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Q9Y5Y6

- ST14_HUMAN

UniProt

Q9Y5Y6 - ST14_HUMAN

Protein

Suppressor of tumorigenicity 14 protein

Gene

ST14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (01 May 2000)
      Previous versions | rss
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    Functioni

    Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site. Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing.1 Publication

    Catalytic activityi

    Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei656 – 6561Charge relay system
    Active sitei711 – 7111Charge relay system
    Active sitei805 – 8051Charge relay system

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro
    2. serine-type peptidase activity Source: UniProtKB

    GO - Biological processi

    1. keratinocyte differentiation Source: UniProtKB
    2. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    BRENDAi3.4.21.109. 2681.

    Protein family/group databases

    MEROPSiS01.302.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Suppressor of tumorigenicity 14 protein (EC:3.4.21.109)
    Alternative name(s):
    Matriptase
    Membrane-type serine protease 1
    Short name:
    MT-SP1
    Prostamin
    Serine protease 14
    Serine protease TADG-15
    Tumor-associated differentially-expressed gene 15 protein
    Gene namesi
    Name:ST14
    Synonyms:PRSS14, SNC19, TADG15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:11344. ST14.

    Subcellular locationi

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. extracellular space Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. extrinsic component of plasma membrane Source: Ensembl
    5. integral component of plasma membrane Source: ProtInc
    6. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Ichthyosis, congenital, autosomal recessive 11 (ARCI11) [MIM:602400]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti827 – 8271G → R in ARCI11. 1 Publication
    VAR_032849

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi656 – 6561H → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi711 – 7111D → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi805 – 8051S → A: Abolishes catalytic activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Hypotrichosis, Ichthyosis

    Organism-specific databases

    MIMi602400. phenotype.
    Orphaneti91132. Ichthyosis-hypotrichosis syndrome.
    PharmGKBiPA36168.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 855855Suppressor of tumorigenicity 14 proteinPRO_0000088712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi214 ↔ 244By similarity
    Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi340 ↔ 366By similarity
    Disulfide bondi397 ↔ 410By similarity
    Disulfide bondi453 ↔ 464By similarity
    Disulfide bondi459 ↔ 477By similarity
    Disulfide bondi471 ↔ 486By similarity
    Glycosylationi485 – 4851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi488 ↔ 501By similarity
    Disulfide bondi496 ↔ 514By similarity
    Disulfide bondi508 ↔ 523By similarity
    Disulfide bondi525 ↔ 537By similarity
    Disulfide bondi532 ↔ 550By similarity
    Disulfide bondi544 ↔ 559By similarity
    Disulfide bondi567 ↔ 579By similarity
    Disulfide bondi574 ↔ 593By similarity
    Disulfide bondi587 ↔ 602By similarity
    Disulfide bondi641 ↔ 6571 Publication
    Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi776 ↔ 7901 Publication
    Disulfide bondi801 ↔ 8301 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9Y5Y6.
    PaxDbiQ9Y5Y6.
    PeptideAtlasiQ9Y5Y6.
    PRIDEiQ9Y5Y6.

    PTM databases

    PhosphoSiteiQ9Y5Y6.

    Miscellaneous databases

    PMAP-CutDBQ9Y5Y6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y5Y6.
    BgeeiQ9Y5Y6.
    CleanExiHS_ST14.
    GenevestigatoriQ9Y5Y6.

    Interactioni

    Subunit structurei

    Interacts with CDCP1. May interact with TMEFF1.2 Publications

    Protein-protein interaction databases

    BioGridi112645. 4 interactions.
    IntActiQ9Y5Y6. 3 interactions.
    MINTiMINT-6784312.
    STRINGi9606.ENSP00000278742.

    Structurei

    Secondary structure

    1
    855
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi629 – 6346
    Turni635 – 6373
    Beta strandi638 – 6458
    Beta strandi647 – 6537
    Helixi655 – 6584
    Helixi669 – 6713
    Beta strandi672 – 6776
    Beta strandi690 – 69910
    Turni705 – 7073
    Beta strandi713 – 7197
    Beta strandi724 – 7263
    Beta strandi744 – 75411
    Beta strandi764 – 7707
    Helixi773 – 7797
    Turni781 – 7833
    Beta strandi788 – 7925
    Beta strandi797 – 7993
    Turni802 – 8065
    Beta strandi808 – 8125
    Beta strandi818 – 8269
    Beta strandi828 – 8314
    Beta strandi837 – 8426
    Helixi843 – 8453
    Helixi846 – 8538

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EAWX-ray2.93A/C615-855[»]
    1EAXX-ray1.30A615-855[»]
    2FMVmodel-A214-447[»]
    2GV6X-ray2.10A615-855[»]
    2GV7X-ray2.20A615-855[»]
    3BN9X-ray2.17A/B615-855[»]
    3NCLX-ray1.19A615-855[»]
    3NPSX-ray1.50A615-855[»]
    3P8FX-ray2.00A615-855[»]
    3P8GX-ray1.20A615-855[»]
    3SO3X-ray2.10A615-855[»]
    4IS5X-ray1.48A615-855[»]
    4ISLX-ray2.29A615-855[»]
    4ISNX-ray2.45A615-855[»]
    4ISOX-ray2.01A615-855[»]
    4JYTX-ray2.00A615-855[»]
    4JZ1X-ray1.90A615-855[»]
    4JZIX-ray2.00A615-855[»]
    4O97X-ray2.20A615-855[»]
    B604-607[»]
    4O9VX-ray1.90A615-855[»]
    B604-607[»]
    ProteinModelPortaliQ9Y5Y6.
    SMRiQ9Y5Y6. Positions 228-855.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5Y6.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5555CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini77 – 855779ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei56 – 7621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini86 – 203118SEAPROSITE-ProRule annotationAdd
    BLAST
    Domaini214 – 334121CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini340 – 447108CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini452 – 48736LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini487 – 52438LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini524 – 56037LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini566 – 60338LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 854240Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 2 CUB domains.PROSITE-ProRule annotation
    Contains 4 LDL-receptor class A domains.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 1 SEA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000136851.
    HOVERGENiHBG012556.
    InParanoidiQ9Y5Y6.
    KOiK08670.
    OMAiDSSDPCP.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ9Y5Y6.
    TreeFamiTF330647.

    Family and domain databases

    Gene3Di2.60.120.290. 2 hits.
    4.10.400.10. 4 hits.
    InterProiIPR000859. CUB_dom.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR017051. Peptidase_S1A_matripase.
    IPR000082. SEA_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00431. CUB. 2 hits.
    PF00057. Ldl_recept_a. 4 hits.
    PF01390. SEA. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036370. ST14. 1 hit.
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00042. CUB. 2 hits.
    SM00192. LDLa. 4 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 2 hits.
    SSF50494. SSF50494. 1 hit.
    SSF57424. SSF57424. 4 hits.
    SSF82671. SSF82671. 1 hit.
    PROSITEiPS01180. CUB. 2 hits.
    PS01209. LDLRA_1. 3 hits.
    PS50068. LDLRA_2. 4 hits.
    PS50024. SEA. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y5Y6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSDRARKGG GGPKDFGAGL KYNSRHEKVN GLEEGVEFLP VNNVKKVEKH    50
    GPGRWVVLAA VLIGLLLVLL GIGFLVWHLQ YRDVRVQKVF NGYMRITNEN 100
    FVDAYENSNS TEFVSLASKV KDALKLLYSG VPFLGPYHKE SAVTAFSEGS 150
    VIAYYWSEFS IPQHLVEEAE RVMAEERVVM LPPRARSLKS FVVTSVVAFP 200
    TDSKTVQRTQ DNSCSFGLHA RGVELMRFTT PGFPDSPYPA HARCQWALRG 250
    DADSVLSLTF RSFDLASCDE RGSDLVTVYN TLSPMEPHAL VQLCGTYPPS 300
    YNLTFHSSQN VLLITLITNT ERRHPGFEAT FFQLPRMSSC GGRLRKAQGT 350
    FNSPYYPGHY PPNIDCTWNI EVPNNQHVKV RFKFFYLLEP GVPAGTCPKD 400
    YVEINGEKYC GERSQFVVTS NSNKITVRFH SDQSYTDTGF LAEYLSYDSS 450
    DPCPGQFTCR TGRCIRKELR CDGWADCTDH SDELNCSCDA GHQFTCKNKF 500
    CKPLFWVCDS VNDCGDNSDE QGCSCPAQTF RCSNGKCLSK SQQCNGKDDC 550
    GDGSDEASCP KVNVVTCTKH TYRCLNGLCL SKGNPECDGK EDCSDGSDEK 600
    DCDCGLRSFT RQARVVGGTD ADEGEWPWQV SLHALGQGHI CGASLISPNW 650
    LVSAAHCYID DRGFRYSDPT QWTAFLGLHD QSQRSAPGVQ ERRLKRIISH 700
    PFFNDFTFDY DIALLELEKP AEYSSMVRPI CLPDASHVFP AGKAIWVTGW 750
    GHTQYGGTGA LILQKGEIRV INQTTCENLL PQQITPRMMC VGFLSGGVDS 800
    CQGDSGGPLS SVEADGRIFQ AGVVSWGDGC AQRNKPGVYT RLPLFRDWIK 850
    ENTGV 855
    Length:855
    Mass (Da):94,770
    Last modified:May 1, 2000 - v2
    Checksum:i26143132C01F99C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti674 – 6741A → V in BAB20376. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti285 – 2851M → I.
    Corresponds to variant rs7126904 [ dbSNP | Ensembl ].
    VAR_032847
    Natural varianti381 – 3811R → S.1 Publication
    Corresponds to variant rs17667603 [ dbSNP | Ensembl ].
    VAR_032848
    Natural varianti827 – 8271G → R in ARCI11. 1 Publication
    VAR_032849

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF118224 mRNA. Translation: AAD42765.2.
    AF133086 mRNA. Translation: AAF00109.1.
    AB030036 mRNA. Translation: BAB20376.1.
    AF057145 mRNA. Translation: AAG15395.1.
    BC005826 mRNA. Translation: AAH05826.2.
    BC030532 mRNA. Translation: AAH30532.1.
    AF283256 Genomic DNA. Translation: AAG13949.1.
    CCDSiCCDS8487.1.
    RefSeqiNP_068813.1. NM_021978.3.
    UniGeneiHs.504315.

    Genome annotation databases

    EnsembliENST00000278742; ENSP00000278742; ENSG00000149418.
    GeneIDi6768.
    KEGGihsa:6768.
    UCSCiuc001qfw.3. human.

    Polymorphism databases

    DMDMi13124575.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF118224 mRNA. Translation: AAD42765.2 .
    AF133086 mRNA. Translation: AAF00109.1 .
    AB030036 mRNA. Translation: BAB20376.1 .
    AF057145 mRNA. Translation: AAG15395.1 .
    BC005826 mRNA. Translation: AAH05826.2 .
    BC030532 mRNA. Translation: AAH30532.1 .
    AF283256 Genomic DNA. Translation: AAG13949.1 .
    CCDSi CCDS8487.1.
    RefSeqi NP_068813.1. NM_021978.3.
    UniGenei Hs.504315.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EAW X-ray 2.93 A/C 615-855 [» ]
    1EAX X-ray 1.30 A 615-855 [» ]
    2FMV model - A 214-447 [» ]
    2GV6 X-ray 2.10 A 615-855 [» ]
    2GV7 X-ray 2.20 A 615-855 [» ]
    3BN9 X-ray 2.17 A/B 615-855 [» ]
    3NCL X-ray 1.19 A 615-855 [» ]
    3NPS X-ray 1.50 A 615-855 [» ]
    3P8F X-ray 2.00 A 615-855 [» ]
    3P8G X-ray 1.20 A 615-855 [» ]
    3SO3 X-ray 2.10 A 615-855 [» ]
    4IS5 X-ray 1.48 A 615-855 [» ]
    4ISL X-ray 2.29 A 615-855 [» ]
    4ISN X-ray 2.45 A 615-855 [» ]
    4ISO X-ray 2.01 A 615-855 [» ]
    4JYT X-ray 2.00 A 615-855 [» ]
    4JZ1 X-ray 1.90 A 615-855 [» ]
    4JZI X-ray 2.00 A 615-855 [» ]
    4O97 X-ray 2.20 A 615-855 [» ]
    B 604-607 [» ]
    4O9V X-ray 1.90 A 615-855 [» ]
    B 604-607 [» ]
    ProteinModelPortali Q9Y5Y6.
    SMRi Q9Y5Y6. Positions 228-855.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112645. 4 interactions.
    IntActi Q9Y5Y6. 3 interactions.
    MINTi MINT-6784312.
    STRINGi 9606.ENSP00000278742.

    Chemistry

    BindingDBi Q9Y5Y6.
    ChEMBLi CHEMBL3018.
    DrugBanki DB00013. Urokinase.

    Protein family/group databases

    MEROPSi S01.302.

    PTM databases

    PhosphoSitei Q9Y5Y6.

    Polymorphism databases

    DMDMi 13124575.

    Proteomic databases

    MaxQBi Q9Y5Y6.
    PaxDbi Q9Y5Y6.
    PeptideAtlasi Q9Y5Y6.
    PRIDEi Q9Y5Y6.

    Protocols and materials databases

    DNASUi 6768.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278742 ; ENSP00000278742 ; ENSG00000149418 .
    GeneIDi 6768.
    KEGGi hsa:6768.
    UCSCi uc001qfw.3. human.

    Organism-specific databases

    CTDi 6768.
    GeneCardsi GC11P130063.
    HGNCi HGNC:11344. ST14.
    MIMi 602400. phenotype.
    606797. gene.
    neXtProti NX_Q9Y5Y6.
    Orphaneti 91132. Ichthyosis-hypotrichosis syndrome.
    PharmGKBi PA36168.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000136851.
    HOVERGENi HBG012556.
    InParanoidi Q9Y5Y6.
    KOi K08670.
    OMAi DSSDPCP.
    OrthoDBi EOG75B84T.
    PhylomeDBi Q9Y5Y6.
    TreeFami TF330647.

    Enzyme and pathway databases

    BRENDAi 3.4.21.109. 2681.

    Miscellaneous databases

    ChiTaRSi ST14. human.
    EvolutionaryTracei Q9Y5Y6.
    GenomeRNAii 6768.
    NextBioi 26412.
    PMAP-CutDB Q9Y5Y6.
    PROi Q9Y5Y6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5Y6.
    Bgeei Q9Y5Y6.
    CleanExi HS_ST14.
    Genevestigatori Q9Y5Y6.

    Family and domain databases

    Gene3Di 2.60.120.290. 2 hits.
    4.10.400.10. 4 hits.
    InterProi IPR000859. CUB_dom.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR017051. Peptidase_S1A_matripase.
    IPR000082. SEA_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00431. CUB. 2 hits.
    PF00057. Ldl_recept_a. 4 hits.
    PF01390. SEA. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036370. ST14. 1 hit.
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00042. CUB. 2 hits.
    SM00192. LDLa. 4 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 2 hits.
    SSF50494. SSF50494. 1 hit.
    SSF57424. SSF57424. 4 hits.
    SSF82671. SSF82671. 1 hit.
    PROSITEi PS01180. CUB. 2 hits.
    PS01209. LDLRA_1. 3 hits.
    PS50068. LDLRA_2. 4 hits.
    PS50024. SEA. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity."
      Lin C.Y., Anders J., Johnson M., Sang Q.A., Dickson R.B.
      J. Biol. Chem. 274:18231-18236(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue."
      Takeuchi T., Shuman M.A., Craik C.S.
      Proc. Natl. Acad. Sci. U.S.A. 96:11054-11061(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Molecular cloning of a novel transmembrane serine protease expressed in human prostate."
      Yamaguchi N., Mitsui S.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Prostate.
    4. Tanimoto H., Underwood L.J., Wang Y., Shigemasa K., Parmley T.H., O'Brien T.J.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-381.
    5. "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].
      Tissue: Blood and Muscle.
    6. "Genomic analysis of a novel human serine protease SNC19."
      Cao J., Fan W., Zheng S.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-664.
    7. "Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk."
      Lin C.Y., Anders J., Johnson M., Dickson R.B.
      J. Biol. Chem. 274:18237-18242(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Tissue: Milk.
    8. "Adhesion signaling by a novel mitotic substrate of src kinases."
      Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.
      Oncogene 24:5333-5343(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDCP1.
    9. "Protein interaction analysis of ST14 domains and their point and deletion mutants."
      Ge W., Hu H., Ding K., Sun L., Zheng S.
      J. Biol. Chem. 281:7406-7412(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-656; ASP-711 AND SER-805, POSSIBLE INTERACTION WITH TMEFF1.
    10. "Ichthyosis, follicular atrophoderma, and hypotrichosis caused by mutations in ST14 is associated with impaired profilaggrin processing."
      Alef T., Torres S., Hausser I., Metze D., Tursen U., Lestringant G.G., Hennies H.C.
      J. Invest. Dermatol. 129:862-869(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INVOLVEMENT IN ARCI11.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase."
      Friedrich R., Fuentes-Prior P., Ong E., Coombs G., Hunter M., Oehler R., Pierson D., Gonzalez R., Huber R., Bode W., Madison E.L.
      J. Biol. Chem. 277:2160-2168(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 615-855 IN COMPLEX WITH INHIBITORS, DISULFIDE BONDS.
    13. "Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase."
      Basel-Vanagaite L., Attia R., Ishida-Yamamoto A., Rainshtein L., Ben Amitai D., Lurie R., Pasmanik-Chor M., Indelman M., Zvulunov A., Saban S., Magal N., Sprecher E., Shohat M.
      Am. J. Hum. Genet. 80:467-477(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARCI11 ARG-827.

    Entry informationi

    Entry nameiST14_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5Y6
    Secondary accession number(s): Q9BS01
    , Q9H3S0, Q9HB36, Q9HCA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 148 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 11
      Human chromosome 11: 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