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Protein

Nucleolin

Gene

Ncl

Organism
Mus musculus (Mouse)
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

GO - Biological processi

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
Synonyms:Nuc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97286. Ncl.

Subcellular locationi

  • Nucleusnucleolus
  • Cytoplasm By similarity

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

GO - Cellular componenti

  • cell cortex Source: MGI
  • cell surface Source: Ensembl
  • cytoplasmic ribonucleoprotein granule Source: MGI
  • dense fibrillar component Source: Ensembl
  • extracellular exosome Source: MGI
  • fibrillar center Source: Ensembl
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: MGI
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 707706NucleolinPRO_0000081693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysineCombined sources
Modified residuei15 – 151N6-acetyllysineCombined sources
Modified residuei16 – 161N6-acetyllysineCombined sources
Modified residuei28 – 281PhosphoserineCombined sources
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei41 – 411PhosphoserineCombined sources
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei69 – 691PhosphothreonineBy similarity
Modified residuei76 – 761PhosphothreonineBy similarity
Modified residuei84 – 841PhosphothreonineBy similarity
Modified residuei92 – 921PhosphothreonineBy similarity
Modified residuei96 – 961N6-acetyllysineCombined sources
Modified residuei99 – 991PhosphothreonineBy similarity
Modified residuei102 – 1021N6-acetyllysineCombined sources
Modified residuei106 – 1061PhosphothreonineBy similarity
Modified residuei109 – 1091N6-acetyllysineCombined sources
Modified residuei116 – 1161N6-acetyllysineCombined sources
Modified residuei121 – 1211PhosphothreonineBy similarity
Modified residuei124 – 1241N6-acetyllysineBy similarity
Modified residuei145 – 1451PhosphoserineCombined sources
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei189 – 1891PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei220 – 2201PhosphothreonineBy similarity
Cross-linki299 – 299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki299 – 299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei303 – 3031PhosphoserineCombined sources
Modified residuei320 – 3201N6-acetyllysineBy similarity
Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei350 – 3501N6-acetyllysineCombined sources
Modified residuei358 – 3581PhosphoserineBy similarity
Modified residuei369 – 3691PhosphothreonineBy similarity
Modified residuei379 – 3791N6-acetyllysineBy similarity
Modified residuei400 – 4001N6-acetyllysineBy similarity
Modified residuei403 – 4031PhosphoserineCombined sources
Modified residuei407 – 4071PhosphothreonineBy similarity
Modified residuei429 – 4291N6-acetyllysineCombined sources
Modified residuei446 – 4461N6-acetyllysineCombined sources
Modified residuei460 – 4601PhosphoserineCombined sources
Modified residuei462 – 4621PhosphoserineBy similarity
Modified residuei469 – 4691N6-acetyllysineCombined sources
Modified residuei478 – 4781N6-acetyllysineCombined sources
Modified residuei514 – 5141N6-acetyllysineBy similarity
Modified residuei522 – 5221N6-acetyllysineCombined sources
Modified residuei569 – 5691N6-acetyllysineBy similarity
Modified residuei574 – 5741N6-acetyllysineCombined sources
Modified residuei577 – 5771PhosphoserineBy similarity
Cross-linki586 – 586Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei588 – 5881PhosphoserineBy similarity
Modified residuei616 – 6161PhosphoserineCombined sources
Modified residuei643 – 6431N6-acetyllysineCombined sources
Modified residuei653 – 6531Asymmetric dimethylarginineBy similarity
Modified residuei657 – 6571Asymmetric dimethylarginineBy similarity
Modified residuei663 – 6631Asymmetric dimethylarginineBy similarity
Modified residuei667 – 6671Asymmetric dimethylarginineBy similarity
Modified residuei670 – 6701Asymmetric 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.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP09405.
MaxQBiP09405.
PaxDbiP09405.
PeptideAtlasiP09405.
PRIDEiP09405.
TopDownProteomicsiP09405.

2D gel databases

REPRODUCTION-2DPAGEP09405.

PTM databases

iPTMnetiP09405.
PhosphoSiteiP09405.
SwissPalmiP09405.

Miscellaneous databases

PMAP-CutDBP09405.

Expressioni

Tissue specificityi

Expressed in B-cells that have been induced to switch to various Ig isotypes.1 Publication

Gene expression databases

BgeeiP09405.
CleanExiMM_NCL.
ExpressionAtlasiP09405. baseline and differential.
GenevisibleiP09405. MM.

Interactioni

Subunit structurei

Interacts with APTX and NSUN2. Component of the SWAP complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70 (PubMed:9642267). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. 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 (PubMed:21474449). Interacts with C1QBP. Interacts with AICDA (PubMed:21518874). Interacts (via N-terminus domain) with SETX (By similarity). Interacts (via C-terminus) with FMR1 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ankrd1Q9CR425EBI-641864,EBI-8308696
Gnai3Q9DC514EBI-641864,EBI-641852
Tpt1P630284EBI-641864,EBI-1635228

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201706. 11 interactions.
IntActiP09405. 11 interactions.
MINTiMINT-111156.
STRINGi10090.ENSMUSP00000027438.

Structurei

3D structure databases

ProteinModelPortaliP09405.
SMRiP09405. Positions 300-648.
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
Domaini309 – 38577RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini395 – 46874RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini487 – 56175RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini569 – 64476RRM 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 – 17028Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi190 – 21526Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi241 – 27333Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi646 – 69752Arg/Gly/Phe-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IRS7. Eukaryota.
ENOG410XSFV. LUCA.
GeneTreeiENSGT00840000129894.
HOGENOMiHOG000113885.
HOVERGENiHBG002295.
InParanoidiP09405.
KOiK11294.
OMAiARTHREP.
OrthoDBiEOG73V6KP.
PhylomeDBiP09405.
TreeFamiTF328499.

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.

P09405-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLAKAGKT HGEAKKMAPP PKEVEEDSED EEMSEDEDDS SGEEEVVIPQ
60 70 80 90 100
KKGKKATTTP AKKVVVSQTK KAAVPTPAKK AAVTPGKKAV ATPAKKNITP
110 120 130 140 150
AKVIPTPGKK GAAQAKALVP TPGKKGAATP AKGAKNGKNA KKEDSDEDED
160 170 180 190 200
EEDEDDSDED EDDEEEDEFE PPIVKGVKPA KAAPAAPASE DEEDDEDEDD
210 220 230 240 250
EEDDDEEEED DSEEEVMEIT TAKGKKTPAK VVPMKAKSVA EEEDDEEEDE
260 270 280 290 300
DDEDEDDEEE DDEDDDEEEE EEEPVKAAPG KRKKEMTKQK EAPEAKKQKV
310 320 330 340 350
EGSEPTTPFN LFIGNLNPNK SVNELKFAIS ELFAKNDLAV VDVRTGTNRK
360 370 380 390 400
FGYVDFESAE DLEKALELTG LKVFGNEIKL EKPKGRDSKK VRAARTLLAK
410 420 430 440 450
NLSFNITEDE LKEVFEDAME IRLVSQDGKS KGIAYIEFKS EADAEKNLEE
460 470 480 490 500
KQGAEIDGRS VSLYYTGEKG QRQERTGKTS TWSGESKTLV LSNLSYSATK
510 520 530 540 550
ETLEEVFEKA TFIKVPQNPH GKPKGYAFIE FASFEDAKEA LNSCNKMEIE
560 570 580 590 600
GRTIRLELQG SNSRSQPSKT LFVKGLSEDT TEETLKESFE GSVRARIVTD
610 620 630 640 650
RETGSSKGFG FVDFNSEEDA KAAKEAMEDG EIDGNKVTLD WAKPKGEGGF
660 670 680 690 700
GGRGGGRGGF GGRGGGRGGR GGFGGRGRGG FGGRGGFRGG RGGGGDFKPQ

GKKTKFE
Length:707
Mass (Da):76,723
Last modified:January 23, 2007 - v2
Checksum:iEE2CE2ACDBF54CD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551D → E in AAH05460 (PubMed:15489334).Curated
Sequence conflicti203 – 2042DD → EE in AAH05460 (PubMed:15489334).Curated
Sequence conflicti245 – 2451D → E in AAH05460 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35646.1.
PIRiA29958. DNMS.
RefSeqiNP_035010.3. NM_010880.3.
UniGeneiMm.154378.
Mm.474153.

Genome annotation databases

EnsembliENSMUST00000027438; ENSMUSP00000027438; ENSMUSG00000026234.
GeneIDi17975.
KEGGimmu:17975.
UCSCiuc007bvl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35646.1.
PIRiA29958. DNMS.
RefSeqiNP_035010.3. NM_010880.3.
UniGeneiMm.154378.
Mm.474153.

3D structure databases

ProteinModelPortaliP09405.
SMRiP09405. Positions 300-648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201706. 11 interactions.
IntActiP09405. 11 interactions.
MINTiMINT-111156.
STRINGi10090.ENSMUSP00000027438.

PTM databases

iPTMnetiP09405.
PhosphoSiteiP09405.
SwissPalmiP09405.

2D gel databases

REPRODUCTION-2DPAGEP09405.

Proteomic databases

EPDiP09405.
MaxQBiP09405.
PaxDbiP09405.
PeptideAtlasiP09405.
PRIDEiP09405.
TopDownProteomicsiP09405.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027438; ENSMUSP00000027438; ENSMUSG00000026234.
GeneIDi17975.
KEGGimmu:17975.
UCSCiuc007bvl.1. mouse.

Organism-specific databases

CTDi4691.
MGIiMGI:97286. Ncl.

Phylogenomic databases

eggNOGiENOG410IRS7. Eukaryota.
ENOG410XSFV. LUCA.
GeneTreeiENSGT00840000129894.
HOGENOMiHOG000113885.
HOVERGENiHBG002295.
InParanoidiP09405.
KOiK11294.
OMAiARTHREP.
OrthoDBiEOG73V6KP.
PhylomeDBiP09405.
TreeFamiTF328499.

Miscellaneous databases

ChiTaRSiNcl. mouse.
PMAP-CutDBP09405.
PROiP09405.
SOURCEiSearch...

Gene expression databases

BgeeiP09405.
CleanExiMM_NCL.
ExpressionAtlasiP09405. baseline and differential.
GenevisibleiP09405. MM.

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...

Publicationsi

« Hide 'large scale' publications
  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/cJ.
  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.
    , 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Brain and Hippocampus.
  8. Cited for: IDENTIFICATION IN SWAP COMPLEX, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Spleen.
  9. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40; SER-41 AND SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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.
  12. "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; SER-41 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40; SER-41; SER-145; SER-157; SER-189; SER-212; SER-303; SER-403; SER-460 AND SER-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  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.
  15. Cited for: INTERACTION WITH AICDA.
  16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-15; LYS-16; LYS-96; LYS-102; LYS-109; LYS-116; LYS-350; LYS-429; LYS-446; LYS-469; LYS-478; LYS-522; LYS-574 AND LYS-643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNUCL_MOUSE
AccessioniPrimary (citable) accession number: P09405
Secondary accession number(s): Q548M9
, Q61991, Q8BQD8, Q99K50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 172 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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