ID   TSH3_HUMAN              Reviewed;        1081 AA.
AC   Q63HK5; A1L0U7; Q9H0G6; Q9P254;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   02-OCT-2024, entry version 180.
DE   RecName: Full=Teashirt homolog 3;
DE   AltName: Full=Zinc finger protein 537;
GN   Name=TSHZ3; Synonyms=KIAA1474, TSH3, ZNF537;
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 [LARGE SCALE MRNA], AND VARIANT GLY-469.
RC   TISSUE=Endometrial tumor;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1081.
RC   TISSUE=Brain;
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-1081.
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-1081.
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   TISSUE SPECIFICITY.
RX   PubMed=18776146; DOI=10.1242/dev.022442;
RA   Caubit X., Lye C.M., Martin E., Core N., Long D.A., Vola C., Jenkins D.,
RA   Garratt A.N., Skaer H., Woolf A.S., Fasano L.;
RT   "Teashirt 3 is necessary for ureteral smooth muscle differentiation
RT   downstream of SHH and BMP4.";
RL   Development 135:3301-3310(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [7]
RP   FUNCTION, INTERACTION WITH APBB1; HDAC1 AND HDAC2, IDENTIFICATION IN A
RP   TRIMERIC COMPLEX WITH APBB1 AND HDAC1, CHROMATIN-BINDING, MUTAGENESIS OF
RP   953-VAL--TYR-955, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA   Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA   Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT   "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT   caspase-4.";
RL   PLoS ONE 4:E5071-E5071(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   TISSUE SPECIFICITY, AND INVOLVEMENT IN NEURODEVELOPMENTAL DISORDER.
RX   PubMed=27668656; DOI=10.1038/ng.3681;
RA   Caubit X., Gubellini P., Andrieux J., Roubertoux P.L., Metwaly M., Jacq B.,
RA   Fatmi A., Had-Aissouni L., Kwan K.Y., Salin P., Carlier M., Lieden A.,
RA   Rudd E., Shinawi M., Vincent-Delorme C., Cuisset J.M., Lemaitre M.P.,
RA   Abderrehamane F., Duban B., Lemaitre J.F., Woolf A.S., Bockenhauer D.,
RA   Severac D., Dubois E., Zhu Y., Sestan N., Garratt A.N.,
RA   Kerkerian-Le Goff L., Fasano L.;
RT   "TSHZ3 deletion causes an autism syndrome and defects in cortical
RT   projection neurons.";
RL   Nat. Genet. 48:1359-1369(2016).
RN   [11]
RP   VARIANT GLY-469, AND DEVELOPMENTAL STAGE.
RX   PubMed=19745106; DOI=10.1093/ndt/gfp453;
RA   Jenkins D., Caubit X., Dimovski A., Matevska N., Lye C.M., Cabuk F.,
RA   Gucev Z., Tasic V., Fasano L., Woolf A.S.;
RT   "Analysis of TSHZ2 and TSHZ3 genes in congenital pelvi-ureteric junction
RT   obstruction.";
RL   Nephrol. Dial. Transplant. 25:54-60(2010).
RN   [12]
RP   STRUCTURE BY NMR OF 200-303.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the first and the second ZF-C2H2-like domains of
RT   human teashirt homolog 3.";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: Transcriptional regulator involved in developmental
CC       processes. Functions in association with APBB1, SET and HDAC factors as
CC       a transcriptional repressor, that inhibits the expression of CASP4.
CC       TSHZ3-mediated transcription repression involves the recruitment of
CC       histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a
CC       region surrounding the CASP4 transcriptional start site(s)
CC       (PubMed:19343227). Regulates the development of neurons involved in
CC       both respiratory rhythm and airflow control. Promotes maintenance of
CC       nucleus ambiguus (nA) motoneurons, which govern upper airway function,
CC       and establishes a respiratory rhythm generator (RRG) activity
CC       compatible with survival at birth. Involved in the differentiation of
CC       the proximal uretic smooth muscle cells during developmental processes.
CC       Involved in the up-regulation of myocardin, that directs the expression
CC       of smooth muscle cells in the proximal ureter (By similarity). Involved
CC       in the modulation of glutamatergic synaptic transmission and long-term
CC       synaptic potentiation (By similarity). {ECO:0000250|UniProtKB:Q8CGV9,
CC       ECO:0000269|PubMed:19343227}.
CC   -!- SUBUNIT: Interacts (via homeobox domain) with APBB1 (via PID domain 1).
CC       Interacts (via N-terminus) with HDAC1 and HDAC2; the interaction is
CC       direct. Found in a trimeric complex with APBB1 and HDAC1; the
CC       interaction between HDAC1 and APBB1 is mediated by TSHZ3.
CC       {ECO:0000269|PubMed:19343227}.
CC   -!- INTERACTION:
CC       Q63HK5; Q9H9E1: ANKRA2; NbExp=3; IntAct=EBI-9053916, EBI-10215533;
CC       Q63HK5; Q9UBZ4: APEX2; NbExp=3; IntAct=EBI-9053916, EBI-742588;
CC       Q63HK5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-9053916, EBI-10175300;
CC       Q63HK5; Q96MT8: CEP63; NbExp=3; IntAct=EBI-9053916, EBI-741977;
CC       Q63HK5; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-9053916, EBI-739624;
CC       Q63HK5; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-9053916, EBI-3866319;
CC       Q63HK5; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-9053916, EBI-10171858;
CC       Q63HK5; P56545-3: CTBP2; NbExp=6; IntAct=EBI-9053916, EBI-10171902;
CC       Q63HK5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-9053916, EBI-618309;
CC       Q63HK5; O75031: HSF2BP; NbExp=3; IntAct=EBI-9053916, EBI-7116203;
CC       Q63HK5; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-9053916, EBI-749265;
CC       Q63HK5; Q15323: KRT31; NbExp=3; IntAct=EBI-9053916, EBI-948001;
CC       Q63HK5; Q6A162: KRT40; NbExp=3; IntAct=EBI-9053916, EBI-10171697;
CC       Q63HK5; Q5JTD7: LRRC73; NbExp=3; IntAct=EBI-9053916, EBI-12003882;
CC       Q63HK5; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-9053916, EBI-742610;
CC       Q63HK5; Q13084: MRPL28; NbExp=3; IntAct=EBI-9053916, EBI-723426;
CC       Q63HK5; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-9053916, EBI-742948;
CC       Q63HK5; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-9053916, EBI-11522433;
CC       Q63HK5; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-9053916, EBI-14066006;
CC       Q63HK5; Q6NUQ1: RINT1; NbExp=5; IntAct=EBI-9053916, EBI-726876;
CC       Q63HK5; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-9053916, EBI-1378139;
CC       Q63HK5; Q96R06: SPAG5; NbExp=3; IntAct=EBI-9053916, EBI-413317;
CC       Q63HK5; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-9053916, EBI-529518;
CC       Q63HK5; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-9053916, EBI-11139477;
CC       Q63HK5; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-9053916, EBI-1105213;
CC       Q63HK5; Q12933: TRAF2; NbExp=3; IntAct=EBI-9053916, EBI-355744;
CC       Q63HK5; P36406: TRIM23; NbExp=3; IntAct=EBI-9053916, EBI-740098;
CC       Q63HK5; P14373: TRIM27; NbExp=3; IntAct=EBI-9053916, EBI-719493;
CC       Q63HK5; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-9053916, EBI-2130429;
CC       Q63HK5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-9053916, EBI-12806590;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC       ECO:0000269|PubMed:19343227}. Cell projection, growth cone
CC       {ECO:0000250}. Note=Colocalizes with APBB1 in axonal growth cone (By
CC       similarity). Colocalizes with APBB1 in the nucleus. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain; strongly reduced in post-mortem
CC       elderly subjects with Alzheimer disease (PubMed:18776146,
CC       PubMed:19343227). Expressed in the fetal neocortex (PubMed:27668656).
CC       {ECO:0000269|PubMed:18776146, ECO:0000269|PubMed:19343227,
CC       ECO:0000269|PubMed:27668656}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in peri-urothelial cells of the proximal
CC       ureter and renal pelvis at 9 weeks of gestation.
CC       {ECO:0000269|PubMed:19745106}.
CC   -!- DISEASE: Note=TSHZ3 haploinsufficiency due to proximal chromosome
CC       19q13.11 deletions causes a neurodevelopmental disorder characterized
CC       by developmental delay, absent or delayed speech, intellectual
CC       disability, and autistic features. Some patients may have reanal tract
CC       abnormalities. {ECO:0000269|PubMed:27668656}.
CC   -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI27096.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI27097.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB66739.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life's first breath - Issue
CC       122 of October 2010;
CC       URL="https://web.expasy.org/spotlight/back_issues/122";
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DR   EMBL; BX648745; CAH56184.1; -; mRNA.
DR   EMBL; AB040907; BAA95998.1; -; mRNA.
DR   EMBL; AL136805; CAB66739.1; ALT_INIT; mRNA.
DR   EMBL; BC127095; AAI27096.1; ALT_INIT; mRNA.
DR   EMBL; BC127096; AAI27097.1; ALT_INIT; mRNA.
DR   CCDS; CCDS12421.2; -.
DR   RefSeq; NP_065907.2; NM_020856.3.
DR   PDB; 2DMI; NMR; -; A=202-303.
DR   PDBsum; 2DMI; -.
DR   AlphaFoldDB; Q63HK5; -.
DR   SMR; Q63HK5; -.
DR   BioGRID; 121663; 76.
DR   CORUM; Q63HK5; -.
DR   IntAct; Q63HK5; 55.
DR   MINT; Q63HK5; -.
DR   STRING; 9606.ENSP00000240587; -.
DR   GlyCosmos; Q63HK5; 2 sites, 1 glycan.
DR   GlyGen; Q63HK5; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q63HK5; -.
DR   PhosphoSitePlus; Q63HK5; -.
DR   BioMuta; TSHZ3; -.
DR   DMDM; 85541971; -.
DR   jPOST; Q63HK5; -.
DR   MassIVE; Q63HK5; -.
DR   PaxDb; 9606-ENSP00000240587; -.
DR   PeptideAtlas; Q63HK5; -.
DR   ProteomicsDB; 65878; -.
DR   Pumba; Q63HK5; -.
DR   Antibodypedia; 1780; 122 antibodies from 28 providers.
DR   DNASU; 57616; -.
DR   Ensembl; ENST00000240587.5; ENSP00000240587.4; ENSG00000121297.8.
DR   GeneID; 57616; -.
DR   KEGG; hsa:57616; -.
DR   MANE-Select; ENST00000240587.5; ENSP00000240587.4; NM_020856.4; NP_065907.2.
DR   UCSC; uc002nsy.5; human.
DR   AGR; HGNC:30700; -.
DR   CTD; 57616; -.
DR   DisGeNET; 57616; -.
DR   GeneCards; TSHZ3; -.
DR   HGNC; HGNC:30700; TSHZ3.
DR   HPA; ENSG00000121297; Tissue enhanced (ovary).
DR   MIM; 614119; gene.
DR   neXtProt; NX_Q63HK5; -.
DR   OpenTargets; ENSG00000121297; -.
DR   PharmGKB; PA134887020; -.
DR   VEuPathDB; HostDB:ENSG00000121297; -.
DR   eggNOG; ENOG502RJS7; Eukaryota.
DR   GeneTree; ENSGT00950000183051; -.
DR   HOGENOM; CLU_010469_0_0_1; -.
DR   InParanoid; Q63HK5; -.
DR   OMA; KELVKPM; -.
DR   OrthoDB; 5407068at2759; -.
DR   PhylomeDB; Q63HK5; -.
DR   TreeFam; TF328447; -.
DR   PathwayCommons; Q63HK5; -.
DR   SignaLink; Q63HK5; -.
DR   SIGNOR; Q63HK5; -.
DR   BioGRID-ORCS; 57616; 11 hits in 1172 CRISPR screens.
DR   ChiTaRS; TSHZ3; human.
DR   EvolutionaryTrace; Q63HK5; -.
DR   GeneWiki; TSHZ3; -.
DR   GenomeRNAi; 57616; -.
DR   Pharos; Q63HK5; Tbio.
DR   PRO; PR:Q63HK5; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q63HK5; protein.
DR   Bgee; ENSG00000121297; Expressed in cortical plate and 152 other cell types or tissues.
DR   ExpressionAtlas; Q63HK5; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR   InterPro; IPR001356; HD.
DR   InterPro; IPR027008; Teashirt_fam.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR12487:SF5; TEASHIRT HOMOLOG 3; 1.
DR   PANTHER; PTHR12487; TEASHIRT-RELATED; 1.
DR   Pfam; PF13912; zf-C2H2_6; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cell projection; Coiled coil; Developmental protein;
KW   DNA-binding; Homeobox; Metal-binding; Nucleus; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1081
FT                   /note="Teashirt homolog 3"
FT                   /id="PRO_0000047066"
FT   ZN_FING         214..238
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         275..299
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         386..404
FT                   /note="C2H2-type 3; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   DNA_BIND        891..961
FT                   /note="Homeobox; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   ZN_FING         976..998
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1041..1064
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          141..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          606..630
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        330..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..890
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         682
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VARIANT         469
FT                   /note="E -> G (in dbSNP:rs143453460)"
FT                   /evidence="ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|PubMed:19745106"
FT                   /id="VAR_063635"
FT   VARIANT         687
FT                   /note="P -> L (in dbSNP:rs4805664)"
FT                   /id="VAR_052708"
FT   MUTAGEN         953..955
FT                   /note="VKY->ATA: Does not inhibit interaction with APBB1."
FT                   /evidence="ECO:0000269|PubMed:19343227"
FT   CONFLICT        176
FT                   /note="L -> V (in Ref. 4; AAI27096/AAI27097)"
FT                   /evidence="ECO:0000305"
FT   STRAND          213..220
FT                   /evidence="ECO:0007829|PDB:2DMI"
FT   STRAND          222..225
FT                   /evidence="ECO:0007829|PDB:2DMI"
FT   HELIX           226..235
FT                   /evidence="ECO:0007829|PDB:2DMI"
FT   STRAND          278..280
FT                   /evidence="ECO:0007829|PDB:2DMI"
FT   HELIX           287..296
FT                   /evidence="ECO:0007829|PDB:2DMI"
FT   TURN            297..301
FT                   /evidence="ECO:0007829|PDB:2DMI"
SQ   SEQUENCE   1081 AA;  118566 MW;  B4E0A4347B04E74A CRC64;
     MPRRKQQAPR RAAAYVSEEL KAAALVDEGL DPEEHTADGE PSAKYMCPEK ELARACPSYQ
     NSPAAEFSCH EMDSESHISE TSDRMADFES GSIKNEEETK EVTVPLEDTT VSDSLEQMKA
     VYNNFLSNSY WSNLNLNLHQ PSSEKNNGSS SSSSSSSSSC GSGSFDWHQS AMAKTLQQVS
     QSRMLPEPSL FSTVQLYRQS SKLYGSIFTG ASKFRCKDCS AAYDTLVELT VHMNETGHYR
     DDNHETDNNN PKRWSKPRKR SLLEMEGKED AQKVLKCMYC GHSFESLQDL SVHMIKTKHY
     QKVPLKEPVT PVAAKIIPAT RKKASLELEL PSSPDSTGGT PKATISDTND ALQKNSNPYI
     TPNNRYGHQN GASYAWHFEA RKSQILKCME CGSSHDTLQE LTAHMMVTGH FIKVTNSAMK
     KGKPIVETPV TPTITTLLDE KVQSVPLAAT TFTSPSNTPA SISPKLNVEV KKEVDKEKAV
     TDEKPKQKDK PGEEEEKCDI SSKYHYLTEN DLEESPKGGL DILKSLENTV TSAINKAQNG
     TPSWGGYPSI HAAYQLPNMM KLSLGSSGKS TPLKPMFGNS EIVSPTKNQT LVSPPSSQTS
     PMPKTNFHAM EELVKKVTEK VAKVEEKMKE PDGKLSPPKR ATPSPCSSEV GEPIKMEASS
     DGGFRSQENS PSPPRDGCKD GSPLAEPVEN GKELVKPLAS SLSGSTAIIT DHPPEQPFVN
     PLSALQSVMN IHLGKAAKPS LPALDPMSML FKMSNSLAEK AAVATPPPLQ SKKADHLDRY
     FYHVNNDQPI DLTKGKSDKG CSLGSVLLSP TSTAPATSSS TVTTAKTSAV VSFMSNSPLR
     ENALSDISDM LKNLTESHTS KSSTPSSISE KSDIDGATLE EAEESTPAQK RKGRQSNWNP
     QHLLILQAQF AASLRQTSEG KYIMSDLSPQ ERMHISRFTG LSMTTISHWL ANVKYQLRRT
     GGTKFLKNLD TGHPVFFCND CASQIRTPST YISHLESHLG FRLRDLSKLS TEQINSQIAQ
     TKSPSEKMVT SSPEEDLGTS YQCKLCNRTF ASKHAVKLHL SKTHGKSPED HLLYVSELEK
     Q
//