LIN54_PONAB
ID LIN54_PONAB Reviewed; 528 AA.
AC Q5RBN8; Q5R9N8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein lin-54 homolog;
GN Name=LIN54;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR858600; CAH90822.1; -; mRNA.
DR EMBL; CR859347; CAH91522.1; -; mRNA.
DR RefSeq; NP_001125469.1; NM_001131997.1.
DR RefSeq; XP_009238425.1; XM_009240150.1.
DR AlphaFoldDB; Q5RBN8; -.
DR SMR; Q5RBN8; -.
DR STRING; 9601.ENSPPYP00000016629; -.
DR Ensembl; ENSPPYT00000034097; ENSPPYP00000037383; ENSPPYG00000014892.
DR GeneID; 100172377; -.
DR KEGG; pon:100172377; -.
DR CTD; 132660; -.
DR eggNOG; KOG1171; Eukaryota.
DR GeneTree; ENSGT00940000155881; -.
DR InParanoid; Q5RBN8; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..528
FT /note="Protein lin-54 homolog"
FT /id="PRO_0000341391"
FT DOMAIN 300..413
FT /note="CRC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00971"
FT REGION 148..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..315
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT REGION 362..375
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT REGION 378..391
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 315
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 353
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 389
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT CONFLICT 265
FT /note="Y -> C (in Ref. 1; CAH91522)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="F -> C (in Ref. 1; CAH91522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 56284 MW; 7EEAFDD538973450 CRC64;
MEVVPAEIAK KPRTPTSGPV ITKLIFAKPI NSKAVTGQTT QVSPPVIAGR VLSQSTPGTP
SKTITISESG VIGSTLNSTT QTPNKIAISP LKSPNKAVKS TVQTITVGGV STSQFKTIIP
LATAPNVQQI QVPGSKFHYV RLVTATSASS STQPVSQNPS TNTQPLQQAK PVVVNTTPVR
MSVPIVSAQA VKQVVPKPIN PTSQIVTTSQ PQQRLIMPAT PLPQIQPNLT NLPPGTVLAP
APGTGNVGYA VLPAQYVTQL QQSSYVSIAS NSTFTGTSGI QTQARLPFNG IIPSESASRP
RKPCNCTKSL CLKLYCDCFA NGEFCNNCNC TNCYNNLEHE NERQKAIKAC LDRNPEAFKP
KIGKGKEGES DRRHSKGCNC KRSGCLKNYC ECYEAKIMCS SICKCIGCKN FEESPERKTL
MHLADAAEVR VQQQTAAKTK LSSQISDLLT RPTPALNSGG GKLPFTFVTK EVAEATCNCL
LAQAEQADKK GKSKAAAERM ILEEFGRCLM SVINSAGKAK SDPCAMNC
