Sequence of CAN1_HUMAN
EC Number:3.4.22.52
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
broad endopeptidase specificity
General information:
Sequence
0 MSEEIITPVY CTGVSAQVQK QRARELGLGR HENAIKYLGQ DYEQLRVRCL QSGTLFRDEA
60 FPPVPQSLGY KDLGPNSSKT YGIKWKRPTE LLSNPQFIVD GATRTDICQG ALGDCWLLAA
120 IASLTLNDTL LHRVVPHGQS FQNGYAGIFH FQLWQFGEWV DVVVDDLLPI KDGKLVFVHS
180 AEGNEFWSAL LEKAYAKVNG SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYQIILK
240 ALERGSLLGC SIDISSVLDM EAITFKKLVK GHAYSVTGAK QVNYRGQVVS LIRMRNPWGE
300 VEWTGAWSDS SSEWNNVDPY ERDQLRVKME DGEFWMSFRD FMREFTRLEI CNLTPDALKS
360 RTIRKWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LDETDDPDDY GDRESGCSFV
420 LALMQKHRRR ERRFGRDMET IGFAVYEVPP ELVGQPAVHL KRDFFLANAS RARSEQFINL
480 REVSTRFRLP PGEYVVVPST FEPNKEGDFV LRFFSEKSAG TVELDDQIQA NLPDEQVLSE
540 EEIDENFKAL FRQLAGEDME ISVKELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD
600 GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK LNKKLYELII
660 TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV TFDLFKWLQL TMFA
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
355119
Aoki K.,Imajoh S.,Ohno S.,Emori Y.,Koike M.,Kosaki G.,Suzuki K.
Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence.
FEBS Lett.
205
313-317
1986
355120
Sorimachi H.,Ohmi S.,Emori Y.,Kawasaki H.,Saido T.C.,Ohno S.,Minami Y.,Suzuki K.
A novel member of the calcium-dependent cysteine protease family.
Biol. Chem. Hoppe-Seyler
371
171-176
1990
355123
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
355124
Melloni E.,Michetti M.,Salamino F.,Minafra R.,Pontremoli S.
Modulation of the calpain autoproteolysis by calpastatin and phospholipids.
Biochem. Biophys. Res. Commun.
229
193-197
1996
355125
Michetti M.,Salamino F.,Tedesco I.,Averna M.,Minafra R.,Melloni E.,Pontremoli S.
Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization.
FEBS Lett.
392
11-15
1996
355126
Michetti M.,Salamino F.,Minafra R.,Melloni E.,Pontremoli S.
Calcium-binding properties of human erythrocyte calpain.
Biochem. J.
325
721-726
1997
355127
Gauci S.,Helbig A.O.,Slijper M.,Krijgsveld J.,Heck A.J.,Mohammed S.
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem.
81
4493-4501
2009
355128
Gafni J.,Cong X.,Chen S.F.,Gibson B.W.,Ellerby L.M.
Calpain-1 cleaves and activates caspase-7.
J. Biol. Chem.
284
25441-25449
2009
355129
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
355130
Hsu C.Y.,Henry J.,Raymond A.A.,Mechin M.C.,Pendaries V.,Nassar D.,Hansmann B.,Balica S.,Burlet-Schiltz O.,Schmitt A.M.,Takahara H.,Paul C.,Serre G.,Simon M.
Deimination of human filaggrin-2 promotes its proteolysis by calpain 1.
J. Biol. Chem.
286
23222-23233
2011
355131
Bienvenut W.V.,Sumpton D.,Martinez A.,Lilla S.,Espagne C.,Meinnel T.,Giglione C.
Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
Mol. Cell. Proteomics
11
M111.015131-M111.015131
2012
355132
Van Damme P.,Lasa M.,Polevoda B.,Gazquez C.,Elosegui-Artola A.,Kim D.S.,De Juan-Pardo E.,Demeyer K.,Hole K.,Larrea E.,Timmerman E.,Prieto J.,Arnesen T.,Sherman F.,Gevaert K.,Aldabe R.
N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
Proc. Natl. Acad. Sci. U.S.A.
109
12449-12454
2012
355133
Ono Y.,Iemura S.,Novak S.M.,Doi N.,Kitamura F.,Natsume T.,Gregorio C.C.,Sorimachi H.
PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.
J. Mol. Biol.
425
2955-2972
2013
355134
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
355135
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
355136
Gan-Or Z.,Bouslam N.,Birouk N.,Lissouba A.,Chambers D.B.,Veriepe J.,Androschuck A.,Laurent S.B.,Rochefort D.,Spiegelman D.,Dionne-Laporte A.,Szuto A.,Liao M.,Figlewicz D.A.,Bouhouche A.,Benomar A.,Yahyaoui M.,Ouazzani R.,Yoon G.,Dupre N.,Suchowersky O.,Bolduc F.V.,Parker J.A.,Dion P.A.,Drapeau P.,Rouleau G.A.,Bencheikh B.O.
Mutations in CAPN1 cause autosomal-recessive hereditary spastic paraplegia.
Am. J. Hum. Genet.
98
1038-1046
2016
355137
Li Q.,Hanzlik R.P.,Weaver R.F.,Schonbrunn E.
Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core.
Biochemistry
45
701-708
2006
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