HEAT1_HUMAN
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 03-AUG-2022, entry version 188.
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; 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).
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. {ECO:0000269|PubMed:17699751}.
CC -!- SUBUNIT: May be a component of the proposed t-UTP subcomplex of the
CC ribosomal small subunit (SSU) processome containing at least UTP4,
CC WDR43, HEATR1, UTP15, WDR75. {ECO:0000305|PubMed:17699751}.
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}.
CC -!- SIMILARITY: Belongs to the HEATR1/UTP10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 SMR; Q9H583; -.
DR BioGRID; 120433; 227.
DR IntAct; Q9H583; 46.
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 SWISS-2DPAGE; Q9H583; -.
DR EPD; Q9H583; -.
DR jPOST; Q9H583; -.
DR MassIVE; Q9H583; -.
DR MaxQB; Q9H583; -.
DR PaxDb; Q9H583; -.
DR PeptideAtlas; Q9H583; -.
DR PRIDE; Q9H583; -.
DR ProteomicsDB; 80900; -.
DR Antibodypedia; 34700; 93 antibodies from 18 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 CTD; 55127; -.
DR DisGeNET; 55127; -.
DR GeneCards; HEATR1; -.
DR HGNC; HGNC:25517; HEATR1.
DR HPA; ENSG00000119285; Low tissue specificity.
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; 524830at2759; -.
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; 802 hits in 1091 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 198 other tissues.
DR ExpressionAtlas; Q9H583; baseline and differential.
DR Genevisible; Q9H583; HS.
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; IBA:GO_Central.
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 Gene3D; 1.25.10.10; -; 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; PTHR13457; 1.
DR Pfam; PF08146; BP28CT; 1.
DR Pfam; PF12397; U3snoRNP10; 1.
DR SMART; SM01036; BP28CT; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
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
