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Protein

Kallikrein-2

Gene

KLK2

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 sitei213 – 2131Charge relay system

GO - Molecular functioni

  • serine-type endopeptidase activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

Protein family/group databases

MEROPSiS01.161.

Names & Taxonomyi

Protein namesi
Recommended name:
Kallikrein-2 (EC:3.4.21.35)
Alternative name(s):
Glandular kallikrein-1
Short name:
hGK-1
Tissue kallikrein-2
Gene namesi
Name:KLK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6363. KLK2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • intracellular Source: GOC
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30152.

Polymorphism and mutation databases

BioMutaiKLK2.
DMDMi125174.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818CuratedAdd
BLAST
Propeptidei19 – 246Activation peptideCuratedPRO_0000027929
Chaini25 – 261237Kallikrein-2PRO_0000027930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 173PROSITE-ProRule annotation
Disulfide bondi50 ↔ 66PROSITE-ProRule annotation
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi152 ↔ 219PROSITE-ProRule annotation
Disulfide bondi184 ↔ 198PROSITE-ProRule annotation
Disulfide bondi209 ↔ 234PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP20151.
PaxDbiP20151.
PRIDEiP20151.

PTM databases

PhosphoSiteiP20151.

Miscellaneous databases

PMAP-CutDBP20151.

Expressioni

Gene expression databases

BgeeiP20151.
CleanExiHS_KLK2.
ExpressionAtlasiP20151. baseline and differential.
GenevisibleiP20151. HS.

Organism-specific databases

HPAiHPA000764.

Interactioni

Protein-protein interaction databases

BioGridi110017. 10 interactions.
STRINGi9606.ENSP00000313581.

Structurei

Secondary structure

1
261
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 strandi72 – 765Combined sources
Beta strandi88 – 9710Combined sources
Helixi103 – 1053Combined sources
Beta strandi122 – 1287Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi151 – 1588Combined sources
Beta strandi160 – 1645Combined sources
Beta strandi172 – 1798Combined sources
Helixi181 – 1877Combined sources
Beta strandi196 – 2005Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi222 – 2298Combined sources
Beta strandi241 – 2455Combined sources
Helixi246 – 2494Combined sources
Helixi250 – 25910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NFEX-ray1.90A25-261[»]
4NFFX-ray1.90A25-261[»]
ProteinModelPortaliP20151.
SMRiP20151. Positions 25-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 258234Peptidase 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.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP20151.
KOiK01325.
OMAiVHYQKWI.
PhylomeDBiP20151.
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P20151-1) [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
MWDLVLSIAL SVGCTGAVPL IQSRIVGGWE CEKHSQPWQV AVYSHGWAHC
60 70 80 90 100
GGVLVHPQWV LTAAHCLKKN SQVWLGRHNL FEPEDTGQRV PVSHSFPHPL
110 120 130 140 150
YNMSLLKHQS LRPDEDSSHD LMLLRLSEPA KITDVVKVLG LPTQEPALGT
160 170 180 190 200
TCYASGWGSI EPEEFLRPRS LQCVSLHLLS NDMCARAYSE KVTEFMLCAG
210 220 230 240 250
LWTGGKDTCG GDSGGPLVCN GVLQGITSWG PEPCALPEKP AVYTKVVHYR
260
KWIKDTIAAN P
Length:261
Mass (Da):28,671
Last modified:February 1, 1991 - v1
Checksum:i9CF7F4A1162EF42D
GO
Isoform 2 (identifier: P20151-2) [UniParc]FASTAAdd to basket

Also known as: PGK-10A

The sequence of this isoform differs from the canonical sequence as follows:
     211-261: GDSGGPLVCNGVLQGITSWGPEPCALPEKPAVYTKVVHYRKWIKDTIAANP → VSHPYSQHLEGKG

Show »
Length:223
Mass (Da):24,674
Checksum:i051F76900C2AFEA9
GO
Isoform 3 (identifier: P20151-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-261: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:164
Mass (Da):18,162
Checksum:i00D2AE5561DB788E
GO
Isoform 4 (identifier: P20151-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.

Note: No experimental confirmation available.
Show »
Length:159
Mass (Da):17,301
Checksum:iB978EFD702D36903
GO

Sequence cautioni

The sequence AAD13817.1 differs from that shown.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431T → A in BAG62255 (PubMed:14702039).Curated
Isoform 2 (identifier: P20151-2)
Sequence conflicti223 – 2231G → GE in BAG62272 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181V → L.1 Publication
Corresponds to variant rs6072 [ dbSNP | Ensembl ].
VAR_014164
Natural varianti250 – 2501R → W.
Corresponds to variant rs198977 [ dbSNP | Ensembl ].
VAR_020178
Natural varianti255 – 2551D → A.
Corresponds to variant rs60268688 [ dbSNP | Ensembl ].
VAR_061775

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 102102Missing in isoform 4. 1 PublicationVSP_044709Add
BLAST
Alternative sequencei165 – 26197Missing in isoform 3. CuratedVSP_005400Add
BLAST
Alternative sequencei211 – 26151GDSGG…IAANP → VSHPYSQHLEGKG in isoform 2. 2 PublicationsVSP_005399Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18156 Genomic DNA. No translation available.
M18157 Genomic DNA. Translation: AAA74454.1.
S39329 mRNA. Translation: AAD13816.1.
S39329 mRNA. Translation: AAD13817.1. Sequence problems.
AF188745 mRNA. Translation: AAF08275.1.
AF188746 mRNA. Translation: AAF08276.1.
AF188747 mRNA. Translation: AAF08277.1.
AF243527 Genomic DNA. Translation: AAG33356.1.
BT006650 mRNA. Translation: AAP35296.1.
AK300549 mRNA. Translation: BAG62255.1.
AK300566 mRNA. Translation: BAG62272.1.
AC037199 Genomic DNA. No translation available.
BC005196 mRNA. Translation: AAH05196.1.
CCDSiCCDS12808.1. [P20151-1]
CCDS42597.1. [P20151-2]
CCDS58675.1. [P20151-4]
PIRiA29586.
RefSeqiNP_001002231.1. NM_001002231.2. [P20151-2]
NP_001243009.1. NM_001256080.1. [P20151-4]
NP_005542.1. NM_005551.4. [P20151-1]
XP_006723272.1. XM_006723209.2. [P20151-3]
UniGeneiHs.515560.

Genome annotation databases

EnsembliENST00000325321; ENSP00000313581; ENSG00000167751. [P20151-1]
ENST00000358049; ENSP00000350748; ENSG00000167751. [P20151-2]
ENST00000391810; ENSP00000375686; ENSG00000167751. [P20151-4]
ENST00000597439; ENSP00000471214; ENSG00000167751. [P20151-3]
GeneIDi3817.
KEGGihsa:3817.
UCSCiuc002ptu.3. human. [P20151-2]
uc002ptv.3. human. [P20151-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18156 Genomic DNA. No translation available.
M18157 Genomic DNA. Translation: AAA74454.1.
S39329 mRNA. Translation: AAD13816.1.
S39329 mRNA. Translation: AAD13817.1. Sequence problems.
AF188745 mRNA. Translation: AAF08275.1.
AF188746 mRNA. Translation: AAF08276.1.
AF188747 mRNA. Translation: AAF08277.1.
AF243527 Genomic DNA. Translation: AAG33356.1.
BT006650 mRNA. Translation: AAP35296.1.
AK300549 mRNA. Translation: BAG62255.1.
AK300566 mRNA. Translation: BAG62272.1.
AC037199 Genomic DNA. No translation available.
BC005196 mRNA. Translation: AAH05196.1.
CCDSiCCDS12808.1. [P20151-1]
CCDS42597.1. [P20151-2]
CCDS58675.1. [P20151-4]
PIRiA29586.
RefSeqiNP_001002231.1. NM_001002231.2. [P20151-2]
NP_001243009.1. NM_001256080.1. [P20151-4]
NP_005542.1. NM_005551.4. [P20151-1]
XP_006723272.1. XM_006723209.2. [P20151-3]
UniGeneiHs.515560.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NFEX-ray1.90A25-261[»]
4NFFX-ray1.90A25-261[»]
ProteinModelPortaliP20151.
SMRiP20151. Positions 25-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110017. 10 interactions.
STRINGi9606.ENSP00000313581.

Chemistry

BindingDBiP20151.
ChEMBLiCHEMBL2442.

Protein family/group databases

MEROPSiS01.161.

PTM databases

PhosphoSiteiP20151.

Polymorphism and mutation databases

BioMutaiKLK2.
DMDMi125174.

Proteomic databases

MaxQBiP20151.
PaxDbiP20151.
PRIDEiP20151.

Protocols and materials databases

DNASUi3817.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325321; ENSP00000313581; ENSG00000167751. [P20151-1]
ENST00000358049; ENSP00000350748; ENSG00000167751. [P20151-2]
ENST00000391810; ENSP00000375686; ENSG00000167751. [P20151-4]
ENST00000597439; ENSP00000471214; ENSG00000167751. [P20151-3]
GeneIDi3817.
KEGGihsa:3817.
UCSCiuc002ptu.3. human. [P20151-2]
uc002ptv.3. human. [P20151-1]

Organism-specific databases

CTDi3817.
GeneCardsiGC19P051369.
HGNCiHGNC:6363. KLK2.
HPAiHPA000764.
MIMi147960. gene.
neXtProtiNX_P20151.
PharmGKBiPA30152.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP20151.
KOiK01325.
OMAiVHYQKWI.
PhylomeDBiP20151.
TreeFamiTF331065.

Enzyme and pathway databases

ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

Miscellaneous databases

ChiTaRSiKLK2. human.
GenomeRNAii3817.
NextBioi15005.
PMAP-CutDBP20151.
PROiP20151.
SOURCEiSearch...

Gene expression databases

BgeeiP20151.
CleanExiHS_KLK2.
ExpressionAtlasiP20151. baseline and differential.
GenevisibleiP20151. 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. "Primary structure of a human glandular kallikrein gene."
    Schedlich L.J., Bennetts B.H., Morris B.J.
    DNA 6:429-437(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "Identification and androgen-regulated expression of two major human glandular kallikrein-1 (hGK-1) mRNA species."
    Riegman P.H., Vlietstra R.J., der Korput H.A., Romijn J.C., Trapman J.
    Mol. Cell. Endocrinol. 76:181-190(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Prostate.
  3. "Identification of three new alternate human kallikrein 2 transcripts: evidence of long transcript and alternative splicing."
    Liu X.F., Essand M., Vasmatzis G., Lee B., Pastan I.
    Biochem. Biophys. Res. Commun. 264:833-839(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  4. "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].
  5. "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).
  6. "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] (ISOFORMS 2 AND 4).
    Tissue: Prostate.
  7. "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].
  8. "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: Prostate.
  9. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  10. Cited for: VARIANT LEU-18.

Entry informationi

Entry nameiKLK2_HUMAN
AccessioniPrimary (citable) accession number: P20151
Secondary accession number(s): B4DU93
, B4DUB0, F5H8L3, Q15946, Q9UJZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 24, 2015
This is version 157 of the entry and version 1 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, 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.