logo CaMPDB: Calpain for Modulatory Proteolysis Database

XSB0173 : Calpain, small subunit 1 [Homo sapiens]

[ CaMP Format ]

This entry is computationally expanded from SB0017

* Basic Information

OrganismHomo sapiens (human)
Protein NamesCalpain small subunit 1; CSS1; Calcium-dependent protease small subunit 1; Calcium-dependent protease small subunit; CDPS; Calpain regulatory subunit; Calcium-activated neutral proteinase small subunit; CANP small subunit; calpain; small subunit 1
Gene LocusNot available
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
AAH21933 N/A 826 P04632 114170 1481 N/A hsa:826

* Information From OMIM

Description: Calcium-dependent cysteine proteinases, or calpains (EC, are widely distributed in mammalian cells. There are 2 distinct molecular forms, calpains I and II, which differ in the quantity of calcium required. Both calpains I and II are heterodimeric; each is composed of 1 heavy (about 80 kD), CAPN1 (OMIM:114220) and CAPN2 (OMIM:114230), respectively, and 1 shared light (about 30 kD) subunit, CAPNS1. The heavy subunit has a catalytic function, and the light subunit is regulatory.

* Structure Information

1. Primary Information

Length: 268 aa

Average Mass: 28.300 kDa

Monoisotopic Mass: 28.282 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
DUF2078 1. 10110-21.31.5
--- cleavage 141 ---
efhand 1. 14317118.40.03
efhand 2. 17320116.30.13
efhand 3. 2092360.917
efhand 4. 2382658.22.7

3. Sequence Information

Fasta Sequence: XSB0173.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1KFU (X-ray; 250 A; S=85-268), 1KFX (X-ray; 315 A; S=85-268)

* Cleavage Information

1 [sites]

Cleavage sites (±10aa)


Ile141 Asp

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: 12477932] Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA, Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.