ID ARM10_HUMAN Reviewed; 343 AA. AC Q8N2F6; A8K703; B4DWJ8; F5GX65; Q75K91; Q75MG6; Q75ML8; Q8IZC1; Q8IZC2; AC Q8IZC3; Q9BTM6; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 154. DE RecName: Full=Armadillo repeat-containing protein 10; DE AltName: Full=Splicing variant involved in hepatocarcinogenesis protein; GN Name=ARMC10; Synonyms=SVH; ORFNames=PSEC0198; 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] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Hepatoma; RX PubMed=12839973; RA Huang R., Xing Z., Luan Z., Wu T., Wu X., Hu G.; RT "A specific splicing variant of SVH, a novel human armadillo repeat RT protein, is up-regulated in hepatocellular carcinomas."; RL Cancer Res. 63:3775-3782(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryo; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5). RC TISSUE=Mammary gland, and Prostate; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-190. RC TISSUE=Eye; 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 [6] RP PROTEIN SEQUENCE OF 45-100 (ISOFORM 2), INTERACTION WITH TP53, AND RP FUNCTION. RX PubMed=17904127; DOI=10.1016/j.febslet.2007.09.025; RA Zhou X., Yang G., Huang R., Chen X., Hu G.; RT "SVH-B interacts directly with p53 and suppresses the transcriptional RT activity of p53."; RL FEBS Lett. 581:4943-4948(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 (ISOFORMS 2; 4; 5 AND 6), RP AND 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 (ISOFORMS 2; 4; 5 AND 6), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-50 (ISOFORMS 2; 4; RP 5 AND 6), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP IDENTIFICATION BY 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 [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 (ISOFORMS 2; 4; 5 AND 6), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, 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). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 (ISOFORMS 2; 4; 5 AND 6), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [16] RP SUBCELLULAR LOCATION (ISOFORM 2). RX PubMed=27184847; DOI=10.1016/j.celrep.2016.04.064; RA Lee S.Y., Kang M.G., Park J.S., Lee G., Ting A.Y., Rhee H.W.; RT "APEX Fingerprinting Reveals the Subcellular Localization of Proteins of RT Interest."; RL Cell Rep. 15:1837-1847(2016). CC -!- FUNCTION: May play a role in cell survival and cell growth. May CC suppress the transcriptional activity of p53/TP53. CC {ECO:0000269|PubMed:12839973, ECO:0000269|PubMed:17904127}. CC -!- SUBUNIT: Interacts with the DNA-binding domain of p53/TP53. CC {ECO:0000269|PubMed:17904127}. CC -!- INTERACTION: CC Q8N2F6-2; Q96L46: CAPNS2; NbExp=3; IntAct=EBI-12902762, EBI-12188723; CC Q8N2F6-2; B3EWG5: FAM25C; NbExp=5; IntAct=EBI-12902762, EBI-14240149; CC Q8N2F6-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-12902762, EBI-358489; CC Q8N2F6-2; Q15560: TCEA2; NbExp=3; IntAct=EBI-12902762, EBI-710310; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12839973}; Single-pass membrane protein CC {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion outer membrane CC {ECO:0000269|PubMed:27184847}; Single-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=SVH-A; CC IsoId=Q8N2F6-1; Sequence=Displayed; CC Name=2; Synonyms=SVH-B; CC IsoId=Q8N2F6-2; Sequence=VSP_027361; CC Name=3; Synonyms=SVH-C; CC IsoId=Q8N2F6-3; Sequence=VSP_027362; CC Name=4; Synonyms=SVH-D; CC IsoId=Q8N2F6-4; Sequence=VSP_027361, VSP_027362; CC Name=5; CC IsoId=Q8N2F6-5; Sequence=VSP_027361, VSP_043290; CC Name=6; CC IsoId=Q8N2F6-6; Sequence=VSP_027361, VSP_047404; CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested with higher CC expression in placenta, liver, kidney, heart and brain. CC {ECO:0000269|PubMed:12839973}. CC -!- MISCELLANEOUS: Depletion of isoform 2 results in cell apoptosis while CC its overexpression in cells leads to accelerated growth rate and CC tumorogenicity. CC -!- SEQUENCE CAUTION: CC Sequence=AAS07482.1; Type=Erroneous gene model prediction; 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; AY150851; AAN72313.1; -; mRNA. DR EMBL; AY150852; AAN72314.1; -; mRNA. DR EMBL; AY150853; AAN72315.1; -; mRNA. DR EMBL; AY150854; AAN72316.1; -; mRNA. DR EMBL; AK075500; BAC11655.1; -; mRNA. DR EMBL; AK291818; BAF84507.1; -; mRNA. DR EMBL; AK301565; BAG63060.1; -; mRNA. DR EMBL; AC007683; AAS07531.1; -; Genomic_DNA. DR EMBL; AC073127; AAS07482.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC108167; AAS07456.1; -; Genomic_DNA. DR EMBL; BC003586; AAH03586.1; -; mRNA. DR CCDS; CCDS55145.1; -. [Q8N2F6-3] DR CCDS; CCDS55146.1; -. [Q8N2F6-2] DR CCDS; CCDS55147.1; -. [Q8N2F6-5] DR CCDS; CCDS55148.1; -. [Q8N2F6-4] DR CCDS; CCDS55149.1; -. [Q8N2F6-6] DR CCDS; CCDS5728.1; -. [Q8N2F6-1] DR RefSeq; NP_001154481.1; NM_001161009.2. [Q8N2F6-2] DR RefSeq; NP_001154482.1; NM_001161010.2. [Q8N2F6-3] DR RefSeq; NP_001154483.1; NM_001161011.2. [Q8N2F6-5] DR RefSeq; NP_001154484.1; NM_001161012.2. [Q8N2F6-4] DR RefSeq; NP_001154485.1; NM_001161013.2. [Q8N2F6-6] DR RefSeq; NP_114111.2; NM_031905.4. [Q8N2F6-1] DR AlphaFoldDB; Q8N2F6; -. DR SMR; Q8N2F6; -. DR BioGRID; 123762; 38. DR IntAct; Q8N2F6; 8. DR MINT; Q8N2F6; -. DR STRING; 9606.ENSP00000319412; -. DR iPTMnet; Q8N2F6; -. DR PhosphoSitePlus; Q8N2F6; -. DR SwissPalm; Q8N2F6; -. DR BioMuta; ARMC10; -. DR DMDM; 74714720; -. DR EPD; Q8N2F6; -. DR jPOST; Q8N2F6; -. DR MassIVE; Q8N2F6; -. DR MaxQB; Q8N2F6; -. DR PaxDb; 9606-ENSP00000319412; -. DR PeptideAtlas; Q8N2F6; -. DR ProteomicsDB; 24326; -. DR ProteomicsDB; 71688; -. [Q8N2F6-1] DR ProteomicsDB; 71689; -. [Q8N2F6-2] DR ProteomicsDB; 71690; -. [Q8N2F6-3] DR ProteomicsDB; 71691; -. [Q8N2F6-4] DR ProteomicsDB; 71692; -. [Q8N2F6-5] DR Pumba; Q8N2F6; -. DR Antibodypedia; 2627; 200 antibodies from 26 providers. DR DNASU; 83787; -. DR Ensembl; ENST00000323716.8; ENSP00000319412.3; ENSG00000170632.14. [Q8N2F6-1] DR Ensembl; ENST00000425331.5; ENSP00000397969.1; ENSG00000170632.14. [Q8N2F6-5] DR Ensembl; ENST00000428183.6; ENSP00000396654.2; ENSG00000170632.14. [Q8N2F6-3] DR Ensembl; ENST00000441711.6; ENSP00000413619.2; ENSG00000170632.14. [Q8N2F6-2] DR Ensembl; ENST00000454559.5; ENSP00000405612.1; ENSG00000170632.14. [Q8N2F6-4] DR Ensembl; ENST00000541300.5; ENSP00000440463.1; ENSG00000170632.14. [Q8N2F6-6] DR GeneID; 83787; -. DR KEGG; hsa:83787; -. DR MANE-Select; ENST00000323716.8; ENSP00000319412.3; NM_031905.5; NP_114111.2. DR UCSC; uc003vaw.3; human. [Q8N2F6-1] DR AGR; HGNC:21706; -. DR CTD; 83787; -. DR DisGeNET; 83787; -. DR GeneCards; ARMC10; -. DR HGNC; HGNC:21706; ARMC10. DR HPA; ENSG00000170632; Low tissue specificity. DR MIM; 611864; gene. DR neXtProt; NX_Q8N2F6; -. DR OpenTargets; ENSG00000170632; -. DR PharmGKB; PA162376895; -. DR VEuPathDB; HostDB:ENSG00000170632; -. DR eggNOG; ENOG502RZRU; Eukaryota. DR GeneTree; ENSGT00940000159546; -. DR HOGENOM; CLU_037187_0_0_1; -. DR InParanoid; Q8N2F6; -. DR OMA; VFITQVC; -. DR OrthoDB; 2912889at2759; -. DR PhylomeDB; Q8N2F6; -. DR TreeFam; TF335652; -. DR PathwayCommons; Q8N2F6; -. DR SignaLink; Q8N2F6; -. DR SIGNOR; Q8N2F6; -. DR BioGRID-ORCS; 83787; 53 hits in 1120 CRISPR screens. DR ChiTaRS; ARMC10; human. DR GenomeRNAi; 83787; -. DR Pharos; Q8N2F6; Tbio. DR PRO; PR:Q8N2F6; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q8N2F6; Protein. DR Bgee; ENSG00000170632; Expressed in prefrontal cortex and 106 other cell types or tissues. DR ExpressionAtlas; Q8N2F6; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0050692; F:DNA binding domain binding; IDA:UniProtKB. DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB. DR GO; GO:0040010; P:positive regulation of growth rate; IDA:UniProtKB. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR006911; ARM-rpt_dom. DR InterPro; IPR016024; ARM-type_fold. DR PANTHER; PTHR15712:SF23; ARM_2 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR15712; ARMADILLO REPEAT CONTAINING PROTEIN; 1. DR Pfam; PF04826; Arm_2; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q8N2F6; HS. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Endoplasmic reticulum; KW Growth regulation; Membrane; Mitochondrion; Mitochondrion outer membrane; KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..343 FT /note="Armadillo repeat-containing protein 10" FT /id="PRO_0000297707" FT TRANSMEM 5..27 FT /note="Helical" FT /evidence="ECO:0000255" FT REPEAT 138..180 FT /note="ARM" FT REGION 43..83 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 59..83 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 85 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9D0L7" FT VAR_SEQ 47..81 FT /note="Missing (in isoform 2, isoform 4, isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:12839973, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_027361" FT VAR_SEQ 176..234 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:12839973" FT /id="VSP_027362" FT VAR_SEQ 177..259 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_047404" FT VAR_SEQ 236..259 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043290" FT VARIANT 190 FT /note="P -> S (in dbSNP:rs17849774)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_034681" FT CONFLICT 343 FT /note="I -> V (in Ref. 3; BAF84507)" FT /evidence="ECO:0000305" FT MOD_RES Q8N2F6-2:45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES Q8N2F6-2:50 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES Q8N2F6-4:45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES Q8N2F6-4:50 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES Q8N2F6-5:45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES Q8N2F6-5:50 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES Q8N2F6-6:45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES Q8N2F6-6:50 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" SQ SEQUENCE 343 AA; 37540 MW; 8DCA090DF3BBE759 CRC64; MGGPRGAGWV AAGLLLGAGA CYCIYRLTRG RRRGDRELGI RSSKSAGALE EGTSEGQLCG RSARPQTGGT WESQWSKTSQ PEDLTDGSYD DVLNAEQLQK LLYLLESTED PVIIERALIT LGNNAAFSVN QAIIRELGGI PIVANKINHS NQSIKEKALN ALNNLSVNVE NQIKIKIYIS QVCEDVFSGP LNSAVQLAGL TLLTNMTVTN DHQHMLHSYI TDLFQVLLTG NGNTKVQVLK LLLNLSENPA MTEGLLRAQV DSSFLSLYDS HVAKEILLRV LTLFQNIKNC LKIEGHLAVQ PTFTEGSLFF LLHGEECAQK IRALVDHHDA EVKEKVVTII PKI //