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Q9Y5Y6

- ST14_HUMAN

UniProt

Q9Y5Y6 - ST14_HUMAN

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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

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei56 – 7621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini77 – 855779ExtracellularSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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

BgeeiQ9Y5Y6.
CleanExiHS_ST14.
ExpressionAtlasiQ9Y5Y6. baseline and differential.
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 – 6346Combined sources
Turni635 – 6373Combined sources
Beta strandi638 – 6458Combined sources
Beta strandi647 – 6537Combined sources
Helixi655 – 6584Combined sources
Helixi669 – 6713Combined sources
Beta strandi672 – 6776Combined sources
Beta strandi690 – 69910Combined sources
Turni705 – 7073Combined sources
Beta strandi713 – 7197Combined sources
Beta strandi724 – 7263Combined sources
Beta strandi744 – 75411Combined sources
Beta strandi764 – 7707Combined sources
Helixi773 – 7797Combined sources
Turni781 – 7833Combined sources
Beta strandi788 – 7925Combined sources
Beta strandi797 – 7993Combined sources
Turni802 – 8065Combined sources
Beta strandi808 – 8125Combined sources
Beta strandi818 – 8269Combined sources
Beta strandi828 – 8314Combined sources
Beta strandi837 – 8426Combined sources
Helixi843 – 8453Combined sources
Helixi846 – 8538Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00760000118962.
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

        10         20         30         40         50
MGSDRARKGG GGPKDFGAGL KYNSRHEKVN GLEEGVEFLP VNNVKKVEKH
60 70 80 90 100
GPGRWVVLAA VLIGLLLVLL GIGFLVWHLQ YRDVRVQKVF NGYMRITNEN
110 120 130 140 150
FVDAYENSNS TEFVSLASKV KDALKLLYSG VPFLGPYHKE SAVTAFSEGS
160 170 180 190 200
VIAYYWSEFS IPQHLVEEAE RVMAEERVVM LPPRARSLKS FVVTSVVAFP
210 220 230 240 250
TDSKTVQRTQ DNSCSFGLHA RGVELMRFTT PGFPDSPYPA HARCQWALRG
260 270 280 290 300
DADSVLSLTF RSFDLASCDE RGSDLVTVYN TLSPMEPHAL VQLCGTYPPS
310 320 330 340 350
YNLTFHSSQN VLLITLITNT ERRHPGFEAT FFQLPRMSSC GGRLRKAQGT
360 370 380 390 400
FNSPYYPGHY PPNIDCTWNI EVPNNQHVKV RFKFFYLLEP GVPAGTCPKD
410 420 430 440 450
YVEINGEKYC GERSQFVVTS NSNKITVRFH SDQSYTDTGF LAEYLSYDSS
460 470 480 490 500
DPCPGQFTCR TGRCIRKELR CDGWADCTDH SDELNCSCDA GHQFTCKNKF
510 520 530 540 550
CKPLFWVCDS VNDCGDNSDE QGCSCPAQTF RCSNGKCLSK SQQCNGKDDC
560 570 580 590 600
GDGSDEASCP KVNVVTCTKH TYRCLNGLCL SKGNPECDGK EDCSDGSDEK
610 620 630 640 650
DCDCGLRSFT RQARVVGGTD ADEGEWPWQV SLHALGQGHI CGASLISPNW
660 670 680 690 700
LVSAAHCYID DRGFRYSDPT QWTAFLGLHD QSQRSAPGVQ ERRLKRIISH
710 720 730 740 750
PFFNDFTFDY DIALLELEKP AEYSSMVRPI CLPDASHVFP AGKAIWVTGW
760 770 780 790 800
GHTQYGGTGA LILQKGEIRV INQTTCENLL PQQITPRMMC VGFLSGGVDS
810 820 830 840 850
CQGDSGGPLS SVEADGRIFQ AGVVSWGDGC AQRNKPGVYT RLPLFRDWIK

ENTGV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00760000118962.
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

Bgeei Q9Y5Y6.
CleanExi HS_ST14.
ExpressionAtlasi Q9Y5Y6. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 150 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