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Protein

Piezo-type mechanosensitive ion channel component 1

Gene

PIEZO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pore-forming subunit of a mechanosensitive non-specific cation channel (PubMed:23479567, PubMed:23695678). Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. 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 (PubMed:20016066). In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation (PubMed:25119035). Plays a key role in blood vessel formation and vascular structure in both development and adult physiology (By similarity).By similarity4 Publications

GO - Molecular functioni

GO - Biological processi

  • cation transport Source: UniProtKB
  • positive regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
  • positive regulation of integrin activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000103335-MONOMER.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:28993. PIEZO1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei5 – 25HelicalSequence analysisAdd BLAST21
Transmembranei27 – 47HelicalSequence analysisAdd BLAST21
Transmembranei64 – 84HelicalSequence analysisAdd BLAST21
Transmembranei118 – 138HelicalSequence analysisAdd BLAST21
Transmembranei194 – 214HelicalSequence analysisAdd BLAST21
Transmembranei218 – 238HelicalSequence analysisAdd BLAST21
Transmembranei248 – 268HelicalSequence analysisAdd BLAST21
Transmembranei302 – 322HelicalSequence analysisAdd BLAST21
Transmembranei428 – 448HelicalSequence analysisAdd BLAST21
Transmembranei460 – 480HelicalSequence analysisAdd BLAST21
Transmembranei514 – 534HelicalSequence analysisAdd BLAST21
Transmembranei579 – 599HelicalSequence analysisAdd BLAST21
Transmembranei602 – 622HelicalSequence analysisAdd BLAST21
Transmembranei629 – 649HelicalSequence analysisAdd BLAST21
Transmembranei681 – 701HelicalSequence analysisAdd BLAST21
Transmembranei823 – 843HelicalSequence analysisAdd BLAST21
Transmembranei852 – 872HelicalSequence analysisAdd BLAST21
Transmembranei926 – 946HelicalSequence analysisAdd BLAST21
Transmembranei987 – 1007HelicalSequence analysisAdd BLAST21
Transmembranei1043 – 1063HelicalSequence analysisAdd BLAST21
Transmembranei1160 – 1180HelicalSequence analysisAdd BLAST21
Transmembranei1184 – 1204HelicalSequence analysisAdd BLAST21
Transmembranei1218 – 1240HelicalSequence analysisAdd BLAST23
Transmembranei1247 – 1264HelicalSequence analysisAdd BLAST18
Transmembranei1277 – 1297HelicalSequence analysisAdd BLAST21
Transmembranei1678 – 1698HelicalSequence analysisAdd BLAST21
Transmembranei1700 – 1720HelicalSequence analysisAdd BLAST21
Transmembranei1734 – 1754HelicalSequence analysisAdd BLAST21
Transmembranei1962 – 1982HelicalSequence analysisAdd BLAST21
Transmembranei2003 – 2023HelicalSequence analysisAdd BLAST21
Transmembranei2032 – 2052HelicalSequence analysisAdd BLAST21
Transmembranei2061 – 2081HelicalSequence analysisAdd BLAST21
Transmembranei2100 – 2122HelicalSequence analysisAdd BLAST23
Transmembranei2129 – 2149HelicalSequence analysisAdd BLAST21
Transmembranei2177 – 2197HelicalSequence analysisAdd BLAST21
Topological domaini2198 – 2431ExtracellularBy similarityAdd BLAST234
Transmembranei2432 – 2452HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Dehydrated hereditary stomatocytosis 1 with or without pseudohyperkalemia and/or perinatal edema (DHS1)6 Publications
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.
Disease descriptionAn 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.
See also OMIM:194380
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069822718G → S in DHS1. 1 PublicationCorresponds to variant rs755885744dbSNPEnsembl.1
Natural variantiVAR_069823782G → S in DHS1. 1 PublicationCorresponds to variant rs200970763dbSNPEnsembl.1
Natural variantiVAR_069824808R → Q in DHS1. 1 PublicationCorresponds to variant rs202103485dbSNPEnsembl.1
Natural variantiVAR_0698251117S → L in DHS1. 1 PublicationCorresponds to variant rs587777765dbSNPEnsembl.1
Natural variantiVAR_0698261358R → P in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 PublicationCorresponds to variant rs587776990dbSNPEnsembl.1
Natural variantiVAR_0698272003A → D in DHS1. 1 Publication1
Natural variantiVAR_0698282020A → T in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 PublicationCorresponds to variant rs587776989dbSNPEnsembl.1
Natural variantiVAR_0698292020A → V in DHS1. 1 PublicationCorresponds to variant rs587777764dbSNPEnsembl.1
Natural variantiVAR_0698302127T → M in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 2 PublicationsCorresponds to variant rs587776991dbSNPEnsembl.1
Natural variantiVAR_0698312166 – 2169Missing in DHS1. 1 Publication4
Natural variantiVAR_0698322225M → R in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 3 PublicationsCorresponds to variant rs587776987dbSNPEnsembl.1
Natural variantiVAR_0698332456R → H in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 6 PublicationsCorresponds to variant rs587776988dbSNPEnsembl.1
Natural variantiVAR_0698342488R → Q in DHS1; increased cation transport in erythroid cells. 1 PublicationCorresponds to variant rs749288233dbSNPEnsembl.1
Natural variantiVAR_0698352496E → ELE in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 Publication1
Lymphedema, hereditary, 3 (LMPH3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe form of lymphedema, a chronic disabling condition which results in swelling of the extremities due to altered lymphatic flow. Patients with lymphedema suffer from recurrent local infections, and physical impairment. LMPH3 manifests as generalized lymphatic dysplasia, characterized by uniform, widespread lymphedema affecting all segments of the body, with systemic involvement such as intestinal and/or pulmonary lymphangiectasia, pleural effusions, chylothoraces and/or pericardial effusions, and with a high incidence of non-immune hydrops fetalis.
See also OMIM:616843
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076407939L → M in LMPH3; unknown pathological significance; found in compound heterozygous state. 1 PublicationCorresponds to variant rs201226914dbSNPEnsembl.1
Natural variantiVAR_0764082430P → L in LMPH3; unknown pathological significance; found in compound heterozygous state. 1 Publication1
Natural variantiVAR_0764092456R → C in LMPH3; unknown pathological significance; found in compound heterozygous state. 1 Publication1
Natural variantiVAR_0764102458F → L in LMPH3; unknown pathological significance; found in compound heterozygous state. 1 PublicationCorresponds to variant rs577860843dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2456R → K: Does not inactivate the protein. gives rise to mechanically activated currents that inactivate more slowly than wild-type currents, suggesting it could shift the channel kinetics from phasic to tonic. 1 Publication1

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

DisGeNETi9780.
MalaCardsiPIEZO1.
MIMi194380. phenotype.
616843. phenotype.
OpenTargetsiENSG00000103335.
Orphaneti3202. Dehydrated hereditary stomatocytosis.

Polymorphism and mutation databases

BioMutaiPIEZO1.
DMDMi317373533.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001868171 – 2521Piezo-type mechanosensitive ion channel component 1Add BLAST2521

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi295N-linked (GlcNAc...)Sequence analysis1
Modified residuei734PhosphothreonineCombined sources1
Modified residuei758PhosphoserineCombined sources1
Modified residuei1391PhosphoserineCombined sources1
Modified residuei1396PhosphoserineCombined sources1
Modified residuei1636PhosphoserineCombined sources1
Modified residuei1646PhosphoserineCombined sources1
Modified residuei1854PhosphothreonineCombined sources1
Glycosylationi2294N-linked (GlcNAc...)1 Publication1
Disulfide bondi2411 ↔ 2415By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ92508.
MaxQBiQ92508.
PaxDbiQ92508.
PeptideAtlasiQ92508.
PRIDEiQ92508.

PTM databases

iPTMnetiQ92508.
PhosphoSitePlusiQ92508.

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

BgeeiENSG00000103335.
CleanExiHS_FAM38A.
ExpressionAtlasiQ92508. baseline and differential.
GenevisibleiQ92508. HS.

Organism-specific databases

HPAiHPA047185.

Interactioni

Subunit structurei

Homotrimer. Interacts with PKD2. Interacts with STOML3.By similarity

Protein-protein interaction databases

BioGridi115124. 11 interactors.
IntActiQ92508. 10 interactors.
MINTiMINT-4991257.
STRINGi9606.ENSP00000301015.

Structurei

3D structure databases

ProteinModelPortaliQ92508.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1339 – 1368Sequence analysisAdd BLAST30

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi6 – 91Leu-richAdd BLAST86

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1893. Eukaryota.
ENOG410YVF6. LUCA.
GeneTreeiENSGT00390000013029.
HOVERGENiHBG107901.
InParanoidiQ92508.
OMAiWDSICFF.
OrthoDBiEOG091G0SD8.
PhylomeDBiQ92508.
TreeFamiTF314295.

Family and domain databases

InterProiIPR027272. Piezo.
IPR031805. Piezo_dom.
IPR031334. Piezo_RRas-bd_dom.
[Graphical view]
PANTHERiPTHR13167. PTHR13167. 2 hits.
PfamiPF15917. PIEZO. 1 hit.
PF12166. Piezo_RRas_bdg. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92508-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPHVLGAVL YWLLLPCALL AACLLRFSGL SLVYLLFLLL LPWFPGPTRC
60 70 80 90 100
GLQGHTGRLL RALLGLSLLF LVAHLALQIC LHIVPRLDQL LGPSCSRWET
110 120 130 140 150
LSRHIGVTRL DLKDIPNAIR LVAPDLGILV VSSVCLGICG RLARNTRQSP
160 170 180 190 200
HPRELDDDER DVDASPTAGL QEAATLAPTR RSRLAARFRV TAHWLLVAAG
210 220 230 240 250
RVLAVTLLAL AGIAHPSALS SVYLLLFLAL CTWWACHFPI STRGFSRLCV
260 270 280 290 300
AVGCFGAGHL ICLYCYQMPL AQALLPPAGI WARVLGLKDF VGPTNCSSPH
310 320 330 340 350
ALVLNTGLDW PVYASPGVLL LLCYATASLR KLRAYRPSGQ RKEAAKGYEA
360 370 380 390 400
RELELAELDQ WPQERESDQH VVPTAPDTEA DNCIVHELTG QSSVLRRPVR
410 420 430 440 450
PKRAEPREAS PLHSLGHLIM DQSYVCALIA MMVWSITYHS WLTFVLLLWA
460 470 480 490 500
CLIWTVRSRH QLAMLCSPCI LLYGMTLCCL RYVWAMDLRP ELPTTLGPVS
510 520 530 540 550
LRQLGLEHTR YPCLDLGAML LYTLTFWLLL RQFVKEKLLK WAESPAALTE
560 570 580 590 600
VTVADTEPTR TQTLLQSLGE LVKGVYAKYW IYVCAGMFIV VSFAGRLVVY
610 620 630 640 650
KIVYMFLFLL CLTLFQVYYS LWRKLLKAFW WLVVAYTMLV LIAVYTFQFQ
660 670 680 690 700
DFPAYWRNLT GFTDEQLGDL GLEQFSVSEL FSSILVPGFF LLACILQLHY
710 720 730 740 750
FHRPFMQLTD MEHVSLPGTR LPRWAHRQDA VSGTPLLREE QQEHQQQQQE
760 770 780 790 800
EEEEEEDSRD EGLGVATPHQ ATQVPEGAAK WGLVAERLLE LAAGFSDVLS
810 820 830 840 850
RVQVFLRRLL ELHVFKLVAL YTVWVALKEV SVMNLLLVVL WAFALPYPRF
860 870 880 890 900
RPMASCLSTV WTCVIIVCKM LYQLKVVNPQ EYSSNCTEPF PNSTNLLPTE
910 920 930 940 950
ISQSLLYRGP VDPANWFGVR KGFPNLGYIQ NHLQVLLLLV FEAIVYRRQE
960 970 980 990 1000
HYRRQHQLAP LPAQAVFASG TRQQLDQDLL GCLKYFINFF FYKFGLEICF
1010 1020 1030 1040 1050
LMAVNVIGQR MNFLVTLHGC WLVAILTRRH RQAIARLWPN YCLFLALFLL
1060 1070 1080 1090 1100
YQYLLCLGMP PALCIDYPWR WSRAVPMNSA LIKWLYLPDF FRAPNSTNLI
1110 1120 1130 1140 1150
SDFLLLLCAS QQWQVFSAER TEEWQRMAGV NTDRLEPLRG EPNPVPNFIH
1160 1170 1180 1190 1200
CRSYLDMLKV AVFRYLFWLV LVVVFVTGAT RISIFGLGYL LACFYLLLFG
1210 1220 1230 1240 1250
TALLQRDTRA RLVLWDCLIL YNVTVIISKN MLSLLACVFV EQMQTGFCWV
1260 1270 1280 1290 1300
IQLFSLVCTV KGYYDPKEMM DRDQDCLLPV EEAGIIWDSV CFFFLLLQRR
1310 1320 1330 1340 1350
VFLSHYYLHV RADLQATALL ASRGFALYNA ANLKSIDFHR RIEEKSLAQL
1360 1370 1380 1390 1400
KRQMERIRAK QEKHRQGRVD RSRPQDTLGP KDPGLEPGPD SPGGSSPPRR
1410 1420 1430 1440 1450
QWWRPWLDHA TVIHSGDYFL FESDSEEEEE AVPEDPRPSA QSAFQLAYQA
1460 1470 1480 1490 1500
WVTNAQAVLR RRQQEQEQAR QEQAGQLPTG GGPSQEVEPA EGPEEAAAGR
1510 1520 1530 1540 1550
SHVVQRVLST AQFLWMLGQA LVDELTRWLQ EFTRHHGTMS DVLRAERYLL
1560 1570 1580 1590 1600
TQELLQGGEV HRGVLDQLYT SQAEATLPGP TEAPNAPSTV SSGLGAEEPL
1610 1620 1630 1640 1650
SSMTDDMGSP LSTGYHTRSG SEEAVTDPGE REAGASLYQG LMRTASELLL
1660 1670 1680 1690 1700
DRRLRIPELE EAELFAEGQG RALRLLRAVY QCVAAHSELL CYFIIILNHM
1710 1720 1730 1740 1750
VTASAGSLVL PVLVFLWAML SIPRPSKRFW MTAIVFTEIA VVVKYLFQFG
1760 1770 1780 1790 1800
FFPWNSHVVL RRYENKPYFP PRILGLEKTD GYIKYDLVQL MALFFHRSQL
1810 1820 1830 1840 1850
LCYGLWDHEE DSPSKEHDKS GEEEQGAEEG PGVPAATTED HIQVEARVGP
1860 1870 1880 1890 1900
TDGTPEPQVE LRPRDTRRIS LRFRRRKKEG PARKGAAAIE AEDREEEEGE
1910 1920 1930 1940 1950
EEKEAPTGRE KRPSRSGGRV RAAGRRLQGF CLSLAQGTYR PLRRFFHDIL
1960 1970 1980 1990 2000
HTKYRAATDV YALMFLADVV DFIIIIFGFW AFGKHSAATD ITSSLSDDQV
2010 2020 2030 2040 2050
PEAFLVMLLI QFSTMVVDRA LYLRKTVLGK LAFQVALVLA IHLWMFFILP
2060 2070 2080 2090 2100
AVTERMFNQN VVAQLWYFVK CIYFALSAYQ IRCGYPTRIL GNFLTKKYNH
2110 2120 2130 2140 2150
LNLFLFQGFR LVPFLVELRA VMDWVWTDTT LSLSSWMCVE DIYANIFIIK
2160 2170 2180 2190 2200
CSRETEKKYP QPKGQKKKKI VKYGMGGLII LFLIAIIWFP LLFMSLVRSV
2210 2220 2230 2240 2250
VGVVNQPIDV TVTLKLGGYE PLFTMSAQQP SIIPFTAQAY EELSRQFDPQ
2260 2270 2280 2290 2300
PLAMQFISQY SPEDIVTAQI EGSSGALWRI SPPSRAQMKR ELYNGTADIT
2310 2320 2330 2340 2350
LRFTWNFQRD LAKGGTVEYA NEKHMLALAP NSTARRQLAS LLEGTSDQSV
2360 2370 2380 2390 2400
VIPNLFPKYI RAPNGPEANP VKQLQPNEEA DYLGVRIQLR REQGAGATGF
2410 2420 2430 2440 2450
LEWWVIELQE CRTDCNLLPM VIFSDKVSPP SLGFLAGYGI MGLYVSIVLV
2460 2470 2480 2490 2500
IGKFVRGFFS EISHSIMFEE LPCVDRILKL CQDIFLVRET RELELEEELY
2510 2520
AKLIFLYRSP ETMIKWTREK E
Length:2,521
Mass (Da):286,790
Last modified:January 11, 2011 - v4
Checksum:i127A3DA3E7CBD2DD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti750Missing in BAA13240 (PubMed:9039502).Curated1
Sequence conflicti750Missing in AAI50272 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069822718G → S in DHS1. 1 PublicationCorresponds to variant rs755885744dbSNPEnsembl.1
Natural variantiVAR_069823782G → S in DHS1. 1 PublicationCorresponds to variant rs200970763dbSNPEnsembl.1
Natural variantiVAR_069824808R → Q in DHS1. 1 PublicationCorresponds to variant rs202103485dbSNPEnsembl.1
Natural variantiVAR_076407939L → M in LMPH3; unknown pathological significance; found in compound heterozygous state. 1 PublicationCorresponds to variant rs201226914dbSNPEnsembl.1
Natural variantiVAR_0698251117S → L in DHS1. 1 PublicationCorresponds to variant rs587777765dbSNPEnsembl.1
Natural variantiVAR_0698261358R → P in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 PublicationCorresponds to variant rs587776990dbSNPEnsembl.1
Natural variantiVAR_0698272003A → D in DHS1. 1 Publication1
Natural variantiVAR_0698282020A → T in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 PublicationCorresponds to variant rs587776989dbSNPEnsembl.1
Natural variantiVAR_0698292020A → V in DHS1. 1 PublicationCorresponds to variant rs587777764dbSNPEnsembl.1
Natural variantiVAR_0698302127T → M in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 2 PublicationsCorresponds to variant rs587776991dbSNPEnsembl.1
Natural variantiVAR_0698312166 – 2169Missing in DHS1. 1 Publication4
Natural variantiVAR_0698322225M → R in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 3 PublicationsCorresponds to variant rs587776987dbSNPEnsembl.1
Natural variantiVAR_0764082430P → L in LMPH3; unknown pathological significance; found in compound heterozygous state. 1 Publication1
Natural variantiVAR_0764092456R → C in LMPH3; unknown pathological significance; found in compound heterozygous state. 1 Publication1
Natural variantiVAR_0698332456R → H in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 6 PublicationsCorresponds to variant rs587776988dbSNPEnsembl.1
Natural variantiVAR_0764102458F → L in LMPH3; unknown pathological significance; found in compound heterozygous state. 1 PublicationCorresponds to variant rs577860843dbSNPEnsembl.1
Natural variantiVAR_0698342488R → Q in DHS1; increased cation transport in erythroid cells. 1 PublicationCorresponds to variant rs749288233dbSNPEnsembl.1
Natural variantiVAR_0698352496E → ELE in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001142864.3.
UniGeneiHs.377001.
Hs.592074.

Genome annotation databases

EnsembliENST00000301015; ENSP00000301015; ENSG00000103335.
GeneIDi9780.
KEGGihsa:9780.
UCSCiuc010vpb.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001142864.3.
UniGeneiHs.377001.
Hs.592074.

3D structure databases

ProteinModelPortaliQ92508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115124. 11 interactors.
IntActiQ92508. 10 interactors.
MINTiMINT-4991257.
STRINGi9606.ENSP00000301015.

Protein family/group databases

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

PTM databases

iPTMnetiQ92508.
PhosphoSitePlusiQ92508.

Polymorphism and mutation databases

BioMutaiPIEZO1.
DMDMi317373533.

Proteomic databases

EPDiQ92508.
MaxQBiQ92508.
PaxDbiQ92508.
PeptideAtlasiQ92508.
PRIDEiQ92508.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301015; ENSP00000301015; ENSG00000103335.
GeneIDi9780.
KEGGihsa:9780.
UCSCiuc010vpb.3. human.

Organism-specific databases

CTDi9780.
DisGeNETi9780.
GeneCardsiPIEZO1.
H-InvDBHIX0022749.
HIX0173225.
HGNCiHGNC:28993. PIEZO1.
HPAiHPA047185.
MalaCardsiPIEZO1.
MIMi194380. phenotype.
611184. gene.
616843. phenotype.
neXtProtiNX_Q92508.
OpenTargetsiENSG00000103335.
Orphaneti3202. Dehydrated hereditary stomatocytosis.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1893. Eukaryota.
ENOG410YVF6. LUCA.
GeneTreeiENSGT00390000013029.
HOVERGENiHBG107901.
InParanoidiQ92508.
OMAiWDSICFF.
OrthoDBiEOG091G0SD8.
PhylomeDBiQ92508.
TreeFamiTF314295.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000103335-MONOMER.

Miscellaneous databases

ChiTaRSiPIEZO1. human.
GenomeRNAii9780.
PROiQ92508.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103335.
CleanExiHS_FAM38A.
ExpressionAtlasiQ92508. baseline and differential.
GenevisibleiQ92508. HS.

Family and domain databases

InterProiIPR027272. Piezo.
IPR031805. Piezo_dom.
IPR031334. Piezo_RRas-bd_dom.
[Graphical view]
PANTHERiPTHR13167. PTHR13167. 2 hits.
PfamiPF15917. PIEZO. 1 hit.
PF12166. Piezo_RRas_bdg. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.