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P19338

- NUCL_HUMAN

UniProt

P19338 - NUCL_HUMAN

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Protein

Nucleolin

Gene

NCL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein C-terminus binding Source: UniProtKB
  5. RNA binding Source: UniProtKB
  6. telomeric DNA binding Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProt
Complete GO annotation...

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolin
Alternative name(s):
Protein C23
Gene namesi
Name:NCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:7667. NCL.

Subcellular locationi

Nucleusnucleolus. Cytoplasm
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB
  5. nucleolus Source: UniProtKB
  6. nucleoplasm Source: Ensembl
  7. nucleus Source: ParkinsonsUK-UCL
  8. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 710709NucleolinPRO_0000081691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine1 Publication
Modified residuei15 – 151N6-acetyllysine1 Publication
Modified residuei16 – 161N6-acetyllysineBy similarity
Modified residuei28 – 281Phosphoserine2 Publications
Modified residuei34 – 341Phosphoserine2 Publications
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei42 – 421Phosphoserine1 Publication
Modified residuei67 – 671Phosphoserine3 Publications
Modified residuei69 – 691Phosphothreonine3 Publications
Modified residuei76 – 761Phosphothreonine2 Publications
Modified residuei84 – 841Phosphothreonine1 Publication
Modified residuei92 – 921Phosphothreonine1 Publication
Modified residuei96 – 961N6-acetyllysineBy similarity
Modified residuei99 – 991Phosphothreonine1 Publication
Modified residuei102 – 1021N6-acetyllysine1 Publication
Modified residuei106 – 1061Phosphothreonine1 Publication
Modified residuei109 – 1091N6-acetyllysineBy similarity
Modified residuei113 – 1131Phosphothreonine1 Publication
Modified residuei116 – 1161N6-acetyllysine1 Publication
Modified residuei121 – 1211Phosphothreonine2 Publications
Modified residuei124 – 1241N6-acetyllysine1 Publication
Modified residuei145 – 1451Phosphoserine3 Publications
Modified residuei153 – 1531Phosphoserine2 Publications
Modified residuei184 – 1841Phosphoserine2 Publications
Modified residuei206 – 2061Phosphoserine2 Publications
Modified residuei214 – 2141Phosphothreonine1 Publication
Modified residuei301 – 3011Phosphothreonine1 Publication
Modified residuei304 – 3041Phosphothreonine1 Publication
Modified residuei305 – 3051Phosphothreonine1 Publication
Modified residuei318 – 3181N6-acetyllysine1 Publication
Modified residuei348 – 3481N6-acetyllysineBy similarity
Modified residuei377 – 3771N6-acetyllysine1 Publication
Modified residuei398 – 3981N6-acetyllysine1 Publication
Modified residuei403 – 4031N6-acetyllysine1 Publication
Modified residuei427 – 4271N6-acetyllysineBy similarity
Modified residuei444 – 4441N6-acetyllysineBy similarity
Modified residuei467 – 4671N6-acetyllysineBy similarity
Modified residuei477 – 4771N6-acetyllysineBy similarity
Modified residuei513 – 5131N6-acetyllysine1 Publication
Modified residuei521 – 5211N6-acetyllysineBy similarity
Modified residuei563 – 5631Phosphoserine3 Publications
Modified residuei572 – 5721N6-acetyllysine1 Publication
Modified residuei577 – 5771N6-acetyllysine1 Publication
Modified residuei580 – 5801Phosphoserine2 Publications
Modified residuei619 – 6191Phosphoserine2 Publications
Modified residuei646 – 6461N6-acetyllysine1 Publication
Modified residuei656 – 6561Asymmetric dimethylarginineBy similarity
Modified residuei660 – 6601Asymmetric dimethylarginineBy similarity
Modified residuei666 – 6661Asymmetric dimethylarginineBy similarity
Modified residuei670 – 6701Asymmetric dimethylarginineBy similarity
Modified residuei673 – 6731Asymmetric dimethylarginineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP19338.
PaxDbiP19338.
PRIDEiP19338.

2D gel databases

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

PTM databases

PhosphoSiteiP19338.

Miscellaneous databases

PMAP-CutDBP19338.

Expressioni

Gene expression databases

BgeeiP19338.
CleanExiHS_NCL.
ExpressionAtlasiP19338. baseline and differential.
GenevestigatoriP19338.

Organism-specific databases

HPAiCAB004210.
HPA023981.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-346967,EBI-346967
P279584EBI-346967,EBI-6904388From a different organism.
ARRB1P494073EBI-346967,EBI-743313
ARRB2P321213EBI-346967,EBI-714559
COL18A1P3906012EBI-346967,EBI-2566375
EBNA-LPQ8AZK72EBI-346967,EBI-1185167From a different organism.
MDM2Q009878EBI-346967,EBI-389668
MYH9P355793EBI-346967,EBI-350338
PA2G4Q9UQ802EBI-346967,EBI-924893
PAX8Q067102EBI-346967,EBI-2683132
RHOAP615863EBI-346967,EBI-446668
TP53P046372EBI-346967,EBI-366083
YWHAZP631042EBI-346967,EBI-347088

Protein-protein interaction databases

BioGridi110771. 186 interactions.
DIPiDIP-89N.
IntActiP19338. 73 interactions.
MINTiMINT-4999081.
STRINGi9606.ENSP00000318195.

Structurei

Secondary structure

1
710
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi304 – 3063Combined sources
Beta strandi308 – 3125Combined sources
Beta strandi316 – 3183Combined sources
Helixi321 – 33313Combined sources
Beta strandi338 – 3436Combined sources
Beta strandi345 – 35612Combined sources
Helixi357 – 3659Combined sources
Beta strandi377 – 3793Combined sources
Helixi388 – 3914Combined sources
Beta strandi394 – 3996Combined sources
Helixi406 – 4138Combined sources
Beta strandi416 – 4249Combined sources
Beta strandi427 – 4359Combined sources
Helixi439 – 4424Combined sources
Turni443 – 4453Combined sources
Helixi446 – 4494Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi486 – 4927Combined sources
Helixi499 – 5057Combined sources
Beta strandi510 – 5134Combined sources
Beta strandi518 – 5203Combined sources
Beta strandi524 – 5296Combined sources
Helixi533 – 54210Combined sources
Beta strandi544 – 5485Combined sources
Beta strandi551 – 5577Combined sources
Beta strandi565 – 5684Combined sources
Beta strandi572 – 5776Combined sources
Helixi585 – 5906Combined sources
Beta strandi596 – 6027Combined sources
Beta strandi604 – 6063Combined sources
Beta strandi608 – 6169Combined sources
Helixi620 – 63011Combined sources
Beta strandi641 – 6444Combined sources
Beta strandi650 – 6523Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FC8NMR-A564-652[»]
2FC9NMR-A478-565[»]
2KRRNMR-A300-466[»]
ProteinModelPortaliP19338.
SMRiP19338. Positions 300-653.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19338.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati58 – 6581
Repeati75 – 8282
Repeati83 – 9083
Repeati91 – 9884
Repeati99 – 10465; truncated
Repeati105 – 11286
Repeati120 – 12787
Repeati128 – 13588
Domaini307 – 38377RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini393 – 46674RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini486 – 56075RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini572 – 64776RRM 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 135788 X 8 AA tandem repeats of X-T-P-X-K-K-X-XAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi143 – 17129Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi185 – 20925Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi234 – 27138Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi649 – 69850Arg/Gly/Phe-richAdd
BLAST

Sequence similaritiesi

Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00730000110998.
HOGENOMiHOG000113885.
HOVERGENiHBG002295.
InParanoidiP19338.
KOiK11294.
OMAiEIEPAAM.
OrthoDBiEOG73V6KP.
PhylomeDBiP19338.
TreeFamiTF328499.

Family and domain databases

Gene3Di3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00360. RRM. 4 hits.
[Graphical view]
PROSITEiPS50102. RRM. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19338-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKLAKAGKN QGDPKKMAPP PKEVEEDSED EEMSEDEEDD SSGEEVVIPQ
60 70 80 90 100
KKGKKAAATS AKKVVVSPTK KVAVATPAKK AAVTPGKKAA ATPAKKTVTP
110 120 130 140 150
AKAVTTPGKK GATPGKALVA TPGKKGAAIP AKGAKNGKNA KKEDSDEEED
160 170 180 190 200
DDSEEDEEDD EDEDEDEDEI EPAAMKAAAA APASEDEDDE DDEDDEDDDD
210 220 230 240 250
DEEDDSEEEA METTPAKGKK AAKVVPVKAK NVAEDEDEEE DDEDEDDDDD
260 270 280 290 300
EDDEDDDDED DEEEEEEEEE EPVKEAPGKR KKEMAKQKAA PEAKKQKVEG
310 320 330 340 350
TEPTTAFNLF VGNLNFNKSA PELKTGISDV FAKNDLAVVD VRIGMTRKFG
360 370 380 390 400
YVDFESAEDL EKALELTGLK VFGNEIKLEK PKGKDSKKER DARTLLAKNL
410 420 430 440 450
PYKVTQDELK EVFEDAAEIR LVSKDGKSKG IAYIEFKTEA DAEKTFEEKQ
460 470 480 490 500
GTEIDGRSIS LYYTGEKGQN QDYRGGKNST WSGESKTLVL SNLSYSATEE
510 520 530 540 550
TLQEVFEKAT FIKVPQNQNG KSKGYAFIEF ASFEDAKEAL NSCNKREIEG
560 570 580 590 600
RAIRLELQGP RGSPNARSQP SKTLFVKGLS EDTTEETLKE SFDGSVRARI
610 620 630 640 650
VTDRETGSSK GFGFVDFNSE EDAKAAKEAM EDGEIDGNKV TLDWAKPKGE
660 670 680 690 700
GGFGGRGGGR GGFGGRGGGR GGRGGFGGRG RGGFGGRGGF RGGRGGGGDH
710
KPQGKKTKFE
Length:710
Mass (Da):76,614
Last modified:January 23, 2007 - v3
Checksum:iC97F6E34E5CA6727
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti549 – 5491E → G in BAC03738. (PubMed:14702039)Curated
Sequence conflicti623 – 6264Missing in AAA59954. (PubMed:2394707)Curated
Sequence conflicti625 – 6273Missing(PubMed:2737305)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681P → L.
Corresponds to variant rs11542691 [ dbSNP | Ensembl ].
VAR_046353
Natural varianti122 – 1221P → L.
Corresponds to variant rs11542687 [ dbSNP | Ensembl ].
VAR_046354
Natural varianti174 – 1741A → V.
Corresponds to variant rs11542689 [ dbSNP | Ensembl ].
VAR_046355

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60858 Genomic DNA. Translation: AAA59954.1.
AK091742 mRNA. Translation: BAC03738.1. Sequence problems.
AC017104 Genomic DNA. Translation: AAY24247.1.
CCDSiCCDS33397.1.
PIRiA35804.
S53728.
RefSeqiNP_005372.2. NM_005381.2.
UniGeneiHs.79110.

Genome annotation databases

EnsembliENST00000322723; ENSP00000318195; ENSG00000115053.
GeneIDi4691.
KEGGihsa:4691.
UCSCiuc002vru.3. human.

Polymorphism databases

DMDMi90110781.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60858 Genomic DNA. Translation: AAA59954.1 .
AK091742 mRNA. Translation: BAC03738.1 . Sequence problems.
AC017104 Genomic DNA. Translation: AAY24247.1 .
CCDSi CCDS33397.1.
PIRi A35804.
S53728.
RefSeqi NP_005372.2. NM_005381.2.
UniGenei Hs.79110.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FC8 NMR - A 564-652 [» ]
2FC9 NMR - A 478-565 [» ]
2KRR NMR - A 300-466 [» ]
ProteinModelPortali P19338.
SMRi P19338. Positions 300-653.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110771. 186 interactions.
DIPi DIP-89N.
IntActi P19338. 73 interactions.
MINTi MINT-4999081.
STRINGi 9606.ENSP00000318195.

PTM databases

PhosphoSitei P19338.

Polymorphism databases

DMDMi 90110781.

2D gel databases

DOSAC-COBS-2DPAGE P19338.
SWISS-2DPAGE P19338.

Proteomic databases

MaxQBi P19338.
PaxDbi P19338.
PRIDEi P19338.

Protocols and materials databases

DNASUi 4691.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322723 ; ENSP00000318195 ; ENSG00000115053 .
GeneIDi 4691.
KEGGi hsa:4691.
UCSCi uc002vru.3. human.

Organism-specific databases

CTDi 4691.
GeneCardsi GC02M232318.
HGNCi HGNC:7667. NCL.
HPAi CAB004210.
HPA023981.
MIMi 164035. gene.
neXtProti NX_P19338.
PharmGKBi PA31469.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00730000110998.
HOGENOMi HOG000113885.
HOVERGENi HBG002295.
InParanoidi P19338.
KOi K11294.
OMAi EIEPAAM.
OrthoDBi EOG73V6KP.
PhylomeDBi P19338.
TreeFami TF328499.

Miscellaneous databases

ChiTaRSi NCL. human.
EvolutionaryTracei P19338.
GenomeRNAii 4691.
NextBioi 18090.
PMAP-CutDB P19338.
PROi P19338.
SOURCEi Search...

Gene expression databases

Bgeei P19338.
CleanExi HS_NCL.
ExpressionAtlasi P19338. baseline and differential.
Genevestigatori P19338.

Family and domain databases

Gene3Di 3.30.70.330. 4 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 4 hits.
[Graphical view ]
SMARTi SM00360. RRM. 4 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: INTERACTION WITH APTX.
  11. 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. Cited for: INTERACTION WITH NSUN2.
  18. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  19. 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. 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.

Entry informationi

Entry nameiNUCL_HUMAN
AccessioniPrimary (citable) accession number: P19338
Secondary accession number(s): Q53SK1
, Q8NB06, Q9UCF0, Q9UDG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3