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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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 714713NucleolinPRO_0000081692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei15 – 151N6-acetyllysineBy similarity
Modified residuei16 – 161N6-acetyllysineBy similarity
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei41 – 411PhosphoserineBy similarity
Modified residuei66 – 661PhosphoserineBy similarity
Modified residuei68 – 681PhosphothreonineBy similarity
Modified residuei75 – 751PhosphothreonineBy similarity
Modified residuei83 – 831PhosphothreonineBy similarity
Modified residuei91 – 911PhosphothreonineBy similarity
Modified residuei95 – 951N6-acetyllysineBy similarity
Modified residuei98 – 981PhosphothreonineBy similarity
Modified residuei101 – 1011N6-acetyllysineBy similarity
Modified residuei105 – 1051PhosphothreonineBy similarity
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei112 – 1121PhosphothreonineBy similarity
Modified residuei115 – 1151N6-acetyllysineBy similarity
Modified residuei120 – 1201PhosphothreonineBy similarity
Modified residuei123 – 1231N6-acetyllysineBy similarity
Modified residuei144 – 1441PhosphoserineBy similarity
Modified residuei157 – 1571PhosphoserineBy similarity
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei219 – 2191PhosphothreonineBy similarity
Cross-linki298 – 298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki298 – 298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei302 – 3021PhosphoserineBy similarity
Modified residuei319 – 3191N6-acetyllysineBy similarity
Cross-linki325 – 325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei349 – 3491N6-acetyllysineBy similarity
Modified residuei357 – 3571PhosphoserineBy similarity
Modified residuei368 – 3681PhosphothreonineBy similarity
Modified residuei378 – 3781N6-acetyllysineBy similarity
Modified residuei399 – 3991N6-acetyllysineBy similarity
Modified residuei402 – 4021PhosphoserineBy similarity
Modified residuei406 – 4061PhosphothreonineBy similarity
Modified residuei428 – 4281N6-acetyllysineBy similarity
Modified residuei445 – 4451N6-acetyllysineBy similarity
Modified residuei459 – 4591PhosphoserineBy similarity
Modified residuei461 – 4611PhosphoserineBy similarity
Modified residuei468 – 4681N6-acetyllysineBy similarity
Modified residuei477 – 4771N6-acetyllysineBy similarity
Modified residuei513 – 5131N6-acetyllysineBy similarity
Modified residuei521 – 5211N6-acetyllysineBy similarity
Modified residuei563 – 5631PhosphoserineBy similarity
Modified residuei572 – 5721N6-acetyllysineBy similarity
Modified residuei577 – 5771N6-acetyllysineBy similarity
Modified residuei580 – 5801PhosphoserineBy similarity
Cross-linki589 – 589Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei591 – 5911PhosphoserineBy similarity
Modified residuei619 – 6191PhosphoserineBy similarity
Modified residuei646 – 6461N6-acetyllysineBy similarity
Modified residuei656 – 6561Asymmetric dimethylarginine1 Publication
Modified residuei660 – 6601Asymmetric dimethylarginine1 Publication
Modified residuei666 – 6661Asymmetric dimethylarginine1 Publication
Modified residuei670 – 6701Asymmetric dimethylarginine1 Publication
Modified residuei674 – 6741Asymmetric dimethylarginine1 Publication
Modified residuei680 – 6801Asymmetric dimethylarginineCurated
Modified residuei682 – 6821Asymmetric dimethylarginineCurated
Modified residuei688 – 6881Asymmetric dimethylarginineCurated
Modified residuei692 – 6921Asymmetric dimethylarginineCurated
Modified residuei695 – 6951Asymmetric dimethylarginineCurated

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. Interacts with APTX and NSUN2. 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 (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with TERT; the interaction is important for nucleolar localization of TERT. Interacts with ERBB4. Interacts with GZF1; this interaction is important for nucleolar localization of GZF1. Interacts with NVL and C1QBP. Interacts with AICDA. Interacts (via N-terminus domain) with SETX. Interacts with WDR46. Interacts (via C-terminus) with FMR1.By similarity

Structurei

Secondary structure

1
714
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi300 – 3034Combined sources
Beta strandi307 – 3137Combined sources
Helixi321 – 33515Combined sources
Beta strandi341 – 3455Combined sources
Turni346 – 3494Combined sources
Beta strandi350 – 3578Combined sources
Helixi358 – 3669Combined sources
Helixi367 – 3693Combined sources
Beta strandi370 – 3723Combined sources
Beta strandi378 – 3803Combined sources
Turni389 – 3913Combined sources
Helixi392 – 3943Combined sources
Beta strandi395 – 4006Combined sources
Helixi407 – 4148Combined sources
Beta strandi416 – 4205Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi428 – 43912Combined sources
Helixi440 – 44910Combined sources
Beta strandi452 – 4554Combined sources
Beta strandi458 – 4647Combined sources
Beta strandi466 – 4683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJ7NMR-A299-391[»]
1FJCNMR-A387-469[»]
1FJENMR-B299-469[»]
1RKJNMR-A299-469[»]
ProteinModelPortaliP08199.
SMRiP08199. Positions 299-469, 484-648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08199.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati57 – 6481
Repeati74 – 8182
Repeati82 – 8983
Repeati90 – 9784
Repeati98 – 10365; truncated
Repeati104 – 11186
Repeati119 – 12687
Repeati127 – 13488
Domaini308 – 38477RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini394 – 46774RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini486 – 56075RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini572 – 64776RRM 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 134788 X 8 AA tandem repeats of X-T-P-X-K-K-X-XAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi142 – 17029Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi189 – 21426Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi240 – 27233Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi649 – 70254Arg/Gly/Phe-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti543 – 5431C → G AA sequence (PubMed:3755137).Curated
Sequence conflicti546 – 5461M → R AA sequence (PubMed:3755137).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJ7NMR-A299-391[»]
1FJCNMR-A387-469[»]
1FJENMR-B299-469[»]
1RKJNMR-A299-469[»]
ProteinModelPortaliP08199.
SMRiP08199. Positions 299-469, 484-648.
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: July 6, 2016
This is version 127 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.