UniProt Accession

 NUCL_MOUSE; P09405; Q548M9; Q61991; Q8BQD8; Q99K50 

Genbank Protein ID

 X07699; AF318184; AK050958; AK083307; AK144894; AK161706; AK163275; BC005460; M22089 

Genbank Nucleotide ID

 CAA30538.1; AAK07920.1; BAC34476.1; BAC38858.1; BAE26119.1; BAE36542.1; BAE37270.1; AAH05460.1; AAA39841.1 

Protein Name

 Nucleolin 

Protein Synonyms/Alias

 Protein C23 

Gene Name

 Ncl 

Gene Synonyms/Alias

 Nuc 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
9	VKLAKAGKTHGEAKK	acetylation	[1, 2, 3]
15	GKTHGEAKKMAPPPK	acetylation	[1, 2, 3, 4, 5]
16	KTHGEAKKMAPPPKE	acetylation	[3]
63	ATTTPAKKVVVSQTK	acetylation	[3]
71	VVVSQTKKAAVPTPA	acetylation	[3]
71	VVVSQTKKAAVPTPA	succinylation	[3]
87	KAAVTPGKKAVATPA	acetylation	[1]
95	KAVATPAKKNITPAK	acetylation	[1]
96	AVATPAKKNITPAKV	acetylation	[3]
102	KKNITPAKVIPTPGK	acetylation	[2, 3, 4, 6]
109	KVIPTPGKKGAAQAK	acetylation	[3]
116	KKGAAQAKALVPTPG	acetylation	[2, 3, 4, 6]
116	KKGAAQAKALVPTPG	succinylation	[3]
125	LVPTPGKKGAATPAK	acetylation	[3]
132	KGAATPAKGAKNGKN	acetylation	[3]
230	KGKKTPAKVVPMKAK	acetylation	[3]
320	IGNLNPNKSVNELKF	acetylation	[6]
320	IGNLNPNKSVNELKF	ubiquitination	[7]
326	NKSVNELKFAISELF	acetylation	[6]
326	NKSVNELKFAISELF	ubiquitination	[7]
335	AISELFAKNDLAVVD	ubiquitination	[7]
350	VRTGTNRKFGYVDFE	acetylation	[3]
372	ALELTGLKVFGNEIK	acetylation	[3, 6]
372	ALELTGLKVFGNEIK	succinylation	[3]
379	KVFGNEIKLEKPKGR	acetylation	[2, 3]
400	AARTLLAKNLSFNIT	acetylation	[2]
400	AARTLLAKNLSFNIT	ubiquitination	[7]
429	RLVSQDGKSKGIAYI	acetylation	[3]
431	VSQDGKSKGIAYIEF	acetylation	[3]
431	VSQDGKSKGIAYIEF	succinylation	[3]
446	KSEADAEKNLEEKQG	acetylation	[3]
451	AEKNLEEKQGAEIDG	ubiquitination	[7]
469	SLYYTGEKGQRQERT	acetylation	[3]
469	SLYYTGEKGQRQERT	ubiquitination	[7]
478	QRQERTGKTSTWSGE	acetylation	[3]
509	TLEEVFEKATFIKVP	acetylation	[6]
509	TLEEVFEKATFIKVP	ubiquitination	[7]
522	VPQNPHGKPKGYAFI	acetylation	[3]
546	EALNSCNKMEIEGRT	acetylation	[3, 6]
546	EALNSCNKMEIEGRT	ubiquitination	[7]
569	NSRSQPSKTLFVKGL	acetylation	[2, 3]
574	PSKTLFVKGLSEDTT	acetylation	[2, 3, 6]
574	PSKTLFVKGLSEDTT	ubiquitination	[7]
586	DTTEETLKESFEGSV	ubiquitination	[7]
607	DRETGSSKGFGFVDF	acetylation	[2]
607	DRETGSSKGFGFVDF	ubiquitination	[7]
621	FNSEEDAKAAKEAME	acetylation	[3]
624	EEDAKAAKEAMEDGE	ubiquitination	[7]
643	KVTLDWAKPKGEGGF	acetylation	[2, 3, 6]
643	KVTLDWAKPKGEGGF	succinylation	[3]

Reference

 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] 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]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [7] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

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 (By similarity). 

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 309 385 RRM 1.
 DOMAIN 395 468 RRM 2.
 DOMAIN 487 561 RRM 3.
 DOMAIN 569 644 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 (By similarity).
 MOD_RES 15 15 N6-acetyllysine (By similarity).
 MOD_RES 28 28 Phosphoserine.
 MOD_RES 34 34 Phosphoserine.
 MOD_RES 40 40 Phosphoserine.
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 67 67 Phosphoserine (By similarity).
 MOD_RES 69 69 Phosphothreonine (By similarity).
 MOD_RES 76 76 Phosphothreonine (By similarity).
 MOD_RES 84 84 Phosphothreonine (By similarity).
 MOD_RES 92 92 Phosphothreonine (By similarity).
 MOD_RES 99 99 Phosphothreonine (By similarity).
 MOD_RES 102 102 N6-acetyllysine (By similarity).
 MOD_RES 106 106 Phosphothreonine (By similarity).
 MOD_RES 116 116 N6-acetyllysine (By similarity).
 MOD_RES 121 121 Phosphothreonine (By similarity).
 MOD_RES 124 124 N6-acetyllysine (By similarity).
 MOD_RES 145 145 Phosphoserine.
 MOD_RES 157 157 Phosphoserine.
 MOD_RES 189 189 Phosphoserine (By similarity).
 MOD_RES 212 212 Phosphoserine (By similarity).
 MOD_RES 220 220 Phosphothreonine (By similarity).
 MOD_RES 306 306 Phosphothreonine (By similarity).
 MOD_RES 307 307 Phosphothreonine (By similarity).
 MOD_RES 320 320 N6-acetyllysine (By similarity).
 MOD_RES 379 379 N6-acetyllysine (By similarity).
 MOD_RES 400 400 N6-acetyllysine (By similarity).
 MOD_RES 514 514 N6-acetyllysine (By similarity).
 MOD_RES 569 569 N6-acetyllysine (By similarity).
 MOD_RES 574 574 N6-acetyllysine (By similarity).
 MOD_RES 577 577 Phosphoserine (By similarity).
 MOD_RES 616 616 Phosphoserine (By similarity).
 MOD_RES 643 643 N6-acetyllysine (By similarity).
 MOD_RES 653 653 Asymmetric dimethylarginine (By
 MOD_RES 657 657 Asymmetric dimethylarginine (By
 MOD_RES 663 663 Asymmetric dimethylarginine (By
 MOD_RES 667 667 Asymmetric dimethylarginine (By
 MOD_RES 670 670 Asymmetric dimethylarginine (By  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 707 AA 

Protein Sequence

Gene Ontology

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

Interpro

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

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS