ID ANS1A_HUMAN Reviewed; 1134 AA. AC Q92625; A2RUC1; B4DQW8; Q5JYI9; Q5SYR2; Q86WQ7; DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 199. DE RecName: Full=Ankyrin repeat and SAM domain-containing protein 1A; DE AltName: Full=Odin; GN Name=ANKS1A; Synonyms=ANKS1, KIAA0229, ODIN; 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] (ISOFORM 1), AND VARIANT SER-694. RC TISSUE=Bone marrow; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-694. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-694. 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 540-564, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS RP SPECTROMETRY, AND CHARACTERIZATION. RC TISSUE=Cervix carcinoma; RX PubMed=12439753; DOI=10.1038/sj.onc.1205988; RA Pandey A., Blagoev B., Kratchmarova I., Fernandez M., Nielsen M., RA Kristiansen T.Z., Ohara O., Podtelejnikov A.V., Roche S., Lodish H.F., RA Mann M.; RT "Cloning of a novel phosphotyrosine binding domain containing molecule, RT Odin, involved in signaling by receptor tyrosine kinases."; RL Oncogene 21:8029-8036(2002). RN [7] RP FUNCTION IN EFNA5-EPHA8 SIGNALING PATHWAY. RX PubMed=17875921; DOI=10.1128/mcb.00794-07; RA Shin J., Gu C., Park E., Park S.; RT "Identification of phosphotyrosine binding domain-containing proteins as RT novel downstream targets of the EphA8 signaling function."; RL Mol. Cell. Biol. 27:8113-8126(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-622; SER-647 AND RP SER-661, 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 [10] RP IDENTIFICATION BY MASS 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, VARIANT [LARGE SCALE RP ANALYSIS] SER-694, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-663, AND 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647; SER-661 AND SER-663, AND RP 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 [15] RP IDENTIFICATION BY MASS 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 THR-318; SER-620; SER-626; RP SER-647; SER-661; SER-663; SER-677 AND SER-887, AND IDENTIFICATION BY MASS RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507 AND SER-628, AND RP 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 [18] RP STRUCTURE BY NMR OF 691-770, AND INTERACTION WITH EPHA2. RX PubMed=22332920; DOI=10.1021/bi300141h; RA Mercurio F.A., Marasco D., Pirone L., Pedone E.M., Pellecchia M., Leone M.; RT "Solution structure of the first Sam domain of Odin and binding studies RT with the EphA2 receptor."; RL Biochemistry 51:2136-2145(2012). CC -!- FUNCTION: Regulator of different signaling pathways. Regulates EPHA8 CC receptor tyrosine kinase signaling to control cell migration and CC neurite retraction (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:17875921}. CC -!- SUBUNIT: Interacts (via SAM domain) with EPHA2 (via SAM domain) CC (PubMed:22332920). Interacts with EPHA8; EPHA8 kinase activity- CC independent but stimulated by EPHA8 ubiquitination. Interacts (via SAM CC domain) with EPHA6 (via SAM domain) (By similarity). CC {ECO:0000250|UniProtKB:P59672, ECO:0000269|PubMed:22332920}. CC -!- INTERACTION: CC Q92625; P00533: EGFR; NbExp=7; IntAct=EBI-1048612, EBI-297353; CC Q92625; P04626: ERBB2; NbExp=2; IntAct=EBI-1048612, EBI-641062; CC Q92625; P31947: SFN; NbExp=4; IntAct=EBI-1048612, EBI-476295; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection {ECO:0000250}. CC Note=Cytoplasmic before and after growth factor treatment. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92625-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92625-2; Sequence=VSP_056512, VSP_056513; CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). CC -!- PTM: Phosphorylated on tyrosine residues in response to EGF and PDGF. CC {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA13218.1; Type=Erroneous initiation; 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; D86982; BAA13218.1; ALT_INIT; mRNA. DR EMBL; AK298987; BAG61080.1; -; mRNA. DR EMBL; AL033520; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138721; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL591002; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03804.1; -; Genomic_DNA. DR EMBL; BC132832; AAI32833.1; -; mRNA. DR CCDS; CCDS4798.1; -. [Q92625-1] DR RefSeq; NP_056060.2; NM_015245.2. [Q92625-1] DR PDB; 2LMR; NMR; -; A=691-770. DR PDB; 2MYQ; NMR; -; A=715-757. DR PDB; 6F7O; NMR; -; A=745-757. DR PDBsum; 2LMR; -. DR PDBsum; 2MYQ; -. DR PDBsum; 6F7O; -. DR AlphaFoldDB; Q92625; -. DR BMRB; Q92625; -. DR SMR; Q92625; -. DR BioGRID; 116889; 169. DR IntAct; Q92625; 33. DR MINT; Q92625; -. DR STRING; 9606.ENSP00000353518; -. DR GlyGen; Q92625; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q92625; -. DR MetOSite; Q92625; -. DR PhosphoSitePlus; Q92625; -. DR BioMuta; ANKS1A; -. DR DMDM; 62511243; -. DR EPD; Q92625; -. DR jPOST; Q92625; -. DR MassIVE; Q92625; -. DR MaxQB; Q92625; -. DR PaxDb; 9606-ENSP00000353518; -. DR PeptideAtlas; Q92625; -. DR ProteomicsDB; 4910; -. DR ProteomicsDB; 75380; -. [Q92625-1] DR Pumba; Q92625; -. DR Antibodypedia; 29433; 128 antibodies from 20 providers. DR DNASU; 23294; -. DR Ensembl; ENST00000360359.5; ENSP00000353518.3; ENSG00000064999.16. [Q92625-1] DR GeneID; 23294; -. DR KEGG; hsa:23294; -. DR MANE-Select; ENST00000360359.5; ENSP00000353518.3; NM_015245.3; NP_056060.2. DR UCSC; uc003ojx.5; human. [Q92625-1] DR AGR; HGNC:20961; -. DR CTD; 23294; -. DR DisGeNET; 23294; -. DR GeneCards; ANKS1A; -. DR HGNC; HGNC:20961; ANKS1A. DR HPA; ENSG00000064999; Low tissue specificity. DR MIM; 608994; gene. DR neXtProt; NX_Q92625; -. DR OpenTargets; ENSG00000064999; -. DR PharmGKB; PA134958476; -. DR VEuPathDB; HostDB:ENSG00000064999; -. DR eggNOG; KOG0507; Eukaryota. DR GeneTree; ENSGT00940000155806; -. DR HOGENOM; CLU_010379_0_0_1; -. DR InParanoid; Q92625; -. DR OrthoDB; 25046at2759; -. DR PhylomeDB; Q92625; -. DR TreeFam; TF320582; -. DR PathwayCommons; Q92625; -. DR SignaLink; Q92625; -. DR BioGRID-ORCS; 23294; 19 hits in 1159 CRISPR screens. DR ChiTaRS; ANKS1A; human. DR GeneWiki; ANKS1A; -. DR GenomeRNAi; 23294; -. DR Pharos; Q92625; Tbio. DR PRO; PR:Q92625; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q92625; Protein. DR Bgee; ENSG00000064999; Expressed in olfactory bulb and 206 other cell types or tissues. DR ExpressionAtlas; Q92625; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central. DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB. DR GO; GO:0006929; P:substrate-dependent cell migration; ISS:UniProtKB. DR CDD; cd01274; PTB_Anks; 1. DR CDD; cd09499; SAM_AIDA1AB-like_repeat1; 1. DR CDD; cd09500; SAM_AIDA1AB-like_repeat2; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2. DR InterPro; IPR033635; ANKS1/Caskin. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR006020; PTB/PI_dom. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR041880; SAM_ANKS1_repeat1. DR InterPro; IPR041882; SAM_ANKS1_repeat2. DR PANTHER; PTHR24174:SF4; ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 1A; 1. DR PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF12796; Ank_2; 3. DR Pfam; PF00640; PID; 1. DR Pfam; PF00536; SAM_1; 2. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 6. DR SMART; SM00462; PTB; 1. DR SMART; SM00454; SAM; 2. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 2. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 6. DR PROSITE; PS01179; PID; 1. DR PROSITE; PS50105; SAM_DOMAIN; 2. DR Genevisible; Q92625; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; KW Cell projection; Cytoplasm; Direct protein sequencing; Phosphoprotein; KW Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12439753" FT CHAIN 2..1134 FT /note="Ankyrin repeat and SAM domain-containing protein 1A" FT /id="PRO_0000066921" FT REPEAT 79..108 FT /note="ANK 1" FT REPEAT 112..141 FT /note="ANK 2" FT REPEAT 148..177 FT /note="ANK 3" FT REPEAT 181..210 FT /note="ANK 4" FT REPEAT 214..243 FT /note="ANK 5" FT REPEAT 246..275 FT /note="ANK 6" FT DOMAIN 696..762 FT /note="SAM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT DOMAIN 770..837 FT /note="SAM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT DOMAIN 936..1091 FT /note="PID" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148" FT REGION 33..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 305..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 375..422 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 469..498 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 569..650 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 856..896 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1079..1134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 469..483 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 569..586 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 624..650 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 878..896 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0000269|PubMed:12439753" FT MOD_RES 318 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 507 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 620 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 622 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 624 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59672" FT MOD_RES 626 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 628 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 647 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 661 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 663 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 666 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59672" FT MOD_RES 677 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 887 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 305..320 FT /note="HMTGKRSTKEVDKTPP -> LDTLQFYFISCPFQGL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056512" FT VAR_SEQ 321..1134 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056513" FT VARIANT 355 FT /note="A -> D (in dbSNP:rs6930932)" FT /id="VAR_048282" FT VARIANT 694 FT /note="L -> S (in dbSNP:rs820085)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9039502, ECO:0000269|Ref.4, FT ECO:0007744|PubMed:19690332" FT /id="VAR_021168" FT HELIX 701..708 FT /evidence="ECO:0007829|PDB:2LMR" FT HELIX 711..713 FT /evidence="ECO:0007829|PDB:2LMR" FT HELIX 714..719 FT /evidence="ECO:0007829|PDB:2LMR" FT TURN 728..730 FT /evidence="ECO:0007829|PDB:2LMR" FT HELIX 735..741 FT /evidence="ECO:0007829|PDB:2LMR" FT HELIX 746..757 FT /evidence="ECO:0007829|PDB:2LMR" FT STRAND 759..761 FT /evidence="ECO:0007829|PDB:2LMR" SQ SEQUENCE 1134 AA; 123108 MW; E519844AD56EE414 CRC64; MGKEQELLEA ARTGHLPAVE KLLSGKRLSS GFGGGGGGGS GGGGGGSGGG GGGLGSSSHP LSSLLSMWRG PNVNCVDSTG YTPLHHAALN GHKDVVEVLL RNDALTNVAD SKGCYPLHLA AWKGDAQIVR LLIHQGPSHT RVNEQNNDNE TALHCAAQYG HTEVVKVLLE ELTDPTMRNN KFETPLDLAA LYGRLEVVKM LLNAHPNLLS CNTKKHTPLH LAARNGHKAV VQVLLDAGMD SNYQTEMGSA LHEAALFGKT DVVQILLAAG TDVNIKDNHG LTALDTVREL PSQKSQQIAA LIEDHMTGKR STKEVDKTPP PQPPLISSMD SISQKSQGDV EKAVTELIID FDANAEEEGP YEALYNAISC HSLDSMASGR SSDQDSTNKE AEAAGVKPAG VRPRERPPPP AKPPPDEEEE DHIDKKYFPL TASEVLSMRP RIHGSAAREE DEHPYELLLT AETKKVVLVD GKTKDHRRSS SSRSQDSAEG QDGQVPEQFS GLLHGSSPVC EVGQDPFQLL CTAGQSHPDG SPQQGACHKA SMQLEETGVH APGASQPSAL DQSKRVGYLT GLPTTNSRSH PETLTHTASP HPGGAEEGDR SGARSRAPPT SKPKAELKLS RSLSKSDSDL LTCSPTEDAT MGSRSESLSN CSIGKKRLEK SPSFASEWDE IEKIMSSIGE GIDFSQERQK ISGLRTLEQS VGEWLESIGL QQYESKLLLN GFDDVHFLGS NVMEEQDLRD IGISDPQHRR KLLQAARSLP KVKALGYDGN SPPSVPSWLD SLGLQDYVHS FLSSGYSSID TVKNLWELEL VNVLKVQLLG HRKRIIASLA DRPYEEPPQK PPRFSQLRCQ DLLSQTSSPL SQNDSCTGRS ADLLLPPGDT GRRRHDSLHD PAAPSRAERF RIQEEHREAK LTLRPPSLAA PYAPVQSWQH QPEKLIFESC GYEANYLGSM LIKDLRGTES TQDACAKMRK STEHMKKIPT IILSITYKGV KFIDASNKNV IAEHEIRNIS CAAQDPEDLC TFAYITKDLQ TSHHYCHVFS TVDVNLTYEI ILTLGQAFEV AYQLALQAQK SRATGASAAE MIETKSSKPV PKPRVGVRKS ALEPPDMDQD AQSHASVSWV VDPKPDSKRS LSTN //