ID HRH1_HUMAN Reviewed; 487 AA. AC P35367; A8K047; Q6P9E5; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 11-NOV-2015, entry version 147. DE RecName: Full=Histamine H1 receptor; DE Short=H1R; DE Short=HH1R; GN Name=HRH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8280179; DOI=10.1006/bbrc.1993.2662; RA de Backer M.D., Gommeren W., Moereels H., Nobels G., van Gompel P., RA Leysen J.E., Luyten W.H.M.L.; RT "Genomic cloning, heterologous expression and pharmacological RT characterization of a human histamine H1 receptor."; RL Biochem. Biophys. Res. Commun. 197:1601-1608(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8003029; DOI=10.1006/bbrc.1994.1786; RA Fukui K., Fujimoto K., Mizuguchi H., Sakamoto K., Horio Y., Takai S., RA Yamada K., Ito S.; RT "Molecular cloning of the human histamine H1 receptor gene."; RL Biochem. Biophys. Res. Commun. 201:894-901(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7925364; DOI=10.1111/j.1432-1033.1994.00489.x; RA Moguilevsky N., Varsalona F., Noyer M., Gillard M., Guillaume J.P., RA Garcia L., Szpirer C., Szpirer J., Bollen A.; RT "Stable expression of human H1-histamine-receptor cDNA in Chinese RT hamster ovary cells. Pharmacological characterisation of the protein, RT tissue distribution of messenger RNA and chromosomal localisation of RT the gene."; RL Eur. J. Biochem. 224:489-495(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lens epithelium; RA Rae J.L., Shepard A.R.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15014171; DOI=10.1093/molbev/msh100; RA Kitano T., Liu Y.-H., Ueda S., Saitou N.; RT "Human-specific amino acid changes found in 103 protein-coding RT genes."; RL Mol. Biol. Evol. 21:936-944(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PHOSPHORYLATION AT THR-140; THR-142; SER-396 AND SER-398. RX PubMed=15328002; DOI=10.1016/j.febslet.2004.07.072; RA Horio S., Kato T., Ogawa M., Fujimoto K., Fukui H.; RT "Two threonine residues and two serine residues in the second and RT third intracellular loops are both involved in histamine H1 receptor RT downregulation."; RL FEBS Lett. 573:226-230(2004). RN [11] RP IDENTIFICATION BY 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279, AND IDENTIFICATION RP 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 [13] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 20-487 IN COMPLEX WITH RP ANTAGONIST, DISULFIDE BOND, SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=21697825; DOI=10.1038/nature10236; RA Shimamura T., Shiroishi M., Weyand S., Tsujimoto H., Winter G., RA Katritch V., Abagyan R., Cherezov V., Liu W., Han G.W., Kobayashi T., RA Stevens R.C., Iwata S.; RT "Structure of the human histamine H1 receptor complex with doxepin."; RL Nature 475:65-70(2011). RN [14] RP VARIANT [LARGE SCALE ANALYSIS] GLU-385. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: In peripheral tissues, the H1 subclass of histamine CC receptors mediates the contraction of smooth muscles, increase in CC capillary permeability due to contraction of terminal venules, and CC catecholamine release from adrenal medulla, as well as mediating CC neurotransmission in the central nervous system. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21697825}; CC Multi-pass membrane protein {ECO:0000269|PubMed:21697825}. CC -!- PTM: Phosphorylation at sites in the second and third cytoplasmic CC loops independently contribute to agonist-induced receptor CC downregulation. {ECO:0000269|PubMed:15328002}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. 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; Z34897; CAA84380.1; -; mRNA. DR EMBL; X76786; CAA54182.1; -; Genomic_DNA. DR EMBL; D14436; BAA03319.1; -; Genomic_DNA. DR EMBL; D28481; BAA05840.1; -; mRNA. DR EMBL; AF026261; AAB95156.1; -; mRNA. DR EMBL; AB041380; BAA94465.1; -; Genomic_DNA. DR EMBL; AY136743; AAN01269.1; -; mRNA. DR EMBL; AK289412; BAF82101.1; -; mRNA. DR EMBL; CH471055; EAW64092.1; -; Genomic_DNA. DR EMBL; BC060802; AAH60802.1; -; mRNA. DR CCDS; CCDS2604.1; -. DR PIR; JC2495; JC2495. DR RefSeq; NP_000852.1; NM_000861.3. DR RefSeq; NP_001091681.1; NM_001098211.1. DR RefSeq; NP_001091682.1; NM_001098212.1. DR RefSeq; NP_001091683.1; NM_001098213.1. DR RefSeq; XP_011531954.1; XM_011533652.1. DR RefSeq; XP_011531955.1; XM_011533653.1. DR RefSeq; XP_011531956.1; XM_011533654.1. DR RefSeq; XP_011531957.1; XM_011533655.1. DR UniGene; Hs.1570; -. DR PDB; 3RZE; X-ray; 3.10 A; A=20-221, A=405-487. DR PDBsum; 3RZE; -. DR ProteinModelPortal; P35367; -. DR SMR; P35367; 19-256, 405-485. DR DIP; DIP-41996N; -. DR IntAct; P35367; 1. DR MINT; MINT-190077; -. DR STRING; 9606.ENSP00000380247; -. DR BindingDB; P35367; -. DR ChEMBL; CHEMBL231; -. DR DrugBank; DB01615; Aceprometazine. DR DrugBank; DB06766; Alcaftadine. DR DrugBank; DB01246; Alimemazine. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB08799; Antazoline. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB00637; Astemizole. DR DrugBank; DB00719; Azatadine. DR DrugBank; DB00972; Azelastine. DR DrugBank; DB00245; Benzatropine. DR DrugBank; DB04890; Bepotastine. DR DrugBank; DB06698; Betahistine. DR DrugBank; DB01237; Bromodiphenhydramine. DR DrugBank; DB00835; Brompheniramine. DR DrugBank; DB00354; Buclizine. DR DrugBank; DB09016; Butriptyline. DR DrugBank; DB00748; Carbinoxamine. DR DrugBank; DB00341; Cetirizine. DR DrugBank; DB08936; Chlorcyclizine. DR DrugBank; DB08800; Chloropyramine. DR DrugBank; DB01114; Chlorphenamine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB01239; Chlorprothixene. DR DrugBank; DB00568; Cinnarizine. DR DrugBank; DB00215; Citalopram. DR DrugBank; DB00283; Clemastine. DR DrugBank; DB04837; Clofedanol. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB01176; Cyclizine. DR DrugBank; DB00434; Cyproheptadine. DR DrugBank; DB01151; Desipramine. DR DrugBank; DB00967; Desloratadine. DR DrugBank; DB00405; Dexbrompheniramine. DR DrugBank; DB00985; Dimenhydrinate. DR DrugBank; DB08801; Dimetindene. DR DrugBank; DB01075; Diphenhydramine. DR DrugBank; DB01146; Diphenylpyraline. DR DrugBank; DB01142; Doxepin. DR DrugBank; DB00366; Doxylamine. DR DrugBank; DB01084; Emedastine. DR DrugBank; DB00751; Epinastine. DR DrugBank; DB01175; Escitalopram. DR DrugBank; DB00950; Fexofenadine. DR DrugBank; DB04841; Flunarizine. DR DrugBank; DB00667; Histamine Phosphate. DR DrugBank; DB00557; Hydroxyzine. DR DrugBank; DB04946; Iloperidone. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB08802; Isothipendyl. DR DrugBank; DB00920; Ketotifen. DR DrugBank; DB01106; Levocabastine. DR DrugBank; DB00455; Loratadine. DR DrugBank; DB00408; Loxapine. DR DrugBank; DB00934; Maprotiline. DR DrugBank; DB00737; Meclizine. DR DrugBank; DB06691; Mepyramine. DR DrugBank; DB01071; Mequitazine. DR DrugBank; DB00902; Methdilazine. DR DrugBank; DB01403; Methotrimeprazine. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB00370; Mirtazapine. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB00768; Olopatadine. DR DrugBank; DB01173; Orphenadrine. DR DrugBank; DB01267; Paliperidone. DR DrugBank; DB01619; Phenindamine. DR DrugBank; DB01620; Pheniramine. DR DrugBank; DB00420; Promazine. DR DrugBank; DB01069; Promethazine. DR DrugBank; DB00777; Propiomazine. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB00734; Risperidone. DR DrugBank; DB00797; Tolazoline. DR DrugBank; DB00656; Trazodone. DR DrugBank; DB00726; Trimipramine. DR DrugBank; DB00792; Tripelennamine. DR DrugBank; DB00427; Triprolidine. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB01624; Zuclopenthixol. DR GuidetoPHARMACOLOGY; 262; -. DR PhosphoSite; P35367; -. DR BioMuta; HRH1; -. DR DMDM; 547645; -. DR MaxQB; P35367; -. DR PaxDb; P35367; -. DR PRIDE; P35367; -. DR DNASU; 3269; -. DR Ensembl; ENST00000397056; ENSP00000380247; ENSG00000196639. DR Ensembl; ENST00000431010; ENSP00000397028; ENSG00000196639. DR Ensembl; ENST00000438284; ENSP00000406705; ENSG00000196639. DR GeneID; 3269; -. DR KEGG; hsa:3269; -. DR UCSC; uc003bwb.4; human. DR CTD; 3269; -. DR GeneCards; HRH1; -. DR HGNC; HGNC:5182; HRH1. DR HPA; HPA029740; -. DR MIM; 600167; gene. DR neXtProt; NX_P35367; -. DR PharmGKB; PA29456; -. DR eggNOG; KOG4220; Eukaryota. DR eggNOG; ENOG410YCQR; LUCA. DR GeneTree; ENSGT00780000121874; -. DR HOGENOM; HOG000273869; -. DR HOVERGEN; HBG101103; -. DR InParanoid; P35367; -. DR KO; K04149; -. DR OMA; YIKFTWK; -. DR OrthoDB; EOG70CR7W; -. DR PhylomeDB; P35367; -. DR TreeFam; TF333432; -. DR Reactome; R-HSA-390650; Histamine receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR ChiTaRS; HRH1; human. DR GeneWiki; Histamine_H1_receptor; -. DR GenomeRNAi; 3269; -. DR NextBio; 12981; -. DR PRO; PR:P35367; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; P35367; -. DR CleanEx; HS_HRH1; -. DR ExpressionAtlas; P35367; baseline and differential. DR Genevisible; P35367; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc. DR GO; GO:0051381; F:histamine binding; IBA:GO_Central. DR GO; GO:0004969; F:histamine receptor activity; ISS:UniProtKB. DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB. DR GO; GO:0048245; P:eosinophil chemotaxis; IEA:InterPro. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0048016; P:inositol phosphate-mediated signaling; ISS:BHF-UCL. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0050804; P:modulation of synaptic transmission; IBA:GO_Central. DR GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISS:BHF-UCL. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:InterPro. DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl. DR GO; GO:0043114; P:regulation of vascular permeability; IEA:InterPro. DR GO; GO:0019229; P:regulation of vasoconstriction; IBA:GO_Central. DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central. DR GO; GO:0008542; P:visual learning; IEA:Ensembl. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR000921; Histamine_H1_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00530; HISTAMINEH1R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; KW Polymorphism; Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1 487 Histamine H1 receptor. FT /FTId=PRO_0000069676. FT TOPO_DOM 1 29 Extracellular. FT {ECO:0000269|PubMed:21697825}. FT TRANSMEM 30 52 Helical; Name=1. FT TOPO_DOM 53 62 Cytoplasmic. FT {ECO:0000269|PubMed:21697825}. FT TRANSMEM 63 83 Helical; Name=2. FT TOPO_DOM 84 101 Extracellular. FT {ECO:0000269|PubMed:21697825}. FT TRANSMEM 102 123 Helical; Name=3. FT TOPO_DOM 124 143 Cytoplasmic. FT {ECO:0000269|PubMed:21697825}. FT TRANSMEM 144 164 Helical; Name=4. FT TOPO_DOM 165 189 Extracellular. FT {ECO:0000269|PubMed:21697825}. FT TRANSMEM 190 210 Helical; Name=5. FT TOPO_DOM 211 416 Cytoplasmic. FT {ECO:0000269|PubMed:21697825}. FT TRANSMEM 417 438 Helical; Name=6. FT TOPO_DOM 439 450 Extracellular. FT {ECO:0000269|PubMed:21697825}. FT TRANSMEM 451 470 Helical; Name=7. FT TOPO_DOM 471 487 Cytoplasmic. FT {ECO:0000269|PubMed:21697825}. FT REGION 107 112 Important for agonist binding. FT REGION 424 428 Important for agonist binding. FT MOD_RES 140 140 Phosphothreonine. FT {ECO:0000269|PubMed:15328002}. FT MOD_RES 142 142 Phosphothreonine. FT {ECO:0000269|PubMed:15328002}. FT MOD_RES 279 279 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 344 344 Phosphoserine. FT {ECO:0000250|UniProtKB:P70174}. FT MOD_RES 347 347 Phosphoserine. FT {ECO:0000250|UniProtKB:P70174}. FT MOD_RES 380 380 Phosphoserine. FT {ECO:0000250|UniProtKB:P70174}. FT MOD_RES 396 396 Phosphoserine. FT {ECO:0000269|PubMed:15328002}. FT MOD_RES 398 398 Phosphoserine. FT {ECO:0000269|PubMed:15328002}. FT CARBOHYD 5 5 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 18 18 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 100 180 {ECO:0000255|PROSITE-ProRule:PRU00521, FT ECO:0000269|PubMed:21697825}. FT DISULFID 441 444 {ECO:0000255|PROSITE-ProRule:PRU00521, FT ECO:0000269|PubMed:21697825}. FT VARIANT 19 19 K -> N (in dbSNP:rs2067466). FT /FTId=VAR_049410. FT VARIANT 270 270 G -> E (in dbSNP:rs7651620). FT /FTId=VAR_033476. FT VARIANT 385 385 D -> E (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_035761. FT CONFLICT 308 308 V -> E (in Ref. 9; AAH60802). FT {ECO:0000305}. FT HELIX 29 31 {ECO:0000244|PDB:3RZE}. FT HELIX 33 54 {ECO:0000244|PDB:3RZE}. FT HELIX 61 63 {ECO:0000244|PDB:3RZE}. FT HELIX 64 78 {ECO:0000244|PDB:3RZE}. FT HELIX 80 89 {ECO:0000244|PDB:3RZE}. FT STRAND 90 92 {ECO:0000244|PDB:3RZE}. FT HELIX 96 130 {ECO:0000244|PDB:3RZE}. FT TURN 135 138 {ECO:0000244|PDB:3RZE}. FT HELIX 141 155 {ECO:0000244|PDB:3RZE}. FT HELIX 156 158 {ECO:0000244|PDB:3RZE}. FT HELIX 159 163 {ECO:0000244|PDB:3RZE}. FT STRAND 177 180 {ECO:0000244|PDB:3RZE}. FT HELIX 188 198 {ECO:0000244|PDB:3RZE}. FT HELIX 200 216 {ECO:0000244|PDB:3RZE}. FT HELIX 408 441 {ECO:0000244|PDB:3RZE}. FT TURN 447 449 {ECO:0000244|PDB:3RZE}. FT HELIX 450 471 {ECO:0000244|PDB:3RZE}. FT HELIX 473 483 {ECO:0000244|PDB:3RZE}. SQ SEQUENCE 487 AA; 55784 MW; E5DB418A4C17A985 CRC64; MSLPNSSCLL EDKMCEGNKT TMASPQLMPL VVVLSTICLV TVGLNLLVLY AVRSERKLHT VGNLYIVSLS VADLIVGAVV MPMNILYLLM SKWSLGRPLC LFWLSMDYVA STASIFSVFI LCIDRYRSVQ QPLRYLKYRT KTRASATILG AWFLSFLWVI PILGWNHFMQ QTSVRREDKC ETDFYDVTWF KVMTAIINFY LPTLLMLWFY AKIYKAVRQH CQHRELINRS LPSFSEIKLR PENPKGDAKK PGKESPWEVL KRKPKDAGGG SVLKSPSQTP KEMKSPVVFS QEDDREVDKL YCFPLDIVHM QAAAEGSSRD YVAVNRSHGQ LKTDEQGLNT HGASEISEDQ MLGDSQSFSR TDSDTTTETA PGKGKLRSGS NTGLDYIKFT WKRLRSHSRQ YVSGLHMNRE RKAAKQLGFI MAAFILCWIP YFIFFMVIAF CKNCCNEHLH MFTIWLGYIN STLNPLIYPL CNENFKKTFK RILHIRS //