IGBP1_HUMAN
ID IGBP1_HUMAN Reviewed; 339 AA.
AC P78318; Q8TAB2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Immunoglobulin-binding protein 1;
DE AltName: Full=B-cell signal transduction molecule alpha 4;
DE Short=Protein alpha-4;
DE AltName: Full=CD79a-binding protein 1;
DE AltName: Full=Protein phosphatase 2/4/6 regulatory subunit;
DE AltName: Full=Renal carcinoma antigen NY-REN-16;
GN Name=IGBP1; Synonyms=IBP1;
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].
RC TISSUE=B-cell;
RX PubMed=9441740; DOI=10.1006/geno.1997.5048;
RA Onda M., Inui S., Maeda K., Suzuki M., Takahashi E., Sakaguchi N.;
RT "Expression and chromosomal localization of the human alpha 4/IGBP1 gene,
RT the structure of which is closely related to the yeast TAP42 protein of the
RT rapamycin-sensitive signal transduction pathway.";
RL Genomics 46:373-378(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP INTERACTION WITH SERINE/THREONINE PROTEIN PHOSPHATASES.
RX PubMed=9647778; DOI=10.1006/bbrc.1998.8792;
RA Chen J., Peterson R.T., Schreiber S.L.;
RT "Alpha 4 associates with protein phosphatases 2A, 4, and 6.";
RL Biochem. Biophys. Res. Commun. 247:827-832(1998).
RN [6]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [7]
RP INTERACTION WITH MID1 AND MID2.
RX PubMed=11806752; DOI=10.1186/1471-2121-3-1;
RA Short K.M., Hopwood B., Yi Z., Cox T.C.;
RT "MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive
RT PP2A regulatory subunit, Alpha 4, to microtubules: implications for the
RT clinical variability of X-linked Opitz GBBB syndrome and other
RT developmental disorders.";
RL BMC Cell Biol. 3:1-1(2002).
RN [8]
RP INVOLVEMENT IN MRXS28.
RX PubMed=14556245; DOI=10.1002/ajmg.a.20504;
RA Graham J.M. Jr., Wheeler P., Tackels-Horne D., Lin A.E., Hall B.D., May M.,
RA Short K.M., Schwartz C.E., Cox T.C.;
RT "A new X-linked syndrome with agenesis of the corpus callosum, mental
RT retardation, coloboma, micrognathia, and a mutation in the alpha 4 gene at
RT Xq13.";
RL Am. J. Med. Genet. A 123:37-44(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH PPP2CA.
RX PubMed=19818709; DOI=10.1016/j.molcel.2009.09.025;
RA Kong M., Ditsworth D., Lindsten T., Thompson C.B.;
RT "Alpha4 is an essential regulator of PP2A phosphatase activity.";
RL Mol. Cell 36:51-60(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP UBIQUITINATION, AND INTERACTION WITH PPP2CA AND UBIQUITIN.
RX PubMed=20092282; DOI=10.1021/bi901837h;
RA McConnell J.L., Watkins G.R., Soss S.E., Franz H.S., McCorvey L.R.,
RA Spiller B.W., Chazin W.J., Wadzinski B.E.;
RT "Alpha4 is a ubiquitin-binding protein that regulates protein
RT serine/threonine phosphatase 2A ubiquitination.";
RL Biochemistry 49:1713-1718(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP UBIQUITINATION BY MID1, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=22613722; DOI=10.1074/jbc.m112.368613;
RA Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R.,
RA Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.;
RT "Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A
RT (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-
RT associated protein phosphorylation.";
RL J. Biol. Chem. 287:24207-24215(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234 IN COMPLEX WITH PPP2CA,
RP FUNCTION, MUTAGENESIS OF ARG-155; LYS-158; TYR-162 AND GLU-214, AND
RP INTERACTION WITH PPP2CA.
RX PubMed=23591866; DOI=10.1038/ncomms2663;
RA Jiang L., Stanevich V., Satyshur K.A., Kong M., Watkins G.R.,
RA Wadzinski B.E., Sengupta R., Xing Y.;
RT "Structural basis of protein phosphatase 2A stable latency.";
RL Nat. Commun. 4:1699-1699(2013).
CC -!- FUNCTION: Associated to surface IgM-receptor; may be involved in signal
CC transduction. Involved in regulation of the catalytic activity of the
CC phosphatases PP2A, PP4 and PP6 by protecting their partially folded
CC catalytic subunits from degradative polyubiquitination until they
CC associate with regulatory subunits. {ECO:0000269|PubMed:19818709,
CC ECO:0000269|PubMed:23591866}.
CC -!- SUBUNIT: Interacts with partially folded PPP2CA, but not with the fully
CC active protein. Interacts with PPP2CB, and with PP4 and PP6. Interacts
CC with MID1 and MID2. Interacts with ubiquitin.
CC {ECO:0000269|PubMed:11806752, ECO:0000269|PubMed:19818709,
CC ECO:0000269|PubMed:20092282, ECO:0000269|PubMed:23591866,
CC ECO:0000269|PubMed:9647778}.
CC -!- INTERACTION:
CC P78318; P04792: HSPB1; NbExp=3; IntAct=EBI-1055954, EBI-352682;
CC P78318; Q92993: KAT5; NbExp=3; IntAct=EBI-1055954, EBI-399080;
CC P78318; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1055954, EBI-11742507;
CC P78318; O15344: MID1; NbExp=4; IntAct=EBI-1055954, EBI-2340316;
CC P78318; P67775: PPP2CA; NbExp=18; IntAct=EBI-1055954, EBI-712311;
CC P78318; P62714: PPP2CB; NbExp=6; IntAct=EBI-1055954, EBI-1044367;
CC P78318; P60510: PPP4C; NbExp=15; IntAct=EBI-1055954, EBI-1046072;
CC P78318; O00743: PPP6C; NbExp=17; IntAct=EBI-1055954, EBI-359751;
CC P78318; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1055954, EBI-9090795;
CC P78318; O15266-2: SHOX; NbExp=3; IntAct=EBI-1055954, EBI-12825957;
CC P78318; O75663: TIPRL; NbExp=2; IntAct=EBI-1055954, EBI-1054735;
CC P78318; P61981: YWHAG; NbExp=3; IntAct=EBI-1055954, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC heart, skeletal muscle and pancreas.
CC -!- DOMAIN: The UIM domain is required for protective effect on PP2A.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Monoubiquitination by MID1 triggers calpain-mediated cleavage and
CC switches IGBP1 activity from protective to destructive.
CC {ECO:0000269|PubMed:22613722}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 28
CC (MRXS28) [MIM:300472]: An intellectual disability syndrome
CC characterized by agenesis of the corpus callosum, coloboma of the iris
CC and optic nerve, severe retrognathia, and intellectual deficit.
CC Intellectual disability is defined by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:14556245}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the IGBP1/TAP42 family. {ECO:0000305}.
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DR EMBL; Y08915; CAA70119.1; -; mRNA.
DR EMBL; BT006736; AAP35382.1; -; mRNA.
DR EMBL; AL139111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004137; AAH04137.1; -; mRNA.
DR CCDS; CCDS14396.1; -.
DR RefSeq; NP_001542.1; NM_001551.2.
DR RefSeq; XP_016884978.1; XM_017029489.1.
DR PDB; 4IYP; X-ray; 2.80 A; A=2-234.
DR PDBsum; 4IYP; -.
DR AlphaFoldDB; P78318; -.
DR SMR; P78318; -.
DR BioGRID; 109698; 150.
DR CORUM; P78318; -.
DR IntAct; P78318; 52.
DR MINT; P78318; -.
DR STRING; 9606.ENSP00000363661; -.
DR CarbonylDB; P78318; -.
DR GlyGen; P78318; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P78318; -.
DR MetOSite; P78318; -.
DR PhosphoSitePlus; P78318; -.
DR BioMuta; IGBP1; -.
DR DMDM; 14285501; -.
DR EPD; P78318; -.
DR jPOST; P78318; -.
DR MassIVE; P78318; -.
DR MaxQB; P78318; -.
DR PaxDb; P78318; -.
DR PeptideAtlas; P78318; -.
DR PRIDE; P78318; -.
DR ProteomicsDB; 57563; -.
DR Antibodypedia; 359; 253 antibodies from 28 providers.
DR DNASU; 3476; -.
DR Ensembl; ENST00000342206.10; ENSP00000363661.5; ENSG00000089289.16.
DR Ensembl; ENST00000356413.5; ENSP00000348784.4; ENSG00000089289.16.
DR GeneID; 3476; -.
DR KEGG; hsa:3476; -.
DR MANE-Select; ENST00000356413.5; ENSP00000348784.4; NM_001551.3; NP_001542.1.
DR UCSC; uc004dxv.4; human.
DR CTD; 3476; -.
DR DisGeNET; 3476; -.
DR GeneCards; IGBP1; -.
DR HGNC; HGNC:5461; IGBP1.
DR HPA; ENSG00000089289; Low tissue specificity.
DR MalaCards; IGBP1; -.
DR MIM; 300139; gene.
DR MIM; 300472; phenotype.
DR neXtProt; NX_P78318; -.
DR OpenTargets; ENSG00000089289; -.
DR Orphanet; 52055; Corpus callosum agenesis-intellectual disability-coloboma-micrognathia syndrome.
DR PharmGKB; PA29694; -.
DR VEuPathDB; HostDB:ENSG00000089289; -.
DR eggNOG; KOG2830; Eukaryota.
DR GeneTree; ENSGT00390000002414; -.
DR HOGENOM; CLU_041824_1_0_1; -.
DR InParanoid; P78318; -.
DR OMA; RAWDEFT; -.
DR OrthoDB; 1348942at2759; -.
DR PhylomeDB; P78318; -.
DR TreeFam; TF313433; -.
DR PathwayCommons; P78318; -.
DR SignaLink; P78318; -.
DR BioGRID-ORCS; 3476; 408 hits in 703 CRISPR screens.
DR ChiTaRS; IGBP1; human.
DR GeneWiki; IGBP1; -.
DR GenomeRNAi; 3476; -.
DR Pharos; P78318; Tbio.
DR PRO; PR:P78318; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P78318; protein.
DR Bgee; ENSG00000089289; Expressed in cortical plate and 212 other tissues.
DR Genevisible; P78318; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035303; P:regulation of dephosphorylation; IBA:GO_Central.
DR GO; GO:0060632; P:regulation of microtubule-based movement; IMP:UniProtKB.
DR GO; GO:0070555; P:response to interleukin-1; IMP:UniProtKB.
DR GO; GO:0034612; P:response to tumor necrosis factor; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR Gene3D; 1.25.40.540; -; 1.
DR InterPro; IPR038511; TAP42/TAP46-like_sf.
DR InterPro; IPR007304; TAP46-like.
DR PANTHER; PTHR10933; PTHR10933; 1.
DR Pfam; PF04177; TAP42; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; B-cell activation; Chaperone; Cytoplasm;
KW Intellectual disability; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..339
FT /note="Immunoglobulin-binding protein 1"
FT /id="PRO_0000218618"
FT DOMAIN 46..60
FT /note="UIM"
FT /evidence="ECO:0000305"
FT REGION 98..202
FT /note="Interaction with PPP2CA"
FT REGION 221..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..290
FT /note="Interaction with MID1"
FT /evidence="ECO:0000269|PubMed:11806752"
FT REGION 289..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 255..256
FT /note="Cleavage; by calpain"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 20
FT /note="R -> K (in dbSNP:rs6625580)"
FT /id="VAR_049570"
FT MUTAGEN 155
FT /note="R->E: Abolishes interaction with PPP2CA."
FT /evidence="ECO:0000269|PubMed:23591866"
FT MUTAGEN 158
FT /note="K->D: Abolishes interaction with PPP2CA."
FT /evidence="ECO:0000269|PubMed:23591866"
FT MUTAGEN 162
FT /note="Y->D: Abolishes interaction with PPP2CA."
FT /evidence="ECO:0000269|PubMed:23591866"
FT MUTAGEN 214
FT /note="E->R: Abolishes interaction with PPP2CA."
FT /evidence="ECO:0000269|PubMed:23591866"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 12..27
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 36..59
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4IYP"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:4IYP"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 156..180
FT /evidence="ECO:0007829|PDB:4IYP"
FT HELIX 186..219
FT /evidence="ECO:0007829|PDB:4IYP"
SQ SEQUENCE 339 AA; 39222 MW; BB00A116EB45273A CRC64;
MAAEDELQLP RLPELFETGR QLLDEVEVAT EPAGSRIVQE KVFKGLDLLE KAAEMLSQLD
LFSRNEDLEE IASTDLKYLL VPAFQGALTM KQVNPSKRLD HLQRAREHFI NYLTQCHCYH
VAEFELPKTM NNSAENHTAN SSMAYPSLVA MASQRQAKIQ RYKQKKELEH RLSAMKSAVE
SGQADDERVR EYYLLHLQRW IDISLEEIES IDQEIKILRE RDSSREASTS NSSRQERPPV
KPFILTRNMA QAKVFGAGYP SLPTMTVSDW YEQHRKYGAL PDQGIAKAAP EEFRKAAQQQ
EEQEEKEEED DEQTLHRARE WDDWKDTHPR GYGNRQNMG
