NUCL_PONAB
ID NUCL_PONAB Reviewed; 712 AA.
AC Q5RF26;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Nucleolin;
GN Name=NCL;
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: 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 the PRMT5
CC for symmetrically methylation (By similarity). Interacts with ZBTB7B
CC (By 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; CR857335; CAH89631.1; -; mRNA.
DR RefSeq; NP_001127178.1; NM_001133706.1.
DR AlphaFoldDB; Q5RF26; -.
DR SMR; Q5RF26; -.
DR STRING; 9601.ENSPPYP00000014829; -.
DR GeneID; 100174230; -.
DR KEGG; pon:100174230; -.
DR CTD; 4691; -.
DR eggNOG; KOG0123; Eukaryota.
DR InParanoid; Q5RF26; -.
DR OrthoDB; 1479417at2759; -.
DR Proteomes; UP000001595; Unplaced.
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..712
FT /note="Nucleolin"
FT /id="PRO_0000223182"
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 309..385
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 395..468
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 488..562
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 574..649
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..305
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 642..712
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..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..301
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 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 320
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 369
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 379
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 405
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 407
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 429
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 469
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 479
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 515
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 523
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 574
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 579
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 648
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 658
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 662
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 668
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 672
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 675
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 681
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 683
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 689
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 693
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 696
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 696
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 591
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 591
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 626
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
SQ SEQUENCE 712 AA; 76859 MW; 3E651D1A5F0E6D4C CRC64;
MVKLAKAGKN QGDPKKMAPP PKEVEEDSED EEMSEDEEDD SSGEEVVIPQ KKGKKAAATS
AKKVVVSPTK KVAVATPAKK AAVTPGKKAA ATPAKKTVTP AKAVTTPGKK GATPGKALVA
TPGKKGAAIP AKGAKNGKNA KKEDSDEEEE DDSEEDEDDD EDEDEDEDEI EPAAMKAAAA
APASEDEDDE DDEDDEDEDD DEEDDSEEEA METTPAKGKK AAKVVPVKAK NVAEDEDEEE
DDEDEDDDDD DDDDDEDDED EDDEEEEEEE EEEPVKEAPG KRKKEMAKQK AAPEAKKQKV
EGTEPTTAFN LFVGNLNFNK SAPELKTGIS DVFAKNDLAV VDVRIGMTRK FGYVDFESAE
DLEKALELTG LKVFGNEIKL EKPKGKDSKK ERDARTLLAK NLPYKVTQDE LKEVFEDAAE
IRLVSKDGKS KGIAYIEFKT EADAEKTFEE KQGTEIDGRS ISLYYTGEKG QNQDYRGGKN
STWSGESKTL VLSNLSYSAT EETLQEVFEK ATFIKVPQNQ NGKSKGYAFI EFASFEDAKE
ALNSCNKREI EGRAIRLELQ GPRGSPNARS QPSKTLFVKG LSEDTTEETL KESFDGSVRA
RIVTDRETGS SKGFGFVDFN SEEDAKAAKE AMEDGEIDGN KVTLDWAKPK GEGGFGGRGG
GRGGFGGRGG GRGGRGGFGG RGRGGFGGRG GFRGGRGGGG DHKPQGKKTK FE
