ARMC5_HUMAN
ID ARMC5_HUMAN Reviewed; 935 AA.
AC Q96C12; Q86WM9; Q9H7P8; Q9H925;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Armadillo repeat-containing protein 5 {ECO:0000305};
GN Name=ARMC5 {ECO:0000312|HGNC:HGNC:25781};
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] (ISOFORM 4).
RA Shan Y.X., Yu L., Huang C.Q.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP VAL-170.
RC TISSUE=Spleen, and Teratocarcinoma;
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].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [7]
RP VARIANTS AIMAH2 PRO-548 AND TRP-898, FUNCTION, SUBCELLULAR LOCATION,
RP INVOLVEMENT IN AIMAH2, AND CHARACTERIZATION OF VARIANTS AIMAH2 PRO-548 AND
RP TRP-898.
RX PubMed=24283224; DOI=10.1056/nejmoa1304603;
RA Assie G., Libe R., Espiard S., Rizk-Rabin M., Guimier A., Luscap W.,
RA Barreau O., Lefevre L., Sibony M., Guignat L., Rodriguez S., Perlemoine K.,
RA Rene-Corail F., Letourneur F., Trabulsi B., Poussier A.,
RA Chabbert-Buffet N., Borson-Chazot F., Groussin L., Bertagna X.,
RA Stratakis C.A., Ragazzon B., Bertherat J.;
RT "ARMC5 mutations in macronodular adrenal hyperplasia with Cushing's
RT syndrome.";
RL N. Engl. J. Med. 369:2105-2114(2013).
RN [8]
RP VARIANTS AIMAH2 PHE-156; GLN-315; TRP-593 AND TRP-898, AND VARIANTS TYR-14;
RP PRO-115; VAL-170 AND ALA-798.
RX PubMed=24601692; DOI=10.1210/jc.2013-4280;
RA Faucz F.R., Zilbermint M., Lodish M.B., Szarek E., Trivellin G., Sinaii N.,
RA Berthon A., Libe R., Assie G., Espiard S., Drougat L., Ragazzon B.,
RA Bertherat J., Stratakis C.A.;
RT "Macronodular adrenal hyperplasia due to mutations in an armadillo repeat
RT containing 5 (ARMC5) gene: a clinical and genetic investigation.";
RL J. Clin. Endocrinol. Metab. 99:E1113-E1119(2014).
RN [9]
RP VARIANTS AIMAH2 VAL-318; PRO-365; 386-TRP--ALA-935 DEL; PRO-394; TRP-657;
RP 779-SER--ALA-935 DEL AND PRO-808.
RX PubMed=24708098; DOI=10.1210/jc.2013-4237;
RA Alencar G.A., Lerario A.M., Nishi M.Y., Mariani B.M., Almeida M.Q.,
RA Tremblay J., Hamet P., Bourdeau I., Zerbini M.C., Pereira M.A., Gomes G.C.,
RA Rocha Mde S., Chambo J.L., Lacroix A., Mendonca B.B., Fragoso M.C.;
RT "ARMC5 mutations are a frequent cause of primary macronodular adrenal
RT Hyperplasia.";
RL J. Clin. Endocrinol. Metab. 99:E1501-E1509(2014).
RN [10]
RP VARIANTS AIMAH2 TRP-315 AND TRP-593.
RX PubMed=24905064; DOI=10.1210/jc.2014-1265;
RA Gagliardi L., Schreiber A.W., Hahn C.N., Feng J., Cranston T., Boon H.,
RA Hotu C., Oftedal B.E., Cutfield R., Adelson D.L., Braund W.J., Gordon R.D.,
RA Rees D.A., Grossman A.B., Torpy D.J., Scott H.S.;
RT "ARMC5 mutations are common in familial bilateral macronodular adrenal
RT hyperplasia.";
RL J. Clin. Endocrinol. Metab. 99:E1784-E1792(2014).
RN [11]
RP VARIANTS TYR-14; VAL-170; LEU-507 AND ALA-798, AND VARIANTS AIMAH2 PHE-156;
RP ALA-323; MET-643; THR-826 AND TRP-898.
RX PubMed=25822102; DOI=10.1210/jc.2014-4167;
RA Zilbermint M., Xekouki P., Faucz F.R., Berthon A., Gkourogianni A.,
RA Schernthaner-Reiter M.H., Batsis M., Sinaii N., Quezado M.M., Merino M.,
RA Hodes A., Abraham S.B., Libe R., Assie G., Espiard S., Drougat L.,
RA Ragazzon B., Davis A., Gebreab S.Y., Neff R., Kebebew E., Bertherat J.,
RA Lodish M.B., Stratakis C.A.;
RT "Primary Aldosteronism and ARMC5 Variants.";
RL J. Clin. Endocrinol. Metab. 100:E900-E909(2015).
RN [12]
RP VARIANTS AIMAH2 31-LYS--ALA-935 DEL; 76-ARG--ALA-935 DEL; 86-GLN--ALA-935
RP DEL; ARG-139; 267-ARG--ALA-935 DEL; TRP-315; PRO-331; LEU-362;
RP 430-GLU--ALA-935 DEL; PRO-548; 619-ARG--ALA-935 DEL; ARG-657; SER-664;
RP PHE-700 DEL; 702-ALA--SER-706 DEL; SER-736; PRO-754; 764-ARG--ALA-935 DEL
RP AND TRP-898, AND CHARACTERIZATION OF VARIANTS AIMAH2 ARG-139; TRP-315;
RP PRO-331; LEU-362; ARG-657; SER-664; PHE-700 DEL; SER-736 AND PRO-754.
RX PubMed=25853793; DOI=10.1210/jc.2014-4204;
RA Espiard S., Drougat L., Libe R., Assie G., Perlemoine K., Guignat L.,
RA Barrande G., Brucker-Davis F., Doullay F., Lopez S., Sonnet E.,
RA Torremocha F., Pinsard D., Chabbert-Buffet N., Raffin-Sanson M.L.,
RA Groussin L., Borson-Chazot F., Coste J., Bertagna X., Stratakis C.A.,
RA Beuschlein F., Ragazzon B., Bertherat J.;
RT "ARMC5 Mutations in a Large Cohort of Primary Macronodular Adrenal
RT Hyperplasia: Clinical and Functional Consequences.";
RL J. Clin. Endocrinol. Metab. 100:E926-E935(2015).
RN [13]
RP INVOLVEMENT IN AIMAH2.
RX PubMed=26604299; DOI=10.1530/eje-15-0642;
RA Bourdeau I., Oble S., Magne F., Levesque I., Caceres-Gorriti K.Y.,
RA Nolet S., Awadalla P., Tremblay J., Hamet P., Fragoso M.C., Lacroix A.;
RT "ARMC5 mutations in a large French-Canadian family with cortisol-secreting
RT beta-adrenergic/vasopressin responsive bilateral macronodular adrenal
RT hyperplasia.";
RL Eur. J. Endocrinol. 174:85-96(2016).
RN [14]
RP VARIANTS TYR-14; VAL-170 AND HIS-502.
RX PubMed=26446392; DOI=10.1038/jhh.2015.98;
RA Mulatero P., Schiavi F., Williams T.A., Monticone S., Barbon G.,
RA Opocher G., Fallo F.;
RT "ARMC5 mutation analysis in patients with primary aldosteronism and
RT bilateral adrenal lesions.";
RL J. Hum. Hypertens. 30:374-378(2016).
RN [15]
RP VARIANTS ALA-56 AND LEU-483, AND VARIANTS AIMAH2 TRP-362; 364-ARG--ALA-935
RP DEL; PRO-580; ARG-731 AND 764-ARG--ALA-935 DEL.
RX PubMed=27094308; DOI=10.1007/s12020-016-0956-z;
RA Albiger N.M., Regazzo D., Rubin B., Ferrara A.M., Rizzati S., Taschin E.,
RA Ceccato F., Arnaldi G., Pecori Giraldi F., Stigliano A., Cerquetti L.,
RA Grimaldi F., De Menis E., Boscaro M., Iacobone M., Occhi G., Scaroni C.;
RT "A multicenter experience on the prevalence of ARMC5 mutations in patients
RT with primary bilateral macronodular adrenal hyperplasia: from genetic
RT characterization to clinical phenotype.";
RL Endocrine 55:959-968(2017).
RN [16]
RP INVOLVEMENT IN AIMAH2.
RX PubMed=28458897; DOI=10.1530/edm-16-0135;
RA Rego T., Fonseca F., Espiard S., Perlemoine K., Bertherat J., Agapito A.;
RT "ARMC5 mutation in a Portuguese family with primary bilateral macronodular
RT adrenal hyperplasia (PBMAH).";
RL Endocrinol. Diabetes Metab. Case Rep. 2017:0-0(2017).
RN [17]
RP INVOLVEMENT IN AIMAH2, AND FUNCTION.
RX PubMed=28676429; DOI=10.1016/j.mce.2017.06.027;
RA Cavalcante I.P., Nishi M., Zerbini M.C.N., Almeida M.Q., Brondani V.B.,
RA Botelho M.L.A.A., Tanno F.Y., Srougi V., Chambo J.L., Mendonca B.B.,
RA Bertherat J., Lotfi C.F.P., Fragoso M.C.B.V.;
RT "The role of ARMC5 in human cell cultures from nodules of primary
RT macronodular adrenocortical hyperplasia (PMAH).";
RL Mol. Cell. Endocrinol. 460:36-46(2018).
CC -!- FUNCTION: Involved in fetal development, T-cell function and adrenal
CC gland growth homeostasis (By similarity). Negatively regulates adrenal
CC cells survival. Plays a role in steroidogenesis, modulates
CC steroidogenic enzymes expression and cortisol production
CC (PubMed:24283224, PubMed:28676429). {ECO:0000250|UniProtKB:Q5EBP3,
CC ECO:0000269|PubMed:24283224, ECO:0000269|PubMed:28676429}.
CC -!- INTERACTION:
CC Q96C12; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-6425121, EBI-743033;
CC Q96C12; P27658: COL8A1; NbExp=3; IntAct=EBI-6425121, EBI-747133;
CC Q96C12; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-6425121, EBI-744099;
CC Q96C12; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-6425121, EBI-748515;
CC Q96C12; Q13064: MKRN3; NbExp=3; IntAct=EBI-6425121, EBI-2340269;
CC Q96C12; P0CG20: PRR35; NbExp=3; IntAct=EBI-6425121, EBI-11986293;
CC Q96C12; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-6425121, EBI-11959123;
CC Q96C12; O43711: TLX3; NbExp=3; IntAct=EBI-6425121, EBI-3939165;
CC Q96C12; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-6425121, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24283224}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96C12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96C12-2; Sequence=VSP_024505;
CC Name=3;
CC IsoId=Q96C12-3; Sequence=VSP_024505, VSP_024507;
CC Name=4;
CC IsoId=Q96C12-4; Sequence=VSP_024506, VSP_024508;
CC -!- DISEASE: ACTH-independent macronodular adrenal hyperplasia 2 (AIMAH2)
CC [MIM:615954]: A form of macronodular adrenal hyperplasia characterized
CC by multiple, bilateral, non-pigmented, benign, adrenocortical nodules.
CC It results in excessive production of cortisol leading to ACTH-
CC independent Cushing syndrome. Clinical manifestations of Cushing
CC syndrome include facial and truncal obesity, abdominal striae, muscular
CC weakness, osteoporosis, arterial hypertension, diabetes.
CC {ECO:0000269|PubMed:24283224, ECO:0000269|PubMed:24601692,
CC ECO:0000269|PubMed:24708098, ECO:0000269|PubMed:24905064,
CC ECO:0000269|PubMed:25822102, ECO:0000269|PubMed:25853793,
CC ECO:0000269|PubMed:26604299, ECO:0000269|PubMed:27094308,
CC ECO:0000269|PubMed:28458897, ECO:0000269|PubMed:28676429}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15720.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AY217348; AAO45101.1; -; mRNA.
DR EMBL; AK023125; BAB14418.1; -; mRNA.
DR EMBL; AK024430; BAB15720.1; ALT_INIT; mRNA.
DR EMBL; AC026471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014945; AAH14945.1; -; mRNA.
DR CCDS; CCDS42155.1; -. [Q96C12-4]
DR CCDS; CCDS45472.1; -. [Q96C12-1]
DR RefSeq; NP_001098717.1; NM_001105247.1. [Q96C12-1]
DR RefSeq; NP_001275696.1; NM_001288767.1.
DR RefSeq; NP_001288749.1; NM_001301820.1.
DR RefSeq; NP_079018.1; NM_024742.2. [Q96C12-4]
DR AlphaFoldDB; Q96C12; -.
DR SMR; Q96C12; -.
DR BioGRID; 122895; 43.
DR IntAct; Q96C12; 18.
DR STRING; 9606.ENSP00000386125; -.
DR iPTMnet; Q96C12; -.
DR PhosphoSitePlus; Q96C12; -.
DR BioMuta; ARMC5; -.
DR DMDM; 145558851; -.
DR EPD; Q96C12; -.
DR jPOST; Q96C12; -.
DR MassIVE; Q96C12; -.
DR MaxQB; Q96C12; -.
DR PaxDb; Q96C12; -.
DR PeptideAtlas; Q96C12; -.
DR PRIDE; Q96C12; -.
DR ProteomicsDB; 76146; -. [Q96C12-1]
DR ProteomicsDB; 76147; -. [Q96C12-2]
DR ProteomicsDB; 76148; -. [Q96C12-3]
DR ProteomicsDB; 76149; -. [Q96C12-4]
DR Antibodypedia; 51623; 84 antibodies from 19 providers.
DR DNASU; 79798; -.
DR Ensembl; ENST00000268314.9; ENSP00000268314.4; ENSG00000140691.18. [Q96C12-1]
DR Ensembl; ENST00000457010.6; ENSP00000399561.2; ENSG00000140691.18. [Q96C12-4]
DR Ensembl; ENST00000563544.5; ENSP00000456877.1; ENSG00000140691.18. [Q96C12-1]
DR GeneID; 79798; -.
DR KEGG; hsa:79798; -.
DR MANE-Select; ENST00000268314.9; ENSP00000268314.4; NM_001105247.2; NP_001098717.1.
DR UCSC; uc002eca.5; human. [Q96C12-1]
DR CTD; 79798; -.
DR DisGeNET; 79798; -.
DR GeneCards; ARMC5; -.
DR HGNC; HGNC:25781; ARMC5.
DR HPA; ENSG00000140691; Low tissue specificity.
DR MalaCards; ARMC5; -.
DR MIM; 615549; gene.
DR MIM; 615954; phenotype.
DR neXtProt; NX_Q96C12; -.
DR OpenTargets; ENSG00000140691; -.
DR Orphanet; 189427; Cushing syndrome due to macronodular adrenal hyperplasia.
DR PharmGKB; PA134926941; -.
DR VEuPathDB; HostDB:ENSG00000140691; -.
DR eggNOG; ENOG502QSYU; Eukaryota.
DR GeneTree; ENSGT00390000009109; -.
DR HOGENOM; CLU_007517_2_0_1; -.
DR InParanoid; Q96C12; -.
DR OrthoDB; 174815at2759; -.
DR PhylomeDB; Q96C12; -.
DR TreeFam; TF337762; -.
DR PathwayCommons; Q96C12; -.
DR SignaLink; Q96C12; -.
DR BioGRID-ORCS; 79798; 190 hits in 1115 CRISPR screens.
DR ChiTaRS; ARMC5; human.
DR GenomeRNAi; 79798; -.
DR Pharos; Q96C12; Tbio.
DR PRO; PR:Q96C12; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96C12; protein.
DR Bgee; ENSG00000140691; Expressed in tendon of biceps brachii and 180 other tissues.
DR ExpressionAtlas; Q96C12; baseline and differential.
DR Genevisible; Q96C12; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0035801; P:adrenal cortex development; IEA:Ensembl.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR SMART; SM00185; ARM; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cushing syndrome; Cytoplasm; Disease variant;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..935
FT /note="Armadillo repeat-containing protein 5"
FT /id="PRO_0000284405"
FT REPEAT 143..183
FT /note="ARM 1"
FT REPEAT 185..225
FT /note="ARM 2"
FT REPEAT 227..267
FT /note="ARM 3"
FT REPEAT 271..310
FT /note="ARM 4"
FT REPEAT 312..357
FT /note="ARM 5"
FT REPEAT 359..403
FT /note="ARM 6"
FT REPEAT 405..444
FT /note="ARM 7"
FT DOMAIN 748..816
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 82..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024505"
FT VAR_SEQ 624..725
FT /note="RLLQNLTVQAESPFGVGALTHLLLSGSPEDRVACALTLPFICRKPSLWRRLL
FT LEQGGLRLLLAALTRPAPHPLFLFFAADSLSCLQDLVSPTVSPAVPQAVP -> FPYPP
FT VSLPPCESPSSPMASMGPEPHLPTHLSSPARPPDNLSPEWGGEQGVPVPPWAHRQSSAV
FT SSALALGPRYPNSRCSPAPRIWAGLCFFPGSAIGSALS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_024506"
FT VAR_SEQ 667..935
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024507"
FT VAR_SEQ 726..935
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_024508"
FT VARIANT 14
FT /note="F -> Y (in dbSNP:rs151069962)"
FT /evidence="ECO:0000269|PubMed:24601692,
FT ECO:0000269|PubMed:25822102, ECO:0000269|PubMed:26446392"
FT /id="VAR_072352"
FT VARIANT 31..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079096"
FT VARIANT 56
FT /note="G -> A (in dbSNP:rs780112907)"
FT /evidence="ECO:0000269|PubMed:27094308"
FT /id="VAR_079097"
FT VARIANT 76..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079098"
FT VARIANT 86..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079099"
FT VARIANT 115
FT /note="S -> P (in dbSNP:rs199693319)"
FT /evidence="ECO:0000269|PubMed:24601692"
FT /id="VAR_072353"
FT VARIANT 139
FT /note="C -> R (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079100"
FT VARIANT 156
FT /note="L -> F (in AIMAH2; dbSNP:rs114930262)"
FT /evidence="ECO:0000269|PubMed:24601692,
FT ECO:0000269|PubMed:25822102"
FT /id="VAR_072354"
FT VARIANT 170
FT /note="I -> V (in dbSNP:rs35923277)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:24601692, ECO:0000269|PubMed:25822102,
FT ECO:0000269|PubMed:26446392"
FT /id="VAR_050674"
FT VARIANT 267..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079101"
FT VARIANT 315
FT /note="R -> Q (in AIMAH2; dbSNP:rs1415974570)"
FT /evidence="ECO:0000269|PubMed:24601692"
FT /id="VAR_072355"
FT VARIANT 315
FT /note="R -> W (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:24905064,
FT ECO:0000269|PubMed:25853793"
FT /id="VAR_072356"
FT VARIANT 318
FT /note="L -> V (in AIMAH2; unknown pathological
FT significance; dbSNP:rs1293014259)"
FT /evidence="ECO:0000269|PubMed:24708098"
FT /id="VAR_079102"
FT VARIANT 323
FT /note="G -> A (in AIMAH2; unknown pathological
FT significance; dbSNP:rs35461188)"
FT /evidence="ECO:0000269|PubMed:25822102"
FT /id="VAR_079103"
FT VARIANT 331
FT /note="L -> P (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079104"
FT VARIANT 362
FT /note="R -> L (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079105"
FT VARIANT 362
FT /note="R -> W (in AIMAH2; dbSNP:rs1385397608)"
FT /evidence="ECO:0000269|PubMed:27094308"
FT /id="VAR_079106"
FT VARIANT 364..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:27094308"
FT /id="VAR_079107"
FT VARIANT 365
FT /note="L -> P (in AIMAH2; dbSNP:rs587777663)"
FT /evidence="ECO:0000269|PubMed:24708098"
FT /id="VAR_079108"
FT VARIANT 386..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:24708098"
FT /id="VAR_079109"
FT VARIANT 394
FT /note="L -> P (in AIMAH2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24708098"
FT /id="VAR_079110"
FT VARIANT 430..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079111"
FT VARIANT 483
FT /note="P -> L (in dbSNP:rs552657393)"
FT /evidence="ECO:0000269|PubMed:27094308"
FT /id="VAR_079112"
FT VARIANT 502
FT /note="R -> H (in dbSNP:rs200054015)"
FT /evidence="ECO:0000269|PubMed:26446392"
FT /id="VAR_079113"
FT VARIANT 507
FT /note="P -> L (in dbSNP:rs142376949)"
FT /evidence="ECO:0000269|PubMed:25822102"
FT /id="VAR_079114"
FT VARIANT 548
FT /note="L -> P (in AIMAH2; loss of function in promoting
FT apoptosis; unknown pathological significance;
FT dbSNP:rs587777661)"
FT /evidence="ECO:0000269|PubMed:24283224,
FT ECO:0000269|PubMed:25853793"
FT /id="VAR_072357"
FT VARIANT 580
FT /note="L -> P (in AIMAH2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27094308"
FT /id="VAR_079115"
FT VARIANT 593
FT /note="R -> W (in AIMAH2; dbSNP:rs587777662)"
FT /evidence="ECO:0000269|PubMed:24601692,
FT ECO:0000269|PubMed:24905064"
FT /id="VAR_072358"
FT VARIANT 619..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079116"
FT VARIANT 643
FT /note="T -> M (in AIMAH2; unknown pathological
FT significance; dbSNP:rs370836071)"
FT /evidence="ECO:0000269|PubMed:25822102"
FT /id="VAR_079117"
FT VARIANT 657
FT /note="C -> R (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079118"
FT VARIANT 657
FT /note="C -> W (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:24708098"
FT /id="VAR_079119"
FT VARIANT 664
FT /note="I -> S (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079120"
FT VARIANT 700
FT /note="Missing (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079121"
FT VARIANT 702..706
FT /note="Missing (in AIMAH2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079122"
FT VARIANT 731
FT /note="P -> R (in AIMAH2; dbSNP:rs200951744)"
FT /evidence="ECO:0000269|PubMed:27094308"
FT /id="VAR_079123"
FT VARIANT 736
FT /note="Y -> S (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079124"
FT VARIANT 754
FT /note="L -> P (in AIMAH2; loss of function in promoting
FT apoptosis)"
FT /evidence="ECO:0000269|PubMed:25853793"
FT /id="VAR_079125"
FT VARIANT 764..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:25853793,
FT ECO:0000269|PubMed:27094308"
FT /id="VAR_079126"
FT VARIANT 779..935
FT /note="Missing (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:24708098"
FT /id="VAR_079127"
FT VARIANT 798
FT /note="G -> A (in dbSNP:rs115611533)"
FT /evidence="ECO:0000269|PubMed:24601692,
FT ECO:0000269|PubMed:25822102"
FT /id="VAR_072359"
FT VARIANT 808
FT /note="H -> P (in AIMAH2)"
FT /evidence="ECO:0000269|PubMed:24708098"
FT /id="VAR_079128"
FT VARIANT 826
FT /note="P -> T (in AIMAH2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25822102"
FT /id="VAR_079129"
FT VARIANT 898
FT /note="R -> W (in AIMAH2; loss of function in promoting
FT apoptosis; dbSNP:rs587777659)"
FT /evidence="ECO:0000269|PubMed:24283224,
FT ECO:0000269|PubMed:24601692, ECO:0000269|PubMed:25822102,
FT ECO:0000269|PubMed:25853793"
FT /id="VAR_072360"
SQ SEQUENCE 935 AA; 97682 MW; EA2F94BA028C3B1C CRC64;
MAAAKPTLTD SLSFCLAQLA AAAGEALGGE KDPATNETPL SRALLALRTR HIKAAGGIER
FRARGGLRPL LALLRRAAAA GSAPSQAGPG SAPSSAASGA SSPAPASGPA PSAVSSSSPT
PPVRLRKTLD LALSILADCC TEGACRTEVR RLGGILPLVT ILQCMKTDSI QNRTARALGN
LAMEPESCGD IHCAGAVPLL VESLTACQDS QCLQSVVRAL RNLADSPQHR LALAQQGAVR
PLAELLATAP DAALTLALVR ALLELSRGCS RACAEQLSLG GGLGPLVSLA SHPKRAVREG
TILILANLCA QGLIRPALGN AGGVEVLVDE LRQRRDPNGA SPTSQQPLVR AVCLLCREAI
NRARLRDAGG LDLLMGLLRD PRASAWHPRI VAALVGFLYD TGALGRLQAL GLVPLLAGQL
CGEAGEEEEE GREAASWDFP EERTPERAQG GSFRSLRSWL ISEGYATGPD DISPDWSPEQ
CPPEPMEPAS PAPTPTSLRA PRTQRTPGRS PAAAIEEPWG REGPALLLLS RFSQAPDPSG
ALVTGPALYG LLTYVTGAPG PPSPRALRIL SRLTCNPACL EAFVRSYGAA LLRAWLVLGV
APDDWPAPRA RPTLHSRHRE LGERLLQNLT VQAESPFGVG ALTHLLLSGS PEDRVACALT
LPFICRKPSL WRRLLLEQGG LRLLLAALTR PAPHPLFLFF AADSLSCLQD LVSPTVSPAV
PQAVPMDLDS PSPCLYEPLL GPAPVPAPDL HFLLDSGLQL PAQRAASATA SPFFRALLSG
SFAEAQMDLV PLRGLSPGAA WPVLHHLHGC RGCGAALGPV PPPGQPLLGS EAEEALEAAG
RFLLPGLEEE LEEAVGRIHL GPQGGPESVG EVFRLGRPRL AAHCARWTLG SEQCPRKRGL
ALVGLVEAAG EEAGPLTEAL LAVVMGIELG ARVPA
