RAB9B_HUMAN
ID RAB9B_HUMAN Reviewed; 201 AA.
AC Q9NP90; B2R8M0; Q52LX2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Ras-related protein Rab-9B;
DE AltName: Full=Rab-9-like protein;
DE Short=Rab-9L;
GN Name=RAB9B; Synonyms=RAB9L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11043518; DOI=10.1007/s100380070025;
RA Seki N., Azuma T., Yoshikawa T., Masuho Y., Muramatsu M., Saito T.;
RT "cDNA cloning of a new member of the Ras superfamily, RAB9-like, on the
RT human chromosome Xq22.1-q22.3 region.";
RL J. Hum. Genet. 45:318-322(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH HPS4 AND BLOC-3 COMPLEX, AND ABSENCE OF INTERACTION WITH
RP HPS1.
RX PubMed=20048159; DOI=10.1074/jbc.m109.069088;
RA Kloer D.P., Rojas R., Ivan V., Moriyama K., van Vlijmen T., Murthy N.,
RA Ghirlando R., van der Sluijs P., Hurley J.H., Bonifacino J.S.;
RT "Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-
RT 3) and its interaction with Rab9.";
RL J. Biol. Chem. 285:7794-7804(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [7]
RP INTERACTION WITH SGSM1.
RX PubMed=22637480; DOI=10.1074/jbc.m112.362558;
RA Nottingham R.M., Pusapati G.V., Ganley I.G., Barr F.A., Lambright D.G.,
RA Pfeffer S.R.;
RT "RUTBC2 protein, a Rab9A effector and GTPase-activating protein for
RT Rab36.";
RL J. Biol. Chem. 287:22740-22748(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-180 IN COMPLEX WITH GTP ANALOG.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB9B in complex with a GTP analogue.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in the transport of proteins between the endosomes
CC and the trans Golgi network. {ECO:0000250|UniProtKB:P24408}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with SGSM1; the GDP-bound form has
CC much lower affinity for SGSM1 (PubMed:22637480). The GTP-bound form but
CC not the GDP-bound form interacts with HPS4 and the BLOC-3 complex
CC (heterodimer of HPS1 and HPS4) but does not interact with HPS1 alone
CC (PubMed:20048159). {ECO:0000269|PubMed:20048159,
CC ECO:0000269|PubMed:22637480}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or
CC M.tuberculosis.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11043518}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB036693; BAA89542.1; -; mRNA.
DR EMBL; AK313425; BAG36217.1; -; mRNA.
DR EMBL; AL139228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093756; AAH93756.1; -; mRNA.
DR EMBL; BC093758; AAH93758.1; -; mRNA.
DR CCDS; CCDS14515.1; -.
DR RefSeq; NP_057454.1; NM_016370.2.
DR PDB; 2OCB; X-ray; 2.20 A; A=2-180.
DR PDBsum; 2OCB; -.
DR AlphaFoldDB; Q9NP90; -.
DR SMR; Q9NP90; -.
DR BioGRID; 119382; 24.
DR IntAct; Q9NP90; 12.
DR STRING; 9606.ENSP00000243298; -.
DR iPTMnet; Q9NP90; -.
DR PhosphoSitePlus; Q9NP90; -.
DR BioMuta; RAB9B; -.
DR DMDM; 13124471; -.
DR EPD; Q9NP90; -.
DR jPOST; Q9NP90; -.
DR MassIVE; Q9NP90; -.
DR MaxQB; Q9NP90; -.
DR PaxDb; Q9NP90; -.
DR PeptideAtlas; Q9NP90; -.
DR PRIDE; Q9NP90; -.
DR ProteomicsDB; 81933; -.
DR Antibodypedia; 29164; 86 antibodies from 27 providers.
DR DNASU; 51209; -.
DR Ensembl; ENST00000243298.3; ENSP00000243298.2; ENSG00000123570.4.
DR GeneID; 51209; -.
DR KEGG; hsa:51209; -.
DR MANE-Select; ENST00000243298.3; ENSP00000243298.2; NM_016370.4; NP_057454.1.
DR UCSC; uc004ell.3; human.
DR CTD; 51209; -.
DR DisGeNET; 51209; -.
DR GeneCards; RAB9B; -.
DR HGNC; HGNC:14090; RAB9B.
DR HPA; ENSG00000123570; Tissue enhanced (heart).
DR MalaCards; RAB9B; -.
DR MIM; 300285; gene.
DR neXtProt; NX_Q9NP90; -.
DR OpenTargets; ENSG00000123570; -.
DR PharmGKB; PA34153; -.
DR VEuPathDB; HostDB:ENSG00000123570; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000160481; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q9NP90; -.
DR OMA; NRKAPRS; -.
DR PhylomeDB; Q9NP90; -.
DR TreeFam; TF326442; -.
DR PathwayCommons; Q9NP90; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-HSA-9706019; RHOBTB3 ATPase cycle.
DR SignaLink; Q9NP90; -.
DR BioGRID-ORCS; 51209; 8 hits in 694 CRISPR screens.
DR ChiTaRS; RAB9B; human.
DR EvolutionaryTrace; Q9NP90; -.
DR GenomeRNAi; 51209; -.
DR Pharos; Q9NP90; Tbio.
DR PRO; PR:Q9NP90; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NP90; protein.
DR Bgee; ENSG00000123570; Expressed in left ventricle myocardium and 150 other tissues.
DR Genevisible; Q9NP90; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
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; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR CDD; cd04116; Rab9; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041824; Rab9.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasmic vesicle; GTP-binding; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Ras-related protein Rab-9B"
FT /id="PRO_0000121142"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 14..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:2OCB"
FT BINDING 33..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:2OCB"
FT BINDING 38..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:2OCB"
FT BINDING 65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:2OCB"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:2OCB"
FT BINDING 155..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:2OCB"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHH2"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:2OCB"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:2OCB"
FT STRAND 41..53
FT /evidence="ECO:0007829|PDB:2OCB"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:2OCB"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2OCB"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:2OCB"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2OCB"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:2OCB"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:2OCB"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2OCB"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2OCB"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2OCB"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:2OCB"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2OCB"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:2OCB"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:2OCB"
SQ SEQUENCE 201 AA; 22719 MW; B35EDA8E8358C49C CRC64;
MSGKSLLLKV ILLGDGGVGK SSLMNRYVTN KFDSQAFHTI GVEFLNRDLE VDGRFVTLQI
WDTAGQERFK SLRTPFYRGA DCCLLTFSVD DRQSFENLGN WQKEFIYYAD VKDPEHFPFV
VLGNKVDKED RQVTTEEAQT WCMENGDYPY LETSAKDDTN VTVAFEEAVR QVLAVEEQLE
HCMLGHTIDL NSGSKAGSSC C
