Reviewed, UniProtKB/Swiss-Prot Q8R1N0 (ZN830_MOUSE)

Names and origin

Protein names

Recommended name:
Zinc finger protein 830

Alternative name(s):
Coiled-coil domain-containing protein 16
Ovus mutant candidate gene 1 protein

Gene names

Name:	Znf830
Synonyms:	Ccdc16, Omcg1, Zfp830

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	363 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	Acts as an important regulator of the cell cycle in the preimplantation embryo by controlling different aspects of M phase. Ref.5
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. Ref.5
Tissue specificity	Widely expressed at low level. Ref.5
Developmental stage	Expressed in preimplantation embryos.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.4 Ref.6 Ref.7
Disruption phenotype	Mice 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. Ref.5
Sequence similarities	Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	blastocyst growth Ref.5 Inferred from mutant phenotype. Source: MGI cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.5 Inferred from direct assay. Source: MGI
Molecular function	zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 363	362	Zinc finger protein 830		PRO_0000076194
Regions
	Zinc finger	53 – 75	23	C2H2-type
	Coiled coil	16 – 40	25	Potential
	Coiled coil	303 – 331	29	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	342	1	Phosphoserine Ref.4 Ref.6 Ref.7
	Modified residue	353	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	81 – 82	2	EL → DV in BAB30851. Ref.1
	Sequence conflict	111	1	Q → L in BAB26873. Ref.1
	Sequence conflict	305	1	C → G in BAE37178. Ref.1
	Sequence conflict	309	1	V → G in BAE37178. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8R1N0-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 1247580A0D8B6E60	FASTA	363	40,658
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney, Liver, Skin and Thymus.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon.
[4]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Impaired mitotic progression and preimplantation lethality in mice lacking OMCG1, a new evolutionarily conserved nuclear protein." Artus J., Vandormael-Pournin S., Froedin M., Nacerddine K., Babinet C., Cohen-Tannoudji M. Mol. Cell. Biol. 25:6289-6302(2005) [PubMed: 15988037] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342 AND SER-353, MASS SPECTROMETRY.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK050043 mRNA. Translation: BAC34045.1. AK010353 mRNA. Translation: BAB26873.1. AK017640 mRNA. Translation: BAB30851.1. AK132497 mRNA. Translation: BAE21204.1. AK148058 mRNA. Translation: BAE28318.1. AK163064 mRNA. Translation: BAE37178.1. AK167656 mRNA. Translation: BAE39707.1. AK168417 mRNA. Translation: BAE40331.1. AL645594 Genomic DNA. Translation: CAI25093.1. BC024340 mRNA. Translation: AAH24340.1.
IPI	IPI00320645.
RefSeq	NP_080160.2.
UniGene	Mm.29622
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8R1N0.
PTM databases
PhosphoSite	Q8R1N0.
Proteomic databases
PRIDE	Q8R1N0.
Genome annotation databases
Ensembl	ENSMUST00000056677; ENSMUSP00000056154; ENSMUSG00000046010; Mus musculus. [Genome view]
GeneID	66983.
KEGG	mmu:66983.
UCSC	uc007kmy.1. mouse.
Organism-specific databases
CTD	66983.
MGI	MGI:1914233. Zfp830.
Phylogenomic databases
eggNOG	roNOG15199.
HOGENOM	HBG713871.
HOVERGEN	HBG105347.
InParanoid	Q8R1N0.
OMA	ESPFAKY.
OrthoDB	EOG9XWJHM.
PhylomeDB	Q8R1N0.
Gene expression databases
ArrayExpress	Q8R1N0.
Bgee	Q8R1N0.
CleanEx	MM_ZFP830.
Genevestigator	Q8R1N0.
GermOnline	ENSMUSG00000046010. Mus musculus.
Family and domain databases
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 1 hit. PS50157. ZINC_FINGER_C2H2_2. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	323216.
SOURCE	Search...

Entry information

Entry name

ZN830_MOUSE

Accession

Primary (citable) accession number: Q8R1N0
Secondary accession number(s): Q3TR52, Q9CWV9, Q9CYI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	June 1, 2002
Last modified:	March 2, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)