ID   ZEP2_HUMAN              Reviewed;        2446 AA.
AC   P31629; Q02646; Q5THT5; Q9NS05;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Transcription factor HIVEP2;
DE   AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 2;
DE            Short=HIV-EP2;
DE   AltName: Full=MHC-binding protein 2;
DE            Short=MBP-2;
GN   Name=HIVEP2;
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 [GENOMIC DNA], AND VARIANT PRO-1538.
RX   PubMed=2022670; DOI=10.1016/s0021-9258(18)93015-2;
RA   Nomura N., Zhao M.-J., Nagase T., Maekawa T., Ishizaki R., Tabata S.,
RA   Ishii S.;
RT   "HIV-EP2, a new member of the gene family encoding the human
RT   immunodeficiency virus type 1 enhancer-binding protein. Comparison with
RT   HIV-EP1/PRDII-BF1/MBP-1.";
RL   J. Biol. Chem. 266:8590-8594(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-1538.
RX   PubMed=1409593; DOI=10.1073/pnas.89.19.8971;
RA   Van't Veer L.J., Lutz P., Isselbacher K.J., Bernards R.;
RT   "Structure and expression of MBP-2: a 275 kDa zinc finger protein that
RT   binds to an enhancer of major histocompatibility complex class 1 genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8971-8975(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-1538.
RA   Kukita Y., Komiya T., Tahira T., Asakawa S., Shimizu N., Suzuki Y.,
RA   Sugano S., Hayashi K.;
RT   "Characterization of the human MBP-2/HIV-EP2 gene: identification of
RT   multiple promoters and alternative splicing of 5' untranslated region.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1797-1936.
RX   PubMed=2247438; DOI=10.1073/pnas.87.22.8707;
RA   Rustgi A.K., Van't Veer L.J., Bernards R.;
RT   "Two genes encode factors with NF-kappa B- and H2TF1-like DNA-binding
RT   properties.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8707-8710(1990).
RN   [6]
RP   TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10207097; DOI=10.1128/mcb.19.5.3736;
RA   Doerflinger U., Pscherer A., Moser M., Ruemmele P., Schuele R.,
RA   Buettner R.;
RT   "Activation of somatostatin receptor II expression by transcription factors
RT   MIBP1 and SEF-2 in the murine brain.";
RL   Mol. Cell. Biol. 19:3736-3747(1999).
RN   [7]
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   [8]
RP   INVOLVEMENT IN MRD43.
RX   PubMed=23020937; DOI=10.1016/s0140-6736(12)61480-9;
RA   Rauch A., Wieczorek D., Graf E., Wieland T., Endele S., Schwarzmayr T.,
RA   Albrecht B., Bartholdi D., Beygo J., Di Donato N., Dufke A., Cremer K.,
RA   Hempel M., Horn D., Hoyer J., Joset P., Roepke A., Moog U., Riess A.,
RA   Thiel C.T., Tzschach A., Wiesener A., Wohlleber E., Zweier C., Ekici A.B.,
RA   Zink A.M., Rump A., Meisinger C., Grallert H., Sticht H., Schenck A.,
RA   Engels H., Rappold G., Schroeck E., Wieacker P., Riess O., Meitinger T.,
RA   Reis A., Strom T.M.;
RT   "Range of genetic mutations associated with severe non-syndromic sporadic
RT   intellectual disability: an exome sequencing study.";
RL   Lancet 380:1674-1682(2012).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2118; SER-2297 AND SER-2301,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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).
RN   [11]
RP   INVOLVEMENT IN MRD43.
RX   PubMed=26153216; DOI=10.1038/ejhg.2015.151;
RA   Srivastava S., Engels H., Schanze I., Cremer K., Wieland T., Menzel M.,
RA   Schubach M., Biskup S., Kreiss M., Endele S., Strom T.M., Wieczorek D.,
RA   Zenker M., Gupta S., Cohen J., Zink A.M., Naidu S.;
RT   "Loss-of-function variants in HIVEP2 are a cause of intellectual
RT   disability.";
RL   Eur. J. Hum. Genet. 24:556-561(2016).
CC   -!- FUNCTION: This protein specifically binds to the DNA sequence 5'-
CC       GGGACTTTCC-3' which is found in the enhancer elements of numerous viral
CC       promoters such as those of SV40, CMV, or HIV1. In addition, related
CC       sequences are found in the enhancer elements of a number of cellular
CC       promoters, including those of the class I MHC, interleukin-2 receptor,
CC       somatostatin receptor II, and interferon-beta genes. It may act in T-
CC       cell activation.
CC   -!- SUBUNIT: Interacts with TCF4. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P31629; P61981: YWHAG; NbExp=3; IntAct=EBI-2514157, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and skeletal muscle.
CC       {ECO:0000269|PubMed:10207097}.
CC   -!- INDUCTION: By mitogens and phorbol ester.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal dominant 43
CC       (MRD43) [MIM:616977]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period. MRD43
CC       patients manifest developmental delay, intellectual disability,
CC       hypotonia, and dysmorphic features. {ECO:0000269|PubMed:23020937,
CC       ECO:0000269|PubMed:26153216}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB88218.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA46596.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M60119; AAB88218.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X65644; CAA46596.1; ALT_INIT; mRNA.
DR   EMBL; AF153836; AAF81365.1; -; Genomic_DNA.
DR   EMBL; AL023584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M61744; AAA36202.1; -; mRNA.
DR   CCDS; CCDS43510.1; -.
DR   PIR; S26661; WMHUE2.
DR   RefSeq; NP_006725.3; NM_006734.3.
DR   RefSeq; XP_016866294.1; XM_017010805.1.
DR   AlphaFoldDB; P31629; -.
DR   BioGRID; 109344; 22.
DR   IntAct; P31629; 21.
DR   STRING; 9606.ENSP00000356576; -.
DR   ChEMBL; CHEMBL4523214; -.
DR   GlyCosmos; P31629; 23 sites, 2 glycans.
DR   GlyGen; P31629; 34 sites, 2 O-linked glycans (34 sites).
DR   iPTMnet; P31629; -.
DR   PhosphoSitePlus; P31629; -.
DR   BioMuta; HIVEP2; -.
DR   DMDM; 83305815; -.
DR   EPD; P31629; -.
DR   jPOST; P31629; -.
DR   MassIVE; P31629; -.
DR   MaxQB; P31629; -.
DR   PaxDb; 9606-ENSP00000356575; -.
DR   PeptideAtlas; P31629; -.
DR   ProteomicsDB; 54794; -.
DR   Pumba; P31629; -.
DR   Antibodypedia; 46676; 60 antibodies from 18 providers.
DR   DNASU; 3097; -.
DR   Ensembl; ENST00000012134.7; ENSP00000012134.2; ENSG00000010818.11.
DR   Ensembl; ENST00000367603.8; ENSP00000356575.2; ENSG00000010818.11.
DR   Ensembl; ENST00000367604.6; ENSP00000356576.1; ENSG00000010818.11.
DR   Ensembl; ENST00000703918.1; ENSP00000515552.1; ENSG00000010818.11.
DR   GeneID; 3097; -.
DR   KEGG; hsa:3097; -.
DR   MANE-Select; ENST00000367603.8; ENSP00000356575.2; NM_006734.4; NP_006725.3.
DR   UCSC; uc003qjd.4; human.
DR   AGR; HGNC:4921; -.
DR   CTD; 3097; -.
DR   DisGeNET; 3097; -.
DR   GeneCards; HIVEP2; -.
DR   HGNC; HGNC:4921; HIVEP2.
DR   HPA; ENSG00000010818; Low tissue specificity.
DR   MalaCards; HIVEP2; -.
DR   MIM; 143054; gene.
DR   MIM; 616977; phenotype.
DR   neXtProt; NX_P31629; -.
DR   OpenTargets; ENSG00000010818; -.
DR   Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR   PharmGKB; PA29298; -.
DR   VEuPathDB; HostDB:ENSG00000010818; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000156512; -.
DR   HOGENOM; CLU_000719_0_0_1; -.
DR   InParanoid; P31629; -.
DR   OMA; EHHGRMS; -.
DR   OrthoDB; 3353821at2759; -.
DR   PhylomeDB; P31629; -.
DR   TreeFam; TF331837; -.
DR   PathwayCommons; P31629; -.
DR   SignaLink; P31629; -.
DR   SIGNOR; P31629; -.
DR   BioGRID-ORCS; 3097; 10 hits in 1175 CRISPR screens.
DR   ChiTaRS; HIVEP2; human.
DR   GeneWiki; HIVEP2; -.
DR   GenomeRNAi; 3097; -.
DR   Pharos; P31629; Tbio.
DR   PRO; PR:P31629; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P31629; Protein.
DR   Bgee; ENSG00000010818; Expressed in tendon of biceps brachii and 215 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45944; SCHNURRI, ISOFORM F; 1.
DR   PANTHER; PTHR45944:SF1; TRANSCRIPTION FACTOR HIVEP2; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
DR   Genevisible; P31629; HS.
PE   1: Evidence at protein level;
KW   DNA-binding; Intellectual disability; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..2446
FT                   /note="Transcription factor HIVEP2"
FT                   /id="PRO_0000047371"
FT   REPEAT          2053..2056
FT                   /note="1"
FT   REPEAT          2059..2062
FT                   /note="2"
FT   REPEAT          2071..2074
FT                   /note="3"
FT   REPEAT          2083..2086
FT                   /note="4"
FT   REPEAT          2089..2092
FT                   /note="5"
FT   REPEAT          2106..2109
FT                   /note="6"
FT   REPEAT          2112..2115
FT                   /note="7"
FT   REPEAT          2118..2121
FT                   /note="8"
FT   REPEAT          2130..2133
FT                   /note="9"
FT   REPEAT          2145..2148
FT                   /note="10"
FT   ZN_FING         189..211
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         217..239
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1799..1821
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1827..1851
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1485..1603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1882..1951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2024..2129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2053..2148
FT                   /note="10 X 4 AA tandem repeats of S-P-[RGMKC]-[RK]"
FT   REGION          2242..2325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2371..2403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2423..2446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           937..943
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        30..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..919
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..950
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1505..1535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1576..1590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1900..1924
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1930..1944
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2033..2054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2067..2111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2291..2313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         819
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00900"
FT   MOD_RES         950
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT   MOD_RES         955
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT   MOD_RES         1048
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT   MOD_RES         1443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT   MOD_RES         1447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT   MOD_RES         2118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2429
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT   MOD_RES         2431
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT   VARIANT         46
FT                   /note="R -> Q (in dbSNP:rs17072013)"
FT                   /id="VAR_052754"
FT   VARIANT         1041
FT                   /note="A -> V (in dbSNP:rs34875559)"
FT                   /id="VAR_052755"
FT   VARIANT         1293
FT                   /note="L -> I (in dbSNP:rs35675714)"
FT                   /id="VAR_052756"
FT   VARIANT         1538
FT                   /note="L -> P (in dbSNP:rs109836)"
FT                   /evidence="ECO:0000269|PubMed:1409593,
FT                   ECO:0000269|PubMed:2022670, ECO:0000269|Ref.3"
FT                   /id="VAR_052757"
FT   CONFLICT        2091
FT                   /note="R -> T (in Ref. 2; CAA46596)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2446 AA;  269053 MW;  482E2C577EF9449A CRC64;
     MDTGDTALGQ KATSRSGETD KASGRWRQEQ SAVIKMSTFG SHEGQRQPQI EPEQIGNTAS
     AQLFGSGKLA SPSEVVQQVA EKQYPPHRPS PYSCQHSLSF PQHSLPQGVM HSTKPHQSLE
     GPPWLFPGPL PSVASEDLFP FPIHGHSGGY PRKKISSLNP AYSQYSQKSI EQAEEAHKKE
     HKPKKPGKYI CPYCSRACAK PSVLKKHIRS HTGERPYPCI PCGFSFKTKS NLYKHRKSHA
     HAIKAGLVPF TESAVSKLDL EAGFIDVEAE IHSDGEQSTD TDEESSLFAE ASDKMSPGPP
     IPLDIASRGG YHGSLEESLG GPMKVPILII PKSGIPLPNE SSQYIGPDML PNPSLNTKAD
     DSHTVKQKLA LRLSEKKGQD SEPSLNLLSP HSKGSTDSGY FSRSESAEQQ ISPPNTNAKS
     YEEIIFGKYC RLSPRNALSV TTTSQERAAM GRKGIMEPLP HVNTRLDVKM FEDPVSQLIP
     SKGDVDPSQT SMLKSTKFNS ESRQPQIIPS SIRNEGKLYP ANFQGSNPVL LEAPVDSSPL
     IRSNSVPTSS ATNLTIPPSL RGSHSFDERM TGSDDVFYPG TVGIPPQRML RRQAAFELPS
     VQEGHVEVEH HGRMLKGISS SSLKEKKLSP GDRVGYDYDV CRKPYKKWED SETPKQNYRD
     ISCLSSLKHG GEYFMDPVVP LQGVPSMFGT TCENRKRRKE KSVGDEEDTP MICSSIVSTP
     VGIMASDYDP KLQMQEGVRS GFAMAGHENL SHGHTERFDP CRPQLQPGSP SLVSEESPSA
     IDSDKMSDLG GRKPPGNVIS VIQHTNSLSR PNSFERSESA ELVACTQDKA PSPSETCDSE
     ISEAPVSPEW APPGDGAESG GKPSPSQQVQ QQSYHTQPRL VRQHNIQVPE IRVTEEPDKP
     EKEKEAQSKE PEKPVEEFQW PQRSETLSQL PAEKLPPKKK RLRLADMEHS SGESSFESTG
     TGLSRSPSQE SNLSHSSSFS MSFEREETSK LSALPKQDEF GKHSEFLTVP AGSYSLSVPG
     HHHQKEMRRC SSEQMPCPHP AEVPEVRSKS FDYGNLSHAP VSGAAASTVS PSRERKKCFL
     VRQASFSGSP EISQGEVGMD QSVKQEQLEH LHAGLRSGWH HGPPAVLPPL QQEDPGKQVA
     GPCPPLSSGP LHLAQPQIMH MDSQESLRNP LIQPTSYMTS KHLPEQPHLF PHQETIPFSP
     IQNALFQFQY PTVCMVHLPA QQPPWWQAHF PHPFAQHPQK SYGKPSFQTE IHSSYPLEHV
     AEHTGKKPAE YAHTKEQTYP CYSGASGLHP KNLLPKFPSD QSSKSTETPS EQVLQEDFAS
     ANAGSLQSLP GTVVPVRIQT HVPSYGSVMY TSISQILGQN SPAIVICKVD ENMTQRTLVT
     NAAMQGIGFN IAQVLGQHAG LEKYPIWKAP QTLPLGLESS IPLCLPSTSD SVATLGGSKR
     MLSPASSLEL FMETKQQKRV KEEKMYGQIV EELSAVELTN SDIKKDLSRP QKPQLVRQGC
     ASEPKDGLQS GSSSFSSLSP SSSQDYPSVS PSSREPFLPS KEMLSGSRAP LPGQKSSGPS
     ESKESSDELD IDETASDMSM SPQSSSLPAG DGQLEEEGKG HKRPVGMLVR MASAPSGNVA
     DSTLLLTDMA DFQQILQFPS LRTTTTVSWC FLNYTKPNYV QQATFKSSVY ASWCISSCNP
     NPSGLNTKTT LALLRSKQKI TAEIYTLAAM HRPGTGKLTS SSAWKQFTQM KPDASFLFGS
     KLERKLVGNI LKERGKGDIH GDKDIGSKQT EPIRIKIFEG GYKSNEDYVY VRGRGRGKYI
     CEECGIRCKK PSMLKKHIRT HTDVRPYVCK LCNFAFKTKG NLTKHMKSKA HMKKCLELGV
     SMTSVDDTET EEAENLEDLH KAAEKHSMSS ISTDHQFSDA EESDGEDGDD NDDDDEDEDD
     FDDQGDLTPK TRSRSTSPQP PRFSSLPVNV GAVPHGVPSD SSLGHSSLIS YLVTLPSIRV
     TQLMTPSDSC EDTQMTEYQR LFQSKSTDSE PDKDRLDIPS CMDEECMLPS EPSSSPRDFS
     PSSHHSSPGY DSSPCRDNSP KRYLIPKGDL SPRRHLSPRR DLSPMRHLSP RKEAALRREM
     SQRDVSPRRH LSPRRPVSPG KDITARRDLS PRRERRYMTT IRAPSPRRAL YHNPPLSMGQ
     YLQAEPIVLG PPNLRRGLPQ VPYFSLYGDQ EGAYEHPGSS LFPEGPNDYV FSHLPLHSQQ
     QVRAPIPMVP VGGIQMVHSM PPALSSLHPS PTLPLPMEGF EEKKGASGES FSKDPYVLSK
     QHEKRGPHAL QSSGPPSTPS SPRLLMKQST SEDSLNATER EQEENIQTCT KAIASLRIAT
     EEAALLGPDQ PARVQEPHQN PLGSAHVSIR HFSRPEPGQP CTSATHPDLH DGEKDNFGTS
     QTPLAHSTFY SKSCVDDKQL DFHSSKELSS STEESKDPSS EKSQLH
//