Q92876 (KLK6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Nucleus › nucleolus. 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 component	Cytoplasm Endoplasmic reticulum Microsome Mitochondrion Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Autocatalytic cleavage Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	amyloid 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 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 electronic annotation. Source: UniProtKB-KW regulation of cell differentiation Non-traceable author statement Ref.15. Source: UniProtKB regulation of neuron projection development Inferred from electronic annotation. Source: Compara tissue regeneration Non-traceable author statement Ref.16. Source: UniProtKB
Cellular_component	cytoplasm 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 mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Potential

Propeptide

17 – 21

5

Activation peptide Potential

PRO_0000027940

Chain

22 – 244

223

Kallikrein-6

PRO_0000027941

Regions

Domain

22 – 242

221

Peptidase S1

Sites

Active site

62

1

Charge relay system Ref.22

Active site

106

1

Charge relay system Ref.22

Active site

197

1

Charge relay system Ref.22

Site

80 – 81

2

Cleavage; by autolysis

Amino acid modifications

Glycosylation

134

1

N-linked (GlcNAc...) Potential

Disulfide bond

28 ↔ 157

Ref.22 Ref.23

Disulfide bond

47 ↔ 63

Ref.22 Ref.23

Disulfide bond

131 ↔ 231

Ref.22 Ref.23

Disulfide bond

138 ↔ 203

Ref.22 Ref.23

Disulfide bond

168 ↔ 182

Ref.22 Ref.23

Disulfide bond

193 ↔ 218

Ref.22 Ref.23

Natural variations

Alternative sequence

1 – 107

107

Missing in isoform 2.

VSP_034403

Alternative sequence

14 – 40

27

AWAEE…QAALY → GIFRSSWGSITFGKGRVPRS RVLLSGL in isoform 3.

VSP_034404

Alternative sequence

41 – 244

204

Missing in isoform 3.

VSP_034405

Natural variant

78

1

R → W.
Corresponds to variant rs61469141 [ dbSNP | Ensembl ].

VAR_061776

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

244

Helix Strand Turn

Details...

Helix

27 – 29

3

Beta strand

36 – 41

6

Beta strand

44 – 53

10

Beta strand

56 – 59

4

Helix

61 – 63

3

Beta strand

69 – 73

5

Beta strand

75 – 77

3

Beta strand

85 – 94

10

Turn

100 – 102

3

Beta strand

108 – 114

7

Beta strand

137 – 144

8

Beta strand

146 – 149

4

Beta strand

156 – 163

8

Helix

165 – 171

7

Turn

173 – 175

3

Beta strand

180 – 184

5

Turn

186 – 188

3

Turn

194 – 198

5

Beta strand

200 – 203

4

Beta strand

206 – 213

8

Beta strand

221 – 223

3

Beta strand

225 – 229

5

Helix

230 – 233

4

Helix

234 – 237

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: AEA03F9145D87AAB	FASTA	244	26,856
	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
	Isoform 2 [UniParc]. Checksum: 25A421C212869BEA	FASTA	137	15,055
	10 20 30 40 50 60 MLLRLARPAK LSELIQPLPL ERDCSANTTS CHILGWGKTA DGDFPDTIQC AYIHLVSREE 70 80 90 100 110 120 CEHAYPGQIT QNMLCAGDEK YGKDSCQGDS GGPLVCGDHL RGLVSWGNIP CGSKEKPGVY 130 TNVCRYTNWI QKTIQAK
	Isoform 3 [UniParc]. Checksum: 323721E6AE557378	FASTA	40	4,333
	10 20 30 40 MKKLMVVLSL IAAGIFRSSW GSITFGKGRV PRSRVLLSGL

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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.

IPI

IPI00023845.
IPI00554738.
IPI00896372.

RefSeq

NP_001012982.1. NM_001012964.1.
NP_001012983.1. NM_001012965.1.
NP_002765.1. NM_002774.3.

UniGene

Hs.79361.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GVL	X-ray	1.80	A	21-243	[»]
1L2E	X-ray	1.75	A	22-244	[»]
1LO6	X-ray	1.56	A	22-237	[»]
3VFE	X-ray	1.88	A	22-244	[»]
4D8N	X-ray	1.68	A	22-244	[»]

ProteinModelPortal

Q92876.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92876. 12 interactions.

STRING

9606.ENSP00000309148.

Protein family/group databases

MEROPS

S01.236.

PTM databases

PhosphoSite

Q92876.

Polymorphism databases

DMDM

3914480.

Proteomic databases

PaxDb

Q92876.

PeptideAtlas

Q92876.

PRIDE

Q92876.

Protocols and materials databases

DNASU

5653.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310157; ENSP00000309148; ENSG00000167755.
ENST00000376851; ENSP00000366047; ENSG00000167755.
ENST00000391808; ENSP00000375684; ENSG00000167755.
ENST00000424910; ENSP00000396012; ENSG00000167755.
ENST00000456750; ENSP00000409241; ENSG00000167755.
ENST00000594641; ENSP00000470482; ENSG00000167755.
ENST00000597379; ENSP00000469630; ENSG00000167755.
ENST00000599881; ENSP00000471948; ENSG00000167755.

GeneID

5653.

KEGG

hsa:5653.

UCSC

uc002puh.3. human.

Organism-specific databases

CTD

5653.

GeneCards

GC19M051461.

HGNC

HGNC:6367. KLK6.

MIM

602652. gene.

neXtProt

NX_Q92876.

PharmGKB

PA30156.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

HOGENOM

HOG000251820.

HOVERGEN

HBG013304.

InParanoid

Q92876.

KO

K08667.

OMA

CAGDEKY.

PhylomeDB

Q92876.

Enzyme and pathway databases

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.

SABIO-RK

Q92876.

Gene expression databases

ArrayExpress

Q92876.

Bgee

Q92876.

CleanEx

HS_KLK6.

Genevestigator

Q92876.

GermOnline

ENSG00000167755. Homo sapiens.

Family and domain databases

InterPro

IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q92876.

ChEMBL

CHEMBL4448.

EvolutionaryTrace

Q92876.

GenomeRNAi

5653.

NextBio

21966.

PMAP-CutDB

Q92876.

SOURCE

Search...

Entry information

Entry name

KLK6_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.