RAI14_HUMAN
ID RAI14_HUMAN Reviewed; 980 AA.
AC Q9P0K7; E9PED3; Q6V1W9; Q7Z5I4; Q7Z733; Q9P2L2; Q9Y3T5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ankycorbin;
DE AltName: Full=Ankyrin repeat and coiled-coil structure-containing protein;
DE AltName: Full=Novel retinal pigment epithelial cell protein;
DE AltName: Full=Retinoic acid-induced protein 14;
GN Name=RAI14; Synonyms=KIAA1334, NORPEG;
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] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Retinal pigment epithelium;
RX PubMed=11042181; DOI=10.1074/jbc.m007421200;
RA Kutty R.K., Kutty G., Samuel W., Duncan T., Bridges C.C., El-Sherbeeny A.,
RA Nagineni C.N., Smith S.B., Wiggert B.;
RT "Molecular characterization and developmental expression of NORPEG, a novel
RT gene induced by retinoic acid.";
RL J. Biol. Chem. 276:2831-2840(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=16110356; DOI=10.1111/j.1745-7262.2005.00040.x;
RA Yuan W., Zheng Y., Huo R., Lu L., Huang X.-Y., Yin L.-L., Li J.-M.,
RA Zhou Z.-M., Sha J.-H.;
RT "Expression of a novel alternative transcript of the novel retinal pigment
RT epithelial cell gene NORPEG in human testes.";
RL Asian J. Androl. 7:277-288(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RA Sha J.H., Zhou Z.M., Li J.M.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT SER-870.
RC TISSUE=Placenta;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-870.
RC TISSUE=Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 636-980.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=11168586; DOI=10.1046/j.1365-2443.2000.00381.x;
RA Peng Y.-F., Mandai K., Sakisaka T., Okabe N., Yamamoto Y., Yokoyama S.,
RA Mizoguchi A., Shiozaki H., Monden M., Takai Y.;
RT "Ankycorbin: a novel actin cytoskeleton-associated protein.";
RL Genes Cells 5:1001-1008(2000).
RN [10]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RC TISSUE=Retinal pigment epithelium;
RX PubMed=16729964; DOI=10.1016/j.bbrc.2006.04.184;
RA Kutty R.K., Chen S., Samuel W., Vijayasarathy C., Duncan T., Tsai J.Y.,
RA Fariss R.N., Carper D., Jaworski C., Wiggert B.;
RT "Cell density-dependent nuclear/cytoplasmic localization of NORPEG (RAI14)
RT protein.";
RL Biochem. Biophys. Res. Commun. 345:1333-1341(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, 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=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-249; SER-340; SER-341;
RP SER-358; SER-512 AND SER-515, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; THR-295; THR-297 AND
RP SER-300, AND 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-11; THR-249; THR-297;
RP SER-358; SER-419 AND SER-667, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-249; SER-281; SER-286;
RP SER-327; SER-329; SER-350 AND SER-358, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Plays a role in actin regulation at the ectoplasmic
CC specialization, a type of cell junction specific to testis. Important
CC for establishment of sperm polarity and normal spermatid adhesion. May
CC also promote integrity of Sertoli cell tight junctions at the blood-
CC testis barrier. {ECO:0000250|UniProtKB:Q5U312}.
CC -!- SUBUNIT: Interacts with PALLD. Associates with actin. However, does not
CC bind F-actin directly. {ECO:0000250|UniProtKB:Q5U312,
CC ECO:0000250|UniProtKB:Q9EP71}.
CC -!- INTERACTION:
CC Q9P0K7; P63104: YWHAZ; NbExp=2; IntAct=EBI-1023749, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:11042181, ECO:0000305|PubMed:16729964}. Cytoplasm,
CC cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9EP71}. Cytoplasm,
CC cell cortex {ECO:0000250|UniProtKB:Q5U312}. Cell junction
CC {ECO:0000250|UniProtKB:Q5U312}. Nucleus {ECO:0000269|PubMed:16729964}.
CC Note=Associated with the cortical actin cytoskeleton structures in
CC terminal web and cell-cell adhesion sites (By similarity). Highly
CC expressed at the ectoplasmic specialization, an actin-rich cell
CC junction specific to the testis (By similarity). Predominantly nuclear
CC in nonconfluent cells (PubMed:16729964). {ECO:0000250|UniProtKB:Q5U312,
CC ECO:0000269|PubMed:16729964}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9P0K7-1; Sequence=Displayed;
CC Name=2; Synonyms=sNORPEG;
CC IsoId=Q9P0K7-2; Sequence=VSP_019248;
CC Name=3;
CC IsoId=Q9P0K7-3; Sequence=VSP_019249;
CC Name=4;
CC IsoId=Q9P0K7-4; Sequence=VSP_045814;
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, muscle, kidney and
CC testis. Moderately expressed in heart, brain, lung, liver and
CC intestine. Isoform 2 is widely expressed and expressed in fetal and
CC adult testes, and spermatozoa. {ECO:0000269|PubMed:11042181,
CC ECO:0000269|PubMed:11168586, ECO:0000269|PubMed:16110356}.
CC -!- INDUCTION: Up-regulated by all-trans-retinoic acid (ATRA) in retinal
CC pigment epithelial cells (ARPE-19). {ECO:0000269|PubMed:11042181}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92572.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB43236.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF155135; AAF44722.1; -; mRNA.
DR EMBL; AY317139; AAP84319.1; -; mRNA.
DR EMBL; AY354204; AAQ63889.2; -; mRNA.
DR EMBL; AB037755; BAA92572.1; ALT_INIT; mRNA.
DR EMBL; AK314379; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC016602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052988; AAH52988.1; -; mRNA.
DR EMBL; AL050011; CAB43236.2; ALT_INIT; mRNA.
DR CCDS; CCDS34142.1; -. [Q9P0K7-1]
DR CCDS; CCDS54837.1; -. [Q9P0K7-4]
DR CCDS; CCDS54838.1; -. [Q9P0K7-3]
DR CCDS; CCDS54839.1; -. [Q9P0K7-2]
DR PIR; T08700; T08700.
DR RefSeq; NP_001138992.1; NM_001145520.1. [Q9P0K7-1]
DR RefSeq; NP_001138993.1; NM_001145521.1. [Q9P0K7-1]
DR RefSeq; NP_001138994.1; NM_001145522.1. [Q9P0K7-4]
DR RefSeq; NP_001138995.1; NM_001145523.1. [Q9P0K7-3]
DR RefSeq; NP_001138997.1; NM_001145525.1. [Q9P0K7-2]
DR RefSeq; NP_056392.2; NM_015577.2. [Q9P0K7-1]
DR RefSeq; XP_006714532.1; XM_006714469.2. [Q9P0K7-1]
DR RefSeq; XP_011512319.1; XM_011514017.2. [Q9P0K7-1]
DR RefSeq; XP_011512320.1; XM_011514018.1. [Q9P0K7-1]
DR RefSeq; XP_011512321.1; XM_011514019.1. [Q9P0K7-1]
DR RefSeq; XP_011512322.1; XM_011514020.1. [Q9P0K7-1]
DR RefSeq; XP_011512323.1; XM_011514021.1. [Q9P0K7-1]
DR RefSeq; XP_011512324.1; XM_011514022.1. [Q9P0K7-1]
DR RefSeq; XP_016864824.1; XM_017009335.1. [Q9P0K7-4]
DR AlphaFoldDB; Q9P0K7; -.
DR SMR; Q9P0K7; -.
DR BioGRID; 117526; 192.
DR IntAct; Q9P0K7; 90.
DR MINT; Q9P0K7; -.
DR STRING; 9606.ENSP00000427123; -.
DR CarbonylDB; Q9P0K7; -.
DR GlyGen; Q9P0K7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P0K7; -.
DR MetOSite; Q9P0K7; -.
DR PhosphoSitePlus; Q9P0K7; -.
DR SwissPalm; Q9P0K7; -.
DR BioMuta; RAI14; -.
DR DMDM; 108860920; -.
DR EPD; Q9P0K7; -.
DR jPOST; Q9P0K7; -.
DR MassIVE; Q9P0K7; -.
DR MaxQB; Q9P0K7; -.
DR PaxDb; Q9P0K7; -.
DR PeptideAtlas; Q9P0K7; -.
DR PRIDE; Q9P0K7; -.
DR ProteomicsDB; 19863; -.
DR ProteomicsDB; 83561; -. [Q9P0K7-1]
DR ProteomicsDB; 83562; -. [Q9P0K7-2]
DR ProteomicsDB; 83563; -. [Q9P0K7-3]
DR Antibodypedia; 22784; 83 antibodies from 21 providers.
DR DNASU; 26064; -.
DR Ensembl; ENST00000265109.8; ENSP00000265109.3; ENSG00000039560.14. [Q9P0K7-1]
DR Ensembl; ENST00000428746.6; ENSP00000388725.2; ENSG00000039560.14. [Q9P0K7-1]
DR Ensembl; ENST00000503673.5; ENSP00000422942.1; ENSG00000039560.14. [Q9P0K7-1]
DR Ensembl; ENST00000506376.1; ENSP00000423854.1; ENSG00000039560.14. [Q9P0K7-3]
DR Ensembl; ENST00000512629.5; ENSP00000422377.1; ENSG00000039560.14. [Q9P0K7-4]
DR Ensembl; ENST00000515799.5; ENSP00000427123.1; ENSG00000039560.14. [Q9P0K7-2]
DR GeneID; 26064; -.
DR KEGG; hsa:26064; -.
DR MANE-Select; ENST00000265109.8; ENSP00000265109.3; NM_015577.3; NP_056392.2.
DR UCSC; uc003jir.4; human. [Q9P0K7-1]
DR CTD; 26064; -.
DR DisGeNET; 26064; -.
DR GeneCards; RAI14; -.
DR HGNC; HGNC:14873; RAI14.
DR HPA; ENSG00000039560; Low tissue specificity.
DR MIM; 606586; gene.
DR neXtProt; NX_Q9P0K7; -.
DR OpenTargets; ENSG00000039560; -.
DR PharmGKB; PA34189; -.
DR VEuPathDB; HostDB:ENSG00000039560; -.
DR eggNOG; ENOG502QUEG; Eukaryota.
DR GeneTree; ENSGT00940000157400; -.
DR HOGENOM; CLU_005323_2_0_1; -.
DR InParanoid; Q9P0K7; -.
DR OMA; XDGNIPL; -.
DR OrthoDB; 876605at2759; -.
DR PhylomeDB; Q9P0K7; -.
DR TreeFam; TF331274; -.
DR PathwayCommons; Q9P0K7; -.
DR SignaLink; Q9P0K7; -.
DR SIGNOR; Q9P0K7; -.
DR BioGRID-ORCS; 26064; 12 hits in 1084 CRISPR screens.
DR ChiTaRS; RAI14; human.
DR GeneWiki; RAI14; -.
DR GenomeRNAi; 26064; -.
DR Pharos; Q9P0K7; Tbio.
DR PRO; PR:Q9P0K7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9P0K7; protein.
DR Bgee; ENSG00000039560; Expressed in stromal cell of endometrium and 185 other tissues.
DR ExpressionAtlas; Q9P0K7; baseline and differential.
DR Genevisible; Q9P0K7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042420; RAI14.
DR PANTHER; PTHR24129; PTHR24129; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Cell junction; Coiled coil;
KW Cytoplasm; Cytoskeleton; Differentiation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..980
FT /note="Ankycorbin"
FT /id="PRO_0000239630"
FT REPEAT 18..51
FT /note="ANK 1"
FT REPEAT 52..81
FT /note="ANK 2"
FT REPEAT 85..114
FT /note="ANK 3"
FT REPEAT 118..147
FT /note="ANK 4"
FT REPEAT 151..180
FT /note="ANK 5"
FT REPEAT 184..213
FT /note="ANK 6"
FT REPEAT 217..247
FT /note="ANK 7"
FT REGION 247..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..374
FT /evidence="ECO:0000255"
FT COILED 425..947
FT /evidence="ECO:0000255"
FT MOTIF 270..276
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:16729964"
FT COMPBIAS 247..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
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 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 249
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 295
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 297
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP71"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U312"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP71"
FT VAR_SEQ 1..12
FT /note="MKSLKAKFRKSD -> MQPTYLPWLSAKEKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16110356"
FT /id="VSP_019248"
FT VAR_SEQ 1..12
FT /note="MKSLKAKFRKSD -> MEAK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019249"
FT VAR_SEQ 255..283
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045814"
FT VARIANT 44
FT /note="A -> T (in dbSNP:rs17521570)"
FT /id="VAR_026673"
FT VARIANT 45
FT /note="S -> N (in dbSNP:rs35941954)"
FT /id="VAR_055517"
FT VARIANT 499
FT /note="V -> L (in dbSNP:rs10472941)"
FT /id="VAR_055518"
FT VARIANT 870
FT /note="A -> S (in dbSNP:rs1048944)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_055519"
FT CONFLICT 104
FT /note="K -> R (in Ref. 1; AAF44722)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="K -> T (in Ref. 1; AAF44722 and 3; AAQ63889)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="L -> P (in Ref. 3; AAQ63889)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="K -> Q (in Ref. 3; AAQ63889)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="Q -> P (in Ref. 3; AAQ63889)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="E -> G (in Ref. 3; AAQ63889)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="K -> E (in Ref. 3; AAQ63889)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="R -> G (in Ref. 8; CAB43236)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="A -> L (in Ref. 3; AAQ63889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 110041 MW; DFCF4B7913B30B69 CRC64;
MKSLKAKFRK SDTNEWNKND DRLLQAVENG DAEKVASLLG KKGASATKHD SEGKTAFHLA
AAKGHVECLR VMITHGVDVT AQDTTGHSAL HLAAKNSHHE CIRKLLQSKC PAESVDSSGK
TALHYAAAQG CLQAVQILCE HKSPINLKDL DGNIPLLLAV QNGHSEICHF LLDHGADVNS
RNKSGRTALM LACEIGSSNA VEALIKKGAD LNLVDSLGYN ALHYSKLSEN AGIQSLLLSK
ISQDADLKTP TKPKQHDQVS KISSERSGTP KKRKAPPPPI SPTQLSDVSS PRSITSTPLS
GKESVFFAEP PFKAEISSIR ENKDRLSDST TGADSLLDIS SEADQQDLLS LLQAKVASLT
LHNKELQDKL QAKSPKEAEA DLSFDSYHST QTDLGPSLGK PGETSPPDSK SSPSVLIHSL
GKSTTDNDVR IQQLQEILQD LQKRLESSEA ERKQLQVELQ SRRAELVCLN NTEISENSSD
LSQKLKETQS KYEEAMKEVL SVQKQMKLGL VSPESMDNYS HFHELRVTEE EINVLKQDLQ
NALEESERNK EKVRELEEKL VEREKGTVIK PPVEEYEEMK SSYCSVIENM NKEKAFLFEK
YQEAQEEIMK LKDTLKSQMT QEASDEAEDM KEAMNRMIDE LNKQVSELSQ LYKEAQAELE
DYRKRKSLED VTAEYIHKAE HEKLMQLTNV SRAKAEDALS EMKSQYSKVL NELTQLKQLV
DAQKENSVSI TEHLQVITTL RTAAKEMEEK ISNLKEHLAS KEVEVAKLEK QLLEEKAAMT
DAMVPRSSYE KLQSSLESEV SVLASKLKES VKEKEKVHSE VVQIRSEVSQ VKREKENIQT
LLKSKEQEVN ELLQKFQQAQ EELAEMKRYA ESSSKLEEDK DKKINEMSKE VTKLKEALNS
LSQLSYSTSS SKRQSQQLEA LQQQVKQLQN QLAECKKQHQ EVISVYRMHL LYAVQGQMDE
DVQKVLKQIL TMCKNQSQKK
