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Q76FK4

- NOL8_HUMAN

UniProt

Q76FK4 - NOL8_HUMAN

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Protein
Nucleolar protein 8
Gene
NOL8, C9orf34, NOP132
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays an essential role in the survival of diffuse-type gastric cancer cells. Acts as a nucleolar anchoring protein for DDX47. May be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells.3 Publications

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA replication Source: HGNC
  2. positive regulation of cell growth Source: HGNC
  3. rRNA processing Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolar protein 8
Alternative name(s):
Nucleolar protein Nop132
Gene namesi
Name:NOL8
Synonyms:C9orf34, NOP132
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:23387. NOL8.

Subcellular locationi

Nucleusnucleolus
Note: Localizes in the nucleolar-organizing region during ribosome biogenesis.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleolus Source: UniProtKB
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134918056.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11671167Nucleolar protein 8
PRO_0000239443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei298 – 2981Phosphoserine2 Publications
Modified residuei302 – 3021Phosphothreonine2 Publications
Modified residuei304 – 3041Phosphoserine2 Publications
Modified residuei365 – 3651Phosphoserine4 Publications
Modified residuei376 – 3761Phosphotyrosine1 Publication
Modified residuei378 – 3781Phosphoserine3 Publications
Modified residuei381 – 3811Phosphothreonine3 Publications
Modified residuei801 – 8011Phosphoserine By similarity
Modified residuei837 – 8371Phosphoserine2 Publications
Modified residuei838 – 8381Phosphoserine1 Publication
Modified residuei843 – 8431Phosphoserine2 Publications
Modified residuei845 – 8451Phosphoserine2 Publications
Modified residuei888 – 8881Phosphothreonine4 Publications
Modified residuei890 – 8901Phosphoserine4 Publications
Modified residuei1036 – 10361Phosphoserine1 Publication
Modified residuei1082 – 10821Phosphoserine3 Publications
Modified residuei1083 – 10831Phosphoserine3 Publications
Modified residuei1084 – 10841Phosphoserine3 Publications
Modified residuei1099 – 10991Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated Inferred.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ76FK4.
PaxDbiQ76FK4.
PRIDEiQ76FK4.

PTM databases

PhosphoSiteiQ76FK4.

Expressioni

Tissue specificityi

Expressed in various diffuse-type gastric cancers. Detected at lower levels in skeletal muscle.1 Publication

Inductioni

Up-regulated in diffuse-type gastric cancers.1 Publication

Gene expression databases

ArrayExpressiQ76FK4.
BgeeiQ76FK4.
GenevestigatoriQ76FK4.

Organism-specific databases

HPAiHPA044440.

Interactioni

Subunit structurei

Interacts with the GTP form of RRAGA, RRAGC and RRAGD. Interacts with NIP7. Interacts with DDX18; the interaction is RNA-dependent. Interacts with DDX47; the interaction is RNA-dependent.2 Publications

Protein-protein interaction databases

BioGridi120364. 4 interactions.
IntActiQ76FK4. 3 interactions.
MINTiMINT-4539421.

Structurei

3D structure databases

ProteinModelPortaliQ76FK4.
SMRiQ76FK4. Positions 8-88.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 8982RRM
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili753 – 77927 Reviewed prediction
Add
BLAST
Coiled coili886 – 92439 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1113 – 11164Poly-Phe

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG73280.
HOVERGENiHBG057565.
InParanoidiQ76FK4.
OMAiFQAFKGI.
OrthoDBiEOG70CR60.
PhylomeDBiQ76FK4.
TreeFamiTF323283.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 12 Publications (identifier: Q76FK4-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MKVNRETKRL YVGGLSQDIS EADLQNQFSR FGEVSDVEII TRKDDQGNPQ     50
KVFAYINISV AEADLKKCMS VLNKTKWKGG TLQIQLAKES FLHRLAQERE 100
AAKAKKEEST TGNANLLEKT GGVDFHMKAV PGTEVPGHKN WVVSKFGRVL 150
PVLHLKNQHK RKIIKYDPSK YCHNLKKIGE DFSNTIPISS LTWELEGGND 200
PMSKKRRGEF SDFHGPPKKI IKVQKDESST GSLAMSTRPR RVIERPPLTQ 250
QQAAQKRTCD SITPSKSSPV PVSDTQKLKN LPFKTSGLET AKKRNSISDD 300
DTDSEDELRM MIAKEENLQR TTQPSINESE SDPFEVVRDD FKSGVHKLHS 350
LIGLGIKNRV SCHDSDDDIM RNDREYDSGD TDEIIAMKKN VAKVKNSTEF 400
SQMEKSTKKT SFKNRENCEL SDHCIKLQKR KSNVESALSH GLKSLNRKSP 450
SHSSSSEDAD SASELADSEG GEEYNAMMKN CLRVNLTLAD LEQLAGSDLK 500
VPNEDTKSDG PETTTQCKFD RGSKSPKTPT GLRRGRQCIR PAEIVASLLE 550
GEENTCGKQK PKENNLKPKF QAFKGVGCLY EKESMKKSLK DSVASNNKDQ 600
NSMKHEDPSI ISMEDGSPYV NGSLGEVTPC QHAKKANGPN YIQPQKRQTT 650
FESQDRKAVS PSSSEKRSKN PISRPLEGKK SLSLSAKTHN IGFDKDSCHS 700
TTKTEASQEE RSDSSGLTSL KKSPKVSSKD TREIKTDFSL SISNSSDVSA 750
KDKHAEDNEK RLAALEARQK AKEVQKKLVH NALANLDGHP EDKPTHIIFG 800
SDSECETEET STQEQSHPGE EWVKESMGKT SGKLFDSSDD DESDSEDDSN 850
RFKIKPQFEG RAGQKLMDLQ SHFGTDDRFR MDSRFLETDS EEEQEEVNEK 900
KTAEEEELAE EKKKALNVVQ SVLQINLSNS TNRGSVAAKK FKDIIHYDPT 950
KQDHATYERK RDDKPKESKA KRKKKREEAE KLPEVSKEMY YNIAMDLKEI 1000
FQTTKYTSEK EEGTPWNEDC GKEKPEEIQD PAALTSDAEQ PSGFTFSFFD 1050
SDTKDIKEET YRVETVKPGK IVWQEDPRLQ DSSSEEEDVT EETDHRNSSP 1100
GEASLLEKET TRFFFFSKND ERLQGSDLFW RGVGSNMSRN SWEARTTNLR 1150
MDCRKKHKDA KRKMKPK 1167
Length:1,167
Mass (Da):131,616
Last modified:July 5, 2004 - v1
Checksum:i6E64780D6F0E7415
GO
Isoform 21 Publication (identifier: Q76FK4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:1,099
Mass (Da):123,927
Checksum:iBED9401AC2D5ABE8
GO
Isoform 41 Publication (identifier: Q76FK4-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     787-824: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:1,129
Mass (Da):127,337
Checksum:iCF4642596A282A1A
GO

Sequence cautioni

The sequence BAA91356.1 differs from that shown. Reason: Frameshift at position 1136.
The sequence BAA91356.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAB14229.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAB15003.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti470 – 4701G → E.
Corresponds to variant rs58545014 [ dbSNP | Ensembl ].
VAR_061830
Natural varianti748 – 7481V → L.
Corresponds to variant rs2236344 [ dbSNP | Ensembl ].
VAR_052211
Natural varianti841 – 8411D → E.
Corresponds to variant rs15717 [ dbSNP | Ensembl ].
VAR_052212
Natural varianti988 – 9881E → D.
Corresponds to variant rs34224798 [ dbSNP | Ensembl ].
VAR_052213
Natural varianti1021 – 10211G → S.
Corresponds to variant rs921122 [ dbSNP | Ensembl ].
VAR_052214

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6868Missing in isoform 2. 1 Publication
VSP_052055Add
BLAST
Alternative sequencei787 – 82438Missing in isoform 4. 1 Publication
VSP_052056Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691M → I in BAC99315. 1 Publication
Sequence conflicti69 – 691M → I in BAA91479. 1 Publication
Sequence conflicti454 – 4541S → G in BAB14857. 1 Publication
Sequence conflicti479 – 4791K → E in BAB14857. 1 Publication
Sequence conflicti630 – 6301C → W in BAC99315. 1 Publication
Sequence conflicti630 – 6301C → W in BAA91356. 1 Publication
Sequence conflicti733 – 7331E → G in BAB14857. 1 Publication
Sequence conflicti749 – 7491S → G in BAB14857. 1 Publication
Sequence conflicti945 – 9451I → L in BAC99315. 1 Publication
Sequence conflicti945 – 9451I → L in BAA91356. 1 Publication
Sequence conflicti966 – 9661K → R in BAC99315. 1 Publication
Sequence conflicti966 – 9661K → R in BAA91356. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB105104 mRNA. Translation: BAD12268.1.
AB109030 mRNA. Translation: BAC99315.1.
AK000743 mRNA. Translation: BAA91356.1. Sequence problems.
AK001049 mRNA. Translation: BAA91479.1.
AK022755 mRNA. Translation: BAB14229.1. Different initiation.
AK024245 mRNA. Translation: BAB14857.1.
AK024786 mRNA. Translation: BAB15003.1. Different initiation.
AL136097 Genomic DNA. No translation available.
BC013788 mRNA. Translation: AAH13788.2.
CCDSiCCDS47993.1. [Q76FK4-1]
CCDS59135.1. [Q76FK4-2]
RefSeqiNP_001243323.1. NM_001256394.1. [Q76FK4-2]
NP_060418.4. NM_017948.5. [Q76FK4-1]
XP_006717229.1. XM_006717166.1. [Q76FK4-1]
XP_006717230.1. XM_006717167.1. [Q76FK4-1]
XP_006717231.1. XM_006717168.1. [Q76FK4-4]
XP_006717232.1. XM_006717169.1. [Q76FK4-2]
XP_006717233.1. XM_006717170.1. [Q76FK4-2]
UniGeneiHs.442199.

Genome annotation databases

EnsembliENST00000358855; ENSP00000351723; ENSG00000198000. [Q76FK4-2]
ENST00000442668; ENSP00000401177; ENSG00000198000. [Q76FK4-1]
ENST00000535387; ENSP00000441300; ENSG00000198000. [Q76FK4-4]
ENST00000542053; ENSP00000440709; ENSG00000198000. [Q76FK4-2]
ENST00000545558; ENSP00000441140; ENSG00000198000. [Q76FK4-1]
GeneIDi55035.
KEGGihsa:55035.
UCSCiuc022bjw.1. human. [Q76FK4-1]

Polymorphism databases

DMDMi74758950.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB105104 mRNA. Translation: BAD12268.1 .
AB109030 mRNA. Translation: BAC99315.1 .
AK000743 mRNA. Translation: BAA91356.1 . Sequence problems.
AK001049 mRNA. Translation: BAA91479.1 .
AK022755 mRNA. Translation: BAB14229.1 . Different initiation.
AK024245 mRNA. Translation: BAB14857.1 .
AK024786 mRNA. Translation: BAB15003.1 . Different initiation.
AL136097 Genomic DNA. No translation available.
BC013788 mRNA. Translation: AAH13788.2 .
CCDSi CCDS47993.1. [Q76FK4-1 ]
CCDS59135.1. [Q76FK4-2 ]
RefSeqi NP_001243323.1. NM_001256394.1. [Q76FK4-2 ]
NP_060418.4. NM_017948.5. [Q76FK4-1 ]
XP_006717229.1. XM_006717166.1. [Q76FK4-1 ]
XP_006717230.1. XM_006717167.1. [Q76FK4-1 ]
XP_006717231.1. XM_006717168.1. [Q76FK4-4 ]
XP_006717232.1. XM_006717169.1. [Q76FK4-2 ]
XP_006717233.1. XM_006717170.1. [Q76FK4-2 ]
UniGenei Hs.442199.

3D structure databases

ProteinModelPortali Q76FK4.
SMRi Q76FK4. Positions 8-88.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120364. 4 interactions.
IntActi Q76FK4. 3 interactions.
MINTi MINT-4539421.

PTM databases

PhosphoSitei Q76FK4.

Polymorphism databases

DMDMi 74758950.

Proteomic databases

MaxQBi Q76FK4.
PaxDbi Q76FK4.
PRIDEi Q76FK4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358855 ; ENSP00000351723 ; ENSG00000198000 . [Q76FK4-2 ]
ENST00000442668 ; ENSP00000401177 ; ENSG00000198000 . [Q76FK4-1 ]
ENST00000535387 ; ENSP00000441300 ; ENSG00000198000 . [Q76FK4-4 ]
ENST00000542053 ; ENSP00000440709 ; ENSG00000198000 . [Q76FK4-2 ]
ENST00000545558 ; ENSP00000441140 ; ENSG00000198000 . [Q76FK4-1 ]
GeneIDi 55035.
KEGGi hsa:55035.
UCSCi uc022bjw.1. human. [Q76FK4-1 ]

Organism-specific databases

CTDi 55035.
GeneCardsi GC09M095059.
HGNCi HGNC:23387. NOL8.
HPAi HPA044440.
MIMi 611534. gene.
neXtProti NX_Q76FK4.
PharmGKBi PA134918056.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73280.
HOVERGENi HBG057565.
InParanoidi Q76FK4.
OMAi FQAFKGI.
OrthoDBi EOG70CR60.
PhylomeDBi Q76FK4.
TreeFami TF323283.

Miscellaneous databases

GeneWikii NOL8.
GenomeRNAii 55035.
NextBioi 58463.
PROi Q76FK4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q76FK4.
Bgeei Q76FK4.
Genevestigatori Q76FK4.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of NOL8, a nucleolar protein containing an RNA recognition motif (RRM), which was overexpressed in diffuse-type gastric cancer."
    Jinawath N., Furukawa Y., Nakamura Y.
    Cancer Sci. 95:430-435(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, PHOSPHORYLATION.
  2. "A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D."
    Sekiguchi T., Todaka Y., Wang Y., Hirose E., Nakashima N., Nishimoto T.
    J. Biol. Chem. 279:8343-8350(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 946-964, FUNCTION, INTERACTION WITH NIP7; RRAGA; RRAGC AND RRAGD.
  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] (ISOFORM 1).
    Tissue: Embryonic head, Hepatoma, Smooth muscle and Teratocarcinoma.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 473-1167 (ISOFORMS 1/2).
    Tissue: Colon.
  6. "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-365; THR-888 AND SER-890, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47."
    Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.
    Nucleic Acids Res. 34:4593-4608(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDX18 AND DDX47, SUBCELLULAR LOCATION.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-378; THR-381; SER-837; SER-838; SER-843; SER-845; SER-1036; SER-1082; SER-1083; SER-1084 AND SER-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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-298; THR-302; SER-304; SER-378; THR-381; SER-837; SER-843; SER-845; THR-888; SER-890; SER-1082; SER-1083 AND SER-1084, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-365; THR-888 AND SER-890, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-298; THR-302; SER-304; SER-365; TYR-376; SER-378; THR-381; THR-888; SER-890; SER-1082; SER-1083; SER-1084 AND SER-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNOL8_HUMAN
AccessioniPrimary (citable) accession number: Q76FK4
Secondary accession number(s): Q5TCC7
, Q5TCC8, Q5TCD3, Q5TCD5, Q5TCD6, Q5TCD7, Q76D35, Q7L3E2, Q9H586, Q9H795, Q9H7W7, Q9H9J6, Q9NWA4, Q9NWM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 96 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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