LOCUS       NP_002472                982 aa            linear   PRI 19-SEP-2024
DEFINITION  protein phosphatase 1 regulatory subunit 12B isoform a [Homo
            sapiens].
ACCESSION   NP_002472
VERSION     NP_002472.2
DBSOURCE    REFSEQ: accession NM_002481.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Jia,D., Wang,K., Huang,L., Zhou,Z., Zhang,Y., Chen,N., Yang,Q.,
            Wen,Z., Jiang,H., Yao,C. and Wu,R.
  TITLE     Revealing PPP1R12B and COL1A1 as piRNA pathway genes contributing
            to abdominal aortic aneurysm through integrated analysis and
            experimental validation
  JOURNAL   Gene 897, 148068 (2024)
   PUBMED   38070790
  REMARK    GeneRIF: Revealing PPP1R12B and COL1A1 as piRNA pathway genes
            contributing to abdominal aortic aneurysm through integrated
            analysis and experimental validation.
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Song,S.E., Kim,Y., Jeong,H., Lee,B., Lee,J., Roh,J.S., So,M.W.,
            Lee,S.G. and Sohn,D.H.
  TITLE     FAT10 differentially stabilizes MYPT2 isoforms
  JOURNAL   Biochem Biophys Res Commun 676, 115-120 (2023)
   PUBMED   37506472
  REMARK    GeneRIF: FAT10 differentially stabilizes MYPT2 isoforms.
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Tan,J., Lu,T., Xu,J., Hou,Y., Chen,Z., Zhou,K., Ding,Y., Jiang,B.
            and Zhu,Y.
  TITLE     MicroRNA-4463 facilitates the development of colon cancer by
            suppression of the expression of PPP1R12B
  JOURNAL   Clin Transl Oncol 24 (6), 1115-1123 (2022)
   PUBMED   35064454
  REMARK    GeneRIF: MicroRNA-4463 facilitates the development of colon cancer
            by suppression of the expression of PPP1R12B.
REFERENCE   4  (residues 1 to 982)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 982)
  AUTHORS   Bannert,N., Vollhardt,K., Asomuddinov,B., Haag,M., Konig,H.,
            Norley,S. and Kurth,R.
  TITLE     PDZ Domain-mediated interaction of interleukin-16 precursor
            proteins with myosin phosphatase targeting subunits
  JOURNAL   J Biol Chem 278 (43), 42190-42199 (2003)
   PUBMED   12923170
REFERENCE   6  (residues 1 to 982)
  AUTHORS   Arimura,T., Suematsu,N., Zhou,Y.B., Nishimura,J., Satoh,S.,
            Takeshita,A., Kanaide,H. and Kimura,A.
  TITLE     Identification, characterization, and functional analysis of
            heart-specific myosin light chain phosphatase small subunit
  JOURNAL   J Biol Chem 276 (9), 6073-6082 (2001)
   PUBMED   11067852
REFERENCE   7  (residues 1 to 982)
  AUTHORS   Somlyo,A.P.
  TITLE     Kinases, myosin phosphatase and Rho proteins: curiouser and
            curiouser
  JOURNAL   J Physiol 516 (Pt 3) (Pt 3), 630 (1999)
   PUBMED   10200412
REFERENCE   8  (residues 1 to 982)
  AUTHORS   Somlyo,A.P., Wu,X., Walker,L.A. and Somlyo,A.V.
  TITLE     Pharmacomechanical coupling: the role of calcium, G-proteins,
            kinases and phosphatases
  JOURNAL   Rev Physiol Biochem Pharmacol 134, 201-234 (1999)
   PUBMED   10087910
  REMARK    Review article
REFERENCE   9  (residues 1 to 982)
  AUTHORS   Moorhead,G., Johnson,D., Morrice,N. and Cohen,P.
  TITLE     The major myosin phosphatase in skeletal muscle is a complex
            between the beta-isoform of protein phosphatase 1 and the MYPT2
            gene product
  JOURNAL   FEBS Lett 438 (3), 141-144 (1998)
   PUBMED   9827534
REFERENCE   10 (residues 1 to 982)
  AUTHORS   Fujioka,M., Takahashi,N., Odai,H., Araki,S., Ichikawa,K., Feng,J.,
            Nakamura,M., Kaibuchi,K., Hartshorne,D.J., Nakano,T. and Ito,M.
  TITLE     A new isoform of human myosin phosphatase targeting/regulatory
            subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal
            mapping
  JOURNAL   Genomics 49 (1), 59-68 (1998)
   PUBMED   9570949
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356953.17, AK307591.1,
            BC144699.1, AF324888.1, AC099336.2 and AC118556.2.
            
            On Nov 18, 2009 this sequence version replaced NP_002472.1.
            
            Summary: Myosin phosphatase is a protein complex comprised of three
            subunits: a catalytic subunit (PP1c-delta, protein phosphatase 1,
            catalytic subunit delta), a large regulatory subunit (MYPT, myosin
            phosphatase target) and small regulatory subunit (sm-M20). Two
            isoforms of MYPT have been isolated--MYPT1 and MYPT2, the first of
            which is widely expressed, and the second of which may be specific
            to heart, skeletal muscle, and brain. Each of the MYPT isoforms
            functions to bind PP1c-delta and increase phosphatase activity.
            This locus encodes both MYTP2 and M20. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified. Related pseudogenes have been defined on the Y
            chromosome. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) lacks an alternate in-frame
            exon compared to variant 8. The resulting isoform (a, also known as
            the large myosin binding subunit) has the same N- and C-termini but
            is shorter compared to isoform h.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.139958.1, AF324888.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000608999.6/ ENSP00000476755.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..982
                     /product="protein phosphatase 1 regulatory subunit 12B
                     isoform a"
                     /EC_number="3.1.3.53"
                     /note="myosin phosphatase target subunit 2; myosin
                     phosphatase-targeting subunit 2; protein phosphatase 1,
                     regulatory (inhibitor) subunit 12B"
                     /calculated_mol_wt=110273
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Region          57..86
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          <62..308
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(67..69,71..72,76,79,88,90,92,96..97,100..102,
                     104..105,109,112,121,123,125,129..130,133..135,137..138,
                     142,145,154)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          90..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          90..119
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          123..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..152
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          156..247
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <169..>257
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          216..245
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          249..280
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          249..278
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          342..517
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Region          556..579
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          606..864
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          608..664
                     /region_name="IPD_MYPT1"
                     /note="inhibitory phosphorylation domain of myosin
                     phosphatase targeting subunit 1(MYPT1); cd21944"
                     /db_xref="CDD:412019"
     Region          <624..>738
                     /region_name="PspC_subgroup_1"
                     /note="pneumococcal surface protein PspC, choline-binding
                     form; NF033838"
                     /db_xref="CDD:468201"
     Site            646
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Site            839
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Region          881..982
                     /region_name="PRKG1_interact"
                     /note="cGMP-dependent protein kinase interacting domain;
                     pfam15898"
                     /db_xref="CDD:464927"
     Region          918..948
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     CDS             1..982
                     /gene="PPP1R12B"
                     /gene_synonym="MYPT2; PP1bp55"
                     /coded_by="NM_002481.4:154..3102"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1426.1"
                     /db_xref="GeneID:4660"
                     /db_xref="HGNC:HGNC:7619"
                     /db_xref="MIM:603768"
ORIGIN      
        1 maelehlggk raesarmrra eqlrrwrgsl teqepaerrg agrqpltrrg sprvrfedga
       61 vflaacssgd tdevrkllar gadintvnvd gltalhqaci denldmvkfl venranvnqq
      121 dnegwtplha aascgylnia eyfinhgasv givnsegevp sdlaeepamk dllleqvkkq
      181 gvdleqsrke eeqqmlqdar qwlnsgkied vrqarsgata lhvaaakgys evlrlliqag
      241 yelnvqdydg wtplhaaahw gvkeacsila ealcdmdirn klgqtpfdva deglvehlel
      301 lqkkqnvlrs eketrnklie sdlnskiqsg ffknkekmly eeetpksqem eeenkessss
      361 sseeeegede asesetekea dkkpeafvnh snseskssit eqipapaqnt fsassarrfs
      421 sglfnkpeep kdespsswrl glrktgshnm lsevansrep irdrgssiyr ssssprisal
      481 ldnkdkeren ksyisslapr klnstsdiee kenresavnl vrsgsytrql wrdeakgnei
      541 pqtiapstyv stylkrtphk sqadttaekt adnvssstpl cvitnrplps tangvtatpv
      601 lsitgtdssv earekrrsyl tpvrdeeaes lrkarsrqar qtrrstqgvt ltdlqeaert
      661 fsrsraerqa qeqprekptd teglegspek hepsavpate agegqqpwgr sldeepichr
      721 lrcpaqpdkp ttpaspstsr pslytsshll wtnrfsvpds essetttntt takemdknen
      781 eeadldeqss krlsirerrr pkerrrgtgi nfwtkdedet dgseevketw herlsrlesg
      841 gsnpttsdsy gdrasararr earearlatl tsrveedsnr dykklyesal tenqklktkl
      901 qeaqleladi ksklekvaqq kqektsdrss vlemekrerr alerkmseme eemkvltelk
      961 sdnqrlkden galirviskl sk
//
