PPP1R12A

PPP1R12A
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	2KJY, 2MXR, 5HUZ
Identifikatori
Aliasi	PPP1R12A
Vanjski ID-jevi	OMIM: 602021 MGI: 1309528 HomoloGene: 1855 GeneCards: PPP1R12A
Lokacija gena (čovjek)
Hrom.	Hromosom 12 (čovjek)
Kraj	79,935,460 bp
Lokacija gena (miš)
Hrom.	Hromosom 10 (miš)
Kraj	108,120,336 bp
Obrazac RNK ekspresije
	; ; ; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• GO:0048551 enzyme inhibitor activity; • 14-3-3 protein binding; • signal transducer activity; • GO:0001948, GO:0016582 vezivanje za proteine; • protein kinase binding; • phosphatase regulator activity;
Ćelijska komponenta	• centrosom; • focal adhesion; • nukleoplazma; • Z discdkac; • PTW/PP1 phosphatase complex; • actin cytoskeleton; • contractile fiber; • A band; • kinetohor; • citoplazma; • citosol; • citoskelet;
Biološki proces	• regulation of nucleocytoplasmic transport; • positive regulation of myosin-light-chain-phosphatase activity; • GO:0048553 negative regulation of catalytic activity; • regulation of cell adhesion; • G2/M transition of mitotic cell cycle; • regulation of myosin-light-chain-phosphatase activity; • regulation of establishment of endothelial barrier; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • GO:0072468 Transdukcija signala; • GO:0016576 protein dephosphorylation; • GO:0007067 Mitoza; • centrosome cycle;
	Izvori:Amigo / QuickGO
Ortolozi
	4659
	17931
	ENSG00000058272
	ENSMUSG00000019907
	O14974
	Q9DBR7
	NM_001143885; NM_001143886; NM_001244990; NM_001244992; NM_002480
	NM_027892; NM_001368736; NM_001368737
	NP_001137357; NP_001137358; NP_001231919; NP_001231921; NP_002471
	NP_082168; NP_001355665; NP_001355666
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Regulacijska podjedinica 12A protein-fosfataze 1 je enzim koji je kod ljudi kodiran genom PPP1R12A.^[5]^[6]

Ciljna podjedinica miozin-fosfataze 1, koja se naziva i miozin-vezujuća podjedinica miozin-fosfataze, jedna je od podjedinica ove fosfataze. Miozin-fosfataza regulira interakciju aktina i miozina nizvodno od gvanozin-trifosfataze Rho. U fosforilaciju lahkog lanca miozina (MLC), uključena je mala gvanozin-trifosfataza Rho, što rezultira kontrakcijom glatkih mišića^[7] i interakcija aktina i miozina u nemišićnim ćelijama. Aktivni oblik RhoA (GTP.RhoA) vezan za gvanozin-trifosfat (GTP) specifično stupa u interakciju s podjedinicom koja veže miozin (MBS) iz miozin-fosfataze, koja regulira opseg fosforilacije MLC. Rho-asocirana kinaza (Rho-kinaza), koju aktivira GTP. RhoA, fosforilirani MBS i inaktivirana miozin fosfataza. Prekomjerna ekspresija RhoA ili aktiviranog RhoA u ćelijama NIH 3T3 povećala je razinu fosforilacije MBS i MLC. Stoga se čini da Rho inhibira miozin-fosfatazu, djelovanjem Rho-kinaze.^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 1.030 aminokiselina, a molekulska težina 115.281 Da.^[8]

10	20	30	40	50
MKMADAKQKR	NEQLKRWIGS	ETDLEPPVVK	RQKTKVKFDD	GAVFLAACSS
GDTDEVLKLL	HRGADINYAN	VDGLTALHQA	CIDDNVDMVK	FLVENGANIN
QPDNEGWIPL	HAAASCGYLD	IAEFLIGQGA	HVGAVNSEGD	TPLDIAEEEA
MEELLQNEVN	RQGVDIEAAR	KEEERIMLRD	ARQWLNSGHI	NDVRHAKSGG
TALHVAAAKG	YTEVLKLLIQ	AGYDVNIKDY	DGWTPLHAAA	HWGKEEACRI
LVDNLCDMEM	VNKVGQTAFD	VADEDILGYL	EELQKKQNLL	HSEKRDKKSP
LIESTANMDN	NQSQKTFKNK	ETLIIEPEKN	ASRIESLEQE	KVDEEEEGKK
DESSCSSEED	EEDDSESEAE	TDKTKPLASV	TNANTSSTQA	APVAVTTPTV
SSGQATPTSP	IKKFPTTATK	ISPKEEERKD	ESPATWRLGL	RKTGSYGALA
EITASKEGQK	EKDTAGVTRS	ASSPRLSSSL	DNKEKEKDSK	GTRLAYVAPT
IPRRLASTSD	IEEKENRDSS	SLRTSSSYTR	RKWEDDLKKN	SSVNEGSTYH
KSCSFGRRQD	DLISSSVPST	TSTPTVTSAA	GLQKSLLSST	STTTKITTGS
SSAGTQSSTS	NRLWAEDSTE	KEKDSVPTAV	TIPVAPTVVN	AAASTTTLTT
TTAGTVSSTT	EVRERRRSYL	TPVRDEESES	QRKARSRQAR	QSRRSTQGVT
LTDLQEAEKT	IGRSRSTRTR	EQENEEKEKE	EKEKQDKEKQ	EEKKESETSR
EDEYKQKYSR	TYDETYQRYR	PVSTSSSTTP	SSSLSTMSSS	LYASSQLNRP
NSLVGITSAY	SRGITKENER	EGEKREEEKE	GEDKSQPKSI	RERRRPREKR
RSTGVSFWTQ	DSDENEQEQQ	SDTEEGSNKK	ETQTDSISRY	ETSSTSAGDR
YDSLLGRSGS	YSYLEERKPY	SSRLEKDDST	DFKKLYEQIL	AENEKLKAQL
HDTNMELTDL	KLQLEKATQR	QERFADRSLL	EMEKRERRAL	ERRISEMEEE
LKMLPDLKAD	NQRLKDENGA	LIRVISKLSK

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

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000058272 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000019907 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Takahashi N, Ito M, Tanaka J, Nakano T, Kaibuchi K, Odai H, Takemura K (Nov 1997). "Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21". Genomics. 44 (1): 150–2. doi:10.1006/geno.1997.4859. PMID 9286714.
^ ^a ^b "Entrez Gene: PPP1R12A protein phosphatase 1, regulatory (inhibitor) subunit 12A".
^ Michael P. Walsh; et all. "Thromboxane A2-induced contraction of rat caudal arterial smooth muscle involves activation of Ca2+ entry and Ca2+sensitization: Rho-associated kinase-mediated phosphorylation of MYPT1 at Thr-855 but not Thr-697" (PDF). Arhivirano s originala (PDF), 13. 7. 2011.
^ "UniProt, O14974". Pristupljeno 13. 8. 2021.

Dopunska literatura

Somlyo AP, Wu X, Walker LA, Somlyo AV (1999). "Pharmacomechanical coupling: the role of calcium, G-proteins, kinases and phosphatases". Rev. Physiol. Biochem. Pharmacol. 134: 201–34. doi:10.1007/3-540-64753-8_5. ISBN 978-3-540-64753-9. PMID 10087910.
Ziter FA, Wiser WC, Robinson A (1977). "Three-generation pedigree of a Möbius syndrome variant with chromosome translocation". Arch. Neurol. 34 (7): 437–42. doi:10.1001/archneur.1977.00500190071011. PMID 880069.
Slee JJ, Smart RD, Viljoen DL (1991). "Deletion of chromosome 13 in Moebius syndrome". J. Med. Genet. 28 (6): 413–4. doi:10.1136/jmg.28.6.413. PMC 1016909. PMID 1870098.
Kimura K, Ito M, Amano M, et al. (1996). "Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)". Science. 273 (5272): 245–8. Bibcode:1996Sci...273..245K. doi:10.1126/science.273.5272.245. PMID 8662509. S2CID 37249779.
Ito M, Feng J, Tsujino S, et al. (1997). "Interaction of smooth muscle myosin phosphatase with phospholipids". Biochemistry. 36 (24): 7607–14. doi:10.1021/bi9702647. PMID 9200713.
Nakai K, Suzuki Y, Kihira H, et al. (1997). "Regulation of myosin phosphatase through phosphorylation of the myosin-binding subunit in platelet activation". Blood. 90 (10): 3936–42. doi:10.1182/blood.V90.10.3936. PMID 9354661.
Somlyo AP (1999). "Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser". J. Physiol. 516 (3): 630. doi:10.1111/j.1469-7793.1999.0630u.x. PMC 2269296. PMID 10200412.
Surks HK, Mochizuki N, Kasai Y, et al. (1999). "Regulation of myosin phosphatase by a specific interaction with cGMP- dependent protein kinase Ialpha". Science. 286 (5444): 1583–7. doi:10.1126/science.286.5444.1583. PMID 10567269.
Feng J, Ito M, Ichikawa K, et al. (2000). "Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase". J. Biol. Chem. 274 (52): 37385–90. doi:10.1074/jbc.274.52.37385. PMID 10601309.
Arimura T, Suematsu N, Zhou YB, et al. (2001). "Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit". J. Biol. Chem. 276 (9): 6073–82. doi:10.1074/jbc.M008566200. PMID 11067852.
Sebbagh M, Renvoizé C, Hamelin J, et al. (2001). "Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing". Nat. Cell Biol. 3 (4): 346–52. doi:10.1038/35070019. PMID 11283607. S2CID 36187702.
Murányi A, Zhang R, Liu F, et al. (2001). "Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity". FEBS Lett. 493 (2–3): 80–4. doi:10.1016/S0014-5793(01)02283-9. PMID 11287000. S2CID 26428853.
Machida H, Ito M, Okamoto R, et al. (2001). "Molecular cloning and analysis of the 5'-flanking region of the human MYPT1 gene". Biochim. Biophys. Acta. 1517 (3): 424–9. doi:10.1016/s0167-4781(00)00285-2. PMID 11342221.
Kiss E, Murányi A, Csortos C, et al. (2002). "Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton". Biochem. J. 365 (Pt 1): 79–87. doi:10.1042/BJ20011295. PMC 1222641. PMID 11931630.
Velasco G, Armstrong C, Morrice N, et al. (2002). "Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin". FEBS Lett. 527 (1–3): 101–4. doi:10.1016/S0014-5793(02)03175-7. PMID 12220642. S2CID 39366441.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Kitazawa T, Eto M, Woodsome TP, Khalequzzaman M (2003). "Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca2+ sensitization in rabbit smooth muscle". J. Physiol. 546 (Pt 3): 879–89. doi:10.1113/jphysiol.2002.029306. PMC 2342583. PMID 12563012.
Seko T, Ito M, Kureishi Y, et al. (2003). "Activation of RhoA and inhibition of myosin phosphatase as important components in hypertension in vascular smooth muscle". Circ. Res. 92 (4): 411–8. doi:10.1161/01.RES.0000059987.90200.44. PMID 12600888.

Vanjski linkovi

PPP1R12A Info with links in the Cell Migration Gateway Arhivirano 11. 12. 2014. na Wayback Machine

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000058272 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000019907 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9286714-5] Takahashi N, Ito M, Tanaka J, Nakano T, Kaibuchi K, Odai H, Takemura K (Nov 1997). "Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21". Genomics. 44 (1): 150–2. doi:10.1006/geno.1997.4859. PMID 9286714.

[entrez-6] "Entrez Gene: PPP1R12A protein phosphatase 1, regulatory (inhibitor) subunit 12A".

[7] Michael P. Walsh; et all. "Thromboxane A2-induced contraction of rat caudal arterial smooth muscle involves activation of Ca2+ entry and Ca2+sensitization: Rho-associated kinase-mediated phosphorylation of MYPT1 at Thr-855 but not Thr-697" (PDF). Arhivirano s originala (PDF), 13. 7. 2011.

[UniProt-8] "UniProt, O14974". Pristupljeno 13. 8. 2021.

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