ANR54_HUMAN
ID ANR54_HUMAN Reviewed; 300 AA.
AC Q6NXT1; Q6ZSB1; Q9UGV1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ankyrin repeat domain-containing protein 54;
DE AltName: Full=Lyn-interacting ankyrin repeat protein;
GN Name=ANKRD54; Synonyms=LIAR;
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).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
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=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-63, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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).
CC -!- FUNCTION: Plays an important role in regulating intracellular signaling
CC events associated with erythroid terminal differentiation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via ankyrin repeat region) with LYN (via SH3-
CC domain) in an activation-independent status of LYN. Forms a
CC multiprotein complex with LYN and HCLS1. Interacts with TSN2, VAV1,
CC DBNL AND LASP1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q6NXT1; O75386: TULP3; NbExp=8; IntAct=EBI-10102770, EBI-5357290;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Midbody {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm
CC during the cell cycle. EPO stimulation induces nuclear accumulation (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NXT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NXT1-2; Sequence=VSP_022770, VSP_022771;
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DR EMBL; CR456471; CAG30357.1; -; mRNA.
DR EMBL; AK127583; BAC87043.1; -; mRNA.
DR EMBL; Z97630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014641; AAH14641.1; -; mRNA.
DR EMBL; BC066909; AAH66909.1; -; mRNA.
DR CCDS; CCDS13959.1; -. [Q6NXT1-1]
DR RefSeq; NP_620152.1; NM_138797.2. [Q6NXT1-1]
DR AlphaFoldDB; Q6NXT1; -.
DR SMR; Q6NXT1; -.
DR BioGRID; 126185; 17.
DR IntAct; Q6NXT1; 10.
DR STRING; 9606.ENSP00000215941; -.
DR GlyGen; Q6NXT1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6NXT1; -.
DR PhosphoSitePlus; Q6NXT1; -.
DR BioMuta; ANKRD54; -.
DR DMDM; 125987708; -.
DR EPD; Q6NXT1; -.
DR jPOST; Q6NXT1; -.
DR MassIVE; Q6NXT1; -.
DR MaxQB; Q6NXT1; -.
DR PaxDb; Q6NXT1; -.
DR PeptideAtlas; Q6NXT1; -.
DR PRIDE; Q6NXT1; -.
DR ProteomicsDB; 66769; -. [Q6NXT1-1]
DR ProteomicsDB; 66770; -. [Q6NXT1-2]
DR Antibodypedia; 26115; 139 antibodies from 27 providers.
DR DNASU; 129138; -.
DR Ensembl; ENST00000215941.9; ENSP00000215941.4; ENSG00000100124.15. [Q6NXT1-1]
DR GeneID; 129138; -.
DR KEGG; hsa:129138; -.
DR MANE-Select; ENST00000215941.9; ENSP00000215941.4; NM_138797.4; NP_620152.1.
DR UCSC; uc003auc.4; human. [Q6NXT1-1]
DR CTD; 129138; -.
DR DisGeNET; 129138; -.
DR GeneCards; ANKRD54; -.
DR HGNC; HGNC:25185; ANKRD54.
DR HPA; ENSG00000100124; Low tissue specificity.
DR MIM; 613383; gene.
DR neXtProt; NX_Q6NXT1; -.
DR OpenTargets; ENSG00000100124; -.
DR PharmGKB; PA145149843; -.
DR VEuPathDB; HostDB:ENSG00000100124; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000157805; -.
DR HOGENOM; CLU_072816_0_0_1; -.
DR InParanoid; Q6NXT1; -.
DR OMA; DDMGNGA; -.
DR OrthoDB; 1559479at2759; -.
DR PhylomeDB; Q6NXT1; -.
DR TreeFam; TF330790; -.
DR PathwayCommons; Q6NXT1; -.
DR SignaLink; Q6NXT1; -.
DR BioGRID-ORCS; 129138; 37 hits in 1079 CRISPR screens.
DR ChiTaRS; ANKRD54; human.
DR GenomeRNAi; 129138; -.
DR Pharos; Q6NXT1; Tbio.
DR PRO; PR:Q6NXT1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q6NXT1; protein.
DR Bgee; ENSG00000100124; Expressed in right uterine tube and 171 other tissues.
DR ExpressionAtlas; Q6NXT1; baseline and differential.
DR Genevisible; Q6NXT1; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IEA:Ensembl.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:1902531; P:regulation of intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0045859; P:regulation of protein kinase activity; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..300
FT /note="Ankyrin repeat domain-containing protein 54"
FT /id="PRO_0000274493"
FT REPEAT 109..138
FT /note="ANK 1"
FT REPEAT 142..171
FT /note="ANK 2"
FT REPEAT 175..204
FT /note="ANK 3"
FT REPEAT 208..244
FT /note="ANK 4"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..241
FT /note="LYN-binding"
FT /evidence="ECO:0000250"
FT MOTIF 99..117
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250"
FT MOTIF 283..293
FT /note="Nuclear export signal (NES)"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022770"
FT VAR_SEQ 140..198
FT /note="DDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPV
FT ITTLLRG -> MVLILTSEMGWGTRHCTWRPAPTTFLSSPHCYEEVCGFFPSLSSFSPS
FT PPECSPQLVPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022771"
FT CONFLICT 99
FT /note="R -> W (in Ref. 4; AAH66909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 32505 MW; 89D48FA14975FB63 CRC64;
MAAAAGDADD EPRSGHSSSE GECAVAPEPL TDAEGLFSFA DFGSALGGGG AGLSGRASGG
AQSPLRYLHV LWQQDAEPRD ELRCKIPAGR LRRAARPHRR LGPTGKEVHA LKRLRDSANA
NDVETVQQLL EDGADPCAAD DKGRTALHFA SCNGNDQIVQ LLLDHGADPN QRDGLGNTPL
HLAACTNHVP VITTLLRGGA RVDALDRAGR TPLHLAKSKL NILQEGHAQC LEAVRLEVKQ
IIHMLREYLE RLGQHEQRER LDDLCTRLQM TSTKEQVDEV TDLLASFTSL SLQMQSMEKR
