ID HEAT1_HUMAN Reviewed; 2144 AA. AC Q9H583; Q5T3Q8; Q6P197; Q9NW23; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 3. DT 27-MAR-2024, entry version 197. DE RecName: Full=HEAT repeat-containing protein 1; DE AltName: Full=Protein BAP28; DE AltName: Full=U3 small nucleolar RNA-associated protein 10 homolog; DE Contains: DE RecName: Full=HEAT repeat-containing protein 1, N-terminally processed; GN Name=HEATR1 {ECO:0000312|HGNC:HGNC:25517}; Synonyms=BAP28, UTP10; 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], AND VARIANTS ARG-348; VAL-607; SER-1694; RP ALA-1854; ASP-1967 AND GLY-2017. RA Bougueleret L., Chumakov I., Barry C., Cohen-Akenine A.; RT "A novel BAP28 gene and protein."; RL Patent number WO0100669, 04-JAN-2001. RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1039-2144, AND VARIANTS SER-1694; RP ALA-1854; ASP-1967 AND GLY-2017. RC TISSUE=Lymph; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1777-2144. 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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=17699751; DOI=10.1101/gad.436707; RA Prieto J.L., McStay B.; RT "Recruitment of factors linking transcription and processing of pre-rRNA to RT NOR chromatin is UBF-dependent and occurs independent of transcription in RT human cells."; RL Genes Dev. 21:2041-2054(2007). RN [7] RP IDENTIFICATION BY 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1190, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1190, AND IDENTIFICATION BY RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516; SER-1190 AND SER-1492, RP AND 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 [14] RP VARIANT GLY-2017, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17488105; DOI=10.1021/pr0700908; RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A., RA Hendrickson R.C., Stephenson J.L. Jr.; RT "Detection and validation of non-synonymous coding SNPs from orthogonal RT analysis of shotgun proteomics data."; RL J. Proteome Res. 6:2331-2340(2007). RN [15] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=34516797; DOI=10.1126/science.abj5338; RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.; RT "Nucleolar maturation of the human small subunit processome."; RL Science 373:eabj5338-eabj5338(2021). CC -!- FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing CC of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA CC transcription by RNA polymerase I (PubMed:17699751). Part of the small CC subunit (SSU) processome, first precursor of the small eukaryotic CC ribosomal subunit. During the assembly of the SSU processome in the CC nucleolus, many ribosome biogenesis factors, an RNA chaperone and CC ribosomal proteins associate with the nascent pre-rRNA and work in CC concert to generate RNA folding, modifications, rearrangements and CC cleavage as well as targeted degradation of pre-ribosomal RNA by the CC RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:17699751, CC ECO:0000269|PubMed:34516797}. CC -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more CC than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3. CC {ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:34516797}. CC -!- INTERACTION: CC Q9H583; Q76353; Xeno; NbExp=3; IntAct=EBI-1048716, EBI-6248077; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, CC ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:34516797}. CC -!- SIMILARITY: Belongs to the HEATR1/UTP10 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91564.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AX067150; CAC26776.1; -; mRNA. DR EMBL; AL359921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC065205; AAH65205.1; -; mRNA. DR EMBL; AK001221; BAA91564.1; ALT_INIT; mRNA. DR CCDS; CCDS31066.1; -. DR RefSeq; NP_060542.4; NM_018072.5. DR PDB; 7MQ8; EM; 3.60 A; LM=1-2144. DR PDB; 7MQ9; EM; 3.87 A; LM=1-2144. DR PDB; 7MQA; EM; 2.70 A; LM=1-2144. DR PDBsum; 7MQ8; -. DR PDBsum; 7MQ9; -. DR PDBsum; 7MQA; -. DR AlphaFoldDB; Q9H583; -. DR EMDB; EMD-23936; -. DR EMDB; EMD-23937; -. DR EMDB; EMD-23938; -. DR SMR; Q9H583; -. DR BioGRID; 120433; 249. DR ComplexPortal; CPX-2450; UTP-A complex. DR IntAct; Q9H583; 48. DR MINT; Q9H583; -. DR STRING; 9606.ENSP00000355541; -. DR GlyGen; Q9H583; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H583; -. DR MetOSite; Q9H583; -. DR PhosphoSitePlus; Q9H583; -. DR SwissPalm; Q9H583; -. DR BioMuta; HEATR1; -. DR DMDM; 71153494; -. DR EPD; Q9H583; -. DR jPOST; Q9H583; -. DR MassIVE; Q9H583; -. DR MaxQB; Q9H583; -. DR PaxDb; 9606-ENSP00000355541; -. DR PeptideAtlas; Q9H583; -. DR ProteomicsDB; 80900; -. DR Pumba; Q9H583; -. DR Antibodypedia; 34700; 115 antibodies from 19 providers. DR DNASU; 55127; -. DR Ensembl; ENST00000366582.8; ENSP00000355541.3; ENSG00000119285.11. DR GeneID; 55127; -. DR KEGG; hsa:55127; -. DR MANE-Select; ENST00000366582.8; ENSP00000355541.3; NM_018072.6; NP_060542.4. DR UCSC; uc001hyd.3; human. DR AGR; HGNC:25517; -. DR CTD; 55127; -. DR DisGeNET; 55127; -. DR GeneCards; HEATR1; -. DR HGNC; HGNC:25517; HEATR1. DR HPA; ENSG00000119285; Low tissue specificity. DR MIM; 620390; gene. DR neXtProt; NX_Q9H583; -. DR OpenTargets; ENSG00000119285; -. DR PharmGKB; PA142671697; -. DR VEuPathDB; HostDB:ENSG00000119285; -. DR eggNOG; KOG1837; Eukaryota. DR GeneTree; ENSGT00390000015845; -. DR InParanoid; Q9H583; -. DR OMA; NDVMWKQ; -. DR OrthoDB; 5480100at2759; -. DR PhylomeDB; Q9H583; -. DR TreeFam; TF314593; -. DR PathwayCommons; Q9H583; -. DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; Q9H583; -. DR BioGRID-ORCS; 55127; 834 hits in 1169 CRISPR screens. DR ChiTaRS; HEATR1; human. DR GeneWiki; HEATR1; -. DR GenomeRNAi; 55127; -. DR Pharos; Q9H583; Tbio. DR PRO; PR:Q9H583; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9H583; Protein. DR Bgee; ENSG00000119285; Expressed in pancreatic ductal cell and 199 other cell types or tissues. DR ExpressionAtlas; Q9H583; baseline and differential. DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0034455; C:t-UTP complex; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:UniProtKB. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR012954; BP28_C_dom. DR InterPro; IPR022125; U3snoRNP10_N. DR InterPro; IPR040191; UTP10. DR PANTHER; PTHR13457; BAP28; 1. DR PANTHER; PTHR13457:SF1; HEAT REPEAT-CONTAINING PROTEIN 1; 1. DR Pfam; PF08146; BP28CT; 1. DR Pfam; PF12397; U3snoRNP10; 1. DR SMART; SM01036; BP28CT; 1. DR SUPFAM; SSF48371; ARM repeat; 3. DR SWISS-2DPAGE; Q9H583; -. DR Genevisible; Q9H583; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome; KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; Transcription; KW Transcription regulation. FT CHAIN 1..2144 FT /note="HEAT repeat-containing protein 1" FT /id="PRO_0000424485" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..2144 FT /note="HEAT repeat-containing protein 1, N-terminally FT processed" FT /id="PRO_0000186201" FT REPEAT 2106..2142 FT /note="HEAT" FT REGION 1170..1191 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="N-acetylthreonine; in HEAT repeat-containing protein FT 1, N-terminally processed" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1492 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VARIANT 348 FT /note="H -> R (in dbSNP:rs2794751)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_049329" FT VARIANT 607 FT /note="M -> V (in dbSNP:rs2794763)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_049330" FT VARIANT 957 FT /note="D -> G (in dbSNP:rs16833953)" FT /id="VAR_049331" FT VARIANT 1433 FT /note="Y -> C (in dbSNP:rs653737)" FT /id="VAR_049332" FT VARIANT 1559 FT /note="S -> N (in dbSNP:rs6661946)" FT /id="VAR_049333" FT VARIANT 1654 FT /note="R -> H (in dbSNP:rs16833884)" FT /id="VAR_049334" FT VARIANT 1694 FT /note="N -> S (in dbSNP:rs2275689)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1" FT /id="VAR_010939" FT VARIANT 1854 FT /note="V -> A (in dbSNP:rs1885533)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1" FT /id="VAR_010940" FT VARIANT 1967 FT /note="N -> D (in dbSNP:rs1126627)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1" FT /id="VAR_010941" FT VARIANT 2017 FT /note="E -> G (confirmed at protein level; FT dbSNP:rs2275687)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17488105, ECO:0000269|Ref.1" FT /id="VAR_010942" FT VARIANT 2077 FT /note="S -> L (in dbSNP:rs6664730)" FT /id="VAR_049335" SQ SEQUENCE 2144 AA; 242370 MW; 7590EEA17A5FF39D CRC64; MTSLAQQLQR LALPQSDASL LSRDEVASLL FDPKEAATID RDTAFAIGCT GLEELLGIDP SFEQFEAPLF SQLAKTLERS VQTKAVNKQL DENISLFLIH LSPYFLLKPA QKCLEWLIHR FHIHLYNQDS LIACVLPYHE TRIFVRVIQL LKINNSKHRW FWLLPVKQSG VPLAKGTLIT HCYKDLGFMD FICSLVTKSV KVFAEYPGSS AQLRVLLAFY ASTIVSALVA AEDVSDNIIA KLFPYIQKGL KSSLPDYRAA TYMIICQISV KVTMENTFVN SLASQIIKTL TKIPSLIKDG LSCLIVLLQR QKPESLGKKP FPHLCNVPDL ITILHGISET YDVSPLLHYM LPHLVVSIIH HVTGEETEGM DGQIYKRHLE AILTKISLKN NLDHLLASLL FEEYISYSSQ EEMDSNKVSL LNEQFLPLIR LLESKYPRTL DVVLEEHLKE IADLKKQELF HQFVSLSTSG GKYQFLADSD TSLMLSLNHP LAPVRILAMN HLKKIMKTSK EGVDESFIKE AVLARLGDDN IDVVLSAISA FEIFKEHFSS EVTISNLLNL FQRAELSKNG EWYEVLKIAA DILIKEEILS ENDQLSNQVV VCLLPFMVIN NDDTESAEMK IAIYLSKSGI CSLHPLLRGW EEALENVIKS TKPGKLIGVA NQKMIELLAD NINLGDPSSM LKMVEDLISV GEEESFNLKQ KVTFHVILSV LVSCCSSLKE THFPFAIRVF SLLQKKIKKL ESVITAVEIP SEWHIELMLD RGIPVELWAH YVEELNSTQR VAVEDSVFLV FSLKKFIYAL KAPKSFPKGD IWWNPEQLKE DSRDYLHLLI GLFEMMLNGA DAVHFRVLMK LFIKVHLEDV FQLFKFCSVL WTYGSSLSNP LNCSVKTVLQ TQALYVGCAM LSSQKTQCKH QLASISSPVV TSLLINLGSP VKEVRRAAIQ CLQALSGVAS PFYLIIDHLI SKAEEITSDA AYVIQDLATL FEELQREKKL KSHQKLSETL KNLLSCVYSC PSYIAKDLMK VLQGVNGEMV LSQLLPMAEQ LLEKIQKEPT AVLKDEAMVL HLTLGKYNEF SVSLLNEDPK SLDIFIKAVH TTKELYAGMP TIQITALEKI TKPFFAAISD EKVQQKLLRM LFDLLVNCKN SHCAQTVSSV FKGISVNAEQ VRIELEPPDK AKPLGTVQQK RRQKMQQKKS QDLESVQEVG GSYWQRVTLI LELLQHKKKL RSPQILVPTL FNLLSRCLEP LPQEQGNMEY TKQLILSCLL NICQKLSPDG GKIPKDILDE EKFNVELIVQ CIRLSEMPQT HHHALLLLGT VAGIFPDKVL HNIMSIFTFM GANVMRLDDT YSFQVINKTV KMVIPALIQS DSGDSIEVSR NVEEIVVKII SVFVDALPHV PEHRRLPILV QLVDTLGAEK FLWILLILLF EQYVTKTVLA AAYGEKDAIL EADTEFWFSV CCEFSVQHQI QSLMNILQYL LKLPEEKEET IPKAVSFNKS ESQEEMLQVF NVETHTSKQL RHFKFLSVSF MSQLLSSNNF LKKVVESGGP EILKGLEERL LETVLGYISA VAQSMERNAD KLTVKFWRAL LSKAYDLLDK VNALLPTETF IPVIRGLVGN PLPSVRRKAL DLLNNKLQQN ISWKKTIVTR FLKLVPDLLA IVQRKKKEGE EEQAINRQTA LYTLKLLCKN FGAENPDPFV PVLNTAVKLI APERKEEKNV LGSALLCIAE VTSTLEALAI PQLPSLMPSL LTTMKNTSEL VSSEVYLLSA LAALQKVVET LPHFISPYLE GILSQVIHLE KITSEMGSAS QANIRLTSLK KTLATTLAPR VLLPAIKKTY KQIEKNWKNH MGPFMSILQE HIGVMKKEEL TSHQSQLTAF FLEALDFRAQ HSENDLEEVG KTENCIIDCL VAMVVKLSEV TFRPLFFKLF DWAKTEDAPK DRLLTFYNLA DCIAEKLKGL FTLFAGHLVK PFADTLNQVN ISKTDEAFFD SENDPEKCCL LLQFILNCLY KIFLFDTQHF ISKERAEALM MPLVDQLENR LGGEEKFQER VTKHLIPCIA QFSVAMADDS LWKPLNYQIL LKTRDSSPKV RFAALITVLA LAEKLKENYI VLLPESIPFL AELMEDECEE VEHQCQKTIQ QLETVLGEPL QSYF //