SPTB

Spectrin, beta, erythrocytic

PDB rendering based on 1s35.

Available structures
PDB	1S35, 3EDU, 3F57, 3KBT, 3KBU, 3LBX

Identifiers

Symbols

SPTB; EL3; HS2; HSPTB1; SPH2

External IDs

OMIM: 182870 MGI: 98387 HomoloGene: 295 GeneCards: SPTB Gene

Gene Ontology
Molecular function	• actin binding • structural constituent of cytoskeleton • protein binding • actin filament binding
Cellular component	• cytoplasm • cytosol • cytosol • cell cortex • spectrin • cell surface • spectrin-associated cytoskeleton • actin cytoskeleton • intrinsic to internal side of plasma membrane • protein complex
Biological process	• axon guidance • actin filament capping
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
65.21 – 65.35 Mb

Chr 12:
77.68 – 77.81 Mb

PubMed search

[1]

[2]

Spectrin beta chain, erythrocyte is a protein that in humans is encoded by the SPTB gene.^[1]^[2]

References

^ Fukushima Y, Byers MG, Watkins PC, Winkelmann JC, Forget BG, Shows TB (Nov 1990). "Assignment of the gene for beta-spectrin (SPTB) to chromosome 14q23----q24.2 by in situ hybridization". Cytogenet Cell Genet 53 (4): 232–3. doi:10.1159/000132939. PMID 2209094.
^ "Entrez Gene: SPTB spectrin, beta, erythrocytic (includes spherocytosis, clinical type I)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6710.

Bennett V, Baines AJ (2001). "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues.". Physiol. Rev. 81 (3): 1353–92. PMID 11427698.
Kanzaki A, Rabodonirina M, Yawata Y et al. (1992). "A deletional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Tokyo (beta 220/216)". Blood 80 (8): 2115–21. PMID 1391962.
Speicher DW, Weglarz L, DeSilva TM (1992). "Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site". J. Biol. Chem. 267 (21): 14775–82. PMID 1634521.
Gallagher PG, Tse WT, Costa F et al. (1991). "A splice site mutation of the beta-spectrin gene causing exon skipping in hereditary elliptocytosis associated with a truncated beta-spectrin chain". J. Biol. Chem. 266 (23): 15154–9. PMID 1840591.
Tse WT, Lecomte MC, Costa FF et al. (1990). "Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association". J. Clin. Invest. 86 (3): 909–16. doi:10.1172/JCI114792. PMC 296810. PMID 1975598. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=296810.
Yoon SH, Kentros CG, Prchal JT (1990). "Identification of an unusual deletion within homologous repeats of human reticulocyte beta-spectrin and probable peptide polymorphism". Gene 91 (2): 297–302. doi:10.1016/0378-1119(90)90104-Y. PMID 1976574.
Garbarz M, Tse WT, Gallagher PG et al. (1991). "Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation". J. Clin. Invest. 88 (1): 76–81. doi:10.1172/JCI115307. PMC 296005. PMID 2056132. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=296005.
Tse WT, Gallagher PG, Pothier B et al. (1991). "An insertional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin nice (beta 220/216)". Blood 78 (2): 517–23. PMID 2070088.
Winkelmann JC, Chang JG, Tse WT et al. (1990). "Full-length sequence of the cDNA for human erythroid beta-spectrin". J. Biol. Chem. 265 (20): 11827–32. PMID 2195026.
Winkelmann JC, Costa FF, Linzie BL, Forget BG (1990). "Beta spectrin in human skeletal muscle. Tissue-specific differential processing of 3' beta spectrin pre-mRNA generates a beta spectrin isoform with a unique carboxyl terminus". J. Biol. Chem. 265 (33): 20449–54. PMID 2243099.
Coetzer T, Palek J, Lawler J et al. (1990). "Structural and functional heterogeneity of alpha spectrin mutations involving the spectrin heterodimer self-association site: relationships to hematologic expression of homozygous hereditary elliptocytosis and hereditary pyropoikilocytosis". Blood 75 (11): 2235–44. PMID 2346784.
Winkelmann JC, Leto TL, Watkins PC et al. (1988). "Molecular cloning of the cDNA for human erythrocyte beta-spectrin". Blood 72 (1): 328–34. PMID 3390609.
Prchal JT, Morley BJ, Yoon SH et al. (1987). "Isolation and characterization of cDNA clones for human erythrocyte beta-spectrin". Proc. Natl. Acad. Sci. U.S.A. 84 (21): 7468–72. doi:10.1073/pnas.84.21.7468. PMC 299317. PMID 3478706. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=299317.
Pothier B, Morlé L, Alloisio N et al. (1987). "Spectrin Nice (beta 220/216): a shortened beta-chain variant associated with an increase of the alpha I/74 fragment in a case of elliptocytosis". Blood 69 (6): 1759–65. PMID 3580577.
Wolfe LC, John KM, Falcone JC et al. (1982). "A genetic defect in the binding of protein 4.1 to spectrin in a kindred with hereditary spherocytosis". N. Engl. J. Med. 307 (22): 1367–74. doi:10.1056/NEJM198211253072203. PMID 6215583.
Speicher DW, Marchesi VT (1984). "Erythrocyte spectrin is composed of many homologous triple helical segments". Nature 311 (5982): 177–80. doi:10.1038/311177a0. PMID 6472478.
Carlier MF, Simon C, Cassoly R, Pradel LA (1984). "Interaction between microtubule-associated protein tau and spectrin". Biochimie 66 (4): 305–11. doi:10.1016/0300-9084(84)90007-5. PMID 6743699.
Goodman SR, Shiffer KA, Casoria LA, Eyster ME (1982). "Identification of the molecular defect in the erythrocyte membrane skeleton of some kindreds with hereditary spherocytosis". Blood 60 (3): 772–84. PMID 7104494.
Schischmanoff PO, Winardi R, Discher DE et al. (1995). "Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding". J. Biol. Chem. 270 (36): 21243–50. doi:10.1074/jbc.270.36.21243. PMID 7673158.

PDB gallery

1s35: Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin

Proteins of the cytoskeleton

Human

Microfilaments
(ABPs)

Myofilament

Actins	A1, A2, B, C1, G1, G2

Myosins	I (MYO1A, MYO1B, MYO1C, MYO1D, MYO1E, MYO1F, MYO1G, MYO1H) · II (MYH1, MYH2, MYH3, MYH4, MYH6, MYH7, MYH7B, MYH8, MYH9, MYH10, MYH11, MYH13, MYH14, MYH15, MYH16) · III (MYO3A, MYO3B) · V (MYO5A, MYO5B, MYO5C) · VI (MYO6) · VII (MYO7A, MYO7B) · IX (MYO9A, MYO9B) · X (MYO10) · XV (MYO15A) · XVIII (MYO18A, MYO18B) · LC (MYL1, MYL2, MYL3, MYL4, MYL5, MYL6, MYL6B, MYL7, MYL9, MYLIP, MYLK, MYLK2, MYLL1)

Other	Tropomodulin (1, 2, 3, 4) · Troponin (T 1 2 3, C 1 2, I 1 2 3) · Tropomyosin (1, 2, 3, 4) Actinin (1, 2, 3, 4) · Arp2/3 complex · actin depolymerizing factors (Cofilin (1, 2) · Destrin) · Gelsolin · Profilin (1, 2) · Titin

Other

Wiskott-Aldrich syndrome protein · Fibrillin · Filamin (FLNA, FLNB, FLNC) · Espin · TRIOBP

IFs

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 (10, 12, 13, 14, 15, 16, 17, 19, 20) · chromosome 12 (18) · none (21) type II/chromosome 12 (1, 2A, 3, 4, 5, 6A, 6B, 7, 8, 9)

Hair keratins (hard alpha-keratins)	type I/chromosome 17 (31, 32, 33A, 33B, 34, 35, 36, 37, 38) type II/chromosome 12 (81, 82, 83, 84, 85, 86)

Ungrouped alpha	chromosome 17 (23, 24, 25, 26, 27, 28, 39, 40) chromosome 12 (71, 72, 73, 74, 75, 76, 77, 78, 79, 80)

Not alpha	Beta-keratin

Type 3

Desmin, GFAP, Peripherin, Vimentin

Type 4

Internexin, Nestin, Neurofilament (NEFL, NEFM, NEFH), Synemin, Syncoilin

Type 5

Lamin A, B

Microtubules/
MAPs

Kinesins	KIF1A, KIF1B, KIF2A, KIF2C, KIF3B, KIF3C, KIF4A, KIF4B, KIF5A, KIF5B, KIF5C, KIF6, KIF7, KIF9, KIF11, KIF12, KIF13A, KIF13B, KIF14, KIF15, KIF16B, KIF17, KIF18A, KIF18B, KIF19, KIF20A, KIF20B, KIF21A, KIF21B, KIF22, KIF23, KIF24, KIF25, KIF26A, KIF26B, KIF27, KIFC1, KIFC2, KIFC3

Dyneins	axonemal: DNAH1, DNAH2, DNAH3, DNAH5, DNAH6, DNAH7, DNAH8, DNAH9, DNAH10, DNAH11, DNAH12, DNAH13, DNAH14, DNAH17, DNAI1, DNAI2, DNALI1, DNAL1, DNAL4 cytoplasmic: DYNC1H1, DYNC2H1, DYNC1I1, DYNC1I2, DYNC1LI1, DYNC1LI2, DYNC2LI1, DYNLL1, DYNLL2, DYNLRB1, DYNLRB2, DYNLT1, DYNLT3

Other	Tau protein · Dynactin (DCTN1) · Tubulins (TUBA1A, TUBA1B, TUBA1C, TUBA3C, TUBA3D, TUBA3E, TUBA4A, TUBA8) · Stathmin · Tektin (TEKT1, TEKT2, TEKT3, TEKT4, TEKT5) · Dynamin (DNM1, DNM2, DNM3)

Catenins

Alpha catenin · Beta catenin (APC) · Plakoglobin (gamma catenin) · Delta catenin · GAN

Membrane

Dystrophin (Dystroglycan) · Utrophin · Ankyrin (ANK1, ANK2, ANK3) · Spectrin (SPTA1, SPTAN1, SPTB, SPTBN1, SPTBN2, SPTBN4, SPTBN5)

Other

plakin (Desmoplakin, Plectin) · Talin (TLN1) · Vinculin · Plakophilin (PKP1, PKP2)

Nonhuman

Major sperm proteins · Prokaryotic cytoskeleton (Crescentin, FtsZ, MreB)

see also cytoskeletal defects
B strc: edmb (perx), skel (ctrs), epit, cili, mito, nucl (chro)

SPTB

References

Further reading