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Protein

Nucleolin

Gene

Ncl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity).By similarity

GO - Molecular functioni

  • calcium ion binding Source: RGD
  • ErbB-4 class receptor binding Source: RGD
  • histone binding Source: RGD
  • laminin binding Source: RGD
  • receptor binding Source: RGD
  • RNA binding Source: RGD
  • rRNA primary transcript binding Source: RGD
  • selenocysteine insertion sequence binding Source: RGD
  • sequence-specific DNA binding Source: RGD
  • single-stranded DNA binding Source: RGD
  • telomeric DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to lipopolysaccharide Source: RGD
  • endocytosis Source: RGD
  • liver regeneration Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • positive regulation of interleukin-6 secretion Source: RGD
  • positive regulation of tumor necrosis factor production Source: RGD
  • regulation of rRNA processing Source: RGD
  • spermatogenesis Source: RGD

Keywordsi

Molecular functionDNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolin
Alternative name(s):
Protein C23
Gene namesi
Name:Ncl
Synonyms:Nuc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3153. Ncl.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000816941 – 713NucleolinAdd BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei15N6-acetyllysineBy similarity1
Modified residuei16N6-acetyllysineBy similarity1
Modified residuei28PhosphoserineCombined sources1
Modified residuei34PhosphoserineBy similarity1
Modified residuei40PhosphoserineCombined sources1
Modified residuei41PhosphoserineCombined sources1
Modified residuei67PhosphoserineBy similarity1
Modified residuei69PhosphothreonineBy similarity1
Modified residuei76PhosphothreonineBy similarity1
Modified residuei84PhosphothreonineBy similarity1
Modified residuei92PhosphothreonineBy similarity1
Modified residuei96N6-acetyllysineBy similarity1
Modified residuei99PhosphothreonineBy similarity1
Modified residuei102N6-acetyllysineBy similarity1
Modified residuei106PhosphothreonineBy similarity1
Modified residuei109N6-acetyllysineBy similarity1
Modified residuei116N6-acetyllysineBy similarity1
Modified residuei121PhosphothreonineBy similarity1
Modified residuei124N6-acetyllysineBy similarity1
Modified residuei145PhosphoserineCombined sources1
Modified residuei157PhosphoserineCombined sources1
Modified residuei187PhosphoserineCombined sources1
Modified residuei213PhosphoserineCombined sources1
Modified residuei221PhosphothreonineBy similarity1
Cross-linki301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei305PhosphoserineCombined sources1
Modified residuei322N6-acetyllysineBy similarity1
Cross-linki328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei352N6-acetyllysineBy similarity1
Modified residuei360PhosphoserineBy similarity1
Modified residuei371PhosphothreonineBy similarity1
Cross-linki374Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei381N6-acetyllysine; alternateBy similarity1
Cross-linki381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei402N6-acetyllysineBy similarity1
Modified residuei405PhosphoserineCombined sources1
Modified residuei409PhosphothreonineBy similarity1
Modified residuei448N6-acetyllysineBy similarity1
Modified residuei462PhosphoserineBy similarity1
Modified residuei464PhosphoserineBy similarity1
Modified residuei471N6-acetyllysineBy similarity1
Modified residuei480N6-acetyllysineBy similarity1
Modified residuei516N6-acetyllysine; alternateBy similarity1
Cross-linki516Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei524N6-acetyllysineBy similarity1
Modified residuei566PhosphoserineCombined sources1
Modified residuei575N6-acetyllysineBy similarity1
Modified residuei580N6-acetyllysine; alternateBy similarity1
Cross-linki580Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei583PhosphoserineCombined sources1
Cross-linki592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei594PhosphoserineBy similarity1
Modified residuei622PhosphoserineCombined sources1
Cross-linki627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei649N6-acetyllysineBy similarity1
Modified residuei659Asymmetric dimethylarginineBy similarity1
Modified residuei663Asymmetric dimethylarginineBy similarity1
Modified residuei669Asymmetric dimethylarginineBy similarity1
Modified residuei673Asymmetric dimethylarginineBy similarity1
Modified residuei676Asymmetric dimethylarginineBy similarity1
Modified residuei697Omega-N-methylarginineBy similarity1

Post-translational modificationi

Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP13383.
PRIDEiP13383.

PTM databases

iPTMnetiP13383.
PhosphoSitePlusiP13383.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the SWAP complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. Interacts with AICDA. Interacts with APTX. Interacts with C1QBP. Interacts with ERBB4. Interacts (via C-terminus) with FMR1 isoform 6 (via N-terminus). Interacts with GZF1; this interaction is important for nucleolar localization of GZF1. Interacts with NSUN2. Interacts with NVL. Interacts (via N-terminus domain) with SETX. Interacts (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with TERT; the interaction is important for nucleolar localization of TERT. Interacts with WDR46. Interacts with ZFP36. Interacts with LRRC34.By similarity

GO - Molecular functioni

  • ErbB-4 class receptor binding Source: RGD
  • histone binding Source: RGD
  • laminin binding Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

IntActiP13383. 2 interactors.
STRINGi10116.ENSRNOP00000024712.

Structurei

3D structure databases

ProteinModelPortaliP13383.
SMRiP13383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati58 – 6518
Repeati75 – 8228
Repeati83 – 9038
Repeati91 – 9848
Repeati99 – 1045; truncated6
Repeati105 – 11268
Repeati120 – 12778
Repeati128 – 13588
Domaini311 – 387RRM 1PROSITE-ProRule annotationAdd BLAST77
Domaini397 – 470RRM 2PROSITE-ProRule annotationAdd BLAST74
Domaini489 – 563RRM 3PROSITE-ProRule annotationAdd BLAST75
Domaini575 – 650RRM 4PROSITE-ProRule annotationAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni58 – 1358 X 8 AA tandem repeats of X-T-P-X-K-K-X-XAdd BLAST78

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi143 – 168Asp/Glu-rich (acidic)Add BLAST26
Compositional biasi188 – 216Asp/Glu-rich (acidic)Add BLAST29
Compositional biasi242 – 275Asp/Glu-rich (acidic)Add BLAST34
Compositional biasi652 – 703Arg/Gly/Phe-richAdd BLAST52

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IRS7. Eukaryota.
ENOG410XSFV. LUCA.
HOVERGENiHBG002295.
InParanoidiP13383.

Family and domain databases

CDDicd12403. RRM1_NCL. 1 hit.
cd12404. RRM2_NCL. 1 hit.
cd12405. RRM3_NCL. 1 hit.
cd12406. RRM4_NCL. 1 hit.
InterProiView protein in InterPro
IPR034230. Nucleolin_RRM1.
IPR034233. Nucleolin_RRM2.
IPR034234. Nucleolin_RRM3.
IPR034235. Nucleolin_RRM4.
IPR000504. RRM_dom.
PfamiView protein in Pfam
PF00076. RRM_1. 4 hits.
SMARTiView protein in SMART
SM00360. RRM. 4 hits.
SUPFAMiSSF54928. SSF54928. 4 hits.
PROSITEiView protein in PROSITE
PS50102. RRM. 4 hits.

Sequencei

Sequence statusi: Complete.

P13383-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLAKAGKT HGESKKMAPP PKEVEEDSED EEMSEDEDDS SGEEEVVIPQ
60 70 80 90 100
KKGKKATTTP AKKVVVSQTK KAAVPTPAKK AAVTPGKKAA ATPAKKAVTP
110 120 130 140 150
AKVVPTPGKK GAAQAKALVP TPGKKGAVTP AKGAKNGKNA KKEDSDEDED
160 170 180 190 200
EEDEDDSDED EDEEDEFEPP VVKGVKPAKA APAAPASEDE DEEDDDDEDD
210 220 230 240 250
DDDDEEEEEE DDSEEEVMEI TPAKGKKTPA KVVPVKAKSV AEEEEDDEDD
260 270 280 290 300
EDEEEDEDEE DEEDDEDEDE EEEEEPVKAA PGKRKKEMTK QKEAPEAKKQ
310 320 330 340 350
KIEGSEPTTP FNLFIGNLNP NKSVAELKVA ISELFAKNDL AAVDVRTGTN
360 370 380 390 400
RKFGYVDFES AEDLEKALEL TGLKVFGNEI KLEKPKGRDS KKVRAARTLL
410 420 430 440 450
AKNLSFNITE DELKEVFEDA VEIRLVSQDG RSKGIAYIEF KSEADAEKNL
460 470 480 490 500
EEKQGAEIDG RSVSLYYTGE KGQRQERTGK NSTWSGESKT LVLSNLSYSA
510 520 530 540 550
TEETLQEVFE KATFIKVPQN PHGKSKGYAF IEFASFEDAK EALNSCNKME
560 570 580 590 600
IEGRTIRLEL QGPRGSPNAR SQPSKTLFVK GLSEDTTEET LKESFEGSVR
610 620 630 640 650
ARIVTDRETG SSKGFGFVDF NSEEDAKAAK EAMEDGEIDG NKVTLDWAKP
660 670 680 690 700
KGEGGFGGRG GGRGGFGGRG GGRGGRGGFG GRGRGGFGGR GGFRGGRGGG
710
GDFKPQGKKT KFE
Length:713
Mass (Da):77,147
Last modified:January 23, 2007 - v3
Checksum:i9652B27BFD12C8EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55022
, M55015, M55017, M55020 Genomic DNA. Translation: AAA41732.1.
M22090 Genomic DNA. Translation: AAA41733.1.
PIRiJH0148.
UniGeneiRn.144561.

Genome annotation databases

UCSCiRGD:3153. rat.

Similar proteinsi

Entry informationi

Entry nameiNUCL_RAT
AccessioniPrimary (citable) accession number: P13383
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 142 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome