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Protein

Ras-related protein Rab-8B

Gene

RAB8B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may be involved in polarized vesicular trafficking and neurotransmitter release. May participate in cell junction dynamics in Sertoli cells (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228GTPBy similarity
Nucleotide bindingi63 – 675GTPBy similarity
Nucleotide bindingi121 – 1244GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: GO_Central
  4. receptor binding Source: UniProtKB

GO - Biological processi

  1. adherens junction organization Source: UniProtKB
  2. antigen processing and presentation Source: UniProtKB
  3. cellular response to insulin stimulus Source: GO_Central
  4. Golgi vesicle fusion to target membrane Source: GO_Central
  5. GTP catabolic process Source: GO_Central
  6. positive regulation of cell projection organization Source: Ensembl
  7. positive regulation of corticotropin secretion Source: Ensembl
  8. protein import into peroxisome membrane Source: UniProtKB
  9. protein localization to plasma membrane Source: GO_Central
  10. protein secretion Source: GO_Central
  11. Rab protein signal transduction Source: GO_Central
  12. regulation of exocytosis Source: GO_Central
  13. synaptic vesicle exocytosis Source: GO_Central
  14. vesicle docking involved in exocytosis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-8B
Gene namesi
Name:RAB8B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:30273. RAB8B.

Subcellular locationi

Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Cytoplasmic vesiclephagosome 1 Publication. Cytoplasmic vesiclephagosome membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication
Note: Recruited to phagosomes containing S.aureus or M.tuberculosis.

GO - Cellular componenti

  1. cell tip Source: Ensembl
  2. endosome Source: GO_Central
  3. extracellular vesicular exosome Source: UniProtKB
  4. mitochondrion Source: Ensembl
  5. perinuclear region of cytoplasm Source: Ensembl
  6. peroxisomal membrane Source: UniProtKB
  7. phagocytic vesicle Source: UniProtKB
  8. phagocytic vesicle membrane Source: UniProtKB-SubCell
  9. plasma membrane Source: GO_Central
  10. secretory granule membrane Source: GO_Central
  11. synaptic vesicle Source: GO_Central
  12. trans-Golgi network transport vesicle Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134944620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Ras-related protein Rab-8BPRO_0000121134Add
BLAST
Propeptidei205 – 2073Removed in mature formSequence AnalysisPRO_0000370800

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801PhosphoserineBy similarity
Modified residuei204 – 2041Cysteine methyl esterSequence Analysis
Lipidationi204 – 2041S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ92930.
PaxDbiQ92930.
PeptideAtlasiQ92930.
PRIDEiQ92930.

PTM databases

PhosphoSiteiQ92930.

Expressioni

Gene expression databases

BgeeiQ92930.
CleanExiHS_RAB8B.
ExpressionAtlasiQ92930. baseline and differential.
GenevestigatoriQ92930.

Interactioni

Subunit structurei

Associated with actin, delta-catenin and alpha and beta tubulins (By similarity). Interacts with OTOF (By similarity). Interacts with PEX5R (By similarity). Interacts with RAB3IP. Interacts with VIM (By similarity). Interacts with CDH1 (By similarity). Interacts with MICALL2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi119719. 18 interactions.
IntActiQ92930. 2 interactions.
MINTiMINT-3049578.
STRINGi9606.ENSP00000312734.

Structurei

3D structure databases

ProteinModelPortaliQ92930.
SMRiQ92930. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 459Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ92930.
KOiK07902.
OMAiGNKSDWS.
OrthoDBiEOG7VB2H4.
PhylomeDBiQ92930.
TreeFamiTF314097.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTYDYLFK LLLIGDSGVG KTCLLFRFSE DAFNTTFIST IGIDFKIRTI
60 70 80 90 100
ELDGKKIKLQ IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIK
110 120 130 140 150
NWIRNIEEHA SSDVERMILG NKCDMNDKRQ VSKERGEKLA IDYGIKFLET
160 170 180 190 200
SAKSSANVEE AFFTLARDIM TKLNRKMNDS NSAGAGGPVK ITENRSKKTS

FFRCSLL
Length:207
Mass (Da):23,584
Last modified:April 27, 2001 - v2
Checksum:i5960993C0F87F944
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038995 mRNA. Translation: BAA92249.1.
AK001111 mRNA. Translation: BAG50856.1.
AL833365 mRNA. Translation: CAI46143.1.
AC016207 Genomic DNA. No translation available.
BC020654 mRNA. Translation: AAH20654.1.
U66624 mRNA. Translation: AAC51199.1.
CCDSiCCDS10183.1.
RefSeqiNP_057614.1. NM_016530.2.
UniGeneiHs.389733.

Genome annotation databases

EnsembliENST00000321437; ENSP00000312734; ENSG00000166128.
GeneIDi51762.
KEGGihsa:51762.
UCSCiuc002alz.3. human.

Polymorphism databases

DMDMi13638434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038995 mRNA. Translation: BAA92249.1.
AK001111 mRNA. Translation: BAG50856.1.
AL833365 mRNA. Translation: CAI46143.1.
AC016207 Genomic DNA. No translation available.
BC020654 mRNA. Translation: AAH20654.1.
U66624 mRNA. Translation: AAC51199.1.
CCDSiCCDS10183.1.
RefSeqiNP_057614.1. NM_016530.2.
UniGeneiHs.389733.

3D structure databases

ProteinModelPortaliQ92930.
SMRiQ92930. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119719. 18 interactions.
IntActiQ92930. 2 interactions.
MINTiMINT-3049578.
STRINGi9606.ENSP00000312734.

PTM databases

PhosphoSiteiQ92930.

Polymorphism databases

DMDMi13638434.

Proteomic databases

MaxQBiQ92930.
PaxDbiQ92930.
PeptideAtlasiQ92930.
PRIDEiQ92930.

Protocols and materials databases

DNASUi51762.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321437; ENSP00000312734; ENSG00000166128.
GeneIDi51762.
KEGGihsa:51762.
UCSCiuc002alz.3. human.

Organism-specific databases

CTDi51762.
GeneCardsiGC15P063481.
HGNCiHGNC:30273. RAB8B.
MIMi613532. gene.
neXtProtiNX_Q92930.
PharmGKBiPA134944620.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ92930.
KOiK07902.
OMAiGNKSDWS.
OrthoDBiEOG7VB2H4.
PhylomeDBiQ92930.
TreeFamiTF314097.

Miscellaneous databases

ChiTaRSiRAB8B. human.
GeneWikiiRAB8B.
GenomeRNAii51762.
NextBioi55874.
PROiQ92930.
SOURCEiSearch...

Gene expression databases

BgeeiQ92930.
CleanExiHS_RAB8B.
ExpressionAtlasiQ92930. baseline and differential.
GenevestigatoriQ92930.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Seki N., Saito T.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph node.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  6. "RAB GTPases expressed in human melanoma cells."
    Chen D., Guo J., Gahl W.A.
    Biochim. Biophys. Acta 1355:1-6(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-119.
    Tissue: Melanoma.
  7. "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
    Hattula K., Furuhjelm J., Arffman A., Peranen J.
    Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB3IP.
    Tissue: Brain.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
    Seto S., Tsujimura K., Koide Y.
    Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRAB8B_HUMAN
AccessioniPrimary (citable) accession number: Q92930
Secondary accession number(s): Q5JPC4, Q9P293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 27, 2001
Last modified: March 4, 2015
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.