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KLK12 (kallikrein-related peptidase 12)

Written2020-04Paraskevi Karousi, Andreas Scorilas, Christos K. Kontos
Department of Biochemistry and Molecular Biology, Faculty of Biology, National and Kapodistrian University of Athens, Athens, Greece /
This article is an update of :
2016-09Christos K. Kontos, Andreas Scorilas
Department of Biochemistry and Molecular Biology, National and Kapodistrian University of Athens, Athens, Greece /

Abstract Review on KLK12, with data on DNA, on the protein encoded, and where the gene is implicated.

Keywords Kallikreins; KLK12; Prostate cancer; Breast cancer; Colorectal cancer; Gastric cancer; Non-small cell lung cancer;

(Note : for Links provided by Atlas : click)


Alias (NCBI)KLK-L5
HGNC (Hugo) KLK12
HGNC Alias symbKLK-L5
HGNC Previous namekallikrein 12
LocusID (NCBI) 43849
Atlas_Id 41078
Location 19q13.41  [Link to chromosome band 19q13]
Location_base_pair Starts at 51029094 and ends at 51035002 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping KLK12.png]
Local_order Telomere to centromere
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


  Figure 1. Schematic representation of the KLK12 gene. Exons are shown as boxes and introns as connecting lines. The coding sequences are highlighted as red, while 5' and 3' untranslated regions (UTRs) are shown in white. Numbers inside or outside boxes indicate lengths (nt) of exons and introns, respectively, while numbers in parentheses indicate lengths (aa) of protein isoforms. The question mark (?) denotes an undetermined 5' UTR. Arrows (↓) show the position of the start codons (ATG) and asterisks (*) denote the position of the stop codons (TAA or TGA). The figure is drawn to scale, except for the introns containing the (//) symbol.
Description The KLK12 gene has a total length of 6,695 nt and comprises 7 exons and 6 intervening introns. The structure of the KLK12 gene is similar to that of the other KLK family members (Yousef et al., 2000). Four different genetic polymorphisms have been described so far: one at a splice-donor site of intron 4 (c.457+2T>C), two in exon 6 (c.618_619delTG:p.Cys206fsX72 and c.735G>A:p.Met245Ile), and one in intron 3. The c.457+2T>C polymorphism was detected at a high frequency (allele frequency:0.63), compared to the frequencies of the two polymorphisms in exon 6 (allele frequency:0.01) (Shinmura et al., 2004).
Transcription The KLK12 pre-mRNA is subjected to alternative splicing, generating ten splice variants, nine of which are considered to encode distinct protein isoforms (Kurlender et al., 2005; Adamopoulos et al., 2018). Seven transcripts are accessible in the GenBank Reference Sequence (RefSeq) database. The predominant transcript (GenBank accession number: NM_019598.3), consisting of 1053 nt, includes all 7 exons and encodes isoform 1 precursor. The second transcript (GenBank accession number: NM_145894.2) uses alternative splice sites in the 3' coding region, in comparison with the aforementioned transcripts, generating a protein with a distinct C-terminus compared to the isoform 1 precursor. The third transcript (GenBank accession number: NM_145895.2)has a different open reading frame (ORF); it lacks an exon in the coding region and uses different splice sites in the 3' coding region, compared to the first transcript, generating a protein with a distinct N-terminus and the same C-terminus as isoform 2. The fourth transcript (GenBank accession number: NM_001370125.1) comprises an alternative exon in 5' untranslated region (5'-UTR) and generates the same protein isoform as transcript 2. The fifth transcript (GenBank accession number: NM_001370126.1) comprises two alternative exons in 5'-UTR, shows a different ORF and lacks an exon in the coding region, generating a protein with different N- and C-termini, in comparison with isoform 1. The sixth transcript (GenBank accession number: NM_001370127.1) includes an alternative exon in 5'-UTR, lacks an exon within the coding region and uses alternative splice sites in the 3' coding region, generating the same protein isoform as transcript 3. The exon structure of the seventh transcript (GenBank accession number: NM_001370128.1) resembles that of the fourth one; it only lacks one exon within the coding region and generates the same protein isoform as transcripts 3 and 6.
Recently, members of our research group revealed the exon structure of a new KLK12 splice variant (GenBank accession number: KY697987.1) (Adamopoulos et al., 2018). This transcript lacks two exons within the coding sequence and uses alternative splice sites in the 3' coding region, while its 5' UTR has not been determined yet. This transcript is predicted to encode a distinct KLK12 protein isoform of 111 amino acid residues.
The sequences of seven transcripts have been deposited in the Ensembl database; only two of them have a different exon combination, compared to those of the RefSeq database. The structure of the first one (Ensembl accession number: ENST00000525263.5) is similar to the second transcript; it only lacks an exon in the 5' UTR, and has a 5' extended second exon, leading to the same protein isoform as variant 2. The other one (Ensembl accession number: ENST00000531374.5) has a distinct exon structure, which generates a premature translation termination codon.
One more splice variant (GenBank accession number: XM_005258951.3) is predicted to be encoded by the KLK12 gene, based on automatic sequence analysis of expressed sequence tags (ESTs). This transcript is similar to the third variant; it differs by having longer 5'- and 3'-UTRs, and a different ORF. The protein generated by the predicted transcript has a different C-terminus, compared to isoform 1.
KLK12 mRNA is primarily expressed in the salivary gland, stomach, uterus trachea, prostate, thymus, lung, colon, brain, breast, and thyroid gland. However, lower levels of KLK12 mRNA expression are found in other tissues too, including testis, pancreas, small intestine, spinal cord and tonsil (Yousef et al., 2000; Filippou et al., 2020).
Pseudogene Not identified so far.


  Figure 2. Alignment of amino acid sequences of the precursors of the KLK12 protein isoforms. The three amino acid residues (positions: 62, 108, and 200) constituting the catalytic triad that is required for protease activity are shown in red; the N-terminal signal peptide (positions: 1-17) is shown in blue; putative N-glycosylation sites (positions: 24 and 163) are shown in green; substrate-binding sites (positions: 197, 215, and 217) are shown in light blue; and the cleavage position is shown in orange (position 22). Numbering of amino acid residue positions is based on the sequence of the main KLK12 isoform (isoform 1) precursor.
Description Five distinct protein isoforms are generated by KLK12 transcript variants, while one more is most likely generated by the predicted transcript The main KLK12 isoform (isoform 1; GenBank accession number: NP_062544.1) precursor, designated as the classical one, consists of 254 amino acid residues and has a molecular mass of 25.3 kDa. The N-terminal signal peptide comprises 17 amino acid residues. KLK12 is a secreted trypsin-like serine protease, cleaving peptide bonds after both arginine and lysine (Memari et al., 2007; Yousef et al., 2000). KLK12 protein isoforms are synthesized as inactive precursor zymogens that are cleaved at position 22 during limited proteolysis to generate their active forms. Amino acid residues 24 and 163 represent glycosylation positions, while positions 194, 215, and 217 are substrate-binding sites. Three amino acid residues (positions: 62, 108, and 200) constitute the catalytic triad that is required for protease activity. KLK12 isoform 2 (GenBank accession number: NP_665901.1) has a distinct C-terminus compared to isoform 1, and its precursor form consists of 248 amino acid residues. KLK12 isoform 3 (GenBank accession number: NP_665902.2) has a different N-terminus compared to isoform 1 and the same C-terminus as isoform 2, and its precursor form consists of 138 amino acid residues. KLK12 isoform 4 (GenBank accession number: NP_001357055.1) has the same N-terminus as isoform 3, and a distinct C-terminus, including 144 amino acid residues. Another KLK14 precursor isoform (isoform 5; GenBank accession number: AUS91425.1) is composed of 111 amino acid residues and has a different C-terminus, in comparison with the classical isoform. One more isoform (GenBank accession number: XP_005259008.1) is predicted to be composed by 111 amino acid residues and possesses a distinct C-terminus.
KLK12 is secreted as an inactive pro-enzyme, which can be self-activated to gain enzymatic activity. Active KLK12 shows trypsin-like activity, but quickly loses its activity due to autodegradation. KLK12 activity can also be rapidly inhibited by zinc ions and by α2-antiplasmin through covalent complex formation. It has been suggested that KLK12 participates in enzymatic cascades involving other KLKs (Memari et al., 2007). KLK12 is able to cleave all six members of the CCN family (CYR61, CTGF, NOV, WISP1, WIPS2, and WISP3) at different proteolytic sites, thus indirectly regulating the bioavailability and activity of several growth factors through processing of their CCN-binding partners (Guillon-Munos et al., 2011). In vivo substrates include also the thrombolytic zymogens plasminogen, urokinase, and plasma kallikrein. Another substrate of KLK12 secreted by the respiratory tract is influenza HA protein (Hamilton and Whittaker, 2013). Furthermore, KLK12 participates in the control of angiogenesis via a PDGFB-dependent paracrine pathway and by cleaving the extracellular matrix proteins fibronectin and tenascin. These proteins play a crucial role in endothelial cell adhesion and migration (Kryza et al., 2013; 2014; 2018). On the other hand, the proteolytic activity of KLK12 is inhibited by the action of serine peptidase inhibitor, Kazal type 6 (SPINK6) in the skin (Kantyka et al., 2011).
  Figure 3. Predicted models of the precursors of the KLK12 protein isoforms, using the I-TASSER server (Yang and Zhang, 2015). For each protein, only the 3D structure with the highest confidence score is presented. The RasMol 'Group' color scheme color codes residues by their position in a macromolecular chain. Each polypeptide is drawn as a smooth spectrum from blue through green, yellow and orange to red. Thus, the N-termini are colored blue and the C-termini are drawn in red.
Expression KLK12 mRNA is primarily expressed in the salivary gland, stomach, uterus trachea, prostate, thymus, lung, colon, brain, breast, and thyroid gland. However, lower levels of KLK12 mRNA expression are found in other tissues too, including testis, pancreas, small intestine, and spinal cord (Yousef et al., 2000).

Implicated in

Entity Prostate cancer
Note KLK12 single nucleotide polymorphism (SNP) rs3865443 is significantly associated with increased risk of prostate cancer; still, this association has been described as marginal (Lose et al., 2013).
Entity Breast cancer
Note KLK12 mRNA expression is downregulated in breast cancer tissues and is upregulated by steroid hormones in breast and prostate cancer cell lines (Talieri et al., 2012; Yousef et al., 2000).
Prognosis KLK12 expression was associated with shorter disease-free (DFS) and overall survival (OS) time intervals of patients with triple-negative breast cancer (Gong et al., 2020). KLK12 variant 3 expression is downregulated in breast tumors of small size, high grade, and advanced TNM stage. Moreover, KLK12 variant 3 overexpression is associated with higher disease-free survival (DFS) rates for breast cancer patients, as well as with elevated progesterone receptor (PR) concentration (Talieri et al., 2012). KLK12 variant 3 constitutes an independent favorable marker with additional prognostic information to TNM staging of breast cancer patients. KLK12 variants 1, 2, and 3 can be used to distinguish benign from malignant breast tissue (Papachristopoulou et al., 2018).
Entity Colorectal cancer
Note KLK12 was overexpressed in HT-29 colorectal cancer cells. Silencing of KLK12 via siRNA was shown to inhibit invasion and migration of these cells. Furthermore, expression levels CDH1 were increased upon KLK12 silencing, whereas expression levels of Vimentin, SNAI1, and matrix MMP2 and MMP9 (metallopeptidases 2 and 9) decreased, thereby indicating the role of KLK12 in epithelial to mesenchymal transition (EMT). KLK12 silencing in the colorectal cancer HT-29 cells resulted in the reduction of the expression of the antiapoptotic BCL2 protein and the parallel increase in the expression levels of the proapoptotic BAX protein, thus enhancing CASP3 (Caspase3) cleavage and mediating apoptosis. Loss of KLK12 expression increased, also, the phosphorylation of PRKAA2 (5' adenosine monophosphate 5' AMP-activated protein kinase AMPK), which in turn decreased the phosphorylation of mechanistic target of rapamycin kinase ( MTOR), a central controller of cell growth and proliferation. These findings indicate that HT-29 cell viability and metastasis may be regulated by KLK12 (Li et al., 2019).
Entity Gastric cancer
Note Expression of the KLK12 gene is significantly upregulated in gastric cancer tissues, as compared with normal gastric tissues, both at the mRNA and protein level. Knockdown of KLK12 expression via siRNA resulted in a reduction of proliferation and migration of MKN-45 and AGS gastric cancer cells (Zhao et al., 2012; Li and He, 2016).
Prognosis KLK12 overexpression is significantly associated with lymph node metastasis, histological type, and TNM. Furthermore, patients with gastric tumors showing high KLK12 expression have a significantly worse five-year survival rate than those with tumors with low KLK12 expression (Zhao et al., 2012).
Entity Non-small cell lung cancer
Note KLK12 levels are lower in sera from non-small cell lung cancer patients than in sera from normal controls. Serum KLK12 concentration is likely to be associated with disease stage (Planque et al., 2008). Furthermore, CASC15, a cancer-related long non-coding RNA, was reported to contribute to proliferation and invasion of A549 and H1299 lung cancer cells through regulation of the miR-766-5p / KLK12 axis, thus increasing the expression levels of KLK12 (Bai et al., 2019).


Novel splice variants of the human kallikrein-related peptidases 11 (KLK11) and 12 (KLK12), unraveled by next-generation sequencing technology
Adamopoulos PG, Kontos CK, Scorilas A
Biol Chem 2018 Sep 25;399(9):1065-1071
PMID 29874189
CASC15 contributes to proliferation and invasion through regulating miR-766-5p/ KLK12 axis in lung cancer
Bai Y, Zhang G, Cheng R, Yang R, Chu H
Cell Cycle 2019 Sep;18(18):2323-2331
PMID 31378128
Kallikrein-related peptidases protein expression in lymphoid tissues suggests potential implications in immune response
Filippou PS, Ren AH, Soosaipillai A, Safar R, Prassas I, Diamandis EP, Conner JR
Clin Biochem 2020 Mar;77:41-47
PMID 31904348
Prognostic value of kallikrein-related peptidase 12 (KLK12) mRNA expression in triple-negative breast cancer patients
Gong W, Liu Y, Preis S, Geng X, Petit-Courty A, Kiechle M, Muckenhuber A, Dreyer T, Dorn J, Courty Y, Magdolen V
Mol Med 2020 Feb 7;26(1):19
PMID 32028882
Kallikrein-related peptidase 12 hydrolyzes matricellular proteins of the CCN family and modifies interactions of CCN1 and CCN5 with growth factors
Guillon-Munos A, Oikonomopoulou K, Michel N, Smith CR, Petit-Courty A, Canepa S, Reverdiau P, Heuzé-Vourc'h N, Diamandis EP, Courty Y
J Biol Chem 2011 Jul 22;286(29):25505-18
PMID 21628462
Cleavage activation of human-adapted influenza virus subtypes by kallikrein-related peptidases 5 and 12
Hamilton BS, Whittaker GR
J Biol Chem 2013 Jun 14;288(24):17399-407
PMID 23612974
Inhibition of kallikrein-related peptidases by the serine protease inhibitor of Kazal-type 6
Kantyka T, Fischer J, Wu Z, Declercq W, Reiss K, Schröder JM, Meyer-Hoffert U
Peptides 2011 Jun;32(6):1187-92
PMID 21439340
Angiogenesis stimulated by human kallikrein-related peptidase 12 acting via a platelet-derived growth factor B-dependent paracrine pathway
Kryza T, Achard C, Parent C, Marchand-Adam S, Guillon-Munos A, Iochmann S, Korkmaz B, Respaud R, Courty Y, Heuzé-Vourc'h N
FASEB J 2014 Feb;28(2):740-51
PMID 24225148
Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor
Kryza T, Lalmanach G, Lavergne M, Lecaille F, Reverdiau P, Courty Y, Heuzé-Vourc'h N
Biol Chem 2013 Mar;394(3):385-91
PMID 23152405
Human kallikrein-related peptidase 12 stimulates endothelial cell migration by remodeling the fibronectin matrix
Kryza T, Parent C, Pardessus J, Petit A, Burlaud-Gaillard J, Reverdiau P, Iochmann S, Labas V, Courty Y, Heuzé-Vourc'h N
Sci Rep 2018 Apr 20;8(1):6331
PMID 29679011
A survey of alternative transcripts of human tissue kallikrein genes
Kurlender L, Borgono C, Michael IP, Obiezu C, Elliott MB, Yousef GM, Diamandis EP
Biochim Biophys Acta 2005 May 25;1755(1):1-14
PMID 15878240
Knockdown of KLK12 inhibits viability and induces apoptosis in human colorectal cancer HT-29 cell line
Li Q, Zhou X, Fang Z, Zhou H
Int J Mol Med 2019 Nov;44(5):1667-1676
Kallikrein 12 downregulation reduces AGS gastric cancer cell proliferation and migration
Li XS, He XL
Genet Mol Res 2016 Aug 29;15(3)
PMID 27706634
Common variation in Kallikrein genes KLK5, KLK6, KLK12, and KLK13 and risk of prostate cancer and tumor aggressiveness
Lose F, Batra J, O'Mara T, Fahey P, Marquart L, Eeles RA, Easton DF, Al Olama AA, Kote-Jarai Z, Guy M, Muir K, Lophatananon A, Rahman AA, Neal DE, Hamdy FC, Donovan JL, Chambers S, Gardiner RA, Aitken JF, Yaxley J, Alexander K, Clements JA, Spurdle AB, Kedda MA; Australian Prostate Cancer BioResource
Urol Oncol 2013 Jul;31(5):635-43
PMID 21741862
Enzymatic properties of human kallikrein-related peptidase 12 (KLK12)
Memari N, Jiang W, Diamandis EP, Luo LY
Biol Chem 2007 Apr;388(4):427-35
PMID 17391064
Human kallikrein-related peptidase 12 (KLK12) splice variants discriminate benign from cancerous breast tumors
Papachristopoulou G, Tsapralis N, Michaelidou K, Ardavanis-Loukeris G, Griniatsos I, Scorilas A, Talieri M
Clin Biochem 2018 Aug;58:78-85
PMID 29807016
A multiparametric serum kallikrein panel for diagnosis of non-small cell lung carcinoma
Planque C, Li L, Zheng Y, Soosaipillai A, Reckamp K, Chia D, Diamandis EP, Goodglick L
Clin Cancer Res 2008 Mar 1;14(5):1355-62
PMID 18316555
Splice-site genetic polymorphism of the human kallikrein 12 (KLK12) gene correlates with no substantial expression of KLK12 protein having serine protease activity
Shinmura K, Tao H, Yamada H, Kataoka H, Sanjar R, Wang J, Yoshimura K, Sugimura H
Hum Mutat 2004 Sep;24(3):273-4
PMID 15300858
Human kallikrein-related peptidase 12 (KLK12) splice variants expression in breast cancer and their clinical impact
Talieri M, Devetzi M, Scorilas A, Pappa E, Tsapralis N, Missitzis I, Ardavanis A
Tumour Biol 2012 Aug;33(4):1075-84
PMID 22351561
I-TASSER server: new development for protein structure and function predictions
Yang J, Zhang Y
Nucleic Acids Res 2015 Jul 1;43(W1):W174-81
PMID 25883148
KLK12 is a novel serine protease and a new member of the human kallikrein gene family-differential expression in breast cancer
Yousef GM, Magklara A, Diamandis EP
Genomics 2000 Nov 1;69(3):331-41
PMID 11056051
Clinical significance of human kallikrein 12 gene expression in gastric cancer
Zhao EH, Shen ZY, Liu H, Jin X, Cao H
World J Gastroenterol 2012 Dec 7;18(45):6597-604
PMID 23236234


This paper should be referenced as such :
Paraskevi Karousi, Christos K Kontos, Andreas Scorilas
KLK12 (kallikrein-related peptidase 12)
Atlas Genet Cytogenet Oncol Haematol. 2020;24(12):451-456.
Free journal version : [ pdf ]   [ DOI ]
History of this paper:
Christos K Kontos, Andreas Scorilas. KLK12 (kallikrein-related peptidase 12). Atlas Genet Cytogenet Oncol Haematol. 2017;21(4):130-133.

External links


HGNC (Hugo)KLK12   6360
Entrez_Gene (NCBI)KLK12    kallikrein related peptidase 12
AliasesKLK-L5; KLKL5
GeneCards (Weizmann)KLK12
Ensembl hg19 (Hinxton)ENSG00000186474 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000186474 [Gene_View]  ENSG00000186474 [Sequence]  chr19:51029094-51035002 [Contig_View]  KLK12 [Vega]
ICGC DataPortalENSG00000186474
TCGA cBioPortalKLK12
AceView (NCBI)KLK12
Genatlas (Paris)KLK12
SOURCE (Princeton)KLK12
Genetics Home Reference (NIH)KLK12
Genomic and cartography
GoldenPath hg38 (UCSC)KLK12  -     chr19:51029094-51035002 -  19q13.41   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)KLK12  -     19q13.41   [Description]    (hg19-Feb_2009)
GoldenPathKLK12 - 19q13.41 [CytoView hg19]  KLK12 - 19q13.41 [CytoView hg38]
Genome Data Viewer NCBIKLK12 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AY358524 BC035385 BC136341 BC143988 BC143990
RefSeq transcript (Entrez)NM_001370125 NM_001370126 NM_001370127 NM_001370128 NM_019598 NM_145894 NM_145895
Consensus coding sequences : CCDS (NCBI)KLK12
Gene ExpressionKLK12 [ NCBI-GEO ]   KLK12 [ EBI - ARRAY_EXPRESS ]   KLK12 [ SEEK ]   KLK12 [ MEM ]
Gene Expression Viewer (FireBrowse)KLK12 [ Firebrowse - Broad ]
GenevisibleExpression of KLK12 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)43849
GTEX Portal (Tissue expression)KLK12
Human Protein AtlasENSG00000186474-KLK12 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UKR0   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UKR0  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UKR0
Catalytic activity : Enzyme3.4.21.- [ Enzyme-Expasy ]   3.4.21.-3.4.21.- [ IntEnz-EBI ]   3.4.21.- [ BRENDA ]   3.4.21.- [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)TRYPSIN_DOM (PS50240)    TRYPSIN_HIS (PS00134)    TRYPSIN_SER (PS00135)   
Domains : Interpro (EBI)Peptidase_S1_PA    Peptidase_S1_PA_chymotrypsin    Peptidase_S1A    Trypsin_dom    TRYPSIN_HIS    TRYPSIN_SER   
Domain families : Pfam (Sanger)Trypsin (PF00089)   
Domain families : Pfam (NCBI)pfam00089   
Domain families : Smart (EMBL)Tryp_SPc (SM00020)  
Conserved Domain (NCBI)KLK12
AlphaFold pdb e-kbQ9UKR0   
Human Protein Atlas [tissue]ENSG00000186474-KLK12 [tissue]
Protein Interaction databases
IntAct (EBI)Q9UKR0
Ontologies - Pathways
Ontology : AmiGOserine-type endopeptidase activity  extracellular region  extracellular space  proteolysis  peptidase activity  serine-type peptidase activity  secretory granule  cornification  
Ontology : EGO-EBIserine-type endopeptidase activity  extracellular region  extracellular space  proteolysis  peptidase activity  serine-type peptidase activity  secretory granule  cornification  
REACTOMEQ9UKR0 [protein]
REACTOME PathwaysR-HSA-6809371 [pathway]   
NDEx NetworkKLK12
Atlas of Cancer Signalling NetworkKLK12
Wikipedia pathwaysKLK12
Orthology - Evolution
GeneTree (enSembl)ENSG00000186474
Phylogenetic Trees/Animal Genes : TreeFamKLK12
Homologs : HomoloGeneKLK12
Homology/Alignments : Family Browser (UCSC)KLK12
Gene fusions - Rearrangements
Fusion : QuiverKLK12
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerKLK12 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)KLK12
Exome Variant ServerKLK12
GNOMAD BrowserENSG00000186474
Varsome BrowserKLK12
ACMGKLK12 variants
Genomic Variants (DGV)KLK12 [DGVbeta]
DECIPHERKLK12 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisKLK12 
ICGC Data PortalKLK12 
TCGA Data PortalKLK12 
Broad Tumor PortalKLK12
OASIS PortalKLK12 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICKLK12  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DKLK12
Mutations and Diseases : HGMDKLK12
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)KLK12
DoCM (Curated mutations)KLK12
CIViC (Clinical Interpretations of Variants in Cancer)KLK12
NCG (London)KLK12
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry KLK12
NextProtQ9UKR0 [Medical]
Target ValidationKLK12
Huge Navigator KLK12 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDKLK12
Pharm GKB GenePA30149
Clinical trialKLK12
DataMed IndexKLK12
PubMed31 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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