ID   ANKH1_HUMAN             Reviewed;        2542 AA.
AC   Q8IWZ3; A6NH85; Q149P2; Q8IWZ2; Q8WY90; Q96G77; Q96GK0; Q9H2U0; Q9HA95;
AC   Q9NWG4; Q9UPR7;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Ankyrin repeat and KH domain-containing protein 1;
DE   AltName: Full=HIV-1 Vpr-binding ankyrin repeat protein;
DE   AltName: Full=Multiple ankyrin repeats single KH domain;
DE            Short=hMASK;
GN   Name=ANKHD1; Synonyms=KIAA1085, MASK, VBARP; ORFNames=PP2500;
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 AND 6), AND TISSUE SPECIFICITY.
RX   PubMed=14557257; DOI=10.1074/jbc.m310761200;
RA   Poulin F., Brueschke A., Sonenberg N.;
RT   "Gene fusion and overlapping reading frames in the mammalian genes for 4E-
RT   BP3 and MASK.";
RL   J. Biol. Chem. 278:52290-52297(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5), AND VARIANTS
RP   MET-175 AND CYS-228.
RC   TISSUE=Lung;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 670-1189 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-2542 (ISOFORM 2).
RC   TISSUE=Embryo;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 924-1455 (ISOFORM 1).
RA   Cheng C.M., Yuo C.Y.;
RT   "A novel protein with ten ankyrin repeats.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1961-2542 (ISOFORM 4).
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [9]
RP   INTERACTION WITH HIV-1 VPR, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16098192; DOI=10.1111/j.1742-4658.2005.04821.x;
RA   Miles M.C., Janket M.L., Wheeler E.D., Chattopadhyay A., Majumder B.,
RA   Dericco J., Schafer E.A., Ayyavoo V.;
RT   "Molecular and functional characterization of a novel splice variant of
RT   ANKHD1 that lacks the KH domain and its role in cell survival and
RT   apoptosis.";
RL   FEBS J. 272:4091-4102(2005).
RN   [10]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH PTPN11.
RX   PubMed=16956752; DOI=10.1016/j.bbadis.2006.07.010;
RA   Traina F., Favaro P.M.B., Medina Sde S., Duarte Ada S., Winnischofer S.M.,
RA   Costa F.F., Saad S.T.O.;
RT   "ANKHD1, ankyrin repeat and KH domain containing 1, is overexpressed in
RT   acute leukemias and is associated with SHP2 in K562 cells.";
RL   Biochim. Biophys. Acta 1762:828-834(2006).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1653, AND IDENTIFICATION BY
RP   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   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP   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   [15]
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   [16]
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   [17]
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).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803; SER-1540; THR-1553;
RP   SER-1632 AND THR-1653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP   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   [20]
RP   INTERACTION WITH NOD2.
RX   PubMed=27812135; DOI=10.1371/journal.pone.0165420;
RA   Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A., Nicoletti C.,
RA   Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P., Ollendorff V.;
RT   "Characterization and Genetic Analyses of New Genes Coding for NOD2
RT   Interacting Proteins.";
RL   PLoS ONE 11:E0165420-E0165420(2016).
CC   -!- FUNCTION: May play a role as a scaffolding protein that may be
CC       associated with the abnormal phenotype of leukemia cells. Isoform 2 may
CC       possess an antiapoptotic effect and protect cells during normal cell
CC       survival through its regulation of caspases.
CC       {ECO:0000269|PubMed:16098192}.
CC   -!- SUBUNIT: Interacts with PTPN11. Isoform 2 interacts with HIV-1 VPR.
CC       Interacts with NOD2 (PubMed:27812135). {ECO:0000269|PubMed:16098192,
CC       ECO:0000269|PubMed:16956752, ECO:0000269|PubMed:27812135}.
CC   -!- INTERACTION:
CC       Q8IWZ3; O00221: NFKBIE; NbExp=2; IntAct=EBI-359558, EBI-355098;
CC       Q8IWZ3-1; Q9NRI5: DISC1; NbExp=6; IntAct=EBI-1785446, EBI-529989;
CC       Q8IWZ3-2; P54253: ATXN1; NbExp=3; IntAct=EBI-9641396, EBI-930964;
CC       Q8IWZ3-2; P23560-2: BDNF; NbExp=3; IntAct=EBI-9641396, EBI-12275524;
CC       Q8IWZ3-3; P54253: ATXN1; NbExp=6; IntAct=EBI-25833200, EBI-930964;
CC       Q8IWZ3-3; P23560-2: BDNF; NbExp=3; IntAct=EBI-25833200, EBI-12275524;
CC       Q8IWZ3-3; P08574: CYC1; NbExp=3; IntAct=EBI-25833200, EBI-1224514;
CC       Q8IWZ3-3; P42858: HTT; NbExp=3; IntAct=EBI-25833200, EBI-466029;
CC       Q8IWZ3-3; Q92993: KAT5; NbExp=3; IntAct=EBI-25833200, EBI-399080;
CC       Q8IWZ3-3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-25833200, EBI-11742507;
CC       Q8IWZ3-3; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-25833200, EBI-9090795;
CC       Q8IWZ3-3; P61981: YWHAG; NbExp=3; IntAct=EBI-25833200, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16098192,
CC       ECO:0000269|PubMed:16956752}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q8IWZ3-1; Sequence=Displayed;
CC       Name=2; Synonyms=VBARP-L;
CC         IsoId=Q8IWZ3-2; Sequence=VSP_028455, VSP_028456;
CC       Name=3;
CC         IsoId=Q8IWZ3-3; Sequence=VSP_028452, VSP_028455, VSP_028456;
CC       Name=4;
CC         IsoId=Q8IWZ3-4; Sequence=VSP_028457, VSP_028458;
CC       Name=5;
CC         IsoId=Q8IWZ3-5; Sequence=VSP_028453, VSP_028454;
CC       Name=6;
CC         IsoId=Q8IWZ3-6; Sequence=VSP_044231;
CC   -!- TISSUE SPECIFICITY: Ubiquitous with high expression in cervix, spleen
CC       and brain. Expressed in hematopoietic cells with increased expression
CC       in leukemia cells. Isoform 2 is highly expressed in spleen with almost
CC       no expression in muscle and brain. {ECO:0000269|PubMed:14557257,
CC       ECO:0000269|PubMed:16098192, ECO:0000269|PubMed:16956752}.
CC   -!- SIMILARITY: Belongs to the mask family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91417.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB13958.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF521882; AAO14943.1; -; mRNA.
DR   EMBL; AF521883; AAO14944.1; -; mRNA.
DR   EMBL; AF258557; AAG23760.1; -; mRNA.
DR   EMBL; AC008438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471062; EAW62055.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW62058.1; -; Genomic_DNA.
DR   EMBL; BC004457; AAH04457.2; -; mRNA.
DR   EMBL; BC009420; AAH09420.1; -; mRNA.
DR   EMBL; BC009909; AAH09909.1; -; mRNA.
DR   EMBL; BC117677; AAI17678.1; -; mRNA.
DR   EMBL; BC117678; AAI17679.1; -; mRNA.
DR   EMBL; BC127127; AAI27128.1; -; mRNA.
DR   EMBL; BC150486; AAI50487.1; -; mRNA.
DR   EMBL; AK000904; BAA91417.1; ALT_INIT; mRNA.
DR   EMBL; AK022041; BAB13958.1; ALT_INIT; mRNA.
DR   EMBL; AF217646; AAG41779.1; -; mRNA.
DR   EMBL; AB029008; BAA83037.1; -; mRNA.
DR   CCDS; CCDS4225.1; -. [Q8IWZ3-1]
DR   CCDS; CCDS43371.1; -. [Q8IWZ3-2]
DR   CCDS; CCDS43372.1; -. [Q8IWZ3-3]
DR   CCDS; CCDS75319.1; -. [Q8IWZ3-5]
DR   RefSeq; NP_001183959.1; NM_001197030.1. [Q8IWZ3-5]
DR   RefSeq; NP_060217.1; NM_017747.2. [Q8IWZ3-1]
DR   RefSeq; NP_060448.1; NM_017978.2. [Q8IWZ3-3]
DR   RefSeq; NP_065741.3; NM_020690.5. [Q8IWZ3-6]
DR   RefSeq; NP_078944.2; NM_024668.3. [Q8IWZ3-2]
DR   AlphaFoldDB; Q8IWZ3; -.
DR   SMR; Q8IWZ3; -.
DR   BioGRID; 120230; 237.
DR   BioGRID; 135698; 115.
DR   DIP; DIP-36371N; -.
DR   IntAct; Q8IWZ3; 70.
DR   MINT; Q8IWZ3; -.
DR   STRING; 9606.ENSP00000354085; -.
DR   GlyCosmos; Q8IWZ3; 19 sites, 2 glycans.
DR   GlyGen; Q8IWZ3; 25 sites, 2 O-linked glycans (25 sites).
DR   iPTMnet; Q8IWZ3; -.
DR   PhosphoSitePlus; Q8IWZ3; -.
DR   SwissPalm; Q8IWZ3; -.
DR   BioMuta; ANKHD1; -.
DR   DMDM; 74750718; -.
DR   EPD; Q8IWZ3; -.
DR   jPOST; Q8IWZ3; -.
DR   MassIVE; Q8IWZ3; -.
DR   MaxQB; Q8IWZ3; -.
DR   PaxDb; 9606-ENSP00000354085; -.
DR   PeptideAtlas; Q8IWZ3; -.
DR   ProteomicsDB; 70934; -.
DR   ProteomicsDB; 70935; -. [Q8IWZ3-1]
DR   ProteomicsDB; 70936; -. [Q8IWZ3-2]
DR   ProteomicsDB; 70937; -. [Q8IWZ3-3]
DR   ProteomicsDB; 70938; -. [Q8IWZ3-4]
DR   ProteomicsDB; 70939; -. [Q8IWZ3-5]
DR   Pumba; Q8IWZ3; -.
DR   Antibodypedia; 1444; 184 antibodies from 25 providers.
DR   DNASU; 404734; -.
DR   DNASU; 54882; -.
DR   Ensembl; ENST00000360839.7; ENSP00000354085.2; ENSG00000131503.21. [Q8IWZ3-1]
DR   Ensembl; ENST00000394722.7; ENSP00000378211.3; ENSG00000131503.21. [Q8IWZ3-3]
DR   Ensembl; ENST00000394723.7; ENSP00000378212.3; ENSG00000131503.21. [Q8IWZ3-2]
DR   Ensembl; ENST00000616482.4; ENSP00000478529.1; ENSG00000131503.21. [Q8IWZ3-5]
DR   GeneID; 404734; -.
DR   GeneID; 54882; -.
DR   KEGG; hsa:404734; -.
DR   KEGG; hsa:54882; -.
DR   MANE-Select; ENST00000360839.7; ENSP00000354085.2; NM_017747.3; NP_060217.1.
DR   UCSC; uc003lfo.4; human. [Q8IWZ3-1]
DR   AGR; HGNC:24714; -.
DR   AGR; HGNC:33530; -.
DR   CTD; 404734; -.
DR   CTD; 54882; -.
DR   DisGeNET; 404734; -.
DR   DisGeNET; 54882; -.
DR   GeneCards; ANKHD1; -.
DR   HGNC; HGNC:24714; ANKHD1.
DR   HPA; ENSG00000131503; Low tissue specificity.
DR   MIM; 610500; gene.
DR   neXtProt; NX_Q8IWZ3; -.
DR   OpenTargets; ENSG00000131503; -.
DR   PharmGKB; PA134947858; -.
DR   PharmGKB; PA162376432; -.
DR   VEuPathDB; HostDB:ENSG00000131503; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG4369; Eukaryota.
DR   GeneTree; ENSGT00940000153768; -.
DR   HOGENOM; CLU_000590_0_1_1; -.
DR   InParanoid; Q8IWZ3; -.
DR   OMA; ERMITIX; -.
DR   OrthoDB; 5480610at2759; -.
DR   PhylomeDB; Q8IWZ3; -.
DR   TreeFam; TF328552; -.
DR   PathwayCommons; Q8IWZ3; -.
DR   SignaLink; Q8IWZ3; -.
DR   BioGRID-ORCS; 404734; 41 hits in 1086 CRISPR screens.
DR   BioGRID-ORCS; 54882; 21 hits in 766 CRISPR screens.
DR   ChiTaRS; ANKHD1; human.
DR   GeneWiki; ANKHD1; -.
DR   Pharos; Q8IWZ3; Tbio.
DR   PRO; PR:Q8IWZ3; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q8IWZ3; Protein.
DR   Bgee; ENSG00000131503; Expressed in sural nerve and 149 other cell types or tissues.
DR   ExpressionAtlas; Q8IWZ3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   CDD; cd22503; KH-I_ANKHD1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 8.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR047374; KH-I_ANKHD1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   PANTHER; PTHR23206:SF5; ANKYRIN REPEAT AND KH DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR23206; MASK PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 8.
DR   Pfam; PF13637; Ank_4; 2.
DR   Pfam; PF00013; KH_1; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 25.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 3.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   Genevisible; Q8IWZ3; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ANK repeat; Coiled coil; Cytoplasm;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..2542
FT                   /note="Ankyrin repeat and KH domain-containing protein 1"
FT                   /id="PRO_0000306326"
FT   REPEAT          204..233
FT                   /note="ANK 1"
FT   REPEAT          237..266
FT                   /note="ANK 2"
FT   REPEAT          271..300
FT                   /note="ANK 3"
FT   REPEAT          304..333
FT                   /note="ANK 4"
FT   REPEAT          337..366
FT                   /note="ANK 5"
FT   REPEAT          371..400
FT                   /note="ANK 6"
FT   REPEAT          404..433
FT                   /note="ANK 7"
FT   REPEAT          437..466
FT                   /note="ANK 8"
FT   REPEAT          470..499
FT                   /note="ANK 9"
FT   REPEAT          504..533
FT                   /note="ANK 10"
FT   REPEAT          534..563
FT                   /note="ANK 11"
FT   REPEAT          567..596
FT                   /note="ANK 12"
FT   REPEAT          600..629
FT                   /note="ANK 13"
FT   REPEAT          634..663
FT                   /note="ANK 14"
FT   REPEAT          667..696
FT                   /note="ANK 15"
FT   REPEAT          1054..1083
FT                   /note="ANK 16"
FT   REPEAT          1087..1116
FT                   /note="ANK 17"
FT   REPEAT          1121..1150
FT                   /note="ANK 18"
FT   REPEAT          1154..1183
FT                   /note="ANK 19"
FT   REPEAT          1189..1218
FT                   /note="ANK 20"
FT   REPEAT          1223..1252
FT                   /note="ANK 21"
FT   REPEAT          1256..1285
FT                   /note="ANK 22"
FT   REPEAT          1291..1320
FT                   /note="ANK 23"
FT   REPEAT          1324..1353
FT                   /note="ANK 24"
FT   REPEAT          1357..1386
FT                   /note="ANK 25"
FT   DOMAIN          1695..1759
FT                   /note="KH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1441..1517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1534..1614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1632..1664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1886..1923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1987..2106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2260..2367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          775..852
FT                   /evidence="ECO:0000255"
FT   COILED          1415..1485
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1465..1484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1485..1502
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1591..1614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1896..1923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2272..2305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2322..2356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         803
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1553
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1632
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1653
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         154..164
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028452"
FT   VAR_SEQ         559..581
FT                   /note="ANVHATTATGDTALTYACENGHT -> QAGGHEDYFGGHRSGQASGEGGL
FT                   (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028453"
FT   VAR_SEQ         582..2542
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028454"
FT   VAR_SEQ         595..627
FT                   /note="EHESEGGRTPLMKAARAGHLCTVQFLISKGANV -> DKQEDMKTILEGIDP
FT                   AKHQVRVAFDACKLLRKE (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15498874"
FT                   /id="VSP_028455"
FT   VAR_SEQ         628..2542
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15498874"
FT                   /id="VSP_028456"
FT   VAR_SEQ         2342..2343
FT                   /note="SS -> SCDSPIPSVSSGSSSPLSA (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10470851"
FT                   /id="VSP_028457"
FT   VAR_SEQ         2524..2542
FT                   /note="IWPGTWAPHIGNMHLKYVN -> VKWA (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10470851"
FT                   /id="VSP_028458"
FT   VAR_SEQ         2524..2542
FT                   /note="IWPGTWAPHIGNMHLKYVN -> ASLLPSVPALKGEIPSPQLTRPKKRIGRP
FT                   MVASPNQRHQDHLRPKVPAGVQELTHCPDTPLLPPSDSRGHNSSNSPSLQAGGAEGAGD
FT                   RGRDTR (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14557257"
FT                   /id="VSP_044231"
FT   VARIANT         175
FT                   /note="L -> M (in dbSNP:rs17850570)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_035291"
FT   VARIANT         228
FT                   /note="G -> C (in dbSNP:rs17850572)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_035292"
FT   VARIANT         1586
FT                   /note="G -> S (in dbSNP:rs1051309)"
FT                   /id="VAR_048281"
FT   VARIANT         1760
FT                   /note="N -> S (in dbSNP:rs3752704)"
FT                   /id="VAR_035293"
SQ   SEQUENCE   2542 AA;  269458 MW;  AB310E826A4134D0 CRC64;
     MLTDSGGGGT SFEEDLDSVA PRSAPAGASE PPPPGGVGLG IRTVRLFGEA GPASGVGSSG
     GGGSGSGTGG GDAALDFKLA AAVLRTGGGG GASGSDEDEV SEVESFILDQ EDLDNPVLKT
     TSEIFLSSTA EGADLRTVDP ETQARLEALL EAAGIGKLST ADGKAFADPE VLRRLTSSVS
     CALDEAAAAL TRMKAENSHN AGQVDTRSLA EACSDGDVNA VRKLLDEGRS VNEHTEEGES
     LLCLACSAGY YELAQVLLAM HANVEDRGNK GDITPLMAAS SGGYLDIVKL LLLHDADVNS
     QSATGNTALT YACAGGFVDI VKVLLNEGAN IEDHNENGHT PLMEAASAGH VEVARVLLDH
     GAGINTHSNE FKESALTLAC YKGHLDMVRF LLEAGADQEH KTDEMHTALM EACMDGHVEV
     ARLLLDSGAQ VNMPADSFES PLTLAACGGH VELAALLIER GANLEEVNDE GYTPLMEAAR
     EGHEEMVALL LAQGANINAQ TEETQETALT LACCGGFSEV ADFLIKAGAD IELGCSTPLM
     EASQEGHLEL VKYLLASGAN VHATTATGDT ALTYACENGH TDVADVLLQA GADLEHESEG
     GRTPLMKAAR AGHLCTVQFL ISKGANVNRA TANNDHTVVS LACAGGHLAV VELLLAHGAD
     PTHRLKDGST MLIEAAKGGH TNVVSYLLDY PNNVLSVPTT DVSQLPPPSQ DQSQVPRVPT
     HTLAMVVPPQ EPDRTSQENS PALLGVQKGT SKQKSSSLQV ADQDLLPSFH PYQPLECIVE
     ETEGKLNELG QRISAIEKAQ LKSLELIQGE PLNKDKIEEL KKNREEQVQK KKKILKELQK
     VERQLQMKTQ QQFTKEYLET KGQKDTVSLH QQCSHRGVFP EGEGDGSLPE DHFSELPQVD
     TILFKDNDVD DEQQSPPSAE QIDFVPVQPL SSPQCNFSSD LGSNGTNSLE LQKVSGNQQI
     VGQPQIAITG HDQGLLVQEP DGLMVATPAQ TLTDTLDDLI AAVSTRVPTG SNSSSQTTEC
     LTPESCSQTT SNVASQSMPP VYPSVDIDAH TESNHDTALT LACAGGHEEL VSVLIARDAK
     IEHRDKKGFT PLILAATAGH VGVVEILLDK GGDIEAQSER TKDTPLSLAC SGGRQEVVDL
     LLARGANKEH RNVSDYTPLS LAASGGYVNI IKILLNAGAE INSRTGSKLG ISPLMLAAMN
     GHVPAVKLLL DMGSDINAQI ETNRNTALTL ACFQGRAEVV SLLLDRKANV EHRAKTGLTP
     LMEAASGGYA EVGRVLLDKG ADVNAPPVPS SRDTALTIAA DKGHYKFCEL LIHRGAHIDV
     RNKKGNTPLW LASNGGHFDV VQLLVQAGAD VDAADNRKIT PLMSAFRKGH VKVVQYLVKE
     VNQFPSDIEC MRYIATITDK ELLKKCHQCV ETIVKAKDQQ AAEANKNASI LLKELDLEKS
     REESRKQALA AKREKRKEKR KKKKEEQKRK QEEDEENKPK ENSELPEDED EEENDEDVEQ
     EVPIEPPSAT TTTTIGISAT SATFTNVFGK KRANVVTTPS TNRKNKKNKT KETPPTAHLI
     LPEQHMSLAQ QKADKNKING EPRGGGAGGN SDSDNLDSTD CNSESSSGGK SQELNFVMDV
     NSSKYPSLLL HSQEEKTSTA TSKTQTRLEG EVTPNSLSTS YKTVSLPLSS PNIKLNLTSP
     KRGQKREEGW KEVVRRSKKL SVPASVVSRI MGRGGCNITA IQDVTGAHID VDKQKDKNGE
     RMITIRGGTE STRYAVQLIN ALIQDPAKEL EDLIPKNHIR TPASTKSIHA NFSSGVGTTA
     ASSKNAFPLG APTLVTSQAT TLSTFQPANK LNKNVPTNVR SSFPVSLPLA YPHPHFALLA
     AQTMQQIRHP RLPMAQFGGT FSPSPNTWGP FPVRPVNPGN TNSSPKHNNT SRLPNQNGTV
     LPSESAGLAT ASCPITVSSV VAASQQLCVT NTRTPSSVRK QLFACVPKTS PPATVISSVT
     STCSSLPSVS SAPITSGQAP TTFLPASTSQ AQLSSQKMES FSAVPPTKEK VSTQDQPMAN
     LCTPSSTANS CSSSASNTPG APETHPSSSP TPTSSNTQEE AQPSSVSDLS PMSMPFASNS
     EPAPLTLTSP RMVAADNQDT SNLPQLAVPA PRVSHRMQPR GSFYSMVPNA TIHQDPQSIF
     VTNPVTLTPP QGPPAAVQLS SAVNIMNGSQ MHINPANKSL PPTFGPATLF NHFSSLFDSS
     QVPANQGWGD GPLSSRVATD ASFTVQSAFL GNSVLGHLEN MHPDNSKAPG FRPPSQRVST
     SPVGLPSIDP SGSSPSSSSA PLASFSGIPG TRVFLQGPAP VGTPSFNRQH FSPHPWTSAS
     NSSTSAPPTL GQPKGVSASQ DRKIPPPIGT ERLARIRQGG SVAQAPAGTS FVAPVGHSGI
     WSFGVNAVSE GLSGWSQSVM GNHPMHQQLS DPSTFSQHQP MERDDSGMVA PSNIFHQPMA
     SGFVDFSKGL PISMYGGTII PSHPQLADVP GGPLFNGLHN PDPAWNPMIK VIQNSTECTD
     AQQIWPGTWA PHIGNMHLKY VN
//