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Protein

Nucleolin

Gene

NCL

Organism
Mesocricetus auratus (Golden hamster)
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 similarity1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolin
Alternative name(s):
Protein C23
Gene namesi
Name:NCL
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

  • Nucleusnucleolus
  • Cytoplasm By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000816922 – 714NucleolinAdd BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei15N6-acetyllysineBy similarity1
Modified residuei16N6-acetyllysineBy similarity1
Modified residuei28PhosphoserineBy similarity1
Modified residuei34PhosphoserineBy similarity1
Modified residuei40PhosphoserineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei66PhosphoserineBy similarity1
Modified residuei68PhosphothreonineBy similarity1
Modified residuei75PhosphothreonineBy similarity1
Modified residuei83PhosphothreonineBy similarity1
Modified residuei91PhosphothreonineBy similarity1
Modified residuei95N6-acetyllysineBy similarity1
Modified residuei98PhosphothreonineBy similarity1
Modified residuei101N6-acetyllysineBy similarity1
Modified residuei105PhosphothreonineBy similarity1
Modified residuei108N6-acetyllysineBy similarity1
Modified residuei112PhosphothreonineBy similarity1
Modified residuei115N6-acetyllysineBy similarity1
Modified residuei120PhosphothreonineBy similarity1
Modified residuei123N6-acetyllysineBy similarity1
Modified residuei144PhosphoserineBy similarity1
Modified residuei157PhosphoserineBy similarity1
Modified residuei188PhosphoserineBy similarity1
Modified residuei219PhosphothreonineBy similarity1
Cross-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei302PhosphoserineBy similarity1
Modified residuei319N6-acetyllysineBy similarity1
Cross-linki325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei349N6-acetyllysineBy similarity1
Modified residuei357PhosphoserineBy similarity1
Modified residuei368PhosphothreonineBy similarity1
Modified residuei378N6-acetyllysineBy similarity1
Modified residuei399N6-acetyllysineBy similarity1
Modified residuei402PhosphoserineBy similarity1
Modified residuei406PhosphothreonineBy similarity1
Modified residuei428N6-acetyllysineBy similarity1
Modified residuei445N6-acetyllysineBy similarity1
Modified residuei459PhosphoserineBy similarity1
Modified residuei461PhosphoserineBy similarity1
Modified residuei468N6-acetyllysineBy similarity1
Modified residuei477N6-acetyllysineBy similarity1
Modified residuei513N6-acetyllysineBy similarity1
Modified residuei521N6-acetyllysineBy similarity1
Modified residuei563PhosphoserineBy similarity1
Modified residuei572N6-acetyllysineBy similarity1
Modified residuei577N6-acetyllysineBy similarity1
Modified residuei580PhosphoserineBy similarity1
Cross-linki589Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei591PhosphoserineBy similarity1
Modified residuei619PhosphoserineBy similarity1
Modified residuei646N6-acetyllysineBy similarity1
Modified residuei656Asymmetric dimethylarginine1 Publication1
Modified residuei660Asymmetric dimethylarginine1 Publication1
Modified residuei666Asymmetric dimethylarginine1 Publication1
Modified residuei670Asymmetric dimethylarginine1 Publication1
Modified residuei674Asymmetric dimethylarginine1 Publication1
Modified residuei680Asymmetric dimethylarginineCurated1
Modified residuei682Asymmetric dimethylarginineCurated1
Modified residuei688Asymmetric dimethylarginineCurated1
Modified residuei692Asymmetric dimethylarginineCurated1
Modified residuei695Asymmetric dimethylarginine; alternateCurated1
Modified residuei695Omega-N-methylarginine; alternateBy similarity1

Post-translational modificationi

Contains 8 dimethylated arginine residues, of which 5 were localized.
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

PRIDEiP08199.

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.By similarity

Structurei

Secondary structure

1714
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi300 – 303Combined sources4
Beta strandi307 – 313Combined sources7
Helixi321 – 335Combined sources15
Beta strandi341 – 345Combined sources5
Turni346 – 349Combined sources4
Beta strandi350 – 357Combined sources8
Helixi358 – 366Combined sources9
Helixi367 – 369Combined sources3
Beta strandi370 – 372Combined sources3
Beta strandi378 – 380Combined sources3
Turni389 – 391Combined sources3
Helixi392 – 394Combined sources3
Beta strandi395 – 400Combined sources6
Helixi407 – 414Combined sources8
Beta strandi416 – 420Combined sources5
Beta strandi423 – 425Combined sources3
Beta strandi428 – 439Combined sources12
Helixi440 – 449Combined sources10
Beta strandi452 – 455Combined sources4
Beta strandi458 – 464Combined sources7
Beta strandi466 – 468Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FJ7NMR-A299-391[»]
1FJCNMR-A387-469[»]
1FJENMR-B299-469[»]
1RKJNMR-A299-469[»]
ProteinModelPortaliP08199.
SMRiP08199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08199.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati57 – 6418
Repeati74 – 8128
Repeati82 – 8938
Repeati90 – 9748
Repeati98 – 1035; truncated6
Repeati104 – 11168
Repeati119 – 12678
Repeati127 – 13488
Domaini308 – 384RRM 1PROSITE-ProRule annotationAdd BLAST77
Domaini394 – 467RRM 2PROSITE-ProRule annotationAdd BLAST74
Domaini486 – 560RRM 3PROSITE-ProRule annotationAdd BLAST75
Domaini572 – 647RRM 4PROSITE-ProRule annotationAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 1348 X 8 AA tandem repeats of X-T-P-X-K-K-X-XAdd BLAST78

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi142 – 170Asp/Glu-rich (acidic)Add BLAST29
Compositional biasi189 – 214Asp/Glu-rich (acidic)Add BLAST26
Compositional biasi240 – 272Asp/Glu-rich (acidic)Add BLAST33
Compositional biasi649 – 702Arg/Gly/Phe-richAdd BLAST54

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG002295.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P08199-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLAKAGKT HGEAKKMAPP PKEVEEDSED EEMSEEEDDS SGEEVVIPQK
60 70 80 90 100
KGKKATATPA KKVVVSQTKK VAVPTPAKKA AVTPGKKAAA TPAKKAVTPA
110 120 130 140 150
KAVATPGKKG ATQAKALVAT PGKKGAVTPA KGAKNGKNAK KEDSDEDEDD
160 170 180 190 200
DDDEDDSDED EEDEEEDEFE PPVVKGKQGK VAAAAPASED EDEEEDEEEE
210 220 230 240 250
EEDEEEEDDS EEEEAMEITP AKGKKAPAKV VPVKAKNVAE EDDDDEEEDE
260 270 280 290 300
DEEEDEEEEE DEEEEEEEEE EEPVKPAPGK RKKEMTKQKE VPEAKKQKVE
310 320 330 340 350
GSESTTPFNL FIGNLNPNKS VAELKVAISE PFAKNDLAVV DVRTGTNRKF
360 370 380 390 400
GYVDFESAED LEKALELTGL KVFGNEIKLE KPKGRDSKKV RAARTLLAKN
410 420 430 440 450
LSFNITEDEL KEVFEDALEI RLVSQDGKSK GIAYIEFKSE ADAEKNLEEK
460 470 480 490 500
QGAEIDGRSV SLYYTGEKGQ RQERTGKNST WSGESKTLVL SNLSYSATEE
510 520 530 540 550
TLQEVFEKAT FIKVPQNQQG KSKGYAFIEF ASFEDAKEAL NSCNKMEIEG
560 570 580 590 600
RTIRLELQGP RGSPNARSQP SKTLFVKGLS EDTTEETLKE SFEGSVRARI
610 620 630 640 650
VTDRETGSSK GFGFVDFNSE EDAKAAKEAM EDGEIDGNKV TLDWAKPKGE
660 670 680 690 700
GGFGGRGGGR GGFGGRGGGR GGGRGGFGGR GRGGFGGRGG FRGGRGGGGG
710
GGDFKPQGKK TKFE
Length:714
Mass (Da):77,128
Last modified:January 23, 2007 - v2
Checksum:i3363EA8A165E3A73
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti543C → G AA sequence (PubMed:3755137).Curated1
Sequence conflicti546M → R AA sequence (PubMed:3755137).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15825 mRNA. Translation: AAA36966.1.
PIRiA27441.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15825 mRNA. Translation: AAA36966.1.
PIRiA27441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FJ7NMR-A299-391[»]
1FJCNMR-A387-469[»]
1FJENMR-B299-469[»]
1RKJNMR-A299-469[»]
ProteinModelPortaliP08199.
SMRiP08199.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP08199.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG002295.

Miscellaneous databases

EvolutionaryTraceiP08199.

Family and domain databases

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

Entry informationi

Entry nameiNUCL_MESAU
AccessioniPrimary (citable) accession number: P08199
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.