LIN54_HUMAN
ID LIN54_HUMAN Reviewed; 749 AA.
AC Q6MZP7; Q32M68; Q32M69; Q6N071; Q76B60;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein lin-54 homolog;
DE AltName: Full=CXC domain-containing protein 1;
GN Name=LIN54; Synonyms=CXCDC1, KIAA2037;
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 4).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Uterine endothelium;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
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 FUNCTION, AND IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17671431; DOI=10.4161/cc.6.15.4512;
RA Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B.,
RA Gagrica S., Haenel F., Brehm A., Gaubatz S.;
RT "LINC, a human complex that is related to pRB-containing complexes in
RT invertebrates regulates the expression of G2/M genes.";
RL Cell Cycle 6:1903-1913(2007).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
RA Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
RA Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
RT "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex
RT represses human cell cycle-dependent genes in quiescence.";
RL Mol. Cell 26:539-551(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP FUNCTION, DNA-BINDING TO CDK1 PROMOTER, DOMAIN, CELL CYCLE INVOLVEMENT, AND
RP MUTAGENESIS OF CYS-525 AND CYS-527.
RX PubMed=19725879; DOI=10.1111/j.1742-4658.2009.07261.x;
RA Schmit F., Cremer S., Gaubatz S.;
RT "LIN54 is an essential core subunit of the DREAM/LINC complex that binds to
RT the cdc2 promoter in a sequence-specific manner.";
RL FEBS J. 276:5703-5716(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-244 AND LYS-249, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-314, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-282; SER-310;
RP SER-314 AND SER-635, 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-139; LYS-357; LYS-639; LYS-659
RP AND LYS-661, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 515-646 IN COMPLEX WITH DNA AND
RP ZINC, FUNCTION, DOMAIN, AND MUTAGENESIS OF TYR-536 AND TYR-610.
RX PubMed=27465258; DOI=10.1038/ncomms12301;
RA Marceau A.H., Felthousen J.G., Goetsch P.D., Iness A.N., Lee H.W.,
RA Tripathi S.M., Strome S., Litovchick L., Rubin S.M.;
RT "Structural basis for LIN54 recognition of CHR elements in cell cycle-
RT regulated promoters.";
RL Nat. Commun. 7:12301-12301(2016).
CC -!- FUNCTION: Component of the DREAM complex, a multiprotein complex that
CC can both act as a transcription activator or repressor depending on the
CC context (PubMed:17671431, PubMed:17531812). In G0 phase, the complex
CC binds to more than 800 promoters and is required for repression of E2F
CC target genes (PubMed:17671431, PubMed:17531812). In S phase, the
CC complex selectively binds to the promoters of G2/M genes whose products
CC are required for mitosis and participates in their cell cycle dependent
CC activation (PubMed:17671431, PubMed:17531812). In the complex, acts as
CC a DNA-binding protein that binds the promoter of CDK1 in a sequence-
CC specific manner (PubMed:19725879). Specifically recognizes the
CC consensus motif 5'-TTYRAA-3' in target DNA (PubMed:27465258).
CC {ECO:0000269|PubMed:17531812, ECO:0000269|PubMed:17671431,
CC ECO:0000269|PubMed:19725879, ECO:0000269|PubMed:27465258}.
CC -!- SUBUNIT: Component of the DREAM complex (also named LINC complex) at
CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes. It dissociates in
CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC to MYBL2. {ECO:0000269|PubMed:17531812, ECO:0000269|PubMed:17671431}.
CC -!- INTERACTION:
CC Q6MZP7; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-1389411, EBI-11524452;
CC Q6MZP7; P10244: MYBL2; NbExp=4; IntAct=EBI-1389411, EBI-1389468;
CC Q6MZP7; Q13952-2: NFYC; NbExp=3; IntAct=EBI-1389411, EBI-11956831;
CC Q6MZP7; Q08999: RBL2; NbExp=10; IntAct=EBI-1389411, EBI-971439;
CC Q6MZP7; Q15428: SF3A2; NbExp=3; IntAct=EBI-1389411, EBI-2462271;
CC Q6MZP7; Q02447: SP3; NbExp=3; IntAct=EBI-1389411, EBI-348158;
CC Q6MZP7; P52747: ZNF143; NbExp=3; IntAct=EBI-1389411, EBI-2849334;
CC Q6MZP7; P36508: ZNF76; NbExp=3; IntAct=EBI-1389411, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6MZP7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6MZP7-2; Sequence=VSP_034274;
CC Name=3;
CC IsoId=Q6MZP7-3; Sequence=VSP_034273;
CC Name=4;
CC IsoId=Q6MZP7-4; Sequence=VSP_034272;
CC Name=5;
CC IsoId=Q6MZP7-5; Sequence=VSP_034275, VSP_034276;
CC -!- DOMAIN: The CRC domain mediates DNA-binding (PubMed:19725879,
CC PubMed:27465258). It contains two CXC subdomains (joined by a flexible
CC linker) which are both required for efficient association with target
CC DNA (PubMed:27465258). Each CXC subdomain coordinates three Zn(2+) ions
CC (PubMed:27465258). {ECO:0000269|PubMed:19725879,
CC ECO:0000269|PubMed:27465258}.
CC -!- SIMILARITY: Belongs to the lin-54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98377.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB111889; BAC98377.1; ALT_INIT; mRNA.
DR EMBL; AK292769; BAF85458.1; -; mRNA.
DR EMBL; BX640657; CAE45799.1; -; mRNA.
DR EMBL; BX640966; CAE45981.1; -; mRNA.
DR EMBL; AC021105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109277; AAI09278.1; -; mRNA.
DR EMBL; BC109278; AAI09279.1; -; mRNA.
DR CCDS; CCDS3599.1; -. [Q6MZP7-1]
DR CCDS; CCDS47089.1; -. [Q6MZP7-3]
DR CCDS; CCDS75157.1; -. [Q6MZP7-2]
DR RefSeq; NP_001108479.1; NM_001115007.2. [Q6MZP7-3]
DR RefSeq; NP_001108480.1; NM_001115008.2. [Q6MZP7-3]
DR RefSeq; NP_001275925.1; NM_001288996.1. [Q6MZP7-2]
DR RefSeq; NP_001275926.1; NM_001288997.1. [Q6MZP7-3]
DR RefSeq; NP_919258.2; NM_194282.3. [Q6MZP7-1]
DR RefSeq; XP_005262807.1; XM_005262750.4. [Q6MZP7-1]
DR RefSeq; XP_006714144.1; XM_006714081.3. [Q6MZP7-1]
DR RefSeq; XP_016863217.1; XM_017007728.1. [Q6MZP7-2]
DR RefSeq; XP_016863218.1; XM_017007729.1. [Q6MZP7-4]
DR RefSeq; XP_016863219.1; XM_017007730.1. [Q6MZP7-4]
DR PDB; 5FD3; X-ray; 2.42 A; A/B=515-646.
DR PDBsum; 5FD3; -.
DR AlphaFoldDB; Q6MZP7; -.
DR SMR; Q6MZP7; -.
DR BioGRID; 126328; 71.
DR CORUM; Q6MZP7; -.
DR IntAct; Q6MZP7; 71.
DR MINT; Q6MZP7; -.
DR STRING; 9606.ENSP00000341947; -.
DR GlyConnect; 2849; 1 O-Linked glycan (1 site).
DR GlyGen; Q6MZP7; 15 sites, 2 O-linked glycans (15 sites).
DR iPTMnet; Q6MZP7; -.
DR PhosphoSitePlus; Q6MZP7; -.
DR BioMuta; LIN54; -.
DR DMDM; 313104222; -.
DR EPD; Q6MZP7; -.
DR jPOST; Q6MZP7; -.
DR MassIVE; Q6MZP7; -.
DR MaxQB; Q6MZP7; -.
DR PaxDb; Q6MZP7; -.
DR PeptideAtlas; Q6MZP7; -.
DR PRIDE; Q6MZP7; -.
DR ProteomicsDB; 66576; -. [Q6MZP7-1]
DR ProteomicsDB; 66577; -. [Q6MZP7-2]
DR ProteomicsDB; 66578; -. [Q6MZP7-3]
DR ProteomicsDB; 66579; -. [Q6MZP7-4]
DR ProteomicsDB; 66580; -. [Q6MZP7-5]
DR Antibodypedia; 55895; 61 antibodies from 18 providers.
DR DNASU; 132660; -.
DR Ensembl; ENST00000340417.8; ENSP00000341947.3; ENSG00000189308.11. [Q6MZP7-1]
DR Ensembl; ENST00000442461.6; ENSP00000398265.2; ENSG00000189308.11. [Q6MZP7-3]
DR Ensembl; ENST00000446851.6; ENSP00000407139.2; ENSG00000189308.11. [Q6MZP7-3]
DR Ensembl; ENST00000505397.1; ENSP00000425844.1; ENSG00000189308.11. [Q6MZP7-1]
DR Ensembl; ENST00000506560.5; ENSP00000423475.1; ENSG00000189308.11. [Q6MZP7-2]
DR Ensembl; ENST00000508171.5; ENSP00000427413.1; ENSG00000189308.11. [Q6MZP7-5]
DR Ensembl; ENST00000510557.5; ENSP00000421045.1; ENSG00000189308.11. [Q6MZP7-3]
DR GeneID; 132660; -.
DR KEGG; hsa:132660; -.
DR MANE-Select; ENST00000340417.8; ENSP00000341947.3; NM_194282.4; NP_919258.2.
DR UCSC; uc003hnx.5; human. [Q6MZP7-1]
DR CTD; 132660; -.
DR DisGeNET; 132660; -.
DR GeneCards; LIN54; -.
DR HGNC; HGNC:25397; LIN54.
DR HPA; ENSG00000189308; Low tissue specificity.
DR MIM; 613367; gene.
DR neXtProt; NX_Q6MZP7; -.
DR OpenTargets; ENSG00000189308; -.
DR PharmGKB; PA162394056; -.
DR VEuPathDB; HostDB:ENSG00000189308; -.
DR eggNOG; KOG1171; Eukaryota.
DR GeneTree; ENSGT00940000155881; -.
DR HOGENOM; CLU_024128_1_0_1; -.
DR InParanoid; Q6MZP7; -.
DR OMA; IVNHTTA; -.
DR PhylomeDB; Q6MZP7; -.
DR TreeFam; TF313189; -.
DR PathwayCommons; Q6MZP7; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR Reactome; R-HSA-1538133; G0 and Early G1.
DR Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR SignaLink; Q6MZP7; -.
DR BioGRID-ORCS; 132660; 220 hits in 1089 CRISPR screens.
DR ChiTaRS; LIN54; human.
DR GenomeRNAi; 132660; -.
DR Pharos; Q6MZP7; Tbio.
DR PRO; PR:Q6MZP7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6MZP7; protein.
DR Bgee; ENSG00000189308; Expressed in ventricular zone and 105 other tissues.
DR ExpressionAtlas; Q6MZP7; baseline and differential.
DR Genevisible; Q6MZP7; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001067; F:transcription regulatory region nucleic acid binding; IDA:ARUK-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034728; P:nucleosome organization; IDA:ARUK-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR005172; CRC.
DR InterPro; IPR028307; Lin-54_fam.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR12446; PTHR12446; 1.
DR Pfam; PF03638; TCR; 2.
DR SMART; SM01114; CXC; 2.
DR PROSITE; PS51634; CRC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Cell cycle;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc.
FT CHAIN 1..749
FT /note="Protein lin-54 homolog"
FT /id="PRO_0000341389"
FT DOMAIN 521..634
FT /note="CRC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00971"
FT REGION 369..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..536
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:27465258"
FT REGION 583..596
FT /note="Linker"
FT /evidence="ECO:0000269|PubMed:27465258"
FT REGION 599..612
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:27465258"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 611
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 626
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:5FD3"
FT BINDING 629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:5FD3"
FT SITE 536
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000269|PubMed:27465258"
FT SITE 574
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:27465258"
FT SITE 610
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000269|PubMed:27465258"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..401
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_034272"
FT VAR_SEQ 8..228
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_034273"
FT VAR_SEQ 229..317
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034274"
FT VAR_SEQ 229..243
FT /note="IAKKPRTPTSGPVIT -> VGFFHSLLPELHQRP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034275"
FT VAR_SEQ 244..749
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034276"
FT MUTAGEN 525
FT /note="C->Y: Abolishes DNA-binding to the CDK1 promoter;
FT when associated with Y-527."
FT /evidence="ECO:0000269|PubMed:19725879"
FT MUTAGEN 527
FT /note="C->Y: Abolishes DNA-binding to the CDK1 promoter;
FT when associated with Y-525."
FT /evidence="ECO:0000269|PubMed:19725879"
FT MUTAGEN 536
FT /note="Y->A,F,R: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:27465258"
FT MUTAGEN 610
FT /note="Y->A,F,R: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:27465258"
FT CONFLICT 9
FT /note="N -> S (in Ref. 3; CAE45981)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="D -> A (in Ref. 3; CAE45981)"
FT /evidence="ECO:0000305"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:5FD3"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:5FD3"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:5FD3"
FT HELIX 561..574
FT /evidence="ECO:0007829|PDB:5FD3"
FT TURN 576..579
FT /evidence="ECO:0007829|PDB:5FD3"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:5FD3"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:5FD3"
FT HELIX 636..642
FT /evidence="ECO:0007829|PDB:5FD3"
SQ SEQUENCE 749 AA; 79494 MW; A3E4513CB0118B78 CRC64;
MEVVPAEVNS LLPEEIMDTG ITLVDDDSIE AVIVSSPIPM ETELEEIVNI NSTGDSTATP
ISTEPITVYS NHTNQVAVNT TITKADSNTT VKPAFPSGLQ KLGAQTPVTI SANQIILNKV
SQTSDLKLGN QTLKPDGQKL ILTTLGKSGS PIVLALPHSQ LPQAQKVTTQ AQSGDAKLPP
QQIKVVTIGG RPEVKPVIGV SALTPGSQLI NTTTQPSVLQ TQQLKTVQIA KKPRTPTSGP
VITKLIFAKP INSKAVTGQT TQVSPPVIAG RVLSQSTPGT PSKTITISES GVIGSTLNST
TQTPNKIAIS PLKSPNKAVK STVQTITVGG VSTSQFKTII PLATAPNVQQ IQVPGSKFHY
VRLVTATSAS SSTQPVSQNP STNTQPLQQA KPVVVNTTPV RMSVPIVSAQ AVKQVVPKPI
NPTSQIVTTS QPQQRLIMPA TPLPQIQPNL TNLPPGTVLA PAPGTGNVGY AVLPAQYVTQ
LQQSSYVSIA SNSTFTGTSG IQTQARLPFN GIIPSESASR PRKPCNCTKS LCLKLYCDCF
ANGEFCNNCN CTNCYNNLEH ENERQKAIKA CLDRNPEAFK PKIGKGKEGE SDRRHSKGCN
CKRSGCLKNY CECYEAKIMC SSICKCIGCK NFEESPERKT LMHLADAAEV RVQQQTAAKT
KLSSQISDLL TRPTPALNSG GGKLPFTFVT KEVAEATCNC LLAQAEQADK KGKSKAAAER
MILEEFGRCL MSVINSAGKA KSDPCAMNC
