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Q9NQ38 (ISK5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Hemofiltrate peptide HF6478
  2. Hemofiltrate peptide HF7665
Gene names
Name:SPINK5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1064 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7 Ref.8

Subcellular location

Secreted.

Tissue specificity

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. Ref.1

Domain

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

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2

Sequence similarities

Contains 15 Kazal-like domains.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseHypotrichosis
Ichthyosis
   DomainRepeat
Signal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processanagen

Traceable author statement PubMed 12915442. Source: UniProtKB

epidermal cell differentiation

Inferred from direct assay PubMed 12915442. Source: UniProtKB

epithelial cell differentiation

Traceable author statement PubMed 12915442. Source: UniProtKB

extracellular matrix organization

Traceable author statement PubMed 15680911. Source: UniProtKB

hair cell differentiation

Traceable author statement PubMed 12915442. Source: UniProtKB

negative regulation of angiogenesis

Traceable author statement PubMed 15680911. Source: UniProtKB

negative regulation of endopeptidase activity

Inferred from direct assay Ref.1PubMed 15680911. Source: GOC

negative regulation of immune response

Traceable author statement PubMed 12915442. Source: UniProtKB

negative regulation of proteolysis

Inferred from electronic annotation. Source: Ensembl

regulation of T cell differentiation

Traceable author statement PubMed 12915442. Source: UniProtKB

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell cortex

Inferred from direct assay PubMed 12915442. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 12915442. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 15680911. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 15680911. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay PubMed 15680911. Source: UniProtKB

epidermal lamellar body

Inferred from direct assay PubMed 15675955. Source: UniProtKB

extracellular region

Inferred from direct assay PubMed 15680911. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 15680911. Source: UniProtKB

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from direct assay Ref.1PubMed 15680911. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform f-l (identifier: Q9NQ38-1)

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.
Isoform short (identifier: Q9NQ38-2)

The sequence of this isoform differs from the canonical sequence as follows:
     914-916: DEC → VIY
     917-1064: Missing.
Isoform long (identifier: Q9NQ38-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 10641042Serine protease inhibitor Kazal-type 5
PRO_0000016572
Peptide23 – 7755Hemofiltrate peptide HF6478
PRO_0000016573
Peptide356 – 42368Hemofiltrate peptide HF7665
PRO_0000016574

Regions

Domain28 – 6639Kazal-like 1; atypical
Domain91 – 15363Kazal-like 2
Domain155 – 21662Kazal-like 3
Domain219 – 28567Kazal-like 4
Domain291 – 35262Kazal-like 5
Domain361 – 42363Kazal-like 6
Domain431 – 48959Kazal-like 7
Domain490 – 55162Kazal-like 8
Domain561 – 62262Kazal-like 9
Domain626 – 68863Kazal-like 10
Domain701 – 75757Kazal-like 11
Domain768 – 83063Kazal-like 12
Domain843 – 90563Kazal-like 13
Domain910 – 97162Kazal-like 14
Domain987 – 104862Kazal-like 15

Sites

Site46 – 472Reactive bond Potential

Amino acid modifications

Disulfide bond30 ↔ 66
Disulfide bond44 ↔ 63
Disulfide bond97 ↔ 133 By similarity
Disulfide bond111 ↔ 130 By similarity
Disulfide bond119 ↔ 151 By similarity
Disulfide bond161 ↔ 197 By similarity
Disulfide bond175 ↔ 194 By similarity
Disulfide bond225 ↔ 261 By similarity
Disulfide bond239 ↔ 258 By similarity
Disulfide bond297 ↔ 333 By similarity
Disulfide bond311 ↔ 330 By similarity
Disulfide bond367 ↔ 403
Disulfide bond381 ↔ 400
Disulfide bond437 ↔ 473 By similarity
Disulfide bond451 ↔ 470 By similarity
Disulfide bond496 ↔ 532 By similarity
Disulfide bond510 ↔ 529 By similarity
Disulfide bond567 ↔ 603 By similarity
Disulfide bond581 ↔ 600 By similarity
Disulfide bond632 ↔ 668 By similarity
Disulfide bond646 ↔ 665 By similarity
Disulfide bond707 ↔ 743 By similarity
Disulfide bond721 ↔ 740 By similarity
Disulfide bond774 ↔ 810 By similarity
Disulfide bond788 ↔ 807 By similarity
Disulfide bond849 ↔ 885 By similarity
Disulfide bond863 ↔ 882 By similarity
Disulfide bond916 ↔ 952 By similarity
Disulfide bond930 ↔ 949 By similarity
Disulfide bond993 ↔ 1028
Disulfide bond1006 ↔ 1025
Disulfide bond1014 ↔ 1046

Natural variations

Alternative sequence914 – 9163DEC → VIY in isoform short.
VSP_040019
Alternative sequence9141D → DQCRQVQNEAEDAKFRQPGR SLASVARMSTD in isoform long.
VSP_040020
Alternative sequence917 – 1064148Missing in isoform short.
VSP_040021
Natural variant2671Q → R. Ref.1 Ref.2 Ref.3
Corresponds to variant rs6892205 [ dbSNP | Ensembl ].
VAR_047115
Natural variant3351A → V. Ref.1 Ref.3
Corresponds to variant rs34482796 [ dbSNP | Ensembl ].
VAR_061337
Natural variant3681S → N. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2303063 [ dbSNP | Ensembl ].
VAR_047116
Natural variant3861D → N.
Corresponds to variant rs2303064 [ dbSNP | Ensembl ].
VAR_047117
Natural variant3951V → M.
Corresponds to variant rs17775319 [ dbSNP | Ensembl ].
VAR_047118
Natural variant4201K → E. Ref.1 Ref.3 Ref.11
Corresponds to variant rs2303067 [ dbSNP | Ensembl ].
VAR_015537
Natural variant4411R → H.
Corresponds to variant rs34393923 [ dbSNP | Ensembl ].
VAR_047119
Natural variant5881I → M.
Corresponds to variant rs35877540 [ dbSNP | Ensembl ].
VAR_047120
Natural variant7111R → Q. Ref.1 Ref.3
Corresponds to variant rs3777134 [ dbSNP | Ensembl ].
VAR_047121
Natural variant8251E → D.
Corresponds to variant rs2303070 [ dbSNP | Ensembl ].
VAR_047122
Natural variant8871S → R.
Corresponds to variant rs28408445 [ dbSNP | Ensembl ].
VAR_047123
Natural variant9691K → E.
Corresponds to variant rs3188691 [ dbSNP | Ensembl ].
VAR_047124
Natural variant9721H → R.
Corresponds to variant rs17705005 [ dbSNP | Ensembl ].
VAR_047125

Experimental info

Sequence conflict19 – 279DAASKNEDQ → GQCEKDSLS in CAB96877. Ref.2

Secondary structure

................................. 1064
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform f-l [UniParc].

Last modified November 4, 2008. Version 2.
Checksum: 6CBEF39BB9E6D75D

FASTA1,064120,714
        10         20         30         40         50         60 
MKIATVSVLL PLALCLIQDA ASKNEDQEMC HEFQAFMKNG KLFCPQDKKF FQSLDGIMFI 

        70         80         90        100        110        120 
NKCATCKMIL EKEAKSQKRA RHLARAPKAT APTELNCDDF KKGERDGDFI CPDYYEAVCG 

       130        140        150        160        170        180 
TDGKTYDNRC ALCAENAKTG SQIGVKSEGE CKSSNPEQDV CSAFRPFVRD GRLGCTREND 

       190        200        210        220        230        240 
PVLGPDGKTH GNKCAMCAEL FLKEAENAKR EGETRIRRNA EKDFCKEYEK QVRNGRLFCT 

       250        260        270        280        290        300 
RESDPVRGPD GRMHGNKCAL CAEIFKQRFS EENSKTDQNL GKAEEKTKVK REIVKLCSQY 

       310        320        330        340        350        360 
QNQAKNGILF CTRENDPIRG PDGKMHGNLC SMCQAYFQAE NEEKKKAEAR ARNKRESGKA 

       370        380        390        400        410        420 
TSYAELCSEY RKLVRNGKLA CTRENDPIQG PDGKVHGNTC SMCEVFFQAE EEEKKKKEGK 

       430        440        450        460        470        480 
SRNKRQSKST ASFEELCSEY RKSRKNGRLF CTRENDPIQG PDGKMHGNTC SMCEAFFQQE 

       490        500        510        520        530        540 
ERARAKAKRE AAKEICSEFR DQVRNGTLIC TREHNPVRGP DGKMHGNKCA MCASVFKLEE 

       550        560        570        580        590        600 
EEKKNDKEEK GKVEAEKVKR EAVQELCSEY RHYVRNGRLP CTRENDPIEG LDGKIHGNTC 

       610        620        630        640        650        660 
SMCEAFFQQE AKEKERAEPR AKVKREAEKE TCDEFRRLLQ NGKLFCTREN DPVRGPDGKT 

       670        680        690        700        710        720 
HGNKCAMCKA VFQKENEERK RKEEEDQRNA AGHGSSGGGG GNTQDECAEY REQMKNGRLS 

       730        740        750        760        770        780 
CTRESDPVRD ADGKSYNNQC TMCKAKLERE AERKNEYSRS RSNGTGSESG KDTCDEFRSQ 

       790        800        810        820        830        840 
MKNGKLICTR ESDPVRGPDG KTHGNKCTMC KEKLEREAAE KKKKEDEDRS NTGERSNTGE 

       850        860        870        880        890        900 
RSNDKEDLCR EFRSMQRNGK LICTRENNPV RGPYGKMHIN KCAMCQSIFD REANERKKKD 

       910        920        930        940        950        960 
EEKSSSKPSN NAKDECSEFR NYIRNNELIC PRENDPVHGA DGKFYTNKCY MCRAVFLTEA 

       970        980        990       1000       1010       1020 
LERAKLQEKP SHVRASQEED SPDSFSSLDS EMCKDYRVLP RIGYLCPKDL KPVCGDDGQT 

      1030       1040       1050       1060 
YNNPCMLCHE NLIRQTNTHI RSTGKCEESS TPGTTAASMP PSDE 

« Hide

Isoform short [UniParc].

Checksum: 82A029D102BD8C26
Show »

FASTA916104,017
Isoform long [UniParc].

Checksum: 8EF0D8DE3A62227A
Show »

FASTA1,094124,076

References

« Hide 'large scale' references
[1]"LEKTI, a novel 15-domain type of human serine proteinase inhibitor."
Maegert H.-J., Staendker L., Kreutzmann P., Zucht H.-D., Reinecke M., Sommerhoff C.P., Fritz H., Forssmann W.-G.
J. Biol. Chem. 274:21499-21502(1999) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in SPINK5, encoding a serine protease inhibitor, cause Netherton syndrome."
Chavanas S., Bodemer C., Rochat A., Hamel-Teillac D., Ali M., Irvine A.D., Bonafe J.-L., Wilkinson J., Taieb A., Barrandon Y., Harper J.I., de Prost Y., Hovnanian A.
Nat. Genet. 25:141-142(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Gene polymorphism in Netherton and common atopic disease."
Walley A.J., Chavanas S., Moffatt M.F., Esnouf R.M., Ubhi B., Lawrence R., Wong K., Abecasis G.R., Jones E.Y., Harper J.I., Hovnanian A., Cookson W.O.C.M.
Nat. Genet. 29:175-178(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLU-420.
+Additional computationally mapped references.

Web resources

SPINK5base

SPINK5 mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ228139 mRNA. Translation: CAB40839.1.
AJ391230 expand/collapse EMBL AC list , 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.
RefSeqNP_001121170.1. NM_001127698.1.
NP_001121171.1. NM_001127699.1.
NP_006837.2. NM_006846.3.
UniGeneHs.331555.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0ZNMR-A356-423[»]
1HDLNMR-A23-77[»]
1UUCNMR-A23-77[»]
1UVFNMR-A989-1047[»]
1UVGNMR-A989-1064[»]
ProteinModelPortalQ9NQ38.
SMRQ9NQ38. Positions 23-201, 223-266, 295-353, 356-423, 426-478, 493-673, 707-744, 768-811, 841-889, 916-1064.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000352936.

Protein family/group databases

MEROPSI01.950.

PTM databases

PhosphoSiteQ9NQ38.

Polymorphism databases

DMDM212276440.

Proteomic databases

PaxDbQ9NQ38.
PRIDEQ9NQ38.

Protocols and materials databases

DNASU11005.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256084; ENSP00000256084; ENSG00000133710. [Q9NQ38-1]
ENST00000359874; ENSP00000352936; ENSG00000133710. [Q9NQ38-3]
ENST00000398454; ENSP00000381472; ENSG00000133710. [Q9NQ38-2]
GeneID11005.
KEGGhsa:11005.
UCSCuc003low.2. human. [Q9NQ38-2]
uc003lox.2. human. [Q9NQ38-1]
uc003loy.2. human. [Q9NQ38-3]

Organism-specific databases

CTD11005.
GeneCardsGC05P147423.
H-InvDBHIX0005288.
HGNCHGNC:15464. SPINK5.
HPACAB015347.
HPA009067.
HPA011351.
MIM256500. phenotype.
605010. gene.
neXtProtNX_Q9NQ38.
Orphanet634. Netherton syndrome.
PharmGKBPA37962.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253835.
HOVERGENHBG006183.
OMANGKLICT.
OrthoDBEOG7BW0M2.
PhylomeDBQ9NQ38.
TreeFamTF336724.

Enzyme and pathway databases

SABIO-RKQ9NQ38.

Gene expression databases

ArrayExpressQ9NQ38.
BgeeQ9NQ38.
CleanExHS_SPINK5.
GenevestigatorQ9NQ38.

Family and domain databases

InterProIPR002350. Kazal_dom.
[Graphical view]
PfamPF00050. Kazal_1. 1 hit.
PF07648. Kazal_2. 13 hits.
[Graphical view]
SMARTSM00280. KAZAL. 14 hits.
[Graphical view]
PROSITEPS00282. KAZAL_1. 2 hits.
PS51465. KAZAL_2. 14 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NQ38.
GeneWikiLEKTI.
GenomeRNAi11005.
NextBio41803.
PMAP-CutDBQ9NQ38.
PROQ9NQ38.
SOURCESearch...

Entry information

Entry nameISK5_HUMAN
AccessionPrimary (citable) accession number: Q9NQ38
Secondary accession number(s): A8MYE8 expand/collapse secondary AC list , B7WPB7, D6REN5, O75770, Q3LX95, Q3LX96, Q3LX97, Q96PP2, Q96PP3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM