Full text data of ANKRD54
ANKRD54
(LIAR)
[Confidence: low (only semi-automatic identification from reviews)]
Ankyrin repeat domain-containing protein 54 (Lyn-interacting ankyrin repeat protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ankyrin repeat domain-containing protein 54 (Lyn-interacting ankyrin repeat protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6NXT1
ID ANR54_HUMAN Reviewed; 300 AA.
AC Q6NXT1; Q6ZSB1; Q9UGV1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 82.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Plays an important role in regulating intracellular
CC signaling events associated with erythroid terminal
CC differentiation (By similarity).
CC -!- SUBUNIT: Interacts (via ankyrin repeat region) with LYN (via SH3-
CC domain) in an activation-independent status of LYN (By
CC similarity). Forms a multiprotein complex with LYN and HCLS1 (By
CC similarity). Interacts with TSN2, VAV1, DBNL AND LASP1 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC similarity). Midbody (By similarity). Note=Shuttles between
CC nucleus and cytoplasm during the cell cycle. EPO stimulation
CC induces nuclear accumulation (By similarity).
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;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 4 ANK repeats.
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DR EMBL; CR456471; CAG30357.1; -; mRNA.
DR EMBL; AK127583; BAC87043.1; -; mRNA.
DR EMBL; Z97630; CAB63057.1; -; Genomic_DNA.
DR EMBL; BC014641; AAH14641.1; -; mRNA.
DR EMBL; BC066909; AAH66909.1; -; mRNA.
DR RefSeq; NP_620152.1; NM_138797.2.
DR UniGene; Hs.135259; -.
DR ProteinModelPortal; Q6NXT1; -.
DR SMR; Q6NXT1; 117-245.
DR STRING; 9606.ENSP00000215941; -.
DR PhosphoSite; Q6NXT1; -.
DR DMDM; 125987708; -.
DR PaxDb; Q6NXT1; -.
DR PRIDE; Q6NXT1; -.
DR DNASU; 129138; -.
DR Ensembl; ENST00000215941; ENSP00000215941; ENSG00000100124.
DR GeneID; 129138; -.
DR KEGG; hsa:129138; -.
DR UCSC; uc003auc.3; human.
DR CTD; 129138; -.
DR GeneCards; GC22M038226; -.
DR HGNC; HGNC:25185; ANKRD54.
DR MIM; 613383; gene.
DR neXtProt; NX_Q6NXT1; -.
DR PharmGKB; PA145149843; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000008674; -.
DR HOVERGEN; HBG080858; -.
DR InParanoid; Q6NXT1; -.
DR OMA; SLQMQNM; -.
DR OrthoDB; EOG722J9P; -.
DR PhylomeDB; Q6NXT1; -.
DR GenomeRNAi; 129138; -.
DR NextBio; 82553; -.
DR PRO; PR:Q6NXT1; -.
DR ArrayExpress; Q6NXT1; -.
DR Bgee; Q6NXT1; -.
DR CleanEx; HS_ANKRD54; -.
DR Genevestigator; Q6NXT1; -.
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; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; 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:0010627; P:regulation of intracellular protein kinase cascade; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR Pfam; PF12796; Ank_2; 2.
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; Complete proteome;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 300 Ankyrin repeat domain-containing protein
FT 54.
FT /FTId=PRO_0000274493.
FT REPEAT 109 138 ANK 1.
FT REPEAT 142 171 ANK 2.
FT REPEAT 175 204 ANK 3.
FT REPEAT 208 244 ANK 4.
FT REGION 99 117 Nuclear localization signal (NLS) (By
FT similarity).
FT REGION 141 241 LYN-binding (By similarity).
FT REGION 283 293 Nuclear export signal (NES) (By
FT similarity).
FT COMPBIAS 47 52 Poly-Gly.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 58 58 Phosphoserine.
FT MOD_RES 63 63 Phosphoserine.
FT VAR_SEQ 1 139 Missing (in isoform 2).
FT /FTId=VSP_022770.
FT VAR_SEQ 140 198 DDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPL
FT HLAACTNHVPVITTLLRG -> MVLILTSEMGWGTRHCTWR
FT PAPTTFLSSPHCYEEVCGFFPSLSSFSPSPPECSPQLVPA
FT (in isoform 2).
FT /FTId=VSP_022771.
FT CONFLICT 99 99 R -> W (in Ref. 4; AAH66909).
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
//
ID ANR54_HUMAN Reviewed; 300 AA.
AC Q6NXT1; Q6ZSB1; Q9UGV1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 82.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Plays an important role in regulating intracellular
CC signaling events associated with erythroid terminal
CC differentiation (By similarity).
CC -!- SUBUNIT: Interacts (via ankyrin repeat region) with LYN (via SH3-
CC domain) in an activation-independent status of LYN (By
CC similarity). Forms a multiprotein complex with LYN and HCLS1 (By
CC similarity). Interacts with TSN2, VAV1, DBNL AND LASP1 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC similarity). Midbody (By similarity). Note=Shuttles between
CC nucleus and cytoplasm during the cell cycle. EPO stimulation
CC induces nuclear accumulation (By similarity).
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;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 4 ANK repeats.
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DR EMBL; CR456471; CAG30357.1; -; mRNA.
DR EMBL; AK127583; BAC87043.1; -; mRNA.
DR EMBL; Z97630; CAB63057.1; -; Genomic_DNA.
DR EMBL; BC014641; AAH14641.1; -; mRNA.
DR EMBL; BC066909; AAH66909.1; -; mRNA.
DR RefSeq; NP_620152.1; NM_138797.2.
DR UniGene; Hs.135259; -.
DR ProteinModelPortal; Q6NXT1; -.
DR SMR; Q6NXT1; 117-245.
DR STRING; 9606.ENSP00000215941; -.
DR PhosphoSite; Q6NXT1; -.
DR DMDM; 125987708; -.
DR PaxDb; Q6NXT1; -.
DR PRIDE; Q6NXT1; -.
DR DNASU; 129138; -.
DR Ensembl; ENST00000215941; ENSP00000215941; ENSG00000100124.
DR GeneID; 129138; -.
DR KEGG; hsa:129138; -.
DR UCSC; uc003auc.3; human.
DR CTD; 129138; -.
DR GeneCards; GC22M038226; -.
DR HGNC; HGNC:25185; ANKRD54.
DR MIM; 613383; gene.
DR neXtProt; NX_Q6NXT1; -.
DR PharmGKB; PA145149843; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000008674; -.
DR HOVERGEN; HBG080858; -.
DR InParanoid; Q6NXT1; -.
DR OMA; SLQMQNM; -.
DR OrthoDB; EOG722J9P; -.
DR PhylomeDB; Q6NXT1; -.
DR GenomeRNAi; 129138; -.
DR NextBio; 82553; -.
DR PRO; PR:Q6NXT1; -.
DR ArrayExpress; Q6NXT1; -.
DR Bgee; Q6NXT1; -.
DR CleanEx; HS_ANKRD54; -.
DR Genevestigator; Q6NXT1; -.
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; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; 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:0010627; P:regulation of intracellular protein kinase cascade; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR Pfam; PF12796; Ank_2; 2.
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; Complete proteome;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 300 Ankyrin repeat domain-containing protein
FT 54.
FT /FTId=PRO_0000274493.
FT REPEAT 109 138 ANK 1.
FT REPEAT 142 171 ANK 2.
FT REPEAT 175 204 ANK 3.
FT REPEAT 208 244 ANK 4.
FT REGION 99 117 Nuclear localization signal (NLS) (By
FT similarity).
FT REGION 141 241 LYN-binding (By similarity).
FT REGION 283 293 Nuclear export signal (NES) (By
FT similarity).
FT COMPBIAS 47 52 Poly-Gly.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 58 58 Phosphoserine.
FT MOD_RES 63 63 Phosphoserine.
FT VAR_SEQ 1 139 Missing (in isoform 2).
FT /FTId=VSP_022770.
FT VAR_SEQ 140 198 DDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPL
FT HLAACTNHVPVITTLLRG -> MVLILTSEMGWGTRHCTWR
FT PAPTTFLSSPHCYEEVCGFFPSLSSFSPSPPECSPQLVPA
FT (in isoform 2).
FT /FTId=VSP_022771.
FT CONFLICT 99 99 R -> W (in Ref. 4; AAH66909).
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
//
MIM
613383
*RECORD*
*FIELD* NO
613383
*FIELD* TI
*613383 ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 54; ANKRD54
;;LYN-INTERACTING ANKYRIN REPEAT PROTEIN; LIAR
read more*FIELD* TX
CLONING
Samuels et al. (2009) cloned mouse Ankrd54, which they called Liar. The
deduced 299-amino acid protein has an N-terminal ATP-binding P loop,
followed by a nuclear localization signal, 4 ankyrin (see 612641)
repeats, and a C-terminal nuclear export signal. It has several
potential serine phosphorylation sites. Mouse and human LIAR share 92%
amino acid identity. Northern blot analysis detected variable Liar
expression in all mouse tissues examined, with highest expression in
testis. Variable mRNA and protein expression was also detected in all
erythropoietic cell lines examined. In situ hybridization of mouse
embryos at embryonic day 10 revealed Liar expression in brachial arches,
maxillary process, fore and hind limb buds, and gastrointestinal tract.
GENE FUNCTION
Samuels et al. (2009) showed that mouse Lyn (165120) and Liar interacted
in a yeast 2-hybrid screen. Liar was not a substrate for Lyn kinase
activity. Domain analysis revealed that the SH3 domain of Lyn and the
ankyrin repeat domain of Liar were required for the interaction. Lyn and
Liar formed a multiprotein complex with Hs1 (HCLS1; 601306) in mouse
erythroid cells. Samuels et al. (2009) observed a transient
translocation and accumulation of Liar within the nuclear compartment
that was associated with terminal differentiation in mouse erythroid
cells, and expression of Liar decreased following differentiation.
Overexpression of Liar inhibited erythroid differentiation and altered
erythropoietin (EPO; 133170) signaling via Erk2 (MAPK1; 176948), Stat5
(STAT5A; 601511), Akt (see 164730), and Lyn.
MAPPING
By genomic sequence analysis, Samuels et al. (2009) mapped the ANKRD54
gene to chromosome 22q13.1. They mapped the mouse Ankrd54 gene to a
region of chromosome 15 that shares homology of synteny with human
chro0mosome 22q13.1.
*FIELD* RF
1. Samuels, A. L.; Klinken, S. P.; Ingley, E.: Liar, a novel Lyn-binding
nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced
differentiation. Blood 113: 3845-3856, 2009.
*FIELD* CD
Patricia A. Hartz: 4/26/2010
*FIELD* ED
terry: 12/03/2010
mgross: 4/29/2010
mgross: 4/26/2010
*RECORD*
*FIELD* NO
613383
*FIELD* TI
*613383 ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 54; ANKRD54
;;LYN-INTERACTING ANKYRIN REPEAT PROTEIN; LIAR
read more*FIELD* TX
CLONING
Samuels et al. (2009) cloned mouse Ankrd54, which they called Liar. The
deduced 299-amino acid protein has an N-terminal ATP-binding P loop,
followed by a nuclear localization signal, 4 ankyrin (see 612641)
repeats, and a C-terminal nuclear export signal. It has several
potential serine phosphorylation sites. Mouse and human LIAR share 92%
amino acid identity. Northern blot analysis detected variable Liar
expression in all mouse tissues examined, with highest expression in
testis. Variable mRNA and protein expression was also detected in all
erythropoietic cell lines examined. In situ hybridization of mouse
embryos at embryonic day 10 revealed Liar expression in brachial arches,
maxillary process, fore and hind limb buds, and gastrointestinal tract.
GENE FUNCTION
Samuels et al. (2009) showed that mouse Lyn (165120) and Liar interacted
in a yeast 2-hybrid screen. Liar was not a substrate for Lyn kinase
activity. Domain analysis revealed that the SH3 domain of Lyn and the
ankyrin repeat domain of Liar were required for the interaction. Lyn and
Liar formed a multiprotein complex with Hs1 (HCLS1; 601306) in mouse
erythroid cells. Samuels et al. (2009) observed a transient
translocation and accumulation of Liar within the nuclear compartment
that was associated with terminal differentiation in mouse erythroid
cells, and expression of Liar decreased following differentiation.
Overexpression of Liar inhibited erythroid differentiation and altered
erythropoietin (EPO; 133170) signaling via Erk2 (MAPK1; 176948), Stat5
(STAT5A; 601511), Akt (see 164730), and Lyn.
MAPPING
By genomic sequence analysis, Samuels et al. (2009) mapped the ANKRD54
gene to chromosome 22q13.1. They mapped the mouse Ankrd54 gene to a
region of chromosome 15 that shares homology of synteny with human
chro0mosome 22q13.1.
*FIELD* RF
1. Samuels, A. L.; Klinken, S. P.; Ingley, E.: Liar, a novel Lyn-binding
nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced
differentiation. Blood 113: 3845-3856, 2009.
*FIELD* CD
Patricia A. Hartz: 4/26/2010
*FIELD* ED
terry: 12/03/2010
mgross: 4/29/2010
mgross: 4/26/2010