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Protein

Ras-related protein Rab-11B

Gene

RAB11B

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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis.6 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 26GTP9
Nucleotide bindingi66 – 70GTP5
Nucleotide bindingi124 – 127GTP4
Nucleotide bindingi154 – 156GTP3

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • myosin V binding Source: UniProtKB

GO - Biological processi

  • cellular response to acidic pH Source: UniProtKB
  • constitutive secretory pathway Source: UniProtKB
  • establishment of protein localization to membrane Source: UniProtKB
  • insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • melanosome transport Source: UniProtKB
  • receptor recycling Source: UniProtKB
  • regulated exocytosis Source: UniProtKB
  • regulation of anion transport Source: UniProtKB
  • regulation of endocytic recycling Source: UniProtKB
  • regulation of protein localization to cell surface Source: UniProtKB
  • retrograde transport, endosome to plasma membrane Source: UniProtKB
  • small GTPase mediated signal transduction Source: InterPro
  • transferrin transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:G66-32577-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-11B
Alternative name(s):
GTP-binding protein YPT3
Gene namesi
Name:RAB11B
Synonyms:YPT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9761. RAB11B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Endosome, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25S → N: Dominant negative mutant locked in the inactive GDP-bound form; alters apical recycling. Does not interact with ZFYV2E and KIF5A. 2 Publications1
Mutagenesisi70Q → L: Constitutively active mutant locked in the active GTP-bound form; alters apical recycling. 1 Publication1

Organism-specific databases

DisGeNETi9230.
OpenTargetsiENSG00000185236.
PharmGKBiPA34102.

Polymorphism and mutation databases

BioMutaiRAB11B.
DMDMi38258938.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001211582 – 215Ras-related protein Rab-11BAdd BLAST214
PropeptideiPRO_0000370815216 – 218Removed in mature formSequence analysis3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycine1 Publication1
Modified residuei4CitrullineBy similarity1
Lipidationi214S-geranylgeranyl cysteine1 Publication1
Modified residuei215Cysteine methyl esterSequence analysis1
Lipidationi215S-geranylgeranyl cysteine1 Publication1

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Lipoprotein, Methylation, Prenylation

Proteomic databases

EPDiQ15907.
MaxQBiQ15907.
PaxDbiQ15907.
PeptideAtlasiQ15907.
PRIDEiQ15907.
TopDownProteomicsiQ15907-1. [Q15907-1]

PTM databases

iPTMnetiQ15907.
PhosphoSitePlusiQ15907.
SwissPalmiQ15907.

Expressioni

Inductioni

Up-regulated by extracellular acidosis and down-regulated by alkalosis (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000185236.
CleanExiHS_RAB11B.
ExpressionAtlasiQ15907. baseline and differential.
GenevisibleiQ15907. HS.

Organism-specific databases

HPAiHPA045753.

Interactioni

Subunit structurei

Interacts with KCNMA1 (By similarity). Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4 (PubMed:11495908). May interact with TBC1D14 (PubMed:22613832). Interacts with ATP6V1E1 (PubMed:20717956). Interacts with PI4KB (PubMed:23572552). Interacts (GDP-bound form) with ZFYVE27. Interacts (GDP-bound form) with KIF5A in a ZFYVE27-dependent manner (PubMed:21976701).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TBC1D14Q9P2M42EBI-722234,EBI-2797718

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • myosin V binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114661. 83 interactors.
DIPiDIP-50898N.
IntActiQ15907. 24 interactors.
STRINGi9606.ENSP00000333547.

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 19Combined sources11
Helixi24 – 33Combined sources10
Beta strandi47 – 55Combined sources9
Beta strandi58 – 66Combined sources9
Helixi70 – 72Combined sources3
Helixi74 – 76Combined sources3
Helixi78 – 81Combined sources4
Beta strandi85 – 92Combined sources8
Helixi96 – 100Combined sources5
Helixi102 – 112Combined sources11
Beta strandi118 – 124Combined sources7
Helixi129 – 131Combined sources3
Helixi136 – 145Combined sources10
Beta strandi149 – 152Combined sources4
Turni155 – 157Combined sources3
Helixi161 – 177Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F9LX-ray1.55A8-205[»]
2F9MX-ray1.95A8-205[»]
4OJKX-ray2.66A/B8-205[»]
ProteinModelPortaliQ15907.
SMRiQ15907.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15907.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi40 – 48Effector regionBy similarity9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0087. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ15907.
KOiK07905.
OMAiETKQGCC.
OrthoDBiEOG091G0O1R.
PhylomeDBiQ15907.
TreeFamiTF300099.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15907-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT
60 70 80 90 100
RSIQVDGKTI KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE
110 120 130 140 150
NVERWLKELR DHADSNIVIM LVGNKSDLRH LRAVPTDEAR AFAEKNNLSF
160 170 180 190 200
IETSALDSTN VEEAFKNILT EIYRIVSQKQ IADRAAHDES PGNNVVDISV
210
PPTTDGQKPN KLQCCQNL
Length:218
Mass (Da):24,489
Last modified:January 23, 2007 - v4
Checksum:i8DF146BA39EBD9FF
GO
Isoform 2 (identifier: Q15907-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     171-218: EIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL → GGRGPDGCG

Note: No experimental confirmation available.
Show »
Length:179
Mass (Da):19,971
Checksum:i9D14388D83279277
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti75A → R in CAA56176 (PubMed:7811277).Curated1
Sequence conflicti116N → D in AAV38342 (Ref. 5) Curated1
Sequence conflicti154S → A in CAG38733 (Ref. 6) Curated1
Sequence conflicti184R → C in CAG46492 (Ref. 6) Curated1
Sequence conflicti216Q → R in ABQ59034 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055832171 – 218EIYRI…CCQNL → GGRGPDGCG in isoform 2. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79780 mRNA. Translation: CAA56176.1.
EF560724 mRNA. Translation: ABQ59034.1.
AF498947 mRNA. Translation: AAM21095.1.
AK297498 mRNA. Translation: BAG59912.1.
AK312994 mRNA. Translation: BAG35831.1.
BT019535 mRNA. Translation: AAV38342.1.
BT019536 mRNA. Translation: AAV38343.1.
CR536494 mRNA. Translation: CAG38733.1.
CR541691 mRNA. Translation: CAG46492.1.
AC136469 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68927.1.
BC110081 mRNA. Translation: AAI10082.1.
CCDSiCCDS12201.1. [Q15907-1]
PIRiJC2487.
RefSeqiNP_004209.2. NM_004218.3. [Q15907-1]
UniGeneiHs.558403.
Hs.626404.

Genome annotation databases

EnsembliENST00000328024; ENSP00000333547; ENSG00000185236. [Q15907-1]
ENST00000594216; ENSP00000471148; ENSG00000185236. [Q15907-2]
GeneIDi9230.
KEGGihsa:9230.
UCSCiuc002mju.5. human. [Q15907-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79780 mRNA. Translation: CAA56176.1.
EF560724 mRNA. Translation: ABQ59034.1.
AF498947 mRNA. Translation: AAM21095.1.
AK297498 mRNA. Translation: BAG59912.1.
AK312994 mRNA. Translation: BAG35831.1.
BT019535 mRNA. Translation: AAV38342.1.
BT019536 mRNA. Translation: AAV38343.1.
CR536494 mRNA. Translation: CAG38733.1.
CR541691 mRNA. Translation: CAG46492.1.
AC136469 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68927.1.
BC110081 mRNA. Translation: AAI10082.1.
CCDSiCCDS12201.1. [Q15907-1]
PIRiJC2487.
RefSeqiNP_004209.2. NM_004218.3. [Q15907-1]
UniGeneiHs.558403.
Hs.626404.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F9LX-ray1.55A8-205[»]
2F9MX-ray1.95A8-205[»]
4OJKX-ray2.66A/B8-205[»]
ProteinModelPortaliQ15907.
SMRiQ15907.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114661. 83 interactors.
DIPiDIP-50898N.
IntActiQ15907. 24 interactors.
STRINGi9606.ENSP00000333547.

PTM databases

iPTMnetiQ15907.
PhosphoSitePlusiQ15907.
SwissPalmiQ15907.

Polymorphism and mutation databases

BioMutaiRAB11B.
DMDMi38258938.

Proteomic databases

EPDiQ15907.
MaxQBiQ15907.
PaxDbiQ15907.
PeptideAtlasiQ15907.
PRIDEiQ15907.
TopDownProteomicsiQ15907-1. [Q15907-1]

Protocols and materials databases

DNASUi9230.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328024; ENSP00000333547; ENSG00000185236. [Q15907-1]
ENST00000594216; ENSP00000471148; ENSG00000185236. [Q15907-2]
GeneIDi9230.
KEGGihsa:9230.
UCSCiuc002mju.5. human. [Q15907-1]

Organism-specific databases

CTDi9230.
DisGeNETi9230.
GeneCardsiRAB11B.
HGNCiHGNC:9761. RAB11B.
HPAiHPA045753.
MIMi604198. gene.
neXtProtiNX_Q15907.
OpenTargetsiENSG00000185236.
PharmGKBiPA34102.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0087. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ15907.
KOiK07905.
OMAiETKQGCC.
OrthoDBiEOG091G0O1R.
PhylomeDBiQ15907.
TreeFamiTF300099.

Enzyme and pathway databases

BioCyciZFISH:G66-32577-MONOMER.

Miscellaneous databases

ChiTaRSiRAB11B. human.
EvolutionaryTraceiQ15907.
GeneWikiiRAB11B.
GenomeRNAii9230.
PROiQ15907.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185236.
CleanExiHS_RAB11B.
ExpressionAtlasiQ15907. baseline and differential.
GenevisibleiQ15907. HS.

Family and domain databases

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

Entry informationi

Entry nameiRB11B_HUMAN
AccessioniPrimary (citable) accession number: Q15907
Secondary accession number(s): A5YM50
, B2R7I4, B4DMK0, D6W671, Q2YDT2, Q5U0I1, Q6FHR0, Q6FI42, Q8NI07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 171 of the entry and version 4 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.