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Q92508

- PIEZ1_HUMAN

UniProt

Q92508 - PIEZ1_HUMAN

Protein

Piezo-type mechanosensitive ion channel component 1

Gene

PIEZO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Pore-forming subunit of a mechanosensitive non-specific cation channel, that conducts both sodium and potassium ions. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling.1 Publication

    GO - Molecular functioni

    1. cation channel activity Source: UniProtKB
    2. mechanically-gated ion channel activity Source: Ensembl

    GO - Biological processi

    1. cation transport Source: UniProtKB
    2. detection of mechanical stimulus Source: Ensembl
    3. positive regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
    4. positive regulation of integrin activation Source: UniProtKB
    5. regulation of membrane potential Source: Ensembl

    Keywords - Molecular functioni

    Ion channel

    Keywords - Biological processi

    Ion transport, Transport

    Protein family/group databases

    TCDBi1.A.75.1.1. the mechanical nociceptor, piezo (piezo) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Piezo-type mechanosensitive ion channel component 1
    Alternative name(s):
    Membrane protein induced by beta-amyloid treatment
    Short name:
    Mib
    Protein FAM38A
    Gene namesi
    Name:PIEZO1
    Synonyms:FAM38A, KIAA0233
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:28993. PIEZO1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Dehydrated hereditary stomatocytosis with or without pseudohyperkalemia and/or perinatal edema (DHS) [MIM:194380]: An autosomal dominant hemolytic anemia characterized by primary erythrocyte dehydration. DHS erythrocytes exhibit decreased total cation and potassium content that are not accompanied by a proportional net gain of sodium and water. DHS patients typically exhibit mild to moderate compensated hemolytic anemia, with an increased erythrocyte mean corpuscular hemoglobin concentration and a decreased osmotic fragility, both of which reflect cellular dehydration. Patients may also show perinatal edema and pseudohyperkalemia due to loss of potassium from red cells stored at room temperature. A minor proportion of red cells appear as stomatocytes on blood films. Complications such as splenomegaly and cholelithiasis, resulting from increased red cell trapping in the spleen and elevated bilirubin levels, respectively, may occur. The course of DHS is frequently associated with iron overload, which may lead to hepatosiderosis.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. All disease-causing mutations characterized so far produce a gain-of-function phenotype, mutated channels exhibiting increased cation transport in erythroid cells, that could be due to slower channel inactivation rate compared to the wild-type protein.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti718 – 7181G → S in DHS. 1 Publication
    VAR_069822
    Natural varianti782 – 7821G → S in DHS. 1 Publication
    VAR_069823
    Natural varianti808 – 8081R → Q in DHS. 1 Publication
    VAR_069824
    Natural varianti1117 – 11171S → L in DHS. 1 Publication
    VAR_069825
    Natural varianti1358 – 13581R → P in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 Publication
    VAR_069826
    Natural varianti2003 – 20031A → D in DHS. 1 Publication
    VAR_069827
    Natural varianti2020 – 20201A → T in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 Publication
    VAR_069828
    Natural varianti2020 – 20201A → V in DHS. 1 Publication
    VAR_069829
    Natural varianti2127 – 21271T → M in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 2 Publications
    VAR_069830
    Natural varianti2166 – 21694Missing in DHS.
    VAR_069831
    Natural varianti2225 – 22251M → R in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 Publication
    VAR_069832
    Natural varianti2456 – 24561R → H in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 2 Publications
    VAR_069833
    Natural varianti2488 – 24881R → Q in DHS; increased cation transport in erythroid cells. 1 Publication
    VAR_069834
    Natural varianti2496 – 24961E → ELE in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents.
    VAR_069835

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi194380. phenotype.
    Orphaneti3202. Dehydrated hereditary stomatocytosis.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25212521Piezo-type mechanosensitive ion channel component 1PRO_0000186817Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1391 – 13911Phosphoserine2 Publications
    Modified residuei1646 – 16461Phosphoserine3 Publications
    Modified residuei1854 – 18541Phosphothreonine1 Publication
    Glycosylationi2294 – 22941N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ92508.
    PaxDbiQ92508.
    PRIDEiQ92508.

    PTM databases

    PhosphoSiteiQ92508.

    Expressioni

    Tissue specificityi

    Expressed in numerous tissues. In normal brain, expressed exclusively in neurons, not in astrocytes. In Alzheimer disease brains, expressed in about half of the activated astrocytes located around classical senile plaques. In Parkinson disease substantia nigra, not detected in melanin-containing neurons nor in activated astrocytes. Expressed in erythrocytes (at protein level).3 Publications

    Developmental stagei

    At 17 weeks of gestation, strongly expressed in hepatic erythroblasts. At that stage, also expressed in fetal splenic plasma cells and in lymphatic vessel of fetal peritoneum. In vitro, up-regulated during the erythroid differentiation of CD34+ cells from healthy donors (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ92508.
    BgeeiQ92508.
    CleanExiHS_FAM38A.
    GenevestigatoriQ92508.

    Organism-specific databases

    HPAiHPA047185.

    Interactioni

    Subunit structurei

    Homooligomer, most likely homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi115124. 3 interactions.
    MINTiMINT-4991257.
    STRINGi9606.ENSP00000301015.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92508.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei27 – 4721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei64 – 8421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei118 – 13821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei194 – 21421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei218 – 23821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei248 – 26821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei302 – 32221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei428 – 44821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei460 – 48021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei514 – 53421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei579 – 59921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei602 – 62221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei629 – 64921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei681 – 70121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei823 – 84321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei852 – 87221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei926 – 94621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei987 – 100721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1043 – 106321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1160 – 118021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1184 – 120421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1218 – 124023HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1247 – 126418HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1277 – 129721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1678 – 169821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1700 – 172021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1734 – 175421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1962 – 198221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2003 – 202321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2032 – 205221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2061 – 208121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2100 – 212223HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2129 – 214921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2177 – 219721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2432 – 245221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1339 – 136830Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 9186Leu-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG298938.
    HOVERGENiHBG107901.
    InParanoidiQ92508.
    OMAiHEYSSNC.
    OrthoDBiEOG7J445T.
    PhylomeDBiQ92508.
    TreeFamiTF314295.

    Family and domain databases

    InterProiIPR027272. Piezo.
    [Graphical view]
    PANTHERiPTHR13167. PTHR13167. 1 hit.
    PfamiPF12166. DUF3595. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q92508-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPHVLGAVL YWLLLPCALL AACLLRFSGL SLVYLLFLLL LPWFPGPTRC     50
    GLQGHTGRLL RALLGLSLLF LVAHLALQIC LHIVPRLDQL LGPSCSRWET 100
    LSRHIGVTRL DLKDIPNAIR LVAPDLGILV VSSVCLGICG RLARNTRQSP 150
    HPRELDDDER DVDASPTAGL QEAATLAPTR RSRLAARFRV TAHWLLVAAG 200
    RVLAVTLLAL AGIAHPSALS SVYLLLFLAL CTWWACHFPI STRGFSRLCV 250
    AVGCFGAGHL ICLYCYQMPL AQALLPPAGI WARVLGLKDF VGPTNCSSPH 300
    ALVLNTGLDW PVYASPGVLL LLCYATASLR KLRAYRPSGQ RKEAAKGYEA 350
    RELELAELDQ WPQERESDQH VVPTAPDTEA DNCIVHELTG QSSVLRRPVR 400
    PKRAEPREAS PLHSLGHLIM DQSYVCALIA MMVWSITYHS WLTFVLLLWA 450
    CLIWTVRSRH QLAMLCSPCI LLYGMTLCCL RYVWAMDLRP ELPTTLGPVS 500
    LRQLGLEHTR YPCLDLGAML LYTLTFWLLL RQFVKEKLLK WAESPAALTE 550
    VTVADTEPTR TQTLLQSLGE LVKGVYAKYW IYVCAGMFIV VSFAGRLVVY 600
    KIVYMFLFLL CLTLFQVYYS LWRKLLKAFW WLVVAYTMLV LIAVYTFQFQ 650
    DFPAYWRNLT GFTDEQLGDL GLEQFSVSEL FSSILVPGFF LLACILQLHY 700
    FHRPFMQLTD MEHVSLPGTR LPRWAHRQDA VSGTPLLREE QQEHQQQQQE 750
    EEEEEEDSRD EGLGVATPHQ ATQVPEGAAK WGLVAERLLE LAAGFSDVLS 800
    RVQVFLRRLL ELHVFKLVAL YTVWVALKEV SVMNLLLVVL WAFALPYPRF 850
    RPMASCLSTV WTCVIIVCKM LYQLKVVNPQ EYSSNCTEPF PNSTNLLPTE 900
    ISQSLLYRGP VDPANWFGVR KGFPNLGYIQ NHLQVLLLLV FEAIVYRRQE 950
    HYRRQHQLAP LPAQAVFASG TRQQLDQDLL GCLKYFINFF FYKFGLEICF 1000
    LMAVNVIGQR MNFLVTLHGC WLVAILTRRH RQAIARLWPN YCLFLALFLL 1050
    YQYLLCLGMP PALCIDYPWR WSRAVPMNSA LIKWLYLPDF FRAPNSTNLI 1100
    SDFLLLLCAS QQWQVFSAER TEEWQRMAGV NTDRLEPLRG EPNPVPNFIH 1150
    CRSYLDMLKV AVFRYLFWLV LVVVFVTGAT RISIFGLGYL LACFYLLLFG 1200
    TALLQRDTRA RLVLWDCLIL YNVTVIISKN MLSLLACVFV EQMQTGFCWV 1250
    IQLFSLVCTV KGYYDPKEMM DRDQDCLLPV EEAGIIWDSV CFFFLLLQRR 1300
    VFLSHYYLHV RADLQATALL ASRGFALYNA ANLKSIDFHR RIEEKSLAQL 1350
    KRQMERIRAK QEKHRQGRVD RSRPQDTLGP KDPGLEPGPD SPGGSSPPRR 1400
    QWWRPWLDHA TVIHSGDYFL FESDSEEEEE AVPEDPRPSA QSAFQLAYQA 1450
    WVTNAQAVLR RRQQEQEQAR QEQAGQLPTG GGPSQEVEPA EGPEEAAAGR 1500
    SHVVQRVLST AQFLWMLGQA LVDELTRWLQ EFTRHHGTMS DVLRAERYLL 1550
    TQELLQGGEV HRGVLDQLYT SQAEATLPGP TEAPNAPSTV SSGLGAEEPL 1600
    SSMTDDMGSP LSTGYHTRSG SEEAVTDPGE REAGASLYQG LMRTASELLL 1650
    DRRLRIPELE EAELFAEGQG RALRLLRAVY QCVAAHSELL CYFIIILNHM 1700
    VTASAGSLVL PVLVFLWAML SIPRPSKRFW MTAIVFTEIA VVVKYLFQFG 1750
    FFPWNSHVVL RRYENKPYFP PRILGLEKTD GYIKYDLVQL MALFFHRSQL 1800
    LCYGLWDHEE DSPSKEHDKS GEEEQGAEEG PGVPAATTED HIQVEARVGP 1850
    TDGTPEPQVE LRPRDTRRIS LRFRRRKKEG PARKGAAAIE AEDREEEEGE 1900
    EEKEAPTGRE KRPSRSGGRV RAAGRRLQGF CLSLAQGTYR PLRRFFHDIL 1950
    HTKYRAATDV YALMFLADVV DFIIIIFGFW AFGKHSAATD ITSSLSDDQV 2000
    PEAFLVMLLI QFSTMVVDRA LYLRKTVLGK LAFQVALVLA IHLWMFFILP 2050
    AVTERMFNQN VVAQLWYFVK CIYFALSAYQ IRCGYPTRIL GNFLTKKYNH 2100
    LNLFLFQGFR LVPFLVELRA VMDWVWTDTT LSLSSWMCVE DIYANIFIIK 2150
    CSRETEKKYP QPKGQKKKKI VKYGMGGLII LFLIAIIWFP LLFMSLVRSV 2200
    VGVVNQPIDV TVTLKLGGYE PLFTMSAQQP SIIPFTAQAY EELSRQFDPQ 2250
    PLAMQFISQY SPEDIVTAQI EGSSGALWRI SPPSRAQMKR ELYNGTADIT 2300
    LRFTWNFQRD LAKGGTVEYA NEKHMLALAP NSTARRQLAS LLEGTSDQSV 2350
    VIPNLFPKYI RAPNGPEANP VKQLQPNEEA DYLGVRIQLR REQGAGATGF 2400
    LEWWVIELQE CRTDCNLLPM VIFSDKVSPP SLGFLAGYGI MGLYVSIVLV 2450
    IGKFVRGFFS EISHSIMFEE LPCVDRILKL CQDIFLVRET RELELEEELY 2500
    AKLIFLYRSP ETMIKWTREK E 2521
    Length:2,521
    Mass (Da):286,790
    Last modified:January 11, 2011 - v4
    Checksum:i127A3DA3E7CBD2DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti750 – 7501Missing in BAA13240. (PubMed:9039502)Curated
    Sequence conflicti750 – 7501Missing in AAI50272. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti718 – 7181G → S in DHS. 1 Publication
    VAR_069822
    Natural varianti782 – 7821G → S in DHS. 1 Publication
    VAR_069823
    Natural varianti808 – 8081R → Q in DHS. 1 Publication
    VAR_069824
    Natural varianti1117 – 11171S → L in DHS. 1 Publication
    VAR_069825
    Natural varianti1358 – 13581R → P in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 Publication
    VAR_069826
    Natural varianti2003 – 20031A → D in DHS. 1 Publication
    VAR_069827
    Natural varianti2020 – 20201A → T in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 Publication
    VAR_069828
    Natural varianti2020 – 20201A → V in DHS. 1 Publication
    VAR_069829
    Natural varianti2127 – 21271T → M in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 2 Publications
    VAR_069830
    Natural varianti2166 – 21694Missing in DHS.
    VAR_069831
    Natural varianti2225 – 22251M → R in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 Publication
    VAR_069832
    Natural varianti2456 – 24561R → H in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 2 Publications
    VAR_069833
    Natural varianti2488 – 24881R → Q in DHS; increased cation transport in erythroid cells. 1 Publication
    VAR_069834
    Natural varianti2496 – 24961E → ELE in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents.
    VAR_069835

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC138028 Genomic DNA. No translation available.
    AB161230 mRNA. Translation: BAF03565.1.
    D87071 mRNA. Translation: BAA13240.1.
    BC150271 mRNA. Translation: AAI50272.1.
    CCDSiCCDS54058.1.
    RefSeqiNP_001136336.2. NM_001142864.2.
    UniGeneiHs.377001.
    Hs.592074.

    Genome annotation databases

    EnsembliENST00000301015; ENSP00000301015; ENSG00000103335.
    GeneIDi9780.
    KEGGihsa:9780.
    UCSCiuc010vpb.2. human.

    Polymorphism databases

    DMDMi317373533.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC138028 Genomic DNA. No translation available.
    AB161230 mRNA. Translation: BAF03565.1 .
    D87071 mRNA. Translation: BAA13240.1 .
    BC150271 mRNA. Translation: AAI50272.1 .
    CCDSi CCDS54058.1.
    RefSeqi NP_001136336.2. NM_001142864.2.
    UniGenei Hs.377001.
    Hs.592074.

    3D structure databases

    ProteinModelPortali Q92508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115124. 3 interactions.
    MINTi MINT-4991257.
    STRINGi 9606.ENSP00000301015.

    Protein family/group databases

    TCDBi 1.A.75.1.1. the mechanical nociceptor, piezo (piezo) family.

    PTM databases

    PhosphoSitei Q92508.

    Polymorphism databases

    DMDMi 317373533.

    Proteomic databases

    MaxQBi Q92508.
    PaxDbi Q92508.
    PRIDEi Q92508.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301015 ; ENSP00000301015 ; ENSG00000103335 .
    GeneIDi 9780.
    KEGGi hsa:9780.
    UCSCi uc010vpb.2. human.

    Organism-specific databases

    CTDi 9780.
    GeneCardsi GC16M088781.
    H-InvDB HIX0022749.
    HIX0173225.
    HGNCi HGNC:28993. PIEZO1.
    HPAi HPA047185.
    MIMi 194380. phenotype.
    611184. gene.
    neXtProti NX_Q92508.
    Orphaneti 3202. Dehydrated hereditary stomatocytosis.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298938.
    HOVERGENi HBG107901.
    InParanoidi Q92508.
    OMAi HEYSSNC.
    OrthoDBi EOG7J445T.
    PhylomeDBi Q92508.
    TreeFami TF314295.

    Miscellaneous databases

    GenomeRNAii 9780.
    NextBioi 36824.
    PROi Q92508.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92508.
    Bgeei Q92508.
    CleanExi HS_FAM38A.
    Genevestigatori Q92508.

    Family and domain databases

    InterProi IPR027272. Piezo.
    [Graphical view ]
    PANTHERi PTHR13167. PTHR13167. 1 hit.
    Pfami PF12166. DUF3595. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "A novel membrane protein, encoded by the gene covering KIAA0233, is transcriptionally induced in senile plaque-associated astrocytes."
      Satoh K., Hata M., Takahara S., Tsuzaki H., Yokota H., Akatsu H., Yamamoto T., Kosaka K., Yamada T.
      Brain Res. 1108:19-27(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-2521, TISSUE SPECIFICITY.
    3. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-2521.
      Tissue: Bone marrow.
    4. "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] OF 486-2521.
    5. "Mutations in the mechanotransduction protein PIEZO1 are associated with hereditary xerocytosis."
      Zarychanski R., Schulz V.P., Houston B.L., Maksimova Y., Houston D.S., Smith B., Rinehart J., Gallagher P.G.
      Blood 120:1908-1915(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 955-972; 1324-1334; 1548-1562 AND 1656-1671, VARIANTS DHS ARG-2225 AND HIS-2456, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1391; SER-1646 AND THR-1854, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2294.
      Tissue: Leukemic T-cell.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Integrin activation by Fam38A uses a novel mechanism of R-Ras targeting to the endoplasmic reticulum."
      McHugh B.J., Buttery R., Lad Y., Banks S., Haslett C., Sethi T.
      J. Cell Sci. 123:51-61(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1391 AND SER-1646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: VARIANTS DHS SER-718; SER-782; GLN-808; LEU-1117; ASP-2003; VAL-2020; MET-2127; 2166-LYS--LYS-2169 DEL; HIS-2456 AND GLN-2488, CHARACTERIZATION OF VARIANTS DHS HIS-2456 AND GLN-2488, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    13. Cited for: VARIANTS DHS PRO-1358; THR-2020; MET-2127 AND LEU-GLU-2496 INS, CHARACTERIZATION OF VARIANTS DHS PRO-1358; THR-2020; MET-2127; LEU-GLU-2496 INS; ARG-2225 AND HIS-2456.

    Entry informationi

    Entry nameiPIEZ1_HUMAN
    AccessioniPrimary (citable) accession number: Q92508
    Secondary accession number(s): A6NHT9, A7E2B7, Q0KKZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 116 of the entry and version 4 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

    Miscellaneous

    Piezo comes from the Greek 'piesi' meaning pressure.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3