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P09405 (NUCL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolin
Alternative name(s):
Protein C23
Gene names
Name:Ncl
Synonyms:Nuc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

Interacts with APTX and NSUN2. Component of the SWAP complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs 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. 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 By similarity. Interacts with ERBB4. Interacts with GZF1; this interaction is important for nucleolar localization of GZF1 By similarity. Interacts with NVL and C1QBP. Ref.8 Ref.14

Subcellular location

Nucleus › nucleolus. Cytoplasm By similarity. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs By similarity.

Tissue specificity

Expressed in B-cells that have been induced to switch to various Ig isotypes. Ref.8

Post-translational modification

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.

Sequence similarities

Contains 4 RRM (RNA recognition motif) domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Gnai3Q9DC514EBI-641864,EBI-641852

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 707706Nucleolin
PRO_0000081693

Regions

Repeat58 – 6581
Repeat75 – 8282
Repeat83 – 9083
Repeat91 – 9884
Repeat99 – 10465; truncated
Repeat105 – 11286
Repeat120 – 12787
Repeat128 – 13588
Domain309 – 38577RRM 1
Domain395 – 46874RRM 2
Domain487 – 56175RRM 3
Domain569 – 64476RRM 4
Region58 – 135788 X 8 AA tandem repeats of X-T-P-X-K-K-X-X
Compositional bias143 – 17028Asp/Glu-rich (acidic)
Compositional bias190 – 21526Asp/Glu-rich (acidic)
Compositional bias241 – 27333Asp/Glu-rich (acidic)
Compositional bias646 – 69752Arg/Gly/Phe-rich

Amino acid modifications

Modified residue91N6-acetyllysine By similarity
Modified residue151N6-acetyllysine By similarity
Modified residue281Phosphoserine Ref.11 Ref.13
Modified residue341Phosphoserine Ref.11 Ref.13
Modified residue401Phosphoserine Ref.11 Ref.13
Modified residue411Phosphoserine Ref.11 Ref.13
Modified residue671Phosphoserine By similarity
Modified residue691Phosphothreonine By similarity
Modified residue761Phosphothreonine By similarity
Modified residue841Phosphothreonine By similarity
Modified residue921Phosphothreonine By similarity
Modified residue991Phosphothreonine By similarity
Modified residue1021N6-acetyllysine By similarity
Modified residue1061Phosphothreonine By similarity
Modified residue1161N6-acetyllysine By similarity
Modified residue1211Phosphothreonine By similarity
Modified residue1241N6-acetyllysine By similarity
Modified residue1451Phosphoserine Ref.9 Ref.10
Modified residue1571Phosphoserine Ref.9 Ref.10
Modified residue1891Phosphoserine By similarity
Modified residue2121Phosphoserine By similarity
Modified residue2201Phosphothreonine By similarity
Modified residue3061Phosphothreonine By similarity
Modified residue3071Phosphothreonine By similarity
Modified residue3201N6-acetyllysine By similarity
Modified residue3791N6-acetyllysine By similarity
Modified residue4001N6-acetyllysine By similarity
Modified residue5141N6-acetyllysine By similarity
Modified residue5691N6-acetyllysine By similarity
Modified residue5741N6-acetyllysine By similarity
Modified residue5771Phosphoserine By similarity
Modified residue6161Phosphoserine By similarity
Modified residue6431N6-acetyllysine By similarity
Modified residue6531Asymmetric dimethylarginine By similarity
Modified residue6571Asymmetric dimethylarginine By similarity
Modified residue6631Asymmetric dimethylarginine By similarity
Modified residue6671Asymmetric dimethylarginine By similarity
Modified residue6701Asymmetric dimethylarginine By similarity

Experimental info

Sequence conflict1551D → E in AAH05460. Ref.3
Sequence conflict203 – 2042DD → EE in AAH05460. Ref.3
Sequence conflict2451D → E in AAH05460. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P09405 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EE2CE2ACDBF54CD4

FASTA70776,723
        10         20         30         40         50         60 
MVKLAKAGKT HGEAKKMAPP PKEVEEDSED EEMSEDEDDS SGEEEVVIPQ KKGKKATTTP 

        70         80         90        100        110        120 
AKKVVVSQTK KAAVPTPAKK AAVTPGKKAV ATPAKKNITP AKVIPTPGKK GAAQAKALVP 

       130        140        150        160        170        180 
TPGKKGAATP AKGAKNGKNA KKEDSDEDED EEDEDDSDED EDDEEEDEFE PPIVKGVKPA 

       190        200        210        220        230        240 
KAAPAAPASE DEEDDEDEDD EEDDDEEEED DSEEEVMEIT TAKGKKTPAK VVPMKAKSVA 

       250        260        270        280        290        300 
EEEDDEEEDE DDEDEDDEEE DDEDDDEEEE EEEPVKAAPG KRKKEMTKQK EAPEAKKQKV 

       310        320        330        340        350        360 
EGSEPTTPFN LFIGNLNPNK SVNELKFAIS ELFAKNDLAV VDVRTGTNRK FGYVDFESAE 

       370        380        390        400        410        420 
DLEKALELTG LKVFGNEIKL EKPKGRDSKK VRAARTLLAK NLSFNITEDE LKEVFEDAME 

       430        440        450        460        470        480 
IRLVSQDGKS KGIAYIEFKS EADAEKNLEE KQGAEIDGRS VSLYYTGEKG QRQERTGKTS 

       490        500        510        520        530        540 
TWSGESKTLV LSNLSYSATK ETLEEVFEKA TFIKVPQNPH GKPKGYAFIE FASFEDAKEA 

       550        560        570        580        590        600 
LNSCNKMEIE GRTIRLELQG SNSRSQPSKT LFVKGLSEDT TEETLKESFE GSVRARIVTD 

       610        620        630        640        650        660 
RETGSSKGFG FVDFNSEEDA KAAKEAMEDG EIDGNKVTLD WAKPKGEGGF GGRGGGRGGF 

       670        680        690        700 
GGRGGGRGGR GGFGGRGRGG FGGRGGFRGG RGGGGDFKPQ GKKTKFE

« Hide

References

« Hide 'large scale' references
[1]"Structure of the mouse nucleolin gene. The complete sequence reveals that each RNA binding domain is encoded by two independent exons."
Bourbon H.-M., Lapeyre B., Amalric F.
J. Mol. Biol. 200:627-638(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Egg, Lung and Thymus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
[4]"Sequence and structure of the nucleolin promoter in rodents: characterization of a strikingly conserved CpG island."
Bourbon H.-M., Prudhomme M., Amalric F.
Gene 68:73-84(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
[5]"Granzyme A binding to target cell proteins. Granzyme A binds to and cleaves nucleolin in vitro."
Pasternack M.S., Bleier K.J., McInerney T.N.
J. Biol. Chem. 266:14703-14708(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-24.
[6]"Purification and characterization of nucleolin and its identification as a transcription repressor."
Yang T.-H., Tsai W.-H., Lee Y.-M., Lei H.-Y., Lai M.-Y., Chen D.-S., Yeh N.-H., Lee S.-C.
Mol. Cell. Biol. 14:6068-6074(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19 AND 558-567, FUNCTION.
[7]Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 327-344; 351-364; 401-412; 432-439; 460-469; 488-500; 525-538; 575-586 AND 608-621, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Brain and Hippocampus.
[8]"A B-cell-specific DNA recombination complex."
Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.
J. Biol. Chem. 273:17025-17035(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SWAP COMPLEX, TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Spleen.
[9]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-157, MASS SPECTROMETRY.
Tissue: Embryonic brain.
[10]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-157, MASS SPECTROMETRY.
Tissue: Teratocarcinoma.
[11]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40 AND SER-41, MASS SPECTROMETRY.
Tissue: Liver.
[12]"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCYLATION.
[13]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40 AND SER-41, MASS SPECTROMETRY.
Tissue: Macrophage.
[14]"Structure and function of the N-terminal nucleolin binding domain of nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar localization signal."
Fujiwara Y., Fujiwara K., Goda N., Iwaya N., Tenno T., Shirakawa M., Hiroaki H.
J. Biol. Chem. 286:21732-21741(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NVL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X07699 Genomic DNA. Translation: CAA30538.1.
AF318184 mRNA. Translation: AAK07920.1.
AK050958 mRNA. Translation: BAC34476.1.
AK083307 mRNA. Translation: BAC38858.1.
AK144894 mRNA. Translation: BAE26119.1.
AK161706 mRNA. Translation: BAE36542.1.
AK163275 mRNA. Translation: BAE37270.1.
BC005460 mRNA. Translation: AAH05460.1.
M22089 Genomic DNA. Translation: AAA39841.1.
IPIIPI00317794.
PIRDNMS. A29958.
RefSeqNP_035010.3. NM_010880.3.
UniGeneMm.154378.
Mm.474153.

3D structure databases

ProteinModelPortalP09405.
SMRP09405. Positions 300-648.
ModBaseSearch...

Protein-protein interaction databases

IntActP09405. 3 interactions.

PTM databases

PhosphoSiteP09405.

2D gel databases

REPRODUCTION-2DPAGEP09405.

Proteomic databases

PaxDbP09405.
PRIDEP09405.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027438; ENSMUSP00000027438; ENSMUSG00000026234.
GeneID17975.
KEGGmmu:17975.
UCSCuc007bvl.1. mouse.

Organism-specific databases

CTD4691.
MGIMGI:97286. Ncl.

Phylogenomic databases

eggNOGCOG0724.
GeneTreeENSGT00550000074656.
HOGENOMHOG000113885.
HOVERGENHBG002295.
InParanoidP09405.
KOK11294.
OMAKERDTRT.
OrthoDBEOG45MN5J.

Gene expression databases

BgeeP09405.
CleanExMM_NCL.
GenevestigatorP09405.
GermOnlineENSMUSG00000026234. Mus musculus.

Family and domain databases

Gene3D3.30.70.330. 4 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 4 hits.
[Graphical view]
SMARTSM00360. RRM. 4 hits.
[Graphical view]
PROSITEPS50102. RRM. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCL. mouse.
NextBio292933.
PMAP-CutDBP09405.
SOURCESearch...

Entry information

Entry nameNUCL_MOUSE
AccessionPrimary (citable) accession number: P09405
Secondary accession number(s): Q548M9 expand/collapse secondary AC list , Q61991, Q8BQD8, Q99K50
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents