ID   ZEP3_HUMAN              Reviewed;        2406 AA.
AC   Q5T1R4; A7YY91; Q5T1R5; Q9BZS0; Q9HCL7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Transcription factor HIVEP3;
DE   AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 3;
DE   AltName: Full=Kappa-B and V(D)J recombination signal sequences-binding protein;
DE   AltName: Full=Kappa-binding protein 1;
DE            Short=KBP-1;
DE   AltName: Full=Zinc finger protein ZAS3;
GN   Name=HIVEP3; Synonyms=KBP1, KIAA1555, KRC, ZAS3;
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), FUNCTION, ALTERNATIVE SPLICING,
RP   DOMAIN, AND VARIANTS ARG-575; PRO-2023; ALA-2109; ARG-2272 AND ALA-2339.
RC   TISSUE=Brain;
RX   PubMed=11161801; DOI=10.1006/geno.2000.6425;
RA   Hicar M.D., Liu Y., Allen C.E., Wu L.-C.;
RT   "Structure of the human zinc finger protein HIVEP3: molecular cloning,
RT   expression, exon-intron structure, and comparison with paralogous genes
RT   HIVEP1 and HIVEP2.";
RL   Genomics 71:89-100(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-575;
RP   PRO-2023; ALA-2109 AND ALA-2339.
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
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 MRNA] (ISOFORM 2), AND VARIANTS ARG-575;
RP   PRO-2023; ALA-2109 AND ALA-2339.
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   [6]
RP   VARIANT [LARGE SCALE ANALYSIS] MET-484.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [7]
RP   VARIANT LEU-2348.
RX   PubMed=34750991; DOI=10.15252/emmm.202114397;
RA   Vidali S., Gerlini R., Thompson K., Urquhart J.E., Meisterknecht J.,
RA   Aguilar-Pimentel J.A., Amarie O.V., Becker L., Breen C., Calzada-Wack J.,
RA   Chhabra N.F., Cho Y.L., da Silva-Buttkus P., Feichtinger R.G., Gampe K.,
RA   Garrett L., Hoefig K.P., Hoelter S.M., Jameson E., Klein-Rodewald T.,
RA   Leuchtenberger S., Marschall S., Mayer-Kuckuk P., Miller G.,
RA   Oestereicher M.A., Pfannes K., Rathkolb B., Rozman J., Sanders C.,
RA   Spielmann N., Stoeger C., Szibor M., Treise I., Walter J.H., Wurst W.,
RA   Mayr J.A., Fuchs H., Gaertner U., Wittig I., Taylor R.W., Newman W.G.,
RA   Prokisch H., Gailus-Durner V., Hrabe de Angelis M.;
RT   "Characterising a homozygous two-exon deletion in UQCRH: comparing human
RT   and mouse phenotypes.";
RL   EMBO Mol. Med. 13:e14397-e14397(2021).
CC   -!- FUNCTION: Plays a role of transcription factor; binds to recognition
CC       signal sequences (Rss heptamer) for somatic recombination of
CC       immunoglobulin and T-cell receptor gene segments; Binds also to the
CC       kappa-B motif of gene such as S100A4, involved in cell progression and
CC       differentiation. Kappa-B motif is a gene regulatory element found in
CC       promoters and enhancers of genes involved in immunity, inflammation,
CC       and growth and that responds to viral antigens, mitogens, and
CC       cytokines. Involvement of HIVEP3 in cell growth is strengthened by the
CC       fact that its down-regulation promotes cell cycle progression with
CC       ultimate formation of multinucleated giant cells. Strongly inhibits
CC       TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor
CC       NF-kappa-B by several mechanisms: as transcription factor, by competing
CC       for Kappa-B motif and by repressing transcription in the nucleus;
CC       through a non transcriptional process, by inhibiting nuclear
CC       translocation of RELA by association with TRAF2, an adapter molecule in
CC       the tumor necrosis factor signaling, which blocks the formation of IKK
CC       complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-
CC       mediated and c-Jun N-terminal kinase/JNK-mediated responses that
CC       include apoptosis and pro-inflammatory cytokine gene expression.
CC       Positively regulates the expression of IL2 in T-cell. Essential
CC       regulator of adult bone formation. {ECO:0000269|PubMed:11161801}.
CC   -!- SUBUNIT: Interacts with TRAF1 and TRAF2 as well as with JUN. Forms a
CC       multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q5T1R4; P31947: SFN; NbExp=5; IntAct=EBI-28989979, EBI-476295;
CC       Q5T1R4; P61981: YWHAG; NbExp=2; IntAct=EBI-28989979, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms can be generated by alternative splicing
CC         or polyadenylation. HIVEP3L transcript may lack exon 7 leading to a
CC         premature codon stop. {ECO:0000269|PubMed:11161801};
CC       Name=1; Synonyms=HIVEP3S;
CC         IsoId=Q5T1R4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5T1R4-2; Sequence=VSP_033279;
CC   -!- INDUCTION: By 12-O-tetradecanoylphorbol-13 acetate (TPA).
CC   -!- DOMAIN: The ZAS2 domain binds DNA as dimers, tetramers, and multiple of
CC       tetramers and readily forms highly ordered DNA-protein structures.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on threonine and serine residues. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB13381.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF278765; AAK01082.1; -; mRNA.
DR   EMBL; AB046775; BAB13381.2; ALT_INIT; mRNA.
DR   EMBL; AL445933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC152563; AAI52564.1; -; mRNA.
DR   CCDS; CCDS44124.1; -. [Q5T1R4-2]
DR   CCDS; CCDS463.1; -. [Q5T1R4-1]
DR   RefSeq; NP_001121186.1; NM_001127714.2. [Q5T1R4-2]
DR   RefSeq; NP_078779.2; NM_024503.4. [Q5T1R4-1]
DR   RefSeq; XP_011540186.1; XM_011541884.2.
DR   RefSeq; XP_016857481.1; XM_017001992.1.
DR   RefSeq; XP_016857482.1; XM_017001993.1.
DR   RefSeq; XP_016857483.1; XM_017001994.1.
DR   AlphaFoldDB; Q5T1R4; -.
DR   SMR; Q5T1R4; -.
DR   BioGRID; 121861; 15.
DR   CORUM; Q5T1R4; -.
DR   IntAct; Q5T1R4; 8.
DR   MINT; Q5T1R4; -.
DR   STRING; 9606.ENSP00000361664; -.
DR   GlyCosmos; Q5T1R4; 7 sites, 1 glycan.
DR   GlyGen; Q5T1R4; 23 sites, 1 O-linked glycan (23 sites).
DR   iPTMnet; Q5T1R4; -.
DR   PhosphoSitePlus; Q5T1R4; -.
DR   BioMuta; HIVEP3; -.
DR   DMDM; 74756245; -.
DR   EPD; Q5T1R4; -.
DR   jPOST; Q5T1R4; -.
DR   MassIVE; Q5T1R4; -.
DR   MaxQB; Q5T1R4; -.
DR   PaxDb; 9606-ENSP00000361664; -.
DR   PeptideAtlas; Q5T1R4; -.
DR   ProteomicsDB; 64282; -. [Q5T1R4-1]
DR   ProteomicsDB; 64283; -. [Q5T1R4-2]
DR   Antibodypedia; 32189; 42 antibodies from 9 providers.
DR   DNASU; 59269; -.
DR   Ensembl; ENST00000372583.6; ENSP00000361664.1; ENSG00000127124.16. [Q5T1R4-1]
DR   Ensembl; ENST00000372584.5; ENSP00000361665.1; ENSG00000127124.16. [Q5T1R4-2]
DR   Ensembl; ENST00000643665.1; ENSP00000494598.1; ENSG00000127124.16. [Q5T1R4-2]
DR   GeneID; 59269; -.
DR   KEGG; hsa:59269; -.
DR   MANE-Select; ENST00000372583.6; ENSP00000361664.1; NM_024503.5; NP_078779.2.
DR   UCSC; uc001cgz.5; human. [Q5T1R4-1]
DR   AGR; HGNC:13561; -.
DR   CTD; 59269; -.
DR   DisGeNET; 59269; -.
DR   GeneCards; HIVEP3; -.
DR   HGNC; HGNC:13561; HIVEP3.
DR   HPA; ENSG00000127124; Tissue enhanced (lymphoid).
DR   MIM; 606649; gene.
DR   neXtProt; NX_Q5T1R4; -.
DR   OpenTargets; ENSG00000127124; -.
DR   PharmGKB; PA29299; -.
DR   VEuPathDB; HostDB:ENSG00000127124; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000157218; -.
DR   HOGENOM; CLU_000719_1_0_1; -.
DR   InParanoid; Q5T1R4; -.
DR   OMA; EDRGPPN; -.
DR   OrthoDB; 3353821at2759; -.
DR   PhylomeDB; Q5T1R4; -.
DR   TreeFam; TF331837; -.
DR   PathwayCommons; Q5T1R4; -.
DR   Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR   SignaLink; Q5T1R4; -.
DR   BioGRID-ORCS; 59269; 24 hits in 1171 CRISPR screens.
DR   ChiTaRS; HIVEP3; human.
DR   GeneWiki; HIVEP3; -.
DR   GenomeRNAi; 59269; -.
DR   Pharos; Q5T1R4; Tbio.
DR   PRO; PR:Q5T1R4; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5T1R4; Protein.
DR   Bgee; ENSG00000127124; Expressed in buccal mucosa cell and 155 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR   InterPro; IPR034729; ZF_CCHC_HIVEP.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45944; SCHNURRI, ISOFORM F; 1.
DR   PANTHER; PTHR45944:SF5; TRANSCRIPTION FACTOR HIVEP3; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
DR   Genevisible; Q5T1R4; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..2406
FT                   /note="Transcription factor HIVEP3"
FT                   /id="PRO_0000331627"
FT   REPEAT          1964..1967
FT                   /note="1"
FT   REPEAT          1970..1973
FT                   /note="2"
FT   REPEAT          1993..1996
FT                   /note="3"
FT   REPEAT          1998..2001
FT                   /note="4"
FT   REPEAT          2067..2070
FT                   /note="5"
FT   REPEAT          2079..2082
FT                   /note="6"
FT   ZN_FING         192..214
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         220..242
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         640..670
FT                   /note="CCHC HIVEP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01154"
FT   ZN_FING         1754..1776
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1782..1806
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..242
FT                   /note="ZAS1"
FT   REGION          211..1074
FT                   /note="No DNA binding activity or transactivation activity,
FT                   but complete prevention of TRAF-dependent NF-Kappa-B
FT                   activation; associates with TRAF2 and JUN"
FT                   /evidence="ECO:0000250"
FT   REGION          264..287
FT                   /note="Acidic 1"
FT   REGION          272..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..1115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..883
FT                   /note="Acidic 2"
FT   REGION          1268..1303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1406..1459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1472..1594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1692..1727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1754..1806
FT                   /note="ZAS2"
FT   REGION          1817..1872
FT                   /note="Acidic 3"
FT   REGION          1818..2033
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2052..2113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2053..2148
FT                   /note="6 X 4 AA tandem repeats of S-P-X-[RK]"
FT   REGION          2125..2151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2224..2406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1442..1466
FT                   /evidence="ECO:0000255"
FT   MOTIF           903..909
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..730
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..884
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..946
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1019
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1094
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1268..1283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1406..1430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1445..1459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1476..1490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1494..1508
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1569..1594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1700..1724
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1829..1848
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1849..1873
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1910..1937
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1986..2002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2129..2149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2244..2262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2304..2318
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         2136
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10997877,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033279"
FT   VARIANT         35
FT                   /note="V -> I (in dbSNP:rs2146315)"
FT                   /id="VAR_042910"
FT   VARIANT         484
FT                   /note="V -> M (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs780211835)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_042911"
FT   VARIANT         575
FT                   /note="H -> R (in dbSNP:rs2810566)"
FT                   /evidence="ECO:0000269|PubMed:10997877,
FT                   ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_042912"
FT   VARIANT         1087
FT                   /note="Q -> H (in dbSNP:rs17363472)"
FT                   /id="VAR_042913"
FT   VARIANT         2023
FT                   /note="A -> P (in dbSNP:rs2483689)"
FT                   /evidence="ECO:0000269|PubMed:10997877,
FT                   ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_042914"
FT   VARIANT         2109
FT                   /note="D -> A (in dbSNP:rs2991344)"
FT                   /evidence="ECO:0000269|PubMed:10997877,
FT                   ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_042915"
FT   VARIANT         2272
FT                   /note="G -> R (in dbSNP:rs11809423)"
FT                   /evidence="ECO:0000269|PubMed:11161801"
FT                   /id="VAR_042916"
FT   VARIANT         2339
FT                   /note="T -> A (in dbSNP:rs9439043)"
FT                   /evidence="ECO:0000269|PubMed:10997877,
FT                   ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_042917"
FT   VARIANT         2348
FT                   /note="P -> L"
FT                   /evidence="ECO:0000269|PubMed:34750991"
FT                   /id="VAR_087891"
FT   CONFLICT        44
FT                   /note="A -> P (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94..95
FT                   /note="QL -> HV (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="D -> S (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="P -> L (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133..134
FT                   /note="FV -> LL (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        589
FT                   /note="R -> P (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        901
FT                   /note="L -> A (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        961
FT                   /note="S -> D (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1034..1035
FT                   /note="RV -> GE (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1048..1049
FT                   /note="QA -> SP (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1110
FT                   /note="P -> A (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1180
FT                   /note="P -> L (in Ref. 2; BAB13381 and 5; AAI52564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1279
FT                   /note="T -> Q (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1524
FT                   /note="T -> Q (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2376
FT                   /note="P -> S (in Ref. 1; AAK01082)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2406 AA;  259465 MW;  AFCCFDAF87014A7D CRC64;
     MDPEQSVKGT KKAEGSPRKR LTKGEAIQTS VSSSVPYPGS GTAATQESPA QELLAPQPFP
     GPSSVLREGS QEKTGQQQKP PKRPPIEASV HISQLPQHPL TPAFMSPGKP EHLLEGSTWQ
     LVDPMRPGPS GSFVAPGLHP QSQLLPSHAS IIPPEDLPGV PKVFVPRPSQ VSLKPTEEAH
     KKERKPQKPG KYICQYCSRP CAKPSVLQKH IRSHTGERPY PCGPCGFSFK TKSNLYKHRK
     SHAHRIKAGL ASGMGGEMYP HGLEMERIPG EEFEEPTEGE STDSEEETSA TSGHPAELSP
     RPKQPLLSSG LYSSGSHSSS HERCSLSQSS TAQSLEDPPP FVEPSSEHPL SHKPEDTHTI
     KQKLALRLSE RKKVIDEQAF LSPGSKGSTE SGYFSRSESA EQQVSPPNTN AKSYAEIIFG
     KCGRIGQRTA MLTATSTQPL LPLSTEDKPS LVPLSVPRTQ VIEHITKLIT INEAVVDTSE
     IDSVKPRRSS LSRRSSMESP KSSLYREPLS SHSEKTKPEQ SLLSLQHPPS TAPPVPLLRS
     HSMPSAACTI STPHHPFRGS YSFDDHITDS EALSHSSHVF TSHPRMLKRQ PAIELPLGGE
     YSSEEPGPSS KDTASKPSDE VEPKESELTK KTKKGLKTKG VIYECNICGA RYKKRDNYEA
     HKKYYCSELQ IAKPISAGTH TSPEAEKSQI EHEPWSQMMH YKLGTTLELT PLRKRRKEKS
     LGDEEEPPAF ESTKSQFGSP GPSDAARNLP LESTKSPAEP SKSVPSLEGP TGFQPRTPKP
     GSGSESGKER RTTSKEISVI QHTSSFEKSD SLEQPSGLEG EDKPLAQFPS PPPAPHGRSA
     HSLQPKLVRQ PNIQVPEILV TEEPDRPDTE PEPPPKEPEK TEEFQWPQRS QTLAQLPAEK
     LPPKKKRLRL AEMAQSSGES SFESSVPLSR SPSQESNVSL SGSSRSASFE RDDHGKAEAP
     SPSSDMRPKP LGTHMLTVPS HHPHAREMRR SASEQSPNVS HSAHMTETRS KSFDYGSLSL
     TGPSAPAPVA PPARVAPPER RKCFLVRQAS LSRPPESELE VAPKGRQESE EPQPSSSKPS
     AKSSLSQISS AATSHGGPPG GKGPGQDRPP LGPTVPYTEA LQVFHHPVAQ TPLHEKPYLP
     PPVSLFSFQH LVQHEPGQSP EFFSTQAMSS LLSSPYSMPP LPPSLFQAPP LPLQPTVLHP
     GQLHLPQLMP HPANIPFRQP PSFLPMPYPT SSALSSGFFL PLQSQFALQL PGDVESHLPQ
     IKTSLAPLAT GSAGLSPSTE YSSDIRLPPV APPASSSAPT SAPPLALPAC PDTMVSLVVP
     VRVQTNMPSY GSAMYTTLSQ ILVTQSQGSS ATVALPKFEE PPSKGTTVCG ADVHEVGPGP
     SGLSEEQSRA FPTPYLRVPV TLPERKGTSL SSESILSLEG SSSTAGGSKR VLSPAGSLEL
     TMETQQQKRV KEEEASKADE KLELVKPCSV VLTSTEDGKR PEKSHLGNQG QGRRELEMLS
     SLSSDPSDTK EIPPLPHPAL SHGTAPGSEA LKEYPQPSGK PHRRGLTPLS VKKEDSKEQP
     DLPSLAPPSS LPLSETSSRP AKSQEGTDSK KVLQFPSLHT TTNVSWCYLN YIKPNHIQHA
     DRRSSVYAGW CISLYNPNLP GVSTKAALSL LRSKQKVSKE TYTMATAPHP EAGRLVPSSS
     RKPRMTEVHL PSLVSPEGQK DLARVEKEEE RRGEPEEDAP ASQRGEPARI KIFEGGYKSN
     EEYVYVRGRG RGKYVCEECG IRCKKPSMLK KHIRTHTDVR PYVCKHCHFA FKTKGNLTKH
     MKSKAHSKKC QETGVLEELE AEEGTSDDLF QDSEGREGSE AVEEHQFSDL EDSDSDSDLD
     EDEDEDEEES QDELSRPSSE APPPGPPHAL RADSSPILGP QPPDAPASGT EATRGSSVSE
     AERLTASSCS MSSQSMPGLP WLGPAPLGSV EKDTGSALSY KPVSPRRPWS PSKEAGSRPP
     LARKHSLTKN DSSPQRCSPA REPQASAPSP PGLHVDPGRG MGALPCGSPR LQLSPLTLCP
     LGRELAPRAH VLSKLEGTTD PGLPRYSPTR RWSPGQAESP PRSAPPGKWA LAGPGSPSAG
     EHGPGLGLDP RVLFPPAPLP HKLLSRSPET CASPWQKAES RSPSCSPGPA HPLSSRPFSA
     LHDFHGHILA RTEENIFSHL PLHSQHLTRA PCPLIPIGGI QMVQARPGAH PTLLPGPTAA
     WVSGFSGGGS DLTGAREAQE RGRWSPTESS SASVSPVAKV SKFTLSSELE GGDYPKERER
     TGGGPGRPPD WTPHGTGAPA EPTPTHSPCT PPDTLPRPPQ GRRAAQSWSP RLESPRAPTN
     PEPSATPPLD RSSSVGCLAE ASARFPARTR NLSGEPRTRQ DSPKPSGSGE PRAHPHQPED
     RVPPNA
//