Ras-related protein Rab-11B (RAB11B)

The protein contains 218 amino acids for an estimated molecular weight of 24489 Da.

 

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. The small Rab GTPase RAB11B 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. (updated: May 8, 2019)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 100%
Model score: 99
MODL_MODELLER-9.18

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VariantDescription
NDAGSCW
NDAGSCW

The reference OMIM entry for this protein is 604198

Ras-associated protein rab11b; rab11b

DESCRIPTION

The Ras superfamily of small GTP-binding proteins, which includes the Ras (see 190020), Ral (see 179550), Rho (see 165390), Rap (see 179520), and Rab (see 179508) families, is involved in controlling a diverse set of essential cellular functions. The Rab family, including RAB11B, appears to play a critical role in regulating exocytotic and endocytotic pathways (summary by Zhu et al., 1994).

CLONING

By PCR using degenerate oligonucleotides based on the RAB3D (604350) amino acid sequence, followed by screening of a human fetal skeletal muscle cDNA library with the PCR product, Zhu et al. (1994) isolated cDNAs encoding RAB11B, which they called YPT3, and RAB35 (604199). The deduced 218-amino acid RAB11B protein is similar to yeast Ypt3, 99% identical to mouse Ypt3, and 91% identical to human RAB11A (605570). RAB11B contains the 4 conserved domains important for GTP binding. The C terminus sequence of RAB11B is similar to that of RAB11A; in Rab proteins, this region is thought to be involved in membrane association. Recombinant RAB11B expressed in bacteria had GTP-binding activity. Northern blot analysis detected a 1.3-kb RAB11B transcript in all human tissues examined.

MAPPING

Gross (2014) mapped the RAB11B gene to chromosome 19p13.2 based on an alignment of the RAB11B sequence (GenBank GENBANK AF498947) with the genomic sequence (GRCh38). ... More on the omim web site

Subscribe to this protein entry history

May 11, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 25, 2017: Additional information
No protein expression data in P. Mayeux work for RAB11B

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 604198 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed