ID CENPH_HUMAN Reviewed; 247 AA. AC Q9H3R5; A8K3Y1; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 175. DE RecName: Full=Centromere protein H; DE Short=CENP-H; DE AltName: Full=Interphase centromere complex protein 35; GN Name=CENPH {ECO:0000312|HGNC:HGNC:17268}; Synonyms=ICEN35; 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] {ECO:0000305, ECO:0000312|EMBL:BAB18635.1} RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH KIF2C, AND SUBCELLULAR RP LOCATION. RC TISSUE=Cervix carcinoma; RX PubMed=11092768; DOI=10.1093/hmg/9.19.2919; RA Sugata N., Li S., Earnshaw W.C., Yen T.J., Yoda K., Masumoto H., RA Munekata E., Warburton P.E., Todokoro K.; RT "Human CENP-H multimers colocalize with CENP-A and CENP-C at active RT centromere-kinetochore complexes."; RL Hum. Mol. Genet. 9:2919-2926(2000). RN [2] 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., 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 GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000312|EMBL:AAH15355.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta {ECO:0000312|EMBL:AAH15355.1}, and Testis RC {ECO:0000312|EMBL:AAH12024.1}; 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 [5] RP FUNCTION. RX PubMed=14536089; DOI=10.1016/s1097-2765(03)00279-x; RA Saffery R., Sumer H., Hassan S., Wong L.H., Craig J.M., Todokoro K., RA Anderson M., Stafford A., Choo K.H.A.; RT "Transcription within a functional human centromere."; RL Mol. Cell 12:509-516(2003). RN [6] RP INTERACTION WITH NDC80. RX PubMed=15713649; DOI=10.1128/mcb.25.5.1958-1970.2005; RA Mikami Y., Hori T., Kimura H., Fukagawa T.; RT "The functional region of CENP-H interacts with the Nuf2 complex that RT localizes to centromere during mitosis."; RL Mol. Cell. Biol. 25:1958-1970(2005). RN [7] RP FUNCTION. RX PubMed=16875666; DOI=10.1016/j.bbrc.2006.06.187; RA Orthaus S., Ohndorf S., Diekmann S.; RT "RNAi knockdown of human kinetochore protein CENP-H."; RL Biochem. Biophys. Res. Commun. 348:36-46(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x; RA Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., RA Goshima N., Nomura F., Nomura N., Yoda K.; RT "Comprehensive analysis of the ICEN (Interphase Centromere Complex) RT components enriched in the CENP-A chromatin of human cells."; RL Genes Cells 11:673-684(2006). RN [9] RP IDENTIFICATION IN A COMPLEX WITH CENPI; CENPK; CENPN; CENPO; CENPP; CENPQ; RP CENPR AND CENPU. RX PubMed=16622420; DOI=10.1038/ncb1396; RA Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III, RA Desai A., Fukagawa T.; RT "The CENP-H-I complex is required for the efficient incorporation of newly RT synthesized CENP-A into centromeres."; RL Nat. Cell Biol. 8:446-457(2006). RN [10] RP IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPM; CENPN; RP CENPT AND CENPU. RX PubMed=16622419; DOI=10.1038/ncb1397; RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III, RA Cleveland D.W.; RT "The human CENP-A centromeric nucleosome-associated complex."; RL Nat. Cell Biol. 8:458-469(2006). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18007590; DOI=10.1038/sj.emboj.7601927; RA McClelland S.E., Borusu S., Amaro A.C., Winter J.R., Belwal M., RA McAinsh A.D., Meraldi P.; RT "The CENP-A NAC/CAD kinetochore complex controls chromosome congression and RT spindle bipolarity."; RL EMBO J. 26:5033-5047(2007). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=17651496; DOI=10.1186/gb-2007-8-7-r148; RA Alonso A., Fritz B., Hasson D., Abrusan G., Cheung F., Yoda K., RA Radlwimmer B., Ladurner A.G., Warburton P.E.; RT "Co-localization of CENP-C and CENP-H to discontinuous domains of CENP-A RT chromatin at human neocentromeres."; RL Genome Biol. 8:R148.1-R148.19(2007). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP INTERACTION WITH CENPK. RX PubMed=19381461; DOI=10.1007/s11427-009-0050-3; RA Qiu S., Wang J., Yu C., He D.; RT "CENP-K and CENP-H may form coiled-coils in the kinetochores."; RL Sci. China, Ser. C, Life Sci. 52:352-359(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-68, 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 [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [18] RP VARIANT [LARGE SCALE ANALYSIS] LYS-2. 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., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a CC complex that plays a central role in assembly of kinetochore proteins, CC mitotic progression and chromosome segregation. The CENPA-NAC complex CC recruits the CENPA-CAD (nucleosome distal) complex and may be involved CC in incorporation of newly synthesized CENPA into centromeres. Required CC for chromosome congression and efficiently align the chromosomes on a CC metaphase plate. {ECO:0000269|PubMed:14536089, CC ECO:0000269|PubMed:16875666, ECO:0000269|PubMed:18007590}. CC -!- SUBUNIT: Self-associates. Component of the CENPA-NAC complex, at least CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CC CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CC CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts CC directly with CENPK. Interacts with KIF2C and NDC80. Interacts with CC TRIM36 (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q9H3R5; Q9NYB9-2: ABI2; NbExp=6; IntAct=EBI-1003700, EBI-11096309; CC Q9H3R5; P61158: ACTR3; NbExp=3; IntAct=EBI-1003700, EBI-351428; CC Q9H3R5; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-1003700, EBI-747505; CC Q9H3R5; Q7Z758: C8orf58; NbExp=3; IntAct=EBI-1003700, EBI-13286880; CC Q9H3R5; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-1003700, EBI-10749669; CC Q9H3R5; Q9BS16: CENPK; NbExp=7; IntAct=EBI-1003700, EBI-6871750; CC Q9H3R5; P28329-3: CHAT; NbExp=3; IntAct=EBI-1003700, EBI-25837549; CC Q9H3R5; Q13561: DCTN2; NbExp=5; IntAct=EBI-1003700, EBI-715074; CC Q9H3R5; P84090: ERH; NbExp=3; IntAct=EBI-1003700, EBI-711389; CC Q9H3R5; P22607: FGFR3; NbExp=3; IntAct=EBI-1003700, EBI-348399; CC Q9H3R5; O75409: H2AP; NbExp=3; IntAct=EBI-1003700, EBI-6447217; CC Q9H3R5; P01112: HRAS; NbExp=3; IntAct=EBI-1003700, EBI-350145; CC Q9H3R5; P20700: LMNB1; NbExp=3; IntAct=EBI-1003700, EBI-968218; CC Q9H3R5; Q14696: MESD; NbExp=3; IntAct=EBI-1003700, EBI-6165891; CC Q9H3R5; Q13126: MTAP; NbExp=3; IntAct=EBI-1003700, EBI-2547776; CC Q9H3R5; O14777: NDC80; NbExp=6; IntAct=EBI-1003700, EBI-715849; CC Q9H3R5; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-1003700, EBI-741048; CC Q9H3R5; Q9H2L5: RASSF4; NbExp=3; IntAct=EBI-1003700, EBI-2933362; CC Q9H3R5; Q96R06: SPAG5; NbExp=3; IntAct=EBI-1003700, EBI-413317; CC Q9H3R5; Q6ZR52-3: ZNF493; NbExp=3; IntAct=EBI-1003700, EBI-12856290; CC Q9H3R5; O43309: ZSCAN12; NbExp=3; IntAct=EBI-1003700, EBI-1210440; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. CC Note=Associates with active centromere-kinetochore complexes throughout CC the cell cycle. Colocalizes with inner kinetochore plate proteins CENPA CC and CENPC during both interphase and metaphase. CC -!- SIMILARITY: Belongs to the CENP-H/MCM16 family. {ECO:0000255}. 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; AB035124; BAB18635.1; -; mRNA. DR EMBL; AK290746; BAF83435.1; -; mRNA. DR EMBL; CH471137; EAW51304.1; -; Genomic_DNA. DR EMBL; BC015355; AAH15355.1; -; mRNA. DR EMBL; BC012024; AAH12024.1; -; mRNA. DR CCDS; CCDS3998.1; -. DR RefSeq; NP_075060.1; NM_022909.3. DR PDB; 7PB4; X-ray; 2.49 A; H=199-247. DR PDB; 7PKN; EM; 3.20 A; H=1-247. DR PDB; 7QOO; EM; 4.60 A; H=1-247. DR PDB; 7R5S; EM; 2.83 A; H=1-247. DR PDB; 7R5V; EM; 4.55 A; H=1-247. DR PDB; 7XHN; EM; 3.71 A; H=1-247. DR PDB; 7XHO; EM; 3.29 A; H=1-247. DR PDB; 7YWX; EM; 12.00 A; H=1-247. DR PDB; 7YYH; EM; 8.90 A; H=1-247. DR PDBsum; 7PB4; -. DR PDBsum; 7PKN; -. DR PDBsum; 7QOO; -. DR PDBsum; 7R5S; -. DR PDBsum; 7R5V; -. DR PDBsum; 7XHN; -. DR PDBsum; 7XHO; -. DR PDBsum; 7YWX; -. DR PDBsum; 7YYH; -. DR AlphaFoldDB; Q9H3R5; -. DR EMDB; EMD-13473; -. DR EMDB; EMD-14098; -. DR EMDB; EMD-14336; -. DR EMDB; EMD-14341; -. DR EMDB; EMD-14351; -. DR EMDB; EMD-14375; -. DR EMDB; EMD-33197; -. DR SMR; Q9H3R5; -. DR BioGRID; 122355; 93. DR ComplexPortal; CPX-5646; Kinetochore CCAN complex. DR CORUM; Q9H3R5; -. DR IntAct; Q9H3R5; 58. DR MINT; Q9H3R5; -. DR STRING; 9606.ENSP00000283006; -. DR GlyGen; Q9H3R5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H3R5; -. DR PhosphoSitePlus; Q9H3R5; -. DR BioMuta; CENPH; -. DR DMDM; 74733576; -. DR EPD; Q9H3R5; -. DR jPOST; Q9H3R5; -. DR MassIVE; Q9H3R5; -. DR MaxQB; Q9H3R5; -. DR PaxDb; 9606-ENSP00000283006; -. DR PeptideAtlas; Q9H3R5; -. DR ProteomicsDB; 80745; -. DR Pumba; Q9H3R5; -. DR Antibodypedia; 23919; 442 antibodies from 30 providers. DR DNASU; 64946; -. DR Ensembl; ENST00000283006.7; ENSP00000283006.2; ENSG00000153044.10. DR GeneID; 64946; -. DR KEGG; hsa:64946; -. DR MANE-Select; ENST00000283006.7; ENSP00000283006.2; NM_022909.4; NP_075060.1. DR UCSC; uc003jvp.3; human. DR AGR; HGNC:17268; -. DR CTD; 64946; -. DR DisGeNET; 64946; -. DR GeneCards; CENPH; -. DR HGNC; HGNC:17268; CENPH. DR HPA; ENSG00000153044; Tissue enhanced (bone marrow, testis). DR MIM; 605607; gene. DR neXtProt; NX_Q9H3R5; -. DR OpenTargets; ENSG00000153044; -. DR PharmGKB; PA26402; -. DR VEuPathDB; HostDB:ENSG00000153044; -. DR eggNOG; ENOG502S0VG; Eukaryota. DR GeneTree; ENSGT00390000009578; -. DR InParanoid; Q9H3R5; -. DR OMA; KSHQESW; -. DR OrthoDB; 5393856at2759; -. DR PhylomeDB; Q9H3R5; -. DR TreeFam; TF101134; -. DR PathwayCommons; Q9H3R5; -. DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR SignaLink; Q9H3R5; -. DR SIGNOR; Q9H3R5; -. DR BioGRID-ORCS; 64946; 448 hits in 1128 CRISPR screens. DR ChiTaRS; CENPH; human. DR GeneWiki; CENPH; -. DR GenomeRNAi; 64946; -. DR Pharos; Q9H3R5; Tbio. DR PRO; PR:Q9H3R5; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9H3R5; Protein. DR Bgee; ENSG00000153044; Expressed in primordial germ cell in gonad and 121 other cell types or tissues. DR ExpressionAtlas; Q9H3R5; baseline and differential. DR GO; GO:0005694; C:chromosome; IDA:HPA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000939; C:inner kinetochore; IPI:ComplexPortal. DR GO; GO:0000776; C:kinetochore; IDA:MGI. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043515; F:kinetochore binding; IDA:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central. DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro. DR GO; GO:0051383; P:kinetochore organization; TAS:UniProtKB. DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central. DR InterPro; IPR040034; CENP-H. DR InterPro; IPR008426; CENP-H_C. DR PANTHER; PTHR48122; CENTROMERE PROTEIN H; 1. DR PANTHER; PTHR48122:SF1; CENTROMERE PROTEIN H; 1. DR Pfam; PF05837; CENP-H; 1. DR Genevisible; Q9H3R5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Centromere; Chromosome; Coiled coil; KW Isopeptide bond; Kinetochore; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..247 FT /note="Centromere protein H" FT /id="PRO_0000089478" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 47..192 FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 68 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 67 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 2 FT /note="E -> K (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs777698677)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036167" FT HELIX 36..64 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 76..113 FT /evidence="ECO:0007829|PDB:7R5S" FT TURN 114..117 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 118..121 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 126..187 FT /evidence="ECO:0007829|PDB:7R5S" FT TURN 188..191 FT /evidence="ECO:0007829|PDB:7XHO" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 201..223 FT /evidence="ECO:0007829|PDB:7PB4" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:7PB4" FT HELIX 231..237 FT /evidence="ECO:0007829|PDB:7PB4" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:7R5S" SQ SEQUENCE 247 AA; 28481 MW; E1BCD4022710168F CRC64; MEEQPQMQDA DEPADSGGEG RAGGPPQVAG AQAACSEDRM TLLLRLRAQT KQQLLEYKSM VDASEEKTPE QIMQEKQIEA KIEDLENEIE EVKVAFEIKK LALDRMRLST ALKKNLEKIS RQSSVLMDNM KHLLELNKLI MKSQQESWDL EEKLLDIRKK RLQLKQASES KLLEIQTEKN KQKIDLDSME NSERIKIIRQ NLQMEIKITT VIQHVFQNLI LGSKVNWAED PALKEIVLQL EKNVDMM //