PPP1R12A
entrez
4659
canonical
uniprot
O14974
canonical
ensembl
ENSG00000058272
resolver
ensp
ENSP00000261207
resolver
ensp
ENSP00000389168
resolver
ensp
ENSP00000416769
resolver
ensp
ENSP00000446855
resolver
ensp
ENSP00000449514
resolver
genesymbol
PPP1R12A
resolver
genesymbol_syn
MBS
resolver
genesymbol_syn
MYPT1
resolver
hgnc
HGNC:7618
resolver
uniprot
B2RAH5
resolver
uniprot
B4DZ09
resolver
uniprot
F8VWB4
resolver
uniprot
Q2NKL4
resolver
uniprot
Q569H0
resolver
uniprot
Q86WU3
resolver
uniprot
Q8NFR6
resolver
uniprot
Q9BYH0
resolver
uniprot_entry
B2RAH5_HUMAN
resolver
uniprot_entry
MYPT1_HUMAN
resolver
uniprot_sec
B4DZ09
resolver
uniprot_sec
F8VWB4
resolver
uniprot_sec
Q2NKL4
resolver
uniprot_sec
Q569H0
resolver
uniprot_sec
Q86WU3
resolver
uniprot_sec
Q8NFR6
resolver
uniprot_sec
Q9BYH0
resolver
amino_acid_sequence
MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIEPEKNASRIESLEQEKVDEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPLASVTNANTSSTQAAPVAVTTPTVSSGQATPTSPIKKFPTTATKISPKEEERKDESPATWRLGLRKTGSYGALAEITASKEGQKEKDTAGVTRSASSPRLSSSLDNKEKEKDSKGTRLAYVAPTIPRRLASTSDIEEKENRDSSSLRTSSSYTRRKWEDDLKKNSSVNEGSTYHKSCSFGRRQDDLISSSVPSTTSTPTVTSAAGLQKSLLSSTSTTTKITTGSSSAGTQSSTSNRLWAEDSTEKEKDSVPTAVTIPVAPTVVNAAASTTTLTTTTAGTVSSTTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESETSREDEYKQKYSRTYDETYQRYRPVSTSSSTTPSSSLSTMSSSLYASSQLNRPNSLVGITSAYSRGITKENEREGEKREEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPYSSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSLLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK
uniprot
proteins
disease_involvement
DISEASE: Genitourinary and/or brain malformation syndrome (GUBS) [MIM:618820]: An autosomal dominant syndrome characterized by multiple congenital anomalies including urogenital malformations and brain abnormalities ranging from agenesis of the corpus callosum to anencephaly. {ECO:0000269|PubMed:31883643}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity. {ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:20354225}.
uniprot
proteins
mass_dalton
115281
uniprot
proteins
mutagenesis
MUTAGEN 445; /note="S->A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-472 and A-910."; MUTAGEN 472; /note="S->A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-910."; MUTAGEN 473; /note="S->A: Abolishes binding to the POLO box domains of PLK1."; /evidence="ECO:0000269|PubMed:18477460"; MUTAGEN 910; /note="S->A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-472."; MUTAGEN 1007; /note="L->A: Loss of binding to PRKG1; when associated with A-1014."; /evidence="ECO:0000269|PubMed:12873707"; MUTAGEN 1014; /note="L->A: Loss of binding to PRKG1; when associated with A-1007."; /evidence="ECO:0000269|PubMed:12873707"; MUTAGEN 1021; /note="L->A: Loss of binding to PRKG1; when associated with A-1028."; /evidence="ECO:0000269|PubMed:12873707"; MUTAGEN 1028; /note="L->A: Loss of binding to PRKG1; when associated with A-1021."; /evidence="ECO:0000269|PubMed:12873707
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CIT (Rho-associated kinase) (By similarity). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-696. Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-695 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-696, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-910 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-696 by DMPK; may inhibit the myosin phosphatase activity. Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates PPP1R12A. {ECO:0000250, ECO:0000269|PubMed:10567269, ECO:0000269|PubMed:11283607, ECO:0000269|PubMed:11287000, ECO:0000269|PubMed:11331307, ECO:0000269|PubMed:11719507, ECO:0000269|PubMed:12773565, ECO:0000269|PubMed:15194681, ECO:0000269|PubMed:15723050, ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19701943, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:20354225, ECO:0000269|PubMed:21457715}.
uniprot
proteins
pubmed
10567269
uniprot
proteins
pubmed
11067852
uniprot
proteins
pubmed
11283607
uniprot
proteins
pubmed
11287000
uniprot
proteins
pubmed
11331307
uniprot
proteins
pubmed
11342221
uniprot
proteins
pubmed
11719507
uniprot
proteins
pubmed
12773565
uniprot
proteins
pubmed
12873707
uniprot
proteins
pubmed
12923170
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15194681
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15723050
uniprot
proteins
pubmed
16417406
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17126281
uniprot
proteins
pubmed
17904578
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18477460
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18782776
uniprot
proteins
pubmed
19131646
uniprot
proteins
pubmed
19245366
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19701943
uniprot
proteins
pubmed
19997641
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20354225
uniprot
proteins
pubmed
20634291
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21457715
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
31883643
uniprot
proteins
pubmed
9286714
uniprot
proteins
sequence_length
1030
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12923170, ECO:0000269|PubMed:18477460}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:12923170}. Note=Also along actomyosin filaments. {ECO:0000269|PubMed:12923170}.
uniprot
proteins