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Protein

Kallikrein-6

Gene

KLK6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis.6 Publications

Enzyme regulationi

Inhibited by a range of serine protease inhibitors including soybean trypsin inhibitor, benzamidine and serpins. Activated by a range of glycosaminoglycans including chondroitin sulfate, dermatan sulfate, heparan sulfate and heparin.2 Publications

Kineticsi

  1. KM=1562 µM for Tosyl-Gly-Pro-Arg-AMC2 Publications
  2. KM=777 µM for Tosyl-Gly-Pro-Lys-AMC2 Publications
  3. KM=0.410 mM for Phe-Ser-Arg-AMC2 Publications
  4. KM=0.455 mM for Gly-Gly-Arg-AMC2 Publications
  5. KM=0.335 mM for Asp-Pro-Arg-AMC2 Publications
  6. KM=0.758 mM for Gln-Gly-Arg-AMC2 Publications
  7. KM=0.625 mM for Pro-Phe-Arg-AMC2 Publications
  8. KM=0.271 mM for Val-Pro-Arg-AMC2 Publications
  9. KM=1.72 mM for Val-Leu-Lys-AMC2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei62 – 621Charge relay system1 Publication
    Sitei80 – 812Cleavage; by autolysis
    Active sitei106 – 1061Charge relay system1 Publication
    Active sitei197 – 1971Charge relay system1 Publication

    GO - Molecular functioni

    • serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    • amyloid precursor protein metabolic process Source: UniProtKB
    • central nervous system development Source: UniProtKB
    • collagen catabolic process Source: UniProtKB
    • hormone metabolic process Source: UniProtKB
    • myelination Source: UniProtKB
    • neuron death Source: UniProtKB
    • positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    • protein autoprocessing Source: UniProtKB
    • protein processing Source: GO_Central
    • regulation of cell differentiation Source: UniProtKB
    • regulation of neuron projection development Source: Ensembl
    • response to wounding Source: UniProtKB
    • tissue regeneration Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    BRENDAi3.4.21.104. 2681.
    3.4.21.34. 2681.
    3.4.21.B10. 2681.
    SABIO-RKQ92876.

    Protein family/group databases

    MEROPSiS01.236.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kallikrein-6 (EC:3.4.21.-)
    Alternative name(s):
    Neurosin
    Protease M
    SP59
    Serine protease 18
    Serine protease 9
    Zyme
    Gene namesi
    Name:KLK6
    Synonyms:PRSS18, PRSS9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6367. KLK6.

    Subcellular locationi

    • Secreted
    • Nucleusnucleolus
    • Cytoplasm
    • Mitochondrion
    • Microsome

    • Note: In brain, detected in the nucleus of glial cells and in the nucleus and cytoplasm of neurons. Detected in the mitochondrial and microsomal fractions of HEK-293 cells and released into the cytoplasm following cell stress.

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • endoplasmic reticulum Source: UniProtKB-KW
    • extracellular region Source: UniProtKB
    • extracellular space Source: UniProtKB
    • intercellular bridge Source: HPA
    • microtubule cytoskeleton Source: HPA
    • mitochondrion Source: UniProtKB-SubCell
    • nuclear membrane Source: HPA
    • nucleolus Source: UniProtKB-SubCell
    • nucleoplasm Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30156.

    Polymorphism and mutation databases

    BioMutaiKLK6.
    DMDMi3914480.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Propeptidei17 – 215Activation peptideSequence AnalysisPRO_0000027940
    Chaini22 – 244223Kallikrein-6PRO_0000027941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 157
    Disulfide bondi47 ↔ 63
    Disulfide bondi131 ↔ 231
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi138 ↔ 203
    Disulfide bondi168 ↔ 182
    Disulfide bondi193 ↔ 218

    Post-translational modificationi

    Inactivated by autolytic cleavage after Arg-80.

    Keywords - PTMi

    Autocatalytic cleavage, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ92876.
    PaxDbiQ92876.
    PeptideAtlasiQ92876.
    PRIDEiQ92876.

    PTM databases

    PhosphoSiteiQ92876.

    Miscellaneous databases

    PMAP-CutDBQ92876.

    Expressioni

    Tissue specificityi

    In fluids, highest levels found in milk of lactating women followed by cerebrospinal fluid, nipple aspirate fluid and breast cyst fluid. Also found in serum, seminal plasma and some amniotic fluids and breast tumor cytosolic extracts. Not detected in urine. At the tissue level, highest concentrations found in glandular tissues such as salivary glands followed by lung, colon, fallopian tube, placenta, breast, pituitary and kidney. Not detected in skin, spleen, bone, thyroid, heart, ureter, liver, muscle, endometrium, testis, pancreas, seminal vesicle, ovary, adrenals and prostate. In brain, detected in gray matter neurons (at protein level). Colocalizes with pathological inclusions such as Lewy bodies and glial cytoplasmic inclusions. Overexpressed in primary breast tumors but not expressed in metastatic tumors.5 Publications

    Inductioni

    By spinal cord injury. This effect is particularly prominent in macrophages, microglia and reactive astrocytes.1 Publication

    Gene expression databases

    BgeeiQ92876.
    CleanExiHS_KLK6.
    ExpressionAtlasiQ92876. baseline and differential.
    GenevisibleiQ92876. HS.

    Interactioni

    Protein-protein interaction databases

    BioGridi111634. 1 interaction.
    IntActiQ92876. 16 interactions.
    STRINGi9606.ENSP00000309148.

    Structurei

    Secondary structure

    1
    244
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 293Combined sources
    Beta strandi36 – 416Combined sources
    Beta strandi44 – 5310Combined sources
    Beta strandi56 – 594Combined sources
    Helixi61 – 633Combined sources
    Beta strandi69 – 735Combined sources
    Beta strandi75 – 773Combined sources
    Beta strandi85 – 9410Combined sources
    Turni100 – 1023Combined sources
    Beta strandi108 – 1147Combined sources
    Beta strandi137 – 1448Combined sources
    Beta strandi146 – 1494Combined sources
    Beta strandi156 – 1638Combined sources
    Helixi165 – 1717Combined sources
    Turni173 – 1753Combined sources
    Beta strandi180 – 1845Combined sources
    Turni186 – 1883Combined sources
    Turni194 – 1985Combined sources
    Beta strandi200 – 2034Combined sources
    Beta strandi206 – 2138Combined sources
    Beta strandi221 – 2233Combined sources
    Beta strandi225 – 2295Combined sources
    Helixi230 – 2334Combined sources
    Helixi234 – 2374Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GVLX-ray1.80A21-243[»]
    1L2EX-ray1.75A22-244[»]
    1LO6X-ray1.56A22-237[»]
    3VFEX-ray1.88A22-244[»]
    4D8NX-ray1.68A22-244[»]
    ProteinModelPortaliQ92876.
    SMRiQ92876. Positions 22-242.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92876.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 242221Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Kallikrein subfamily.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118862.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiQ92876.
    KOiK08667.
    OMAiAWAEEQN.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ92876.
    TreeFamiTF331065.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q92876-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MKKLMVVLSL IAAAWAEEQN KLVHGGPCDK TSHPYQAALY TSGHLLCGGV
    60 70 80 90 100
    LIHPLWVLTA AHCKKPNLQV FLGKHNLRQR ESSQEQSSVV RAVIHPDYDA
    110 120 130 140 150
    ASHDQDIMLL RLARPAKLSE LIQPLPLERD CSANTTSCHI LGWGKTADGD
    160 170 180 190 200
    FPDTIQCAYI HLVSREECEH AYPGQITQNM LCAGDEKYGK DSCQGDSGGP
    210 220 230 240
    LVCGDHLRGL VSWGNIPCGS KEKPGVYTNV CRYTNWIQKT IQAK
    Length:244
    Mass (Da):26,856
    Last modified:February 1, 1997 - v1
    Checksum:iAEA03F9145D87AAB
    GO
    Isoform 2 (identifier: Q92876-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-107: Missing.

    Show »
    Length:137
    Mass (Da):15,055
    Checksum:i25A421C212869BEA
    GO
    Isoform 3 (identifier: Q92876-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         14-40: AWAEEQNKLVHGGPCDKTSHPYQAALY → GIFRSSWGSITFGKGRVPRSRVLLSGL
         41-244: Missing.

    Show »
    Length:40
    Mass (Da):4,333
    Checksum:i323721E6AE557378
    GO

    Mass spectrometryi

    Molecular mass is 25866 Da from positions 22 - 244. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti78 – 781R → W.
    Corresponds to variant rs61469141 [ dbSNP | Ensembl ].
    VAR_061776

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 107107Missing in isoform 2. 1 PublicationVSP_034403Add
    BLAST
    Alternative sequencei14 – 4027AWAEE…QAALY → GIFRSSWGSITFGKGRVPRS RVLLSGL in isoform 3. 1 PublicationVSP_034404Add
    BLAST
    Alternative sequencei41 – 244204Missing in isoform 3. 1 PublicationVSP_034405Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U62801 mRNA. Translation: AAB07113.1.
    D78203 mRNA. Translation: BAA11306.1.
    AF013988 mRNA. Translation: AAB66483.1.
    AF149289 Genomic DNA. Translation: AAD51475.1.
    AF243527 Genomic DNA. Translation: AAG33359.1.
    AY318867 mRNA. Translation: AAP82446.1.
    AY318868 mRNA. No translation available.
    AY318869 mRNA. Translation: AAP82448.1.
    AY318870 mRNA. No translation available.
    DQ223012 mRNA. Translation: ABB04464.1.
    AK314897 mRNA. Translation: BAG37411.1.
    BT006852 mRNA. Translation: AAP35498.1.
    AC011483 Genomic DNA. No translation available.
    CH471135 Genomic DNA. Translation: EAW71953.1.
    CH471135 Genomic DNA. Translation: EAW71954.1.
    BC015525 mRNA. Translation: AAH15525.1.
    CCDSiCCDS12811.1. [Q92876-1]
    CCDS42599.1. [Q92876-2]
    RefSeqiNP_001012982.1. NM_001012964.1. [Q92876-1]
    NP_001012983.1. NM_001012965.1. [Q92876-2]
    NP_002765.1. NM_002774.3. [Q92876-1]
    UniGeneiHs.79361.

    Genome annotation databases

    EnsembliENST00000310157; ENSP00000309148; ENSG00000167755.
    ENST00000376851; ENSP00000366047; ENSG00000167755.
    ENST00000391808; ENSP00000375684; ENSG00000167755. [Q92876-2]
    ENST00000594641; ENSP00000470482; ENSG00000167755.
    ENST00000597379; ENSP00000469630; ENSG00000167755. [Q92876-3]
    ENST00000599881; ENSP00000471948; ENSG00000167755. [Q92876-3]
    GeneIDi5653.
    KEGGihsa:5653.
    UCSCiuc002puh.3. human. [Q92876-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U62801 mRNA. Translation: AAB07113.1.
    D78203 mRNA. Translation: BAA11306.1.
    AF013988 mRNA. Translation: AAB66483.1.
    AF149289 Genomic DNA. Translation: AAD51475.1.
    AF243527 Genomic DNA. Translation: AAG33359.1.
    AY318867 mRNA. Translation: AAP82446.1.
    AY318868 mRNA. No translation available.
    AY318869 mRNA. Translation: AAP82448.1.
    AY318870 mRNA. No translation available.
    DQ223012 mRNA. Translation: ABB04464.1.
    AK314897 mRNA. Translation: BAG37411.1.
    BT006852 mRNA. Translation: AAP35498.1.
    AC011483 Genomic DNA. No translation available.
    CH471135 Genomic DNA. Translation: EAW71953.1.
    CH471135 Genomic DNA. Translation: EAW71954.1.
    BC015525 mRNA. Translation: AAH15525.1.
    CCDSiCCDS12811.1. [Q92876-1]
    CCDS42599.1. [Q92876-2]
    RefSeqiNP_001012982.1. NM_001012964.1. [Q92876-1]
    NP_001012983.1. NM_001012965.1. [Q92876-2]
    NP_002765.1. NM_002774.3. [Q92876-1]
    UniGeneiHs.79361.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GVLX-ray1.80A21-243[»]
    1L2EX-ray1.75A22-244[»]
    1LO6X-ray1.56A22-237[»]
    3VFEX-ray1.88A22-244[»]
    4D8NX-ray1.68A22-244[»]
    ProteinModelPortaliQ92876.
    SMRiQ92876. Positions 22-242.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111634. 1 interaction.
    IntActiQ92876. 16 interactions.
    STRINGi9606.ENSP00000309148.

    Chemistry

    BindingDBiQ92876.
    ChEMBLiCHEMBL4448.

    Protein family/group databases

    MEROPSiS01.236.

    PTM databases

    PhosphoSiteiQ92876.

    Polymorphism and mutation databases

    BioMutaiKLK6.
    DMDMi3914480.

    Proteomic databases

    MaxQBiQ92876.
    PaxDbiQ92876.
    PeptideAtlasiQ92876.
    PRIDEiQ92876.

    Protocols and materials databases

    DNASUi5653.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000310157; ENSP00000309148; ENSG00000167755.
    ENST00000376851; ENSP00000366047; ENSG00000167755.
    ENST00000391808; ENSP00000375684; ENSG00000167755. [Q92876-2]
    ENST00000594641; ENSP00000470482; ENSG00000167755.
    ENST00000597379; ENSP00000469630; ENSG00000167755. [Q92876-3]
    ENST00000599881; ENSP00000471948; ENSG00000167755. [Q92876-3]
    GeneIDi5653.
    KEGGihsa:5653.
    UCSCiuc002puh.3. human. [Q92876-1]

    Organism-specific databases

    CTDi5653.
    GeneCardsiGC19M051461.
    HGNCiHGNC:6367. KLK6.
    MIMi602652. gene.
    neXtProtiNX_Q92876.
    PharmGKBiPA30156.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118862.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiQ92876.
    KOiK08667.
    OMAiAWAEEQN.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ92876.
    TreeFamiTF331065.

    Enzyme and pathway databases

    BRENDAi3.4.21.104. 2681.
    3.4.21.34. 2681.
    3.4.21.B10. 2681.
    SABIO-RKQ92876.

    Miscellaneous databases

    ChiTaRSiKLK6. human.
    EvolutionaryTraceiQ92876.
    GeneWikiiKLK6.
    GenomeRNAii5653.
    NextBioi21966.
    PMAP-CutDBQ92876.
    PROiQ92876.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ92876.
    CleanExiHS_KLK6.
    ExpressionAtlasiQ92876. baseline and differential.
    GenevisibleiQ92876. HS.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A novel protease homolog differentially expressed in breast and ovarian cancer."
      Anisowicz A., Sotiropoulou G., Stenman G., Mok S.C., Sager R.
      Mol. Med. 2:624-636(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular cloning of a novel trypsin-like serine protease (neurosin) preferentially expressed in brain."
      Yamashiro K., Tsuruoka N., Kodama S., Tsujimoto M., Yamamura Y., Tanaka T., Nakazato H., Yamaguchi N.
      Biochim. Biophys. Acta 1350:11-14(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Molecular characterization of Zyme/protease M/neurosin(PRSS9), a hormonally regulated kallikrein-like serine protease."
      Yousef G.M., Luo L.Y., Scherer S.W., Sotiropoulou G., Diamandis E.P.
      Genomics 62:251-259(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region."
      Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P., Paeper B., Wang K.
      Gene 257:119-130(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Cloning and characterization of novel isoforms of the human kallikrein 6 gene."
      Pampalakis G., Kurlender L., Diamandis E.P., Sotiropoulou G.
      Biochem. Biophys. Res. Commun. 320:54-61(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Testis.
    7. "Multiple mechanisms underlie the aberrant expression of the human kallikrein 6 gene in breast cancer."
      Pampalakis G., Sotiropoulou G.
      Biol. Chem. 387:773-782(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    8. "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].
    9. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    10. "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].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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] (ISOFORM 1).
      Tissue: Colon.
    13. "Immunofluorometric assay of human kallikrein 6 (zyme/protease M/neurosin) and preliminary clinical applications."
      Diamandis E.P., Yousef G.M., Soosaipillai A.R., Grass L., Porter A., Little S., Sotiropoulou G.
      Clin. Biochem. 33:369-375(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    14. "Localization of a novel type trypsin-like serine protease, neurosin, in brain tissues of Alzheimer's disease and Parkinson's disease."
      Ogawa K., Yamada T., Tsujioka Y., Taguchi J., Takahashi M., Tsuboi Y., Fujino Y., Nakajima M., Yamamoto T., Akatsu H., Mitsui S., Yamaguchi N.
      Psychiatry Clin. Neurosci. 54:419-426(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    15. "The spectrum of human kallikrein 6 (zyme/protease M/neurosin) expression in human tissues as assessed by immunohistochemistry."
      Petraki C.D., Karavana V.N., Skoufogiannis P.T., Little S.P., Howarth D.J.C., Yousef G.M., Diamandis E.P.
      J. Histochem. Cytochem. 49:1431-1441(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    16. "Characterization of the enzymatic activity of human kallikrein 6: autoactivation, substrate specificity, and regulation by inhibitors."
      Magklara A., Mellati A.A., Wasney G.A., Little S.P., Sotiropoulou G., Becker G.W., Diamandis E.P.
      Biochem. Biophys. Res. Commun. 307:948-955(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AUTOCATALYTIC CLEAVAGE.
    17. "Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies."
      Iwata A., Maruyama M., Akagi T., Hashikawa T., Kanazawa I., Tsuji S., Nukina N.
      Hum. Mol. Genet. 12:2625-2635(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    18. "Human kallikrein 6 degrades extracellular matrix proteins and may enhance the metastatic potential of tumour cells."
      Ghosh M.C., Grass L., Soosaipillai A., Sotiropoulou G., Diamandis E.P.
      Tumor Biol. 25:193-199(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. Cited for: FUNCTION, INDUCTION.
    20. "Substrate specificity of human kallikrein 6: salt and glycosaminoglycan activation effects."
      Angelo P.F., Lima A.R., Alves F.M., Blaber S.I., Scarisbrick I.A., Blaber M., Juliano L., Juliano M.A.
      J. Biol. Chem. 281:3116-3126(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    21. "The autolytic regulation of human kallikrein-related peptidase 6."
      Blaber S.I., Yoon H., Scarisbrick I.A., Juliano M.A., Blaber M.
      Biochemistry 46:5209-5217(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOCATALYTIC CLEAVAGE.
    22. "The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family."
      Gomis-Rueth F.X., Bayes A., Sotiropoulou G., Pampalakis G., Tsetsenis T., Villegas V., Aviles F.X., Coll M.
      J. Biol. Chem. 277:27273-27281(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-243, AUTOCATALYTIC CLEAVAGE, ACTIVE SITES, DISULFIDE BONDS.
    23. "Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system."
      Bernett M.J., Blaber S.I., Scarisbrick I.A., Dhanarajan P., Thompson S.M., Blaber M.
      J. Biol. Chem. 277:24562-24570(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 22-244, PROTEIN SEQUENCE OF 22-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AUTOCATALYTIC CLEAVAGE, DISULFIDE BONDS, MASS SPECTROMETRY.

    Entry informationi

    Entry nameiKLK6_HUMAN
    AccessioniPrimary (citable) accession number: Q92876
    Secondary accession number(s): A6NJA1, A8MW09, Q6H301
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: February 1, 1997
    Last modified: July 22, 2015
    This is version 143 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.