ANS1A_HUMAN
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 03-AUG-2022, entry version 190.
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=6; IntAct=EBI-1048612, EBI-297353;
CC Q92625; P04626: ERBB2; NbExp=2; IntAct=EBI-1048612, EBI-641062;
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};
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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; 158.
DR IntAct; Q92625; 30.
DR MINT; Q92625; -.
DR STRING; 9606.ENSP00000353518; -.
DR GlyGen; Q92625; 1 site, 1 O-linked glycan (1 site).
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; Q92625; -.
DR PeptideAtlas; Q92625; -.
DR PRIDE; Q92625; -.
DR ProteomicsDB; 4910; -.
DR ProteomicsDB; 75380; -. [Q92625-1]
DR Antibodypedia; 29433; 107 antibodies from 20 providers.
DR DNASU; 23294; -.
DR Ensembl; ENST00000360359.5; ENSP00000353518.3; ENSG00000064999.15. [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 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; 549581at2759; -.
DR PhylomeDB; Q92625; -.
DR TreeFam; TF320582; -.
DR PathwayCommons; Q92625; -.
DR SignaLink; Q92625; -.
DR BioGRID-ORCS; 23294; 19 hits in 1081 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 204 other tissues.
DR ExpressionAtlas; Q92625; baseline and differential.
DR Genevisible; Q92625; HS.
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:1901187; P:regulation of ephrin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006929; P:substrate-dependent cell migration; ISS:UniProtKB.
DR CDD; cd09499; SAM_AIDA1AB-like_repeat1; 1.
DR CDD; cd09500; SAM_AIDA1AB-like_repeat2; 1.
DR Gene3D; 1.10.150.50; -; 2.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR033637; ANKS1A.
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; PTHR24174:SF4; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00454; SAM; 2.
DR SUPFAM; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
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
