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P07384

- CAN1_HUMAN

UniProt

P07384 - CAN1_HUMAN

Protein

Calpain-1 catalytic subunit

Gene

CAPN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

    Catalytic activityi

    Broad endopeptidase specificity.

    Cofactori

    Binds 4 calcium ions.

    Enzyme regulationi

    Activated by micromolar concentrations of calcium and inhibited by calpastatin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei15 – 162Cleavage; for 78 kDa form
    Sitei27 – 282Cleavage; for 75 kDa form
    Active sitei115 – 1151By similarity
    Active sitei272 – 2721By similarity
    Active sitei296 – 2961By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi99 – 10681
    Calcium bindingi302 – 333322Add
    BLAST
    Calcium bindingi598 – 609123Add
    BLAST
    Calcium bindingi628 – 639124Add
    BLAST

    GO - Molecular functioni

    1. calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
    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: UniProtKB
    5. receptor catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.22.52. 2681.
    ReactomeiREACT_118572. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiC02.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calpain-1 catalytic subunit (EC:3.4.22.52)
    Alternative name(s):
    Calcium-activated neutral proteinase 1
    Short name:
    CANP 1
    Calpain mu-type
    Calpain-1 large subunit
    Cell proliferation-inducing gene 30 protein
    Micromolar-calpain
    Short name:
    muCANP
    Gene namesi
    Name:CAPN1
    Synonyms:CANPL1
    ORF Names:PIG30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1476. CAPN1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication
    Note: Translocates to the plasma membrane upon Ca2+ binding.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: BHF-UCL
    5. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26057.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 714713Calpain-1 catalytic subunitPRO_0000207694Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications

    Post-translational modificationi

    Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms.

    Keywords - PTMi

    Acetylation, Autocatalytic cleavage

    Proteomic databases

    MaxQBiP07384.
    PaxDbiP07384.
    PRIDEiP07384.

    PTM databases

    PhosphoSiteiP07384.

    Miscellaneous databases

    PMAP-CutDBP07384.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP07384.
    BgeeiP07384.
    CleanExiHS_CAPN1.
    GenevestigatoriP07384.

    Organism-specific databases

    HPAiHPA005992.

    Interactioni

    Subunit structurei

    Forms a heterodimer with a small (regulatory) subunit (CAPNS1).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EZRP153112EBI-1542113,EBI-1056902
    PTPN1P180314EBI-1542113,EBI-968788
    STAT3P407632EBI-1542113,EBI-518675

    Protein-protein interaction databases

    BioGridi107273. 68 interactions.
    IntActiP07384. 12 interactions.
    MINTiMINT-5004023.
    STRINGi9606.ENSP00000279247.

    Structurei

    Secondary structure

    1
    714
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi37 – 393
    Helixi42 – 5110
    Helixi65 – 684
    Helixi78 – 803
    Beta strandi84 – 863
    Helixi88 – 914
    Beta strandi99 – 1024
    Helixi104 – 1063
    Beta strandi111 – 1133
    Helixi115 – 12410
    Helixi128 – 1347
    Beta strandi147 – 1559
    Beta strandi158 – 1669
    Beta strandi168 – 1714
    Beta strandi174 – 1774
    Helixi187 – 19812
    Helixi203 – 2053
    Helixi210 – 2167
    Beta strandi217 – 2204
    Beta strandi221 – 2266
    Helixi227 – 2293
    Helixi234 – 24411
    Beta strandi247 – 2515
    Beta strandi256 – 2583
    Beta strandi274 – 28411
    Beta strandi287 – 2959
    Helixi312 – 3165
    Helixi319 – 3257
    Beta strandi331 – 3377
    Helixi338 – 3447
    Beta strandi347 – 3526

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZCMX-ray2.00A33-353[»]
    2ARYX-ray2.40A/B29-360[»]
    ProteinModelPortaliP07384.
    SMRiP07384. Positions 13-713.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07384.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 354300Calpain catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini541 – 57636EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini585 – 61834EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 65036EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini680 – 71435EF-hand 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni355 – 526172Domain IIIAdd
    BLAST
    Regioni527 – 54216LinkerAdd
    BLAST
    Regioni543 – 713171Domain IVAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C2 family.Curated
    Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
    Contains 4 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG327523.
    HOGENOMiHOG000232035.
    HOVERGENiHBG012645.
    InParanoidiP07384.
    KOiK01367.
    OMAiPQSLGYK.
    OrthoDBiEOG7RV9FM.
    PhylomeDBiP07384.
    TreeFamiTF314748.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR022684. Calpain_cysteine_protease.
    IPR022682. Calpain_domain_III.
    IPR022683. Calpain_III.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000169. Pept_cys_AS.
    IPR001300. Peptidase_C2_calpain_cat.
    [Graphical view]
    PfamiPF01067. Calpain_III. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    PF00648. Peptidase_C2. 1 hit.
    [Graphical view]
    PRINTSiPR00704. CALPAIN.
    SMARTiSM00720. calpain_III. 1 hit.
    SM00230. CysPc. 1 hit.
    SM00054. EFh. 3 hits.
    [Graphical view]
    SUPFAMiSSF49758. SSF49758. 1 hit.
    PROSITEiPS50203. CALPAIN_CAT. 1 hit.
    PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 4 hits.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07384-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEEIITPVY CTGVSAQVQK QRARELGLGR HENAIKYLGQ DYEQLRVRCL    50
    QSGTLFRDEA FPPVPQSLGY KDLGPNSSKT YGIKWKRPTE LLSNPQFIVD 100
    GATRTDICQG ALGDCWLLAA IASLTLNDTL LHRVVPHGQS FQNGYAGIFH 150
    FQLWQFGEWV DVVVDDLLPI KDGKLVFVHS AEGNEFWSAL LEKAYAKVNG 200
    SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYQIILK ALERGSLLGC 250
    SIDISSVLDM EAITFKKLVK GHAYSVTGAK QVNYRGQVVS LIRMRNPWGE 300
    VEWTGAWSDS SSEWNNVDPY ERDQLRVKME DGEFWMSFRD FMREFTRLEI 350
    CNLTPDALKS RTIRKWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR 400
    LDETDDPDDY GDRESGCSFV LALMQKHRRR ERRFGRDMET IGFAVYEVPP 450
    ELVGQPAVHL KRDFFLANAS RARSEQFINL REVSTRFRLP PGEYVVVPST 500
    FEPNKEGDFV LRFFSEKSAG TVELDDQIQA NLPDEQVLSE EEIDENFKAL 550
    FRQLAGEDME ISVKELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD 600
    GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK 650
    LNKKLYELII TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV 700
    TFDLFKWLQL TMFA 714
    Length:714
    Mass (Da):81,890
    Last modified:April 1, 1988 - v1
    Checksum:i1CB6D7C56D063498
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti548 – 5481K → N in AAH08751. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031T → A.1 Publication
    Corresponds to variant rs17885718 [ dbSNP | Ensembl ].
    VAR_021085
    Natural varianti433 – 4331R → P.2 Publications
    Corresponds to variant rs10895991 [ dbSNP | Ensembl ].
    VAR_021086
    Natural varianti492 – 4921G → R.1 Publication
    Corresponds to variant rs17883283 [ dbSNP | Ensembl ].
    VAR_021087
    Natural varianti676 – 6761V → I.1 Publication
    Corresponds to variant rs17884773 [ dbSNP | Ensembl ].
    VAR_021088

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04366 mRNA. Translation: CAA27881.1.
    AY550975 mRNA. Translation: AAT52221.1.
    AY796340 Genomic DNA. Translation: AAV41878.1.
    BC008751 mRNA. Translation: AAH08751.1.
    BC017200 mRNA. Translation: AAH17200.1.
    BC075862 mRNA. Translation: AAH75862.1.
    CCDSiCCDS44644.1.
    PIRiA26213. CIHUH.
    RefSeqiNP_001185797.1. NM_001198868.1.
    NP_001185798.1. NM_001198869.1.
    NP_005177.2. NM_005186.3.
    XP_006718761.1. XM_006718698.1.
    UniGeneiHs.502842.
    Hs.735492.

    Genome annotation databases

    EnsembliENST00000279247; ENSP00000279247; ENSG00000014216.
    ENST00000524773; ENSP00000434176; ENSG00000014216.
    ENST00000527323; ENSP00000431984; ENSG00000014216.
    ENST00000533129; ENSP00000431686; ENSG00000014216.
    ENST00000533820; ENSP00000435272; ENSG00000014216.
    GeneIDi823.
    KEGGihsa:823.
    UCSCiuc001odf.2. human.

    Polymorphism databases

    DMDMi115574.

    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
    X04366 mRNA. Translation: CAA27881.1 .
    AY550975 mRNA. Translation: AAT52221.1 .
    AY796340 Genomic DNA. Translation: AAV41878.1 .
    BC008751 mRNA. Translation: AAH08751.1 .
    BC017200 mRNA. Translation: AAH17200.1 .
    BC075862 mRNA. Translation: AAH75862.1 .
    CCDSi CCDS44644.1.
    PIRi A26213. CIHUH.
    RefSeqi NP_001185797.1. NM_001198868.1.
    NP_001185798.1. NM_001198869.1.
    NP_005177.2. NM_005186.3.
    XP_006718761.1. XM_006718698.1.
    UniGenei Hs.502842.
    Hs.735492.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZCM X-ray 2.00 A 33-353 [» ]
    2ARY X-ray 2.40 A/B 29-360 [» ]
    ProteinModelPortali P07384.
    SMRi P07384. Positions 13-713.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107273. 68 interactions.
    IntActi P07384. 12 interactions.
    MINTi MINT-5004023.
    STRINGi 9606.ENSP00000279247.

    Chemistry

    BindingDBi P07384.
    ChEMBLi CHEMBL3038466.

    Protein family/group databases

    MEROPSi C02.001.

    PTM databases

    PhosphoSitei P07384.

    Polymorphism databases

    DMDMi 115574.

    Proteomic databases

    MaxQBi P07384.
    PaxDbi P07384.
    PRIDEi P07384.

    Protocols and materials databases

    DNASUi 823.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000279247 ; ENSP00000279247 ; ENSG00000014216 .
    ENST00000524773 ; ENSP00000434176 ; ENSG00000014216 .
    ENST00000527323 ; ENSP00000431984 ; ENSG00000014216 .
    ENST00000533129 ; ENSP00000431686 ; ENSG00000014216 .
    ENST00000533820 ; ENSP00000435272 ; ENSG00000014216 .
    GeneIDi 823.
    KEGGi hsa:823.
    UCSCi uc001odf.2. human.

    Organism-specific databases

    CTDi 823.
    GeneCardsi GC11P064950.
    HGNCi HGNC:1476. CAPN1.
    HPAi HPA005992.
    MIMi 114220. gene.
    neXtProti NX_P07384.
    PharmGKBi PA26057.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327523.
    HOGENOMi HOG000232035.
    HOVERGENi HBG012645.
    InParanoidi P07384.
    KOi K01367.
    OMAi PQSLGYK.
    OrthoDBi EOG7RV9FM.
    PhylomeDBi P07384.
    TreeFami TF314748.

    Enzyme and pathway databases

    BRENDAi 3.4.22.52. 2681.
    Reactomei REACT_118572. Degradation of the extracellular matrix.

    Miscellaneous databases

    ChiTaRSi CAPN1. human.
    EvolutionaryTracei P07384.
    GeneWikii CAPN1.
    GenomeRNAii 823.
    NextBioi 3370.
    PMAP-CutDB P07384.
    PROi P07384.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07384.
    Bgeei P07384.
    CleanExi HS_CAPN1.
    Genevestigatori P07384.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR022684. Calpain_cysteine_protease.
    IPR022682. Calpain_domain_III.
    IPR022683. Calpain_III.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000169. Pept_cys_AS.
    IPR001300. Peptidase_C2_calpain_cat.
    [Graphical view ]
    Pfami PF01067. Calpain_III. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    PF00648. Peptidase_C2. 1 hit.
    [Graphical view ]
    PRINTSi PR00704. CALPAIN.
    SMARTi SM00720. calpain_III. 1 hit.
    SM00230. CysPc. 1 hit.
    SM00054. EFh. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49758. SSF49758. 1 hit.
    PROSITEi PS50203. CALPAIN_CAT. 1 hit.
    PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 4 hits.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence."
      Aoki K., Imajoh S., Ohno S., Emori Y., Koike M., Kosaki G., Suzuki K.
      FEBS Lett. 205:313-317(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A novel member of the calcium-dependent cysteine protease family."
      Sorimachi H., Ohmi S., Emori Y., Kawasaki H., Saido T.C., Ohno S., Minami Y., Suzuki K.
      Biol. Chem. Hoppe-Seyler 371:171-176(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Identification of a human cell proliferation inducing gene."
      Kim J.W.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-103; PRO-433; ARG-492 AND ILE-676.
    5. "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], VARIANT PRO-433.
      Tissue: Kidney, Pancreas and Placenta.
    6. "Modulation of the calpain autoproteolysis by calpastatin and phospholipids."
      Melloni E., Michetti M., Salamino F., Minafra R., Pontremoli S.
      Biochem. Biophys. Res. Commun. 229:193-197(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPROTEOLYTIC PROCESSING.
    7. "Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization."
      Michetti M., Salamino F., Tedesco I., Averna M., Minafra R., Melloni E., Pontremoli S.
      FEBS Lett. 392:11-15(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
    8. "Calcium-binding properties of human erythrocyte calpain."
      Michetti M., Salamino F., Minafra R., Melloni E., Pontremoli S.
      Biochem. J. 325:721-726(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CALCIUM-BINDING DATA.
    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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core."
      Li Q., Hanzlik R.P., Weaver R.F., Schonbrunn E.
      Biochemistry 45:701-708(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-353 OF MUTANT ALA-213, CALCIUM-BINDING REGIONS.

    Entry informationi

    Entry nameiCAN1_HUMAN
    AccessioniPrimary (citable) accession number: P07384
    Secondary accession number(s): Q2TTR0, Q6DHV4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3