ID   TAF2_HUMAN              Reviewed;        1199 AA.
AC   Q6P1X5; B2RE82; O43487; O43604; O60668; Q86WW7; Q8IWK4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 3.
DT   02-DEC-2020, entry version 140.
DE   RecName: Full=Transcription initiation factor TFIID subunit 2;
DE   AltName: Full=150 kDa cofactor of initiator function;
DE   AltName: Full=RNA polymerase II TBP-associated factor subunit B;
DE   AltName: Full=TBP-associated factor 150 kDa;
DE   AltName: Full=Transcription initiation factor TFIID 150 kDa subunit;
DE            Short=TAF(II)150;
DE            Short=TAFII-150;
DE            Short=TAFII150;
GN   Name=TAF2; Synonyms=CIF150, TAF2B;
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], VARIANT THR-447, FUNCTION, AND INTERACTION WITH
RP   TAF2C1.
RX   PubMed=9418870; DOI=10.1128/mcb.18.1.233;
RA   Kaufmann J., Ahrens K., Koop R., Smale S.T., Muller R.;
RT   "CIF150, a human cofactor for transcription factor IID-dependent initiator
RT   function.";
RL   Mol. Cell. Biol. 18:233-239(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-447, FUNCTION, SUBCELLULAR
RP   LOCATION, IDENTIFICATION IN THE TFIID COMPLEX, AND TISSUE SPECIFICITY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=9774672; DOI=10.1128/mcb.18.11.6571;
RA   Martinez E., Ge H., Tao Y., Yuan C.-X., Palhan V., Roeder R.G.;
RT   "Novel cofactors and TFIIA mediate functional core promoter selectivity by
RT   the human TAFII150-containing TFIID complex.";
RL   Mol. Cell. Biol. 18:6571-6583(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-447.
RC   TISSUE=Cervix carcinoma;
RA   Guermah M., Roeder R.G.R.;
RT   "Human TBP-associated factor (TAFII150).";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-604, AND VARIANT THR-447.
RC   TISSUE=Duodenum, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=12601814; DOI=10.1002/pmic.200390030;
RA   Cavusoglu N., Brand M., Tora L., van Dorsselaer A.;
RT   "Novel subunits of the TATA binding protein free TAFII-containing
RT   transcription complex identified by matrix-assisted laser
RT   desorption/ionization-time of flight mass spectrometry following one-
RT   dimensional gel electrophoresis.";
RL   Proteomics 3:217-223(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194; SER-1196 AND SER-1198,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185 AND SER-1188, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185 AND SER-1188, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   VARIANT MRT40 ARG-649.
RX   PubMed=21937992; DOI=10.1038/nature10423;
RA   Najmabadi H., Hu H., Garshasbi M., Zemojtel T., Abedini S.S., Chen W.,
RA   Hosseini M., Behjati F., Haas S., Jamali P., Zecha A., Mohseni M.,
RA   Puettmann L., Vahid L.N., Jensen C., Moheb L.A., Bienek M., Larti F.,
RA   Mueller I., Weissmann R., Darvish H., Wrogemann K., Hadavi V.,
RA   Lipkowitz B., Esmaeeli-Nieh S., Wieczorek D., Kariminejad R.,
RA   Firouzabadi S.G., Cohen M., Fattahi Z., Rost I., Mojahedi F., Hertzberg C.,
RA   Dehghan A., Rajab A., Banavandi M.J., Hoffer J., Falah M., Musante L.,
RA   Kalscheuer V., Ullmann R., Kuss A.W., Tzschach A., Kahrizi K., Ropers H.H.;
RT   "Deep sequencing reveals 50 novel genes for recessive cognitive
RT   disorders.";
RL   Nature 478:57-63(2011).
RN   [12]
RP   VARIANTS MRT40 ARG-186 AND HIS-416.
RX   PubMed=24084144; DOI=10.1016/j.pediatrneurol.2013.07.017;
RA   Hellman-Aharony S., Smirin-Yosef P., Halevy A., Pasmanik-Chor M.,
RA   Yeheskel A., Har-Zahav A., Maya I., Straussberg R., Dahary D., Haviv A.,
RA   Shohat M., Basel-Vanagaite L.;
RT   "Microcephaly thin corpus callosum intellectual disability syndrome caused
RT   by mutated TAF2.";
RL   Pediatr. Neurol. 49:411-417(2013).
CC   -!- FUNCTION: Transcription factor TFIID is one of the general factors
CC       required for accurate and regulated initiation by RNA polymerase II.
CC       TFIID is a multimeric protein complex that plays a central role in
CC       mediating promoter responses to various activators and repressors. It
CC       requires core promoter-specific cofactors for productive transcription
CC       stimulation. TAF2 stabilizes TFIID binding to core promoter.
CC       {ECO:0000269|PubMed:9418870, ECO:0000269|PubMed:9774672}.
CC   -!- SUBUNIT: Component of transcription factor TFIID which is composed of
CC       TBP and a number of TBP-associated factors. Interacts with TAF2C1.
CC       Component of the TFTC-HAT complex. {ECO:0000269|PubMed:12601814,
CC       ECO:0000269|PubMed:9418870, ECO:0000269|PubMed:9774672}.
CC   -!- INTERACTION:
CC       Q6P1X5; Q9UHX1-2: PUF60; NbExp=3; IntAct=EBI-1560063, EBI-11529177;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9774672}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested.
CC       {ECO:0000269|PubMed:9774672}.
CC   -!- DISEASE: Mental retardation, autosomal recessive 40 (MRT40)
CC       [MIM:615599]: A disorder characterized by significantly below average
CC       general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period. MRT40
CC       affected individuals also show microcephaly, spasticity, thin corpus
CC       callosum, pyramidal signs. {ECO:0000269|PubMed:21937992,
CC       ECO:0000269|PubMed:24084144}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: PubMed:9418870 was unable to show an association between
CC       TAF2 and TFIID.
CC   -!- SIMILARITY: Belongs to the TAF2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC68502.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH64830.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF026445; AAC02966.1; -; mRNA.
DR   EMBL; AF040701; AAC68502.1; ALT_INIT; mRNA.
DR   EMBL; AF057694; AAC13540.1; -; mRNA.
DR   EMBL; AK316592; BAG38179.1; -; mRNA.
DR   EMBL; AC107960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC021945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC035673; AAH35673.1; -; mRNA.
DR   EMBL; BC047732; AAH47732.1; -; mRNA.
DR   EMBL; BC064830; AAH64830.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS34937.1; -.
DR   RefSeq; NP_003175.1; NM_003184.3.
DR   PDB; 5FUR; EM; 8.50 A; I=1-1199.
DR   PDB; 6MZC; EM; 4.50 A; B=1-1199.
DR   PDB; 6MZL; EM; 23.00 A; B=1-1199.
DR   PDB; 6MZM; EM; 7.50 A; B=1-1199.
DR   PDBsum; 5FUR; -.
DR   PDBsum; 6MZC; -.
DR   PDBsum; 6MZL; -.
DR   PDBsum; 6MZM; -.
DR   SMR; Q6P1X5; -.
DR   BioGRID; 112736; 94.
DR   ComplexPortal; CPX-900; SAGA complex.
DR   ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR   ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR   ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
DR   CORUM; Q6P1X5; -.
DR   DIP; DIP-38921N; -.
DR   IntAct; Q6P1X5; 18.
DR   STRING; 9606.ENSP00000367406; -.
DR   MEROPS; M01.972; -.
DR   iPTMnet; Q6P1X5; -.
DR   PhosphoSitePlus; Q6P1X5; -.
DR   BioMuta; TAF2; -.
DR   DMDM; 145559533; -.
DR   EPD; Q6P1X5; -.
DR   jPOST; Q6P1X5; -.
DR   MassIVE; Q6P1X5; -.
DR   MaxQB; Q6P1X5; -.
DR   PaxDb; Q6P1X5; -.
DR   PeptideAtlas; Q6P1X5; -.
DR   PRIDE; Q6P1X5; -.
DR   ProteomicsDB; 66877; -.
DR   Antibodypedia; 26803; 153 antibodies.
DR   DNASU; 6873; -.
DR   Ensembl; ENST00000378164; ENSP00000367406; ENSG00000064313.
DR   GeneID; 6873; -.
DR   KEGG; hsa:6873; -.
DR   UCSC; uc003you.4; human.
DR   CTD; 6873; -.
DR   DisGeNET; 6873; -.
DR   EuPathDB; HostDB:ENSG00000064313.11; -.
DR   GeneCards; TAF2; -.
DR   HGNC; HGNC:11536; TAF2.
DR   HPA; ENSG00000064313; Low tissue specificity.
DR   MalaCards; TAF2; -.
DR   MIM; 604912; gene.
DR   MIM; 615599; phenotype.
DR   neXtProt; NX_Q6P1X5; -.
DR   OpenTargets; ENSG00000064313; -.
DR   Orphanet; 397951; Microcephaly-thin corpus callosum-intellectual disability syndrome.
DR   PharmGKB; PA36311; -.
DR   eggNOG; KOG1932; Eukaryota.
DR   GeneTree; ENSGT00390000000420; -.
DR   HOGENOM; CLU_002317_0_0_1; -.
DR   InParanoid; Q6P1X5; -.
DR   OMA; SHGICPP; -.
DR   OrthoDB; 142542at2759; -.
DR   PhylomeDB; Q6P1X5; -.
DR   TreeFam; TF315208; -.
DR   PathwayCommons; Q6P1X5; -.
DR   Reactome; R-HSA-167161; HIV Transcription Initiation.
DR   Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR   Reactome; R-HSA-167172; Transcription of the HIV genome.
DR   Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   BioGRID-ORCS; 6873; 505 hits in 844 CRISPR screens.
DR   ChiTaRS; TAF2; human.
DR   GeneWiki; TAF2; -.
DR   GenomeRNAi; 6873; -.
DR   Pharos; Q6P1X5; Tbio.
DR   PRO; PR:Q6P1X5; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q6P1X5; protein.
DR   Bgee; ENSG00000064313; Expressed in forebrain and 238 other tissues.
DR   ExpressionAtlas; Q6P1X5; baseline and differential.
DR   Genevisible; Q6P1X5; HS.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR   GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:ARUK-UCL.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR037813; TAF2.
DR   PANTHER; PTHR15137; PTHR15137; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF63737; SSF63737; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disease mutation; Mental retardation; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1199
FT                   /note="Transcription initiation factor TFIID subunit 2"
FT                   /id="PRO_0000252424"
FT   COMPBIAS        600..603
FT                   /note="Poly-Lys"
FT   COMPBIAS        1143..1171
FT                   /note="His-rich"
FT   COMPBIAS        1155..1178
FT                   /note="Lys-rich"
FT   MOD_RES         1185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         1196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         1198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   VARIANT         8
FT                   /note="P -> L (in dbSNP:rs17818842)"
FT                   /id="VAR_027854"
FT   VARIANT         186
FT                   /note="T -> R (in MRT40; unknown pathological significance;
FT                   dbSNP:rs398124656)"
FT                   /evidence="ECO:0000269|PubMed:24084144"
FT                   /id="VAR_070945"
FT   VARIANT         416
FT                   /note="P -> H (in MRT40; unknown pathological significance;
FT                   dbSNP:rs398124655)"
FT                   /evidence="ECO:0000269|PubMed:24084144"
FT                   /id="VAR_070946"
FT   VARIANT         447
FT                   /note="S -> T (in dbSNP:rs9297605)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9418870, ECO:0000269|PubMed:9774672,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_027855"
FT   VARIANT         649
FT                   /note="W -> R (in MRT40; dbSNP:rs398124645)"
FT                   /id="VAR_070947"
FT   VARIANT         686
FT                   /note="E -> K (in dbSNP:rs34154779)"
FT                   /id="VAR_057263"
FT   VARIANT         1122
FT                   /note="S -> N (in dbSNP:rs956749)"
FT                   /id="VAR_027856"
FT   VARIANT         1139
FT                   /note="T -> A (in dbSNP:rs956748)"
FT                   /id="VAR_027857"
FT   CONFLICT        1
FT                   /note="M -> R (in Ref. 2; AAC68502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="Q -> H (in Ref. 1; AAC02966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="P -> L (in Ref. 6; AAH47732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="G -> C (in Ref. 6; AAH64830)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        604
FT                   /note="I -> K (in Ref. 6; AAH35673/AAH47732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        785
FT                   /note="R -> G (in Ref. 2; AAC68502)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1199 AA;  136971 MW;  169DA4A3878CFD59 CRC64;
     MPLTGVEPAR MNRKKGDKGF ESPRPYKLTH QVVCINNINF QRKSVVGFVE LTIFPTVANL
     NRIKLNSKQC RIYRVRINDL EAAFIYNDPT LEVCHSESKQ RNLNYFSNAY AAAVSAVDPD
     AGNGELCIKV PSELWKHVDE LKVLKIHINF SLDQPKGGLH FVVPSVEGSM AERGAHVFSC
     GYQNSTRFWF PCVDSYSELC TWKLEFTVDA AMVAVSNGDL VETVYTHDMR KKTFHYMLTI
     PTAASNISLA IGPFEILVDP YMHEVTHFCL PQLLPLLKHT TSYLHEVFEF YEEILTCRYP
     YSCFKTVFID EAYVEVAAYA SMSIFSTNLL HSAMIIDETP LTRRCLAQSL AQQFFGCFIS
     RMSWSDEWVL KGISGYIYGL WMKKTFGVNE YRHWIKEELD KIVAYELKTG GVLLHPIFGG
     GKEKDNPASH LHFSIKHPHT LSWEYYSMFQ CKAHLVMRLI ENRISMEFML QVFNKLLSLA
     STASSQKFQS HMWSQMLVST SGFLKSISNV SGKDIQPLIK QWVDQSGVVK FYGSFAFNRK
     RNVLELEIKQ DYTSPGTQKY VGPLKVTVQE LDGSFNHTLQ IEENSLKHDI PCHSKSRRNK
     KKKIPLMNGE EVDMDLSAMD ADSPLLWIRI DPDMSVLRKV EFEQADFMWQ YQLRYERDVV
     AQQESILALE KFPTPASRLA LTDILEQEQC FYRVRMSACF CLAKIANSMV STWTGPPAMK
     SLFTRMFCCK SCPNIVKTNN FMSFQSYFLQ KTMPVAMALL RDVHNLCPKE VLTFILDLIK
     YNDNRKNKFS DNYYRAEMID ALANSVTPAV SVNNEVRTLD NLNPDVRLIL EEITRFLNME
     KLLPSYRHTI TVSCLRAIRV LQKNGHVPSD PALFKSYAEY GHFVDIRIAA LEAVVDYTKV
     DRSYEELQWL LNMIQNDPVP YVRHKILNML TKNPPFTKNM ESPLCNEALV DQLWKLMNSG
     TSHDWRLRCG AVDLYFTLFG LSRPSCLPLP ELGLVLNLKE KKAVLNPTII PESVAGNQEA
     ANNPSSHPQL VGFQNPFSSS QDEEEIDMDT VHDSQAFISH HLNMLERPST PGLSKYRPAS
     SRSALIPQHS AGCDSTPTTK PQWSLELARK GTGKEQAPLE MSMHPAASAP LSVFTKESTA
     SKHSDHHHHH HHEHKKKKKK HKHKHKHKHK HDSKEKDKEP FTFSSPASGR SIRSPSLSD
//