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XSB2879 : spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) isoform 2 [Homo sapiens]

[ CaMP Format ]

This entry is computationally expanded from SB0061

* Basic Information

OrganismHomo sapiens (human)
Protein NamesSpectrin alpha chain, brain; Spectrin, non-erythroid alpha chain; Alpha-II spectrin; Fodrin alpha chain; spectrin; alpha; non-erythrocytic 1 (alpha-fodrin) isoform 2; non-erythrocytic spectrin alpha
Gene NamesSPTAN1; SPTA2; spectrin, alpha, non-erythrocytic 1 (alpha-fodrin)
Gene Locus9q33-q34; chromosome 9
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_003118 NM_003127 6709 SPTA2_HUMAN 182810 11273 N/A hsa:6709

* Information From OMIM

Text: The spectrins are a family of widely-distributed filamentous cytoskeletal proteins which have a highly conserved 106-amino acid repeat structure. Spectrins are heterodimers of a constant alpha-chain and variable, tissue-specific beta-chains. Functions of these proteins include regulation of receptor binding and actin crosslinking. Barton et al. (1987) and Leto et al. (1988) used a probe for nonerythroid alpha-spectrin derived from a rat brain cDNA library to map the corresponding gene in man. The findings of somatic cell hybrid studies and in situ hybridization indicated localization in the region 9q33-q34. The cDNA that they used encodes a protein also known as alpha-fodrin. McMahon et al. (1987) cloned the alpha-fodrin gene from a human lung fibroblast cDNA library. From this, they compared the structure of alpha-spectrin and alpha-fodrin with deductions as to their evolution. Birkenmeier et al. (1988) showed that the brain alpha-spectrin gene is located on the centromeric end of mouse chromosome 2 and is not closely linked to any known erythroid or neurologic mutation. They symbolized this gene in the mouse as Spna-2. Leto et al. (1988) found close similarities of sequence in diverse species.

* Structure Information

1. Primary Information

Length: 2472 aa

Average Mass: 284.539 kDa

Monoisotopic Mass: 284.364 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Spectrin 1. 44147128.03.1e-35
Spectrin 2. 149253139.88.3e-39
Spectrin 3. 255359139.51e-38
Spectrin 4. 361465115.02.5e-31
Spectrin 5. 467571131.33e-36
Spectrin 6. 573676125.41.9e-34
Spectrin 7. 678782146.39.3e-41
Spectrin 8. 784888153.37.5e-43
SH3_1 1. 970102478.91.8e-20
Spectrin 9. 1091123171.62.9e-18
--- cleavage 1176 (inside Spectrin 1091..1231) ---
Spectrin 10. 12331337149.21.3e-41
Spectrin 11. 13391443119.79.5e-33
Spectrin 12. 14451549127.93.3e-35
Spectrin 13. 15511656100.84.6e-27
Spectrin 14. 16581762135.12.3e-37
Spectrin 15. 17641868146.86.5e-41
Spectrin 16. 18701974130.94e-36
Spectrin 17. 19762081121.03.8e-33
Spectrin 18. 2091219572.21.9e-18
Spectrin 19. 2205231068.72.1e-17
efhand 1. 2327235536.51e-07
efhand 2. 2370239823.40.00096
efhand_Ca_insen 1. 2402247144.63.8e-10

3. Sequence Information

Fasta Sequence: XSB2879.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 2FOT (X-ray; 245 A; C=1172-1210), 3FB2 (X-ray; 230 A; A/B=1337-1544)

* Cleavage Information

1 [sites]

Cleavage sites (±10aa)


Tyr1176 Gly

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 19217883] McMahon LW, Zhang P, Sridharan DM, Lefferts JA, Lambert MW, Knockdown of alphaII spectrin in normal human cells by siRNA leads to chromosomal instability and decreased DNA interstrand cross-link repair. Biochem Biophys Res Commun. 2009 Apr 3;381(2):288-93. Epub 2009 Feb 13.

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