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Q9DBR7

- MYPT1_MOUSE

UniProt

Q9DBR7 - MYPT1_MOUSE

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Protein

Protein phosphatase 1 regulatory subunit 12A

Gene

Ppp1r12a

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 By similarity.By similarity

GO - Molecular functioni

  1. 14-3-3 protein binding Source: UniProtKB
  2. enzyme inhibitor activity Source: UniProtKB
  3. phosphatase regulator activity Source: UniProtKB

GO - Biological processi

  1. centrosome organization Source: UniProtKB
  2. mitotic nuclear division Source: UniProtKB
  3. negative regulation of catalytic activity Source: UniProtKB
  4. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. protein dephosphorylation Source: MGI
  6. regulation of cell adhesion Source: UniProtKB
  7. regulation of myosin-light-chain-phosphatase activity Source: UniProtKB
  8. regulation of nucleocytoplasmic transport Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.

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
Gene namesi
Name:Ppp1r12a
Synonyms:Mypt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1309528. Ppp1r12a.

Subcellular locationi

Cytoplasm By similarity
Note: Along actomyosin filaments and stress fibers.By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. centrosome Source: UniProtKB
  3. contractile fiber Source: Ensembl
  4. kinetochore Source: UniProtKB
  5. PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10291029Protein phosphatase 1 regulatory subunit 12APRO_0000067026Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei100 – 1001(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei226 – 2261(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei422 – 4221PhosphoserineBy similarity
Modified residuei432 – 4321PhosphoserineBy similarity
Modified residuei443 – 4431Phosphothreonine1 Publication
Modified residuei445 – 4451Phosphoserine; alternate1 Publication
Modified residuei445 – 4451Phosphoserine; by NUAK1; alternate1 Publication
Modified residuei472 – 4721Phosphoserine; by NUAK1By similarity
Modified residuei473 – 4731Phosphoserine; by CDK1By similarity
Modified residuei477 – 4771PhosphoserineBy similarity
Modified residuei507 – 5071Phosphoserine1 Publication
Modified residuei601 – 6011PhosphoserineBy similarity
Modified residuei666 – 6661Phosphoserine1 Publication
Modified residuei690 – 6901Phosphoserine; by PKA and PKG; in vitroBy similarity
Modified residuei693 – 6931Phosphoserine; by PKA and PKG; in vitroBy similarity
Modified residuei694 – 6941Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF11 Publication
Modified residuei851 – 8511Phosphoserine; by ROCK2By similarity
Modified residuei861 – 8611PhosphoserineBy similarity
Modified residuei870 – 8701Phosphoserine1 Publication
Modified residuei909 – 9091Phosphoserine; by NUAK11 Publication
Modified residuei994 – 9941PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CIT (Rho-associated kinase) By similarity. Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-694 By similarity. Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-693 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-694, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-909 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-694 by DMPK; may inhibit the myosin phosphatase activity By similarity. 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 similarity.By similarity

Keywords - PTMi

Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiQ9DBR7.
PaxDbiQ9DBR7.
PRIDEiQ9DBR7.

PTM databases

PhosphoSiteiQ9DBR7.

Miscellaneous databases

PMAP-CutDBQ9DBR7.

Expressioni

Tissue specificityi

Expressed in striated and vascular smooth muscle, specificcally in type 2a fibers (at protein level). Expression levels are 20-30% higher in developed males than females (at protein level).1 Publication

Developmental stagei

In neonates, expressed at low levels in striated and smooth muscles. As the animals mature sexually, expression increases 10-20-fold. Pregnancy promotes a 2-3-fold increase in expression in striated, vascular and uterine muscle (at protein level).1 Publication

Gene expression databases

BgeeiQ9DBR7.
GenevestigatoriQ9DBR7.

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. Binds PPP1R12B, ROCK1 and IL16 By similarity. Interacts with ARHA and CIT. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-909) with 14-3-3 By similarity. Interacts with SMTNL1. Interacts with ZIPK/DAPK3 By similarity. Interacts with RAF1 By similarity. Interacts with HIF1AN By similarity.By similarity

Protein-protein interaction databases

DIPiDIP-29982N.
IntActiQ9DBR7. 3 interactions.
MINTiMINT-4102998.
STRINGi10090.ENSMUSP00000100915.

Structurei

3D structure databases

ProteinModelPortaliQ9DBR7.
SMRiQ9DBR7. Positions 1-291, 656-712.
ModBaseiSearch...
MobiDBiSearch...

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
Regioni680 – 863184Interaction with ROCK2By similarityAdd
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi335 – 37036Glu/Ser-richAdd
BLAST
Compositional biasi771 – 79424Ser-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.By similarity

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000119141.
HOGENOMiHOG000290648.
HOVERGENiHBG052561.
InParanoidiQ9DBR7.
KOiK06270.
OMAiTDKQTTT.
OrthoDBiEOG7060Q5.
PhylomeDBiQ9DBR7.
TreeFamiTF105543.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. Pase-1_reg_su_12A/B/C_euk.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
[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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9DBR7-1) [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 KEEERVMLRD ARQWLNSGHI SDVRHAKSGG
210 220 230 240 250
TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA HWGKEEACRI
260 270 280 290 300
LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQTLL HSEKRDKKSP
310 320 330 340 350
LIESTANMEN NQPQKAFKNK ETLIIEPEKN ASRIESLEHE KADEEEEGKK
360 370 380 390 400
DESSCSSEED EEDDSESEAE TDKTKPMASV SNAHTSSTQA APAAVTAPTL
410 420 430 440 450
SSNQGTPTSP VKKFPISTTK ISPKEEERKD ESPASWRLGL RKTGSYGALA
460 470 480 490 500
EISASKEAQK EKDTAGVMRS ASSPRLSSSL DNKEKEKDNK GTRLAYVTPT
510 520 530 540 550
IPRRLASTSD IEEKENRESS SLRTSSSYTR RKWEDDLKKN SSINEGSTYH
560 570 580 590 600
RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQRSLPSST STAAKTPPGS
610 620 630 640 650
SSAGTQSSTS NRLWAEDSTE KEKDSAPTAV TIPVAPTVVN AAAPSTTTLT
660 670 680 690 700
TTTAGTVSEV RERRRSYLTP VRDEESESQR KARSRQARQS RRSTQGVTLT
710 720 730 740 750
DLQEAEKTIG RSRSTRTREQ ENEEKEKEEK EKQDKEKQEE KKESEASRED
760 770 780 790 800
EYKQKYSRTY DETYTRYRPV STSSSSAPSS SSLSTLGSTL YASSQLNRPN
810 820 830 840 850
SLVGITSAYS RGLAKENERE GEKKEEEKEG EDKSQPKSIR ERRRPREKRR
860 870 880 890 900
STGVSFWTQD SDENEQERQS DTEDGSSKRE TQTDSVSRYD SSSTSSSDRY
910 920 930 940 950
DSLLGRSASY SYLEDRKPYS SRLEKDDSTD FKKLYEQILA ENEKLKAQLH
960 970 980 990 1000
DTNMELTDLK LQLEKATQRQ ERFADRSQLE MEKRERRALE RRISEMEEEL
1010 1020
KMLPDLKADN QRLKDENGAL IRVISKLSK
Length:1,029
Mass (Da):114,996
Last modified:December 15, 2009 - v2
Checksum:iC466573AC1DFC81F
GO
Isoform 2 (identifier: Q9DBR7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     985-1029: ERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK → VAGKSQYLLGGTKSSRKKNI

Show »
Length:1,004
Mass (Da):111,809
Checksum:i1CF7118111B85BF1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei985 – 102945ERRAL…SKLSK → VAGKSQYLLGGTKSSRKKNI in isoform 2. 1 PublicationVSP_038478Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK035230 mRNA. Translation: BAC28990.1.
AK004785 mRNA. Translation: BAB23563.1.
CH466539 Genomic DNA. Translation: EDL21703.1.
BC125381 mRNA. Translation: AAI25382.1.
BC137630 mRNA. Translation: AAI37631.1.
AB042280 Genomic DNA. Translation: BAB39108.1.
CCDSiCCDS36052.1. [Q9DBR7-2]
RefSeqiNP_082168.1. NM_027892.2. [Q9DBR7-2]
XP_006513389.1. XM_006513326.1. [Q9DBR7-1]
UniGeneiMm.422959.
Mm.489819.

Genome annotation databases

EnsembliENSMUST00000070663; ENSMUSP00000069257; ENSMUSG00000019907. [Q9DBR7-2]
GeneIDi17931.
KEGGimmu:17931.
UCSCiuc007gzc.1. mouse. [Q9DBR7-2]
uc007gzd.1. mouse. [Q9DBR7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK035230 mRNA. Translation: BAC28990.1 .
AK004785 mRNA. Translation: BAB23563.1 .
CH466539 Genomic DNA. Translation: EDL21703.1 .
BC125381 mRNA. Translation: AAI25382.1 .
BC137630 mRNA. Translation: AAI37631.1 .
AB042280 Genomic DNA. Translation: BAB39108.1 .
CCDSi CCDS36052.1. [Q9DBR7-2 ]
RefSeqi NP_082168.1. NM_027892.2. [Q9DBR7-2 ]
XP_006513389.1. XM_006513326.1. [Q9DBR7-1 ]
UniGenei Mm.422959.
Mm.489819.

3D structure databases

ProteinModelPortali Q9DBR7.
SMRi Q9DBR7. Positions 1-291, 656-712.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29982N.
IntActi Q9DBR7. 3 interactions.
MINTi MINT-4102998.
STRINGi 10090.ENSMUSP00000100915.

PTM databases

PhosphoSitei Q9DBR7.

Proteomic databases

MaxQBi Q9DBR7.
PaxDbi Q9DBR7.
PRIDEi Q9DBR7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000070663 ; ENSMUSP00000069257 ; ENSMUSG00000019907 . [Q9DBR7-2 ]
GeneIDi 17931.
KEGGi mmu:17931.
UCSCi uc007gzc.1. mouse. [Q9DBR7-2 ]
uc007gzd.1. mouse. [Q9DBR7-1 ]

Organism-specific databases

CTDi 4659.
MGIi MGI:1309528. Ppp1r12a.

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000119141.
HOGENOMi HOG000290648.
HOVERGENi HBG052561.
InParanoidi Q9DBR7.
KOi K06270.
OMAi TDKQTTT.
OrthoDBi EOG7060Q5.
PhylomeDBi Q9DBR7.
TreeFami TF105543.

Enzyme and pathway databases

Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSi PPP1R12A. mouse.
NextBioi 292815.
PMAP-CutDB Q9DBR7.
PROi Q9DBR7.
SOURCEi Search...

Gene expression databases

Bgeei Q9DBR7.
Genevestigatori Q9DBR7.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. Pase-1_reg_su_12A/B/C_euk.
[Graphical view ]
Pfami PF12796. Ank_2. 2 hits.
[Graphical view ]
PIRSFi PIRSF038141. PP1_12ABC_vert. 1 hit.
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 6 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Lung and Urinary bladder.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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).
    Tissue: Brain.
  4. "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.
  5. "Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)."
    Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M., Yamamori B., Feng J., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.
    Science 273:245-248(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH ARHA AND CIT.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "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: INTERACTION WITH SMTNL1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiMYPT1_MOUSE
AccessioniPrimary (citable) accession number: Q9DBR7
Secondary accession number(s): Q05A74, Q8CBV2, Q99NB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 15, 2009
Last modified: October 29, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3