SPTBN5

Spectrin, beta, non-erythrocytic 5 also known as SPTBN5 is a protein that in humans is encoded by the SPTBN5 gene.[4] SPTBN5 belongs to the spectrin family of cytoskeletal proteins.

SPTBN5
Identifiers
Aliases	SPTBN5, BSPECV, HUBSPECV, HUSPECV, spectrin beta, non-erythrocytic 5
External IDs	OMIM: 605916 MGI: 2685200 HomoloGene: 41150 GeneCards: SPTBN5
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q15.1 Start 41,848,146 bp[1] End 41,894,053 bp[1]
Gene ontology Molecular function • dynactin binding • protein self-association • kinesin binding • myosin tail binding • actin binding • dynein intermediate chain binding • spectrin binding • Ras guanyl-nucleotide exchange factor activity Cellular component • cytoplasm • cytosol • spectrin • membrane • photoreceptor connecting cilium • photoreceptor disc membrane • cytoskeleton • microtubule organizing center • filamentous actin Biological process • Golgi organization • MAPK cascade • axon guidance • ER to Golgi vesicle-mediated transport • actin filament capping • lysosomal transport • protein homooligomerization • actin cytoskeleton organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51332	640524
Ensembl	ENSG00000137877	n/a
UniProt	Q9NRC6	n/a
RefSeq (mRNA)	NM_016642	NM_001370938
RefSeq (protein)	NP_057726	n/a
Location (UCSC)	Chr 15: 41.85 – 41.89 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

Structure and function

SPTBN5 contains the following domains:[4]

• actin-binding domain
• membrane-association domain-1
• self-association domain
• C-terminal pleckstrin homology domain.

Based on these structural features it is thought that SPTBN5 is likely to form heterodimers and oligomers with alpha-spectrin and to interact directly with cellular membranes.[4]

SPTBN5 is highly expressed in embryoid bodies.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000137877 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Stabach PR, Morrow JS (July 2000). "Identification and characterization of beta V spectrin, a mammalian ortholog of Drosophila beta H spectrin". J. Biol. Chem. 275 (28): 21385–95. doi:10.1074/jbc.C000159200. PMID 10764729.
5. Chaerkady R, Kerr CL, Marimuthu A, Kelkar DS, Kashyap MK, Gucek M, Gearhart JD, Pandey A (January 2009). "Temporal analysis of neural differentiation using quantitative proteomics". J. Proteome Res. 8 (3): 1315–26. doi:10.1021/pr8006667. PMC 2693473. PMID 19173612.

Further reading

• Odell AF, Van Helden DF, Scott JL (2008). "The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels". J. Biol. Chem. 283 (7): 4395–407. doi:10.1074/jbc.M709729200. PMID 18048348.
• Oguri M, Kato K, Yokoi K, et al. (2010). "Assessment of a polymorphism of SDK1 with hypertension in Japanese Individuals". Am. J. Hypertens. 23 (1): 70–7. doi:10.1038/ajh.2009.190. PMID 19851296.
• Shoeman RL, Hartig R, Hauses C, Traub P (2002). "Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease". Cell Biol. Int. 26 (6): 529–39. doi:10.1006/cbir.2002.0895. PMID 12119179.
• Chardin P, Camonis JH, Gale NW, et al. (1993). "Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2". Science. 260 (5112): 1338–43. doi:10.1126/science.8493579. PMID 8493579.