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Protein

Kallikrein-1

Gene

KLK1

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

Functioni

Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.

Catalytic activityi

Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Charge relay system
Active sitei120 – 1201Charge relay system
Active sitei214 – 2141Charge relay system

GO - Molecular functioni

  • serine-type endopeptidase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.35. 2681.
ReactomeiREACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Names & Taxonomyi

Protein namesi
Recommended name:
Kallikrein-1 (EC:3.4.21.35)
Alternative name(s):
Kidney/pancreas/salivary gland kallikrein
Tissue kallikrein
Gene namesi
Name:KLK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6357. KLK1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

MIMi615953. phenotype.
PharmGKBiPA224.

Chemistry

DrugBankiDB06692. Aprotinin.

Polymorphism and mutation databases

BioMutaiKLK1.
DMDMi269849612.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818CuratedAdd
BLAST
Propeptidei19 – 246Activation peptideCuratedPRO_0000027923
Chaini25 – 262238Kallikrein-1PRO_0000027924Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 174PROSITE-ProRule annotation1 Publication
Disulfide bondi50 ↔ 66PROSITE-ProRule annotation1 Publication
Glycosylationi93 – 931O-linked (GalNAc...)1 Publication
Glycosylationi102 – 1021N-linked (GlcNAc...)1 Publication
Glycosylationi104 – 1041O-linked (GalNAc...)1 Publication
Glycosylationi108 – 1081N-linked (GlcNAc...)2 Publications
Disulfide bondi153 ↔ 220PROSITE-ProRule annotation1 Publication
Glycosylationi165 – 1651N-linked (GlcNAc...); partial1 Publication
Glycosylationi167 – 1671O-linked (GalNAc...)1 Publication
Disulfide bondi185 ↔ 199PROSITE-ProRule annotation1 Publication
Disulfide bondi210 ↔ 235PROSITE-ProRule annotation1 Publication

Post-translational modificationi

The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167 are probably the mucin type linked to GalNAc. In PubMed:3163150, GalNAc was detected with the corresponding peptides but not located.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP06870.
PRIDEiP06870.

PTM databases

UniCarbKBiP06870.

Expressioni

Tissue specificityi

Isoform 2 is expressed in pancreas, salivary glands, kidney, colon, prostate gland, testis, spleen and the colon adenocarcinoma cell line T84.1 Publication

Gene expression databases

BgeeiP06870.
CleanExiHS_KLK1.
ExpressionAtlasiP06870. baseline and differential.
GenevisibleiP06870. HS.

Interactioni

Protein-protein interaction databases

BioGridi110016. 1 interaction.
STRINGi9606.ENSP00000301420.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 446Combined sources
Beta strandi47 – 5610Combined sources
Beta strandi59 – 624Combined sources
Helixi64 – 663Combined sources
Beta strandi69 – 768Combined sources
Beta strandi88 – 903Combined sources
Beta strandi92 – 976Combined sources
Helixi103 – 1064Combined sources
Turni112 – 1143Combined sources
Beta strandi122 – 1287Combined sources
Beta strandi152 – 1598Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi173 – 1808Combined sources
Helixi182 – 1887Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi223 – 2308Combined sources
Beta strandi242 – 2465Combined sources
Helixi247 – 2504Combined sources
Helixi251 – 26010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SPJX-ray1.70A25-262[»]
ProteinModelPortaliP06870.
SMRiP06870. Positions 25-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06870.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 259235Peptidase 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.
HOVERGENiHBG013304.
InParanoidiP06870.
KOiK01325.
OMAiLWLGRHN.
PhylomeDBiP06870.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P06870-1) [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
MWFLVLCLAL SLGGTGAAPP IQSRIVGGWE CEQHSQPWQA ALYHFSTFQC
60 70 80 90 100
GGILVHRQWV LTAAHCISDN YQLWLGRHNL FDDENTAQFV HVSESFPHPG
110 120 130 140 150
FNMSLLENHT RQADEDYSHD LMLLRLTEPA DTITDAVKVV ELPTEEPEVG
160 170 180 190 200
STCLASGWGS IEPENFSFPD DLQCVDLKIL PNDECKKAHV QKVTDFMLCV
210 220 230 240 250
GHLEGGKDTC VGDSGGPLMC DGVLQGVTSW GYVPCGTPNK PSVAVRVLSY
260
VKWIEDTIAE NS
Length:262
Mass (Da):28,890
Last modified:November 24, 2009 - v2
Checksum:i7D8A715E9E104D60
GO
Isoform 2 (identifier: P06870-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MWFLVLCLAL...VLTAAHCISD → MLPCPIPFSPSRLLIPPFPSFPS

Show »
Length:216
Mass (Da):23,835
Checksum:i8FD0C1CEB83D6750
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141D → N in AAU12569 (Ref. 7) Curated
Sequence conflicti139 – 1391V → F in AAU12569 (Ref. 7) Curated
Sequence conflicti188 – 1881A → V in AAP35917 (Ref. 8) Curated
Sequence conflicti188 – 1881A → V in AAH05313 (PubMed:15489334).Curated

Polymorphismi

Genetic variations in KLK1 are the cause of a decreased in urinary kallikrein activity [MIMi:615953]. The His-77 mutation dramatically reduces the activity of the enzyme in the urine. There is a 50 to 60% reduction in urinary kallikrein activity in His-77 individuals, but renal and hormonal adaptation to dietary changes in sodium and potassium are unaffected. However, in studies of brachial artery function, His-77 individuals consistently exhibited an increase in wall shear stress and a paradoxical reduction in artery diameter and lumen compared to Arg-77 individuals. This partial genetic deficiency in kallikrein activity is associated with a form of arterial dysfunction involving inappropriate inward remodeling of the brachial artery despite a chronic increase in shear stress.2 Publications

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771R → H Polymorphism; associated with a significant decrease in urinary kallikrein activity. 1 Publication
Corresponds to variant rs5515 [ dbSNP | Ensembl ].
VAR_014567
Natural varianti145 – 1451E → Q Polymorphism; not associated with changes in urinary kallikrein activity. 8 Publications
Corresponds to variant rs5516 [ dbSNP | Ensembl ].
VAR_006625
Natural varianti186 – 1861K → E.3 Publications
Corresponds to variant rs5517 [ dbSNP | Ensembl ].
VAR_006626
Natural varianti193 – 1931V → E.
Corresponds to variant rs5518 [ dbSNP | Ensembl ].
VAR_014568

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6969MWFLV…HCISD → MLPCPIPFSPSRLLIPPFPS FPS in isoform 2. 1 PublicationVSP_037483Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25629 mRNA. Translation: AAA36136.1.
M33109
, M33105, M33106, M33107, M33108 Genomic DNA. Translation: AAA59455.1.
X13561 mRNA. Translation: CAA31912.1.
AF277050 Genomic DNA. Translation: AAF86333.1.
AF243527 Genomic DNA. Translation: AAG33353.1.
AY703451 mRNA. Translation: AAU12569.1.
BT007253 mRNA. Translation: AAP35917.1.
AY094609 Genomic DNA. Translation: AAM11874.1.
AC010325 Genomic DNA. No translation available.
BC005313 mRNA. Translation: AAH05313.1.
M12706 mRNA. Translation: AAA59201.1.
CCDSiCCDS12804.1. [P06870-1]
PIRiA24696. KQHU.
B24696.
RefSeqiNP_002248.1. NM_002257.3. [P06870-1]
UniGeneiHs.123107.

Genome annotation databases

EnsembliENST00000301420; ENSP00000301420; ENSG00000167748.
GeneIDi3816.
KEGGihsa:3816.
UCSCiuc002ptk.1. human. [P06870-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Kallikrein entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25629 mRNA. Translation: AAA36136.1.
M33109
, M33105, M33106, M33107, M33108 Genomic DNA. Translation: AAA59455.1.
X13561 mRNA. Translation: CAA31912.1.
AF277050 Genomic DNA. Translation: AAF86333.1.
AF243527 Genomic DNA. Translation: AAG33353.1.
AY703451 mRNA. Translation: AAU12569.1.
BT007253 mRNA. Translation: AAP35917.1.
AY094609 Genomic DNA. Translation: AAM11874.1.
AC010325 Genomic DNA. No translation available.
BC005313 mRNA. Translation: AAH05313.1.
M12706 mRNA. Translation: AAA59201.1.
CCDSiCCDS12804.1. [P06870-1]
PIRiA24696. KQHU.
B24696.
RefSeqiNP_002248.1. NM_002257.3. [P06870-1]
UniGeneiHs.123107.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SPJX-ray1.70A25-262[»]
ProteinModelPortaliP06870.
SMRiP06870. Positions 25-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110016. 1 interaction.
STRINGi9606.ENSP00000301420.

Chemistry

BindingDBiP06870.
ChEMBLiCHEMBL2319.
DrugBankiDB06692. Aprotinin.

PTM databases

UniCarbKBiP06870.

Polymorphism and mutation databases

BioMutaiKLK1.
DMDMi269849612.

Proteomic databases

PaxDbiP06870.
PRIDEiP06870.

Protocols and materials databases

DNASUi3816.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301420; ENSP00000301420; ENSG00000167748.
GeneIDi3816.
KEGGihsa:3816.
UCSCiuc002ptk.1. human. [P06870-1]

Organism-specific databases

CTDi3816.
GeneCardsiGC19M051322.
HGNCiHGNC:6357. KLK1.
MIMi147910. gene.
615953. phenotype.
neXtProtiNX_P06870.
PharmGKBiPA224.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOVERGENiHBG013304.
InParanoidiP06870.
KOiK01325.
OMAiLWLGRHN.
PhylomeDBiP06870.
TreeFamiTF331065.

Enzyme and pathway databases

BRENDAi3.4.21.35. 2681.
ReactomeiREACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

ChiTaRSiKLK1. human.
EvolutionaryTraceiP06870.
GeneWikiiKLK1.
GenomeRNAii3816.
NextBioi15001.
PROiP06870.
SOURCEiSearch...

Gene expression databases

BgeeiP06870.
CleanExiHS_KLK1.
ExpressionAtlasiP06870. baseline and differential.
GenevisibleiP06870. 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. "Nucleotide sequence of cloned cDNA for human pancreatic kallikrein."
    Fukushima D., Kitamura N., Nakanishi S.
    Biochemistry 24:8037-8043(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-145 AND GLU-186.
    Tissue: Pancreas.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-145.
    Tissue: Kidney.
  3. "Cloning and expression of human salivary-gland kallikrein in Escherichia coli."
    Angermann A., Bergmann C., Appelhans H.
    Biochem. J. 262:787-793(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Salivary gland.
  4. "Molecular cloning and characterization of a novel kallikrein transcript in colon and its distribution in human tissues."
    Chen L.-M., Murray S.R., Chai K.X., Chao L., Chao J.
    Braz. J. Med. Biol. Res. 27:1829-1838(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  5. "Genomic organization of the human kallikrein gene family on chromosome 19q13.3-q13.4."
    Yousef G.M., Chang A., Scorilas A., Diamandis E.P.
    Biochem. Biophys. Res. Commun. 276:125-133(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "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].
  7. "Kallikrein cDNA from the pancreas of a Chinese patient."
    Li T., Du G., Dai Y.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-145 AND GLU-186.
  8. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-145.
  9. SeattleSNPs variation discovery resource
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-145.
  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. "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), VARIANT GLN-145.
    Tissue: Pancreas.
  12. "Human kidney kallikrein: cDNA cloning and sequence analysis."
    Baker A.R., Shine J.
    DNA 4:445-450(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-262 (ISOFORM 1), VARIANTS GLN-145 AND GLU-186.
    Tissue: Kidney.
  13. "Human urinary kallikrein -- amino acid sequence and carbohydrate attachment sites."
    Kellermann J., Lottspeich F., Geiger R., Deutzmann R.
    Protein Seq. Data Anal. 1:177-182(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-262 (ISOFORM 1), GLYCOSYLATION AT SER-93; ASN-102; SER-104; ASN-108; ASN-165 AND SER-167.
    Tissue: Urine.
  14. "Human urinary kallikrein. Complete amino acid sequence and sites of glycosylation."
    Lu H.S., Lin F.-K., Chao L., Chao J.
    Int. J. Pept. Protein Res. 33:237-249(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-262 (ISOFORM 1).
    Tissue: Urine.
  15. "N-terminal amino acid sequence of human urinary kallikrein homology with other serine proteases."
    Lottspeich F., Geiger R., Henschen A., Kutzbach C.
    Hoppe-Seyler's Z. Physiol. Chem. 360:1947-1950(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-55 (ISOFORM 1).
    Tissue: Urine.
  16. "N-terminal amino acid sequence of human urinary prokallikrein."
    Takahashi S., Irie A., Katayama Y., Ito K., Miyake Y.
    J. Biochem. 99:989-992(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-47 (ISOFORM 1).
    Tissue: Urine.
  17. "1.70 A X-ray structure of human apo kallikrein 1: structural changes upon peptide inhibitor/substrate binding."
    Laxmikanthan G., Blaber S.I., Bernett M.J., Scarisbrick I.A., Juliano M.A., Blaber M.
    Proteins 58:802-814(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-262, GLYCOSYLATION AT ASN-108, DISULFIDE BONDS.
  18. "Loss-of-function polymorphism of the human kallikrein gene with reduced urinary kallikrein activity."
    Slim R., Torremocha F., Moreau T., Pizard A., Hunt S.C., Vuagnat A., Williams G.H., Gauthier F., Jeunemaitre X., Alhenc-Gelas F.
    J. Am. Soc. Nephrol. 13:968-976(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS HIS-77 AND GLN-145, POLYMORPHISM.
  19. "Arterial and renal consequences of partial genetic deficiency in tissue kallikrein activity in humans."
    Azizi M., Boutouyrie P., Bissery A., Agharazii M., Verbeke F., Stern N., Bura-Riviere A., Laurent S., Alhenc-Gelas F., Jeunemaitre X.
    J. Clin. Invest. 115:780-787(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM.

Entry informationi

Entry nameiKLK1_HUMAN
AccessioniPrimary (citable) accession number: P06870
Secondary accession number(s): Q66US9
, Q86U61, Q8TCV8, Q9BS53, Q9NQU4, Q9UD19, Q9UMJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 24, 2009
Last modified: July 22, 2015
This is version 168 of the entry and version 2 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.