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P17655

- CAN2_HUMAN

UniProt

P17655 - CAN2_HUMAN

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Protein

Calpain-2 catalytic subunit

Gene

CAPN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Ca2+By similarityNote: Binds 7 Ca(2+) 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

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
Complete GO annotation...

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. focal adhesion Source: UniProtKB
  9. Golgi apparatus Source: BHF-UCL
  10. membrane raft Source: BHF-UCL
  11. nucleus Source: Ensembl
  12. perinuclear endoplasmic reticulum Source: BHF-UCL
  13. plasma membrane Source: BHF-UCL
  14. pseudopodium Source: BHF-UCL
Complete GO annotation...

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

BgeeiP17655.
CleanExiHS_CAPN2.
ExpressionAtlasiP17655. baseline and differential.
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. 41 interactions.
IntActiP17655. 7 interactions.
MINTiMINT-120195.
STRINGi9606.ENSP00000295006.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118971.
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

        10         20         30         40         50
MAGIAAKLAK DREAAEGLGS HDRAIKYLNQ DYEALRNECL EAGTLFQDPS
60 70 80 90 100
FPAIPSALGF KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG
110 120 130 140 150
ALGDCWLLAA IASLTLNEEI LARVVPLNQS FQENYAGIFH FQFWQYGEWV
160 170 180 190 200
EVVVDDRLPT KDGELLFVHS AEGSEFWSAL LEKAYAKING CYEALSGGAT
210 220 230 240 250
TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC SIDITSAADS
260 270 280 290 300
EAITFQKLVK GHAYSVTGAE EVESNGSLQK LIRIRNPWGE VEWTGRWNDN
310 320 330 340 350
CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS
360 370 380 390 400
DTYKKWKLTK MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED
410 420 430 440 450
GESGCTFLVG LIQKHRRRQR KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK
460 470 480 490 500
NFFLTNRARE RSDTFINLRE VLNRFKLPPG EYILVPSTFE PNKDGDFCIR
510 520 530 540 550
VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ LAGEDAEISA
560 570 580 590 600
FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL
610 620 630 640 650
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF
660 670 680 690 700
ADDQLIIDFD NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL
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.Curated
The sequence AAH11828.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 41 interactions.
IntActi P17655. 7 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.
GeneTreei ENSGT00760000118971.
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

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

Gene expression databases

Bgeei P17655.
CleanExi HS_CAPN2.
ExpressionAtlasi P17655. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 184 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