LIN54_RAT
ID LIN54_RAT Reviewed; 749 AA.
AC Q641Z1; Q4FZV6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein lin-54 homolog;
GN Name=Lin54;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 271-749.
RC TISSUE=Placenta, and Testis;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. In G0 phase, the complex binds to more than 800 promoters and
CC is required for repression of E2F target genes. In S phase, the complex
CC selectively binds to the promoters of G2/M genes whose products are
CC required for mitosis and participates in their cell cycle dependent
CC activation. In the complex, acts as a DNA-binding protein that binds
CC the promoter of CDK1 in a sequence-specific manner. Specifically
CC recognizes the consensus motif 5'-TTYRAA-3' in target DNA.
CC {ECO:0000250|UniProtKB:Q6MZP7}.
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, RBL2, TFDP1 and TFDP2. The complex exists in
CC quiescent cells where it represses cell cycle-dependent genes. It
CC dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a
CC subcomplex that binds to MYBL2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The CRC domain mediates DNA-binding. It contains two CXC
CC subdomains (joined by a flexible linker) which are both required for
CC efficient association with target DNA. Each CXC subdomain coordinates
CC three Zn(2+) ions. {ECO:0000250|UniProtKB:Q6MZP7}.
CC -!- SIMILARITY: Belongs to the lin-54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH82043.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; AABR03090456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03091900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03089973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082043; AAH82043.1; ALT_SEQ; mRNA.
DR EMBL; BC099076; AAH99076.1; -; mRNA.
DR RefSeq; NP_001094034.1; NM_001100564.1.
DR RefSeq; XP_006250720.1; XM_006250658.3.
DR RefSeq; XP_006250721.1; XM_006250659.3.
DR AlphaFoldDB; Q641Z1; -.
DR SMR; Q641Z1; -.
DR STRING; 10116.ENSRNOP00000003006; -.
DR iPTMnet; Q641Z1; -.
DR PhosphoSitePlus; Q641Z1; -.
DR jPOST; Q641Z1; -.
DR PaxDb; Q641Z1; -.
DR PRIDE; Q641Z1; -.
DR GeneID; 305171; -.
DR KEGG; rno:305171; -.
DR CTD; 132660; -.
DR RGD; 1311361; Lin54.
DR VEuPathDB; HostDB:ENSRNOG00000002203; -.
DR eggNOG; KOG1171; Eukaryota.
DR HOGENOM; CLU_024128_0_0_1; -.
DR InParanoid; Q641Z1; -.
DR OMA; IVNHTTA; -.
DR OrthoDB; 389707at2759; -.
DR PhylomeDB; Q641Z1; -.
DR TreeFam; TF313189; -.
DR Reactome; R-RNO-1538133; G0 and Early G1.
DR PRO; PR:Q641Z1; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002203; Expressed in thymus and 19 other tissues.
DR Genevisible; Q641Z1; RN.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISO:RGD.
DR GO; GO:0001067; F:transcription regulatory region nucleic acid binding; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034728; P:nucleosome organization; IEA:Ensembl.
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 Acetylation; Activator; Cell cycle; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..749
FT /note="Protein lin-54 homolog"
FT /id="PRO_0000341392"
FT DOMAIN 521..634
FT /note="CRC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00971"
FT REGION 523..536
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT REGION 583..596
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT REGION 599..612
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 611
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 626
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 536
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 574
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 610
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
SQ SEQUENCE 749 AA; 79261 MW; C0FBA2B414FD9C11 CRC64;
MEVVPAEVNS LLPDDIMDTA ITLVDEDSIE AVIVSSPIPM ETELEEIVSI NSTGDSTATP
ISTEPITVYS NHTNQVAVNT TVSKADSNTT VKPAFPSGLQ KLGAQTPVTI SANQIILNKV
SQTSDLKLGN QTLKPDGQKL ILTTLGKSGS PIVLALPHSQ LPQAQKVTAQ AQPGDAKLPP
QQIKVVTIGG RPEVKPAIGV SALTPGSQLI NTTTQPSVLQ TQQLKTVQIA KKPRTPTSGP
VITKLIFAKP INSKAVTGQT TQASPPVVTG RVLSQSAPGT PSKTITISES GVIGSTLNST
TQTPNKIAIS PLKSPNKTVK SAVQTITVGG MSTSQFKTII PLAAAPNVQP IQVPGSKFHY
VRLVTATTAG SSAPPVSQSP SVNTQPLQQA KPVVVNTTPV RMSVPFVQAQ AVKQVVPKPI
NSTSQIVTTS QPQQRLIMPA TPLPQIQPNL TNLPPGTVLA PAPGTGNVGY AVLPAQYVTQ
LQQSSYVSIA GNSNFTGTSG IQTQARVSFN GIIPSESASR PRKPCNCTKS LCLKLYCDCF
ANGEFCNNCN CTNCYNNLEH ENERQKAIKA CLDRNPEAFK PKIGKGKEGE SDRRHSKGCN
CKRSGCLKNY CECYEAKIMC SSICKCIGCK NFEESPERKT LMHLADAAEV RVQQQTAAKT
KLSSQISDLL TRPTPALNSG GGKLPFTFVT KEVAEATCNC LLAQAEQADK KGKSKAAAER
MILEEFGRCL MSVINSAGKA KSDPCAMHC
