O14974 (MYPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PPP1R12A
Synonyms:	MBS, MYPT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1030 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.8 Ref.24 Ref.33
Subunit structure	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. Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.23 Ref.25 Ref.30 Ref.33
Subcellular location	Cytoplasm. Note: Along actomyosin filaments and stress fibers. Ref.16 Ref.24
Tissue specificity	Expressed in striated muscles, specifically in type 2a fibers (at protein level). Ref.34
Developmental stage	Induced by 2-fold during pregnancy, including in abdominus rectus muscle. Ref.34
Domain	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. Ref.33 The KVKF motif mediates interaction with PPP1CB. Ref.33
Post-translational modification	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. Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20 Ref.21 Ref.24 Ref.29 Ref.30 Ref.31 Ref.33 Ref.37 Ref.39
Sequence similarities	Contains 6 ANK repeats.
Sequence caution	The sequence AAH47898.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH92481.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	ANK repeat Repeat
PTM	Hydroxylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome centrosome organization Inferred from mutant phenotype Ref.24. Source: UniProtKB mitosis Inferred from mutant phenotype Ref.24. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.8. Source: UniProtKB protein dephosphorylation Inferred from mutant phenotype Ref.24. Source: UniProtKB regulation of cell adhesion Inferred from direct assay Ref.33. Source: UniProtKB regulation of myosin-light-chain-phosphatase activity Inferred from direct assay Ref.33. Source: UniProtKB regulation of nucleocytoplasmic transport Inferred from electronic annotation. Source: Compara
Cellular_component	PTW/PP1 phosphatase complex Inferred from direct assay Ref.33. Source: UniProtKB centrosome Inferred from direct assay Ref.24. Source: UniProtKB contractile fiber Inferred from direct assay Ref.34. Source: UniProtKB kinetochore Inferred from direct assay Ref.24. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	14-3-3 protein binding Inferred from direct assay Ref.33. Source: UniProtKB enzyme inhibitor activity Inferred from direct assay Ref.8. Source: UniProtKB phosphatase regulator activity Inferred from direct assay Ref.33. Source: UniProtKB signal transducer activity Non-traceable author statement PubMed 8662509. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14974-1)

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.

Isoform 2 (identifier: O14974-2)

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.

Isoform 3 (identifier: O14974-3)

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.

Isoform 4 (identifier: O14974-4)

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

Note: No experimental confirmation available.

Isoform 5 (identifier: O14974-5)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1030

1030

Protein phosphatase 1 regulatory subunit 12A

PRO_0000067025

Regions

Repeat

39 – 68

30

ANK 1

Repeat

72 – 101

30

ANK 2

Repeat

105 – 134

30

ANK 3

Repeat

138 – 164

27

ANK 4

Repeat

198 – 227

30

ANK 5

Repeat

231 – 260

30

ANK 6

Region

682 – 864

183

Interaction with ROCK2

Motif

35 – 38

4

KVKF motif

Compositional bias

519 – 660

142

Ser/Thr-rich

Compositional bias

721 – 753

33

Glu/Lys-rich

Compositional bias

773 – 795

23

Ser-rich

Amino acid modifications

Modified residue

67

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.8

Modified residue

100

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.8

Modified residue

226

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.8

Modified residue

299

1

Phosphoserine Ref.28 Ref.35 Ref.38

Modified residue

422

1

Phosphoserine Ref.28 Ref.35 Ref.38

Modified residue

432

1

Phosphoserine Ref.24

Modified residue

443

1

Phosphothreonine By similarity

Modified residue

445

1

Phosphoserine; by NUAK1 Ref.28 Ref.29 Ref.33

Modified residue

472

1

Phosphoserine; by NUAK1 Ref.33

Modified residue

473

1

Phosphoserine; by CDK1 Ref.24

Modified residue

477

1

Phosphoserine Ref.28

Modified residue

507

1

Phosphoserine Ref.28 Ref.38

Modified residue

508

1

Phosphothreonine By similarity

Modified residue

509

1

Phosphoserine By similarity

Modified residue

566

1

Phosphoserine By similarity

Modified residue

569

1

Phosphoserine By similarity

Modified residue

601

1

Phosphoserine Ref.24

Modified residue

668

1

Phosphoserine By similarity

Modified residue

692

1

Phosphoserine; by PKA and PKG; in vitro

Modified residue

695

1

Phosphoserine; by PKA and PKG; in vitro

Modified residue

696

1

Phosphothreonine; by ROCK1; ROCK2; CDC42BP; ZIPK/DAPK3 and RAF1 Ref.14 Ref.20 Ref.28 Ref.31 Ref.39

Modified residue

852

1

Phosphoserine; by ROCK2 Ref.12

Modified residue

862

1

Phosphoserine Ref.28

Modified residue

871

1

Phosphoserine Ref.28 Ref.32 Ref.35

Modified residue

910

1

Phosphoserine; by NUAK1 Ref.33

Natural variations

Alternative sequence

1 – 87

87

Missing in isoform 5.

VSP_045079

Alternative sequence

552 – 607

56

Missing in isoform 3.

VSP_009251

Alternative sequence

608 – 666

59

Missing in isoform 4.

VSP_009252

Alternative sequence

935 – 969

35

Missing in isoform 2.

VSP_009253

Natural variant

116

1

C → W.
Corresponds to variant rs12582646 [ dbSNP | Ensembl ].

VAR_038949

Natural variant

305

1

T → P.
Corresponds to variant rs2596781 [ dbSNP | Ensembl ].

VAR_038950

Natural variant

734

1

K → N.
Corresponds to variant rs12820960 [ dbSNP | Ensembl ].

VAR_038951

Experimental info

Mutagenesis

445

1

S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-472 and A-910.

Mutagenesis

472

1

S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-910.

Mutagenesis

473

1

S → A: Abolishes binding to the POLO box domains of PLK1. Ref.24

Mutagenesis

910

1

S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-472.

Mutagenesis

1007

1

L → A: Loss of binding to PRKG1; when associated with A-1014. Ref.15

Mutagenesis

1014

1

L → A: Loss of binding to PRKG1; when associated with A-1007. Ref.15

Mutagenesis

1021

1

L → A: Loss of binding to PRKG1; when associated with A-1028. Ref.15

Mutagenesis

1028

1

L → A: Loss of binding to PRKG1; when associated with A-1021. Ref.15

Sequence conflict

2

1

K → Q in AAI11753. Ref.6

Sequence conflict

322

1

T → A in AAH92481. Ref.6

Sequence conflict

350

1

K → R in BAG63921. Ref.4

Sequence conflict

653

1

A → V in AAH92481. Ref.6

Sequence conflict

690

1

R → G in AAQ88438. Ref.2

Sequence conflict

783

1

S → P in AAQ88438. Ref.2

Sequence conflict

930

1

T → P in AAQ88438. Ref.2

Sequence conflict

959

1

D → G in AAQ88438. Ref.2

Sequence conflict

1027

1

K → Q in AAQ88438. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

1030

Helix Strand Turn

Details...

Helix

659 – 668

10

Helix

674 – 696

23

Turn

699 – 701

3

Helix

702 – 710

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: EA43E9BFF5DA08FF	FASTA	1,030	115,281
	10 20 30 40 50 60 MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 70 80 90 100 110 120 HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 130 140 150 160 170 180 IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 190 200 210 220 230 240 ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA 250 260 270 280 290 300 HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 310 320 330 340 350 360 LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK DESSCSSEED 370 380 390 400 410 420 EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV SSGQATPTSP IKKFPTTATK 430 440 450 460 470 480 ISPKEEERKD ESPATWRLGL RKTGSYGALA EITASKEGQK EKDTAGVTRS ASSPRLSSSL 490 500 510 520 530 540 DNKEKEKDSK GTRLAYVAPT IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN 550 560 570 580 590 600 SSVNEGSTYH KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS 610 620 630 640 650 660 SSAGTQSSTS NRLWAEDSTE KEKDSVPTAV TIPVAPTVVN AAASTTTLTT TTAGTVSSTT 670 680 690 700 710 720 EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT LTDLQEAEKT IGRSRSTRTR 730 740 750 760 770 780 EQENEEKEKE EKEKQDKEKQ EEKKESETSR EDEYKQKYSR TYDETYQRYR PVSTSSSTTP 790 800 810 820 830 840 SSSLSTMSSS LYASSQLNRP NSLVGITSAY SRGITKENER EGEKREEEKE GEDKSQPKSI 850 860 870 880 890 900 RERRRPREKR RSTGVSFWTQ DSDENEQEQQ SDTEEGSNKK ETQTDSISRY ETSSTSAGDR 910 920 930 940 950 960 YDSLLGRSGS YSYLEERKPY SSRLEKDDST DFKKLYEQIL AENEKLKAQL HDTNMELTDL 970 980 990 1000 1010 1020 KLQLEKATQR QERFADRSLL EMEKRERRAL ERRISEMEEE LKMLPDLKAD NQRLKDENGA 1030 LIRVISKLSK
	Isoform 2 (Myosin phosphatase target subunit 1 variant) [UniParc]. Checksum: 67E4FF32DDCCBD78	FASTA	995	111,185
	10 20 30 40 50 60 MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 70 80 90 100 110 120 HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 130 140 150 160 170 180 IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 190 200 210 220 230 240 ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA 250 260 270 280 290 300 HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 310 320 330 340 350 360 LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK DESSCSSEED 370 380 390 400 410 420 EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV SSGQATPTSP IKKFPTTATK 430 440 450 460 470 480 ISPKEEERKD ESPATWRLGL RKTGSYGALA EITASKEGQK EKDTAGVTRS ASSPRLSSSL 490 500 510 520 530 540 DNKEKEKDSK GTRLAYVAPT IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN 550 560 570 580 590 600 SSVNEGSTYH KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS 610 620 630 640 650 660 SSAGTQSSTS NRLWAEDSTE KEKDSVPTAV TIPVAPTVVN AAASTTTLTT TTAGTVSSTT 670 680 690 700 710 720 EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT LTDLQEAEKT IGRSRSTRTR 730 740 750 760 770 780 EQENEEKEKE EKEKQDKEKQ EEKKESETSR EDEYKQKYSR TYDETYQRYR PVSTSSSTTP 790 800 810 820 830 840 SSSLSTMSSS LYASSQLNRP NSLVGITSAY SRGITKENER EGEKREEEKE GEDKSQPKSI 850 860 870 880 890 900 RERRRPREKR RSTGVSFWTQ DSDENEQEQQ SDTEEGSNKK ETQTDSISRY ETSSTSAGDR 910 920 930 940 950 960 YDSLLGRSGS YSYLEERKPY SSRLEKDDST DFKKRQERFA DRSLLEMEKR ERRALERRIS 970 980 990 EMEEELKMLP DLKADNQRLK DENGALIRVI SKLSK
	Isoform 3 (Myosin phosphatase target subunit 1 variant 2) [UniParc]. Checksum: D211212480EF48DE	FASTA	974	109,728
	10 20 30 40 50 60 MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 70 80 90 100 110 120 HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 130 140 150 160 170 180 IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 190 200 210 220 230 240 ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA 250 260 270 280 290 300 HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 310 320 330 340 350 360 LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK DESSCSSEED 370 380 390 400 410 420 EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV SSGQATPTSP IKKFPTTATK 430 440 450 460 470 480 ISPKEEERKD ESPATWRLGL RKTGSYGALA EITASKEGQK EKDTAGVTRS ASSPRLSSSL 490 500 510 520 530 540 DNKEKEKDSK GTRLAYVAPT IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN 550 560 570 580 590 600 SSVNEGSTYH KSTSNRLWAE DSTEKEKDSV PTAVTIPVAP TVVNAAASTT TLTTTTAGTV 610 620 630 640 650 660 SSTTEVRERR RSYLTPVRDE ESESQRKARS RQARQSRRST QGVTLTDLQE AEKTIGRSRS 670 680 690 700 710 720 TRTREQENEE KEKEEKEKQD KEKQEEKKES ETSREDEYKQ KYSRTYDETY QRYRPVSTSS 730 740 750 760 770 780 STTPSSSLST MSSSLYASSQ LNRPNSLVGI TSAYSRGITK ENEREGEKRE EEKEGEDKSQ 790 800 810 820 830 840 PKSIRERRRP REKRRSTGVS FWTQDSDENE QEQQSDTEEG SNKKETQTDS ISRYETSSTS 850 860 870 880 890 900 AGDRYDSLLG RSGSYSYLEE RKPYSSRLEK DDSTDFKKLY EQILAENEKL KAQLHDTNME 910 920 930 940 950 960 LTDLKLQLEK ATQRQERFAD RSLLEMEKRE RRALERRISE MEEELKMLPD LKADNQRLKD 970 ENGALIRVIS KLSK
	Isoform 4 [UniParc]. Checksum: 351DE33C5EB3C276	FASTA	971	109,104
	10 20 30 40 50 60 MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 70 80 90 100 110 120 HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 130 140 150 160 170 180 IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 190 200 210 220 230 240 ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA 250 260 270 280 290 300 HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 310 320 330 340 350 360 LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK DESSCSSEED 370 380 390 400 410 420 EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV SSGQATPTSP IKKFPTTATK 430 440 450 460 470 480 ISPKEEERKD ESPATWRLGL RKTGSYGALA EITASKEGQK EKDTAGVTRS ASSPRLSSSL 490 500 510 520 530 540 DNKEKEKDSK GTRLAYVAPT IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN 550 560 570 580 590 600 SSVNEGSTYH KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS 610 620 630 640 650 660 SSAGTQSRSY LTPVRDEESE SQRKARSRQA RQSRRSTQGV TLTDLQEAEK TIGRSRSTRT 670 680 690 700 710 720 REQENEEKEK EEKEKQDKEK QEEKKESETS REDEYKQKYS RTYDETYQRY RPVSTSSSTT 730 740 750 760 770 780 PSSSLSTMSS SLYASSQLNR PNSLVGITSA YSRGITKENE REGEKREEEK EGEDKSQPKS 790 800 810 820 830 840 IRERRRPREK RRSTGVSFWT QDSDENEQEQ QSDTEEGSNK KETQTDSISR YETSSTSAGD 850 860 870 880 890 900 RYDSLLGRSG SYSYLEERKP YSSRLEKDDS TDFKKLYEQI LAENEKLKAQ LHDTNMELTD 910 920 930 940 950 960 LKLQLEKATQ RQERFADRSL LEMEKRERRA LERRISEMEE ELKMLPDLKA DNQRLKDENG 970 ALIRVISKLS K
	Isoform 5 [UniParc]. Checksum: 0C4751FF983E49F9	FASTA	943	105,641
	10 20 30 40 50 60 MVKFLVENGA NINQPDNEGW IPLHAAASCG YLDIAEFLIG QGAHVGAVNS EGDTPLDIAE 70 80 90 100 110 120 EEAMEELLQN EVNRQGVDIE AARKEEERIM LRDARQWLNS GHINDVRHAK SGGTALHVAA 130 140 150 160 170 180 AKGYTEVLKL LIQAGYDVNI KDYDGWTPLH AAAHWGKEEA CRILVDNLCD MEMVNKVGQT 190 200 210 220 230 240 AFDVADEDIL GYLEELQKKQ NLLHSEKRDK KSPLIESTAN MDNNQSQKTF KNKETLIIEP 250 260 270 280 290 300 EKNASRIESL EQEKVDEEEE GKKDESSCSS EEDEEDDSES EAETDKTKPL ASVTNANTSS 310 320 330 340 350 360 TQAAPVAVTT PTVSSGQATP TSPIKKFPTT ATKISPKEEE RKDESPATWR LGLRKTGSYG 370 380 390 400 410 420 ALAEITASKE GQKEKDTAGV TRSASSPRLS SSLDNKEKEK DSKGTRLAYV APTIPRRLAS 430 440 450 460 470 480 TSDIEEKENR DSSSLRTSSS YTRRKWEDDL KKNSSVNEGS TYHKSCSFGR RQDDLISSSV 490 500 510 520 530 540 PSTTSTPTVT SAAGLQKSLL SSTSTTTKIT TGSSSAGTQS STSNRLWAED STEKEKDSVP 550 560 570 580 590 600 TAVTIPVAPT VVNAAASTTT LTTTTAGTVS STTEVRERRR SYLTPVRDEE SESQRKARSR 610 620 630 640 650 660 QARQSRRSTQ GVTLTDLQEA EKTIGRSRST RTREQENEEK EKEEKEKQDK EKQEEKKESE 670 680 690 700 710 720 TSREDEYKQK YSRTYDETYQ RYRPVSTSSS TTPSSSLSTM SSSLYASSQL NRPNSLVGIT 730 740 750 760 770 780 SAYSRGITKE NEREGEKREE EKEGEDKSQP KSIRERRRPR EKRRSTGVSF WTQDSDENEQ 790 800 810 820 830 840 EQQSDTEEGS NKKETQTDSI SRYETSSTSA GDRYDSLLGR SGSYSYLEER KPYSSRLEKD 850 860 870 880 890 900 DSTDFKKLYE QILAENEKLK AQLHDTNMEL TDLKLQLEKA TQRQERFADR SLLEMEKRER 910 920 930 940 RALERRISEM EEELKMLPDL KADNQRLKDE NGALIRVISK LSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21." Takahashi N., Ito M., Tanaka J., Nakano T., Kaibuchi K., Odai H., Takemura K. Genomics 44:150-152(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain and Liver.
[2]	Guo J.H., Chen X.Y., Yu L. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Liver.
[3]	"Molecular cloning and functional analysis of a new isoform of human MYPT1." Xia D., Kamm K., Stull J.T. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Tissue: Testis.
[5]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-722 (ISOFORM 4). Tissue: Blood and Brain.
[7]	"Molecular cloning and analysis of the 5'-flanking region of human MYPT1 gene." Machida H., Ito M., Okamoto R., Shiraki K., Isaka N., Hartshorne D.J., Nakano T. Biochim. Biophys. Acta 1517:424-429(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
[8]	"MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)." Webb J.D., Muranyi A., Pugh C.W., Ratcliffe P.J., Coleman M.L. Biochem. J. 420:327-333(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 63-76; 95-105 AND 217-228, FUNCTION, HYDROXYLATION AT ASN-67; ASN-100 AND ASN-226 BY HIF1AN.
[9]	"Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Ialpha." Surks H.K., Mochizuki N., Kasai Y., Georgescu S.P., Tang K.M., Ito M., Lincoln T.M., Mendelsohn M.E. Science 286:1583-1587(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKG1, PHOSPHORYLATION BY PRKG1, SUBUNIT.
[10]	"Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity." Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F., Hartshorne D.J. FEBS Lett. 493:80-84(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY DMPK.
[11]	"Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit." Arimura T., Suematsu N., Zhou Y.-B., Nishimura J., Satoh S., Takeshita A., Kanaide H., Kimura A. J. Biol. Chem. 276:6073-6082(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R12B.
[12]	"Rho-kinase--mediated contraction of isolated stress fibers." Katoh K., Kano Y., Amano M., Onishi H., Kaibuchi K., Fujiwara K. J. Cell Biol. 153:569-584(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-852.
[13]	"Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing." Sebbagh M., Renvoize C., Hamelin J., Riche N., Bertoglio J., Breard J. Nat. Cell Biol. 3:346-352(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ROCK1, PHOSPHORYLATION.
[14]	"Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity." Broustas C.G., Grammatikakis N., Eto M., Dent P., Brautigan D.L., Kasid U. J. Biol. Chem. 277:3053-3059(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-696 BY RAF1, INTERACTION WITH RAF1.
[15]	"Dimerization of cGMP-dependent protein kinase 1alpha and the myosin-binding subunit of myosin phosphatase: role of leucine zipper domains." Surks H.K., Mendelsohn M.E. Cell. Signal. 15:937-944(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, MUTAGENESIS OF LEU-1007; LEU-1014; LEU-1021 AND LEU-1028, INTERACTION WITH PRKG1.
[16]	"PDZ domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits." Bannert N., Vollhardt K., Asomuddinov B., Haag M., Koenig H., Norley S., Kurth R. J. Biol. Chem. 278:42190-42199(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IL16, SUBCELLULAR LOCATION.
[17]	"RhoE binds to ROCK I and inhibits downstream signaling." Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J. Mol. Cell. Biol. 23:4219-4229(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ROCK1, PHOSPHORYLATION.
[18]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[19]	"Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides." Wooldridge A.A., MacDonald J.A., Erdodi F., Ma C., Borman M.A., Hartshorne D.J., Haystead T.A.J. J. Biol. Chem. 279:34496-34504(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PRKG1 ON SER-692; SER-695; THR-696 AND SER-852.
[20]	"Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion." Wilkinson S., Paterson H.F., Marshall C.J. Nat. Cell Biol. 7:255-261(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-696. Tissue: Colon.
[21]	"Novel ZIP kinase isoform lacks leucine zipper." Takamoto N., Komatsu S., Komaba S., Niiro N., Ikebe M. Arch. Biochem. Biophys. 456:194-203(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY ZIPK/DAPK3, INTERACTION WITH ZIPK/DAPK3.
[22]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[23]	"Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase." Lee E., Hayes D.B., Langsetmo K., Sundberg E.J., Tao T.C. J. Mol. Biol. 373:1198-1212(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKG1.
[24]	"Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1." Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M., Hartshorne D.J., Matsumura F. Dev. Cell 14:787-797(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-432; SER-473 AND SER-601, PHOSPHORYLATION BY PLK1, MUTAGENESIS OF SER-473.
[25]	"Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase." Sharma A.K., Zhou G.-P., Kupferman J., Surks H.K., Christensen E.N., Chou J.J., Mendelsohn M.E., Rigby A.C. J. Biol. Chem. 283:32860-32869(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKG1, SUBUNIT.
[26]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: T-cell.
[27]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[28]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422; SER-445; SER-477; SER-507; THR-696; SER-862 AND SER-871, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	Carrascal M., Abian J. Submitted (JAN-2008) to UniProtKB Cited for: PHOSPHORYLATION AT SER-445, MASS SPECTROMETRY. Tissue: T-cell.
[30]	"ROCK isoform regulation of myosin phosphatase and contractility in vascular smooth muscle cells." Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K. Circ. Res. 104:531-540(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH ROCK1 AND ROCK2.
[31]	"Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte differentiation." Lock F.E., Hotchin N.A. PLoS ONE 4:E8190-E8190(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-696.
[32]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[33]	"New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion." Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M., Aizawa S., Prescott A.R., Alessi D.R. Sci. Signal. 3:RA25-RA25(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPP1CB AND 14-3-3, DOMAIN KVKF MOTIF, PHOSPHORYLATION AT SER-445; SER-472 AND SER-910.
[34]	"Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy." Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A. J. Biol. Chem. 285:29357-29366(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[35]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422 AND SER-871, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]	"Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase." Tan I., Lai J., Yong J., Li S.F., Leung T. FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CDC42BP AND DMPK.
[38]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422 AND SER-507, MASS SPECTROMETRY.
[39]	"Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1." Mori S., Iwaoka R., Eto M., Ohki S.-Y. Proteins 77:732-735(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 658-714, PHOSPHORYLATION AT THR-696.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00183002.
IPI00397728.
IPI00397730.
IPI00413191.
IPI01021487.

RefSeq

NP_001137357.1. NM_001143885.1.
NP_001137358.1. NM_001143886.1.
NP_001231919.1. NM_001244990.1.
NP_001231921.1. NM_001244992.1.
NP_002471.1. NM_002480.2.

UniGene

Hs.49582.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KJY	NMR	-	A	658-714	[»]

ProteinModelPortal

O14974.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33186N.

IntAct

O14974. 18 interactions.

MINT

MINT-195983.

STRING

9606.ENSP00000261207.

PTM databases

PhosphoSite

O14974.

2D gel databases

OGP

O14974.

Proteomic databases

PaxDb

O14974.

PRIDE

O14974.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261207; ENSP00000261207; ENSG00000058272.
ENST00000437004; ENSP00000416769; ENSG00000058272.
ENST00000450142; ENSP00000389168; ENSG00000058272.
ENST00000546369; ENSP00000449514; ENSG00000058272.
ENST00000550107; ENSP00000446855; ENSG00000058272.

GeneID

4659.

KEGG

hsa:4659.

UCSC

uc001syz.3. human.
uc001sza.3. human.
uc001szb.3. human.

Organism-specific databases

CTD

4659.

GeneCards

GC12M080142.

H-InvDB

HIX0010848.

HGNC

HGNC:7618. PPP1R12A.

HPA

HPA039443.

MIM

602021. gene.

neXtProt

NX_O14974.

PharmGKB

PA33617.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOGENOM

HOG000290648.

HOVERGEN

HBG052561.

InParanoid

O14974.

KO

K06270.

OMA

KDYDGWT.

OrthoDB

EOG4R7V9D.

Gene expression databases

ArrayExpress

O14974.

Bgee

O14974.

CleanEx

HS_PPP1R12A.

Genevestigator

O14974.

GermOnline

ENSG00000058272. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. Pase-1_reg_su_12A/B/C_euk.
[Graphical view]

Pfam

PF00023. Ank. 4 hits.
[Graphical view]

PIRSF

PIRSF038141. PP1_12ABC_vert. 1 hit.

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 6 hits.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3124.

ChiTaRS

PPP1R12A. human.

EvolutionaryTrace

O14974.

GenomeRNAi

4659.

NextBio

17954.

SOURCE

Search...

Entry information

Entry name

MYPT1_HUMAN

Accession

Primary (citable) accession number: O14974
Secondary accession number(s): B4DZ09 , F8VWB4, Q2NKL4, Q569H0, Q86WU3, Q8NFR6, Q9BYH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 1, 1998
Last modified:	May 29, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.