P17655 (CAN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CAPN2
Synonyms:	CANPL2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	700 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Thiol protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blastocyst development Inferred from electronic annotation. Source: Compara myoblast fusion Inferred from electronic annotation. Source: Compara protein autoprocessing Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to hypoxia Inferred from electronic annotation. Source: Compara
Cellular_component	chromatin Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: Compara calcium-dependent cysteine-type endopeptidase activity Inferred from electronic annotation. Source: Compara cysteine-type peptidase activity Traceable author statement PubMed 2209092. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAPNS1	P04632	2	EBI-1028956,EBI-711828

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Propeptide

2 – 19

18

Anchors to the small subunit Potential

PRO_0000026487

Chain

20 – 700

681

Calpain-2 catalytic subunit

PRO_0000026488

Regions

Domain

45 – 344

300

Calpain catalytic

Domain

572 – 605

34

EF-hand 1

Domain

602 – 637

36

EF-hand 2

Domain

667 – 700

34

EF-hand 3

Calcium binding

585 – 596

12

1

Calcium binding

615 – 626

12

2

Region

345 – 514

170

Domain III

Region

515 – 529

15

Linker

Region

530 – 700

171

Domain IV

Sites

Active site

105

1

By similarity

Active site

262

1

By similarity

Active site

286

1

By similarity

Metal binding

89

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

91

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

96

1

Calcium 3 By similarity

Metal binding

175

1

Calcium 3 By similarity

Metal binding

229

1

Calcium 2 By similarity

Metal binding

230

1

Calcium 2 By similarity

Metal binding

292

1

Calcium 4 By similarity

Metal binding

299

1

Calcium 4 By similarity

Metal binding

323

1

Calcium 4; via carbonyl oxygen By similarity

Metal binding

542

1

Calcium 5; via carbonyl oxygen By similarity

Metal binding

545

1

Calcium 5 By similarity

Metal binding

547

1

Calcium 5; via carbonyl oxygen By similarity

Metal binding

552

1

Calcium 5 By similarity

Metal binding

585

1

Calcium 6 By similarity

Metal binding

587

1

Calcium 6 By similarity

Metal binding

589

1

Calcium 6; via carbonyl oxygen By similarity

Metal binding

591

1

Calcium 6; via carbonyl oxygen By similarity

Metal binding

596

1

Calcium 6 By similarity

Metal binding

615

1

Calcium 7 By similarity

Metal binding

617

1

Calcium 7 By similarity

Metal binding

619

1

Calcium 7; via carbonyl oxygen By similarity

Metal binding

621

1

Calcium 7; via carbonyl oxygen By similarity

Metal binding

626

1

Calcium 7 By similarity

Metal binding

658

1

Calcium 1 By similarity

Metal binding

661

1

Calcium 1 By similarity

Natural variations

Alternative sequence

1 – 78

78

Missing in isoform 2.

VSP_043027

Alternative sequence

79

1

T → M in isoform 2.

VSP_043028

Natural variant

22

1

D → E. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7 Ref.10
Corresponds to variant rs25655 [ dbSNP | Ensembl ].

VAR_014435

Natural variant

68

1

S → G. Ref.4 Ref.7
Corresponds to variant rs2230083 [ dbSNP | Ensembl ].

VAR_021404

Natural variant

476

1

K → R. Ref.4
Corresponds to variant rs9804140 [ dbSNP | Ensembl ].

VAR_021405

Natural variant

521

1

E → Q. Ref.4
Corresponds to variant rs28370127 [ dbSNP | Ensembl ].

VAR_021406

Natural variant

568

1

K → Q. Ref.4
Corresponds to variant rs17599 [ dbSNP | Ensembl ].

VAR_014436

Natural variant

677

1

K → Q. Ref.4
Corresponds to variant rs2230082 [ dbSNP | Ensembl ].

VAR_021407

Experimental info

Sequence conflict

73 – 74

2

IE → MR in AAA35645. Ref.1

Sequence conflict

256

1

Q → K in AAF99682. Ref.2

Sequence conflict

300

1

N → S in AAF99682. Ref.2

Sequence conflict

534

1

F → V in AAA35645. Ref.1

Sequence conflict

534

1

F → V in AAF99682. Ref.2

Secondary structure

1

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700

Helix Strand Turn

Details...

Helix

4 – 16

13

Turn

17 – 19

3

Helix

27 – 29

3

Helix

32 – 42

11

Beta strand

49 – 51

3

Helix

55 – 58

4

Beta strand

60 – 68

9

Beta strand

74 – 76

3

Helix

78 – 81

4

Beta strand

82 – 84

3

Helix

94 – 96

3

Beta strand

97 – 99

3

Helix

105 – 115

11

Helix

118 – 124

7

Beta strand

131 – 134

4

Beta strand

136 – 144

9

Beta strand

146 – 155

10

Beta strand

158 – 161

4

Beta strand

164 – 167

4

Beta strand

169 – 175

7

Helix

177 – 189

13

Beta strand

190 – 192

3

Helix

193 – 195

3

Beta strand

196 – 199

4

Turn

204 – 206

3

Helix

207 – 209

3

Beta strand

212 – 216

5

Helix

224 – 233

10

Beta strand

237 – 241

5

Helix

247 – 249

3

Beta strand

259 – 261

3

Beta strand

264 – 274

11

Beta strand

277 – 285

9

Beta strand

294 – 297

4

Beta strand

299 – 301

3

Helix

302 – 306

5

Helix

309 – 315

7

Beta strand

321 – 327

7

Helix

328 – 334

7

Beta strand

336 – 341

6

Helix

344 – 346

3

Beta strand

347 – 349

3

Beta strand

363 – 365

3

Turn

367 – 370

4

Turn

378 – 380

3

Helix

381 – 383

3

Beta strand

388 – 390

3

Beta strand

400 – 402

3

Beta strand

406 – 413

8

Beta strand

420 – 425

6

Beta strand

429 – 435

7

Turn

442 – 444

3

Helix

450 – 455

6

Beta strand

459 – 461

3

Beta strand

466 – 471

6

Beta strand

474 – 476

3

Beta strand

479 – 492

14

Beta strand

495 – 505

11

Beta strand

507 – 509

3

Beta strand

527 – 530

4

Helix

533 – 541

9

Beta strand

542 – 546

5

Helix

550 – 560

11

Turn

561 – 564

4

Helix

574 – 582

9

Beta strand

586 – 588

3

Beta strand

590 – 592

3

Helix

595 – 612

18

Beta strand

622 – 624

3

Helix

627 – 630

4

Turn

631 – 635

5

Helix

640 – 650

11

Beta strand

655 – 657

3

Helix

659 – 679

21

Beta strand

687 – 690

4

Helix

691 – 698

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 6. Checksum: 8CF8294351A024E3	FASTA	700	79,995
	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
	Isoform 2 [UniParc]. Checksum: 60ED3A3498F6DD5D	FASTA	622	71,476
	10 20 30 40 50 60 MEICADPQFI IGGATRTDIC QGALGDCWLL AAIASLTLNE EILARVVPLN QSFQENYAGI 70 80 90 100 110 120 FHFQFWQYGE WVEVVVDDRL PTKDGELLFV HSAEGSEFWS ALLEKAYAKI NGCYEALSGG 130 140 150 160 170 180 ATTEGFEDFT GGIAEWYELK KPPPNLFKII QKALQKGSLL GCSIDITSAA DSEAITFQKL 190 200 210 220 230 240 VKGHAYSVTG AEEVESNGSL QKLIRIRNPW GEVEWTGRWN DNCPSWNTID PEERERLTRR 250 260 270 280 290 300 HEDGEFWMSF SDFLRHYSRL EICNLTPDTL TSDTYKKWKL TKMDGNWRRG STAGGCRNYP 310 320 330 340 350 360 NTFWMNPQYL IKLEEEDEDE EDGESGCTFL VGLIQKHRRR QRKMGEDMHT IGFGIYEVPE 370 380 390 400 410 420 ELSGQTNIHL SKNFFLTNRA RERSDTFINL REVLNRFKLP PGEYILVPST FEPNKDGDFC 430 440 450 460 470 480 IRVFSEKKAD YQAVDDEIEA NLEEFDISED DIDDGFRRLF AQLAGEDAEI SAFELQTILR 490 500 510 520 530 540 RVLAKRQDIK SDGFSIETCK IMVDMLDSDG SGKLGLKEFY ILWTKIQKYQ KIYREIDVDR 550 560 570 580 590 600 SGTMNSYEMR KALEEAGFKM PCQLHQVIVA RFADDQLIID FDNFVRCLVR LETLFKIFKQ 610 620 LDPENTGTIE LDLISWLCFS VL

References

	« Hide 'large scale' referencesShow '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. , 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]	"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).
[10]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00289758.
IPI00641266.

PIR

CIHUH2. S10590.

RefSeq

NP_001139540.1. NM_001146068.1.
NP_001739.2. NM_001748.4.

UniGene

Hs.350899.

3D structure databases

PDBe
RCSB PDB
PDBj

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	26-346	[»]

ProteinModelPortal

P17655.

SMR

P17655. Positions 2-700.

ModBase

Search...

Protein-protein interaction databases

IntAct

P17655. 1 interaction.

MINT

MINT-120195.

STRING

9606.ENSP00000295006.

Protein family/group databases

MEROPS

C02.002.

PTM databases

PhosphoSite

P17655.

Polymorphism databases

DMDM

60416356.

Proteomic databases

PaxDb

P17655.

PeptideAtlas

P17655.

PRIDE

P17655.

Protocols and materials databases

DNASU

824.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295006; ENSP00000295006; ENSG00000162909.
ENST00000433674; ENSP00000413158; ENSG00000162909.

GeneID

824.

KEGG

hsa:824.

UCSC

uc001hob.4. human.
uc010puy.2. human.

Organism-specific databases

CTD

824.

GeneCards

GC01P223890.

HGNC

HGNC:1479. CAPN2.

HPA

HPA024470.

MIM

114230. gene.

neXtProt

NX_P17655.

PharmGKB

PA26060.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG327523.

HOVERGEN

HBG012645.

InParanoid

P17655.

KO

K03853.

OrthoDB

EOG4RR6GS.

Enzyme and pathway databases

BRENDA

3.4.22.53. 2681.

Gene expression databases

ArrayExpress

P17655.

Bgee

P17655.

CleanEx

HS_CAPN2.

Genevestigator

P17655.

GermOnline

ENSG00000162909. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]

Pfam

PF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]

PRINTS

PR00704. CALPAIN.

SMART

SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]

SUPFAM

SSF49758. Peptidase_C2. 1 hit.

PROSITE

PS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P17655.

ChEMBL

CHEMBL2382.

EvolutionaryTrace

P17655.

GenomeRNAi

824.

NextBio

3374.

SOURCE

Search...

Entry information

Entry name

CAN2_HUMAN

Accession

Primary (citable) accession number: P17655
Secondary accession number(s): A6NDG7 , B7ZA96, E7ES58, Q16738, Q6PJT3, Q8WU26, Q9HBB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 11, 2011
Last modified:	May 29, 2013
This is version 168 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.