TAF1C_HUMAN
ID TAF1C_HUMAN Reviewed; 869 AA.
AC Q15572; B7Z5K5; B7Z5S4; B7Z908; B7Z9L7; Q59F67; Q8N6V3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit C;
DE AltName: Full=RNA polymerase I-specific TBP-associated factor 110 kDa;
DE Short=TAFI110;
DE AltName: Full=TATA box-binding protein-associated factor 1C;
DE Short=TBP-associated factor 1C;
DE AltName: Full=Transcription initiation factor SL1/TIF-IB subunit C;
GN Name=TAF1C;
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), PROTEIN SEQUENCE OF 55-65; 96-112;
RP 125-131; 324-337; 338-354; 553-561; 563-582 AND 646-659, INTERACTION WITH
RP TBP; TAF1A AND TAF1B, IDENTIFICATION IN THE SL1 COMPLEX, AND VARIANT
RP TYR-91.
RX PubMed=7801123; DOI=10.1126/science.7801123;
RA Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.;
RT "Reconstitution of transcription factor SL1: exclusive binding of TBP by
RT SL1 or TFIID subunits.";
RL Science 266:1966-1972(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6), AND VARIANTS
RP TYR-91; MET-575 AND LEU-793.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-91; PHE-304; HIS-357;
RP LEU-387; TYR-518; LEU-573; MET-575; GLY-591; SER-635; MET-791; LEU-793 AND
RP HIS-816.
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS TYR-91 AND
RP MET-575.
RC TISSUE=Lung;
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 INTERACTION WITH TP53.
RX PubMed=10913176; DOI=10.1128/mcb.20.16.5930-5938.2000;
RA Zhai W., Comai L.;
RT "Repression of RNA polymerase I transcription by the tumor suppressor
RT p53.";
RL Mol. Cell. Biol. 20:5930-5938(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH RRN3.
RX PubMed=11250903; DOI=10.1093/emboj/20.6.1373;
RA Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I.,
RA Zomerdijk J.C.B.M.;
RT "hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to
RT rRNA gene promoters.";
RL EMBO J. 20:1373-1382(2001).
RN [9]
RP FUNCTION OF THE SL1 COMPLEX.
RX PubMed=15970593; DOI=10.1074/jbc.m501595200;
RA Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.;
RT "TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex
RT formation and stabilizes upstream binding factor at the rDNA promoter.";
RL J. Biol. Chem. 280:29551-29558(2005).
RN [10]
RP INTERACTION WITH MYC.
RX PubMed=15723054; DOI=10.1038/ncb1224;
RA Grandori C., Gomez-Roman N., Felton-Edkins Z.A., Ngouenet C.,
RA Galloway D.A., Eisenman R.N., White R.J.;
RT "c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA
RT genes by RNA polymerase I.";
RL Nat. Cell Biol. 7:311-318(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-848, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-834, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the transcription factor SL1/TIF-IB complex,
CC which is involved in the assembly of the PIC (preinitiation complex)
CC during RNA polymerase I-dependent transcription. The rate of PIC
CC formation probably is primarily dependent on the rate of association of
CC SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in
CC stabilization of nucleolar transcription factor 1/UBTF on rDNA.
CC Formation of SL1/TIF-IB excludes the association of TBP with TFIID
CC subunits. Recruits RNA polymerase I to the rRNA gene promoter via
CC interaction with RRN3. {ECO:0000269|PubMed:11250903,
CC ECO:0000269|PubMed:15970593}.
CC -!- SUBUNIT: Component of the transcription factor SL1/TIF-IB complex,
CC composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the
CC complex interacts directly with TBP, TAF1A and TAF1B. Interaction of
CC the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC transcription factor IID (TFIID) subunits. Interacts with MYC and RRN3.
CC Interacts with p53/TP53; the interaction prevents the association of
CC SL1/TIF-IB with UBTF and represses RNA polymerase I transcription.
CC {ECO:0000269|PubMed:10913176, ECO:0000269|PubMed:11250903,
CC ECO:0000269|PubMed:15723054, ECO:0000269|PubMed:7801123}.
CC -!- INTERACTION:
CC Q15572; Q01105: SET; NbExp=4; IntAct=EBI-2510659, EBI-1053182;
CC Q15572; Q16514: TAF12; NbExp=2; IntAct=EBI-2510659, EBI-1034238;
CC Q15572; P20226: TBP; NbExp=3; IntAct=EBI-2510659, EBI-355371;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q15572-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15572-2; Sequence=VSP_015153, VSP_015154, VSP_015156;
CC Name=4;
CC IsoId=Q15572-4; Sequence=VSP_038087;
CC Name=5;
CC IsoId=Q15572-5; Sequence=VSP_038086;
CC Name=6;
CC IsoId=Q15572-6; Sequence=VSP_015154;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92831.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/taf1c/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L39059; AAA62861.1; -; mRNA.
DR EMBL; AK299060; BAH12941.1; -; mRNA.
DR EMBL; AK299347; BAH13010.1; -; mRNA.
DR EMBL; AK304261; BAH14144.1; -; mRNA.
DR EMBL; AK315982; BAH14353.1; -; mRNA.
DR EMBL; AB209594; BAD92831.1; ALT_SEQ; mRNA.
DR EMBL; AY158985; AAN38818.1; -; Genomic_DNA.
DR EMBL; AC009123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028131; AAH28131.1; -; mRNA.
DR CCDS; CCDS32496.1; -. [Q15572-1]
DR CCDS; CCDS45535.1; -. [Q15572-2]
DR CCDS; CCDS58488.1; -. [Q15572-4]
DR CCDS; CCDS58489.1; -. [Q15572-6]
DR PIR; A55384; A55384.
DR RefSeq; NP_001230085.1; NM_001243156.1. [Q15572-6]
DR RefSeq; NP_001230086.1; NM_001243157.1. [Q15572-4]
DR RefSeq; NP_001230087.1; NM_001243158.1. [Q15572-4]
DR RefSeq; NP_001230088.1; NM_001243159.1. [Q15572-5]
DR RefSeq; NP_005670.3; NM_005679.3. [Q15572-1]
DR RefSeq; NP_647610.2; NM_139353.2. [Q15572-2]
DR RefSeq; XP_005256283.1; XM_005256226.3. [Q15572-1]
DR RefSeq; XP_016879334.1; XM_017023845.1. [Q15572-6]
DR RefSeq; XP_016879337.1; XM_017023848.1.
DR AlphaFoldDB; Q15572; -.
DR BioGRID; 114482; 110.
DR CORUM; Q15572; -.
DR DIP; DIP-269N; -.
DR IntAct; Q15572; 28.
DR MINT; Q15572; -.
DR STRING; 9606.ENSP00000455265; -.
DR GlyGen; Q15572; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15572; -.
DR PhosphoSitePlus; Q15572; -.
DR BioMuta; TAF1C; -.
DR DMDM; 313104019; -.
DR EPD; Q15572; -.
DR jPOST; Q15572; -.
DR MassIVE; Q15572; -.
DR MaxQB; Q15572; -.
DR PaxDb; Q15572; -.
DR PeptideAtlas; Q15572; -.
DR PRIDE; Q15572; -.
DR ProteomicsDB; 60638; -. [Q15572-1]
DR ProteomicsDB; 60639; -. [Q15572-2]
DR ProteomicsDB; 60640; -. [Q15572-4]
DR ProteomicsDB; 60641; -. [Q15572-5]
DR ProteomicsDB; 60642; -. [Q15572-6]
DR Antibodypedia; 17054; 156 antibodies from 26 providers.
DR DNASU; 9013; -.
DR Ensembl; ENST00000341690.10; ENSP00000345305.6; ENSG00000103168.17. [Q15572-2]
DR Ensembl; ENST00000541676.5; ENSP00000437900.2; ENSG00000103168.17. [Q15572-4]
DR Ensembl; ENST00000566732.6; ENSP00000455933.1; ENSG00000103168.17. [Q15572-6]
DR Ensembl; ENST00000567759.5; ENSP00000455265.1; ENSG00000103168.17. [Q15572-1]
DR Ensembl; ENST00000570117.5; ENSP00000455247.1; ENSG00000103168.17. [Q15572-4]
DR GeneID; 9013; -.
DR KEGG; hsa:9013; -.
DR MANE-Select; ENST00000566732.6; ENSP00000455933.1; NM_001243156.2; NP_001230085.2. [Q15572-6]
DR UCSC; uc002fhm.4; human. [Q15572-1]
DR CTD; 9013; -.
DR DisGeNET; 9013; -.
DR GeneCards; TAF1C; -.
DR HGNC; HGNC:11534; TAF1C.
DR HPA; ENSG00000103168; Low tissue specificity.
DR MIM; 604905; gene.
DR neXtProt; NX_Q15572; -.
DR OpenTargets; ENSG00000103168; -.
DR PharmGKB; PA36309; -.
DR VEuPathDB; HostDB:ENSG00000103168; -.
DR eggNOG; ENOG502QTCT; Eukaryota.
DR GeneTree; ENSGT00390000010767; -.
DR HOGENOM; CLU_037918_0_0_1; -.
DR InParanoid; Q15572; -.
DR OMA; CCRRWLK; -.
DR OrthoDB; 372910at2759; -.
DR PhylomeDB; Q15572; -.
DR TreeFam; TF351959; -.
DR PathwayCommons; Q15572; -.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; Q15572; -.
DR BioGRID-ORCS; 9013; 697 hits in 1098 CRISPR screens.
DR GeneWiki; TAF1C; -.
DR GenomeRNAi; 9013; -.
DR Pharos; Q15572; Tbio.
DR PRO; PR:Q15572; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15572; protein.
DR Bgee; ENSG00000103168; Expressed in left ovary and 165 other tissues.
DR ExpressionAtlas; Q15572; baseline and differential.
DR Genevisible; Q15572; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IEA:Ensembl.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0006360; P:transcription by RNA polymerase I; TAS:ProtInc.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; NAS:ParkinsonsUK-UCL.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR038801; TAF1C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15319; PTHR15319; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..869
FT /note="TATA box-binding protein-associated factor RNA
FT polymerase I subunit C"
FT /id="PRO_0000118863"
FT REGION 605..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 834
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 1..409
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038086"
FT VAR_SEQ 1..332
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038087"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015153"
FT VAR_SEQ 280..306
FT /note="SKALIYTFLPHWLTCYLTPGPFHPSSA -> T (in isoform 2 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015154"
FT VAR_SEQ 521
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015156"
FT VARIANT 91
FT /note="C -> Y (in dbSNP:rs4782591)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7801123,
FT ECO:0000269|Ref.4"
FT /id="VAR_058966"
FT VARIANT 304
FT /note="S -> F (in dbSNP:rs4150145)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023245"
FT VARIANT 357
FT /note="R -> H (in dbSNP:rs4150147)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023246"
FT VARIANT 387
FT /note="S -> L (in dbSNP:rs4150151)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023247"
FT VARIANT 518
FT /note="H -> Y (in dbSNP:rs4150165)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023248"
FT VARIANT 523
FT /note="G -> R (in dbSNP:rs4150167)"
FT /id="VAR_057261"
FT VARIANT 573
FT /note="P -> L (in dbSNP:rs4150170)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023249"
FT VARIANT 575
FT /note="L -> M (in dbSNP:rs2230129)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_023250"
FT VARIANT 591
FT /note="A -> G (in dbSNP:rs4150172)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023251"
FT VARIANT 635
FT /note="G -> S (in dbSNP:rs4150173)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023252"
FT VARIANT 791
FT /note="T -> M (in dbSNP:rs4150175)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023253"
FT VARIANT 793
FT /note="P -> L (in dbSNP:rs2230131)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_023254"
FT VARIANT 808
FT /note="P -> S (in dbSNP:rs3743640)"
FT /id="VAR_057262"
FT VARIANT 816
FT /note="R -> H (in dbSNP:rs4150176)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023255"
FT CONFLICT 244
FT /note="E -> K (in Ref. 2; BAH13010)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="N -> S (in Ref. 2; BAH14353)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="S -> G (in Ref. 2; BAH14144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 869 AA; 95213 MW; 6AAFAF296D98A5DB CRC64;
MDFPSSLRPA LFLTGPLGLS DVPDLSFMCS WRDALTLPEA QPQNSENGAL HVTKDLLWEP
ATPGPLPMLP PLIDPWDPGL TARDLLFRGG CRYRKRPRVV LDVTEQISRF LLDHGDVAFA
PLGKLMLENF KLEGAGSRTK KKTVVSVKKL LQDLGGHQPW GCPWAYLSNR QRRFSILGGP
ILGTSVASHL AELLHEELVL RWEQLLLDEA CTGGALAWVP GRTPQFGQLV YPAGGAQDRL
HFQEVVLTPG DNPQFLGKPG RIQLQGPVRQ VVTCTVQGES KALIYTFLPH WLTCYLTPGP
FHPSSALLAV RSDYHCAVWK FGKQWQPTLL QAMQVEKGAT GISLSPHLPG ELAICSRSGA
VCLWSPEDGL RQIYRDPETL VFRDSSSWRW ADFTAHPRVL TVGDRTGVKM LDTQGPPGCG
LLLFRLGAEA SCQKGERVLL TQYLGHSSPK CLPPTLHLVC TQFSLYLVDE RLPLVPMLKW
NHGLPSPLLL ARLLPPPRPS CVQPLLLGGQ GGQLQLLHLA GEGASVPRLA GPPQSLPSRI
DSLPAFPLLE PKIQWRLQER LKAPTIGLAA VVPPLPSAPT PGLVLFQLSA AGDVFYQQLR
PQVDSSLRRD AGPPGDTQPD CHAPTASWTS QDTAGCSQWL KALLKVPLAP PVWTAPTFTH
RQMLGSTELR REEEEGQRLG VLRKAMARGQ LLLQRDLGSL PAAEPPPAPE SGLEDKLSER
LGEAWAGRGA AWWERQQGRT SEPGRQTRRP KRRTQLSSSF SLSGHVDPSE DTSSPHSPEW
PPADALPLPP TTPPSQELTP DACAQGVPSE QRQMLRDYMA KLPPQRDTPG CATTPPHSQA
SSVRATRSQQ HTPVLSSSQP LRKKPRMGF
