 sequence (GENBANK GenBank AF152463) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 3/18/2009.
2. Junutula, J. R.; De Maziere, A. M.; Peden, A. A.; Ervin, K. E.;
Advani, R. J.; van Dijk, S. M.; Klumperman, J.; Scheller, R. H.:
Rab14 is involved in membrane trafficking between the Golgi complex
and endosomes. Molec. Biol. Cell 15: 2218-2229, 2004.
3. Larance, M.; Ramm, G.; Stockli, J.; van Dam, E. M.; Winata, S.;
Wasinger, V.; Simpson, F.; Graham, M.; Junutula, J. R.; Guilhaus,
M.; James, D. E.: Characterization of the role of the Rab GTPase-activating
protein AS160 in insulin-regulated GLUT4 trafficking. J. Biol. Chem. 280:
37803-37813, 2005.
4. Miinea, C. P.; Sano, H.; Kane, S.; Sano, E.; Fukuda, M.; Peranen,
J.; Lane, W. S.; Lienhard, G. E.: AS160, the Akt substrate regulating
GLUT4 translocation, has a functional Rab GTPase-activating protein
domain. Biochem. J. 391: 87-93, 2005.
*FIELD* CD
Patricia A. Hartz: 3/18/2009
*FIELD* ED
mgross: 03/18/2009