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P17655 (CAN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calpain-2 catalytic subunit

EC=3.4.22.53
Alternative name(s):
Calcium-activated neutral proteinase 2
Short name=CANP 2
Calpain M-type
Calpain large polypeptide L2
Calpain-2 large subunit
Millimolar-calpain
Short name=M-calpain
Gene names
Name:CAPN2
Synonyms:CANPL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (Ref.9). Ref.9

Catalytic activity

Broad endopeptidase specificity.

Cofactor

Binds 7 calcium ions By similarity.

Enzyme regulation

Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.

Subunit structure

Forms a heterodimer with a small (regulatory) subunit (CAPNS1).

Subcellular location

Cytoplasm. Cell membrane. Note: Translocates to the plasma membrane upon Ca2+ binding.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the peptidase C2 family.

Contains 1 calpain catalytic domain.

Contains 3 EF-hand domains.

Sequence caution

The sequence AAH07686.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH11828.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblastocyst development

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

myoblast fusion

Inferred from electronic annotation. Source: Ensembl

protein autoprocessing

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis involved in cellular protein catabolic process

Inferred by curator PubMed 12150984. Source: BHF-UCL

regulation of cytoskeleton organization

Traceable author statement PubMed 12150984. Source: BHF-UCL

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 14559243. Source: BHF-UCL

chromatin

Inferred from electronic annotation. Source: Ensembl

cortical actin cytoskeleton

Traceable author statement PubMed 12150984. Source: BHF-UCL

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 12150984PubMed 14559243. Source: BHF-UCL

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 14559243. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

membrane raft

Inferred from direct assay PubMed 14559243. Source: BHF-UCL

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear endoplasmic reticulum

Inferred from direct assay PubMed 14559243. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 12150984. Source: BHF-UCL

pseudopodium

Inferred from direct assay PubMed 14559243. Source: BHF-UCL

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: Ensembl

calcium-dependent cysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type peptidase activity

Traceable author statement PubMed 2209092. Source: ProtInc

cytoskeletal protein binding

Non-traceable author statement PubMed 12150984. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.11PubMed 18519038PubMed 24705354. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAPNS1P046323EBI-1028956,EBI-711828
ZDHHC17Q8IUH52EBI-1028956,EBI-524753

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P17655-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P17655-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
     79-79: T → M
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.10
Propeptide2 – 1918Anchors to the small subunit Potential
PRO_0000026487
Chain20 – 700681Calpain-2 catalytic subunit
PRO_0000026488

Regions

Domain45 – 344300Calpain catalytic
Domain572 – 60534EF-hand 1
Domain602 – 63736EF-hand 2
Domain667 – 70034EF-hand 3
Calcium binding585 – 596121
Calcium binding615 – 626122
Region345 – 514170Domain III
Region515 – 52915Linker
Region530 – 700171Domain IV

Sites

Active site1051 By similarity
Active site2621 By similarity
Active site2861 By similarity
Metal binding891Calcium 3; via carbonyl oxygen By similarity
Metal binding911Calcium 3; via carbonyl oxygen By similarity
Metal binding961Calcium 3 By similarity
Metal binding1751Calcium 3 By similarity
Metal binding2291Calcium 2 By similarity
Metal binding2301Calcium 2 By similarity
Metal binding2921Calcium 4 By similarity
Metal binding2991Calcium 4 By similarity
Metal binding3231Calcium 4; via carbonyl oxygen By similarity
Metal binding5421Calcium 5; via carbonyl oxygen By similarity
Metal binding5451Calcium 5 By similarity
Metal binding5471Calcium 5; via carbonyl oxygen By similarity
Metal binding5521Calcium 5 By similarity
Metal binding5851Calcium 6 By similarity
Metal binding5871Calcium 6 By similarity
Metal binding5891Calcium 6; via carbonyl oxygen By similarity
Metal binding5911Calcium 6; via carbonyl oxygen By similarity
Metal binding5961Calcium 6 By similarity
Metal binding6151Calcium 7 By similarity
Metal binding6171Calcium 7 By similarity
Metal binding6191Calcium 7; via carbonyl oxygen By similarity
Metal binding6211Calcium 7; via carbonyl oxygen By similarity
Metal binding6261Calcium 7 By similarity
Metal binding6581Calcium 1 By similarity
Metal binding6611Calcium 1 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.10

Natural variations

Alternative sequence1 – 7878Missing in isoform 2.
VSP_043027
Alternative sequence791T → M in isoform 2.
VSP_043028
Natural variant221D → E. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7 Ref.12
Corresponds to variant rs25655 [ dbSNP | Ensembl ].
VAR_014435
Natural variant681S → G. Ref.4 Ref.7
Corresponds to variant rs2230083 [ dbSNP | Ensembl ].
VAR_021404
Natural variant4761K → R. Ref.4
Corresponds to variant rs9804140 [ dbSNP | Ensembl ].
VAR_021405
Natural variant5211E → Q. Ref.4
Corresponds to variant rs28370127 [ dbSNP | Ensembl ].
VAR_021406
Natural variant5681K → Q. Ref.4
Corresponds to variant rs17599 [ dbSNP | Ensembl ].
VAR_014436
Natural variant6771K → Q. Ref.4
Corresponds to variant rs2230082 [ dbSNP | Ensembl ].
VAR_021407

Experimental info

Sequence conflict73 – 742IE → MR in AAA35645. Ref.1
Sequence conflict2561Q → K in AAF99682. Ref.2
Sequence conflict3001N → S in AAF99682. Ref.2
Sequence conflict5341F → V in AAA35645. Ref.1
Sequence conflict5341F → V in AAF99682. Ref.2

Secondary structure

.......................................................................................................................................... 700
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 6.
Checksum: 8CF8294351A024E3

FASTA70079,995
        10         20         30         40         50         60 
MAGIAAKLAK DREAAEGLGS HDRAIKYLNQ DYEALRNECL EAGTLFQDPS FPAIPSALGF 

        70         80         90        100        110        120 
KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI 

       130        140        150        160        170        180 
LARVVPLNQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL 

       190        200        210        220        230        240 
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC 

       250        260        270        280        290        300 
SIDITSAADS EAITFQKLVK GHAYSVTGAE EVESNGSLQK LIRIRNPWGE VEWTGRWNDN 

       310        320        330        340        350        360 
CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS DTYKKWKLTK 

       370        380        390        400        410        420 
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED GESGCTFLVG LIQKHRRRQR 

       430        440        450        460        470        480 
KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK NFFLTNRARE RSDTFINLRE VLNRFKLPPG 

       490        500        510        520        530        540 
EYILVPSTFE PNKDGDFCIR VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ 

       550        560        570        580        590        600 
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL 

       610        620        630        640        650        660 
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF ADDQLIIDFD 

       670        680        690        700 
NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL 

« Hide

Isoform 2 [UniParc].

Checksum: 60ED3A3498F6DD5D
Show »

FASTA62271,476

References

« Hide 'large scale' references
[1]"Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease."
Imajoh S., Aoki K., Ohno S., Emori Y., Kawasaki H., Sugihara H., Suzuki K.
Biochemistry 27:8122-8128(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-22.
[2]"cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs."
Ye Z., Connor J.R.
Biochem. Biophys. Res. Commun. 275:223-227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-22.
Tissue: Astrocytoma.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]NIEHS SNPs program
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-22; GLY-68; ARG-476; GLN-521; GLN-568 AND GLN-677.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-22.
Tissue: Pancreas, Placenta and Skin.
[7]"Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease."
Hata A., Ohno S., Akita Y., Suzuki K.
J. Biol. Chem. 264:6404-6411(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79, VARIANTS GLU-22 AND GLY-68.
Tissue: Lymph node.
[8]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12.
Tissue: Platelet.
[9]"Characterization of the intracellular proteolytic cleavage of myocilin and identification of calpain II as a myocilin-processing protease."
Sanchez-Sanchez F., Martinez-Redondo F., Aroca-Aguilar J.D., Coca-Prados M., Escribano J.
J. Biol. Chem. 282:27810-27824(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium."
Strobl S., Fernandez-Catalan C., Braun M., Huber R., Masumoto H., Nakagawa K., Irie A., Sorimachi H., Bourenkow G., Bartunik H., Suzuki K., Bode W.
Proc. Natl. Acad. Sci. U.S.A. 97:588-592(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23254 mRNA. Translation: AAA35645.1.
AF261089 mRNA. Translation: AAF99682.1.
AK316211 mRNA. Translation: BAH14582.1.
AY835586 Genomic DNA. Translation: AAV80421.1.
AC096542 Genomic DNA. No translation available.
AC099065 Genomic DNA. No translation available.
BC007686 mRNA. Translation: AAH07686.1. Sequence problems.
BC011828 mRNA. Translation: AAH11828.1. Sequence problems.
BC021303 mRNA. Translation: AAH21303.1.
J04700 Genomic DNA. Translation: AAA52760.1.
CCDSCCDS31035.1. [P17655-1]
CCDS53478.1. [P17655-2]
PIRCIHUH2. S10590.
RefSeqNP_001139540.1. NM_001146068.1. [P17655-2]
NP_001739.2. NM_001748.4.
UniGeneHs.350899.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KFUX-ray2.50L2-700[»]
1KFXX-ray3.15L2-700[»]
2NQAX-ray2.20A/B48-346[»]
ProteinModelPortalP17655.
SMRP17655. Positions 2-700.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107274. 36 interactions.
IntActP17655. 6 interactions.
MINTMINT-120195.
STRING9606.ENSP00000295006.

Chemistry

BindingDBP17655.
ChEMBLCHEMBL3038466.

Protein family/group databases

MEROPSC02.002.

PTM databases

PhosphoSiteP17655.

Polymorphism databases

DMDM317373596.

Proteomic databases

MaxQBP17655.
PaxDbP17655.
PeptideAtlasP17655.
PRIDEP17655.

Protocols and materials databases

DNASU824.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295006; ENSP00000295006; ENSG00000162909. [P17655-1]
ENST00000433674; ENSP00000413158; ENSG00000162909. [P17655-2]
GeneID824.
KEGGhsa:824.
UCSCuc001hob.4. human. [P17655-1]
uc010puy.2. human. [P17655-2]

Organism-specific databases

CTD824.
GeneCardsGC01P223890.
HGNCHGNC:1479. CAPN2.
HPAHPA024470.
MIM114230. gene.
neXtProtNX_P17655.
PharmGKBPA26060.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327523.
HOVERGENHBG012645.
InParanoidP17655.
KOK03853.
OMADTYKKWK.
OrthoDBEOG7RV9FM.
PhylomeDBP17655.
TreeFamTF314748.

Enzyme and pathway databases

BRENDA3.4.22.53. 2681.

Gene expression databases

ArrayExpressP17655.
BgeeP17655.
CleanExHS_CAPN2.
GenevestigatorP17655.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamPF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSPR00704. CALPAIN.
SMARTSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]
SUPFAMSSF49758. SSF49758. 1 hit.
PROSITEPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17655.
GeneWikiCAPN2.
GenomeRNAi824.
NextBio3374.
PROP17655.
SOURCESearch...

Entry information

Entry nameCAN2_HUMAN
AccessionPrimary (citable) accession number: P17655
Secondary accession number(s): A6NDG7 expand/collapse secondary AC list , B7ZA96, E7ES58, Q16738, Q6PJT3, Q8WU26, Q9HBB1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 180 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM