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Protein

Nucleolin

Gene

NCL

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • telomeric DNA binding Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115053-MONOMER.
SIGNORiP19338.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolin
Alternative name(s):
Protein C23
Gene namesi
Name:NCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:7667. NCL.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • extracellular exosome Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: CACAO
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi4691.
OpenTargetsiENSG00000115053.
PharmGKBiPA31469.

Polymorphism and mutation databases

BioMutaiNCL.
DMDMi90110781.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000816912 – 710NucleolinAdd BLAST709

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9N6-acetyllysineCombined sources1
Modified residuei15N6-acetyllysineBy similarity1
Modified residuei16N6-acetyllysineBy similarity1
Modified residuei28PhosphoserineCombined sources1
Modified residuei34PhosphoserineCombined sources1
Modified residuei41PhosphoserineCombined sources1
Modified residuei42PhosphoserineCombined sources1
Modified residuei67PhosphoserineCombined sources1
Modified residuei69PhosphothreonineCombined sources1
Modified residuei76PhosphothreonineCombined sources1
Modified residuei84PhosphothreonineCombined sources1
Modified residuei92PhosphothreonineCombined sources1
Modified residuei96N6-acetyllysineBy similarity1
Modified residuei99PhosphothreonineCombined sources1
Modified residuei102N6-acetyllysineCombined sources1
Modified residuei106PhosphothreonineCombined sources1
Modified residuei109N6-acetyllysineBy similarity1
Modified residuei113PhosphothreonineCombined sources1
Modified residuei116N6-acetyllysineCombined sources1
Modified residuei121PhosphothreonineCombined sources1
Modified residuei124N6-acetyllysineCombined sources1
Modified residuei145PhosphoserineCombined sources1
Modified residuei153PhosphoserineCombined sources1
Modified residuei184PhosphoserineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Modified residuei214PhosphothreonineCombined sources1
Cross-linki297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei301PhosphothreonineCombined sources1
Modified residuei318N6-acetyllysineCombined sources1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei348N6-acetyllysineBy similarity1
Modified residuei356PhosphoserineCombined sources1
Modified residuei367PhosphothreonineCombined sources1
Modified residuei377N6-acetyllysineCombined sources1
Modified residuei398N6-acetyllysineCombined sources1
Modified residuei403N6-acetyllysineCombined sources1
Modified residuei405PhosphothreonineCombined sources1
Modified residuei427N6-acetyllysineBy similarity1
Modified residuei444N6-acetyllysineBy similarity1
Modified residuei458PhosphoserineCombined sources1
Modified residuei460PhosphoserineCombined sources1
Modified residuei467N6-acetyllysineBy similarity1
Modified residuei477N6-acetyllysineBy similarity1
Modified residuei513N6-acetyllysineCombined sources1
Modified residuei521N6-acetyllysineBy similarity1
Modified residuei563PhosphoserineCombined sources1
Modified residuei572N6-acetyllysineCombined sources1
Modified residuei577N6-acetyllysineCombined sources1
Modified residuei580PhosphoserineCombined sources1
Cross-linki589Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei591PhosphoserineCombined sources1
Modified residuei619PhosphoserineCombined sources1
Modified residuei646N6-acetyllysineCombined sources1
Modified residuei656Asymmetric dimethylarginineBy similarity1
Modified residuei660Asymmetric dimethylarginineBy similarity1
Modified residuei666Asymmetric dimethylarginineBy similarity1
Modified residuei670Asymmetric dimethylarginineBy similarity1
Modified residuei673Asymmetric dimethylarginineBy similarity1
Modified residuei694Omega-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

EPDiP19338.
MaxQBiP19338.
PaxDbiP19338.
PeptideAtlasiP19338.
PRIDEiP19338.
TopDownProteomicsiP19338.

2D gel databases

DOSAC-COBS-2DPAGEP19338.
SWISS-2DPAGEP19338.

PTM databases

iPTMnetiP19338.
PhosphoSitePlusiP19338.
SwissPalmiP19338.

Miscellaneous databases

PMAP-CutDBP19338.

Expressioni

Gene expression databases

BgeeiENSG00000115053.
CleanExiHS_NCL.
ExpressionAtlasiP19338. baseline and differential.
GenevisibleiP19338. HS.

Organism-specific databases

HPAiCAB004210.
HPA023981.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Component of the SWAP complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70 (By similarity). 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 (PubMed:10393184). Interacts with AICDA (By similarity). Interacts with APTX (PubMed:15044383). Interacts with C1QBP (PubMed:21536856). Interacts with ERBB4 (PubMed:20858735). Interacts (via C-terminus) with FMR1 isoform 6 (via N-terminus) (PubMed:24658146). Interacts with GZF1; this interaction is important for nucleolar localization of GZF1 (PubMed:17674968). Interacts with NSUN2 (PubMed:17215513). Interacts with NVL (PubMed:21474449). Interacts (via N-terminus domain) with SETX (PubMed:21700224). Interacts (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with TERT; the interaction is important for nucleolar localization of TERT (PubMed:15371412). Interacts with WDR46 (PubMed:23848194). Interacts with ZFP36 (PubMed:20221403).By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-346967,EBI-346967
P279584EBI-346967,EBI-6904388From a different organism.
Ankrd1Q9CR422EBI-346967,EBI-8308696From a different organism.
ARRB1P494073EBI-346967,EBI-743313
ARRB2P321213EBI-346967,EBI-714559
COL18A1P3906012EBI-346967,EBI-2566375
EBNA-LPQ8AZK72EBI-346967,EBI-1185167From a different organism.
MDM2Q009878EBI-346967,EBI-389668
MYH9P355793EBI-346967,EBI-350338
PA2G4Q9UQ802EBI-346967,EBI-924893
PAX8Q067102EBI-346967,EBI-2683132
RHOAP615863EBI-346967,EBI-446668
TP53P046372EBI-346967,EBI-366083
YWHAZP631042EBI-346967,EBI-347088

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110771. 240 interactors.
DIPiDIP-89N.
IntActiP19338. 89 interactors.
MINTiMINT-4999081.
STRINGi9606.ENSP00000318195.

Structurei

Secondary structure

1710
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi304 – 306Combined sources3
Beta strandi308 – 312Combined sources5
Beta strandi316 – 318Combined sources3
Helixi321 – 333Combined sources13
Beta strandi338 – 343Combined sources6
Beta strandi345 – 356Combined sources12
Helixi357 – 365Combined sources9
Beta strandi377 – 379Combined sources3
Helixi388 – 391Combined sources4
Beta strandi394 – 399Combined sources6
Helixi406 – 413Combined sources8
Beta strandi416 – 424Combined sources9
Beta strandi427 – 435Combined sources9
Helixi439 – 442Combined sources4
Turni443 – 445Combined sources3
Helixi446 – 449Combined sources4
Beta strandi460 – 463Combined sources4
Beta strandi486 – 492Combined sources7
Helixi499 – 505Combined sources7
Beta strandi510 – 513Combined sources4
Beta strandi518 – 520Combined sources3
Beta strandi524 – 529Combined sources6
Helixi533 – 542Combined sources10
Beta strandi544 – 548Combined sources5
Beta strandi551 – 557Combined sources7
Beta strandi565 – 568Combined sources4
Beta strandi572 – 577Combined sources6
Helixi585 – 590Combined sources6
Beta strandi596 – 602Combined sources7
Beta strandi604 – 606Combined sources3
Beta strandi608 – 616Combined sources9
Helixi620 – 630Combined sources11
Beta strandi641 – 644Combined sources4
Beta strandi650 – 652Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FC8NMR-A564-652[»]
2FC9NMR-A478-565[»]
2KRRNMR-A300-466[»]
ProteinModelPortaliP19338.
SMRiP19338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19338.

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
Domaini307 – 383RRM 1PROSITE-ProRule annotationAdd BLAST77
Domaini393 – 466RRM 2PROSITE-ProRule annotationAdd BLAST74
Domaini486 – 560RRM 3PROSITE-ProRule annotationAdd BLAST75
Domaini572 – 647RRM 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 – 171Asp/Glu-rich (acidic)Add BLAST29
Compositional biasi185 – 209Asp/Glu-rich (acidic)Add BLAST25
Compositional biasi234 – 271Asp/Glu-rich (acidic)Add BLAST38
Compositional biasi649 – 698Arg/Gly/Phe-richAdd BLAST50

Sequence similaritiesi

Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IRS7. Eukaryota.
ENOG410XSFV. LUCA.
GeneTreeiENSGT00840000129894.
HOGENOMiHOG000113885.
HOVERGENiHBG002295.
InParanoidiP19338.
KOiK11294.
OMAiSHASCKR.
OrthoDBiEOG091G15MK.
PhylomeDBiP19338.
TreeFamiTF328499.

Family and domain databases

Gene3Di3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00360. RRM. 4 hits.
SM00361. RRM_1. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19338-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLAKAGKN QGDPKKMAPP PKEVEEDSED EEMSEDEEDD SSGEEVVIPQ
60 70 80 90 100
KKGKKAAATS AKKVVVSPTK KVAVATPAKK AAVTPGKKAA ATPAKKTVTP
110 120 130 140 150
AKAVTTPGKK GATPGKALVA TPGKKGAAIP AKGAKNGKNA KKEDSDEEED
160 170 180 190 200
DDSEEDEEDD EDEDEDEDEI EPAAMKAAAA APASEDEDDE DDEDDEDDDD
210 220 230 240 250
DEEDDSEEEA METTPAKGKK AAKVVPVKAK NVAEDEDEEE DDEDEDDDDD
260 270 280 290 300
EDDEDDDDED DEEEEEEEEE EPVKEAPGKR KKEMAKQKAA PEAKKQKVEG
310 320 330 340 350
TEPTTAFNLF VGNLNFNKSA PELKTGISDV FAKNDLAVVD VRIGMTRKFG
360 370 380 390 400
YVDFESAEDL EKALELTGLK VFGNEIKLEK PKGKDSKKER DARTLLAKNL
410 420 430 440 450
PYKVTQDELK EVFEDAAEIR LVSKDGKSKG IAYIEFKTEA DAEKTFEEKQ
460 470 480 490 500
GTEIDGRSIS LYYTGEKGQN QDYRGGKNST WSGESKTLVL SNLSYSATEE
510 520 530 540 550
TLQEVFEKAT FIKVPQNQNG KSKGYAFIEF ASFEDAKEAL NSCNKREIEG
560 570 580 590 600
RAIRLELQGP RGSPNARSQP SKTLFVKGLS EDTTEETLKE SFDGSVRARI
610 620 630 640 650
VTDRETGSSK GFGFVDFNSE EDAKAAKEAM EDGEIDGNKV TLDWAKPKGE
660 670 680 690 700
GGFGGRGGGR GGFGGRGGGR GGRGGFGGRG RGGFGGRGGF RGGRGGGGDH
710
KPQGKKTKFE
Length:710
Mass (Da):76,614
Last modified:January 23, 2007 - v3
Checksum:iC97F6E34E5CA6727
GO

Sequence cautioni

The sequence BAC03738 differs from that shown. Unlikely isoform. Aberrant splice sites.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti549E → G in BAC03738 (PubMed:14702039).Curated1
Sequence conflicti623 – 626Missing in AAA59954 (PubMed:2394707).Curated4
Sequence conflicti625 – 627Missing (PubMed:2737305).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04635368P → L.Corresponds to variant rs11542691dbSNPEnsembl.1
Natural variantiVAR_046354122P → L.Corresponds to variant rs11542687dbSNPEnsembl.1
Natural variantiVAR_046355174A → V.Corresponds to variant rs11542689dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60858 Genomic DNA. Translation: AAA59954.1.
AK091742 mRNA. Translation: BAC03738.1. Sequence problems.
AC017104 Genomic DNA. Translation: AAY24247.1.
CCDSiCCDS33397.1.
PIRiA35804.
S53728.
RefSeqiNP_005372.2. NM_005381.2.
UniGeneiHs.79110.

Genome annotation databases

EnsembliENST00000322723; ENSP00000318195; ENSG00000115053.
GeneIDi4691.
KEGGihsa:4691.
UCSCiuc002vru.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60858 Genomic DNA. Translation: AAA59954.1.
AK091742 mRNA. Translation: BAC03738.1. Sequence problems.
AC017104 Genomic DNA. Translation: AAY24247.1.
CCDSiCCDS33397.1.
PIRiA35804.
S53728.
RefSeqiNP_005372.2. NM_005381.2.
UniGeneiHs.79110.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FC8NMR-A564-652[»]
2FC9NMR-A478-565[»]
2KRRNMR-A300-466[»]
ProteinModelPortaliP19338.
SMRiP19338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110771. 240 interactors.
DIPiDIP-89N.
IntActiP19338. 89 interactors.
MINTiMINT-4999081.
STRINGi9606.ENSP00000318195.

PTM databases

iPTMnetiP19338.
PhosphoSitePlusiP19338.
SwissPalmiP19338.

Polymorphism and mutation databases

BioMutaiNCL.
DMDMi90110781.

2D gel databases

DOSAC-COBS-2DPAGEP19338.
SWISS-2DPAGEP19338.

Proteomic databases

EPDiP19338.
MaxQBiP19338.
PaxDbiP19338.
PeptideAtlasiP19338.
PRIDEiP19338.
TopDownProteomicsiP19338.

Protocols and materials databases

DNASUi4691.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322723; ENSP00000318195; ENSG00000115053.
GeneIDi4691.
KEGGihsa:4691.
UCSCiuc002vru.4. human.

Organism-specific databases

CTDi4691.
DisGeNETi4691.
GeneCardsiNCL.
HGNCiHGNC:7667. NCL.
HPAiCAB004210.
HPA023981.
MIMi164035. gene.
neXtProtiNX_P19338.
OpenTargetsiENSG00000115053.
PharmGKBiPA31469.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IRS7. Eukaryota.
ENOG410XSFV. LUCA.
GeneTreeiENSGT00840000129894.
HOGENOMiHOG000113885.
HOVERGENiHBG002295.
InParanoidiP19338.
KOiK11294.
OMAiSHASCKR.
OrthoDBiEOG091G15MK.
PhylomeDBiP19338.
TreeFamiTF328499.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115053-MONOMER.
SIGNORiP19338.

Miscellaneous databases

ChiTaRSiNCL. human.
EvolutionaryTraceiP19338.
GenomeRNAii4691.
PMAP-CutDBP19338.
PROiP19338.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000115053.
CleanExiHS_NCL.
ExpressionAtlasiP19338. baseline and differential.
GenevisibleiP19338. HS.

Family and domain databases

Gene3Di3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00360. RRM. 4 hits.
SM00361. RRM_1. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNUCL_HUMAN
AccessioniPrimary (citable) accession number: P19338
Secondary accession number(s): Q53SK1
, Q8NB06, Q9UCF0, Q9UDG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 191 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.