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P17655

- CAN2_HUMAN

UniProt

P17655 - CAN2_HUMAN

Protein

Calpain-2 catalytic subunit

Gene

CAPN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 6 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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' (PubMed:17650508).1 Publication

    Catalytic activityi

    Broad endopeptidase specificity.

    Cofactori

    Binds 7 calcium ions.By similarity

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi89 – 891Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi91 – 911Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi96 – 961Calcium 3By similarity
    Active sitei105 – 1051By similarity
    Metal bindingi175 – 1751Calcium 3By similarity
    Metal bindingi229 – 2291Calcium 2By similarity
    Metal bindingi230 – 2301Calcium 2By similarity
    Active sitei262 – 2621By similarity
    Active sitei286 – 2861By similarity
    Metal bindingi292 – 2921Calcium 4By similarity
    Metal bindingi299 – 2991Calcium 4By similarity
    Metal bindingi323 – 3231Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi542 – 5421Calcium 5; via carbonyl oxygenBy similarity
    Metal bindingi545 – 5451Calcium 5By similarity
    Metal bindingi547 – 5471Calcium 5; via carbonyl oxygenBy similarity
    Metal bindingi552 – 5521Calcium 5By similarity
    Metal bindingi585 – 5851Calcium 6By similarity
    Metal bindingi587 – 5871Calcium 6By similarity
    Metal bindingi589 – 5891Calcium 6; via carbonyl oxygenBy similarity
    Metal bindingi591 – 5911Calcium 6; via carbonyl oxygenBy similarity
    Metal bindingi596 – 5961Calcium 6By similarity
    Metal bindingi615 – 6151Calcium 7By similarity
    Metal bindingi617 – 6171Calcium 7By similarity
    Metal bindingi619 – 6191Calcium 7; via carbonyl oxygenBy similarity
    Metal bindingi621 – 6211Calcium 7; via carbonyl oxygenBy similarity
    Metal bindingi626 – 6261Calcium 7By similarity
    Metal bindingi658 – 6581Calcium 1By similarity
    Metal bindingi661 – 6611Calcium 1By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi585 – 596121Add
    BLAST
    Calcium bindingi615 – 626122Add
    BLAST

    GO - Molecular functioni

    1. calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
    2. calcium ion binding Source: Ensembl
    3. cysteine-type peptidase activity Source: ProtInc
    4. cytoskeletal protein binding Source: BHF-UCL
    5. protein binding Source: IntAct

    GO - Biological processi

    1. blastocyst development Source: Ensembl
    2. cellular response to amino acid stimulus Source: UniProtKB
    3. myoblast fusion Source: Ensembl
    4. protein autoprocessing Source: Ensembl
    5. proteolysis Source: UniProtKB
    6. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
    7. regulation of cytoskeleton organization Source: BHF-UCL
    8. response to hypoxia Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.22.53. 2681.

    Protein family/group databases

    MEROPSiC02.002.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:CAPN2
    Synonyms:CANPL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1479. CAPN2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. chromatin Source: Ensembl
    2. cortical actin cytoskeleton Source: BHF-UCL
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: BHF-UCL
    5. dendrite Source: UniProtKB
    6. endoplasmic reticulum Source: BHF-UCL
    7. extracellular vesicular exosome Source: UniProt
    8. Golgi apparatus Source: BHF-UCL
    9. membrane raft Source: BHF-UCL
    10. nucleus Source: Ensembl
    11. perinuclear endoplasmic reticulum Source: BHF-UCL
    12. plasma membrane Source: BHF-UCL
    13. pseudopodium Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26060.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Propeptidei2 – 1918Anchors to the small subunitSequence AnalysisPRO_0000026487Add
    BLAST
    Chaini20 – 700681Calpain-2 catalytic subunitPRO_0000026488Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP17655.
    PaxDbiP17655.
    PeptideAtlasiP17655.
    PRIDEiP17655.

    PTM databases

    PhosphoSiteiP17655.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP17655.
    BgeeiP17655.
    CleanExiHS_CAPN2.
    GenevestigatoriP17655.

    Organism-specific databases

    HPAiHPA024470.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAPNS1P046323EBI-1028956,EBI-711828
    ZDHHC17Q8IUH52EBI-1028956,EBI-524753

    Protein-protein interaction databases

    BioGridi107274. 37 interactions.
    IntActiP17655. 6 interactions.
    MINTiMINT-120195.
    STRINGi9606.ENSP00000295006.

    Structurei

    Secondary structure

    1
    700
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1613
    Turni17 – 193
    Helixi27 – 293
    Helixi32 – 4211
    Beta strandi49 – 513
    Helixi55 – 584
    Beta strandi60 – 689
    Beta strandi74 – 763
    Helixi78 – 814
    Beta strandi82 – 843
    Helixi94 – 963
    Beta strandi97 – 993
    Helixi105 – 11511
    Helixi118 – 1247
    Beta strandi131 – 1344
    Beta strandi136 – 1449
    Beta strandi146 – 15510
    Beta strandi158 – 1614
    Beta strandi164 – 1674
    Beta strandi169 – 1757
    Helixi177 – 18913
    Beta strandi190 – 1923
    Helixi193 – 1953
    Beta strandi196 – 1994
    Turni204 – 2063
    Helixi207 – 2093
    Beta strandi212 – 2165
    Helixi224 – 23310
    Beta strandi237 – 2415
    Helixi247 – 2493
    Beta strandi259 – 2613
    Beta strandi264 – 27411
    Beta strandi277 – 2859
    Beta strandi294 – 2974
    Beta strandi299 – 3013
    Helixi302 – 3065
    Helixi309 – 3157
    Beta strandi321 – 3277
    Helixi328 – 3347
    Beta strandi336 – 3416
    Helixi344 – 3463
    Beta strandi347 – 3493
    Beta strandi363 – 3653
    Turni367 – 3704
    Turni378 – 3803
    Helixi381 – 3833
    Beta strandi388 – 3903
    Beta strandi400 – 4023
    Beta strandi406 – 4138
    Beta strandi420 – 4256
    Beta strandi429 – 4357
    Turni442 – 4443
    Helixi450 – 4556
    Beta strandi459 – 4613
    Beta strandi466 – 4716
    Beta strandi474 – 4763
    Beta strandi479 – 49214
    Beta strandi495 – 50511
    Beta strandi507 – 5093
    Beta strandi527 – 5304
    Helixi533 – 5419
    Beta strandi542 – 5465
    Helixi550 – 56011
    Turni561 – 5644
    Helixi574 – 5829
    Beta strandi586 – 5883
    Beta strandi590 – 5923
    Helixi595 – 61218
    Beta strandi622 – 6243
    Helixi627 – 6304
    Turni631 – 6355
    Helixi640 – 65011
    Beta strandi655 – 6573
    Helixi659 – 67921
    Beta strandi687 – 6904
    Helixi691 – 6988

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KFUX-ray2.50L2-700[»]
    1KFXX-ray3.15L2-700[»]
    2NQAX-ray2.20A/B48-346[»]
    ProteinModelPortaliP17655.
    SMRiP17655. Positions 2-700.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17655.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 344300Calpain catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini572 – 60534EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini602 – 63736EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini667 – 70034EF-hand 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni345 – 514170Domain IIIAdd
    BLAST
    Regioni515 – 52915LinkerAdd
    BLAST
    Regioni530 – 700171Domain IVAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C2 family.Curated
    Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
    Contains 3 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG327523.
    HOVERGENiHBG012645.
    InParanoidiP17655.
    KOiK03853.
    OMAiDTYKKWK.
    OrthoDBiEOG7RV9FM.
    PhylomeDBiP17655.
    TreeFamiTF314748.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR022684. Calpain_cysteine_protease.
    IPR022682. Calpain_domain_III.
    IPR022683. Calpain_III.
    IPR029539. CAPN2.
    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]
    PANTHERiPTHR10183:SF268. PTHR10183:SF268. 1 hit.
    PfamiPF01067. Calpain_III. 1 hit.
    PF00648. Peptidase_C2. 1 hit.
    [Graphical view]
    PRINTSiPR00704. CALPAIN.
    SMARTiSM00720. calpain_III. 1 hit.
    SM00230. CysPc. 1 hit.
    SM00054. EFh. 3 hits.
    [Graphical view]
    SUPFAMiSSF49758. SSF49758. 1 hit.
    PROSITEiPS50203. CALPAIN_CAT. 1 hit.
    PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P17655-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAGIAAKLAK DREAAEGLGS HDRAIKYLNQ DYEALRNECL EAGTLFQDPS    50
    FPAIPSALGF KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG 100
    ALGDCWLLAA IASLTLNEEI LARVVPLNQS FQENYAGIFH FQFWQYGEWV 150
    EVVVDDRLPT KDGELLFVHS AEGSEFWSAL LEKAYAKING CYEALSGGAT 200
    TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC SIDITSAADS 250
    EAITFQKLVK GHAYSVTGAE EVESNGSLQK LIRIRNPWGE VEWTGRWNDN 300
    CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS 350
    DTYKKWKLTK MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED 400
    GESGCTFLVG LIQKHRRRQR KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK 450
    NFFLTNRARE RSDTFINLRE VLNRFKLPPG EYILVPSTFE PNKDGDFCIR 500
    VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ LAGEDAEISA 550
    FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL 600
    WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF 650
    ADDQLIIDFD NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL 700
    Length:700
    Mass (Da):79,995
    Last modified:January 11, 2011 - v6
    Checksum:i8CF8294351A024E3
    GO
    Isoform 2 (identifier: P17655-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-78: Missing.
         79-79: T → M

    Note: No experimental confirmation available.

    Show »
    Length:622
    Mass (Da):71,476
    Checksum:i60ED3A3498F6DD5D
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 742IE → MR in AAA35645. (PubMed:2852952)Curated
    Sequence conflicti256 – 2561Q → K in AAF99682. (PubMed:10944468)Curated
    Sequence conflicti300 – 3001N → S in AAF99682. (PubMed:10944468)Curated
    Sequence conflicti534 – 5341F → V in AAA35645. (PubMed:2852952)Curated
    Sequence conflicti534 – 5341F → V in AAF99682. (PubMed:10944468)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221D → E.6 Publications
    Corresponds to variant rs25655 [ dbSNP | Ensembl ].
    VAR_014435
    Natural varianti68 – 681S → G.2 Publications
    Corresponds to variant rs2230083 [ dbSNP | Ensembl ].
    VAR_021404
    Natural varianti476 – 4761K → R.1 Publication
    Corresponds to variant rs9804140 [ dbSNP | Ensembl ].
    VAR_021405
    Natural varianti521 – 5211E → Q.1 Publication
    Corresponds to variant rs28370127 [ dbSNP | Ensembl ].
    VAR_021406
    Natural varianti568 – 5681K → Q.1 Publication
    Corresponds to variant rs17599 [ dbSNP | Ensembl ].
    VAR_014436
    Natural varianti677 – 6771K → Q.1 Publication
    Corresponds to variant rs2230082 [ dbSNP | Ensembl ].
    VAR_021407

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7878Missing in isoform 2. 1 PublicationVSP_043027Add
    BLAST
    Alternative sequencei79 – 791T → M in isoform 2. 1 PublicationVSP_043028

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS31035.1. [P17655-1]
    CCDS53478.1. [P17655-2]
    PIRiS10590. CIHUH2.
    RefSeqiNP_001139540.1. NM_001146068.1. [P17655-2]
    NP_001739.2. NM_001748.4.
    UniGeneiHs.350899.

    Genome annotation databases

    EnsembliENST00000295006; ENSP00000295006; ENSG00000162909. [P17655-1]
    ENST00000433674; ENSP00000413158; ENSG00000162909. [P17655-2]
    GeneIDi824.
    KEGGihsa:824.
    UCSCiuc001hob.4. human. [P17655-1]
    uc010puy.2. human. [P17655-2]

    Polymorphism databases

    DMDMi317373596.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS31035.1. [P17655-1 ]
    CCDS53478.1. [P17655-2 ]
    PIRi S10590. CIHUH2.
    RefSeqi NP_001139540.1. NM_001146068.1. [P17655-2 ]
    NP_001739.2. NM_001748.4.
    UniGenei Hs.350899.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KFU X-ray 2.50 L 2-700 [» ]
    1KFX X-ray 3.15 L 2-700 [» ]
    2NQA X-ray 2.20 A/B 48-346 [» ]
    ProteinModelPortali P17655.
    SMRi P17655. Positions 2-700.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107274. 37 interactions.
    IntActi P17655. 6 interactions.
    MINTi MINT-120195.
    STRINGi 9606.ENSP00000295006.

    Chemistry

    BindingDBi P17655.
    ChEMBLi CHEMBL3038466.

    Protein family/group databases

    MEROPSi C02.002.

    PTM databases

    PhosphoSitei P17655.

    Polymorphism databases

    DMDMi 317373596.

    Proteomic databases

    MaxQBi P17655.
    PaxDbi P17655.
    PeptideAtlasi P17655.
    PRIDEi P17655.

    Protocols and materials databases

    DNASUi 824.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295006 ; ENSP00000295006 ; ENSG00000162909 . [P17655-1 ]
    ENST00000433674 ; ENSP00000413158 ; ENSG00000162909 . [P17655-2 ]
    GeneIDi 824.
    KEGGi hsa:824.
    UCSCi uc001hob.4. human. [P17655-1 ]
    uc010puy.2. human. [P17655-2 ]

    Organism-specific databases

    CTDi 824.
    GeneCardsi GC01P223890.
    HGNCi HGNC:1479. CAPN2.
    HPAi HPA024470.
    MIMi 114230. gene.
    neXtProti NX_P17655.
    PharmGKBi PA26060.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327523.
    HOVERGENi HBG012645.
    InParanoidi P17655.
    KOi K03853.
    OMAi DTYKKWK.
    OrthoDBi EOG7RV9FM.
    PhylomeDBi P17655.
    TreeFami TF314748.

    Enzyme and pathway databases

    BRENDAi 3.4.22.53. 2681.

    Miscellaneous databases

    EvolutionaryTracei P17655.
    GeneWikii CAPN2.
    GenomeRNAii 824.
    NextBioi 3374.
    PROi P17655.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17655.
    Bgeei P17655.
    CleanExi HS_CAPN2.
    Genevestigatori P17655.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR022684. Calpain_cysteine_protease.
    IPR022682. Calpain_domain_III.
    IPR022683. Calpain_III.
    IPR029539. CAPN2.
    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 ]
    PANTHERi PTHR10183:SF268. PTHR10183:SF268. 1 hit.
    Pfami PF01067. Calpain_III. 1 hit.
    PF00648. Peptidase_C2. 1 hit.
    [Graphical view ]
    PRINTSi PR00704. CALPAIN.
    SMARTi SM00720. calpain_III. 1 hit.
    SM00230. CysPc. 1 hit.
    SM00054. EFh. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49758. SSF49758. 1 hit.
    PROSITEi PS50203. CALPAIN_CAT. 1 hit.
    PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCAN2_HUMAN
    AccessioniPrimary (citable) accession number: P17655
    Secondary accession number(s): A6NDG7
    , B7ZA96, E7ES58, Q16738, Q6PJT3, Q8WU26, Q9HBB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 182 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3