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P04632

- CPNS1_HUMAN

UniProt

P04632 - CPNS1_HUMAN

Protein

Calpain small subunit 1

Gene

CAPNS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    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: RefGenome
    2. calcium ion binding Source: InterPro
    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

    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

    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 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

    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.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

    1
    268
    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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 165 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