NUCL_MACFA
ID NUCL_MACFA Reviewed; 711 AA.
AC Q4R4J7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Nucleolin;
GN Name=NCL; ORFNames=QtrA-10252, QtsA-10605;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex, and Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Nucleolin is the major nucleolar protein of growing
CC eukaryotic cells. It is found associated with intranucleolar chromatin
CC and pre-ribosomal particles. It induces chromatin decondensation by
CC binding to histone H1. It is thought to play a role in pre-rRNA
CC transcription and ribosome assembly. May play a role in the process of
CC transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-
CC 3' repeats more tightly than the telomeric single-stranded DNA 5'-
CC TTAGGG-3' repeats (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Component of the SWAP complex that
CC consists of NPM1, NCL/nucleolin, PARP1 and SWAP70. Component of a
CC complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb
CC complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and
CC NCL/nucleolin. Interacts with AICDA. Interacts with APTX. Interacts
CC with C1QBP. Interacts with ERBB4. Interacts (via C-terminus) with FMR1
CC isoform 6 (via N-terminus). Interacts with GZF1; this interaction is
CC important for nucleolar localization of GZF1. Interacts with NSUN2.
CC Interacts with NVL. Interacts (via N-terminus domain) with SETX.
CC Interacts (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with
CC TERT; the interaction is important for nucleolar localization of TERT.
CC Interacts with WDR46. Interacts with ZFP36. Interacts with LRRC34.
CC Interacts with RRP1B. Interacts with HNRNPU; this interaction occurs
CC during mitosis. Interacts with RIOK1; RIOK1 recruits NCL to PRMT5 for
CC symmetrically methylation (By similarity). Interacts with ZBTB7B (By
CC similarity). Interacts with MDK; this interaction promotes NCL
CC clustering and lateral movements of this complex into lipid rafts
CC leading to MDK internalization (By similarity). Interacts with HDGF (By
CC similarity). Interacts with ALKBH2. {ECO:0000250|UniProtKB:P09405,
CC ECO:0000250|UniProtKB:P19338}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs. {ECO:0000250}.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This modification
CC occurs exclusively on glutamate residues and results in a glycine chain
CC on the gamma-carboxyl group (By similarity). {ECO:0000250}.
CC -!- PTM: Symmetrically methylated by PRMT5 (By similarity).
CC {ECO:0000250|UniProtKB:P19338}.
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DR EMBL; AB169897; BAE01978.1; -; mRNA.
DR EMBL; AB168220; BAE00345.1; -; mRNA.
DR RefSeq; NP_001270477.1; NM_001283548.1.
DR AlphaFoldDB; Q4R4J7; -.
DR SMR; Q4R4J7; -.
DR STRING; 9541.XP_005595980.1; -.
DR PRIDE; Q4R4J7; -.
DR Ensembl; ENSMFAT00000005288; ENSMFAP00000031075; ENSMFAG00000040385.
DR GeneID; 101865794; -.
DR CTD; 4691; -.
DR VEuPathDB; HostDB:ENSMFAG00000040385; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000157437; -.
DR OMA; GYVQYSS; -.
DR OrthoDB; 1479417at2759; -.
DR Proteomes; UP000233100; Chromosome 12.
DR Bgee; ENSMFAG00000040385; Expressed in lymph node and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
DR CDD; cd12403; RRM1_NCL; 1.
DR CDD; cd12405; RRM3_NCL; 1.
DR CDD; cd12406; RRM4_NCL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR034230; Nucleolin_RRM1.
DR InterPro; IPR034234; Nucleolin_RRM3.
DR InterPro; IPR034235; Nucleolin_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 4.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..711
FT /note="Nucleolin"
FT /id="PRO_0000223181"
FT REPEAT 58..65
FT /note="1"
FT REPEAT 75..82
FT /note="2"
FT REPEAT 83..90
FT /note="3"
FT REPEAT 91..98
FT /note="4"
FT REPEAT 99..104
FT /note="5; truncated"
FT REPEAT 105..112
FT /note="6"
FT REPEAT 120..127
FT /note="7"
FT REPEAT 128..135
FT /note="8"
FT DOMAIN 308..384
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 394..467
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 487..561
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 573..648
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..135
FT /note="8 X 8 AA tandem repeats of X-T-P-X-K-K-X-X"
FT REGION 641..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..211
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 349
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 378
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 404
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 428
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 445
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 468
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 478
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 514
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 522
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 573
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 578
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 647
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 657
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 661
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 667
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 671
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 674
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 680
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 682
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 688
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 692
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 695
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 695
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 625
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
SQ SEQUENCE 711 AA; 76742 MW; 94EBE7FE82508714 CRC64;
MVKLAKAGKN QGDPKKMAPP PKEVEEDSED EEMSEDEEDD SSGEEVVIPQ KKGKKAAATS
AKKVVVSPTK KVAVATPAKK AAVTPGKKAA ATPAKKTVTP AKAVATPGKK GATPGKALVA
TPGKKGAAIP AKGAKNGKNA KKEDSDEEEE DDSEEDDEDD EDEDEDEDEI EPAVMKAAAA
APASEDEDDE DDEDDEDEDD DDEEDDSEEE AMETTPAKGK KAAKVVPVKA KNVAEDEDEE
EDDEDEDDDD DEDDEDEDDD DEDEEEEEEE EEPVKEAPGK RKKEMAKQKA APEAKKQKVE
GTEPTTAFNL FVGNLNFNKS APELKTGISD VFAKNDLAVV DVRIGMTRKF GYVDFESAED
LEKALELTGL KVFGNEIKLE KPKGKDSKKE RDARTLLAKN LPYKVTQDEL KEVFEDAAEI
RLVSKDGKSK GIAYIEFKTE ADAEKTFEEK QGTEIDGRSI SLYYTGEKGQ NQDYRGGKNS
TWSGESKTLV LSNLSYSATE ETLQEVFEKA TFIKVPQNQN GKSKGYAFIE FASFEDAKEA
LNSCNKREIE GRAIRLELQG PRGSPNARSQ PSKTLFVKGL SEDTTEETLK ESFDGSVRAR
IVTDRETGSS KGFGFVDFNS EEDAKAAKEA MEDGEIDGNK VTLDWAKPKG EGGFGGRGGG
RGGFGGRGGG RGGRGGFGGR GRGGFGGRGG FRGGRGGGGD HKPQGKKTKF E
