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Protein Page:
CAPN1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CAPN1 Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Forms a heterodimer with a small (regulatory) subunit (CAPNS1). Ubiquitous. Activated by micromolar concentrations of calcium and inhibited by calpastatin. Belongs to the peptidase C2 family. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.22.52; Protease; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 11q13
Cellular Component: cytoplasm; cytosol; focal adhesion; lysosome; membrane; mitochondrion; plasma membrane
Molecular Function: calcium ion binding; calcium-dependent cysteine-type endopeptidase activity; cytoskeletal protein binding; protein binding
Biological Process: extracellular matrix disassembly; mammary gland involution; positive regulation of cell proliferation; protein autoprocessing; proteolysis; receptor catabolic process; regulation of macroautophagy
Reference #:  P07384 (UniProtKB)
Alt. Names/Synonyms: Calcium-activated neutral proteinase 1; Calpain 1; calpain 1, (mu/I) large subunit; Calpain mu-type; calpain, large polypeptide L1; Calpain-1; Calpain-1 catalytic subunit; Calpain-1 large subunit; CAN1; CANP; CANP 1; CANP1; CANPL1; CAPN1; Cell proliferation-inducing gene 30 protein; cell proliferation-inducing protein 30; Micromolar-calpain; muCANP; muCL
Gene Symbols: CAPN1
Molecular weight: 81,890 Da
Basal Isoelectric point: 5.49  Predict pI for various phosphorylation states
CST Pathways:  Alzheimer's Disease  |  Apoptosis Regulation  |  T Cell Receptor Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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CAPN1

Protein Structure Not Found.
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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S2‑p ______MsEEIITPV
0 1 K20‑ub GVSAQVQkQRARELG
0 1 K36‑ub GRHENAIkYLGQDyE
0 2 Y42‑p IkYLGQDyEQLRVRC
0 1 K71‑ub VPQSLGYkDLGPNSS
0 2 K79‑ub DLGPNSSkTYGIkWK
0 2 K84‑ac SSkTYGIkWKRPTEL
0 1 K84‑ub SSkTYGIkWKRPTEL
0 1 S93‑p KRPTELLsNPQFIVD
0 1 K193‑ub FWSALLEkAYAKVNG
0 1 K229‑m3 TEWYELRkAPsDLyQ
0 1 K229‑ub TEWYELRkAPsDLyQ
0 1 S232‑p YELRkAPsDLyQIIL
0 1 Y235‑p RkAPsDLyQIILKAL
0 1 S251‑p RGSLLGCsIDISSVL
0 1 K266 DMEAITFKKLVKGHA
0 1 K280‑ub AYSVTGAkQVNYRGQ
0 1 N316 DSSSEWNNVDPYERD
0 1 K328‑ub ERDQLRVkMEDGEFW
0 1 R347 DFMREFTRLEICNLt
0 3 T354‑p RLEICNLtPDALkSR
0 5 K359‑ub NLtPDALkSRTIRkW
0 3 K365‑ub LkSRTIRkWNTTLyE
0 4 Y371‑p RkWNTTLyEGtWRRG
0 7 T374‑p NTTLyEGtWRRGsTA
1 2 S379‑p EGtWRRGsTAGGCRN
0 9 Y387‑p TAGGCRNyPATFWVN
0 1 T390 GCRNyPATFWVNPQF
0 3 K398‑ub FWVNPQFkIRLDEtD
0 1 T404‑p FkIRLDEtDDPDDyG
0 5 Y410‑p EtDDPDDyGDRESGC
0 1 K461‑ub GQPAVHLkRDFFLAN
0 2 S470‑p DFFLANAsRARsEQF
0 3 S474‑p ANAsRARsEQFINLR
0 1 Y494‑p FRLPPGEyVVVPSTF
0 1 K505‑ub PSTFEPNkEGDFVLR
0 1 S539‑p LPDEQVLsEEEIDEN
0 1 K564‑ub EDMEISVkELRTILN
0 2 S622‑p NRIRNYLsIFRKFDL
0 1 K626 NYLsIFRKFDLDKSG
0 1 S636‑p LDKSGSMsAYEMRMA
  mouse

 
T2 ______MTEELITPV
K20 GVSAQVQKKRDKELG
K36 GRHENAIKYLGQDYE
Y42 IKYLGQDYETLRARC
K71 VSHSLGFKELGPHSS
K79 ELGPHSSKTYGIKWK
K84 SSKTYGIKWKRPTEL
K84 SSKTYGIKWKRPTEL
S93 KRPTELMSNPQFIVD
K193 FWSALLEKAYAKVNG
K229 TEWYDLQKAPSDLYQ
K229 TEWYDLQKAPSDLYQ
S232 YDLQKAPSDLYQIIL
Y235 QKAPSDLYQIILKAL
S251 RGSLLGCSINISDIR
K266‑ub DLEAITFkNLVRGHA
K280 AYSVTGAKQVTYQGQ
K316‑ac DSSYEWNkVDPYERE
K328 EREQLRVKMEDGEFW
K347‑ub DFIREFTkLEICNLt
T354‑p kLEICNLtPDALkSR
K359‑ub NLtPDALkSRTLRNW
N365 LkSRTLRNWNTTFYE
Y371 RNWNTTFYEGTWRRG
T374 NTTFYEGTWRRGsTA
S379‑p EGTWRRGsTAGGCRN
Y387‑p TAGGCRNyPAtFWVN
T390‑p GCRNyPAtFWVNPQF
K398‑ub FWVNPQFkIRLEEVD
V404 FkIRLEEVDDADDYD
Y410 EVDDADDYDNRESGC
K460 AGQPVHLKRDFFLAN
S469‑p DFFLANAsRAQSEHF
S473 ANAsRAQSEHFINLR
Y493 IRLPPGEYIVVPSTF
K504 PSTFEPNKEGDFLLR
S538 LPDEKVLSEEEIDDN
K563 DDMEISVKELQTILN
T621‑p NRIRNYLtIFRKFDL
K625 NYLtIFRKFDLDKSG
S635 LDKSGSMSAYEMRMA
  rat

 
A2 ______MAEELITPV
K20 GVSAQVQKQRDKELG
K36 GRHENAIKYLGQDYE
Y42 IKYLGQDYENLRARC
K71 VSHSLGFKELGPNSS
K79 ELGPNSSKTYGIkWK
K84‑ac SSKTYGIkWKRPTEL
K84 SSKTYGIKWKRPTEL
S93 KRPTELLSNPQFIVD
K193 FWSALLEKAYAKVNG
K229 TEWYDLQKAPSDLYQ
K229 TEWYDLQKAPSDLYQ
S232 YDLQKAPSDLYQIIL
Y235 QKAPSDLYQIILKAL
S251 RGSLLGCSINISDIR
K266 DLEAITFKNLVRGHA
K280 AYSVTDAKQVTYQGQ
K316 DNSYEWNKVDPYERE
K328 EREQLRVKMEDGEFW
K347 DFIREFTKLEICNLT
T354 KLEICNLTPDALKSR
K359 NLTPDALKSRTLRNW
N365 LKSRTLRNWNTTFYE
Y371 RNWNTTFYEGTWRRG
T374 NTTFYEGTWRRGSTA
S379 EGTWRRGSTAGGCRN
Y387 TAGGCRNYPATFWVN
T390 GCRNYPATFWVNPQF
K398 FWVNPQFKIRLEEVD
V404 FKIRLEEVDDADDYD
Y410 EVDDADDYDSRESGC
K460 AGQPVHLKRDFFLAN
S469 DFFLANASRAQSEHF
S473 ANASRAQSEHFINLR
Y493 IRLPPGEYIVVPSTF
K504 PSTFEPNKEGDFLLR
S538 LPDEKVLSEEEIDDN
K563 DDMEISVKELQTILN
T621 NRIRNYLTIFRkFDL
K625‑ac NYLTIFRkFDLDKSG
S635 LDKSGSMSAYEMRMA
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