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 Genevisible; Q8IWZ3; HS.
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.
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
//
