Entry euk:ZN830_RAT

ID   ZN830_RAT               Reviewed;         370 AA.
AC   Q3MHS2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   10-MAY-2017, entry version 90.
DE   RecName: Full=Zinc finger protein 830 {ECO:0000250|UniProtKB:Q96NB3};
DE   AltName: Full=Coiled-coil domain-containing protein 16 {ECO:0000250|UniProtKB:Q96NB3};
GN   Name=Znf830 {ECO:0000250|UniProtKB:Q96NB3};
GN   Synonyms=Ccdc16 {ECO:0000250|UniProtKB:Q96NB3},
GN   Zfp830 {ECO:0000312|RGD:1562573};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Acts as an important regulator of the cell cycle that
CC       participates in the maintenance of genome integrity. During cell
CC       cycle progression in embryonic fibroblast, prevents replication
CC       fork collapse, double-strand break formation and cell cycle
CC       checkpoint activation. Controls mitotic cell cycle progression and
CC       cell survival in rapidly proliferating intestinal epithelium and
CC       embryonic stem cells. During the embryo preimplantation, controls
CC       different aspects of M phase. During early oocyte growth, plays a
CC       role in oocyte survival by preventing chromosomal breaks
CC       formation, activation of TP63 and reduction of transcription.
CC       {ECO:0000250|UniProtKB:Q8R1N0}.
CC   -!- SUBUNIT: Component of the XAB2 complex, a multimeric protein
CC       complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE;
CC       this complex binds preferentially to RNA. Interacts with XAB2.
CC       {ECO:0000250|UniProtKB:Q96NB3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8R1N0}.
CC       Chromosome {ECO:0000250|UniProtKB:Q8R1N0}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q8R1N0}. Note=Excluded from nucleolus.
CC       {ECO:0000250|UniProtKB:Q8R1N0}.
CC   -!- PTM: Phosphorylated in response to DNA damage by the cell cycle
CC       checkpoint kinases ATR/ATM. {ECO:0000250|UniProtKB:Q8R1N0}.
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DR   EMBL; BC104717; AAI04718.1; -; mRNA.
DR   RefSeq; NP_001032437.1; NM_001037360.1.
DR   UniGene; Rn.137587; -.
DR   SMR; Q3MHS2; -.
DR   STRING; 10116.ENSRNOP00000009970; -.
DR   iPTMnet; Q3MHS2; -.
DR   PhosphoSitePlus; Q3MHS2; -.
DR   PaxDb; Q3MHS2; -.
DR   PRIDE; Q3MHS2; -.
DR   Ensembl; ENSRNOT00000009970; ENSRNOP00000009970; ENSRNOG00000007578.
DR   GeneID; 497967; -.
DR   KEGG; rno:497967; -.
DR   CTD; 66983; -.
DR   RGD; 1562573; Zfp830.
DR   eggNOG; KOG3032; Eukaryota.
DR   eggNOG; ENOG4111GTR; LUCA.
DR   GeneTree; ENSGT00390000012151; -.
DR   HOGENOM; HOG000246999; -.
DR   HOVERGEN; HBG105347; -.
DR   InParanoid; Q3MHS2; -.
DR   KO; K13104; -.
DR   OMA; VLGKQHR; -.
DR   OrthoDB; EOG091G0MBX; -.
DR   PhylomeDB; Q3MHS2; -.
DR   TreeFam; TF315895; -.
DR   Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR   Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   PRO; PR:Q3MHS2; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000007578; -.
DR   Genevisible; Q3MHS2; RN.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR   GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl.
DR   GO; GO:0044773; P:mitotic DNA damage checkpoint; IEA:Ensembl.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint; ISS:UniProtKB.
DR   GO; GO:0007067; P:mitotic nuclear division; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0033260; P:nuclear DNA replication; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0001546; P:preantral ovarian follicle growth; ISS:UniProtKB.
DR   GO; GO:0048478; P:replication fork protection; ISS:UniProtKB.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Chromosome; Coiled coil;
KW   Complete proteome; Developmental protein; Metal-binding; Mitosis;
KW   Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q96NB3}.
FT   CHAIN         2    370       Zinc finger protein 830.
FT                                /FTId=PRO_0000076195.
FT   ZN_FING      53     75       C2H2-type.
FT   COILED       16     40       {ECO:0000255}.
FT   COILED      310    338       {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q96NB3}.
FT   MOD_RES     223    223       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96NB3}.
FT   MOD_RES     349    349       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     360    360       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96NB3}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        48     82       ismart:ZnF_U1 [T]
SQ   SEQUENCE   370 AA;  41616 MW;  6CB839F65F0B990B CRC64;
     MASSTSARTP AGKRVVNQEE LRRLMKEKQR LSTNRKRIES PFAKYNRLGQ LSCALCNTPV
     KSELLWQTHV LGKQHRERVA ELKGAKGATQ GPSAGTAPQP TKRKTTDVES QDAKKAKASV
     DQVQPSTSAS SANFEKSGKE ATRVASSKTG LGLLPDYEEE EEEEEEEELG GGEERRDSSK
     HLPDAQGREH SLASPRETTS NVLPNDPFNT NPPKAPLVPH SGSIEKAEIH EKVVERRENT
     AEALPEGFFD DPEVDAKVRK VDAPKDQMDK EWDEFQKAMR QVNTISEAIV AEEDEEGRLD
     RQIGEIDEQI ECYRRVEKLR NRQDEIKNKL KEVLTIKELQ KKEEENVDSD DEGELQDLLS
     QDWRVKGALL
//