Full text data of RAB5B
RAB5B
[Confidence: high (present in two of the MS resources)]
Ras-related protein Rab-5B
Ras-related protein Rab-5B
hRBCD
IPI00017344
IPI00017344 Ras-related protein Rab-5B TAMNVNDLFLAIAK unique Ras-related protein Rab-5B TAMNVNDLFLAIAK unique membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 1 n/a 1 n/a n/a n/a 2 n/a 3 inner surface of plasma membrane, Plasma membrane-associated TAMNVNDLFLAIAK , GVDLHEQSQQNK, SEPQNLGGAAGR found at its expected molecular weight found at molecular weight
IPI00017344 Ras-related protein Rab-5B TAMNVNDLFLAIAK unique Ras-related protein Rab-5B TAMNVNDLFLAIAK unique membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 1 n/a 1 n/a n/a n/a 2 n/a 3 inner surface of plasma membrane, Plasma membrane-associated TAMNVNDLFLAIAK , GVDLHEQSQQNK, SEPQNLGGAAGR found at its expected molecular weight found at molecular weight
UniProt
P61020
ID RAB5B_HUMAN Reviewed; 215 AA.
AC P61020; A8K982; B4DKD7; P35239; P35277; Q6PIK9; Q86TH0; Q8IXL2;
read moreDT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Ras-related protein Rab-5B;
GN Name=RAB5B;
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] (ISOFORM 1).
RX PubMed=1541686; DOI=10.1172/JCI115683;
RA Wilson D.B., Wilson M.P.;
RT "Identification and subcellular localization of human rab5b, a new
RT member of the ras-related superfamily of GTPases.";
RL J. Clin. Invest. 89:996-1005(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, PNS, and Skin;
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 [8]
RP INTERACTION WITH EEA1.
RX PubMed=10491193; DOI=10.1046/j.1432-1327.1999.00743.x;
RA Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.;
RT "Direct interaction of EEA1 with Rab5b.";
RL Eur. J. Biochem. 265:361-366(1999).
RN [9]
RP INTERACTION WITH RIN2 AND RIN3, AND MUTAGENESIS OF SER-34 AND GLN-79.
RX PubMed=11733506; DOI=10.1074/jbc.M106276200;
RA Saito K., Murai J., Kajiho H., Kontani K., Kurosu H., Katada T.;
RT "A novel binding protein composed of homophilic tetramer exhibits
RT unique properties for the small GTPase Rab5.";
RL J. Biol. Chem. 277:3412-3418(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 15-191 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB5B in complex with GDP.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Protein transport. Probably involved in vesicular
CC traffic (By similarity).
CC -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
CC factors (GEFs) which promote the exchange of bound GDP for free
CC GTP.
CC -!- SUBUNIT: Binds EEA1. Interacts with RIN2 and RIN3, which probably
CC regulate its pathway, possibly by acting as GEFs.
CC -!- INTERACTION:
CC Q15075:EEA1; NbExp=3; IntAct=EBI-399401, EBI-298113;
CC Q5S007:LRRK2; NbExp=4; IntAct=EBI-399401, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side. Early endosome membrane; Lipid-anchor. Melanosome.
CC Note=Enriched in stage I melanosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61020-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61020-2; Sequence=VSP_045301;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH40143.1; Type=Erroneous initiation;
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DR EMBL; X54871; CAA38653.1; -; mRNA.
DR EMBL; AF498937; AAM21085.1; -; mRNA.
DR EMBL; AK292597; BAF85286.1; -; mRNA.
DR EMBL; AK296517; BAG59149.1; -; mRNA.
DR EMBL; BX537408; CAD97650.1; -; mRNA.
DR EMBL; AC034102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96862.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96864.1; -; Genomic_DNA.
DR EMBL; BC032740; AAH32740.1; -; mRNA.
DR EMBL; BC040143; AAH40143.1; ALT_INIT; mRNA.
DR EMBL; BC050558; AAH50558.2; -; mRNA.
DR EMBL; BC056422; AAH56422.2; -; mRNA.
DR EMBL; BC065298; AAH65298.2; -; mRNA.
DR PIR; A43925; A43925.
DR RefSeq; NP_001238965.1; NM_001252036.1.
DR RefSeq; NP_001238966.1; NM_001252037.1.
DR RefSeq; NP_002859.1; NM_002868.3.
DR RefSeq; XP_005269108.1; XM_005269051.1.
DR RefSeq; XP_005269109.1; XM_005269052.1.
DR UniGene; Hs.157659; -.
DR PDB; 2HEI; X-ray; 1.55 A; A/B=15-191.
DR PDBsum; 2HEI; -.
DR ProteinModelPortal; P61020; -.
DR SMR; P61020; 17-183.
DR IntAct; P61020; 7.
DR MINT; MINT-3022222; -.
DR STRING; 9606.ENSP00000353444; -.
DR PhosphoSite; P61020; -.
DR DMDM; 46577637; -.
DR PaxDb; P61020; -.
DR PRIDE; P61020; -.
DR DNASU; 5869; -.
DR Ensembl; ENST00000360299; ENSP00000353444; ENSG00000111540.
DR Ensembl; ENST00000448789; ENSP00000391319; ENSG00000111540.
DR Ensembl; ENST00000553116; ENSP00000450168; ENSG00000111540.
DR GeneID; 5869; -.
DR KEGG; hsa:5869; -.
DR UCSC; uc010spz.2; human.
DR CTD; 5869; -.
DR GeneCards; GC12P056368; -.
DR HGNC; HGNC:9784; RAB5B.
DR HPA; CAB010224; -.
DR MIM; 179514; gene.
DR neXtProt; NX_P61020; -.
DR PharmGKB; PA34144; -.
DR eggNOG; COG1100; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P61020; -.
DR KO; K07888; -.
DR OMA; PKNDGAN; -.
DR OrthoDB; EOG77DJ7M; -.
DR PhylomeDB; P61020; -.
DR ChiTaRS; RAB5B; human.
DR EvolutionaryTrace; P61020; -.
DR GeneWiki; RAB5B; -.
DR GenomeRNAi; 5869; -.
DR NextBio; 22794; -.
DR PRO; PR:P61020; -.
DR ArrayExpress; P61020; -.
DR Bgee; P61020; -.
DR CleanEx; HS_RAB5B; -.
DR Genevestigator; P61020; -.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030100; P:regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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; Alternative splicing; Cell membrane;
KW Complete proteome; Endosome; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Ras-related protein Rab-5B.
FT /FTId=PRO_0000121107.
FT NP_BIND 27 35 GTP.
FT NP_BIND 75 79 GTP (By similarity).
FT NP_BIND 133 136 GTP.
FT NP_BIND 163 165 GTP.
FT MOTIF 49 57 Effector region (Potential).
FT MOD_RES 2 2 N-acetylthreonine.
FT LIPID 212 212 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 213 213 S-geranylgeranyl cysteine (By
FT similarity).
FT VAR_SEQ 106 146 Missing (in isoform 2).
FT /FTId=VSP_045301.
FT MUTAGEN 34 34 S->N: Constitutively inactivated.
FT Strongly reduces interaction with RIN2.
FT MUTAGEN 79 79 Q->L: Constitutively active.
FT STRAND 19 26
FT HELIX 33 42
FT STRAND 54 56
FT STRAND 58 62
FT STRAND 69 74
FT HELIX 83 85
FT HELIX 86 90
FT STRAND 95 101
FT HELIX 105 121
FT STRAND 127 133
FT HELIX 135 140
FT HELIX 145 154
FT STRAND 158 161
FT TURN 164 166
FT HELIX 170 180
SQ SEQUENCE 215 AA; 23707 MW; D47AD834BCF8B591 CRC64;
MTSRSTARPN GQPQASKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEYQE STIGAAFLTQ
SVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNQETFAR AKTWVKELQR
QASPSIVIAL AGNKADLANK RMVEYEEAQA YADDNSLLFM ETSAKTAMNV NDLFLAIAKK
LPKSEPQNLG GAAGRSRGVD LHEQSQQNKS QCCSN
//
ID RAB5B_HUMAN Reviewed; 215 AA.
AC P61020; A8K982; B4DKD7; P35239; P35277; Q6PIK9; Q86TH0; Q8IXL2;
read moreDT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Ras-related protein Rab-5B;
GN Name=RAB5B;
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] (ISOFORM 1).
RX PubMed=1541686; DOI=10.1172/JCI115683;
RA Wilson D.B., Wilson M.P.;
RT "Identification and subcellular localization of human rab5b, a new
RT member of the ras-related superfamily of GTPases.";
RL J. Clin. Invest. 89:996-1005(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, PNS, and Skin;
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 [8]
RP INTERACTION WITH EEA1.
RX PubMed=10491193; DOI=10.1046/j.1432-1327.1999.00743.x;
RA Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.;
RT "Direct interaction of EEA1 with Rab5b.";
RL Eur. J. Biochem. 265:361-366(1999).
RN [9]
RP INTERACTION WITH RIN2 AND RIN3, AND MUTAGENESIS OF SER-34 AND GLN-79.
RX PubMed=11733506; DOI=10.1074/jbc.M106276200;
RA Saito K., Murai J., Kajiho H., Kontani K., Kurosu H., Katada T.;
RT "A novel binding protein composed of homophilic tetramer exhibits
RT unique properties for the small GTPase Rab5.";
RL J. Biol. Chem. 277:3412-3418(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 15-191 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB5B in complex with GDP.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Protein transport. Probably involved in vesicular
CC traffic (By similarity).
CC -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
CC factors (GEFs) which promote the exchange of bound GDP for free
CC GTP.
CC -!- SUBUNIT: Binds EEA1. Interacts with RIN2 and RIN3, which probably
CC regulate its pathway, possibly by acting as GEFs.
CC -!- INTERACTION:
CC Q15075:EEA1; NbExp=3; IntAct=EBI-399401, EBI-298113;
CC Q5S007:LRRK2; NbExp=4; IntAct=EBI-399401, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side. Early endosome membrane; Lipid-anchor. Melanosome.
CC Note=Enriched in stage I melanosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61020-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61020-2; Sequence=VSP_045301;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH40143.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; X54871; CAA38653.1; -; mRNA.
DR EMBL; AF498937; AAM21085.1; -; mRNA.
DR EMBL; AK292597; BAF85286.1; -; mRNA.
DR EMBL; AK296517; BAG59149.1; -; mRNA.
DR EMBL; BX537408; CAD97650.1; -; mRNA.
DR EMBL; AC034102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96862.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96864.1; -; Genomic_DNA.
DR EMBL; BC032740; AAH32740.1; -; mRNA.
DR EMBL; BC040143; AAH40143.1; ALT_INIT; mRNA.
DR EMBL; BC050558; AAH50558.2; -; mRNA.
DR EMBL; BC056422; AAH56422.2; -; mRNA.
DR EMBL; BC065298; AAH65298.2; -; mRNA.
DR PIR; A43925; A43925.
DR RefSeq; NP_001238965.1; NM_001252036.1.
DR RefSeq; NP_001238966.1; NM_001252037.1.
DR RefSeq; NP_002859.1; NM_002868.3.
DR RefSeq; XP_005269108.1; XM_005269051.1.
DR RefSeq; XP_005269109.1; XM_005269052.1.
DR UniGene; Hs.157659; -.
DR PDB; 2HEI; X-ray; 1.55 A; A/B=15-191.
DR PDBsum; 2HEI; -.
DR ProteinModelPortal; P61020; -.
DR SMR; P61020; 17-183.
DR IntAct; P61020; 7.
DR MINT; MINT-3022222; -.
DR STRING; 9606.ENSP00000353444; -.
DR PhosphoSite; P61020; -.
DR DMDM; 46577637; -.
DR PaxDb; P61020; -.
DR PRIDE; P61020; -.
DR DNASU; 5869; -.
DR Ensembl; ENST00000360299; ENSP00000353444; ENSG00000111540.
DR Ensembl; ENST00000448789; ENSP00000391319; ENSG00000111540.
DR Ensembl; ENST00000553116; ENSP00000450168; ENSG00000111540.
DR GeneID; 5869; -.
DR KEGG; hsa:5869; -.
DR UCSC; uc010spz.2; human.
DR CTD; 5869; -.
DR GeneCards; GC12P056368; -.
DR HGNC; HGNC:9784; RAB5B.
DR HPA; CAB010224; -.
DR MIM; 179514; gene.
DR neXtProt; NX_P61020; -.
DR PharmGKB; PA34144; -.
DR eggNOG; COG1100; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P61020; -.
DR KO; K07888; -.
DR OMA; PKNDGAN; -.
DR OrthoDB; EOG77DJ7M; -.
DR PhylomeDB; P61020; -.
DR ChiTaRS; RAB5B; human.
DR EvolutionaryTrace; P61020; -.
DR GeneWiki; RAB5B; -.
DR GenomeRNAi; 5869; -.
DR NextBio; 22794; -.
DR PRO; PR:P61020; -.
DR ArrayExpress; P61020; -.
DR Bgee; P61020; -.
DR CleanEx; HS_RAB5B; -.
DR Genevestigator; P61020; -.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030100; P:regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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; Alternative splicing; Cell membrane;
KW Complete proteome; Endosome; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Ras-related protein Rab-5B.
FT /FTId=PRO_0000121107.
FT NP_BIND 27 35 GTP.
FT NP_BIND 75 79 GTP (By similarity).
FT NP_BIND 133 136 GTP.
FT NP_BIND 163 165 GTP.
FT MOTIF 49 57 Effector region (Potential).
FT MOD_RES 2 2 N-acetylthreonine.
FT LIPID 212 212 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 213 213 S-geranylgeranyl cysteine (By
FT similarity).
FT VAR_SEQ 106 146 Missing (in isoform 2).
FT /FTId=VSP_045301.
FT MUTAGEN 34 34 S->N: Constitutively inactivated.
FT Strongly reduces interaction with RIN2.
FT MUTAGEN 79 79 Q->L: Constitutively active.
FT STRAND 19 26
FT HELIX 33 42
FT STRAND 54 56
FT STRAND 58 62
FT STRAND 69 74
FT HELIX 83 85
FT HELIX 86 90
FT STRAND 95 101
FT HELIX 105 121
FT STRAND 127 133
FT HELIX 135 140
FT HELIX 145 154
FT STRAND 158 161
FT TURN 164 166
FT HELIX 170 180
SQ SEQUENCE 215 AA; 23707 MW; D47AD834BCF8B591 CRC64;
MTSRSTARPN GQPQASKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEYQE STIGAAFLTQ
SVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNQETFAR AKTWVKELQR
QASPSIVIAL AGNKADLANK RMVEYEEAQA YADDNSLLFM ETSAKTAMNV NDLFLAIAKK
LPKSEPQNLG GAAGRSRGVD LHEQSQQNKS QCCSN
//
MIM
179514
*RECORD*
*FIELD* NO
179514
*FIELD* TI
*179514 RAS-ASSOCIATED PROTEIN RAB5B; RAB5B
*FIELD* TX
A number of processes in eukaryotic cells are believed to be regulated
read moreby small, monomeric GTPases belonging to the RAS superfamily. A subset
of these GTPases (the yeast YPTI/SEC4 gene products and their mammalian
counterparts, the RAB proteins) plays a central role in membrane
trafficking. Each of the several proteins of this subfamily that have
been identified is thought to regulate vesicular trafficking at a
specific subcellular compartment. The subcellular location of several
RAB proteins has been determined by immunohistochemical methods. For
example, RAB2 (179509) is found in the intermediate recycling pathway
between the endoplasmic reticulum and the Golgi complex. RAB6 (179513)
is distributed in the medial and trans Golgi. RAB4 (179511) and RAB5A
(179512) are associated with the plasma membrane and early endosomes.
Wilson and Wilson (1992) cloned cDNA of a novel member of the RAB family
by screening a human umbilical vein endothelial cell cDNA library with
oligonucleotide probes corresponding to a region conserved in all RAB
proteins. The newly identified RAB protein was 81% identical to human
RAB5, the canine counterpart of which had been localized to the plasma
membrane and early endosomes. In light of this homology, Wilson and
Wilson (1992) called the new member of the GTPase superfamily RAB5B. It
is presumably involved in vesicular trafficking at the plasma membrane.
By fluorescence in situ hybridization, Korenberg et al. (1995) mapped
the RAB5B gene to 12q13.
*FIELD* RF
1. Korenberg, J. R.; Chen, X.-N.; Adams, M. D.; Venter, J. C.: Toward
a cDNA map of the human genome. Genomics 29: 364-370, 1995.
2. Wilson, D. B.; Wilson, M. P.: Identification and subcellular localization
of human rab5b, a new member of the ras-related superfamily of GTPases. J.
Clin. Invest. 89: 996-1005, 1992.
*FIELD* CN
Rebekah S. Rasooly - updated: 03/09/1999
*FIELD* CD
Victor A. McKusick: 5/4/1992
*FIELD* ED
mgross: 03/09/1999
carol: 5/4/1992
*RECORD*
*FIELD* NO
179514
*FIELD* TI
*179514 RAS-ASSOCIATED PROTEIN RAB5B; RAB5B
*FIELD* TX
A number of processes in eukaryotic cells are believed to be regulated
read moreby small, monomeric GTPases belonging to the RAS superfamily. A subset
of these GTPases (the yeast YPTI/SEC4 gene products and their mammalian
counterparts, the RAB proteins) plays a central role in membrane
trafficking. Each of the several proteins of this subfamily that have
been identified is thought to regulate vesicular trafficking at a
specific subcellular compartment. The subcellular location of several
RAB proteins has been determined by immunohistochemical methods. For
example, RAB2 (179509) is found in the intermediate recycling pathway
between the endoplasmic reticulum and the Golgi complex. RAB6 (179513)
is distributed in the medial and trans Golgi. RAB4 (179511) and RAB5A
(179512) are associated with the plasma membrane and early endosomes.
Wilson and Wilson (1992) cloned cDNA of a novel member of the RAB family
by screening a human umbilical vein endothelial cell cDNA library with
oligonucleotide probes corresponding to a region conserved in all RAB
proteins. The newly identified RAB protein was 81% identical to human
RAB5, the canine counterpart of which had been localized to the plasma
membrane and early endosomes. In light of this homology, Wilson and
Wilson (1992) called the new member of the GTPase superfamily RAB5B. It
is presumably involved in vesicular trafficking at the plasma membrane.
By fluorescence in situ hybridization, Korenberg et al. (1995) mapped
the RAB5B gene to 12q13.
*FIELD* RF
1. Korenberg, J. R.; Chen, X.-N.; Adams, M. D.; Venter, J. C.: Toward
a cDNA map of the human genome. Genomics 29: 364-370, 1995.
2. Wilson, D. B.; Wilson, M. P.: Identification and subcellular localization
of human rab5b, a new member of the ras-related superfamily of GTPases. J.
Clin. Invest. 89: 996-1005, 1992.
*FIELD* CN
Rebekah S. Rasooly - updated: 03/09/1999
*FIELD* CD
Victor A. McKusick: 5/4/1992
*FIELD* ED
mgross: 03/09/1999
carol: 5/4/1992