RL1D1_PONAB
ID RL1D1_PONAB Reviewed; 490 AA.
AC Q5RCE6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Ribosomal L1 domain-containing protein 1;
GN Name=RSL1D1;
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=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates cellular senescence through inhibition of PTEN
CC translation. Acts as a pro-apoptotic regulator in response to DNA
CC damage. {ECO:0000250|UniProtKB:O76021}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O76021}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC Highly divergent. {ECO:0000305}.
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DR EMBL; CR858325; CAH90561.1; -; mRNA.
DR AlphaFoldDB; Q5RCE6; -.
DR SMR; Q5RCE6; -.
DR STRING; 9601.ENSPPYP00000008041; -.
DR eggNOG; KOG1685; Eukaryota.
DR InParanoid; Q5RCE6; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2000772; P:regulation of cellular senescence; ISS:UniProtKB.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..490
FT /note="Ribosomal L1 domain-containing protein 1"
FT /id="PRO_0000125845"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..313
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..311
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 415
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 468
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT CROSSLNK 380
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O76021"
SQ SEQUENCE 490 AA; 54973 MW; 5E5CDB8AA8BC3709 CRC64;
MEDSASASLS SAAATGTSTS TPAAPTARKQ LDKEQVRKAV DALLTHCKSR KNNYGLLLNE
NESLFLMVVL WKIPSKELRV RLTLPHSIRS DSEDICLFTK DEPNSTPEKT EQFYRKLLNK
HGIKTVSQII SLQTLKKEYK SYEAKLRLLS SFDFFLTDAR IRRLLPSLIG RHFYQRKKVP
VSVNLLSKNL SREINDCIGG TVLNISKSGS CSAIRIGHVG MQIEHIIENI VAVTKGLSEK
LPEKWESVKL LFVKTEKSAA LPIFSSFVSN WDEATKRSLL NKKKKEARRK RRERNFEKQK
ERKKKRQQAR KTASVLSKDD VAPESGDTTV KKPESKKEQT PEHGKKKRGR GKAQVKATNE
SEDEIPQLVP IGKKTPANEK VEIQKHATGK KSPAKSPNPS TPRGKKRKAL PASETPKAAE
SETPGKSPEK KPKIKEEAVK EKSPSLGKKD ARQTPKKPEA KFFTTPSKSV RKASHTPKKW
PKKPKVPQST
