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Reviewed, UniProtKB/Swiss-Prot P04632 (CPNS1_HUMAN)

Last modified January 19, 2010. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Calpain small subunit 1
      Short name=CSS1
Alternative name(s):
    Calcium-dependent protease small subunit 1
    Calcium-dependent protease small subunit
      Short name=CDPS
    Calpain regulatory subunit
    Calcium-activated neutral proteinase small subunit
      Short name=CANP small subunit
Gene names
Name: CAPNS1
Synonyms: CAPN4, CAPNS
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.

Cofactor

Calcium By similarity.

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.

Miscellaneous

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.

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Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandCalcium
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processpositive regulation of cell proliferation

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-dependent cysteine-type endopeptidase activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAPN2P176551EBI-711828,EBI-1028956

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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

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.10
Modified residue1791N6-acetyllysine Ref.11

Natural variations

Natural variant2241M → V: dbSNP rs17878750. Ref.5
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

1 ........................... 268
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P04632-1 [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

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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: 3016651] [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: 3024120] [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: 14702039] [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: 15057824] [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: 15489334] [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, MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, MASS SPECTROMETRY.
[12]"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: 10639123] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

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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.
IPIIPI00025084.
PIRCIHUL. A26107.
RefSeqNP_001003962.1.
NP_001740.1.
UniGeneHs.515371

3D structure databases

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

Protein-protein interaction databases

IntActP04632. 11 interactions.
STRINGP04632.

PTM databases

PhosphoSiteP04632.

2-D gel databases

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

Proteomic databases

PRIDEP04632.

Genome annotation databases

EnsemblENST00000246533; ENSP00000246533; ENSG00000126247; Homo sapiens. [Genome view]
ENST00000457326; ENSP00000400882; ENSG00000126247; Homo sapiens. [Genome view]
GeneID826.
KEGGhsa:826.
UCSCuc002odj.1. human.

Organism-specific databases

CTD826.
GeneCardsGC19P041322.
H-InvDBHIX0015056.
HGNCHGNC:1481. CAPNS1.
HPAHPA006872.
MIM114170. gene.
PharmGKBPA26067.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05540.
HOGENOMHBG747897.
HOVERGENP04632.
InParanoidP04632.
OMARRYSDEG.
OrthoDBEOG9MGVTV.
PhylomeDBP04632.

Gene expression databases

ArrayExpressP04632.
BgeeP04632.
CleanExHS_CAPNS1.
GenevestigatorP04632.
GermOnlineENSG00000126247. Homo sapiens.

Family and domain databases

InterProIPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio3398.
SOURCESearch...

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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: January 19, 2010
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 19

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents