UniProt Accession

 NUCL_HUMAN; P19338; Q53SK1; Q8NB06; Q9UCF0; Q9UDG1 

Genbank Protein ID

 M60858; AK091742; AC017104 

Genbank Nucleotide ID

 AAA59954.1; BAC03738.1; AAY24247.1 

Protein Name

 Nucleolin 

Protein Synonyms/Alias

 Protein C23 

Gene Name

 NCL 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
9	VKLAKAGKNQGDPKK	acetylation	[1, 2, 3]
15	GKNQGDPKKMAPPPK	acetylation	[1, 2, 3]
63	AAATSAKKVVVSPTK	acetylation	[2]
70	KVVVSPTKKVAVATP	acetylation	[2]
79	VAVATPAKKAAVTPG	acetylation	[2]
80	AVATPAKKAAVTPGK	acetylation	[2]
80	AVATPAKKAAVTPGK	ubiquitination	[4]
87	KAAVTPGKKAAATPA	acetylation	[2]
88	AAVTPGKKAAATPAK	acetylation	[2]
102	KKTVTPAKAVTTPGK	acetylation	[1, 2, 5]
102	KKTVTPAKAVTTPGK	ubiquitination	[4, 6]
109	KAVTTPGKKGATPGK	acetylation	[2]
110	AVTTPGKKGATPGKA	acetylation	[2]
116	KKGATPGKALVATPG	acetylation	[1, 2, 5]
116	KKGATPGKALVATPG	ubiquitination	[7]
124	ALVATPGKKGAAIPA	acetylation	[1, 2]
125	LVATPGKKGAAIPAK	acetylation	[2]
125	LVATPGKKGAAIPAK	ubiquitination	[4]
132	KGAAIPAKGAKNGKN	acetylation	[1]
135	AIPAKGAKNGKNAKK	acetylation	[2]
223	AKGKKAAKVVPVKAK	acetylation	[3]
297	APEAKKQKVEGTEPT	acetylation	[8]
318	VGNLNFNKSAPELKT	acetylation	[1]
318	VGNLNFNKSAPELKT	ubiquitination	[7]
324	NKSAPELKTGISDVF	acetylation	[8]
324	NKSAPELKTGISDVF	ubiquitination	[3, 4, 6, 9, 10, 11]
333	GISDVFAKNDLAVVD	acetylation	[1]
333	GISDVFAKNDLAVVD	ubiquitination	[3, 4, 6, 7, 10, 12, 13]
348	VRIGMTRKFGYVDFE	ubiquitination	[3, 4, 6, 9, 10, 11]
370	ALELTGLKVFGNEIK	acetylation	[3]
370	ALELTGLKVFGNEIK	ubiquitination	[3, 4, 6, 7, 9, 10, 11]
377	KVFGNEIKLEKPKGK	acetylation	[1, 3, 8, 14]
377	KVFGNEIKLEKPKGK	ubiquitination	[3]
398	DARTLLAKNLPYKVT	acetylation	[1, 3, 8, 14]
398	DARTLLAKNLPYKVT	ubiquitination	[3, 4, 6, 9, 11]
403	LAKNLPYKVTQDELK	acetylation	[1, 3]
403	LAKNLPYKVTQDELK	ubiquitination	[3, 4, 6, 9, 10, 11]
410	KVTQDELKEVFEDAA	ubiquitination	[4]
467	SLYYTGEKGQNQDYR	ubiquitination	[4, 6, 7]
477	NQDYRGGKNSTWSGE	acetylation	[3]
477	NQDYRGGKNSTWSGE	ubiquitination	[3, 7, 10]
513	FEKATFIKVPQNQNG	acetylation	[1]
513	FEKATFIKVPQNQNG	ubiquitination	[4, 6, 9, 11, 13]
521	VPQNQNGKSKGYAFI	ubiquitination	[4, 9, 11]
523	QNQNGKSKGYAFIEF	ubiquitination	[4]
545	EALNSCNKREIEGRA	ubiquitination	[6]
572	NARSQPSKTLFVKGL	acetylation	[1]
572	NARSQPSKTLFVKGL	ubiquitination	[4, 9, 11]
577	PSKTLFVKGLSEDTT	acetylation	[1, 15]
577	PSKTLFVKGLSEDTT	ubiquitination	[4, 6, 7, 9, 11]
610	DRETGSSKGFGFVDF	ubiquitination	[4, 7, 9, 11]
646	KVTLDWAKPKGEGGF	acetylation	[1]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Characterization of nucleolin K88 acetylation defines a new pool of nucleolin colocalizing with pre-mRNA splicing factors.
 Das S, Cong R, Shandilya J, Senapati P, Moindrot B, Monier K, Delage H, Mongelard F, Kumar S, Kundu TK, Bouvet P.
 FEBS Lett. 2013 Mar 1;587(5):417-24. [PMID: 23353999]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics.
 Yang YY, Grammel M, Hang HC.
 Bioorg Med Chem Lett. 2011 Sep 1;21(17):4976-9. [PMID: 21669532]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [10] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [11] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [12] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [13] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [14] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [15] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 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. 

Sequence Annotation

 REPEAT 58 65 1.
 REPEAT 75 82 2.
 REPEAT 83 90 3.
 REPEAT 91 98 4.
 REPEAT 99 104 5; truncated.
 REPEAT 105 112 6.
 REPEAT 120 127 7.
 REPEAT 128 135 8.
 DOMAIN 307 383 RRM 1.
 DOMAIN 393 466 RRM 2.
 DOMAIN 486 560 RRM 3.
 DOMAIN 572 647 RRM 4.
 REGION 58 135 8 X 8 AA tandem repeats of X-T-P-X-K-K-X-
 MOD_RES 9 9 N6-acetyllysine.
 MOD_RES 15 15 N6-acetyllysine.
 MOD_RES 28 28 Phosphoserine.
 MOD_RES 34 34 Phosphoserine.
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 42 42 Phosphoserine.
 MOD_RES 67 67 Phosphoserine.
 MOD_RES 69 69 Phosphothreonine.
 MOD_RES 76 76 Phosphothreonine.
 MOD_RES 84 84 Phosphothreonine.
 MOD_RES 92 92 Phosphothreonine.
 MOD_RES 99 99 Phosphothreonine.
 MOD_RES 102 102 N6-acetyllysine.
 MOD_RES 106 106 Phosphothreonine.
 MOD_RES 113 113 Phosphothreonine.
 MOD_RES 116 116 N6-acetyllysine.
 MOD_RES 121 121 Phosphothreonine.
 MOD_RES 124 124 N6-acetyllysine.
 MOD_RES 145 145 Phosphoserine.
 MOD_RES 153 153 Phosphoserine.
 MOD_RES 184 184 Phosphoserine.
 MOD_RES 206 206 Phosphoserine.
 MOD_RES 214 214 Phosphothreonine.
 MOD_RES 301 301 Phosphothreonine.
 MOD_RES 304 304 Phosphothreonine.
 MOD_RES 305 305 Phosphothreonine.
 MOD_RES 318 318 N6-acetyllysine.
 MOD_RES 377 377 N6-acetyllysine.
 MOD_RES 398 398 N6-acetyllysine.
 MOD_RES 403 403 N6-acetyllysine.
 MOD_RES 513 513 N6-acetyllysine.
 MOD_RES 563 563 Phosphoserine.
 MOD_RES 572 572 N6-acetyllysine.
 MOD_RES 577 577 N6-acetyllysine.
 MOD_RES 580 580 Phosphoserine.
 MOD_RES 619 619 Phosphoserine.
 MOD_RES 646 646 N6-acetyllysine.
 MOD_RES 656 656 Asymmetric dimethylarginine (By
 MOD_RES 660 660 Asymmetric dimethylarginine (By
 MOD_RES 666 666 Asymmetric dimethylarginine (By
 MOD_RES 670 670 Asymmetric dimethylarginine (By
 MOD_RES 673 673 Asymmetric dimethylarginine (By  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 710 AA 

Protein Sequence

Gene Ontology

 GO:0005938; C:cell cortex; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:Compara.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0042162; F:telomeric DNA binding; IDA:UniProtKB.
 GO:0001525; P:angiogenesis; IDA:UniProtKB. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS