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Q92508 (PIEZ1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Piezo-type mechanosensitive ion channel component 1
Alternative name(s):
Membrane protein induced by beta-amyloid treatment
Short name=Mib
Protein FAM38A
Gene names
Name:PIEZO1
Synonyms:FAM38A, KIAA0233
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2521 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Subunit structure

Homooligomer, most likely homotetramer By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane. Cell membrane; Multi-pass membrane protein. Note: In erythrocytes, located in the plasma membrane. Ref.5 Ref.10 Ref.12

Tissue specificity

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). Ref.2 Ref.5 Ref.12

Developmental stage

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). Ref.12

Involvement in disease

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.
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. Ref.5 Ref.12 Ref.13

Miscellaneous

Piezo comes from the Greek 'piesi' meaning pressure.

Sequence similarities

Belongs to the PIEZO family.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell membrane
Endoplasmic reticulum
Membrane
   DiseaseDisease mutation
Hereditary hemolytic anemia
   DomainCoiled coil
Transmembrane
Transmembrane helix
   Molecular functionIon channel
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcation transport

Inferred from sequence or structural similarity. Source: UniProtKB

detection of mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-cell adhesion mediated by integrin

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of integrin activation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.10. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncation channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

mechanically-gated ion channel activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25212521Piezo-type mechanosensitive ion channel component 1
PRO_0000186817

Regions

Transmembrane5 – 2521Helical; Potential
Transmembrane27 – 4721Helical; Potential
Transmembrane64 – 8421Helical; Potential
Transmembrane118 – 13821Helical; Potential
Transmembrane194 – 21421Helical; Potential
Transmembrane218 – 23821Helical; Potential
Transmembrane248 – 26821Helical; Potential
Transmembrane302 – 32221Helical; Potential
Transmembrane428 – 44821Helical; Potential
Transmembrane460 – 48021Helical; Potential
Transmembrane514 – 53421Helical; Potential
Transmembrane579 – 59921Helical; Potential
Transmembrane602 – 62221Helical; Potential
Transmembrane629 – 64921Helical; Potential
Transmembrane681 – 70121Helical; Potential
Transmembrane823 – 84321Helical; Potential
Transmembrane852 – 87221Helical; Potential
Transmembrane926 – 94621Helical; Potential
Transmembrane987 – 100721Helical; Potential
Transmembrane1043 – 106321Helical; Potential
Transmembrane1160 – 118021Helical; Potential
Transmembrane1184 – 120421Helical; Potential
Transmembrane1218 – 124023Helical; Potential
Transmembrane1247 – 126418Helical; Potential
Transmembrane1277 – 129721Helical; Potential
Transmembrane1678 – 169821Helical; Potential
Transmembrane1700 – 172021Helical; Potential
Transmembrane1734 – 175421Helical; Potential
Transmembrane1962 – 198221Helical; Potential
Transmembrane2003 – 202321Helical; Potential
Transmembrane2032 – 205221Helical; Potential
Transmembrane2061 – 208121Helical; Potential
Transmembrane2100 – 212223Helical; Potential
Transmembrane2129 – 214921Helical; Potential
Transmembrane2177 – 219721Helical; Potential
Transmembrane2432 – 245221Helical; Potential
Coiled coil1339 – 136830 Potential
Compositional bias6 – 9186Leu-rich

Amino acid modifications

Modified residue13911Phosphoserine Ref.7 Ref.11
Modified residue16461Phosphoserine Ref.7 Ref.9 Ref.11
Modified residue18541Phosphothreonine Ref.7
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation22941N-linked (GlcNAc...) Ref.8

Natural variations

Natural variant7181G → S in DHS. Ref.12
VAR_069822
Natural variant7821G → S in DHS. Ref.12
VAR_069823
Natural variant8081R → Q in DHS. Ref.12
VAR_069824
Natural variant11171S → L in DHS. Ref.12
VAR_069825
Natural variant13581R → P in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. Ref.13
VAR_069826
Natural variant20031A → D in DHS. Ref.12
VAR_069827
Natural variant20201A → T in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. Ref.13
VAR_069828
Natural variant20201A → V in DHS. Ref.12
VAR_069829
Natural variant21271T → M in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. Ref.12 Ref.13
VAR_069830
Natural variant2166 – 21694Missing in DHS.
VAR_069831
Natural variant22251M → R in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. Ref.5 Ref.13
VAR_069832
Natural variant24561R → H in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. Ref.5 Ref.12 Ref.13
VAR_069833
Natural variant24881R → Q in DHS; increased cation transport in erythroid cells. Ref.12
VAR_069834
Natural variant24961E → ELE in DHS; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents.
VAR_069835

Experimental info

Sequence conflict7501Missing in BAA13240. Ref.3
Sequence conflict7501Missing in AAI50272. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q92508 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: 127A3DA3E7CBD2DD

FASTA2,521286,790
        10         20         30         40         50         60 
MEPHVLGAVL YWLLLPCALL AACLLRFSGL SLVYLLFLLL LPWFPGPTRC GLQGHTGRLL 

        70         80         90        100        110        120 
RALLGLSLLF LVAHLALQIC LHIVPRLDQL LGPSCSRWET LSRHIGVTRL DLKDIPNAIR 

       130        140        150        160        170        180 
LVAPDLGILV VSSVCLGICG RLARNTRQSP HPRELDDDER DVDASPTAGL QEAATLAPTR 

       190        200        210        220        230        240 
RSRLAARFRV TAHWLLVAAG RVLAVTLLAL AGIAHPSALS SVYLLLFLAL CTWWACHFPI 

       250        260        270        280        290        300 
STRGFSRLCV AVGCFGAGHL ICLYCYQMPL AQALLPPAGI WARVLGLKDF VGPTNCSSPH 

       310        320        330        340        350        360 
ALVLNTGLDW PVYASPGVLL LLCYATASLR KLRAYRPSGQ RKEAAKGYEA RELELAELDQ 

       370        380        390        400        410        420 
WPQERESDQH VVPTAPDTEA DNCIVHELTG QSSVLRRPVR PKRAEPREAS PLHSLGHLIM 

       430        440        450        460        470        480 
DQSYVCALIA MMVWSITYHS WLTFVLLLWA CLIWTVRSRH QLAMLCSPCI LLYGMTLCCL 

       490        500        510        520        530        540 
RYVWAMDLRP ELPTTLGPVS LRQLGLEHTR YPCLDLGAML LYTLTFWLLL RQFVKEKLLK 

       550        560        570        580        590        600 
WAESPAALTE VTVADTEPTR TQTLLQSLGE LVKGVYAKYW IYVCAGMFIV VSFAGRLVVY 

       610        620        630        640        650        660 
KIVYMFLFLL CLTLFQVYYS LWRKLLKAFW WLVVAYTMLV LIAVYTFQFQ DFPAYWRNLT 

       670        680        690        700        710        720 
GFTDEQLGDL GLEQFSVSEL FSSILVPGFF LLACILQLHY FHRPFMQLTD MEHVSLPGTR 

       730        740        750        760        770        780 
LPRWAHRQDA VSGTPLLREE QQEHQQQQQE EEEEEEDSRD EGLGVATPHQ ATQVPEGAAK 

       790        800        810        820        830        840 
WGLVAERLLE LAAGFSDVLS RVQVFLRRLL ELHVFKLVAL YTVWVALKEV SVMNLLLVVL 

       850        860        870        880        890        900 
WAFALPYPRF RPMASCLSTV WTCVIIVCKM LYQLKVVNPQ EYSSNCTEPF PNSTNLLPTE 

       910        920        930        940        950        960 
ISQSLLYRGP VDPANWFGVR KGFPNLGYIQ NHLQVLLLLV FEAIVYRRQE HYRRQHQLAP 

       970        980        990       1000       1010       1020 
LPAQAVFASG TRQQLDQDLL GCLKYFINFF FYKFGLEICF LMAVNVIGQR MNFLVTLHGC 

      1030       1040       1050       1060       1070       1080 
WLVAILTRRH RQAIARLWPN YCLFLALFLL YQYLLCLGMP PALCIDYPWR WSRAVPMNSA 

      1090       1100       1110       1120       1130       1140 
LIKWLYLPDF FRAPNSTNLI SDFLLLLCAS QQWQVFSAER TEEWQRMAGV NTDRLEPLRG 

      1150       1160       1170       1180       1190       1200 
EPNPVPNFIH CRSYLDMLKV AVFRYLFWLV LVVVFVTGAT RISIFGLGYL LACFYLLLFG 

      1210       1220       1230       1240       1250       1260 
TALLQRDTRA RLVLWDCLIL YNVTVIISKN MLSLLACVFV EQMQTGFCWV IQLFSLVCTV 

      1270       1280       1290       1300       1310       1320 
KGYYDPKEMM DRDQDCLLPV EEAGIIWDSV CFFFLLLQRR VFLSHYYLHV RADLQATALL 

      1330       1340       1350       1360       1370       1380 
ASRGFALYNA ANLKSIDFHR RIEEKSLAQL KRQMERIRAK QEKHRQGRVD RSRPQDTLGP 

      1390       1400       1410       1420       1430       1440 
KDPGLEPGPD SPGGSSPPRR QWWRPWLDHA TVIHSGDYFL FESDSEEEEE AVPEDPRPSA 

      1450       1460       1470       1480       1490       1500 
QSAFQLAYQA WVTNAQAVLR RRQQEQEQAR QEQAGQLPTG GGPSQEVEPA EGPEEAAAGR 

      1510       1520       1530       1540       1550       1560 
SHVVQRVLST AQFLWMLGQA LVDELTRWLQ EFTRHHGTMS DVLRAERYLL TQELLQGGEV 

      1570       1580       1590       1600       1610       1620 
HRGVLDQLYT SQAEATLPGP TEAPNAPSTV SSGLGAEEPL SSMTDDMGSP LSTGYHTRSG 

      1630       1640       1650       1660       1670       1680 
SEEAVTDPGE REAGASLYQG LMRTASELLL DRRLRIPELE EAELFAEGQG RALRLLRAVY 

      1690       1700       1710       1720       1730       1740 
QCVAAHSELL CYFIIILNHM VTASAGSLVL PVLVFLWAML SIPRPSKRFW MTAIVFTEIA 

      1750       1760       1770       1780       1790       1800 
VVVKYLFQFG FFPWNSHVVL RRYENKPYFP PRILGLEKTD GYIKYDLVQL MALFFHRSQL 

      1810       1820       1830       1840       1850       1860 
LCYGLWDHEE DSPSKEHDKS GEEEQGAEEG PGVPAATTED HIQVEARVGP TDGTPEPQVE 

      1870       1880       1890       1900       1910       1920 
LRPRDTRRIS LRFRRRKKEG PARKGAAAIE AEDREEEEGE EEKEAPTGRE KRPSRSGGRV 

      1930       1940       1950       1960       1970       1980 
RAAGRRLQGF CLSLAQGTYR PLRRFFHDIL HTKYRAATDV YALMFLADVV DFIIIIFGFW 

      1990       2000       2010       2020       2030       2040 
AFGKHSAATD ITSSLSDDQV PEAFLVMLLI QFSTMVVDRA LYLRKTVLGK LAFQVALVLA 

      2050       2060       2070       2080       2090       2100 
IHLWMFFILP AVTERMFNQN VVAQLWYFVK CIYFALSAYQ IRCGYPTRIL GNFLTKKYNH 

      2110       2120       2130       2140       2150       2160 
LNLFLFQGFR LVPFLVELRA VMDWVWTDTT LSLSSWMCVE DIYANIFIIK CSRETEKKYP 

      2170       2180       2190       2200       2210       2220 
QPKGQKKKKI VKYGMGGLII LFLIAIIWFP LLFMSLVRSV VGVVNQPIDV TVTLKLGGYE 

      2230       2240       2250       2260       2270       2280 
PLFTMSAQQP SIIPFTAQAY EELSRQFDPQ PLAMQFISQY SPEDIVTAQI EGSSGALWRI 

      2290       2300       2310       2320       2330       2340 
SPPSRAQMKR ELYNGTADIT LRFTWNFQRD LAKGGTVEYA NEKHMLALAP NSTARRQLAS 

      2350       2360       2370       2380       2390       2400 
LLEGTSDQSV VIPNLFPKYI RAPNGPEANP VKQLQPNEEA DYLGVRIQLR REQGAGATGF 

      2410       2420       2430       2440       2450       2460 
LEWWVIELQE CRTDCNLLPM VIFSDKVSPP SLGFLAGYGI MGLYVSIVLV IGKFVRGFFS 

      2470       2480       2490       2500       2510       2520 
EISHSIMFEE LPCVDRILKL CQDIFLVRET RELELEEELY AKLIFLYRSP ETMIKWTREK 


E 

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References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Multiple clinical forms of dehydrated hereditary stomatocytosis arise from mutations in PIEZO1."
Andolfo I., Alper S.L., De Franceschi L., Auriemma C., Russo R., De Falco L., Vallefuoco F., Esposito M.R., Vandorpe D.H., Shmukler B.E., Narayan R., Montanaro D., D'Armiento M., Vetro A., Limongelli I., Zuffardi O., Glader B.E., Schrier S.L. expand/collapse author list , Brugnara C., Stewart G.W., Delaunay J., Iolascon A.
Blood 121:3925-3935(2013) [PubMed] [Europe PMC] [Abstract]
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]"Dehydrated hereditary stomatocytosis linked to gain-of-function mutations in mechanically activated PIEZO1 ion channels."
Albuisson J., Murthy S.E., Bandell M., Coste B., Louis-Dit-Picard H., Mathur J., Feneant-Thibault M., Tertian G., de Jaureguiberry J.P., Syfuss P.Y., Cahalan S., Garcon L., Toutain F., Simon Rohrlich P., Delaunay J., Picard V., Jeunemaitre X., Patapoutian A.
Nat. Commun. 4:1884-1884(2013) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC138028 Genomic DNA. No translation available.
AB161230 mRNA. Translation: BAF03565.1.
D87071 mRNA. Translation: BAA13240.1.
BC150271 mRNA. Translation: AAI50272.1.
CCDSCCDS54058.1.
RefSeqNP_001136336.2. NM_001142864.2.
UniGeneHs.377001.
Hs.592074.

3D structure databases

ProteinModelPortalQ92508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115124. 3 interactions.
MINTMINT-4991257.
STRING9606.ENSP00000301015.

Protein family/group databases

TCDB1.A.75.1.1. the mechanical nociceptor, piezo (piezo) family.

PTM databases

PhosphoSiteQ92508.

Polymorphism databases

DMDM317373533.

Proteomic databases

MaxQBQ92508.
PaxDbQ92508.
PRIDEQ92508.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301015; ENSP00000301015; ENSG00000103335.
GeneID9780.
KEGGhsa:9780.
UCSCuc010vpb.2. human.

Organism-specific databases

CTD9780.
GeneCardsGC16M088781.
H-InvDBHIX0022749.
HIX0173225.
HGNCHGNC:28993. PIEZO1.
HPAHPA047185.
MIM194380. phenotype.
611184. gene.
neXtProtNX_Q92508.
Orphanet3202. Dehydrated hereditary stomatocytosis.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298938.
HOVERGENHBG107901.
InParanoidQ92508.
OMAHEYSSNC.
OrthoDBEOG7J445T.
PhylomeDBQ92508.
TreeFamTF314295.

Gene expression databases

ArrayExpressQ92508.
BgeeQ92508.
CleanExHS_FAM38A.
GenevestigatorQ92508.

Family and domain databases

InterProIPR027272. Piezo.
[Graphical view]
PANTHERPTHR13167. PTHR13167. 1 hit.
PfamPF12166. DUF3595. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi9780.
NextBio36824.
PROQ92508.
SOURCESearch...

Entry information

Entry namePIEZ1_HUMAN
AccessionPrimary (citable) accession number: Q92508
Secondary accession number(s): A6NHT9, A7E2B7, Q0KKZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 115 of the entry and version 4 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

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 16

Human chromosome 16: entries, gene names and cross-references to MIM