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Q9Y337

- KLK5_HUMAN

UniProt

Q9Y337 - KLK5_HUMAN

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Protein

Kallikrein-5

Gene
KLK5, SCTE, UNQ570/PRO1132
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in desquamation.

Enzyme regulationi

Inhibited by Zn2+.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081Charge relay system1 Publication
Sitei150 – 1501Major binding site for inhibitory zinc
Active sitei153 – 1531Charge relay system1 Publication
Active sitei245 – 2451Charge relay system1 Publication

GO - Molecular functioni

  1. peptidase activity Source: ProtInc
  2. protein binding Source: UniProtKB
  3. serine-type endopeptidase activity Source: UniProtKB
  4. serine-type peptidase activity Source: ProtInc

GO - Biological processi

  1. epidermis development Source: ProtInc
  2. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Kallikrein-5 (EC:3.4.21.-)
Alternative name(s):
Kallikrein-like protein 2
Short name:
KLK-L2
Stratum corneum tryptic enzyme
Gene namesi
Name:KLK5
Synonyms:SCTE
ORF Names:UNQ570/PRO1132
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:6366. KLK5.

Subcellular locationi

GO - Cellular componenti

  1. epidermal lamellar body Source: UniProtKB
  2. extracellular space Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30155.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed predictionAdd
BLAST
Chaini23 – 293271Kallikrein-5PRO_0000027939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi69 – 691N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi73 ↔ 2061 Publication
Disulfide bondi93 ↔ 1091 Publication
Glycosylationi173 – 1731N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi178 ↔ 2791 Publication
Disulfide bondi185 ↔ 2511 Publication
Glycosylationi208 – 2081N-linked (GlcNAc...)1 Publication
Disulfide bondi217 ↔ 2311 Publication
Disulfide bondi241 ↔ 2661 Publication
Glycosylationi252 – 2521N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y337.
PRIDEiQ9Y337.

PTM databases

PhosphoSiteiQ9Y337.

Miscellaneous databases

PMAP-CutDBQ9Y337.

Expressioni

Tissue specificityi

Expressed in skin, breast, brain and testis. Expressed at the stratum granulosum of palmar skin.1 Publication

Gene expression databases

ArrayExpressiQ9Y337.
BgeeiQ9Y337.
CleanExiHS_KLK5.
GenevestigatoriQ9Y337.

Organism-specific databases

HPAiCAB025503.
CAB026341.
HPA014343.

Interactioni

Subunit structurei

Interacts with SPINK9.1 Publication

Protein-protein interaction databases

BioGridi117346. 1 interaction.
STRINGi9606.ENSP00000337733.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi81 – 866
Turni87 – 893
Beta strandi90 – 9910
Beta strandi102 – 1054
Helixi107 – 1093
Beta strandi115 – 1195
Beta strandi122 – 1243
Beta strandi132 – 14110
Beta strandi147 – 1493
Beta strandi155 – 1617
Beta strandi167 – 1693
Beta strandi184 – 1918
Beta strandi193 – 1975
Beta strandi205 – 2117
Helixi214 – 2207
Turni222 – 2243
Beta strandi229 – 2324
Beta strandi248 – 2514
Beta strandi254 – 2618
Beta strandi273 – 2775
Helixi278 – 2803
Helixi282 – 29110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PSXX-ray2.30A67-293[»]
2PSYX-ray2.30A67-293[»]
ProteinModelPortaliQ9Y337.
SMRiQ9Y337. Positions 35-293.

Miscellaneous databases

EvolutionaryTraceiQ9Y337.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 290224Peptidase S1Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiQ9Y337.
KOiK09617.
OMAiAAHCRKK.
OrthoDBiEOG75B84T.
PhylomeDBiQ9Y337.
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]

Sequencei

Sequence statusi: Complete.

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

Q9Y337-1 [UniParc]FASTAAdd to Basket

« Hide

MATARPPWMW VLCALITALL LGVTEHVLAN NDVSCDHPSN TVPSGSNQDL    50
GAGAGEDARS DDSSSRIING SDCDMHTQPW QAALLLRPNQ LYCGAVLVHP 100
QWLLTAAHCR KKVFRVRLGH YSLSPVYESG QQMFQGVKSI PHPGYSHPGH 150
SNNLMLIKLN RRIRPTKDVR PINVSSHCPS AGTKCLVSGW GTTKSPQVHF 200
PKVLQCLNIS VLSQKRCEDA YPRQIDDTMF CAGDKAGRDS CQGDSGGPVV 250
CNGSLQGLVS WGDYPCARPN RPGVYTNLCK FTKWIQETIQ ANS 293
Length:293
Mass (Da):32,019
Last modified:May 18, 2010 - v2
Checksum:iD92C9F98055131E4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551G → R.
Corresponds to variant rs2232532 [ dbSNP | Ensembl ].
VAR_051853
Natural varianti153 – 1531N → D.8 Publications
Corresponds to variant rs183854 [ dbSNP | Ensembl ].
VAR_051854

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 5632Missing in AAG33358. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF168768 mRNA. Translation: AAF03101.1.
AF135028 Genomic DNA. Translation: AAD26429.1.
AF243527 Genomic DNA. Translation: AAG33358.1.
AY279380 mRNA. Translation: AAP42275.1.
AY279381 mRNA. Translation: AAP42276.1.
AY359010 mRNA. Translation: AAQ89369.1.
BT006867 mRNA. Translation: AAP35513.1.
AC011483 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW71946.1.
BC008036 mRNA. Translation: AAH08036.1.
CCDSiCCDS12810.1.
RefSeqiNP_001070959.1. NM_001077491.1.
NP_001070960.1. NM_001077492.1.
NP_036559.1. NM_012427.4.
UniGeneiHs.50915.

Genome annotation databases

EnsembliENST00000336334; ENSP00000337733; ENSG00000167754.
ENST00000391809; ENSP00000375685; ENSG00000167754.
ENST00000593428; ENSP00000471966; ENSG00000167754.
GeneIDi25818.
KEGGihsa:25818.
UCSCiuc002pue.3. human.

Polymorphism databases

DMDMi296434569.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF168768 mRNA. Translation: AAF03101.1 .
AF135028 Genomic DNA. Translation: AAD26429.1 .
AF243527 Genomic DNA. Translation: AAG33358.1 .
AY279380 mRNA. Translation: AAP42275.1 .
AY279381 mRNA. Translation: AAP42276.1 .
AY359010 mRNA. Translation: AAQ89369.1 .
BT006867 mRNA. Translation: AAP35513.1 .
AC011483 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW71946.1 .
BC008036 mRNA. Translation: AAH08036.1 .
CCDSi CCDS12810.1.
RefSeqi NP_001070959.1. NM_001077491.1.
NP_001070960.1. NM_001077492.1.
NP_036559.1. NM_012427.4.
UniGenei Hs.50915.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PSX X-ray 2.30 A 67-293 [» ]
2PSY X-ray 2.30 A 67-293 [» ]
ProteinModelPortali Q9Y337.
SMRi Q9Y337. Positions 35-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117346. 1 interaction.
STRINGi 9606.ENSP00000337733.

Chemistry

ChEMBLi CHEMBL4447.

Protein family/group databases

MEROPSi S01.017.

PTM databases

PhosphoSitei Q9Y337.

Polymorphism databases

DMDMi 296434569.

Proteomic databases

PaxDbi Q9Y337.
PRIDEi Q9Y337.

Protocols and materials databases

DNASUi 25818.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336334 ; ENSP00000337733 ; ENSG00000167754 .
ENST00000391809 ; ENSP00000375685 ; ENSG00000167754 .
ENST00000593428 ; ENSP00000471966 ; ENSG00000167754 .
GeneIDi 25818.
KEGGi hsa:25818.
UCSCi uc002pue.3. human.

Organism-specific databases

CTDi 25818.
GeneCardsi GC19M051446.
HGNCi HGNC:6366. KLK5.
HPAi CAB025503.
CAB026341.
HPA014343.
MIMi 605643. gene.
neXtProti NX_Q9Y337.
PharmGKBi PA30155.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi Q9Y337.
KOi K09617.
OMAi AAHCRKK.
OrthoDBi EOG75B84T.
PhylomeDBi Q9Y337.
TreeFami TF331065.

Miscellaneous databases

EvolutionaryTracei Q9Y337.
GeneWikii KLK5.
GenomeRNAii 25818.
NextBioi 47059.
PMAP-CutDB Q9Y337.
PROi Q9Y337.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y337.
Bgeei Q9Y337.
CleanExi HS_KLK5.
Genevestigatori Q9Y337.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation."
    Brattsand M., Egelrud T.
    J. Biol. Chem. 274:30033-30040(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-153.
    Tissue: Stratum corneum.
  2. "Identification of novel human kallikrein-like genes on chromosome 19q13.3-q13.4."
    Yousef G.M., Luo L.-Y., Diamandis E.P.
    Anticancer Res. 19:2843-2852(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-153.
  3. "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], VARIANT ASP-153.
  4. "Differential expression of a human kallikrein 5 (KLK5) splice variant in ovarian and prostate cancer."
    Kurlender L., Yousef G.M., Memari N., Robb J.D., Michael I.P., Borgono C., Katsaros D., Stephan C., Jung K., Diamandis E.P.
    Tumor Biol. 25:149-156(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-153.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-153.
  6. "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], VARIANT ASP-153.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-153.
  9. "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], VARIANT ASP-153.
    Tissue: Ovary.
  10. "SPINK9: a selective, skin-specific Kazal-type serine protease inhibitor."
    Brattsand M., Stefansson K., Hubiche T., Nilsson S.K., Egelrud T.
    J. Invest. Dermatol. 129:1656-1665(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPINK9.
  11. "Identification of lympho-epithelial Kazal-type inhibitor 2 in human skin as a kallikrein-related peptidase 5-specific protease inhibitor."
    Meyer-Hoffert U., Wu Z., Schroeder J.M.
    PLoS ONE 4:E4372-E4372(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "Structural basis of the zinc inhibition of human tissue kallikrein 5."
    Debela M., Goettig P., Magdolen V., Huber R., Schechter N.M., Bode W.
    J. Mol. Biol. 373:1017-1031(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 67-293 ALONE AND IN COMPLEX WITH ZINC, ENZYME REGULATION, ACTIVE SITE, GLYCOSYLATION AT ASN-208, DISULFIDE BONDS.

Entry informationi

Entry nameiKLK5_HUMAN
AccessioniPrimary (citable) accession number: Q9Y337
Secondary accession number(s): Q53ZR3, Q9HBG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 127 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, 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

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