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Protein

Protein phosphatase 1 regulatory subunit 12A

Gene

PPP1R12A

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

Functioni

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.3 Publications

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • enzyme inhibitor activity Source: UniProtKB
  • phosphatase regulator activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • signal transducer activity Source: ProtInc

GO - Biological processi

  • cellular response to drug Source: Ensembl
  • centrosome organization Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: Reactome
  • mitotic nuclear division Source: UniProtKB
  • negative regulation of catalytic activity Source: UniProtKB
  • positive regulation of myosin-light-chain-phosphatase activity Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein dephosphorylation Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • regulation of myosin-light-chain-phosphatase activity Source: UniProtKB
  • regulation of nucleocytoplasmic transport Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000058272-MONOMER.
BRENDAi3.1.3.53. 2681.
ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5627117. RHO GTPases Activate ROCKs.
R-HSA-5627123. RHO GTPases activate PAKs.
SIGNORiO14974.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1 regulatory subunit 12A
Alternative name(s):
Myosin phosphatase-targeting subunit 1
Short name:
Myosin phosphatase target subunit 1
Protein phosphatase myosin-binding subunit
Gene namesi
Name:PPP1R12A
Synonyms:MBS, MYPT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7618. PPP1R12A.

Subcellular locationi

GO - Cellular componenti

  • A band Source: UniProtKB
  • actin cytoskeleton Source: HPA
  • centrosome Source: UniProtKB
  • contractile fiber Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • focal adhesion Source: UniProtKB
  • kinetochore Source: UniProtKB
  • nucleoplasm Source: Reactome
  • PTW/PP1 phosphatase complex Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi445S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-472 and A-910. 1
Mutagenesisi472S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-910. 1
Mutagenesisi473S → A: Abolishes binding to the POLO box domains of PLK1. 1 Publication1
Mutagenesisi910S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-472. 1
Mutagenesisi1007L → A: Loss of binding to PRKG1; when associated with A-1014. 1 Publication1
Mutagenesisi1014L → A: Loss of binding to PRKG1; when associated with A-1007. 1 Publication1
Mutagenesisi1021L → A: Loss of binding to PRKG1; when associated with A-1028. 1 Publication1
Mutagenesisi1028L → A: Loss of binding to PRKG1; when associated with A-1021. 1 Publication1

Organism-specific databases

DisGeNETi4659.
OpenTargetsiENSG00000058272.
PharmGKBiPA33617.

Polymorphism and mutation databases

BioMutaiPPP1R12A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000670251 – 1030Protein phosphatase 1 regulatory subunit 12AAdd BLAST1030

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei100(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei226(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei299PhosphoserineCombined sources1
Modified residuei422PhosphoserineCombined sources1
Modified residuei432Phosphoserine1 Publication1
Modified residuei443PhosphothreonineCombined sources1
Modified residuei445Phosphoserine; by NUAK1Combined sources1 Publication1
Modified residuei446PhosphotyrosineCombined sources1
Modified residuei472Phosphoserine; by NUAK11 Publication1
Modified residuei473Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei477PhosphoserineCombined sources1
Modified residuei507PhosphoserineCombined sources1
Modified residuei509PhosphoserineCombined sources1
Modified residuei601Phosphoserine1 Publication1
Modified residuei618PhosphoserineCombined sources1
Modified residuei692Phosphoserine; by PKA and PKG; in vitro1 Publication1
Modified residuei695Phosphoserine; by PKA and PKG; in vitro1 Publication1
Modified residuei696Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF1Combined sources5 Publications1
Modified residuei802PhosphoserineBy similarity1
Modified residuei852Phosphoserine; by ROCK22 Publications1
Modified residuei862PhosphoserineCombined sources1
Modified residuei871PhosphoserineCombined sources1
Modified residuei903PhosphoserineCombined sources1
Modified residuei908PhosphoserineCombined sources1
Modified residuei910Phosphoserine; by NUAK1Combined sources1 Publication1
Modified residuei995PhosphoserineCombined sources1

Post-translational modificationi

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.By similarity15 Publications

Keywords - PTMi

Hydroxylation, Phosphoprotein

Proteomic databases

EPDiO14974.
MaxQBiO14974.
PaxDbiO14974.
PeptideAtlasiO14974.
PRIDEiO14974.

2D gel databases

OGPiO14974.

PTM databases

iPTMnetiO14974.
PhosphoSitePlusiO14974.

Expressioni

Tissue specificityi

Expressed in striated muscles, specifically in type 2a fibers (at protein level).1 Publication

Developmental stagei

Induced by 2-fold during pregnancy, including in abdominus rectus muscle.1 Publication

Gene expression databases

BgeeiENSG00000058272.
CleanExiHS_PPP1R12A.
ExpressionAtlasiO14974. baseline and differential.
GenevisibleiO14974. HS.

Organism-specific databases

HPAiHPA039443.
HPA041296.

Interactioni

Subunit structurei

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Interacts with ARHA and CIT (By similarity). Binds PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with SMTNL1 (By similarity). Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910) with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1 and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN.By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAPK3O432935EBI-351726,EBI-77293
FOSP011002EBI-351726,EBI-852851

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110742. 92 interactors.
DIPiDIP-33186N.
IntActiO14974. 59 interactors.
MINTiMINT-195983.
STRINGi9606.ENSP00000261207.

Structurei

Secondary structure

11030
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi659 – 668Combined sources10
Helixi674 – 696Combined sources23
Turni699 – 701Combined sources3
Helixi702 – 710Combined sources9
Helixi932 – 965Combined sources34

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KJYNMR-A658-714[»]
5HUZNMR-A/B931-978[»]
ProteinModelPortaliO14974.
SMRiO14974.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14974.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati39 – 68ANK 1Add BLAST30
Repeati72 – 101ANK 2Add BLAST30
Repeati105 – 134ANK 3Add BLAST30
Repeati138 – 164ANK 4Add BLAST27
Repeati198 – 227ANK 5Add BLAST30
Repeati231 – 260ANK 6Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni682 – 864Interaction with ROCK21 PublicationAdd BLAST183

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi35 – 38KVKF motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi519 – 660Ser/Thr-richAdd BLAST142
Compositional biasi721 – 753Glu/Lys-richAdd BLAST33
Compositional biasi773 – 795Ser-richAdd BLAST23

Domaini

Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.By similarity
The KVKF motif mediates interaction with PPP1CB.1 Publication

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0505. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00760000119141.
HOGENOMiHOG000290648.
HOVERGENiHBG052561.
InParanoidiO14974.
KOiK06270.
OMAiTDKQTTT.
OrthoDBiEOG091G12CT.
PhylomeDBiO14974.
TreeFamiTF105543.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. MYPT1/MYPT2_chordates.
IPR031775. PRKG1_interact.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF15898. PRKG1_interact. 1 hit.
[Graphical view]
PIRSFiPIRSF038141. PP1_12ABC_vert. 1 hit.
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O14974-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS
60 70 80 90 100
GDTDEVLKLL HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN
110 120 130 140 150
QPDNEGWIPL HAAASCGYLD IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA
160 170 180 190 200
MEELLQNEVN RQGVDIEAAR KEEERIMLRD ARQWLNSGHI NDVRHAKSGG
210 220 230 240 250
TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA HWGKEEACRI
260 270 280 290 300
LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP
310 320 330 340 350
LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK
360 370 380 390 400
DESSCSSEED EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV
410 420 430 440 450
SSGQATPTSP IKKFPTTATK ISPKEEERKD ESPATWRLGL RKTGSYGALA
460 470 480 490 500
EITASKEGQK EKDTAGVTRS ASSPRLSSSL DNKEKEKDSK GTRLAYVAPT
510 520 530 540 550
IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN SSVNEGSTYH
560 570 580 590 600
KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS
610 620 630 640 650
SSAGTQSSTS NRLWAEDSTE KEKDSVPTAV TIPVAPTVVN AAASTTTLTT
660 670 680 690 700
TTAGTVSSTT EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT
710 720 730 740 750
LTDLQEAEKT IGRSRSTRTR EQENEEKEKE EKEKQDKEKQ EEKKESETSR
760 770 780 790 800
EDEYKQKYSR TYDETYQRYR PVSTSSSTTP SSSLSTMSSS LYASSQLNRP
810 820 830 840 850
NSLVGITSAY SRGITKENER EGEKREEEKE GEDKSQPKSI RERRRPREKR
860 870 880 890 900
RSTGVSFWTQ DSDENEQEQQ SDTEEGSNKK ETQTDSISRY ETSSTSAGDR
910 920 930 940 950
YDSLLGRSGS YSYLEERKPY SSRLEKDDST DFKKLYEQIL AENEKLKAQL
960 970 980 990 1000
HDTNMELTDL KLQLEKATQR QERFADRSLL EMEKRERRAL ERRISEMEEE
1010 1020 1030
LKMLPDLKAD NQRLKDENGA LIRVISKLSK
Length:1,030
Mass (Da):115,281
Last modified:January 1, 1998 - v1
Checksum:iEA43E9BFF5DA08FF
GO
Isoform 2 (identifier: O14974-2) [UniParc]FASTAAdd to basket
Also known as: Myosin phosphatase target subunit 1 variant

The sequence of this isoform differs from the canonical sequence as follows:
     935-969: Missing.

Note: No experimental confirmation available.
Show »
Length:995
Mass (Da):111,185
Checksum:i67E4FF32DDCCBD78
GO
Isoform 3 (identifier: O14974-3) [UniParc]FASTAAdd to basket
Also known as: Myosin phosphatase target subunit 1 variant 2

The sequence of this isoform differs from the canonical sequence as follows:
     552-607: Missing.

Show »
Length:974
Mass (Da):109,728
Checksum:iD211212480EF48DE
GO
Isoform 4 (identifier: O14974-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     608-666: Missing.

Note: No experimental confirmation available.
Show »
Length:971
Mass (Da):109,104
Checksum:i351DE33C5EB3C276
GO
Isoform 5 (identifier: O14974-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.

Note: No experimental confirmation available.
Show »
Length:943
Mass (Da):105,641
Checksum:i0C4751FF983E49F9
GO

Sequence cautioni

The sequence AAH47898 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH92481 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2K → Q in AAI11753 (PubMed:15489334).Curated1
Sequence conflicti322T → A in AAH92481 (PubMed:15489334).Curated1
Sequence conflicti350K → R in BAG63921 (PubMed:14702039).Curated1
Sequence conflicti653A → V in AAH92481 (PubMed:15489334).Curated1
Sequence conflicti690R → G in AAQ88438 (Ref. 2) Curated1
Sequence conflicti783S → P in AAQ88438 (Ref. 2) Curated1
Sequence conflicti930T → P in AAQ88438 (Ref. 2) Curated1
Sequence conflicti959D → G in AAQ88438 (Ref. 2) Curated1
Sequence conflicti1027K → Q in AAQ88438 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038949116C → W.Corresponds to variant rs12582646dbSNPEnsembl.1
Natural variantiVAR_038950305T → P.Corresponds to variant rs2596781dbSNPEnsembl.1
Natural variantiVAR_038951734K → N.Corresponds to variant rs12820960dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0450791 – 87Missing in isoform 5. 1 PublicationAdd BLAST87
Alternative sequenceiVSP_009251552 – 607Missing in isoform 3. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_009252608 – 666Missing in isoform 4. 1 PublicationAdd BLAST59
Alternative sequenceiVSP_009253935 – 969Missing in isoform 2. 1 PublicationAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87930 mRNA. Translation: BAA22378.1.
AY380574 mRNA. Translation: AAQ88438.1.
AF458589 mRNA. Translation: AAM49717.1.
AK302692 mRNA. Translation: BAG63921.1.
AC018476 Genomic DNA. No translation available.
AC073569 Genomic DNA. No translation available.
AC074270 Genomic DNA. No translation available.
BC047898 mRNA. Translation: AAH47898.1. Sequence problems.
BC092481 mRNA. Translation: AAH92481.1. Sequence problems.
BC111752 mRNA. Translation: AAI11753.1.
AB042196 Genomic DNA. Translation: BAB39107.1.
CCDSiCCDS44947.1. [O14974-1]
CCDS44948.1. [O14974-5]
CCDS58259.1. [O14974-3]
CCDS58260.1. [O14974-2]
RefSeqiNP_001137357.1. NM_001143885.1. [O14974-1]
NP_001137358.1. NM_001143886.1. [O14974-5]
NP_001231919.1. NM_001244990.1. [O14974-2]
NP_001231921.1. NM_001244992.1. [O14974-3]
NP_002471.1. NM_002480.2. [O14974-1]
XP_011536685.1. XM_011538383.2. [O14974-4]
UniGeneiHs.49582.

Genome annotation databases

EnsembliENST00000261207; ENSP00000261207; ENSG00000058272. [O14974-1]
ENST00000437004; ENSP00000416769; ENSG00000058272. [O14974-2]
ENST00000450142; ENSP00000389168; ENSG00000058272. [O14974-1]
ENST00000546369; ENSP00000449514; ENSG00000058272. [O14974-5]
ENST00000550107; ENSP00000446855; ENSG00000058272. [O14974-3]
GeneIDi4659.
KEGGihsa:4659.
UCSCiuc001syz.4. human. [O14974-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87930 mRNA. Translation: BAA22378.1.
AY380574 mRNA. Translation: AAQ88438.1.
AF458589 mRNA. Translation: AAM49717.1.
AK302692 mRNA. Translation: BAG63921.1.
AC018476 Genomic DNA. No translation available.
AC073569 Genomic DNA. No translation available.
AC074270 Genomic DNA. No translation available.
BC047898 mRNA. Translation: AAH47898.1. Sequence problems.
BC092481 mRNA. Translation: AAH92481.1. Sequence problems.
BC111752 mRNA. Translation: AAI11753.1.
AB042196 Genomic DNA. Translation: BAB39107.1.
CCDSiCCDS44947.1. [O14974-1]
CCDS44948.1. [O14974-5]
CCDS58259.1. [O14974-3]
CCDS58260.1. [O14974-2]
RefSeqiNP_001137357.1. NM_001143885.1. [O14974-1]
NP_001137358.1. NM_001143886.1. [O14974-5]
NP_001231919.1. NM_001244990.1. [O14974-2]
NP_001231921.1. NM_001244992.1. [O14974-3]
NP_002471.1. NM_002480.2. [O14974-1]
XP_011536685.1. XM_011538383.2. [O14974-4]
UniGeneiHs.49582.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KJYNMR-A658-714[»]
5HUZNMR-A/B931-978[»]
ProteinModelPortaliO14974.
SMRiO14974.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110742. 92 interactors.
DIPiDIP-33186N.
IntActiO14974. 59 interactors.
MINTiMINT-195983.
STRINGi9606.ENSP00000261207.

PTM databases

iPTMnetiO14974.
PhosphoSitePlusiO14974.

Polymorphism and mutation databases

BioMutaiPPP1R12A.

2D gel databases

OGPiO14974.

Proteomic databases

EPDiO14974.
MaxQBiO14974.
PaxDbiO14974.
PeptideAtlasiO14974.
PRIDEiO14974.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261207; ENSP00000261207; ENSG00000058272. [O14974-1]
ENST00000437004; ENSP00000416769; ENSG00000058272. [O14974-2]
ENST00000450142; ENSP00000389168; ENSG00000058272. [O14974-1]
ENST00000546369; ENSP00000449514; ENSG00000058272. [O14974-5]
ENST00000550107; ENSP00000446855; ENSG00000058272. [O14974-3]
GeneIDi4659.
KEGGihsa:4659.
UCSCiuc001syz.4. human. [O14974-1]

Organism-specific databases

CTDi4659.
DisGeNETi4659.
GeneCardsiPPP1R12A.
H-InvDBHIX0010848.
HGNCiHGNC:7618. PPP1R12A.
HPAiHPA039443.
HPA041296.
MIMi602021. gene.
neXtProtiNX_O14974.
OpenTargetsiENSG00000058272.
PharmGKBiPA33617.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0505. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00760000119141.
HOGENOMiHOG000290648.
HOVERGENiHBG052561.
InParanoidiO14974.
KOiK06270.
OMAiTDKQTTT.
OrthoDBiEOG091G12CT.
PhylomeDBiO14974.
TreeFamiTF105543.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000058272-MONOMER.
BRENDAi3.1.3.53. 2681.
ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5627117. RHO GTPases Activate ROCKs.
R-HSA-5627123. RHO GTPases activate PAKs.
SIGNORiO14974.

Miscellaneous databases

ChiTaRSiPPP1R12A. human.
EvolutionaryTraceiO14974.
GeneWikiiPPP1R12A.
GenomeRNAii4659.
PROiO14974.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000058272.
CleanExiHS_PPP1R12A.
ExpressionAtlasiO14974. baseline and differential.
GenevisibleiO14974. HS.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. MYPT1/MYPT2_chordates.
IPR031775. PRKG1_interact.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF15898. PRKG1_interact. 1 hit.
[Graphical view]
PIRSFiPIRSF038141. PP1_12ABC_vert. 1 hit.
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYPT1_HUMAN
AccessioniPrimary (citable) accession number: O14974
Secondary accession number(s): B4DZ09
, F8VWB4, Q2NKL4, Q569H0, Q86WU3, Q8NFR6, Q9BYH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 162 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.