Wikipedia

PTPN11

Tirozin-nereceptorski fosfatazni protein tip 11 (PTPN11), znan i kao protein-tirozinska fosfataza 1D (PTP-1D), Src homologijska regija 2 sa domenom fosfataze-2 (SHP-2) ili protein-tirozin fosfataza 2C (PTP-2C) je enzim koji je klod ljudi kodiran]g [genom PTPN11. PTPN11 je proteinska tirozin-fosfataza (PTP) Shp2.[5][6]

PTPN11
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

2SHP, 3B7O, 3MOW, 3O5X, 3TKZ, 3TL0, 4DGP, 4DGX, 4GWF, 4H1O, 4JE4, 4JEG, 3ZM0, 3ZM1, 3ZM2, 3ZM3, 4H34, 4JMG, 4NWF, 4NWG, 4OHD, 4OHE, 4OHH, 4OHI, 4OHL, 4PVG, 4RDD, 4QSY, 5DF6, 5IBS, 5EHP, 5EHR, 5I6V, 5IBM

Identifikatori
AliasiPTPN11
Vanjski ID-jeviOMIM: 176876 MGI: 99511 HomoloGene: 2122 GeneCards: PTPN11
Lokacija gena (čovjek)
Hromosom 12 (čovjek)
Hrom.Hromosom 12 (čovjek)[1]
Hromosom 12 (čovjek)
Genomska lokacija za PTPN11
Genomska lokacija za PTPN11
Bend12q24.13Početak112,418,351 bp[1]
Kraj112,509,918 bp[1]
Lokacija gena (miš)
Hromosom 5 (miš)
Hrom.Hromosom 5 (miš)[2]
Hromosom 5 (miš)
Genomska lokacija za PTPN11
Genomska lokacija za PTPN11
Bend5|5 FPočetak121,268,596 bp[2]
Kraj121,329,460 bp[2]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija• phospholipase binding
• phosphoprotein phosphatase activity
• insulin receptor binding
• GO:0098519, GO:0098518 phosphatase activity
• receptor tyrosine kinase binding
• peptide hormone receptor binding
• GO:0001948, GO:0016582 vezivanje za proteine
• non-membrane spanning protein tyrosine phosphatase activity
• hydrolase activity
• phosphatidylinositol-4,5-bisphosphate 3-kinase activity
• 1-phosphatidylinositol-3-kinase activity
• cell adhesion molecule binding
• protein tyrosine phosphatase activity
• phosphotyrosine residue binding
• protein domain specific binding
• D1 dopamine receptor binding
• insulin receptor substrate binding
• protein tyrosine kinase binding
• protein kinase binding
Ćelijska komponenta• citoplazma
• citosol
• mitohondrija
• jedro
• nukleoplazma
• GO:0009327 makromolekulani kompleks
Biološki proces• GO:0098501, GO:0098502, GO:0006286 Defosforilacija
• megakaryocyte development
• positive regulation of signal transduction
• negative regulation of insulin secretion
• regulation of cell adhesion mediated by integrin
• atrioventricular canal development
• intestinal epithelial cell migration
• organ growth
• epidermal growth factor receptor signaling pathway
• negative regulation of growth hormone secretion
• axonogenesis
• glucose homeostasis
• regulation of protein export from nucleus
• multicellular organism growth
• regulation of multicellular organism growth
• lipid metabolism
• ephrin receptor signaling pathway
• abortive mitotic cell cycle
• DNA damage checkpoint signaling
• GO:0016576 protein dephosphorylation
• T cell costimulation
• platelet formation
• microvillus organization
• positive regulation of mitotic cell cycle
• genitalia development
• platelet activation
• fibroblast growth factor receptor signaling pathway
• heart development
• brain development
• regulation of type I interferon-mediated signaling pathway
• hormone-mediated signaling pathway
• integrin-mediated signaling pathway
• Bergmann glial cell differentiation
• homeostasis of number of cells within a tissue
• inner ear development
• platelet-derived growth factor receptor signaling pathway
• negative regulation of cortisol secretion
• peptidyl-tyrosine dephosphorylation
• ERBB signaling pathway
• negative regulation of hormone secretion
• triglyceride metabolic process
• hormone metabolic process
• positive regulation of hormone secretion
• negative regulation of cell adhesion mediated by integrin
• GO:0106159 regulation of protein-containing complex assembly
• face morphogenesis
• cerebellar cortex formation
• leukocyte migration
• multicellular organismal reproductive process
• phosphatidylinositol phosphate biosynthetic process
• neurotrophin TRK receptor signaling pathway
• phosphatidylinositol-3-phosphate biosynthetic process
• axon guidance
• positive regulation of ERK1 and ERK2 cascade
• cellular response to epidermal growth factor stimulus
• positive regulation of protein kinase B signaling
• cytokine-mediated signaling pathway
• interleukin-6-mediated signaling pathway
• cellular response to cytokine stimulus
• cellular response to mechanical stimulus
• positive regulation of interferon-beta production
• positive regulation of interleukin-6 production
• positive regulation of tumor necrosis factor production
• positive regulation of glucose import
• GO:1903106 positive regulation of insulin receptor signaling pathway
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez

5781

19247

Ensembl

ENSG00000179295

ENSMUSG00000043733

UniProt

Q06124

P35235

RefSeq (mRNK)

NM_002834
NM_080601
NM_001330437
NM_001374625
NM_018508

NM_001109992
NM_011202

RefSeq (bjelančevina)

NP_001317366
NP_002825
NP_542168
NP_001361554

NP_001103462
NP_035332

Lokacija (UCSC)Chr 12: 112.42 – 112.51 MbChr 5: 121.27 – 121.33 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

PTPN11 je član porodice proteinskih tirozin-fosfataza (PTP). Poznato PTP signalne molekule reguliraju različite ćelijske procese, uključujući ćelijski rastra, diferencijaciju, mitotski ciklus i onkogenu transformaciju. Ovaj PTP sadrži dva tandem Src homologijske-2 domena, koji funkcioniraju kao domeni za vezanje fosfo-tirozina i posreduju u interakciji ovog PTP-a sa supstratima. Široko eksprimiran u većini tkiva i ima regulatornu ulogu u raznim ćelijskim signalnim događajima, koji su važni za različite ćelijske funkcije, poput mitogene aktivacije, metaboličke kontrole, regulacije transkripcije i migracije ćelija. Mutacije u ovom genu su uzrok Noonanovog sindroma, kao i akutne mijeloidne leukemije.[7]

Aminokiselinska sekvenca uredi

Dužina polipeptidnog lanca je 597 aminokiselina, a molekulska težina 68.436 Da.[8]

1020304050
MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGA
VTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKY
PLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLS
VRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKN
PMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEE
FETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEP
VSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS
RVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRE
LKLSKVGQALLQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQ
ESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQM
VRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIK
YSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR
Simboli

C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin

Struktura i funkcija uredi

Ova fosfataza, zajedno sa svojim paralogom, Shp1, ima domensku strukturu koja se sastoji od dva tandemska SH2 domena u N-kraju, praćena domenom proteinske tirozin-fosfataze (PTP). U neaktivnom stanju, N2-terminalni SH2 domen veže PTP domen i blokira pristup potencijalnih podloga aktivnom mjestu. Dakle, Shp2 se automatski inhibira.

Nakon vezivanja za ciljne fosfo-tirozilne ostatke, N-terminalni SH2 domen oslobađa se iz PTP domena, katalitski aktivirajući enzim, oslobađanjem od ove auto-inhibicije.

Nasljedne bolesti povezane sa PTPN11 uredi

Misense mutacije u lokusu PTPN11 povezane su sa Noonnovim i Leopardovim sindromom.

Također je povezan sa metahondromatozom.[9]

Noonanov sindrom uredi

U slučaju Noonanovog sindroma, mutacije su široko raspoređene po kodirajućoj regiji gena, ali čini se da sve rezultiraju hiperaktiviranim ili nereguliranim mutantnim oblicima proteina. Većina ovih mutacija remeti vezujući interfejsa između domena N-SH2 i katalitifskog jezgra neophodnog da bi enzim održao autoinhibiranu konformaciju.[10]

Leopardov sindrom uredi

Mutacije koje uzrokuju Leopardov sindrom ograničene su regije koje utiču na katalitsko jezgro enzima za proizvodnju katalitski oštećene varijante Shp2.[11] Još nije jasno kako mutacije koje uzrokuju mutantne varijante Shp2 s biohemijski suprotnim karakteristikama rezultiraju sličnim ljudskim genetičkim sindromima.

Kancer povezan sa PTPN11 uredi

Pacijenti sa podskupinom mutacija PTPN11 Noonanovog sindroma također imaju veću prevalenciju juvenilne mijelomonocitne leukemije s (JMML). Aktivirajuće mutacije Shp2 također su otkrivene u neuroblastomu, melanomu, akutnoj mijeloidnoj leukemiji, raku dojke, pluća i kolorektumskom karcinomu.[12] Nedavno je otkrivena relativno velika prevalencija PTPN11 mutacija (24%) slijedećom generacijom sekvenciranja u kohorti mutiranih pacijenata NPM1 – akutna mijeloidna leukemija,[13] iako prognostički značaj takvih pridruživanja nije razjašnjen. Ovi podaci ukazuju na to da bi Shp2 mogao biti protoonkogen. Međutim, prijavljeno je da PTPN11/Shp2 može djelovati ili kao tumorski promotor ili supresor.[14] U starijem mišjem modelu, delecija PTPN11 / Shp2 specifična za hepatocite podstiče upalnu signalizaciju putem STAT3 i upale jetre /nekroze, što rezultira regenerativnom hiperplazijom i spontanim razvojem tumora. Smanjena ekspresija PTPN11 / Shp2 otkrivena je u potfrakciji ljudskim hepatoćelijskim karcinomma (HCC).[14] Bakterija Helicobacter pylori povezana je s rakom želuca, a smatra se da je to djelomično posredovano interakcijom njenog faktora virulencije CagA s SHP2.[15]

H faktor virulencije Pylori CagA uredi

CagA je protein i faktor virulencije insertiran iz Helicobacter pylori u epitel želuca. Fosforilacijom aktivirani SRC, CagA veže se za SHP2, alosterino ga aktivirajući. To dovodi do morfoloških promjena, abnormalniih mitogenih signala i trajne aktivnosti, što može rezultirati apoptozom ćelijee domaćina.

Epidemiološke studije pokazale su ulogu cagA-pozitivnog H. pylori u razvoju atrofijskog gastritisa, čira na želucu bolesti i karcinom želuca.[16]

Interakcije uredi

Pokazalo se da PTPN11 ima interakcije sa

Reference uredi

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