MYPT2_HUMAN
ID MYPT2_HUMAN Reviewed; 982 AA.
AC O60237; A0A0A0MS24; A8MYF5; B7ZMN6; Q2TAI8; Q5T506; Q5VUK2; Q8N179; Q9HCB7;
AC Q9HCB8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 12B;
DE AltName: Full=Myosin phosphatase-targeting subunit 2;
DE Short=Myosin phosphatase target subunit 2;
GN Name=PPP1R12B; Synonyms=MYPT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-182, FUNCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9570949; DOI=10.1006/geno.1998.5222;
RA Fujioka M., Takahashi N., Odai H., Araki S., Ichikawa K., Feng J.,
RA Nakamura M., Kaibuchi K., Hartshorne D.J., Nakano T., Ito M.;
RT "A new isoform of human myosin phosphatase targeting/regulatory subunit
RT (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping.";
RL Genomics 49:59-68(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ILE-182.
RA Li D., Roberts R.;
RT "Human myosin phosphatase target subunit 2 (MYPT2): full-length cDNA
RT cloning, genomic structure, and mutation analysis in patients with familial
RT dilated cardiomyopathy mapped to 1q32.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH PPP1R12A.
RC TISSUE=Heart;
RX PubMed=11067852; DOI=10.1074/jbc.m008566200;
RA Arimura T., Suematsu N., Zhou Y.-B., Nishimura J., Satoh S., Takeshita A.,
RA Kanaide H., Kimura A.;
RT "Identification, characterization, and functional analysis of heart-
RT specific myosin light chain phosphatase small subunit.";
RL J. Biol. Chem. 276:6073-6082(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH IL16, AND SUBCELLULAR LOCATION.
RX PubMed=12923170; DOI=10.1074/jbc.m306669200;
RA Bannert N., Vollhardt K., Asomuddinov B., Haag M., Koenig H., Norley S.,
RA Kurth R.;
RT "PDZ domain-mediated interaction of interleukin-16 precursor proteins with
RT myosin phosphatase targeting subunits.";
RL J. Biol. Chem. 278:42190-42199(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-646, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Regulates myosin phosphatase activity. Augments Ca(2+)
CC sensitivity of the contractile apparatus. {ECO:0000269|PubMed:11067852,
CC ECO:0000269|PubMed:9570949}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC and one or several targeting or regulatory subunits. PPP1R12B mediates
CC binding to myosin. Isoform 3 and isoform 4 bind PPP1R12A, but not
CC isoform 1 of PPP1R12B itself. Binds IL16.
CC -!- INTERACTION:
CC O60237-2; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-10700351, EBI-356015;
CC O60237-2; P22607: FGFR3; NbExp=3; IntAct=EBI-10700351, EBI-348399;
CC O60237-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-10700351, EBI-8285963;
CC O60237-2; P06396: GSN; NbExp=3; IntAct=EBI-10700351, EBI-351506;
CC O60237-2; Q92569: PIK3R3; NbExp=2; IntAct=EBI-10700351, EBI-79893;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12923170}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:12923170}. Note=Along actomyosin filaments.
CC {ECO:0000269|PubMed:12923170}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O60237-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60237-2; Sequence=VSP_009257, VSP_009258;
CC Name=3; Synonyms=hHS-M21B, Heart-specific myosin light chain
CC phosphatase small subunit B;
CC IsoId=O60237-3; Sequence=VSP_009256, VSP_009259;
CC Name=4; Synonyms=hHS-M21A, Heart-specific myosin light chain
CC phosphatase small subunit A;
CC IsoId=O60237-4; Sequence=VSP_009256;
CC Name=5;
CC IsoId=O60237-5; Sequence=VSP_043159, VSP_043160;
CC Name=6;
CC IsoId=O60237-6; Sequence=VSP_059344;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, fetal and adult heart,
CC brain, placenta, kidney, spleen, thymus, pancreas and lung. Isoform 3
CC and isoform 4 are heart specific. {ECO:0000269|PubMed:11067852,
CC ECO:0000269|PubMed:9570949}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 4. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage.
CC {ECO:0000305}.
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DR EMBL; AB003062; BAA28376.1; -; mRNA.
DR EMBL; AF324888; AAK00337.1; -; mRNA.
DR EMBL; AF324892; AAK00336.1; -; Genomic_DNA.
DR EMBL; AF324889; AAK00336.1; JOINED; Genomic_DNA.
DR EMBL; AF324890; AAK00336.1; JOINED; Genomic_DNA.
DR EMBL; AF324891; AAK00336.1; JOINED; Genomic_DNA.
DR EMBL; AB050641; BAB17610.1; -; mRNA.
DR EMBL; AB050642; BAB17611.1; -; mRNA.
DR EMBL; AC099336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91418.1; -; Genomic_DNA.
DR EMBL; BC034430; AAH34430.1; -; mRNA.
DR EMBL; BC110907; AAI10908.1; -; mRNA.
DR EMBL; BC144699; AAI44700.1; -; mRNA.
DR CCDS; CCDS1426.1; -. [O60237-1]
DR CCDS; CCDS44294.1; -. [O60237-4]
DR CCDS; CCDS44295.1; -. [O60237-3]
DR CCDS; CCDS53458.1; -. [O60237-5]
DR CCDS; CCDS53459.1; -. [O60237-2]
DR CCDS; CCDS81416.1; -. [O60237-6]
DR RefSeq; NP_001161329.1; NM_001167857.1. [O60237-5]
DR RefSeq; NP_001161330.1; NM_001167858.1. [O60237-2]
DR RefSeq; NP_001184060.1; NM_001197131.1.
DR RefSeq; NP_001317958.1; NM_001331029.1. [O60237-6]
DR RefSeq; NP_002472.2; NM_002481.3. [O60237-1]
DR RefSeq; NP_115286.1; NM_032103.2. [O60237-4]
DR RefSeq; NP_115287.1; NM_032104.2. [O60237-3]
DR RefSeq; XP_016856841.1; XM_017001352.1. [O60237-3]
DR RefSeq; XP_016856842.1; XM_017001353.1. [O60237-4]
DR RefSeq; XP_016856843.1; XM_017001354.1. [O60237-3]
DR AlphaFoldDB; O60237; -.
DR SMR; O60237; -.
DR BioGRID; 110743; 63.
DR ELM; O60237; -.
DR IntAct; O60237; 28.
DR MINT; O60237; -.
DR STRING; 9606.ENSP00000476755; -.
DR GlyGen; O60237; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60237; -.
DR PhosphoSitePlus; O60237; -.
DR BioMuta; PPP1R12B; -.
DR UCD-2DPAGE; O60237; -.
DR EPD; O60237; -.
DR jPOST; O60237; -.
DR MassIVE; O60237; -.
DR MaxQB; O60237; -.
DR PaxDb; O60237; -.
DR PeptideAtlas; O60237; -.
DR PRIDE; O60237; -.
DR ProteomicsDB; 49262; -. [O60237-1]
DR ProteomicsDB; 49263; -. [O60237-2]
DR ProteomicsDB; 49264; -. [O60237-3]
DR ProteomicsDB; 49265; -. [O60237-4]
DR ProteomicsDB; 49266; -. [O60237-5]
DR Antibodypedia; 20653; 58 antibodies from 16 providers.
DR DNASU; 4660; -.
DR Ensembl; ENST00000290419.9; ENSP00000484005.1; ENSG00000077157.22. [O60237-3]
DR Ensembl; ENST00000356764.6; ENSP00000349206.2; ENSG00000077157.22. [O60237-2]
DR Ensembl; ENST00000391959.5; ENSP00000375821.5; ENSG00000077157.22. [O60237-6]
DR Ensembl; ENST00000480184.5; ENSP00000417159.1; ENSG00000077157.22. [O60237-5]
DR Ensembl; ENST00000491336.5; ENSP00000480852.1; ENSG00000077157.22. [O60237-4]
DR Ensembl; ENST00000608999.6; ENSP00000476755.1; ENSG00000077157.22. [O60237-1]
DR GeneID; 4660; -.
DR KEGG; hsa:4660; -.
DR MANE-Select; ENST00000608999.6; ENSP00000476755.1; NM_002481.4; NP_002472.2.
DR UCSC; uc001gxy.4; human. [O60237-1]
DR CTD; 4660; -.
DR DisGeNET; 4660; -.
DR GeneCards; PPP1R12B; -.
DR HGNC; HGNC:7619; PPP1R12B.
DR HPA; ENSG00000077157; Tissue enhanced (heart).
DR MIM; 603768; gene.
DR neXtProt; NX_O60237; -.
DR OpenTargets; ENSG00000077157; -.
DR PharmGKB; PA33618; -.
DR VEuPathDB; HostDB:ENSG00000077157; -.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000157067; -.
DR HOGENOM; CLU_000134_54_0_1; -.
DR InParanoid; O60237; -.
DR OMA; GYSEVLX; -.
DR OrthoDB; 477969at2759; -.
DR PhylomeDB; O60237; -.
DR TreeFam; TF105543; -.
DR BRENDA; 3.1.3.53; 2681.
DR PathwayCommons; O60237; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition. [O60237-4]
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR SignaLink; O60237; -.
DR SIGNOR; O60237; -.
DR BioGRID-ORCS; 4660; 11 hits in 1084 CRISPR screens.
DR ChiTaRS; PPP1R12B; human.
DR GeneWiki; PPP1R12B; -.
DR GenomeRNAi; 4660; -.
DR Pharos; O60237; Tbio.
DR PRO; PR:O60237; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60237; protein.
DR Bgee; ENSG00000077157; Expressed in saphenous vein and 196 other tissues.
DR ExpressionAtlas; O60237; baseline and differential.
DR Genevisible; O60237; HS.
DR GO; GO:0031672; C:A band; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR GO; GO:0019208; F:phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0006937; P:regulation of muscle contraction; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017401; MYPT1/MYPT2/Mbs85.
DR InterPro; IPR031775; PRKG1_interact.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; ANK repeat; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..982
FT /note="Protein phosphatase 1 regulatory subunit 12B"
FT /id="PRO_0000067028"
FT REPEAT 57..86
FT /note="ANK 1"
FT REPEAT 90..119
FT /note="ANK 2"
FT REPEAT 123..152
FT /note="ANK 3"
FT REPEAT 216..245
FT /note="ANK 4"
FT REPEAT 249..278
FT /note="ANK 5"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG95"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG95"
FT MOD_RES 646
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG95"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG95"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG95"
FT VAR_SEQ 1..774
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11067852"
FT /id="VSP_009256"
FT VAR_SEQ 381..386
FT /note="DKKPEA -> VLFWPF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009257"
FT VAR_SEQ 387..982
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009258"
FT VAR_SEQ 487..515
FT /note="ERENKSYISSLAPRKLNSTSDIEEKENRE -> VQFGRVWGNSKAVFFFHEN
FT SILGTNENIF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043159"
FT VAR_SEQ 516..982
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043160"
FT VAR_SEQ 555
FT /note="K -> KSASFGRSSDPTSPYISANRNSSPATSPITIGSSTSRGSQWQPASSC
FT PAPISANTTASVHHG (in isoform 6)"
FT /id="VSP_059344"
FT VAR_SEQ 955..982
FT /note="VLTELKSDNQRLKDENGALIRVISKLSK -> NLHQLKQIQTLKQMNEQLQA
FT ENRALTRVVARLSESIESSDTQEL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11067852"
FT /id="VSP_009259"
FT VARIANT 182
FT /note="V -> I (in dbSNP:rs2843414)"
FT /evidence="ECO:0000269|PubMed:9570949, ECO:0000269|Ref.2"
FT /id="VAR_017480"
FT VARIANT 836
FT /note="R -> K (in dbSNP:rs3881953)"
FT /id="VAR_024177"
SQ SEQUENCE 982 AA; 110404 MW; A6EBB6AD4C61DD3B CRC64;
MAELEHLGGK RAESARMRRA EQLRRWRGSL TEQEPAERRG AGRQPLTRRG SPRVRFEDGA
VFLAACSSGD TDEVRKLLAR GADINTVNVD GLTALHQACI DENLDMVKFL VENRANVNQQ
DNEGWTPLHA AASCGYLNIA EYFINHGASV GIVNSEGEVP SDLAEEPAMK DLLLEQVKKQ
GVDLEQSRKE EEQQMLQDAR QWLNSGKIED VRQARSGATA LHVAAAKGYS EVLRLLIQAG
YELNVQDYDG WTPLHAAAHW GVKEACSILA EALCDMDIRN KLGQTPFDVA DEGLVEHLEL
LQKKQNVLRS EKETRNKLIE SDLNSKIQSG FFKNKEKMLY EEETPKSQEM EEENKESSSS
SSEEEEGEDE ASESETEKEA DKKPEAFVNH SNSESKSSIT EQIPAPAQNT FSASSARRFS
SGLFNKPEEP KDESPSSWRL GLRKTGSHNM LSEVANSREP IRDRGSSIYR SSSSPRISAL
LDNKDKEREN KSYISSLAPR KLNSTSDIEE KENRESAVNL VRSGSYTRQL WRDEAKGNEI
PQTIAPSTYV STYLKRTPHK SQADTTAEKT ADNVSSSTPL CVITNRPLPS TANGVTATPV
LSITGTDSSV EAREKRRSYL TPVRDEEAES LRKARSRQAR QTRRSTQGVT LTDLQEAERT
FSRSRAERQA QEQPREKPTD TEGLEGSPEK HEPSAVPATE AGEGQQPWGR SLDEEPICHR
LRCPAQPDKP TTPASPSTSR PSLYTSSHLL WTNRFSVPDS ESSETTTNTT TAKEMDKNEN
EEADLDEQSS KRLSIRERRR PKERRRGTGI NFWTKDEDET DGSEEVKETW HERLSRLESG
GSNPTTSDSY GDRASARARR EAREARLATL TSRVEEDSNR DYKKLYESAL TENQKLKTKL
QEAQLELADI KSKLEKVAQQ KQEKTSDRSS VLEMEKRERR ALERKMSEME EEMKVLTELK
SDNQRLKDEN GALIRVISKL SK
