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Q9NQ38

- ISK5_HUMAN

UniProt

Q9NQ38 - ISK5_HUMAN

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Protein

Serine protease inhibitor Kazal-type 5

Gene

SPINK5

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

Functioni

Serine protease inhibitor, probably important for the anti-inflammatory and/or antimicrobial protection of mucous epithelia. Contribute to the integrity and protective barrier function of the skin by regulating the activity of defense-activating and desquamation-involved proteases. Inhibits KLK5, it's major target, in a pH-dependent manner. Inhibits KLK7, KLK14 CASP14, and trypsin.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei46 – 472Reactive bondPROSITE-ProRule annotation

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

  1. anagen Source: UniProtKB
  2. epidermal cell differentiation Source: UniProtKB
  3. epithelial cell differentiation Source: UniProtKB
  4. extracellular matrix organization Source: UniProtKB
  5. hair cell differentiation Source: UniProtKB
  6. negative regulation of angiogenesis Source: UniProtKB
  7. negative regulation of endopeptidase activity Source: GOC
  8. negative regulation of immune response Source: UniProtKB
  9. negative regulation of proteolysis Source: Ensembl
  10. negative regulation of serine-type peptidase activity Source: Ensembl
  11. regulation of cell adhesion Source: Ensembl
  12. regulation of T cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Enzyme and pathway databases

SABIO-RKQ9NQ38.

Protein family/group databases

MEROPSiI01.032.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease inhibitor Kazal-type 5
Alternative name(s):
Lympho-epithelial Kazal-type-related inhibitor
Short name:
LEKTI
Cleaved into the following 2 chains:
Gene namesi
Name:SPINK5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:15464. SPINK5.

Subcellular locationi

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. endoplasmic reticulum membrane Source: UniProtKB
  6. epidermal lamellar body Source: UniProtKB
  7. extracellular region Source: UniProtKB
  8. extracellular vesicular exosome Source: UniProt
  9. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Netherton syndrome (NETH) [MIM:256500]: An autosomal recessive congenital ichthyosis associated with hair shaft abnormalities and anomalies of the immune system. Typical features are ichthyosis linearis circumflexa, ichthyosiform erythroderma, trichorrhexis invaginata (bamboo hair), atopic dermatitis, and hayfever. High postnatal mortality is due to failure to thrive, infections and hypernatremic dehydration.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Hypotrichosis, Ichthyosis

Organism-specific databases

MIMi256500. phenotype.
Orphaneti634. Netherton syndrome.
PharmGKBiPA37962.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 10641042Serine protease inhibitor Kazal-type 5PRO_0000016572Add
BLAST
Peptidei23 – 7755Hemofiltrate peptide HF6478PRO_0000016573Add
BLAST
Peptidei356 – 42368Hemofiltrate peptide HF7665PRO_0000016574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 66
Disulfide bondi44 ↔ 63
Disulfide bondi97 ↔ 133PROSITE-ProRule annotation
Disulfide bondi111 ↔ 130PROSITE-ProRule annotation
Disulfide bondi119 ↔ 151PROSITE-ProRule annotation
Disulfide bondi161 ↔ 197PROSITE-ProRule annotation
Disulfide bondi175 ↔ 194PROSITE-ProRule annotation
Disulfide bondi225 ↔ 261PROSITE-ProRule annotation
Disulfide bondi239 ↔ 258PROSITE-ProRule annotation
Disulfide bondi297 ↔ 333PROSITE-ProRule annotation
Disulfide bondi311 ↔ 330PROSITE-ProRule annotation
Disulfide bondi367 ↔ 403
Disulfide bondi381 ↔ 400
Disulfide bondi437 ↔ 473PROSITE-ProRule annotation
Disulfide bondi451 ↔ 470PROSITE-ProRule annotation
Disulfide bondi496 ↔ 532PROSITE-ProRule annotation
Disulfide bondi510 ↔ 529PROSITE-ProRule annotation
Disulfide bondi567 ↔ 603PROSITE-ProRule annotation
Disulfide bondi581 ↔ 600PROSITE-ProRule annotation
Disulfide bondi632 ↔ 668PROSITE-ProRule annotation
Disulfide bondi646 ↔ 665PROSITE-ProRule annotation
Disulfide bondi707 ↔ 743PROSITE-ProRule annotation
Disulfide bondi721 ↔ 740PROSITE-ProRule annotation
Disulfide bondi774 ↔ 810PROSITE-ProRule annotation
Disulfide bondi788 ↔ 807PROSITE-ProRule annotation
Disulfide bondi849 ↔ 885PROSITE-ProRule annotation
Disulfide bondi863 ↔ 882PROSITE-ProRule annotation
Disulfide bondi916 ↔ 952PROSITE-ProRule annotation
Disulfide bondi930 ↔ 949PROSITE-ProRule annotation
Disulfide bondi993 ↔ 1028
Disulfide bondi1006 ↔ 1025
Disulfide bondi1014 ↔ 1046

Post-translational modificationi

Proteolytically processed by furin in individual domains (D1, D5, D6, D8 through D11, and D9 through D15) exhibiting various inhibitory potentials for multiple proteases.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiQ9NQ38.
PRIDEiQ9NQ38.

PTM databases

PhosphoSiteiQ9NQ38.

Miscellaneous databases

PMAP-CutDBQ9NQ38.

Expressioni

Tissue specificityi

Highly expressed in the thymus and stratum corneum. Also found in the oral mucosa, parathyroid gland, Bartholin's glands, tonsils, and vaginal epithelium. Very low levels are detected in lung, kidney, and prostate.1 Publication

Gene expression databases

BgeeiQ9NQ38.
CleanExiHS_SPINK5.
ExpressionAtlasiQ9NQ38. baseline and differential.
GenevestigatoriQ9NQ38.

Organism-specific databases

HPAiCAB015347.
HPA009067.
HPA011351.

Interactioni

Protein-protein interaction databases

BioGridi116196. 1 interaction.
STRINGi9606.ENSP00000352936.

Structurei

Secondary structure

1
1064
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni25 – 273
Helixi33 – 364
Beta strandi37 – 404
Helixi48 – 525
Helixi54 – 7623
Helixi363 – 3664
Helixi367 – 3704
Turni371 – 3733
Beta strandi375 – 3773
Helixi399 – 41315
Helixi990 – 9934
Turni1000 – 10023
Beta strandi1013 – 10153
Turni1016 – 10183
Beta strandi1019 – 10246
Helixi1025 – 103410
Beta strandi1040 – 10456
Helixi1047 – 10493
Helixi1055 – 10584

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0ZNMR-A356-423[»]
1HDLNMR-A23-77[»]
1UUCNMR-A23-77[»]
1UVFNMR-A989-1047[»]
1UVGNMR-A989-1064[»]
ProteinModelPortaliQ9NQ38.
SMRiQ9NQ38. Positions 23-77, 159-201, 223-266, 295-353, 356-423, 426-478, 487-537, 556-608, 624-673, 707-744, 768-811, 841-889, 916-956, 989-1064.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQ38.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6639Kazal-like 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Domaini91 – 15363Kazal-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini155 – 21662Kazal-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini219 – 28567Kazal-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini291 – 35262Kazal-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini361 – 42363Kazal-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini431 – 48959Kazal-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini490 – 55162Kazal-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini561 – 62262Kazal-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini626 – 68863Kazal-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini701 – 75757Kazal-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini768 – 83063Kazal-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini843 – 90563Kazal-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini910 – 97162Kazal-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini987 – 104862Kazal-like 15PROSITE-ProRule annotationAdd
BLAST

Domaini

Contains at least one active inhibitory domain for trypsin (domain 6).

Sequence similaritiesi

Contains 15 Kazal-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG253835.
GeneTreeiENSGT00510000048608.
HOVERGENiHBG006183.
InParanoidiQ9NQ38.
OMAiCHENLIR.
OrthoDBiEOG7BW0M2.
PhylomeDBiQ9NQ38.
TreeFamiTF336724.

Family and domain databases

InterProiIPR002350. Kazal_dom.
[Graphical view]
PfamiPF00050. Kazal_1. 1 hit.
PF07648. Kazal_2. 13 hits.
[Graphical view]
SMARTiSM00280. KAZAL. 14 hits.
[Graphical view]
PROSITEiPS00282. KAZAL_1. 2 hits.
PS51465. KAZAL_2. 14 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform f-l (identifier: Q9NQ38-1) [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
MKIATVSVLL PLALCLIQDA ASKNEDQEMC HEFQAFMKNG KLFCPQDKKF
60 70 80 90 100
FQSLDGIMFI NKCATCKMIL EKEAKSQKRA RHLARAPKAT APTELNCDDF
110 120 130 140 150
KKGERDGDFI CPDYYEAVCG TDGKTYDNRC ALCAENAKTG SQIGVKSEGE
160 170 180 190 200
CKSSNPEQDV CSAFRPFVRD GRLGCTREND PVLGPDGKTH GNKCAMCAEL
210 220 230 240 250
FLKEAENAKR EGETRIRRNA EKDFCKEYEK QVRNGRLFCT RESDPVRGPD
260 270 280 290 300
GRMHGNKCAL CAEIFKQRFS EENSKTDQNL GKAEEKTKVK REIVKLCSQY
310 320 330 340 350
QNQAKNGILF CTRENDPIRG PDGKMHGNLC SMCQAYFQAE NEEKKKAEAR
360 370 380 390 400
ARNKRESGKA TSYAELCSEY RKLVRNGKLA CTRENDPIQG PDGKVHGNTC
410 420 430 440 450
SMCEVFFQAE EEEKKKKEGK SRNKRQSKST ASFEELCSEY RKSRKNGRLF
460 470 480 490 500
CTRENDPIQG PDGKMHGNTC SMCEAFFQQE ERARAKAKRE AAKEICSEFR
510 520 530 540 550
DQVRNGTLIC TREHNPVRGP DGKMHGNKCA MCASVFKLEE EEKKNDKEEK
560 570 580 590 600
GKVEAEKVKR EAVQELCSEY RHYVRNGRLP CTRENDPIEG LDGKIHGNTC
610 620 630 640 650
SMCEAFFQQE AKEKERAEPR AKVKREAEKE TCDEFRRLLQ NGKLFCTREN
660 670 680 690 700
DPVRGPDGKT HGNKCAMCKA VFQKENEERK RKEEEDQRNA AGHGSSGGGG
710 720 730 740 750
GNTQDECAEY REQMKNGRLS CTRESDPVRD ADGKSYNNQC TMCKAKLERE
760 770 780 790 800
AERKNEYSRS RSNGTGSESG KDTCDEFRSQ MKNGKLICTR ESDPVRGPDG
810 820 830 840 850
KTHGNKCTMC KEKLEREAAE KKKKEDEDRS NTGERSNTGE RSNDKEDLCR
860 870 880 890 900
EFRSMQRNGK LICTRENNPV RGPYGKMHIN KCAMCQSIFD REANERKKKD
910 920 930 940 950
EEKSSSKPSN NAKDECSEFR NYIRNNELIC PRENDPVHGA DGKFYTNKCY
960 970 980 990 1000
MCRAVFLTEA LERAKLQEKP SHVRASQEED SPDSFSSLDS EMCKDYRVLP
1010 1020 1030 1040 1050
RIGYLCPKDL KPVCGDDGQT YNNPCMLCHE NLIRQTNTHI RSTGKCEESS
1060
TPGTTAASMP PSDE
Length:1,064
Mass (Da):120,714
Last modified:November 4, 2008 - v2
Checksum:i6CBEF39BB9E6D75D
GO
Isoform short (identifier: Q9NQ38-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     914-916: DEC → VIY
     917-1064: Missing.

Show »
Length:916
Mass (Da):104,017
Checksum:i82A029D102BD8C26
GO
Isoform long (identifier: Q9NQ38-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     914-914: D → DQCRQVQNEAEDAKFRQPGRSLASVARMSTD

Show »
Length:1,094
Mass (Da):124,076
Checksum:i8EF0D8DE3A62227A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 279DAASKNEDQ → GQCEKDSLS in CAB96877. (PubMed:10835624)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti267 – 2671Q → R.3 Publications
Corresponds to variant rs6892205 [ dbSNP | Ensembl ].
VAR_047115
Natural varianti335 – 3351A → V.2 Publications
Corresponds to variant rs34482796 [ dbSNP | Ensembl ].
VAR_061337
Natural varianti368 – 3681S → N.3 Publications
Corresponds to variant rs2303063 [ dbSNP | Ensembl ].
VAR_047116
Natural varianti386 – 3861D → N.
Corresponds to variant rs2303064 [ dbSNP | Ensembl ].
VAR_047117
Natural varianti395 – 3951V → M.
Corresponds to variant rs17775319 [ dbSNP | Ensembl ].
VAR_047118
Natural varianti420 – 4201K → E.3 Publications
Corresponds to variant rs2303067 [ dbSNP | Ensembl ].
VAR_015537
Natural varianti441 – 4411R → H.
Corresponds to variant rs34393923 [ dbSNP | Ensembl ].
VAR_047119
Natural varianti588 – 5881I → M.
Corresponds to variant rs35877540 [ dbSNP | Ensembl ].
VAR_047120
Natural varianti711 – 7111R → Q.2 Publications
Corresponds to variant rs3777134 [ dbSNP | Ensembl ].
VAR_047121
Natural varianti825 – 8251E → D.
Corresponds to variant rs2303070 [ dbSNP | Ensembl ].
VAR_047122
Natural varianti887 – 8871S → R.
Corresponds to variant rs28408445 [ dbSNP | Ensembl ].
VAR_047123
Natural varianti969 – 9691K → E.
Corresponds to variant rs3188691 [ dbSNP | Ensembl ].
VAR_047124
Natural varianti972 – 9721H → R.
Corresponds to variant rs17705005 [ dbSNP | Ensembl ].
VAR_047125

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei914 – 9163DEC → VIY in isoform short. 1 PublicationVSP_040019
Alternative sequencei914 – 9141D → DQCRQVQNEAEDAKFRQPGR SLASVARMSTD in isoform long. 1 PublicationVSP_040020
Alternative sequencei917 – 1064148Missing in isoform short. 1 PublicationVSP_040021Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ228139 mRNA. Translation: CAB40839.1.
AJ391230
, AJ270944, AJ391231, AJ391232, AJ391233, AJ391234, AJ391235, AJ276579, AJ391236, AJ276580, AJ391237, AJ391238, AJ391239, AJ391240, AJ391241, AJ276578, AJ391242, AJ391243, AJ391244, AJ391245, AJ391246, AJ391247, AJ391248, AJ391249, AJ391250, AJ391251, AJ391252, AJ391253, AJ391254, AJ276577 Genomic DNA. Translation: CAB96877.1.
DQ149927 mRNA. Translation: ABA06534.1.
DQ149928 mRNA. Translation: ABA06535.1.
DQ149929 mRNA. Translation: ABA06536.1.
AC008722 Genomic DNA. No translation available.
AC116334 Genomic DNA. No translation available.
AF295784 Genomic DNA. Translation: AAK97139.1.
AF295783 Genomic DNA. Translation: AAK97140.1.
CCDSiCCDS43382.1. [Q9NQ38-1]
CCDS47300.1. [Q9NQ38-3]
CCDS47301.1. [Q9NQ38-2]
RefSeqiNP_001121170.1. NM_001127698.1. [Q9NQ38-3]
NP_001121171.1. NM_001127699.1. [Q9NQ38-2]
NP_006837.2. NM_006846.3. [Q9NQ38-1]
UniGeneiHs.331555.

Genome annotation databases

EnsembliENST00000256084; ENSP00000256084; ENSG00000133710. [Q9NQ38-1]
ENST00000359874; ENSP00000352936; ENSG00000133710. [Q9NQ38-3]
ENST00000398454; ENSP00000381472; ENSG00000133710. [Q9NQ38-2]
GeneIDi11005.
KEGGihsa:11005.
UCSCiuc003low.2. human. [Q9NQ38-2]
uc003lox.2. human. [Q9NQ38-1]
uc003loy.2. human. [Q9NQ38-3]

Polymorphism databases

DMDMi212276440.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SPINK5base

SPINK5 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ228139 mRNA. Translation: CAB40839.1 .
AJ391230
, AJ270944 , AJ391231 , AJ391232 , AJ391233 , AJ391234 , AJ391235 , AJ276579 , AJ391236 , AJ276580 , AJ391237 , AJ391238 , AJ391239 , AJ391240 , AJ391241 , AJ276578 , AJ391242 , AJ391243 , AJ391244 , AJ391245 , AJ391246 , AJ391247 , AJ391248 , AJ391249 , AJ391250 , AJ391251 , AJ391252 , AJ391253 , AJ391254 , AJ276577 Genomic DNA. Translation: CAB96877.1 .
DQ149927 mRNA. Translation: ABA06534.1 .
DQ149928 mRNA. Translation: ABA06535.1 .
DQ149929 mRNA. Translation: ABA06536.1 .
AC008722 Genomic DNA. No translation available.
AC116334 Genomic DNA. No translation available.
AF295784 Genomic DNA. Translation: AAK97139.1 .
AF295783 Genomic DNA. Translation: AAK97140.1 .
CCDSi CCDS43382.1. [Q9NQ38-1 ]
CCDS47300.1. [Q9NQ38-3 ]
CCDS47301.1. [Q9NQ38-2 ]
RefSeqi NP_001121170.1. NM_001127698.1. [Q9NQ38-3 ]
NP_001121171.1. NM_001127699.1. [Q9NQ38-2 ]
NP_006837.2. NM_006846.3. [Q9NQ38-1 ]
UniGenei Hs.331555.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H0Z NMR - A 356-423 [» ]
1HDL NMR - A 23-77 [» ]
1UUC NMR - A 23-77 [» ]
1UVF NMR - A 989-1047 [» ]
1UVG NMR - A 989-1064 [» ]
ProteinModelPortali Q9NQ38.
SMRi Q9NQ38. Positions 23-77, 159-201, 223-266, 295-353, 356-423, 426-478, 487-537, 556-608, 624-673, 707-744, 768-811, 841-889, 916-956, 989-1064.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116196. 1 interaction.
STRINGi 9606.ENSP00000352936.

Protein family/group databases

MEROPSi I01.032.

PTM databases

PhosphoSitei Q9NQ38.

Polymorphism databases

DMDMi 212276440.

Proteomic databases

PaxDbi Q9NQ38.
PRIDEi Q9NQ38.

Protocols and materials databases

DNASUi 11005.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256084 ; ENSP00000256084 ; ENSG00000133710 . [Q9NQ38-1 ]
ENST00000359874 ; ENSP00000352936 ; ENSG00000133710 . [Q9NQ38-3 ]
ENST00000398454 ; ENSP00000381472 ; ENSG00000133710 . [Q9NQ38-2 ]
GeneIDi 11005.
KEGGi hsa:11005.
UCSCi uc003low.2. human. [Q9NQ38-2 ]
uc003lox.2. human. [Q9NQ38-1 ]
uc003loy.2. human. [Q9NQ38-3 ]

Organism-specific databases

CTDi 11005.
GeneCardsi GC05P147423.
H-InvDB HIX0005288.
HGNCi HGNC:15464. SPINK5.
HPAi CAB015347.
HPA009067.
HPA011351.
MIMi 256500. phenotype.
605010. gene.
neXtProti NX_Q9NQ38.
Orphaneti 634. Netherton syndrome.
PharmGKBi PA37962.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253835.
GeneTreei ENSGT00510000048608.
HOVERGENi HBG006183.
InParanoidi Q9NQ38.
OMAi CHENLIR.
OrthoDBi EOG7BW0M2.
PhylomeDBi Q9NQ38.
TreeFami TF336724.

Enzyme and pathway databases

SABIO-RK Q9NQ38.

Miscellaneous databases

EvolutionaryTracei Q9NQ38.
GeneWikii LEKTI.
GenomeRNAii 11005.
NextBioi 41803.
PMAP-CutDB Q9NQ38.
PROi Q9NQ38.
SOURCEi Search...

Gene expression databases

Bgeei Q9NQ38.
CleanExi HS_SPINK5.
ExpressionAtlasi Q9NQ38. baseline and differential.
Genevestigatori Q9NQ38.

Family and domain databases

InterProi IPR002350. Kazal_dom.
[Graphical view ]
Pfami PF00050. Kazal_1. 1 hit.
PF07648. Kazal_2. 13 hits.
[Graphical view ]
SMARTi SM00280. KAZAL. 14 hits.
[Graphical view ]
PROSITEi PS00282. KAZAL_1. 2 hits.
PS51465. KAZAL_2. 14 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS F-L), PARTIAL PROTEIN SEQUENCE, VARIANTS ARG-267; VAL-335; ASN-368; GLU-420 AND GLN-711, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Epithelium.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN NETHERTON SYNDROME, VARIANTS ARG-267 AND ASN-368.
  3. "SPINK5, the defective gene in netherton syndrome, encodes multiple LEKTI isoforms derived from alternative pre-mRNA processing."
    Tartaglia-Polcini A., Bonnart C., Micheloni A., Cianfarani F., Andre A., Zambruno G., Hovnanian A., D'Alessio M.
    J. Invest. Dermatol. 126:315-324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT; F-L AND LONG), ALTERNATIVE SPLICING, VARIANTS ARG-267; VAL-335; ASN-368; GLU-420 AND GLN-711.
    Tissue: Keratinocyte.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The spectrum of pathogenic mutations in SPINK5 in 19 families with Netherton syndrome: implications for mutation detection and first case of prenatal diagnosis."
    Sprecher E., Chavanas S., DiGiovanna J.J., Amin S., Nielsen K., Prendiville J.S., Silverman R., Esterly N.B., Spraker M.K., Guelig E., de Luna M.L., Williams M.L., Buehler B., Siegfried E.C., Van Maldergem L., Pfendner E., Bale S.J., Uitto J., Hovnanian A., Richard G.
    J. Invest. Dermatol. 117:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-222 AND 266-294.
  6. "Purification and partial amino acid sequence of proteins from human epidermal keratinocyte conditioned medium."
    Ahmed A., Kandola P., Ziada G., Parenteau N.
    J. Protein Chem. 20:273-278(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 490-507.
    Tissue: Foreskin keratinocyte.
  7. "LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction."
    Deraison C., Bonnart C., Lopez F., Besson C., Robinson R., Jayakumar A., Wagberg F., Brattsand M., Hachem J.P., Leonardsson G., Hovnanian A.
    Mol. Biol. Cell 18:3607-3619(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CLEAVAGE BY FURIN, INHIBITION OF KLK5; KLK7 AND KLK14.
  8. "New role for LEKTI in skin barrier formation: label-free quantitative proteomic identification of caspase 14 as a novel target for the protease inhibitor LEKTI."
    Bennett K., Callard R., Heywood W., Harper J., Jayakumar A., Clayman G.L., Di W.L., Mills K.
    J. Proteome Res. 9:4289-4294(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INHIBITION OF CASP14.
  9. "Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI."
    Lauber T., Schulz A., Schweimer K., Adermann K., Marx U.C.
    J. Mol. Biol. 328:205-219(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-77 AND 356-423.
  10. "The solution structure of a chimeric LEKTI domain reveals a chameleon sequence."
    Tidow H., Lauber T., Vitzithum K., Sommerhoff C.P., Rosch P., Marx U.C.
    Biochemistry 43:11238-11247(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 989-1064.
  11. Cited for: VARIANT GLU-420.

Entry informationi

Entry nameiISK5_HUMAN
AccessioniPrimary (citable) accession number: Q9NQ38
Secondary accession number(s): A8MYE8
, B7WPB7, D6REN5, O75770, Q3LX95, Q3LX96, Q3LX97, Q96PP2, Q96PP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: November 4, 2008
Last modified: October 29, 2014
This is version 143 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 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3