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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
  • phosphoprotein phosphatase activity Source: Ensembl
  • 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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi445 – 4451S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-472 and A-910.
Mutagenesisi472 – 4721S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-910.
Mutagenesisi473 – 4731S → A: Abolishes binding to the POLO box domains of PLK1. 1 Publication
Mutagenesisi910 – 9101S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-472.
Mutagenesisi1007 – 10071L → A: Loss of binding to PRKG1; when associated with A-1014. 1 Publication
Mutagenesisi1014 – 10141L → A: Loss of binding to PRKG1; when associated with A-1007. 1 Publication
Mutagenesisi1021 – 10211L → A: Loss of binding to PRKG1; when associated with A-1028. 1 Publication
Mutagenesisi1028 – 10281L → A: Loss of binding to PRKG1; when associated with A-1021. 1 Publication

Organism-specific databases

PharmGKBiPA33617.

Polymorphism and mutation databases

BioMutaiPPP1R12A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10301030Protein phosphatase 1 regulatory subunit 12APRO_0000067025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei100 – 1001(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei226 – 2261(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei422 – 4221PhosphoserineCombined sources
Modified residuei432 – 4321Phosphoserine1 Publication
Modified residuei443 – 4431PhosphothreonineCombined sources
Modified residuei445 – 4451Phosphoserine; by NUAK1Combined sources1 Publication
Modified residuei446 – 4461PhosphotyrosineCombined sources
Modified residuei472 – 4721Phosphoserine; by NUAK11 Publication
Modified residuei473 – 4731Phosphoserine; by CDK1Combined sources1 Publication
Modified residuei477 – 4771PhosphoserineCombined sources
Modified residuei507 – 5071PhosphoserineCombined sources
Modified residuei509 – 5091PhosphoserineCombined sources
Modified residuei601 – 6011Phosphoserine1 Publication
Modified residuei618 – 6181PhosphoserineCombined sources
Modified residuei692 – 6921Phosphoserine; by PKA and PKG; in vitro1 Publication
Modified residuei695 – 6951Phosphoserine; by PKA and PKG; in vitro1 Publication
Modified residuei696 – 6961Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF1Combined sources5 Publications
Modified residuei802 – 8021PhosphoserineBy similarity
Modified residuei852 – 8521Phosphoserine; by ROCK22 Publications
Modified residuei862 – 8621PhosphoserineCombined sources
Modified residuei871 – 8711PhosphoserineCombined sources
Modified residuei903 – 9031PhosphoserineCombined sources
Modified residuei908 – 9081PhosphoserineCombined sources
Modified residuei910 – 9101Phosphoserine; by NUAK1Combined sources1 Publication
Modified residuei995 – 9951PhosphoserineCombined sources

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.
PhosphoSiteiO14974.

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 interactions.
DIPiDIP-33186N.
IntActiO14974. 59 interactions.
MINTiMINT-195983.
STRINGi9606.ENSP00000261207.

Structurei

Secondary structure

1
1030
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi659 – 66810Combined sources
Helixi674 – 69623Combined sources
Turni699 – 7013Combined sources
Helixi702 – 7109Combined sources
Helixi932 – 96635Combined sources
Beta strandi968 – 9703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJYNMR-A658-714[»]
2MXRNMR-A/B931-975[»]
5HUZNMR-A/B931-974[»]
ProteinModelPortaliO14974.
SMRiO14974. Positions 1-291, 658-714, 931-975.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14974.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati39 – 6830ANK 1Add
BLAST
Repeati72 – 10130ANK 2Add
BLAST
Repeati105 – 13430ANK 3Add
BLAST
Repeati138 – 16427ANK 4Add
BLAST
Repeati198 – 22730ANK 5Add
BLAST
Repeati231 – 26030ANK 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni682 – 864183Interaction with ROCK2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi35 – 384KVKF motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi519 – 660142Ser/Thr-richAdd
BLAST
Compositional biasi721 – 75333Glu/Lys-richAdd
BLAST
Compositional biasi773 – 79523Ser-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21K → Q in AAI11753 (PubMed:15489334).Curated
Sequence conflicti322 – 3221T → A in AAH92481 (PubMed:15489334).Curated
Sequence conflicti350 – 3501K → R in BAG63921 (PubMed:14702039).Curated
Sequence conflicti653 – 6531A → V in AAH92481 (PubMed:15489334).Curated
Sequence conflicti690 – 6901R → G in AAQ88438 (Ref. 2) Curated
Sequence conflicti783 – 7831S → P in AAQ88438 (Ref. 2) Curated
Sequence conflicti930 – 9301T → P in AAQ88438 (Ref. 2) Curated
Sequence conflicti959 – 9591D → G in AAQ88438 (Ref. 2) Curated
Sequence conflicti1027 – 10271K → Q in AAQ88438 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161C → W.
Corresponds to variant rs12582646 [ dbSNP | Ensembl ].
VAR_038949
Natural varianti305 – 3051T → P.
Corresponds to variant rs2596781 [ dbSNP | Ensembl ].
VAR_038950
Natural varianti734 – 7341K → N.
Corresponds to variant rs12820960 [ dbSNP | Ensembl ].
VAR_038951

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8787Missing in isoform 5. 1 PublicationVSP_045079Add
BLAST
Alternative sequencei552 – 60756Missing in isoform 3. 1 PublicationVSP_009251Add
BLAST
Alternative sequencei608 – 66659Missing in isoform 4. 1 PublicationVSP_009252Add
BLAST
Alternative sequencei935 – 96935Missing in isoform 2. 1 PublicationVSP_009253Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJYNMR-A658-714[»]
2MXRNMR-A/B931-975[»]
5HUZNMR-A/B931-974[»]
ProteinModelPortaliO14974.
SMRiO14974. Positions 1-291, 658-714, 931-975.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiO14974.
PhosphoSiteiO14974.

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

Phylogenomic databases

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

Enzyme and pathway databases

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: September 7, 2016
This is version 159 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.