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Q76FK4 (NOL8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar protein 8
Alternative name(s):
Nucleolar protein Nop132
Gene names
Name:NOL8
Synonyms:C9orf34, NOP132
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1167 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.7

Subunit structure

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. Ref.2 Ref.7

Subcellular location

Nucleusnucleolus. Note: Localizes in the nucleolar-organizing region during ribosome biogenesis. Ref.1 Ref.7

Tissue specificity

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

Induction

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

Post-translational modification

Phosphorylated Probable. Ref.1

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence BAA91356.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA91356.1 differs from that shown. Reason: Frameshift at position 1136.

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 (identifier: Q76FK4-1)

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.
Isoform 2 Ref.4 (identifier: Q76FK4-2)

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.
Isoform 4 Ref.4 (identifier: Q76FK4-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11671167Nucleolar protein 8
PRO_0000239443

Regions

Domain8 – 8982RRM
Coiled coil753 – 77927 Potential
Coiled coil886 – 92439 Potential
Compositional bias1113 – 11164Poly-Phe

Amino acid modifications

Modified residue2981Phosphoserine Ref.11 Ref.13
Modified residue3021Phosphothreonine Ref.11 Ref.13
Modified residue3041Phosphoserine Ref.11 Ref.13
Modified residue3651Phosphoserine Ref.6 Ref.9 Ref.12 Ref.13
Modified residue3761Phosphotyrosine Ref.13
Modified residue3781Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue3811Phosphothreonine Ref.9 Ref.11 Ref.13
Modified residue8011Phosphoserine By similarity
Modified residue8371Phosphoserine Ref.9 Ref.11
Modified residue8381Phosphoserine Ref.9
Modified residue8431Phosphoserine Ref.9 Ref.11
Modified residue8451Phosphoserine Ref.9 Ref.11
Modified residue8881Phosphothreonine Ref.6 Ref.11 Ref.12 Ref.13
Modified residue8901Phosphoserine Ref.6 Ref.11 Ref.12 Ref.13
Modified residue10361Phosphoserine Ref.9
Modified residue10821Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue10831Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue10841Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue10991Phosphoserine Ref.9 Ref.13

Natural variations

Alternative sequence1 – 6868Missing in isoform 2. Ref.4
VSP_052055
Alternative sequence787 – 82438Missing in isoform 4. Ref.4
VSP_052056
Natural variant4701G → E.
Corresponds to variant rs58545014 [ dbSNP | Ensembl ].
VAR_061830
Natural variant7481V → L.
Corresponds to variant rs2236344 [ dbSNP | Ensembl ].
VAR_052211
Natural variant8411D → E.
Corresponds to variant rs15717 [ dbSNP | Ensembl ].
VAR_052212
Natural variant9881E → D.
Corresponds to variant rs34224798 [ dbSNP | Ensembl ].
VAR_052213
Natural variant10211G → S.
Corresponds to variant rs921122 [ dbSNP | Ensembl ].
VAR_052214

Experimental info

Sequence conflict691M → I in BAC99315. Ref.2
Sequence conflict691M → I in BAA91479. Ref.3
Sequence conflict4541S → G in BAB14857. Ref.3
Sequence conflict4791K → E in BAB14857. Ref.3
Sequence conflict6301C → W in BAC99315. Ref.2
Sequence conflict6301C → W in BAA91356. Ref.3
Sequence conflict7331E → G in BAB14857. Ref.3
Sequence conflict7491S → G in BAB14857. Ref.3
Sequence conflict9451I → L in BAC99315. Ref.2
Sequence conflict9451I → L in BAA91356. Ref.3
Sequence conflict9661K → R in BAC99315. Ref.2
Sequence conflict9661K → R in BAA91356. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6E64780D6F0E7415

FASTA1,167131,616
        10         20         30         40         50         60 
MKVNRETKRL YVGGLSQDIS EADLQNQFSR FGEVSDVEII TRKDDQGNPQ KVFAYINISV 

        70         80         90        100        110        120 
AEADLKKCMS VLNKTKWKGG TLQIQLAKES FLHRLAQERE AAKAKKEEST TGNANLLEKT 

       130        140        150        160        170        180 
GGVDFHMKAV PGTEVPGHKN WVVSKFGRVL PVLHLKNQHK RKIIKYDPSK YCHNLKKIGE 

       190        200        210        220        230        240 
DFSNTIPISS LTWELEGGND PMSKKRRGEF SDFHGPPKKI IKVQKDESST GSLAMSTRPR 

       250        260        270        280        290        300 
RVIERPPLTQ QQAAQKRTCD SITPSKSSPV PVSDTQKLKN LPFKTSGLET AKKRNSISDD 

       310        320        330        340        350        360 
DTDSEDELRM MIAKEENLQR TTQPSINESE SDPFEVVRDD FKSGVHKLHS LIGLGIKNRV 

       370        380        390        400        410        420 
SCHDSDDDIM RNDREYDSGD TDEIIAMKKN VAKVKNSTEF SQMEKSTKKT SFKNRENCEL 

       430        440        450        460        470        480 
SDHCIKLQKR KSNVESALSH GLKSLNRKSP SHSSSSEDAD SASELADSEG GEEYNAMMKN 

       490        500        510        520        530        540 
CLRVNLTLAD LEQLAGSDLK VPNEDTKSDG PETTTQCKFD RGSKSPKTPT GLRRGRQCIR 

       550        560        570        580        590        600 
PAEIVASLLE GEENTCGKQK PKENNLKPKF QAFKGVGCLY EKESMKKSLK DSVASNNKDQ 

       610        620        630        640        650        660 
NSMKHEDPSI ISMEDGSPYV NGSLGEVTPC QHAKKANGPN YIQPQKRQTT FESQDRKAVS 

       670        680        690        700        710        720 
PSSSEKRSKN PISRPLEGKK SLSLSAKTHN IGFDKDSCHS TTKTEASQEE RSDSSGLTSL 

       730        740        750        760        770        780 
KKSPKVSSKD TREIKTDFSL SISNSSDVSA KDKHAEDNEK RLAALEARQK AKEVQKKLVH 

       790        800        810        820        830        840 
NALANLDGHP EDKPTHIIFG SDSECETEET STQEQSHPGE EWVKESMGKT SGKLFDSSDD 

       850        860        870        880        890        900 
DESDSEDDSN RFKIKPQFEG RAGQKLMDLQ SHFGTDDRFR MDSRFLETDS EEEQEEVNEK 

       910        920        930        940        950        960 
KTAEEEELAE EKKKALNVVQ SVLQINLSNS TNRGSVAAKK FKDIIHYDPT KQDHATYERK 

       970        980        990       1000       1010       1020 
RDDKPKESKA KRKKKREEAE KLPEVSKEMY YNIAMDLKEI FQTTKYTSEK EEGTPWNEDC 

      1030       1040       1050       1060       1070       1080 
GKEKPEEIQD PAALTSDAEQ PSGFTFSFFD SDTKDIKEET YRVETVKPGK IVWQEDPRLQ 

      1090       1100       1110       1120       1130       1140 
DSSSEEEDVT EETDHRNSSP GEASLLEKET TRFFFFSKND ERLQGSDLFW RGVGSNMSRN 

      1150       1160 
SWEARTTNLR MDCRKKHKDA KRKMKPK 

« Hide

Isoform 2 [UniParc].

Checksum: BED9401AC2D5ABE8
Show »

FASTA1,099123,927
Isoform 4 [UniParc].

Checksum: CF4642596A282A1A
Show »

FASTA1,129127,337

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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-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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS47993.1. [Q76FK4-1]
CCDS59135.1. [Q76FK4-2]
RefSeqNP_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]
UniGeneHs.442199.

3D structure databases

ProteinModelPortalQ76FK4.
SMRQ76FK4. Positions 8-88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120364. 4 interactions.
IntActQ76FK4. 3 interactions.
MINTMINT-4539421.

PTM databases

PhosphoSiteQ76FK4.

Polymorphism databases

DMDM74758950.

Proteomic databases

MaxQBQ76FK4.
PaxDbQ76FK4.
PRIDEQ76FK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358855; ENSP00000351723; ENSG00000198000. [Q76FK4-2]
ENST00000442668; ENSP00000401177; ENSG00000198000. [Q76FK4-1]
ENST00000535387; ENSP00000441300; ENSG00000198000. [Q76FK4-4]
ENST00000542053; ENSP00000440709; ENSG00000198000. [Q76FK4-2]
ENST00000545558; ENSP00000441140; ENSG00000198000. [Q76FK4-1]
GeneID55035.
KEGGhsa:55035.
UCSCuc022bjw.1. human. [Q76FK4-1]

Organism-specific databases

CTD55035.
GeneCardsGC09M095059.
HGNCHGNC:23387. NOL8.
HPAHPA044440.
MIM611534. gene.
neXtProtNX_Q76FK4.
PharmGKBPA134918056.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG73280.
HOVERGENHBG057565.
InParanoidQ76FK4.
OMAFQAFKGI.
OrthoDBEOG70CR60.
PhylomeDBQ76FK4.
TreeFamTF323283.

Gene expression databases

ArrayExpressQ76FK4.
BgeeQ76FK4.
GenevestigatorQ76FK4.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNOL8.
GenomeRNAi55035.
NextBio58463.
PROQ76FK4.
SOURCESearch...

Entry information

Entry nameNOL8_HUMAN
AccessionPrimary (citable) accession number: Q76FK4
Secondary accession number(s): Q5TCC7 expand/collapse secondary AC list , Q5TCC8, Q5TCD3, Q5TCD5, Q5TCD6, Q5TCD7, Q76D35, Q7L3E2, Q9H586, Q9H795, Q9H7W7, Q9H9J6, Q9NWA4, Q9NWM4
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM