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Reviewed, UniProtKB/Swiss-Prot P19338 (NUCL_HUMAN)

Last modified July 7, 2009. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nucleolin
Alternative name(s):
    Protein C23
Gene names
Name: NCL
OrganismHomo sapiens (Human) [Complete 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.7

Subunit structure

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. Ref.9 Ref.16

Subcellular location

Nucleusnucleolus. Ref.8

Sequence similarities

Contains 4 RRM (RNA recognition motif) domains.

Sequence caution

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
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 residue281Phosphoserine Ref.10 Ref.12
Modified residue341Phosphoserine Ref.12
Modified residue411Phosphoserine Ref.12
Modified residue421Phosphoserine Ref.12
Modified residue671Phosphoserine Ref.10 Ref.12 Ref.11 Ref.15 Ref.17 Ref.18 Ref.19
Modified residue691Phosphothreonine Ref.15 Ref.18 Ref.19
Modified residue761Phosphothreonine Ref.15 Ref.19 Ref.13
Modified residue991Phosphothreonine Ref.11
Modified residue1051Phosphothreonine Ref.11
Modified residue1211Phosphothreonine Ref.12 Ref.15 Ref.19 Ref.13
Modified residue1451Phosphoserine Ref.10 Ref.12 Ref.19 Ref.14
Modified residue1531Phosphoserine Ref.10 Ref.12 Ref.19 Ref.14
Modified residue1841Phosphoserine Ref.17 Ref.19 Ref.14
Modified residue2061Phosphoserine Ref.19 Ref.14
Modified residue2141Phosphothreonine Ref.17 Ref.19
Modified residue3671Phosphothreonine Ref.19
Modified residue5631Phosphoserine Ref.12 Ref.11 Ref.15 Ref.17 Ref.18 Ref.19
Modified residue5801Phosphoserine Ref.13
Modified residue6191Phosphoserine Ref.19 Ref.13

Natural variations

Natural variant681P → L: dbSNP rs11542691.
VAR_046353
Natural variant1221P → L: dbSNP rs11542687.
VAR_046354
Natural variant1741A → V: dbSNP rs11542689.
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
P19338-1 [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: 2737305] [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: 2394707] [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: 14702039] [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: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 7993898] [Abstract]
Cited for: PROTEIN SEQUENCE OF 231-236; 349-362; 399-403; 458-461 AND 649-653.
[6]"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: 8321232] [Abstract]
Cited for: PROTEIN SEQUENCE OF 458-474, NUCLEOTIDE-BINDING.
Tissue: Cervix carcinoma.
[7]"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: 10393184] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; RNA POLYMERASE II; SUPT5H AND CDK9.
[8]"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: 12429849] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"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: 15044383] [Abstract]
Cited for: INTERACTION WITH APTX.
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-67; SER-145 AND SER-153, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-99; THR-105 AND SER-563, MASS SPECTROMETRY.
[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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-41; SER-42; SER-67; THR-121; SER-145; SER-153 AND SER-563, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76; THR-121; SER-580 AND SER-619, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 17487921] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-153; SER-184 AND SER-206, MASS SPECTROMETRY.
[15]"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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-69; THR-76; THR-121 AND SER-563, MASS SPECTROMETRY.
Tissue: Epithelium.
[16]"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: 17215513] [Abstract]
Cited for: INTERACTION WITH NSUN2.
[17]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-184; THR-214 AND SER-563, MASS SPECTROMETRY.
[18]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-69 AND SER-563, MASS SPECTROMETRY.
[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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-69; THR-76; THR-121; SER-145; SER-153; SER-184; SER-206; THR-214; THR-367; SER-563 AND SER-619, MASS SPECTROMETRY.
[20]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]"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

M60858 Genomic DNA. Translation: AAA59954.1.
AK091742 mRNA. Translation: BAC03738.1. Sequence problems.
AC017104 Genomic DNA. Translation: AAY24247.1.
IPIIPI00604620.
PIRA35804.
RefSeqNP_005372.2.
UniGeneHs.79110

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2FC8NMR-A564-652[»]
2FC9NMR-A478-565[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:89N.
IntActP19338. 23 interactions.

PTM databases

PhosphoSiteP19338.

2-D gel databases

SWISS-2DPAGEP19338.
Aarhus/Ghent-2DPAGE1210. NEPHGE.
DOSAC-COBS-2DPAGEP19338.

Proteomic databases

PRIDEP19338.

Genome annotation databases

EnsemblENSG00000115053. Homo sapiens. [Contig view]
GeneID4691.
KEGGhsa:4691.
NMPDRfig|9606.3.peg.19498.
UCSCuc002vru.1. human.

Organism-specific databases

GeneCardsGC02M232027.
HGNCHGNC:7667. NCL.
HPACAB004210.
MIM164035. gene.
PharmGKBPA134887656.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP19338.
HOVERGENP19338.
OMAP19338. GTEPTTA.

Enzyme and pathway databases

Pathway_Interaction_DBaurora_b_pathway. Aurora B signaling.
telomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpressP19338.
BgeeP19338.
CleanExHS_NCL.
GermOnlineENSG00000115053. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR012644. CHP_FYDLN_acid.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 4 hits.
PfamPF09538. FYDLN_acid. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTSM00360. RRM. 4 hits.
[Graphical view]
PROSITEPS50102. RRM. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio18090.
PMAP-CutDBP19338.
SOURCESearch...

Entry information

Entry nameNUCL_HUMAN
AccessionPrimary (citable) accession number: P19338
Secondary accession number(s): Q53SK1, Q8NB06, Q9UCF0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: July 7, 2009
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents