ID ANR40_HUMAN Reviewed; 368 AA. AC Q6AI12; Q96E32; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 02-SEP-2026, entry version 156. DE RecName: Full=Ankyrin repeat domain-containing protein 40; GN Name=ANKRD40; 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 [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; 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 [3] RP PROTEIN SEQUENCE OF 1-13 AND 178-198, ACETYLATION AT MET-1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lempens A., Norman J.C.; RL Submitted (OCT-2009) to UniProtKB. RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [5] 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). CC -!- INTERACTION: CC Q6AI12; P23526: AHCY; NbExp=10; IntAct=EBI-2838246, EBI-1053240; CC Q6AI12; P51114: FXR1; NbExp=2; IntAct=EBI-2838246, EBI-713291; CC Q6AI12; P01374: LTA; NbExp=3; IntAct=EBI-2838246, EBI-524105; CC Q6AI12; Q13526: PIN1; NbExp=6; IntAct=EBI-2838246, EBI-714158; CC Q6AI12; P54725: RAD23A; NbExp=3; IntAct=EBI-2838246, EBI-746453; CC Q6AI12; Q8NDN9: RCBTB1; NbExp=2; IntAct=EBI-2838246, EBI-2811558; CC Q6AI12; P40938: RFC3; NbExp=3; IntAct=EBI-2838246, EBI-1055010; CC Q6AI12; O00560: SDCBP; NbExp=3; IntAct=EBI-2838246, EBI-727004; CC Q6AI12; Q96C45: ULK4; NbExp=2; IntAct=EBI-2838246, EBI-3922541; 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; CR627413; CAH10502.1; -; mRNA. DR EMBL; BC012978; AAH12978.1; -; mRNA. DR CCDS; CCDS11572.1; -. DR RefSeq; NP_443087.1; NM_052855.4. DR AlphaFoldDB; Q6AI12; -. DR SMR; Q6AI12; -. DR BioGRID; 124821; 123. DR FunCoup; Q6AI12; 108. DR IntAct; Q6AI12; 73. DR MINT; Q6AI12; -. DR STRING; 9606.ENSP00000285243; -. DR GlyCosmos; Q6AI12; 1 site, 1 glycan. DR GlyGen; Q6AI12; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q6AI12; -. DR PhosphoSitePlus; Q6AI12; -. DR BioMuta; ANKRD40; -. DR DMDM; 109940224; -. DR jPOST; Q6AI12; -. DR MassIVE; Q6AI12; -. DR PaxDb; 9606-ENSP00000285243; -. DR PeptideAtlas; Q6AI12; -. DR ProteomicsDB; 66185; -. DR Pumba; Q6AI12; -. DR Antibodypedia; 18157; 123 antibodies from 17 providers. DR DNASU; 91369; -. DR Ensembl; ENST00000285243.7; ENSP00000285243.6; ENSG00000154945.8. DR GeneID; 91369; -. DR KEGG; hsa:91369; -. DR MANE-Select; ENST00000285243.7; ENSP00000285243.6; NM_052855.4; NP_443087.1. DR UCSC; uc002iso.4; human. DR AGR; HGNC:28233; -. DR ClinPGx; PA142672607; -. DR CTD; 91369; -. DR DisGeNET; 91369; -. DR GeneCards; ANKRD40; -. DR HGNC; HGNC:28233; ANKRD40. DR HPA; ENSG00000154945; Tissue enhanced (brain). DR OpenTargets; ENSG00000154945; -. DR VEuPathDB; HostDB:ENSG00000154945; -. DR eggNOG; KOG0307; Eukaryota. DR GeneTree; ENSGT00390000007792; -. DR HOGENOM; CLU_068367_0_0_1; -. DR InParanoid; Q6AI12; -. DR OMA; DYTEDTQ; -. DR OrthoDB; 194358at2759; -. DR PAN-GO; Q6AI12; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q6AI12; -. DR PathwayCommons; Q6AI12; -. DR SignaLink; Q6AI12; -. DR Agora; ENSG00000154945; -. DR BioGRID-ORCS; 91369; 19 hits in 1152 CRISPR screens. DR ChiTaRS; ANKRD40; human. DR GenomeRNAi; 91369; -. DR Pharos; Q6AI12; Tdark. DR PRO; PR:Q6AI12; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q6AI12; protein. DR Bgee; ENSG00000154945; Expressed in medial globus pallidus and 198 other cell types or tissues. DR ExpressionAtlas; Q6AI12; baseline and differential. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR InterPro; IPR039195; ANKRD40. DR InterPro; IPR060551; ANKRD40-like_UBL. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR PANTHER; PTHR24192; ANKYRIN REPEAT DOMAIN 40; 1. DR PANTHER; PTHR24192:SF1; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 40; 1. DR Pfam; PF13637; Ank_4; 1. DR Pfam; PF27687; ANKRD40_UBL; 1. DR SMART; SM00248; ANK; 2. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. PE 1: Evidence at protein level; KW Acetylation; ANK repeat; Direct protein sequencing; KW Proteomics identification; Reference proteome; Repeat. FT CHAIN 1..368 FT /note="Ankyrin repeat domain-containing protein 40" FT /id="PRO_0000244368" FT REPEAT 9..38 FT /note="ANK 1" FT REPEAT 43..72 FT /note="ANK 2" FT REGION 93..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 139..176 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 196..238 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 95..107 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..169 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 212..224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CONFLICT 352 FT /note="T -> A (in Ref. 1; CAH10502)" FT /evidence="ECO:0000305" SQ SEQUENCE 368 AA; 41088 MW; 17999B7FDD3C6A52 CRC64; MNALLEQKEQ QERLREAAAL GDIREVQKLV ESGVDVNSQN EVNGWTCLHW ACKRNHGQVV SYLLKSGADK EILTTKGEMP VQLTSRREIR KIMGVEEEDD DDDDDDNLPQ LKKESELPFV PNYLANPAFP FIYTPTAEDS AQMQNGGPST PPASPPADGS PPLLPPGEPP LLGTFPRDHT SLALVQNGDV SAPSAILRTP ESTKPGPVCQ PPVSQSRSLF SSVPSKPPMS LEPQNGTYAG PAPAFQPFFF TGAFPFNMQE LVLKVRIQNP SLRENDFIEI ELDRQELTYQ ELLRVCCCEL GVNPDQVEKI RKLPNTLLRK DKDVARLQDF QELELVLMIS ENNFLFRNAA STLTERPCYN RRASKLTY //