Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0010406
UniProt IDP62491
Primary gene name(s)RAB11A
Synonym gene name(s)RAB11
Protein nameRas-related protein Rab-11A
Protein functionThe 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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites, AMIS, apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF, Transferrin recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT, receptor of Fc region of monomeric Ig G to basolateral membranes. May also play a role in melanosome transport and release from melanocytes. {ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:15689490, ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:19542231, ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21282656}.
Subcellular locationCell membrane {ECO:0000269|PubMed:15304524};
Lipid-anchor {ECO:0000305|PubMed:24023390}. Recycling endosome membrane {ECO:0000269|PubMed:11994279, ECO:0000269|PubMed:15181150};
Lipid-anchor {ECO:0000305|PubMed:24023390}. Cleavage furrow {ECO:0000269|PubMed:15601896}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Note=Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment, ERC to the plasma membrane, PubMed:11994279. Localizes to the cleavage furrow, PubMed:15601896. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites, AMIS during the generation of apical surface and lumenogenesis, PubMed:20890297. Recruited to phagosomes containing S.aureus or M.tuberculosis, PubMed:21255211. {ECO:0000269|PubMed:11994279, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21255211}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P62491
Gene Ontology
(Biological Process)
Complete annatation
astral microtubule organization [GO:0030953];
cytokinesis [GO:0000910];
establishment of protein localization to membrane [GO:0090150];
establishment of protein localization to organelle [GO:0072594];
establishment of vesicle localization [GO:0051650];
exosomal secretion [GO:1990182];
melanosome transport [GO:0032402];
mitotic metaphase plate congression [GO:0007080];
mitotic spindle assembly [GO:0090307];
multivesicular body assembly [GO:0036258];
neuron projection development [GO:0031175];
plasma membrane to endosome transport [GO:0048227];
positive regulation of axon extension [GO:0045773];
positive regulation of epithelial cell migration [GO:0010634];
positive regulation of G2/M transition of mitotic cell cycle [GO:0010971];
protein localization to plasma membrane [GO:0072659];
protein transport [GO:0015031];
regulation of long-term neuronal synaptic plasticity [GO:0048169];
regulation of multivesicular body size [GO:0010796];
regulation of protein transport [GO:0051223];
regulation of vesicle-mediated transport [GO:0060627];
renal water homeostasis [GO:0003091];
small GTPase mediated signal transduction [GO:0007264];
vesicle-mediated transport [GO:0016192]
Gene Ontology
(Molecular Function)
Complete annatation
GTPase activity [GO:0003924];
GTP binding [GO:0005525];
microtubule binding [GO:0008017];
myosin V binding [GO:0031489];
syntaxin binding [GO:0019905]
Gene Ontology
(Cellular Component)
Complete annatation
axon [GO:0030424];
cleavage furrow [GO:0032154];
cytoplasmic vesicle [GO:0031410];
cytoplasmic vesicle membrane [GO:0030659];
cytosol [GO:0005829];
extracellular exosome [GO:0070062];
Golgi apparatus [GO:0005794];
mitochondrion [GO:0005739];
multivesicular body [GO:0005771];
perinuclear region of cytoplasm [GO:0048471];
phagocytic vesicle [GO:0045335];
plasma membrane [GO:0005886];
protein complex [GO:0043234];
recycling endosome [GO:0055037];
recycling endosome membrane [GO:0055038];
spindle pole [GO:0000922];
trans-Golgi network [GO:0005802];
transport vesicle [GO:0030133];
vesicle [GO:0031982]
Protein-protein interaction114299
Phylogenetic treeP62491
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
Brass et al., Science, 2008
Smith et al., J. Immunol, 2010
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model

DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD30.2431691263386320.4573873177125320.57818851401185
AZA vs. DISU-0.08676502254982690.7313634634176020.974560663114398
AZA vs. IL70.1239982763432720.5187040167489710.999311006273513
AZA vs. SAHA0.1607147102314940.5114905383877410.828075220240232
DISU vs. CD3-0.3416197278424850.3459416993232020.479559056060139
DISU vs. IL70.2014609107394690.4238248622475020.780389555623192
DISU vs. SAHA0.2484458038688360.3949827156990260.757687086398203
DMSO vs. AZA-0.1228097609727410.4633479551118831
DMSO vs. CD3-0.3758171949186150.2399584852537830.344841608351449
DMSO vs. DISU-0.03752771292127780.87765022894830.987443803738299
DMSO vs. IL70.2538040401518030.1581317054588170.662800541158701
DMSO vs. SAHA0.2763271808212160.2429691328814680.591213464261533
HIV vs. Mock in Activation-0.140416613365540.8213659959785020.999983755607037
HIV vs. Mock in Latency0.02359278999930690.8865556283784640.999834320637052
IL7 vs. CD3-0.1113027562127310.7286299474857870.816978293420611
SAHA vs. CD3-0.1073121996961990.7624388798575480.829779296559056
SAHA vs. IL70.03354513707150160.8910808831347430.957046899349706
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change unknown
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
unknown unknown unknown unknown unknown unknown
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) unknown
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK 0.0682079 0.696646
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
unknown unknown

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
unknown unknown unknown unknown unknown
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
unknown unknown unknown unknown

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB01864 5&,39;-Guanosine-Diphosphate-Monothiophosphate experimental unknown unknown
DB04315 Guanosine-5&,39;-Diphosphate experimental unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1OIV X-ray 1.9Å A/B=1-173.
1OIW X-ray 2.0Å A=1-173.
1OIX X-ray 1.7Å A=1-173.
1YZK X-ray 2.0Å A=8-175.
2D7C X-ray 1.7Å A/B=7-173.
2GZD X-ray 2.4Å A/B=2-173.
2GZH X-ray 2.4Å A=2-173.
2HV8 X-ray 1.8Å A/B/C=6-175.
4C4P X-ray 2.0Å A=1-173.
4D0L X-ray 2.9Å B/D/F=1-216.
4D0M X-ray 6.0Å B/D/H/J/N/P/R/T/X/Z/d/h=1-216.
4LWZ X-ray 2.5Å A/C=1-177.
4LX0 X-ray 2.1Å A/C=1-177.
4UJ3 X-ray 3.0Å A/D/G/J/M/P/S/V=4-186.
4UJ4 X-ray 4.2Å A/D/G/J=4-186.
4UJ5 X-ray 2.6Å A/B=6-186.
5C46 X-ray 2.6Å F=1-216.
5C4G X-ray 3.2Å B=1-216.
5EUQ X-ray 3.2Å B=1-216.
5JCZ X-ray 2.0Å A/D/I=1-177.

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
Nef co-localizes with 15569681
reverse transcriptase interacts with 24920821
capsid regulated by 24830293
Pr55(Gag) co-localizes with 21789505
Nef inhibited by 20622010
Pr55(Gag) modulated by 18406652
HIV-1 virus replication enhanced by expression of human gene 22404213

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04144 Endocytosis - Homo sapiens (human)
hsa04961 Endocrine and other factor-regulated calcium reabsorption - Homo sapiens (human)
hsa04962 Vasopressin-regulated water reabsorption - Homo sapiens (human)
hsa04972 Pancreatic secretion - Homo sapiens (human)