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P04632

- CPNS1_HUMAN

UniProt

P04632 - CPNS1_HUMAN

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Protein
Calpain small subunit 1
Gene
CAPNS1, CAPN4, CAPNS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091Calcium 1; via carbonyl oxygen By similarity
Metal bindingi112 – 1121Calcium 1 By similarity
Metal bindingi114 – 1141Calcium 1; via carbonyl oxygen By similarity
Metal bindingi119 – 1191Calcium 1 By similarity
Metal bindingi137 – 1371Calcium 4 By similarity
Metal bindingi152 – 1521Calcium 2 By similarity
Metal bindingi154 – 1541Calcium 2 By similarity
Metal bindingi156 – 1561Calcium 2; via carbonyl oxygen By similarity
Metal bindingi158 – 1581Calcium 2; via carbonyl oxygen By similarity
Metal bindingi163 – 1631Calcium 2 By similarity
Metal bindingi182 – 1821Calcium 3 By similarity
Metal bindingi184 – 1841Calcium 3 By similarity
Metal bindingi186 – 1861Calcium 3; via carbonyl oxygen By similarity
Metal bindingi188 – 1881Calcium 3; via carbonyl oxygen By similarity
Metal bindingi193 – 1931Calcium 3 By similarity
Metal bindingi225 – 2251Calcium 4 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi108 – 119121 By similarity
Add
BLAST
Calcium bindingi152 – 163122 By similarity
Add
BLAST
Calcium bindingi182 – 193123 By similarity
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. calcium-dependent cysteine-type endopeptidase activity Source: RefGenome
  3. protein binding Source: IntAct

GO - Biological processi

  1. extracellular matrix disassembly Source: Reactome
  2. extracellular matrix organization Source: Reactome
  3. positive regulation of cell proliferation Source: ProtInc
  4. proteolysis Source: RefGenome
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain small subunit 1
Short name:
CSS1
Alternative name(s):
Calcium-activated neutral proteinase small subunit
Short name:
CANP small subunit
Calcium-dependent protease small subunit
Short name:
CDPS
Calcium-dependent protease small subunit 1
Calpain regulatory subunit
Gene namesi
Name:CAPNS1
Synonyms:CAPN4, CAPNS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1481. CAPNS1.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity
Note: Translocates to the plasma membrane upon calcium binding By similarity.

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytosol Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: BHF-UCL
  5. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26067.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 268268Calpain small subunit 1
PRO_0000073713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei179 – 1791N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP04632.
PaxDbiP04632.
PRIDEiP04632.

2D gel databases

OGPiP04632.
REPRODUCTION-2DPAGEIPI00025084.
SWISS-2DPAGEP04632.

PTM databases

PhosphoSiteiP04632.

Expressioni

Gene expression databases

ArrayExpressiP04632.
BgeeiP04632.
CleanExiHS_CAPNS1.
GenevestigatoriP04632.

Organism-specific databases

HPAiHPA006872.

Interactioni

Subunit structurei

Homodimer or heterodimer of a large (catalytic) and a small (regulatory) subunit. In presence of calcium, the heterodimer dissociates By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
CAPN2P176553EBI-711828,EBI-1028956
RASA1P209363EBI-711828,EBI-1026476

Protein-protein interaction databases

BioGridi107276. 49 interactions.
IntActiP04632. 23 interactions.
MINTiMINT-5000880.
STRINGi9606.ENSP00000246533.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi96 – 10813
Turni109 – 1113
Helixi117 – 1248
Turni127 – 1293
Helixi141 – 15111
Beta strandi153 – 1575
Helixi162 – 18019
Beta strandi186 – 1894
Helixi191 – 1933
Helixi194 – 2007
Helixi207 – 21711
Turni220 – 2223
Helixi226 – 24621
Beta strandi252 – 2565
Helixi258 – 2669

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KFUX-ray2.50S85-268[»]
1KFXX-ray3.15S85-268[»]
ProteinModelPortaliP04632.
SMRiP04632. Positions 85-268.

Miscellaneous databases

EvolutionaryTraceiP04632.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 12535EF-hand 1; atypical
Add
BLAST
Domaini139 – 17234EF-hand 2
Add
BLAST
Domaini169 – 20436EF-hand 3
Add
BLAST
Domaini205 – 23329EF-hand 4
Add
BLAST
Domaini234 – 26835EF-hand 5
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 6666Gly-rich (hydrophobic)
Add
BLAST
Compositional biasi10 – 2617Poly-Gly
Add
BLAST
Compositional biasi35 – 5622Poly-Gly
Add
BLAST
Compositional biasi78 – 836Poly-Pro

Domaini

The contact of the 5th EF-hand domain from each monomer allows the formation of the homodimer and also appears to mediate the contact between the large catalytic subunit and small regulatory subunit for the formation of the heterodimer By similarity.
EF-hand domains are paired. EF-hand 1 is paired with EF-hand 2 and EF-hand 3 is paired with EF-hand 4. The fifth EF-hand domain, left unpaired, does not bind the calcium but is responsible of the dimerization by EF-embrace. The first four EF-hand domains bind calcium, however it is not sure if the binding of EF-hand 4 to calcium is physiologically relevant.

Sequence similaritiesi

Contains 5 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG277774.
HOGENOMiHOG000063658.
HOVERGENiHBG004492.
InParanoidiP04632.
KOiK08583.
OrthoDBiEOG7RV9FM.
PhylomeDBiP04632.
TreeFamiTF314682.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR029642. CAPN4.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PANTHERiPTHR10183:SF38. PTHR10183:SF38. 1 hit.
PfamiPF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04632-1 [UniParc]FASTAAdd to Basket

« Hide

MFLVNSFLKG GGGGGGGGGG LGGGLGNVLG GLISGAGGGG GGGGGGGGGG    50
GGGGGGTAMR ILGGVISAIS EAAAQYNPEP PPPRTHYSNI EANESEEVRQ 100
FRRLFAQLAG DDMEVSATEL MNILNKVVTR HPDLKTDGFG IDTCRSMVAV 150
MDSDTTGKLG FEEFKYLWNN IKRWQAIYKQ FDTDRSGTIC SSELPGAFEA 200
AGFHLNEHLY NMIIRRYSDE SGNMDFDNFI SCLVRLDAMF RAFKSLDKDG 250
TGQIQVNIQE WLQLTMYS 268
Length:268
Mass (Da):28,316
Last modified:August 13, 1987 - v1
Checksum:i17B87A8E47A90632
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241M → V.1 Publication
Corresponds to variant rs17878750 [ dbSNP | Ensembl ].
VAR_021089

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51N → D in AAH64998. 1 Publication
Sequence conflicti27 – 271N → G in AAH64998. 1 Publication
Sequence conflicti34 – 341S → G in AAH64998. 1 Publication
Sequence conflicti261 – 2688WLQLTMYS → VRTPILGYGCLGGPHPSALH TSSELQSPSSYFASRPWVRA KGLVLLGFPVLTLHPPLPSG CS in AAH11903. 1 Publication
Sequence conflicti267 – 2671Y → F in AAH21933. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04106 mRNA. Translation: CAA27726.1.
M31511
, M31502, M31503, M31504, M31505, M31506, M31507, M31508, M31509, M31510 Genomic DNA. Translation: AAA35646.1.
AK289606 mRNA. Translation: BAF82295.1.
BT009775 mRNA. Translation: AAP88777.1.
AY789642 Genomic DNA. Translation: AAV40829.1.
AD001527 Genomic DNA. Translation: AAB51183.1.
AC002984 Genomic DNA. Translation: AAB81546.1.
BC000592 mRNA. Translation: AAH00592.1.
BC007779 mRNA. Translation: AAH07779.1.
BC011903 mRNA. Translation: AAH11903.1.
BC017308 mRNA. Translation: AAH17308.1.
BC018931 mRNA. Translation: AAH18931.1.
BC021933 mRNA. Translation: AAH21933.1.
BC023643 mRNA. Translation: AAH23643.1.
BC064998 mRNA. Translation: AAH64998.1.
CCDSiCCDS12489.1.
PIRiA26107. CIHUL.
RefSeqiNP_001003962.1. NM_001003962.1.
NP_001740.1. NM_001749.2.
XP_005259352.1. XM_005259295.1.
XP_005259353.1. XM_005259296.1.
UniGeneiHs.515371.

Genome annotation databases

EnsembliENST00000246533; ENSP00000246533; ENSG00000126247.
ENST00000587718; ENSP00000468041; ENSG00000126247.
ENST00000588815; ENSP00000464849; ENSG00000126247.
GeneIDi826.
KEGGihsa:826.
UCSCiuc002odi.1. human.

Polymorphism databases

DMDMi115612.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

CaBP

Calpain

Calpains homepage
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04106 mRNA. Translation: CAA27726.1 .
M31511
, M31502 , M31503 , M31504 , M31505 , M31506 , M31507 , M31508 , M31509 , M31510 Genomic DNA. Translation: AAA35646.1 .
AK289606 mRNA. Translation: BAF82295.1 .
BT009775 mRNA. Translation: AAP88777.1 .
AY789642 Genomic DNA. Translation: AAV40829.1 .
AD001527 Genomic DNA. Translation: AAB51183.1 .
AC002984 Genomic DNA. Translation: AAB81546.1 .
BC000592 mRNA. Translation: AAH00592.1 .
BC007779 mRNA. Translation: AAH07779.1 .
BC011903 mRNA. Translation: AAH11903.1 .
BC017308 mRNA. Translation: AAH17308.1 .
BC018931 mRNA. Translation: AAH18931.1 .
BC021933 mRNA. Translation: AAH21933.1 .
BC023643 mRNA. Translation: AAH23643.1 .
BC064998 mRNA. Translation: AAH64998.1 .
CCDSi CCDS12489.1.
PIRi A26107. CIHUL.
RefSeqi NP_001003962.1. NM_001003962.1.
NP_001740.1. NM_001749.2.
XP_005259352.1. XM_005259295.1.
XP_005259353.1. XM_005259296.1.
UniGenei Hs.515371.

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 S 85-268 [» ]
1KFX X-ray 3.15 S 85-268 [» ]
ProteinModelPortali P04632.
SMRi P04632. Positions 85-268.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107276. 49 interactions.
IntActi P04632. 23 interactions.
MINTi MINT-5000880.
STRINGi 9606.ENSP00000246533.

Chemistry

BindingDBi P04632.
ChEMBLi CHEMBL2111357.

PTM databases

PhosphoSitei P04632.

Polymorphism databases

DMDMi 115612.

2D gel databases

OGPi P04632.
REPRODUCTION-2DPAGE IPI00025084.
SWISS-2DPAGE P04632.

Proteomic databases

MaxQBi P04632.
PaxDbi P04632.
PRIDEi P04632.

Protocols and materials databases

DNASUi 826.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000246533 ; ENSP00000246533 ; ENSG00000126247 .
ENST00000587718 ; ENSP00000468041 ; ENSG00000126247 .
ENST00000588815 ; ENSP00000464849 ; ENSG00000126247 .
GeneIDi 826.
KEGGi hsa:826.
UCSCi uc002odi.1. human.

Organism-specific databases

CTDi 826.
GeneCardsi GC19P036630.
HGNCi HGNC:1481. CAPNS1.
HPAi HPA006872.
MIMi 114170. gene.
neXtProti NX_P04632.
PharmGKBi PA26067.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG277774.
HOGENOMi HOG000063658.
HOVERGENi HBG004492.
InParanoidi P04632.
KOi K08583.
OrthoDBi EOG7RV9FM.
PhylomeDBi P04632.
TreeFami TF314682.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSi CAPNS1. human.
EvolutionaryTracei P04632.
GeneWikii CAPNS1.
GenomeRNAii 826.
NextBioi 3398.
PROi P04632.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04632.
Bgeei P04632.
CleanExi HS_CAPNS1.
Genevestigatori P04632.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR029642. CAPN4.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
PANTHERi PTHR10183:SF38. PTHR10183:SF38. 1 hit.
Pfami PF13405. EF-hand_6. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 3 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a cDNA coding for the small subunit of human calcium-dependent protease."
    Ohno S., Emori Y., Suzuki K.
    Nucleic Acids Res. 14:5559-5559(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Gene organization of the small subunit of human calcium-activated neutral protease."
    Miyake S., Emori Y., Suzuki K.
    Nucleic Acids Res. 14:8805-8817(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-224.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Lung, Muscle, Pancreas, Skin and Uterus.
  8. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-9; 61-84 AND 159-165, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 (2.7 ANGSTROMS).

Entry informationi

Entry nameiCPNS1_HUMAN
AccessioniPrimary (citable) accession number: P04632
Secondary accession number(s): A8K0P1, Q8WTX3, Q96EW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 3, 2014
This is version 164 of the entry and version 1 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 19
    Human chromosome 19: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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