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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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 711710NucleolinPRO_0000223181Add
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 residuei41 – 411PhosphoserineBy similarity
Modified residuei42 – 421PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei69 – 691PhosphothreonineBy similarity
Modified residuei76 – 761PhosphothreonineBy similarity
Modified residuei84 – 841PhosphothreonineBy similarity
Modified residuei92 – 921PhosphothreonineBy similarity
Modified residuei96 – 961N6-acetyllysineBy similarity
Modified residuei99 – 991PhosphothreonineBy similarity
Modified residuei102 – 1021N6-acetyllysineBy similarity
Modified residuei106 – 1061PhosphothreonineBy similarity
Modified residuei109 – 1091N6-acetyllysineBy similarity
Modified residuei113 – 1131PhosphothreonineBy similarity
Modified residuei116 – 1161N6-acetyllysineBy similarity
Modified residuei121 – 1211PhosphothreonineBy similarity
Modified residuei124 – 1241N6-acetyllysineBy similarity
Modified residuei145 – 1451PhosphoserineBy similarity
Modified residuei153 – 1531PhosphoserineBy similarity
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei215 – 2151PhosphothreonineBy similarity
Modified residuei302 – 3021PhosphothreonineBy similarity
Modified residuei319 – 3191N6-acetyllysineBy similarity
Modified residuei349 – 3491N6-acetyllysineBy similarity
Modified residuei378 – 3781N6-acetyllysineBy similarity
Modified residuei399 – 3991N6-acetyllysineBy similarity
Modified residuei404 – 4041N6-acetyllysineBy similarity
Modified residuei428 – 4281N6-acetyllysineBy similarity
Modified residuei445 – 4451N6-acetyllysineBy similarity
Modified residuei459 – 4591PhosphoserineBy similarity
Modified residuei468 – 4681N6-acetyllysineBy similarity
Modified residuei478 – 4781N6-acetyllysineBy similarity
Modified residuei514 – 5141N6-acetyllysineBy similarity
Modified residuei522 – 5221N6-acetyllysineBy similarity
Modified residuei564 – 5641PhosphoserineBy similarity
Modified residuei573 – 5731N6-acetyllysineBy similarity
Modified residuei578 – 5781N6-acetyllysineBy similarity
Modified residuei581 – 5811PhosphoserineBy similarity
Modified residuei592 – 5921PhosphoserineBy similarity
Modified residuei620 – 6201PhosphoserineBy similarity
Modified residuei647 – 6471N6-acetyllysineBy similarity
Modified residuei657 – 6571Asymmetric dimethylarginineBy similarity
Modified residuei661 – 6611Asymmetric dimethylarginineBy similarity
Modified residuei667 – 6671Asymmetric dimethylarginineBy similarity
Modified residuei671 – 6711Asymmetric dimethylarginineBy similarity
Modified residuei674 – 6741Asymmetric dimethylarginineBy similarity

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, Methylation, Phosphoprotein

Proteomic databases

PRIDEiQ4R4J7.

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 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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ4R4J7.
SMRiQ4R4J7. Positions 299-469, 485-649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati58 – 6581
Repeati75 – 8282
Repeati83 – 9083
Repeati91 – 9884
Repeati99 – 10465; truncated
Repeati105 – 11286
Repeati120 – 12787
Repeati128 – 13588
Domaini308 – 38477RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini394 – 46774RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini487 – 56175RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini573 – 64876RRM 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 135788 X 8 AA tandem repeats of X-T-P-X-K-K-X-XAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi143 – 17129Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi185 – 21026Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi235 – 27238Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi650 – 69950Arg/Gly/Phe-richAdd
BLAST

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.
SMRiQ4R4J7. Positions 299-469, 485-649.
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...

Publicationsi

  1. "DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
    International consortium for macaque cDNA sequencing and analysis
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Temporal cortex and Testis.

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: May 11, 2016
This is version 69 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.