(data stored in ACNUC3659 zone)

HOVERGEN: KLK2_HUMAN

ID   KLK2_HUMAN              Reviewed;         261 AA.
AC   P20151; Q15946; Q9UJZ9;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-NOV-2009, entry version 102.
DE   RecName: Full=Kallikrein-2;
DE            EC=3.4.21.35;
DE   AltName: Full=Tissue kallikrein-2;
DE   AltName: Full=Glandular kallikrein-1;
DE            Short=hGK-1;
DE   Flags: Precursor;
GN   Name=KLK2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   MEDLINE=88054467; PubMed=2824146;
RA   Schedlich L.J., Bennetts B.H., Morris B.J.;
RT   "Primary structure of a human glandular kallikrein gene.";
RL   DNA 6:429-437(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Prostate;
RX   MEDLINE=92324494; PubMed=1726490; DOI=10.1016/0303-7207(91)90272-T;
RA   Riegman P.H., Vlietstra R.J., der Korput H.A., Romijn J.C.,
RA   Trapman J.;
RT   "Identification and androgen-regulated expression of two major human
RT   glandular kallikrein-1 (hGK-1) mRNA species.";
RL   Mol. Cell. Endocrinol. 76:181-190(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   MEDLINE=20012757; PubMed=10544017; DOI=10.1006/bbrc.1999.1595;
RA   Liu X.F., Essand M., Vasmatzis G., Lee B., Pastan I.;
RT   "Identification of three new alternate human kallikrein 2 transcripts:
RT   evidence of long transcript and alternative splicing.";
RL   Biochem. Biophys. Res. Commun. 264:833-839(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11054574; DOI=10.1016/S0378-1119(00)00382-6;
RA   Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J.,
RA   Moss P., Paeper B., Wang K.;
RT   "Sequencing and expression analysis of the serine protease gene
RT   cluster located in chromosome 19q13 region.";
RL   Gene 257:119-130(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004).
RN   [9]
RP   VARIANT LEU-18.
RX   MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions
RT   of human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [10]
RP   ERRATUM.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
CC   -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds
CC       in kininogen to release Lys-bradykinin.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in
CC       small molecule substrates. Highly selective action to release
CC       kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of
CC       Met-|-Xaa or Leu-|-Xaa.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P20151-1; Sequence=Displayed;
CC       Name=2; Synonyms=PGK-10A;
CC         IsoId=P20151-2; Sequence=VSP_005399;
CC       Name=3;
CC         IsoId=P20151-3; Sequence=VSP_005400;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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CC   -!- GENE_FAMILY: HBG013304 [ FAMILY / ALN / TREE ]
DR   EMBL; M18156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M18157; AAA74454.1; -; Genomic_DNA.
DR   EMBL; S39329; AAD13816.1; -; mRNA.
DR   EMBL; S39329; AAD13817.1; -; mRNA.
DR   EMBL; AF188745; AAF08275.1; -; mRNA.
DR   EMBL; AF188746; AAF08276.1; -; mRNA.
DR   EMBL; AF188747; AAF08277.1; -; mRNA.
DR   EMBL; AF243527; AAG33356.1; -; Genomic_DNA.
DR   EMBL; BT006650; AAP35296.1; -; mRNA.
DR   EMBL; AC037199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005196; AAH05196.1; -; mRNA.
DR   IPI; IPI00022227; -.
DR   IPI; IPI00219231; -.
DR   IPI; IPI00941408; -.
DR   PIR; A29586; A29586.
DR   RefSeq; NP_001002231.1; -.
DR   RefSeq; NP_005542.1; -.
DR   UniGene; Hs.515560; -.
DR   HSSP; P00760; 1EZX.
DR   STRING; P20151; -.
DR   MEROPS; S01.161; -.
DR   PhosphoSite; P20151; -.
DR   PRIDE; P20151; -.
DR   Ensembl; ENST00000325321; ENSP00000313581; ENSG00000167751; Homo sapiens.
DR   Ensembl; ENST00000358049; ENSP00000350748; ENSG00000167751; Homo sapiens.
DR   Ensembl; ENST00000391810; ENSP00000375686; ENSG00000167751; Homo sapiens.
DR   Ensembl; ENST00000423722; ENSP00000395423; ENSG00000167751; Homo sapiens.
DR   GeneID; 3817; -.
DR   KEGG; hsa:3817; -.
DR   UCSC; uc002ptu.1; human.
DR   UCSC; uc002ptv.1; human.
DR   CTD; 3817; -.
DR   GeneCards; GC19P056068; -.
DR   H-InvDB; HIX0015370; -.
DR   HGNC; HGNC:6363; KLK2.
DR   HPA; HPA000764; -.
DR   MIM; 147960; gene.
DR   PharmGKB; PA30152; -.
DR   HOGENOM; P20151; -.
DR   HOVERGEN; P20151; -.
DR   OMA; AYSEKVT; -.
DR   BRENDA; 3.4.21.35; 247.
DR   Pathway_Interaction_DB; ar_pathway; Coregulation of Androgen receptor activity.
DR   Pathway_Interaction_DB; ar_tf_pathway; Regulation of Androgen receptor activity.
DR   NextBio; 15005; -.
DR   PMAP-CutDB; P20151; -.
DR   ArrayExpress; P20151; -.
DR   Bgee; P20151; -.
DR   CleanEx; HS_KLK2; -.
DR   Genevestigator; P20151; -.
DR   GermOnline; ENSG00000167751; Homo sapiens.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P20151.
DR   SWISS-2DPAGE; P20151.
KW   Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Polymorphism; Protease; Serine protease; Signal; Zymogen.
FT   DOMAIN        4     65       PRODOM:2005.1:PD474467  1445
FT   DOMAIN       66    118       PRODOM:2005.1:PD697704  47
FT   DOMAIN      168    200       PRODOM:2005.1:PD251054  232
FT   DOMAIN      204    255       PRODOM:2005.1:PD000068  1525
FT   SIGNAL        1     18       Probable.
FT   PROPEP       19     24       Activation peptide (Probable).
FT                                /FTId=PRO_0000027929.
FT   CHAIN        25    261       Kallikrein-2.
FT                                /FTId=PRO_0000027930.
FT   DOMAIN       25    258       Peptidase S1.
FT   ACT_SITE     65     65       Charge relay system.
FT   ACT_SITE    120    120       Charge relay system.
FT   ACT_SITE    213    213       Charge relay system.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
FT   DISULFID     31    173       By similarity.
FT   DISULFID     50     66       By similarity.
FT   DISULFID    152    219       By similarity.
FT   DISULFID    184    198       By similarity.
FT   DISULFID    209    234       By similarity.
FT   VAR_SEQ     165    261       Missing (in isoform 3).
FT                                /FTId=VSP_005400.
FT   VAR_SEQ     211    261       GDSGGPLVCNGVLQGITSWGPEPCALPEKPAVYTKVVHYRK
FT                                WIKDTIAANP -> VSHPYSQHLEGK (in isoform
FT                                2).
FT                                /FTId=VSP_005399.
FT   VARIANT      18     18       V -> L (in dbSNP:rs6072).
FT                                /FTId=VAR_014164.
FT   VARIANT     250    250       R -> W (in dbSNP:rs198977).
FT                                /FTId=VAR_020178.
SQ   SEQUENCE   261 AA;  28671 MW;  9CF7F4A1162EF42D CRC64;
     MWDLVLSIAL SVGCTGAVPL IQSRIVGGWE CEKHSQPWQV AVYSHGWAHC GGVLVHPQWV
     LTAAHCLKKN SQVWLGRHNL FEPEDTGQRV PVSHSFPHPL YNMSLLKHQS LRPDEDSSHD
     LMLLRLSEPA KITDVVKVLG LPTQEPALGT TCYASGWGSI EPEEFLRPRS LQCVSLHLLS
     NDMCARAYSE KVTEFMLCAG LWTGGKDTCG GDSGGPLVCN GVLQGITSWG PEPCALPEKP
     AVYTKVVHYR KWIKDTIAAN P
//

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