RBCC

Full text data of RAB8B

RAB8B [Confidence: high (present in two of the MS resources)]
Ras-related protein Rab-8B; Flags: Precursor

hRBCD IPI00024282
IPI00024282 Ras-related protein Rab-8B Ras-related protein Rab-8B membrane 1 1 n/a n/a n/a n/a n/a n/a 12 n/a 2 2 n/a 3 2 n/a 3 2 3 n/a cytoplasmic and membrane associated n/a expected molecular weight found in band ~ 17 kDa

UniProt Q92930
ID RAB8B_HUMAN Reviewed; 207 AA.
AC Q92930; Q5JPC4; Q9P293;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-APR-2001, sequence version 2.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Ras-related protein Rab-8B;
DE Flags: Precursor;
GN Name=RAB8B;
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].
RC TISSUE=Fetal brain;
RA Seki N., Saito T.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph node;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-119.
RC TISSUE=Melanoma;
RX PubMed=9030196; DOI=10.1016/S0167-4889(96)00169-3;
RA Chen D., Guo J., Gahl W.A.;
RT "RAB GTPases expressed in human melanoma cells.";
RL Biochim. Biophys. Acta 1355:1-6(1997).
RN [7]
RP INTERACTION WITH RAB3IP.
RC TISSUE=Brain;
RX PubMed=12221131; DOI=10.1091/mbc.E02-03-0143;
RA Hattula K., Furuhjelm J., Arffman A., Peranen J.;
RT "A Rab8-specific GDP/GTP exchange factor is involved in actin
RT remodeling and polarized membrane transport.";
RL Mol. Biol. Cell 13:3268-3280(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
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 [10]
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).
CC -!- FUNCTION: The small GTPases Rab are key regulators of
CC intracellular membrane trafficking, from the formation of
CC transport vesicles to their fusion with membranes. Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different sets of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab may be involved in polarized
CC vesicular trafficking and neurotransmitter release. May
CC participate in cell junction dynamics in Sertoli cells (By
CC similarity).
CC -!- SUBUNIT: Associated with actin, delta-catenin and alpha and beta
CC tubulins (By similarity). Interacts with OTOF (By similarity).
CC Interacts with PEX5R (By similarity). Interacts with RAB3IP.
CC Interacts with VIM (By similarity). Interacts with CDH1 (By
CC similarity). Interacts with MICALL2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential). Cytoplasmic vesicle, phagosome. Cytoplasmic
CC vesicle, phagosome membrane; Lipid-anchor; Cytoplasmic side.
CC Note=Recruited to phagosomes containing S.aureus or
CC M.tuberculosis.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; AB038995; BAA92249.1; -; mRNA.
DR EMBL; AK001111; BAG50856.1; -; mRNA.
DR EMBL; AL833365; CAI46143.1; -; mRNA.
DR EMBL; AC016207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020654; AAH20654.1; -; mRNA.
DR EMBL; U66624; AAC51199.1; -; mRNA.
DR RefSeq; NP_057614.1; NM_016530.2.
DR UniGene; Hs.389733; -.
DR ProteinModelPortal; Q92930; -.
DR SMR; Q92930; 6-176.
DR IntAct; Q92930; 2.
DR MINT; MINT-3049578; -.
DR STRING; 9606.ENSP00000312734; -.
DR PhosphoSite; Q92930; -.
DR DMDM; 13638434; -.
DR PaxDb; Q92930; -.
DR PeptideAtlas; Q92930; -.
DR PRIDE; Q92930; -.
DR DNASU; 51762; -.
DR Ensembl; ENST00000321437; ENSP00000312734; ENSG00000166128.
DR GeneID; 51762; -.
DR KEGG; hsa:51762; -.
DR UCSC; uc002alz.3; human.
DR CTD; 51762; -.
DR GeneCards; GC15P063481; -.
DR HGNC; HGNC:30273; RAB8B.
DR MIM; 613532; gene.
DR neXtProt; NX_Q92930; -.
DR PharmGKB; PA134944620; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q92930; -.
DR KO; K07902; -.
DR OMA; FLITINK; -.
DR OrthoDB; EOG7VB2H4; -.
DR PhylomeDB; Q92930; -.
DR ChiTaRS; RAB8B; human.
DR GeneWiki; RAB8B; -.
DR GenomeRNAi; 51762; -.
DR NextBio; 55874; -.
DR PRO; PR:Q92930; -.
DR ArrayExpress; Q92930; -.
DR Bgee; Q92930; -.
DR CleanEx; HS_RAB8B; -.
DR Genevestigator; Q92930; -.
DR GO; GO:0051286; C:cell tip; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0034332; P:adherens junction organization; ISS:UniProtKB.
DR GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
DR GO; GO:0051461; P:positive regulation of corticotropin secretion; IEA:Ensembl.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IDA:UniProtKB.
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 Cell membrane; Complete proteome; Cytoplasmic vesicle; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 204 Ras-related protein Rab-8B.
FT /FTId=PRO_0000121134.
FT PROPEP 205 207 Removed in mature form (Potential).
FT /FTId=PRO_0000370800.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 121 124 GTP (By similarity).
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 180 180 Phosphoserine (By similarity).
FT MOD_RES 204 204 Cysteine methyl ester (Potential).
FT LIPID 204 204 S-geranylgeranyl cysteine (By
FT similarity).
SQ SEQUENCE 207 AA; 23584 MW; 5960993C0F87F944 CRC64;
MAKTYDYLFK LLLIGDSGVG KTCLLFRFSE DAFNTTFIST IGIDFKIRTI ELDGKKIKLQ
IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIK NWIRNIEEHA SSDVERMILG
NKCDMNDKRQ VSKERGEKLA IDYGIKFLET SAKSSANVEE AFFTLARDIM TKLNRKMNDS
NSAGAGGPVK ITENRSKKTS FFRCSLL
//

MIM 613532
*RECORD*
*FIELD* NO
613532
*FIELD* TI
*613532 RAS-ASSOCIATED PROTEIN RAB8B; RAB8B
*FIELD* TX

DESCRIPTION

RAB proteins, like RAB8B, are low molecular mass monomeric GTPases that
read morelocalize on the cytoplasmic surfaces of distinct membrane-bound
organelles. RAB proteins function in intracellular vesicle transport by
aiding in the docking and/or fusion of vesicles with their target
membranes (summary by Chen et al., 1997).

CLONING

Using degenerative primers to amplify RAB cDNAs from a human pigmented
melanoma cell line, Chen et al. (1997) obtained a partial RAB8B clone
encoding the highly conserved region encompassing GTP-binding domains II
and III. Within this region, RAB8B shares complete amino acid identity
with rat Rab8b and 96% identity with human RAB8 (RAB8A; 165040).

By RT-PCR of rat tissues, Lau and Mruk (2003) found highest Rab8b
expression in brain and testis, with lower expression in heart, kidney,
and spleen. Rab8b was also expressed in Sertoli and germ cells, and
expression increased in these cells during maturation. Expression of
Rab8b increased in testis during initiation of meiosis, when secondary
spermatocytes first appear. Immunohistochemical analysis of adult rat
testis detected Rab8b in the basal compartment in all stages of the
spermatogenic cycle. In cultured Sertoli cells, Rab8b associated with
membrane junctions. Western blot analysis detected rat Rab8b at an
apparent molecular mass of 24 kD.

Heidrych et al. (2008) noted that mouse Rab8b and Rab8a share about 80%
amino acid identity, with highest conservation in their N-terminal
domains. RT-PCR detected Rab8b expression in both immature and mature
mouse cochlear hair cells. Rab8b was also expressed in rodent brain and
in colonic epithelial cells.

GENE FUNCTION

Throughout spermatogenesis, germ cells migrate from the basal to the
adluminal compartment while remaining attached to Sertoli cells via
actin (see 102560)-based adherens and intermediate filament-based
anchoring junctions. Lau and Mruk (2003) found that when rat Sertoli
cells were cultured at high density, or when germ cells were cocultured
with Sertoli cells, expression of Rab8b increased during cell-cell
junction assembly. In Sertoli cells, expression declined to basal level
after junctions were assembled. Germ cell-conditioned medium stimulated
Rab8b expression in Sertoli cells in a dose-dependent and
androgen-independent manner. Chemical crosslinking and
coimmunoprecipitation analysis revealed that Rab8b associated with
actin, vimentin (VIM; 193060), alpha-tubulin (see 602529), beta-tubulin
(TUBB; 191130), E-cadherin (CDH1; 192090), and gamma-catenin (JUP;
173325), but not with several other cytoskeletal components, including
gamma-tubulin (see 191135). Lau and Mruk (2003) concluded that RAB8B may
participate in cell junction dynamics, but that it is unlikely to be
required for junction maintenance.

Using immunofluorescence microscopy and reciprocal coimmunoprecipitation
analysis, Heidrych et al. (2008) showed that Rab8b colocalized and
interacted directly with otoferlin (OTOF; 603681) in mouse cochlear
inner hair cells and in transfected cell lines. They proposed that
otoferlin-Rab8b complexes may be involved in recycling endosomes and in
basolateral vesicle transport.

MAPPING

Hartz (2010) mapped the RAB8B gene to chromosome 15q22.2 based on an
alignment of the RAB8B sequence (GenBank GENBANK AB038995) with the
genomic sequence (GRCh37).

*FIELD* RF
1. Chen, D.; Guo, J.; Gahl, W. A.: RAB GTPases expressed in human
melanoma cells. Biochim. Biophys. Acta 1355: 1-6, 1997.

2. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/9/2010.

3. Heidrych, P.; Zimmermann, U.; Bress, A.; Pusch, C. M.; Ruth, P.;
Pfister, M.; Knipper, M.; Blin, N.: Rab8b GTPase, a protein transport
regulator, is an interacting partner of otoferlin, defective in a
human autosomal recessive deafness form. Hum. Molec. Genet. 17:
3814-3821, 2008.

4. Lau, A. S. N.; Mruk, D. D.: Rab8B GTPase and junction dynamics
in the testis. Endocrinology 144: 1549-1563, 2003.

*FIELD* CD
Patricia A. Hartz: 9/13/2010

*FIELD* ED
mgross: 09/13/2010

RBCC Red Blood Cell Collection

Full text data of RAB8B