RAB1A

Last updated
RAB1A
Protein RAB1A PDB 2fol.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RAB1A , RAB1, YPT1, member RAS oncogene family
External IDs OMIM: 179508 MGI: 97842 HomoloGene: 36154 GeneCards: RAB1A
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004161
NM_015543

NM_008996

RefSeq (protein)

NP_004152
NP_056358

NP_033022

Location (UCSC) Chr 2: 65.07 – 65.13 Mb Chr 11: 20.15 – 20.18 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ras-related protein Rab-1A is a protein that in humans is encoded by the RAB1A gene. [5] [6]

Interactions

RAB1A has been shown to interact with:

Related Research Articles

The Rab family of proteins is a member of the Ras superfamily of small G proteins. Approximately 70 types of Rabs have now been identified in humans. Rab proteins generally possess a GTPase fold, which consists of a six-stranded beta sheet which is flanked by five alpha helices. Rab GTPases regulate many steps of membrane trafficking, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled. Surface protein recycling returns proteins to the surface whose function involves carrying another protein or substance inside the cell, such as the transferrin receptor, or serves as a means of regulating the number of a certain type of protein molecules on the surface.

<span class="mw-page-title-main">RAB5A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-5A is a protein that in humans is encoded by the RAB5A gene.

<span class="mw-page-title-main">RAB6A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-6A is a protein that in humans is encoded by the RAB6A gene located in the eleventh chromosome. Its main function is the regulation of protein transport from the Golgi complex to the endoplasmic reticulum and the exocytosis along with the microtubules.

<span class="mw-page-title-main">COPB1</span> Protein-coding gene in humans

Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.

<span class="mw-page-title-main">Golgin subfamily A member 2</span> Protein-coding gene in the species Homo sapiens

Golgin subfamily A member 2, also known as 130 kDa cis-Golgi matrix protein 1 (GM130) is a protein that in humans is encoded by the GOLGA2 gene.

<span class="mw-page-title-main">RAB3A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-3A is a protein that in humans is encoded by the RAB3A gene. It is involved in calcium-triggered exocytosis in neurons.

<span class="mw-page-title-main">USO1</span> Protein-coding gene in the species Homo sapiens

General vesicular transport factor p115 is a protein that in humans is encoded by the USO1 gene.

<span class="mw-page-title-main">RAB8A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-8A is a protein that in humans is encoded by the RAB8A gene.

<span class="mw-page-title-main">STX5</span> Protein-coding gene in the species Homo sapiens

Syntaxin-5 is a protein that in humans is encoded by the STX5 gene.

<span class="mw-page-title-main">GOSR1</span> Protein-coding gene in the species Homo sapiens

Golgi SNAP receptor complex member 1 is a protein that in humans is encoded by the GOSR1 gene.

<span class="mw-page-title-main">RAB2A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-2A is a protein that in humans is encoded by the RAB2A gene.

<span class="mw-page-title-main">GRASP55</span> Protein-coding gene in the species Homo sapiens

Golgi reassembly-stacking protein of 55 kDa (GRASP55) also known as golgi reassembly-stacking protein 2 (GORASP2) is a protein that in humans is encoded by the GORASP2 gene. It was identified by its homology with GRASP65 and the protein's amino acid sequence was determined by analysis of a molecular clone of its complementary DNA. The first (N-terminus) 212 amino acid residues of GRASP55 are highly homologous to those of GRASP65, but the remainder of the 454 amino acid residues are highly diverged from GRASP65. The conserved region is known as the GRASP domain, and it is conserved among GRASPs of a wide variety of eukaryotes, but not plants. The C-terminus portion of the molecule is called the SPR domain. GRASP55 is more closely related to homologues in other species, suggesting that GRASP55 is ancestral to GRASP65. GRASP55 is found associated with the medial and trans cisternae of the Golgi apparatus.

<span class="mw-page-title-main">GOLGA5</span> Protein-coding gene in the species Homo sapiens

Golgin subfamily A member 5 is a protein that in humans is encoded by the GOLGA5 gene.

<span class="mw-page-title-main">BLZF1</span> Protein-coding gene in the species Homo sapiens

Golgin-45 is a protein that in humans is encoded by the BLZF1 gene.

<span class="mw-page-title-main">GCC2</span> Protein-coding gene in the species Homo sapiens

GRIP and coiled-coil domain-containing protein 2 is a protein that in humans is encoded by the GCC2 gene.

<span class="mw-page-title-main">SCFD1</span> Protein-coding gene in the species Homo sapiens

Sec1 family domain-containing protein 1 is a protein that in humans is encoded by the SCFD1 gene.

<span class="mw-page-title-main">GOSR2</span> Protein-coding gene in the species Homo sapiens

Golgi SNAP receptor complex member 2 is a protein that in humans is encoded by the GOSR2 gene.

<span class="mw-page-title-main">RAB27A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-27A is a protein that in humans is encoded by the RAB27A gene.

<span class="mw-page-title-main">Giantin</span> Protein-coding gene in the species Homo sapiens

Giantin or Golgin subfamily B member 1 is a protein that in humans is encoded by the GOLGB1 gene. Giantin is located at the cis-medial rims of the Golgi apparatus and is part of the Golgi matrix that is responsible for membrane trafficking in secretory pathway of proteins. This function is key for proper localisation of proteins at the plasma membrane and outside the cell which is important for cell function that is dependent on for example receptors and the extracellular matrix function. Recent animal model knockout studies of GOLGB1 in mice, rat, and zebrafish have shown that phenotypes are different between species ranging from mild to severe craniofacial defects in the rodent models to just minor size defects in zebrafish. However, in adult zebrafish a tumoral calcinosis-like phenotype was observed, and in humans such phenotype has been linked to defective glycosyltransferase function.

<span class="mw-page-title-main">Golgi matrix</span>

The Golgi matrix is a collection of proteins involved in the structure and function of the Golgi apparatus. The matrix was first isolated in 1994 as an amorphous collection of 12 proteins that remained associated together in the presence of detergent and 150 mM NaCl. Treatment with a protease enzyme removed the matrix, which confirmed the importance of proteins for the matrix structure. Modern freeze etch electron microscopy (EM) clearly shows a mesh connecting Golgi cisternae and associated vesicles. Further support for the existence of a matrix comes from EM images showing that ribosomes are excluded from regions between and near Golgi cisternae.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000138069 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020149 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Zahraoui A, Touchot N, Chardin P, Tavitian A (Jul 1989). "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion". The Journal of Biological Chemistry. 264 (21): 12394–401. doi: 10.1016/S0021-9258(18)63872-4 . PMID   2501306.
  6. "Entrez Gene: RAB1A RAB1A, member RAS oncogene family".
  7. 1 2 Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (Jan 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". The Journal of Biological Chemistry. 269 (3): 2111–7. doi: 10.1016/S0021-9258(17)42142-9 . PMID   8294464.
  8. Anant JS, Desnoyers L, Machius M, Demeler B, Hansen JC, Westover KD, Deisenhofer J, Seabra MC (Sep 1998). "Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex". Biochemistry. 37 (36): 12559–68. doi:10.1021/bi980881a. PMID   9730828.
  9. 1 2 Weide T, Teuber J, Bayer M, Barnekow A (Jun 2003). "MICAL-1 isoforms, novel rab1 interacting proteins". Biochemical and Biophysical Research Communications. 306 (1): 79–86. doi:10.1016/s0006-291x(03)00918-5. PMID   12788069.
  10. Valsdottir R, Hashimoto H, Ashman K, Koda T, Storrie B, Nilsson T (Nov 2001). "Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER". FEBS Letters. 508 (2): 201–9. doi: 10.1016/s0014-5793(01)02993-3 . PMID   11718716. S2CID   21545088.
  11. Short B, Preisinger C, Körner R, Kopajtich R, Byron O, Barr FA (Dec 2001). "A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic". The Journal of Cell Biology. 155 (6): 877–83. doi:10.1083/jcb.200108079. PMC   2150909 . PMID   11739401.
  12. Satoh A, Wang Y, Malsam J, Beard MB, Warren G (Mar 2003). "Golgin-84 is a rab1 binding partner involved in Golgi structure". Traffic. 4 (3): 153–61. doi:10.1034/j.1600-0854.2003.00103.x. PMC   3282115 . PMID   12656988.
  13. Diao A, Rahman D, Pappin DJ, Lucocq J, Lowe M (Jan 2003). "The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation". The Journal of Cell Biology. 160 (2): 201–12. doi:10.1083/jcb.200207045. PMC   2172652 . PMID   12538640.
  14. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
  15. Martincic I, Peralta ME, Ngsee JK (Oct 1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". The Journal of Biological Chemistry. 272 (43): 26991–8. doi: 10.1074/jbc.272.43.26991 . PMID   9341137.

Further reading