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UniProtKB/Swiss-Prot entry Q8R1N0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ZN830_MOUSE
Primary accession number Q8R1N0
Secondary accession numbers Q3TR52 Q9CWV9 Q9CYI6
Integrated into Swiss-Prot on December 6, 2005
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Zinc finger protein 830
Synonyms Coiled-coil domain-containing protein 16
Ovus mutant candidate gene 1 protein
Gene name
Name: Znf830
Synonyms: Ccdc16, Omcg1, Zfp830
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Kidney, Liver, Skin, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/mcp.M400085-MCP200; PubMed=15345747 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND KNOCKOUT.
DOI=10.1128/MCB.25.14.6289-6302.2005; PubMed=15988037 [NCBI, ExPASy, EBI, Israel, Japan]
Artus J., Vandormael-Pournin S., Froedin M., Nacerddine K., Babinet C., Cohen-Tannoudji M.;
"Impaired mitotic progression and preimplantation lethality in mice lacking OMCG1, a new evolutionarily conserved nuclear protein.";
Mol. Cell. Biol. 25:6289-6302(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342 AND SER-353, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
Comments
  • FUNCTION: Acts as an important regulator of the cell cycle in the preimplantation embryo by controlling different aspects of M phase.
  • SUBCELLULAR LOCATION: Nucleus. Note=Excluded from nucleolus. In metaphase II oocytes and in mitotic blastomeres, it is detected in cytoplasm, suggesting that it is not associated with chromosomes during mitosis.
  • TISSUE SPECIFICITY: Widely expressed at low level.
  • DEVELOPMENTAL STAGE: Expressed in preimplantation embryos.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
  • MISCELLANEOUS: Mice lacking Ccdc16 die by the end of preimplantation development and exhibit a dramatic reduction in the total cell number, a high mitotic index, and the presence of abnormal mitotic figures.
  • SIMILARITY: Contains 1 C2H2-type zinc finger.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK050043; BAC34045.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK010353; BAB26873.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK017640; BAB30851.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK132497; BAE21204.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK148058; BAE28318.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK163064; BAE37178.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK167656; BAE39707.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK168417; BAE40331.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645594; CAI25093.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024340; AAH24340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_080160.2; -.
UniGene Mm.29622
3D structure databases
ModBase Q8R1N0.
PTM databases
PhosphoSite Q8R1N0; -.
Organism-specific databases
MGI MGI:1914233; Zfp830.
Gene expression databases
ArrayExpress Q8R1N0; -.
CleanEx MM_ZFP830; -.
GermOnline ENSMUSG00000046010; Mus musculus.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0001832; Biological process: blastocyst growth (inferred from mutant phenotype from MGI).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0007067; Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
PROSITE PS00028; ZINC_FINGER_C2H2_1; 1.
PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8R1N0.
Genome annotation databases
Ensembl ENSMUSG00000046010; Mus musculus. [Contig view]
GeneID 66983; -.
KEGG mmu:66983; -.
Phylogenomic databases
HOGENOM Q8R1N0; -.
HOVERGEN Q8R1N0; -.
Other
NextBio 323216; -.
SOURCE Znf830; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell cycle; Cell division; Coiled coil; Developmental protein; Metal-binding; Mitosis; Nucleus; Phosphoprotein; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   363  363     Zinc finger protein 830. PRO_0000076194
ZN_FING   53    75  23     C2H2-type. 
COILED   16    40  25     Potential. 
COILED   303   331  29     Potential. 
MOD_RES   342   342        Phosphoserine. 
MOD_RES   353   353        Phosphoserine. 
CONFLICT   81    82        EL -> DV (in Ref. 1; BAB30851). 
CONFLICT   111   111        Q -> L (in Ref. 1; BAB26873). 
CONFLICT   305   305        C -> G (in Ref. 1; BAE37178). 
CONFLICT   309   309        V -> G (in Ref. 1; BAE37178). 
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 40658 Da [This is the MW of the unprocessed precursor] CRC64: 1247580A0D8B6E60 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASSTSTRTP AGKRVVNQEE LRRLMREKQR LSTNRKRIES PFAKYNRLGQ LSCALCNTPV 

        70         80         90        100        110        120 
KSELLWQTHV LGKQHRERVA ELKGAKGATQ GPSTGTVPQA TKRRATDVES QDAKKAKASA 

       130        140        150        160        170        180 
GPQVQPSTSA SSANLDAARA APSKPGLGLL PDYDDEEEEE EEGGGEERRD SSKHLPDAQG 

       190        200        210        220        230        240 
KEHSLASPRE TTSNVLPNDP FNTNPPKAPL VPHSGSIEKA EIHEKVVERR ENTAEALPEG 

       250        260        270        280        290        300 
FFDDPEVDAK VRKVDAPKDQ MDKEWDEFQK AMRQVNTISE AIVAEEDEEG RLDRQIGEID 

       310        320        330        340        350        360 
EQIECYRRVE KLRNRQDEIK NKLKEVLTIK ELQKKEEENV DSDDEGELQD LLSQDWRVKG 


ALL 

Q8R1N0 in FASTA format

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