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P19338 (NUCL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

Names and origin

Protein namesRecommended name:
Nucleolin
Alternative name(s):
Protein C23
Gene names
Name:NCL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length710 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. Ref.8

Subunit structure

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 By similarity. Ref.8 Ref.10 Ref.11 Ref.15 Ref.17 Ref.18 Ref.23 Ref.26 Ref.27

Subcellular location

Nucleusnucleolus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.9 Ref.15 Ref.18 Ref.23

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 By similarity.

Sequence similarities

Contains 4 RRM (RNA recognition motif) domains.

Sequence caution

The sequence BAC03738.1 differs from that shown. Reason: Unlikely isoform. Aberrant splice sites.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandDNA-binding
RNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from direct assay PubMed 16403913. Source: UniProtKB

positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter

Inferred from mutant phenotype PubMed 24071584. Source: UniProt

   Cellular_componentcell cortex

Inferred from direct assay PubMed 16403913. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

nucleolus

Inferred from direct assay PubMed 19393617. Source: UniProtKB

nucleoplasm

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 24071584. Source: UniProt

ribonucleoprotein complex

Inferred from direct assay Ref.18. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from direct assay Ref.7. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 21575138. Source: IntAct

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 16403913. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15674325PubMed 16648475PubMed 16777843PubMed 19393617Ref.23. Source: UniProtKB

telomeric DNA binding

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 710709Nucleolin
PRO_0000081691

Regions

Repeat58 – 6581
Repeat75 – 8282
Repeat83 – 9083
Repeat91 – 9884
Repeat99 – 10465; truncated
Repeat105 – 11286
Repeat120 – 12787
Repeat128 – 13588
Domain307 – 38377RRM 1
Domain393 – 46674RRM 2
Domain486 – 56075RRM 3
Domain572 – 64776RRM 4
Region58 – 135788 X 8 AA tandem repeats of X-T-P-X-K-K-X-X
Compositional bias143 – 17129Asp/Glu-rich (acidic)
Compositional bias185 – 20925Asp/Glu-rich (acidic)
Compositional bias234 – 27138Asp/Glu-rich (acidic)
Compositional bias649 – 69850Arg/Gly/Phe-rich

Amino acid modifications

Modified residue91N6-acetyllysine Ref.22
Modified residue151N6-acetyllysine Ref.22
Modified residue161N6-acetyllysine By similarity
Modified residue281Phosphoserine Ref.21 Ref.24
Modified residue341Phosphoserine Ref.21 Ref.24
Modified residue411Phosphoserine Ref.21
Modified residue421Phosphoserine Ref.21
Modified residue671Phosphoserine Ref.19 Ref.24 Ref.28
Modified residue691Phosphothreonine Ref.19 Ref.24 Ref.28
Modified residue761Phosphothreonine Ref.16 Ref.24
Modified residue841Phosphothreonine Ref.24
Modified residue921Phosphothreonine Ref.24
Modified residue961N6-acetyllysine By similarity
Modified residue991Phosphothreonine Ref.24
Modified residue1021N6-acetyllysine Ref.22
Modified residue1061Phosphothreonine Ref.24
Modified residue1091N6-acetyllysine By similarity
Modified residue1131Phosphothreonine Ref.24
Modified residue1161N6-acetyllysine Ref.22
Modified residue1211Phosphothreonine Ref.16 Ref.24
Modified residue1241N6-acetyllysine Ref.22
Modified residue1451Phosphoserine Ref.12 Ref.14 Ref.24
Modified residue1531Phosphoserine Ref.12 Ref.14
Modified residue1841Phosphoserine Ref.14 Ref.19
Modified residue2061Phosphoserine Ref.14 Ref.19
Modified residue2141Phosphothreonine Ref.19
Modified residue3011Phosphothreonine Ref.21
Modified residue3041Phosphothreonine Ref.21
Modified residue3051Phosphothreonine Ref.21
Modified residue3181N6-acetyllysine Ref.22
Modified residue3481N6-acetyllysine By similarity
Modified residue3771N6-acetyllysine Ref.22
Modified residue3981N6-acetyllysine Ref.22
Modified residue4031N6-acetyllysine Ref.22
Modified residue4271N6-acetyllysine By similarity
Modified residue4441N6-acetyllysine By similarity
Modified residue4671N6-acetyllysine By similarity
Modified residue4771N6-acetyllysine By similarity
Modified residue5131N6-acetyllysine Ref.22
Modified residue5211N6-acetyllysine By similarity
Modified residue5631Phosphoserine Ref.12 Ref.24 Ref.28
Modified residue5721N6-acetyllysine Ref.22
Modified residue5771N6-acetyllysine Ref.22
Modified residue5801Phosphoserine Ref.13 Ref.28
Modified residue6191Phosphoserine Ref.24 Ref.28
Modified residue6461N6-acetyllysine Ref.22
Modified residue6561Asymmetric dimethylarginine By similarity
Modified residue6601Asymmetric dimethylarginine By similarity
Modified residue6661Asymmetric dimethylarginine By similarity
Modified residue6701Asymmetric dimethylarginine By similarity
Modified residue6731Asymmetric dimethylarginine By similarity

Natural variations

Natural variant681P → L.
Corresponds to variant rs11542691 [ dbSNP | Ensembl ].
VAR_046353
Natural variant1221P → L.
Corresponds to variant rs11542687 [ dbSNP | Ensembl ].
VAR_046354
Natural variant1741A → V.
Corresponds to variant rs11542689 [ dbSNP | Ensembl ].
VAR_046355

Experimental info

Sequence conflict5491E → G in BAC03738. Ref.3
Sequence conflict623 – 6264Missing in AAA59954. Ref.2
Sequence conflict625 – 6273Missing Ref.1

Secondary structure

.................................................................. 710
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19338 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C97F6E34E5CA6727

FASTA71076,614
        10         20         30         40         50         60 
MVKLAKAGKN QGDPKKMAPP PKEVEEDSED EEMSEDEEDD SSGEEVVIPQ KKGKKAAATS 

        70         80         90        100        110        120 
AKKVVVSPTK KVAVATPAKK AAVTPGKKAA ATPAKKTVTP AKAVTTPGKK GATPGKALVA 

       130        140        150        160        170        180 
TPGKKGAAIP AKGAKNGKNA KKEDSDEEED DDSEEDEEDD EDEDEDEDEI EPAAMKAAAA 

       190        200        210        220        230        240 
APASEDEDDE DDEDDEDDDD DEEDDSEEEA METTPAKGKK AAKVVPVKAK NVAEDEDEEE 

       250        260        270        280        290        300 
DDEDEDDDDD EDDEDDDDED DEEEEEEEEE EPVKEAPGKR KKEMAKQKAA PEAKKQKVEG 

       310        320        330        340        350        360 
TEPTTAFNLF VGNLNFNKSA PELKTGISDV FAKNDLAVVD VRIGMTRKFG YVDFESAEDL 

       370        380        390        400        410        420 
EKALELTGLK VFGNEIKLEK PKGKDSKKER DARTLLAKNL PYKVTQDELK EVFEDAAEIR 

       430        440        450        460        470        480 
LVSKDGKSKG IAYIEFKTEA DAEKTFEEKQ GTEIDGRSIS LYYTGEKGQN QDYRGGKNST 

       490        500        510        520        530        540 
WSGESKTLVL SNLSYSATEE TLQEVFEKAT FIKVPQNQNG KSKGYAFIEF ASFEDAKEAL 

       550        560        570        580        590        600 
NSCNKREIEG RAIRLELQGP RGSPNARSQP SKTLFVKGLS EDTTEETLKE SFDGSVRARI 

       610        620        630        640        650        660 
VTDRETGSSK GFGFVDFNSE EDAKAAKEAM EDGEIDGNKV TLDWAKPKGE GGFGGRGGGR 

       670        680        690        700        710 
GGFGGRGGGR GGRGGFGGRG RGGFGGRGGF RGGRGGGGDH KPQGKKTKFE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the human nucleolin cDNA."
Srivastava M., Fleming P.J., Pollard H.B., Burns A.L.
FEBS Lett. 250:99-105(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[2]"Genomic organization and chromosomal localization of the human nucleolin gene."
Srivastava M., McBride O.W., Fleming P.J., Pollard H.B., Burns A.L.
J. Biol. Chem. 265:14922-14931(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hair follicle dermal papilla.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Purification and partial amino acid sequencing of a fructosyllysine-specific binding protein from cell membranes of the monocyte-like cell line U937."
Krantz S., Salazar R., Brandt R., Kellermann J., Lottspeich F.
Biochim. Biophys. Acta 1266:109-112(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-7; 349-362 AND 610-624.
Tissue: Lymphoma.
[6]"Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins."
Jordan P., Heid H., Kinzel V., Kubler D.
Biochemistry 33:14696-14706(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 231-236; 349-362; 399-403; 458-461 AND 649-653.
[7]"Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n."
Ishikawa F., Matunis M.J., Dreyfuss G., Cech T.R.
Mol. Cell. Biol. 13:4301-4310(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 458-474, NUCLEOTIDE-BINDING.
Tissue: Cervix carcinoma.
[8]"A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription."
Parada C.A., Roeder R.G.
EMBO J. 18:3688-3701(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; RNA POLYMERASE II; SUPT5H AND CDK9.
[9]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Aprataxin, a novel protein that protects against genotoxic stress."
Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H., Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F.
Hum. Mol. Genet. 13:1081-1093(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APTX.
[11]"Nucleolin interacts with telomerase."
Khurts S., Masutomi K., Delgermaa L., Arai K., Oishi N., Mizuno H., Hayashi N., Hahn W.C., Murakami S.
J. Biol. Chem. 279:51508-51515(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERT.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-153 AND SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-153; SER-184 AND SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[15]"Nucleolin modulates the subcellular localization of GDNF-inducible zinc finger protein 1 and its roles in transcription and cell proliferation."
Dambara A., Morinaga T., Fukuda N., Yamakawa Y., Kato T., Enomoto A., Asai N., Murakumo Y., Matsuo S., Takahashi M.
Exp. Cell Res. 313:3755-3766(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GZF1, SUBCELLULAR LOCATION.
[16]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76 AND THR-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Aurora-B regulates RNA methyltransferase NSUN2."
Sakita-Suto S., Kanda A., Suzuki F., Sato S., Takata T., Tatsuka M.
Mol. Biol. Cell 18:1107-1117(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NSUN2.
[18]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-69; SER-184; SER-206 AND THR-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-41; SER-42; THR-301; THR-304 AND THR-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-15; LYS-102; LYS-116; LYS-124; LYS-318; LYS-377; LYS-398; LYS-403; LYS-513; LYS-572; LYS-577 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
Gilmore-Hebert M., Ramabhadran R., Stern D.F.
Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[24]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-67; THR-69; THR-76; THR-84; THR-92; THR-99; THR-106; THR-113; THR-121; SER-145; SER-563 AND SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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.
[27]"Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles."
Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K., Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T., Takahashi N.
Mol. Cell. Proteomics 10:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C1QBP.
[28]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-69; SER-563; SER-580 AND SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Solution structure of the RRM_1 domain of NCL protein."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 478-566.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60858 Genomic DNA. Translation: AAA59954.1.
AK091742 mRNA. Translation: BAC03738.1. Sequence problems.
AC017104 Genomic DNA. Translation: AAY24247.1.
CCDSCCDS33397.1.
PIRA35804.
S53728.
RefSeqNP_005372.2. NM_005381.2.
UniGeneHs.79110.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FC8NMR-A564-652[»]
2FC9NMR-A478-565[»]
2KRRNMR-A300-466[»]
ProteinModelPortalP19338.
SMRP19338. Positions 300-649.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110771. 191 interactions.
DIPDIP-89N.
IntActP19338. 72 interactions.
MINTMINT-4999081.
STRING9606.ENSP00000318195.

PTM databases

PhosphoSiteP19338.

Polymorphism databases

DMDM90110781.

2D gel databases

DOSAC-COBS-2DPAGEP19338.
SWISS-2DPAGEP19338.

Proteomic databases

MaxQBP19338.
PaxDbP19338.
PRIDEP19338.

Protocols and materials databases

DNASU4691.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322723; ENSP00000318195; ENSG00000115053.
GeneID4691.
KEGGhsa:4691.
UCSCuc002vru.3. human.

Organism-specific databases

CTD4691.
GeneCardsGC02M232318.
HGNCHGNC:7667. NCL.
HPACAB004210.
HPA023981.
MIM164035. gene.
neXtProtNX_P19338.
PharmGKBPA31469.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000113885.
HOVERGENHBG002295.
InParanoidP19338.
KOK11294.
OMAEIEPAAM.
OrthoDBEOG73V6KP.
PhylomeDBP19338.
TreeFamTF328499.

Gene expression databases

ArrayExpressP19338.
BgeeP19338.
CleanExHS_NCL.
GenevestigatorP19338.

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. human.
EvolutionaryTraceP19338.
GenomeRNAi4691.
NextBio18090.
PMAP-CutDBP19338.
PROP19338.
SOURCESearch...

Entry information

Entry nameNUCL_HUMAN
AccessionPrimary (citable) accession number: P19338
Secondary accession number(s): Q53SK1 expand/collapse secondary AC list , Q8NB06, Q9UCF0, Q9UDG1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM