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P17655

- CAN2_HUMAN

UniProt

P17655 - CAN2_HUMAN

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Protein

Calpain-2 catalytic subunit

Gene
CAPN2, CANPL2
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' (1 Publication).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 oxygen By similarity
Metal bindingi91 – 911Calcium 3; via carbonyl oxygen By similarity
Metal bindingi96 – 961Calcium 3 By similarity
Active sitei105 – 1051 By similarity
Metal bindingi175 – 1751Calcium 3 By similarity
Metal bindingi229 – 2291Calcium 2 By similarity
Metal bindingi230 – 2301Calcium 2 By similarity
Active sitei262 – 2621 By similarity
Active sitei286 – 2861 By similarity
Metal bindingi292 – 2921Calcium 4 By similarity
Metal bindingi299 – 2991Calcium 4 By similarity
Metal bindingi323 – 3231Calcium 4; via carbonyl oxygen By similarity
Metal bindingi542 – 5421Calcium 5; via carbonyl oxygen By similarity
Metal bindingi545 – 5451Calcium 5 By similarity
Metal bindingi547 – 5471Calcium 5; via carbonyl oxygen By similarity
Metal bindingi552 – 5521Calcium 5 By similarity
Metal bindingi585 – 5851Calcium 6 By similarity
Metal bindingi587 – 5871Calcium 6 By similarity
Metal bindingi589 – 5891Calcium 6; via carbonyl oxygen By similarity
Metal bindingi591 – 5911Calcium 6; via carbonyl oxygen By similarity
Metal bindingi596 – 5961Calcium 6 By similarity
Metal bindingi615 – 6151Calcium 7 By similarity
Metal bindingi617 – 6171Calcium 7 By similarity
Metal bindingi619 – 6191Calcium 7; via carbonyl oxygen By similarity
Metal bindingi621 – 6211Calcium 7; via carbonyl oxygen By similarity
Metal bindingi626 – 6261Calcium 7 By similarity
Metal bindingi658 – 6581Calcium 1 By similarity
Metal bindingi661 – 6611Calcium 1 By 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
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. 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
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 subunit Reviewed predictionPRO_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.

Miscellaneous databases

EvolutionaryTraceiP17655.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 344300Calpain catalyticAdd
BLAST
Domaini572 – 60534EF-hand 1Add
BLAST
Domaini602 – 63736EF-hand 2Add
BLAST
Domaini667 – 70034EF-hand 3Add
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.
Contains 3 EF-hand domains.

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.

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. VSP_043027Add
BLAST
Alternative sequencei79 – 791T → M in isoform 2. VSP_043028

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 742IE → MR in AAA35645. 1 Publication
Sequence conflicti256 – 2561Q → K in AAF99682. 1 Publication
Sequence conflicti300 – 3001N → S in AAF99682. 1 Publication
Sequence conflicti534 – 5341F → V in AAA35645. 1 Publication
Sequence conflicti534 – 5341F → V in AAF99682. 1 Publication

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

« 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: September 3, 2014
This is version 181 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

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