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Protein

Nucleolin

Gene

NCL

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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

Complete GO annotation...

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolin
Gene namesi
Name:NCL
ORF Names:QtrA-10252, QtsA-10605
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

  • Nucleusnucleolus By similarity
  • 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 methionineiRemovedBy similarity
ChainiPRO_00002231812 – 711NucleolinAdd BLAST710

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 residuei41PhosphoserineBy similarity1
Modified residuei42PhosphoserineBy similarity1
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 residuei113PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysineBy similarity1
Modified residuei121PhosphothreonineBy similarity1
Modified residuei124N6-acetyllysineBy similarity1
Modified residuei145PhosphoserineBy similarity1
Modified residuei153PhosphoserineBy similarity1
Modified residuei184PhosphoserineBy similarity1
Modified residuei207PhosphoserineBy similarity1
Modified residuei215PhosphothreonineBy 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 residuei302PhosphothreonineBy 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 residuei404N6-acetyllysineBy similarity1
Modified residuei406PhosphothreonineBy similarity1
Modified residuei428N6-acetyllysineBy similarity1
Modified residuei445N6-acetyllysineBy similarity1
Modified residuei459PhosphoserineBy similarity1
Modified residuei461PhosphoserineBy similarity1
Modified residuei468N6-acetyllysineBy similarity1
Modified residuei478N6-acetyllysineBy similarity1
Modified residuei514N6-acetyllysineBy similarity1
Modified residuei522N6-acetyllysineBy similarity1
Modified residuei564PhosphoserineBy similarity1
Modified residuei573N6-acetyllysineBy similarity1
Modified residuei578N6-acetyllysineBy similarity1
Modified residuei581PhosphoserineBy similarity1
Cross-linki590Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei592PhosphoserineBy similarity1
Modified residuei620PhosphoserineBy similarity1
Modified residuei647N6-acetyllysineBy similarity1
Modified residuei657Asymmetric dimethylarginineBy similarity1
Modified residuei661Asymmetric dimethylarginineBy similarity1
Modified residuei667Asymmetric dimethylarginineBy similarity1
Modified residuei671Asymmetric dimethylarginineBy similarity1
Modified residuei674Asymmetric dimethylarginineBy similarity1
Modified residuei695Omega-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

PRIDEiQ4R4J7.

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

3D structure databases

ProteinModelPortaliQ4R4J7.
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
Domaini308 – 384RRM 1PROSITE-ProRule annotationAdd BLAST77
Domaini394 – 467RRM 2PROSITE-ProRule annotationAdd BLAST74
Domaini487 – 561RRM 3PROSITE-ProRule annotationAdd BLAST75
Domaini573 – 648RRM 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 – 210Asp/Glu-rich (acidic)Add BLAST26
Compositional biasi235 – 272Asp/Glu-rich (acidic)Add BLAST38
Compositional biasi650 – 699Arg/Gly/Phe-richAdd BLAST50

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG002295.
KOiK11294.

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.

Q4R4J7-1 [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
AKAVATPGKK GATPGKALVA TPGKKGAAIP AKGAKNGKNA KKEDSDEEEE
160 170 180 190 200
DDSEEDDEDD EDEDEDEDEI EPAVMKAAAA APASEDEDDE DDEDDEDEDD
210 220 230 240 250
DDEEDDSEEE AMETTPAKGK KAAKVVPVKA KNVAEDEDEE EDDEDEDDDD
260 270 280 290 300
DEDDEDEDDD DEDEEEEEEE EEPVKEAPGK RKKEMAKQKA APEAKKQKVE
310 320 330 340 350
GTEPTTAFNL FVGNLNFNKS APELKTGISD VFAKNDLAVV DVRIGMTRKF
360 370 380 390 400
GYVDFESAED LEKALELTGL KVFGNEIKLE KPKGKDSKKE RDARTLLAKN
410 420 430 440 450
LPYKVTQDEL KEVFEDAAEI RLVSKDGKSK GIAYIEFKTE ADAEKTFEEK
460 470 480 490 500
QGTEIDGRSI SLYYTGEKGQ NQDYRGGKNS TWSGESKTLV LSNLSYSATE
510 520 530 540 550
ETLQEVFEKA TFIKVPQNQN GKSKGYAFIE FASFEDAKEA LNSCNKREIE
560 570 580 590 600
GRAIRLELQG PRGSPNARSQ PSKTLFVKGL SEDTTEETLK ESFDGSVRAR
610 620 630 640 650
IVTDRETGSS KGFGFVDFNS EEDAKAAKEA MEDGEIDGNK VTLDWAKPKG
660 670 680 690 700
EGGFGGRGGG RGGFGGRGGG RGGRGGFGGR GRGGFGGRGG FRGGRGGGGD
710
HKPQGKKTKF E
Length:711
Mass (Da):76,742
Last modified:January 23, 2007 - v3
Checksum:i94EBE7FE82508714
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB169897 mRNA. Translation: BAE01978.1.
AB168220 mRNA. Translation: BAE00345.1.
RefSeqiNP_001270477.1. NM_001283548.1.
UniGeneiMfa.1906.

Genome annotation databases

GeneIDi101865794.
KEGGimcf:101865794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB169897 mRNA. Translation: BAE01978.1.
AB168220 mRNA. Translation: BAE00345.1.
RefSeqiNP_001270477.1. NM_001283548.1.
UniGeneiMfa.1906.

3D structure databases

ProteinModelPortaliQ4R4J7.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ4R4J7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101865794.
KEGGimcf:101865794.

Organism-specific databases

CTDi4691.

Phylogenomic databases

HOVERGENiHBG002295.
KOiK11294.

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_MACFA
AccessioniPrimary (citable) accession number: Q4R4J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.