P19338 (NUCL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleolin

Alternative name(s):
Protein C23

Gene names

Name:

NCL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	710 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and 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. Ref.8 Ref.10 Ref.11 Ref.15 Ref.17 Ref.18 Ref.22 Ref.25 Ref.26
Subcellular location	Nucleus › nucleolus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.9 Ref.15 Ref.18 Ref.22
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 component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	DNA-binding RNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from direct assay PubMed 16403913. Source: UniProtKB
Cellular_component	cell cortex Inferred from direct assay PubMed 16403913. Source: UniProtKB nucleolus Inferred from direct assay PubMed 19393617. Source: UniProtKB nucleoplasm Inferred from electronic annotation. Source: Compara ribonucleoprotein complex Inferred from direct assay Ref.18. Source: UniProtKB
Molecular_function	RNA binding Inferred from direct assay Ref.7. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro telomeric DNA binding Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	3	EBI-346967,EBI-743313
ARRB2	P32121	3	EBI-346967,EBI-714559
COL18A1	P39060	12	EBI-346967,EBI-2566375
MDM2	Q00987	2	EBI-346967,EBI-389668
MYH9	P35579	3	EBI-346967,EBI-350338
PA2G4	Q9UQ80	2	EBI-346967,EBI-924893
PAX8	Q06710	2	EBI-346967,EBI-2683132

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 710

709

Nucleolin

PRO_0000081691

Regions

Repeat

58 – 65

8

1

Repeat

75 – 82

8

2

Repeat

83 – 90

8

3

Repeat

91 – 98

8

4

Repeat

99 – 104

6

5; truncated

Repeat

105 – 112

8

6

Repeat

120 – 127

8

7

Repeat

128 – 135

8

8

Domain

307 – 383

77

RRM 1

Domain

393 – 466

74

RRM 2

Domain

486 – 560

75

RRM 3

Domain

572 – 647

76

RRM 4

Region

58 – 135

78

8 X 8 AA tandem repeats of X-T-P-X-K-K-X-X

Compositional bias

143 – 171

29

Asp/Glu-rich (acidic)

Compositional bias

185 – 209

25

Asp/Glu-rich (acidic)

Compositional bias

234 – 271

38

Asp/Glu-rich (acidic)

Compositional bias

649 – 698

50

Arg/Gly/Phe-rich

Amino acid modifications

Modified residue

9

1

N6-acetyllysine Ref.21

Modified residue

15

1

N6-acetyllysine Ref.21

Modified residue

28

1

Phosphoserine Ref.20 Ref.23

Modified residue

34

1

Phosphoserine Ref.20 Ref.23

Modified residue

41

1

Phosphoserine Ref.20

Modified residue

42

1

Phosphoserine Ref.20

Modified residue

67

1

Phosphoserine Ref.19 Ref.23 Ref.27

Modified residue

69

1

Phosphothreonine Ref.19 Ref.23 Ref.27

Modified residue

76

1

Phosphothreonine Ref.16 Ref.23

Modified residue

84

1

Phosphothreonine Ref.23

Modified residue

92

1

Phosphothreonine Ref.23

Modified residue

99

1

Phosphothreonine Ref.23

Modified residue

102

1

N6-acetyllysine Ref.21

Modified residue

106

1

Phosphothreonine Ref.23

Modified residue

113

1

Phosphothreonine Ref.23

Modified residue

116

1

N6-acetyllysine Ref.21

Modified residue

121

1

Phosphothreonine Ref.16 Ref.23

Modified residue

124

1

N6-acetyllysine Ref.21

Modified residue

145

1

Phosphoserine Ref.12 Ref.14 Ref.23

Modified residue

153

1

Phosphoserine Ref.12 Ref.14

Modified residue

184

1

Phosphoserine Ref.14 Ref.19

Modified residue

206

1

Phosphoserine Ref.14 Ref.19

Modified residue

214

1

Phosphothreonine Ref.19

Modified residue

301

1

Phosphothreonine Ref.20

Modified residue

304

1

Phosphothreonine Ref.20

Modified residue

305

1

Phosphothreonine Ref.20

Modified residue

318

1

N6-acetyllysine Ref.21

Modified residue

377

1

N6-acetyllysine Ref.21

Modified residue

398

1

N6-acetyllysine Ref.21

Modified residue

403

1

N6-acetyllysine Ref.21

Modified residue

513

1

N6-acetyllysine Ref.21

Modified residue

563

1

Phosphoserine Ref.12 Ref.23 Ref.27

Modified residue

572

1

N6-acetyllysine Ref.21

Modified residue

577

1

N6-acetyllysine Ref.21

Modified residue

580

1

Phosphoserine Ref.13 Ref.27

Modified residue

619

1

Phosphoserine Ref.23 Ref.27

Modified residue

646

1

N6-acetyllysine Ref.21

Modified residue

656

1

Asymmetric dimethylarginine By similarity

Modified residue

660

1

Asymmetric dimethylarginine By similarity

Modified residue

666

1

Asymmetric dimethylarginine By similarity

Modified residue

670

1

Asymmetric dimethylarginine By similarity

Modified residue

673

1

Asymmetric dimethylarginine By similarity

Natural variations

Natural variant

68

1

P → L.
Corresponds to variant rs11542691 [ dbSNP | Ensembl ].

VAR_046353

Natural variant

122

1

P → L.
Corresponds to variant rs11542687 [ dbSNP | Ensembl ].

VAR_046354

Natural variant

174

1

A → V.
Corresponds to variant rs11542689 [ dbSNP | Ensembl ].

VAR_046355

Experimental info

Sequence conflict

549

1

E → G in BAC03738. Ref.3

Sequence conflict

623 – 626

4

Missing in AAA59954. Ref.2

Sequence conflict

625 – 627

3

Missing Ref.1

Secondary structure

1

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710

Helix Strand Turn

Details...

Beta strand

304 – 306

3

Beta strand

308 – 312

5

Beta strand

316 – 318

3

Helix

321 – 333

13

Beta strand

338 – 343

6

Beta strand

345 – 356

12

Helix

357 – 365

9

Beta strand

377 – 379

3

Helix

388 – 391

4

Beta strand

394 – 399

6

Helix

406 – 413

8

Beta strand

416 – 424

9

Beta strand

427 – 435

9

Helix

439 – 442

4

Turn

443 – 445

3

Helix

446 – 449

4

Beta strand

460 – 463

4

Beta strand

486 – 492

7

Helix

499 – 505

7

Beta strand

510 – 513

4

Beta strand

518 – 520

3

Beta strand

524 – 529

6

Helix

533 – 542

10

Beta strand

544 – 548

5

Beta strand

551 – 557

7

Beta strand

565 – 568

4

Beta strand

572 – 577

6

Helix

585 – 590

6

Beta strand

596 – 602

7

Beta strand

604 – 606

3

Beta strand

608 – 616

9

Helix

620 – 630

11

Beta strand

641 – 644

4

Beta strand

650 – 652

3

Sequences

	Sequence		Length	Mass (Da)
	P19338 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C97F6E34E5CA6727	FASTA	710	76,614
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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, MASS SPECTROMETRY.
[22]	"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.
[23]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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].
[25]	"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.
[26]	"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.
[27]	"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, MASS SPECTROMETRY.
[28]	"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.

IPI

IPI00604620.

PIR

A35804.
S53728.

RefSeq

NP_005372.2. NM_005381.2.

UniGene

Hs.79110.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FC8	NMR	-	A	564-652	[»]
2FC9	NMR	-	A	478-565	[»]
2KRR	NMR	-	A	300-466	[»]

ProteinModelPortal

P19338.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-89N.

IntAct

P19338. 53 interactions.

MINT

MINT-4999081.

STRING

9606.ENSP00000318195.

PTM databases

PhosphoSite

P19338.

Polymorphism databases

DMDM

90110781.

2D gel databases

DOSAC-COBS-2DPAGE

P19338.

SWISS-2DPAGE

P19338.

Proteomic databases

PaxDb

P19338.

PRIDE

P19338.

Protocols and materials databases

DNASU

4691.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322723; ENSP00000318195; ENSG00000115053.

GeneID

4691.

KEGG

hsa:4691.

UCSC

uc002vru.3. human.

Organism-specific databases

CTD

4691.

GeneCards

GC02M232318.

HGNC

HGNC:7667. NCL.

HPA

CAB004210.
HPA023981.

MIM

164035. gene.

neXtProt

NX_P19338.

PharmGKB

PA31469.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000113885.

HOVERGEN

HBG002295.

InParanoid

P19338.

KO

K11294.

OMA

KERDTRT.

OrthoDB

EOG45MN5J.

PhylomeDB

P19338.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Gene expression databases

ArrayExpress

P19338.

Bgee

P19338.

CleanEx

HS_NCL.

Genevestigator

P19338.

GermOnline

ENSG00000115053. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 4 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 4 hits.
[Graphical view]

SMART

SM00360. RRM. 4 hits.
[Graphical view]

PROSITE

PS50102. RRM. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NCL. human.

EvolutionaryTrace

P19338.

GenomeRNAi

4691.

NextBio

18090.

PMAP-CutDB

P19338.

SOURCE

Search...

Entry information

Entry name

NUCL_HUMAN

Accession

Primary (citable) accession number: P19338
Secondary accession number(s): Q53SK1 , Q8NB06, Q9UCF0, Q9UDG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 153 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.