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Q92876 (KLK6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kallikrein-6

EC=3.4.21.-
Alternative name(s):
Neurosin
Protease M
SP59
Serine protease 18
Serine protease 9
Zyme
Gene names
Name:KLK6
Synonyms:PRSS18, PRSS9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23

Enzyme regulation

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. Ref.16 Ref.20

Subcellular location

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. Ref.13 Ref.14 Ref.17

Tissue specificity

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. Ref.7 Ref.13 Ref.14 Ref.15 Ref.17

Induction

By spinal cord injury. This effect is particularly prominent in macrophages, microglia and reactive astrocytes. Ref.16 Ref.19 Ref.20

Post-translational modification

Inactivated by autolytic cleavage after Arg-80.

Sequence similarities

Belongs to the peptidase S1 family. Kallikrein subfamily.

Contains 1 peptidase S1 domain.

Biophysicochemical properties

Kinetic parameters:

KM=1562 µM for Tosyl-Gly-Pro-Arg-AMC Ref.16 Ref.23

KM=777 µM for Tosyl-Gly-Pro-Lys-AMC

KM=0.410 mM for Phe-Ser-Arg-AMC

KM=0.455 mM for Gly-Gly-Arg-AMC

KM=0.335 mM for Asp-Pro-Arg-AMC

KM=0.758 mM for Gln-Gly-Arg-AMC

KM=0.625 mM for Pro-Phe-Arg-AMC

KM=0.271 mM for Val-Pro-Arg-AMC

KM=1.72 mM for Val-Leu-Lys-AMC

Mass spectrometry

Molecular mass is 25866 Da from positions 22 - 244. Determined by MALDI. Ref.23

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Microsome
Mitochondrion
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMAutocatalytic cleavage
Cleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processamyloid precursor protein metabolic process

Non-traceable author statement PubMed 12709365. Source: UniProtKB

central nervous system development

Non-traceable author statement PubMed 12589961. Source: UniProtKB

collagen catabolic process

Non-traceable author statement Ref.16. Source: UniProtKB

hormone metabolic process

Non-traceable author statement Ref.15. Source: UniProtKB

myelination

Non-traceable author statement Ref.15. Source: UniProtKB

neuron death

Inferred from mutant phenotype PubMed 22166940. Source: UniProt

positive regulation of G-protein coupled receptor protein signaling pathway

Inferred from direct assay PubMed 16885167. Source: UniProtKB

protein autoprocessing

Non-traceable author statement Ref.16. Source: UniProtKB

proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of cell differentiation

Non-traceable author statement Ref.15. Source: UniProtKB

regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

response to wounding

Non-traceable author statement Ref.22. Source: UniProtKB

tissue regeneration

Non-traceable author statement Ref.16. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular region

Inferred from direct assay Ref.15. Source: UniProtKB

intercellular bridge

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

secretory granule

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12709365Ref.16. Source: UniProtKB

serine-type endopeptidase activity

Inferred from direct assay PubMed 16885167. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92876-1)

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.
Isoform 2 (identifier: Q92876-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: Missing.
Isoform 3 (identifier: Q92876-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 215Activation peptide Potential
PRO_0000027940
Chain22 – 244223Kallikrein-6
PRO_0000027941

Regions

Domain22 – 242221Peptidase S1

Sites

Active site621Charge relay system Ref.22
Active site1061Charge relay system Ref.22
Active site1971Charge relay system Ref.22
Site80 – 812Cleavage; by autolysis

Amino acid modifications

Glycosylation1341N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 157 Ref.22 Ref.23
Disulfide bond47 ↔ 63 Ref.22 Ref.23
Disulfide bond131 ↔ 231 Ref.22 Ref.23
Disulfide bond138 ↔ 203 Ref.22 Ref.23
Disulfide bond168 ↔ 182 Ref.22 Ref.23
Disulfide bond193 ↔ 218 Ref.22 Ref.23

Natural variations

Alternative sequence1 – 107107Missing in isoform 2.
VSP_034403
Alternative sequence14 – 4027AWAEE…QAALY → GIFRSSWGSITFGKGRVPRS RVLLSGL in isoform 3.
VSP_034404
Alternative sequence41 – 244204Missing in isoform 3.
VSP_034405
Natural variant781R → W.
Corresponds to variant rs61469141 [ dbSNP | Ensembl ].
VAR_061776

Secondary structure

............................................... 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: AEA03F9145D87AAB

FASTA24426,856
        10         20         30         40         50         60 
MKKLMVVLSL IAAAWAEEQN KLVHGGPCDK TSHPYQAALY TSGHLLCGGV LIHPLWVLTA 

        70         80         90        100        110        120 
AHCKKPNLQV FLGKHNLRQR ESSQEQSSVV RAVIHPDYDA ASHDQDIMLL RLARPAKLSE 

       130        140        150        160        170        180 
LIQPLPLERD CSANTTSCHI LGWGKTADGD FPDTIQCAYI HLVSREECEH AYPGQITQNM 

       190        200        210        220        230        240 
LCAGDEKYGK DSCQGDSGGP LVCGDHLRGL VSWGNIPCGS KEKPGVYTNV CRYTNWIQKT 


IQAK 

« Hide

Isoform 2 [UniParc].

Checksum: 25A421C212869BEA
Show »

FASTA13715,055
Isoform 3 [UniParc].

Checksum: 323721E6AE557378
Show »

FASTA404,333

References

« Hide 'large scale' references
[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]"Zyme, a novel and potentially amyloidogenic enzyme cDNA isolated from Alzheimer's disease brain."
Little S.P., Dixon E.P., Norris F., Buckley W., Becker G.W., Johnson M., Dobbins J.R., Wyrick T., Miller J.R., Mackellar W., Hepburn D., Corvalan J., McClure D., Liu X., Stephenson D., Clemens J., Johnstone E.M.
J. Biol. Chem. 272:25135-25142(1997) [PubMed] [Europe PMC] [Abstract]
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. 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].
[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. 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].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Dynamic role of kallikrein 6 in traumatic spinal cord injury."
Scarisbrick I.A., Sabharwal P., Cruz H., Larsen N., Vandell A.G., Blaber S.I., Ameenuddin S., Papke L.M., Fehlings M.G., Reeves R.K., Blaber M., Windebank A.J., Rodriguez M.
Eur. J. Neurosci. 24:1457-1469(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12811.1. [Q92876-1]
CCDS42599.1. [Q92876-2]
RefSeqNP_001012982.1. NM_001012964.1. [Q92876-1]
NP_001012983.1. NM_001012965.1. [Q92876-2]
NP_002765.1. NM_002774.3. [Q92876-1]
UniGeneHs.79361.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GVLX-ray1.80A21-243[»]
1L2EX-ray1.75A22-244[»]
1LO6X-ray1.56A22-237[»]
3VFEX-ray1.88A22-244[»]
4D8NX-ray1.68A22-244[»]
ProteinModelPortalQ92876.
SMRQ92876. Positions 22-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111634. 1 interaction.
IntActQ92876. 12 interactions.
STRING9606.ENSP00000309148.

Chemistry

BindingDBQ92876.
ChEMBLCHEMBL4448.

Protein family/group databases

MEROPSS01.236.

PTM databases

PhosphoSiteQ92876.

Polymorphism databases

DMDM3914480.

Proteomic databases

MaxQBQ92876.
PaxDbQ92876.
PeptideAtlasQ92876.
PRIDEQ92876.

Protocols and materials databases

DNASU5653.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310157; ENSP00000309148; ENSG00000167755. [Q92876-1]
ENST00000376851; ENSP00000366047; ENSG00000167755. [Q92876-1]
ENST00000391808; ENSP00000375684; ENSG00000167755. [Q92876-2]
ENST00000424910; ENSP00000396012; ENSG00000167755. [Q92876-3]
ENST00000456750; ENSP00000409241; ENSG00000167755. [Q92876-2]
ENST00000594641; ENSP00000470482; ENSG00000167755. [Q92876-1]
ENST00000597379; ENSP00000469630; ENSG00000167755. [Q92876-3]
ENST00000599881; ENSP00000471948; ENSG00000167755. [Q92876-3]
GeneID5653.
KEGGhsa:5653.
UCSCuc002puh.3. human. [Q92876-1]

Organism-specific databases

CTD5653.
GeneCardsGC19M051461.
HGNCHGNC:6367. KLK6.
HPAHPA051837.
MIM602652. gene.
neXtProtNX_Q92876.
PharmGKBPA30156.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidQ92876.
KOK08667.
OMAWIRKTIQ.
OrthoDBEOG75B84T.
PhylomeDBQ92876.
TreeFamTF331065.

Enzyme and pathway databases

SABIO-RKQ92876.

Gene expression databases

ArrayExpressQ92876.
BgeeQ92876.
CleanExHS_KLK6.
GenevestigatorQ92876.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ92876.
GeneWikiKLK6.
GenomeRNAi5653.
NextBio21966.
PMAP-CutDBQ92876.
PROQ92876.
SOURCESearch...

Entry information

Entry nameKLK6_HUMAN
AccessionPrimary (citable) accession number: Q92876
Secondary accession number(s): A6NJA1, A8MW09, Q6H301
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 132 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

Peptidase families

Classification of peptidase families and list of entries

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