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UniProtKB - P04632 (CPNS1_HUMAN)

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Protein

Calpain small subunit 1

Gene

CAPNS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi109Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi112Calcium 1By similarity1
Metal bindingi114Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi119Calcium 1By similarity1
Metal bindingi137Calcium 4By similarity1
Metal bindingi152Calcium 2By similarity1
Metal bindingi154Calcium 2By similarity1
Metal bindingi156Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi158Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi163Calcium 2By similarity1
Metal bindingi182Calcium 3By similarity1
Metal bindingi184Calcium 3By similarity1
Metal bindingi186Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi188Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi193Calcium 3By similarity1
Metal bindingi225Calcium 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi108 – 1191PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi152 – 1632PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi182 – 1933PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cornification Source: Reactome
  • positive regulation of cell proliferation Source: ProtInc
  • regulation of macroautophagy Source: ParkinsonsUK-UCL
View the complete GO annotation on QuickGO ...

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.53 2681
3.4.22.B24 2681
ReactomeiR-HSA-1474228 Degradation of the extracellular matrix
R-HSA-6809371 Formation of the cornified envelope
R-HSA-8862803 Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000126247.10
HGNCiHGNC:1481 CAPNS1
MIMi114170 gene
neXtProtiNX_P04632

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi826
OpenTargetsiENSG00000126247
PharmGKBiPA26067

Chemistry databases

ChEMBLiCHEMBL2111357
DrugBankiDB02570 PD150606

Polymorphism and mutation databases

BioMutaiCAPNS1
DMDMi115612

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000737131 – 268Calpain small subunit 1Add BLAST268

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei6PhosphoserineCombined sources1
Modified residuei179N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP04632
MaxQBiP04632
PaxDbiP04632
PeptideAtlasiP04632
PRIDEiP04632
ProteomicsDBi51727
TopDownProteomicsiP04632

2D gel databases

OGPiP04632
REPRODUCTION-2DPAGEiIPI00025084
SWISS-2DPAGEiP04632

PTM databases

iPTMnetiP04632
PhosphoSitePlusiP04632
SwissPalmiP04632

Expressioni

Gene expression databases

BgeeiENSG00000126247
CleanExiHS_CAPNS1
ExpressionAtlasiP04632 baseline and differential
GenevisibleiP04632 HS

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

Show more details

Protein-protein interaction databases

BioGridi107276, 61 interactors
CORUMiP04632
IntActiP04632, 27 interactors
MINTiP04632
STRINGi9606.ENSP00000246533

Chemistry databases

BindingDBiP04632

Structurei

Secondary structure

1268
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi97 – 109Combined sources13
Helixi110 – 112Combined sources3
Helixi117 – 130Combined sources14
Helixi141 – 151Combined sources11
Beta strandi156 – 159Combined sources4
Helixi161 – 181Combined sources21
Beta strandi187 – 190Combined sources4
Turni191 – 193Combined sources3
Helixi194 – 200Combined sources7
Helixi207 – 217Combined sources11
Beta strandi222 – 224Combined sources3
Helixi226 – 246Combined sources21
Turni247 – 249Combined sources3
Beta strandi252 – 256Combined sources5
Helixi258 – 265Combined sources8

3D structure databases

ProteinModelPortaliP04632
SMRiP04632
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04632

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 125EF-hand 1; atypicalPROSITE-ProRule annotationAdd BLAST35
Domaini139 – 172EF-hand 2PROSITE-ProRule annotationAdd BLAST34
Domaini169 – 204EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini205 – 233EF-hand 4PROSITE-ProRule annotationAdd BLAST29
Domaini234 – 268EF-hand 5PROSITE-ProRule annotationAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 66Gly-rich (hydrophobic)Add BLAST66
Compositional biasi10 – 26Poly-GlyAdd BLAST17
Compositional biasi35 – 56Poly-GlyAdd BLAST22
Compositional biasi78 – 83Poly-Pro6

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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0037 Eukaryota
ENOG410YKQK LUCA
GeneTreeiENSGT00620000087734
HOGENOMiHOG000063658
HOVERGENiHBG004492
InParanoidiP04632
KOiK08583
PhylomeDBiP04632
TreeFamiTF314682

Family and domain databases

InterProiView protein in InterPro
IPR029642 CAPN4
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
PANTHERiPTHR44408:SF3 PTHR44408:SF3, 1 hit
PfamiView protein in Pfam
PF13202 EF-hand_5, 1 hit
PF13833 EF-hand_8, 1 hit
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 3 hits

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)DescriptionActionsGraphical viewLength
Sequence conflicti5N → D in AAH64998 (PubMed:15489334).Curated1
Sequence conflicti27N → G in AAH64998 (PubMed:15489334).Curated1
Sequence conflicti34S → G in AAH64998 (PubMed:15489334).Curated1
Sequence conflicti261 – 268WLQLTMYS → VRTPILGYGCLGGPHPSALH TSSELQSPSSYFASRPWVRA KGLVLLGFPVLTLHPPLPSG CS in AAH11903 (PubMed:15489334).Curated8
Sequence conflicti267Y → F in AAH21933 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021089224M → V1 PublicationCorresponds to variant dbSNP:rs17878750Ensembl.1

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.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCPNS1_HUMAN
AccessioniPrimary (citable) accession number: P04632
Secondary accession number(s): A8K0P1, Q8WTX3, Q96EW0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 18, 2018
This is version 202 of the entry and version 1 of the sequence. See 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

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