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Protein

Calpain small subunit 1

Gene

CAPNS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 oxygenBy similarity
Metal bindingi112 – 1121Calcium 1By similarity
Metal bindingi114 – 1141Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi119 – 1191Calcium 1By similarity
Metal bindingi137 – 1371Calcium 4By similarity
Metal bindingi152 – 1521Calcium 2By similarity
Metal bindingi154 – 1541Calcium 2By similarity
Metal bindingi156 – 1561Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi158 – 1581Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi163 – 1631Calcium 2By similarity
Metal bindingi182 – 1821Calcium 3By similarity
Metal bindingi184 – 1841Calcium 3By similarity
Metal bindingi186 – 1861Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi188 – 1881Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi193 – 1931Calcium 3By similarity
Metal bindingi225 – 2251Calcium 4By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi108 – 119121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi152 – 163122PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi182 – 193123PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium-dependent cysteine-type endopeptidase activity Source: GO_Central
  2. calcium ion binding Source: InterPro

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: GO_Central
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.53. 2681.
3.4.22.B24. 2681.
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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1481. CAPNS1.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Cell membrane By similarity

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

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. cytosol Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProtKB
  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.

Polymorphism and mutation databases

BioMutaiCAPNS1.
DMDMi115612.

PTM / Processingi

Molecule processing

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

BgeeiP04632.
CleanExiHS_CAPNS1.
ExpressionAtlasiP04632. baseline and differential.
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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-711828,EBI-741181
CAPN2P176553EBI-711828,EBI-1028956
RASA1P209363EBI-711828,EBI-1026476

Protein-protein interaction databases

BioGridi107276. 59 interactions.
IntActiP04632. 24 interactions.
MINTiMINT-5000880.
STRINGi9606.ENSP00000246533.

Structurei

Secondary structure

1
268
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi97 – 10913Combined sources
Helixi110 – 1123Combined sources
Helixi117 – 13014Combined sources
Helixi141 – 15111Combined sources
Beta strandi156 – 1594Combined sources
Helixi161 – 18121Combined sources
Beta strandi187 – 1904Combined sources
Turni191 – 1933Combined sources
Helixi194 – 2007Combined sources
Helixi207 – 21711Combined sources
Beta strandi222 – 2243Combined sources
Helixi226 – 24621Combined sources
Turni247 – 2493Combined sources
Beta strandi252 – 2565Combined sources
Helixi258 – 2658Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KFUX-ray2.50S85-268[»]
1KFXX-ray3.15S85-268[»]
4PHJX-ray1.60A/B96-268[»]
4PHKX-ray2.05A/B96-268[»]
4PHMX-ray2.03A/B96-268[»]
SMRiP04632. Positions 96-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04632.

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 6666Gly-rich (hydrophobic)Add
BLAST
Compositional biasi10 – 2617Poly-GlyAdd
BLAST
Compositional biasi35 – 5622Poly-GlyAdd
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.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG277774.
GeneTreeiENSGT00620000087734.
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

        10         20         30         40         50
MFLVNSFLKG GGGGGGGGGG LGGGLGNVLG GLISGAGGGG GGGGGGGGGG
60 70 80 90 100
GGGGGGTAMR ILGGVISAIS EAAAQYNPEP PPPRTHYSNI EANESEEVRQ
110 120 130 140 150
FRRLFAQLAG DDMEVSATEL MNILNKVVTR HPDLKTDGFG IDTCRSMVAV
160 170 180 190 200
MDSDTTGKLG FEEFKYLWNN IKRWQAIYKQ FDTDRSGTIC SSELPGAFEA
210 220 230 240 250
AGFHLNEHLY NMIIRRYSDE SGNMDFDNFI SCLVRLDAMF RAFKSLDKDG
260
TGQIQVNIQE WLQLTMYS
Length:268
Mass (Da):28,316
Last modified:August 13, 1987 - v1
Checksum:i17B87A8E47A90632
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51N → D in AAH64998 (PubMed:15489334).Curated
Sequence conflicti27 – 271N → G in AAH64998 (PubMed:15489334).Curated
Sequence conflicti34 – 341S → G in AAH64998 (PubMed:15489334).Curated
Sequence conflicti261 – 2688WLQLTMYS → VRTPILGYGCLGGPHPSALH TSSELQSPSSYFASRPWVRA KGLVLLGFPVLTLHPPLPSG CS in AAH11903 (PubMed:15489334).Curated
Sequence conflicti267 – 2671Y → F in AAH21933 (PubMed:15489334).Curated

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001003962.2.
NP_001289561.1. NM_001302632.1.
NP_001289562.1. NM_001302633.1.
NP_001740.1. NM_001749.3.
XP_005259352.1. XM_005259295.1.
XP_005259353.1. XM_005259296.1.
UniGeneiHs.515371.

Genome annotation databases

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

Polymorphism and mutation databases

BioMutaiCAPNS1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

CaBP

Calpain

Calpains homepage
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001003962.2.
NP_001289561.1. NM_001302632.1.
NP_001289562.1. NM_001302633.1.
NP_001740.1. NM_001749.3.
XP_005259352.1. XM_005259295.1.
XP_005259353.1. XM_005259296.1.
UniGeneiHs.515371.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KFUX-ray2.50S85-268[»]
1KFXX-ray3.15S85-268[»]
4PHJX-ray1.60A/B96-268[»]
4PHKX-ray2.05A/B96-268[»]
4PHMX-ray2.03A/B96-268[»]
SMRiP04632. Positions 96-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107276. 59 interactions.
IntActiP04632. 24 interactions.
MINTiMINT-5000880.
STRINGi9606.ENSP00000246533.

Chemistry

BindingDBiP04632.
ChEMBLiCHEMBL2111357.

PTM databases

PhosphoSiteiP04632.

Polymorphism and mutation databases

BioMutaiCAPNS1.
DMDMi115612.

2D gel databases

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

Proteomic databases

MaxQBiP04632.
PaxDbiP04632.
PRIDEiP04632.

Protocols and materials databases

DNASUi826.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi826.
GeneCardsiGC19P036630.
HGNCiHGNC:1481. CAPNS1.
HPAiHPA006872.
MIMi114170. gene.
neXtProtiNX_P04632.
PharmGKBiPA26067.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG277774.
GeneTreeiENSGT00620000087734.
HOGENOMiHOG000063658.
HOVERGENiHBG004492.
InParanoidiP04632.
KOiK08583.
OrthoDBiEOG7RV9FM.
PhylomeDBiP04632.
TreeFamiTF314682.

Enzyme and pathway databases

BRENDAi3.4.22.53. 2681.
3.4.22.B24. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSiCAPNS1. human.
EvolutionaryTraceiP04632.
GeneWikiiCAPNS1.
GenomeRNAii826.
NextBioi3398.
PROiP04632.
SOURCEiSearch...

Gene expression databases

BgeeiP04632.
CleanExiHS_CAPNS1.
ExpressionAtlasiP04632. baseline and differential.
GenevestigatoriP04632.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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: April 29, 2015
This is version 172 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.