ARM10_HUMAN
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 03-AUG-2022, entry version 145.
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).
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:0000269|PubMed:12839973}.
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};
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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; 36.
DR IntAct; Q8N2F6; 7.
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; Q8N2F6; -.
DR PeptideAtlas; Q8N2F6; -.
DR PRIDE; 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 Antibodypedia; 2627; 181 antibodies from 27 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 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; NNCLRVE; -.
DR OrthoDB; 860703at2759; -.
DR PhylomeDB; Q8N2F6; -.
DR TreeFam; TF335652; -.
DR PathwayCommons; Q8N2F6; -.
DR SignaLink; Q8N2F6; -.
DR SIGNOR; Q8N2F6; -.
DR BioGRID-ORCS; 83787; 53 hits in 1043 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 104 other tissues.
DR ExpressionAtlas; Q8N2F6; baseline and differential.
DR Genevisible; Q8N2F6; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR006911; ARM-rpt_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR Pfam; PF04826; Arm_2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Endoplasmic reticulum;
KW Growth regulation; Membrane; Phosphoprotein; Reference proteome;
KW 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
