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P04632 (CPNS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CAPNS1
Synonyms:CAPN4, CAPNS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

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

Domain

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 similarities

Contains 5 EF-hand domains.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268Calpain small subunit 1
PRO_0000073713

Regions

Domain91 – 12535EF-hand 1; atypical
Domain139 – 17234EF-hand 2
Domain169 – 20436EF-hand 3
Domain205 – 23329EF-hand 4
Domain234 – 26835EF-hand 5
Calcium binding108 – 119121 By similarity
Calcium binding152 – 163122 By similarity
Calcium binding182 – 193123 By similarity
Compositional bias1 – 6666Gly-rich (hydrophobic)
Compositional bias10 – 2617Poly-Gly
Compositional bias35 – 5622Poly-Gly
Compositional bias78 – 836Poly-Pro

Sites

Metal binding1091Calcium 1; via carbonyl oxygen By similarity
Metal binding1121Calcium 1 By similarity
Metal binding1141Calcium 1; via carbonyl oxygen By similarity
Metal binding1191Calcium 1 By similarity
Metal binding1371Calcium 4 By similarity
Metal binding1521Calcium 2 By similarity
Metal binding1541Calcium 2 By similarity
Metal binding1561Calcium 2; via carbonyl oxygen By similarity
Metal binding1581Calcium 2; via carbonyl oxygen By similarity
Metal binding1631Calcium 2 By similarity
Metal binding1821Calcium 3 By similarity
Metal binding1841Calcium 3 By similarity
Metal binding1861Calcium 3; via carbonyl oxygen By similarity
Metal binding1881Calcium 3; via carbonyl oxygen By similarity
Metal binding1931Calcium 3 By similarity
Metal binding2251Calcium 4 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.9
Modified residue1791N6-acetyllysine Ref.10

Natural variations

Natural variant2241M → V. Ref.5
Corresponds to variant rs17878750 [ dbSNP | Ensembl ].
VAR_021089

Experimental info

Sequence conflict51N → D in AAH64998. Ref.7
Sequence conflict271N → G in AAH64998. Ref.7
Sequence conflict341S → G in AAH64998. Ref.7
Sequence conflict261 – 2688WLQLTMYS → VRTPILGYGCLGGPHPSALH TSSELQSPSSYFASRPWVRA KGLVLLGFPVLTLHPPLPSG CS in AAH11903. Ref.7
Sequence conflict2671Y → F in AAH21933. Ref.7

Secondary structure

............................. 268
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04632 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 17B87A8E47A90632

FASTA26828,316
        10         20         30         40         50         60 
MFLVNSFLKG GGGGGGGGGG LGGGLGNVLG GLISGAGGGG GGGGGGGGGG GGGGGGTAMR 

        70         80         90        100        110        120 
ILGGVISAIS EAAAQYNPEP PPPRTHYSNI EANESEEVRQ FRRLFAQLAG DDMEVSATEL 

       130        140        150        160        170        180 
MNILNKVVTR HPDLKTDGFG IDTCRSMVAV MDSDTTGKLG FEEFKYLWNN IKRWQAIYKQ 

       190        200        210        220        230        240 
FDTDRSGTIC SSELPGAFEA AGFHLNEHLY NMIIRRYSDE SGNMDFDNFI SCLVRLDAMF 

       250        260 
RAFKSLDKDG TGQIQVNIQE WLQLTMYS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04106 mRNA. Translation: CAA27726.1.
M31511 expand/collapse EMBL AC list , 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.
CCDSCCDS12489.1.
PIRCIHUL. A26107.
RefSeqNP_001003962.1. NM_001003962.1.
NP_001740.1. NM_001749.2.
XP_005259352.1. XM_005259295.1.
XP_005259353.1. XM_005259296.1.
UniGeneHs.515371.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KFUX-ray2.50S85-268[»]
1KFXX-ray3.15S85-268[»]
ProteinModelPortalP04632.
SMRP04632. Positions 85-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107276. 49 interactions.
IntActP04632. 23 interactions.
MINTMINT-5000880.
STRING9606.ENSP00000246533.

Chemistry

BindingDBP04632.
ChEMBLCHEMBL2111357.

PTM databases

PhosphoSiteP04632.

Polymorphism databases

DMDM115612.

2D gel databases

OGPP04632.
REPRODUCTION-2DPAGEIPI00025084.
SWISS-2DPAGEP04632.

Proteomic databases

MaxQBP04632.
PaxDbP04632.
PRIDEP04632.

Protocols and materials databases

DNASU826.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246533; ENSP00000246533; ENSG00000126247.
ENST00000587718; ENSP00000468041; ENSG00000126247.
ENST00000588815; ENSP00000464849; ENSG00000126247.
GeneID826.
KEGGhsa:826.
UCSCuc002odi.1. human.

Organism-specific databases

CTD826.
GeneCardsGC19P036630.
HGNCHGNC:1481. CAPNS1.
HPAHPA006872.
MIM114170. gene.
neXtProtNX_P04632.
PharmGKBPA26067.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277774.
HOGENOMHOG000063658.
HOVERGENHBG004492.
InParanoidP04632.
KOK08583.
OrthoDBEOG7RV9FM.
PhylomeDBP04632.
TreeFamTF314682.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP04632.
BgeeP04632.
CleanExHS_CAPNS1.
GenevestigatorP04632.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAPNS1. human.
EvolutionaryTraceP04632.
GeneWikiCAPNS1.
GenomeRNAi826.
NextBio3398.
PROP04632.
SOURCESearch...

Entry information

Entry nameCPNS1_HUMAN
AccessionPrimary (citable) accession number: P04632
Secondary accession number(s): A8K0P1, Q8WTX3, Q96EW0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM