SPTBN5 Identifiers Aliases SPTBN5 , BSPECV, HUBSPECV, HUSPECV, spectrin beta, non-erythrocytic 5External 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 location (Mouse ) Chr. Chromosome 2 (mouse)[2] Band 2|2 E5 Start 119,871,974 bp [2] End 119,916,159 bp [2]
Gene ontology Molecular function Cellular component Biological process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez Ensembl UniProt RefSeq (mRNA) RefSeq (protein) Location (UCSC) Chr 15: 41.85 – 41.89 Mb Chr 2: 119.87 – 119.92 Mb PubMed search[3] [4] Wikidata
Spectrin, beta, non-erythrocytic 5 also known as SPTBN5 is a protein that in humans is encoded by the SPTBN5 gene .[5] SPTBN5 belongs to the spectrin family of cytoskeletal proteins.
Structure and function [ ]
SPTBN5 contains the following domains :[5]
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.[5]
SPTBN5 is highly expressed in embryoid bodies .[6]
References [ ]
^ a b c GRCh38: Ensembl release 89: ENSG00000137877 - Ensembl , May 2017
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000074899 - Ensembl , May 2017
^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ a b c 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 .
^ 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 .
Proteins of the cytoskeleton
Human
Microfilaments and ABPs
Myofilament
Actins Myosins
I
II
III
V
VI
VII
IX
X
XV
XVIII
LC
Other
Actinin
Arp2/3 complex
actin depolymerizing factors
Gelsolin
Profilin
Titin
Other
Intermediate filaments
Type 1/2 (Keratin ,Cytokeratin )
Epithelial keratins (soft alpha-keratins)
type I /chromosome 17
chromosome 12
none
Hair keratins (hard alpha-keratins)Ungrouped alpha Not alpha
Type 3 Type 4 Type 5
Nuclear lamins : A/C
B1
B2
Microtubules and MAPs
Tubulins Kinesins Dyneins Other
Catenins Membrane Other
Nonhuman See also: cytoskeletal defects