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 03-AUG-2022, entry version 112.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role in pre-mRNA splicing as component of the
CC spliceosome (By similarity). Acts as an important regulator of the cell
CC cycle that participates in the maintenance of genome integrity. During
CC cell cycle progression in embryonic fibroblast, prevents replication
CC fork collapse, double-strand break formation and cell cycle checkpoint
CC activation. Controls mitotic cell cycle progression and cell survival
CC in rapidly proliferating intestinal epithelium and embryonic stem
CC cells. During the embryo preimplantation, controls different aspects of
CC M phase. During early oocyte growth, plays a role in oocyte survival by
CC preventing chromosomal breaks formation, activation of TP63 and
CC reduction of transcription (By similarity).
CC {ECO:0000250|UniProtKB:Q8R1N0, ECO:0000250|UniProtKB:Q96NB3}.
CC -!- SUBUNIT: Component of the XAB2 complex, a multimeric protein complex
CC composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE; this complex
CC binds preferentially to RNA. Interacts with XAB2. Identified in a
CC pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1,
CC ZNF830 and PPIE that is incorporated into the spliceosome as a
CC preassembled complex. The IB complex does not contain PRPF19.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC104717; AAI04718.1; -; mRNA.
DR RefSeq; NP_001032437.1; NM_001037360.1.
DR AlphaFoldDB; Q3MHS2; -.
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 GeneTree; ENSGT00390000012151; -.
DR HOGENOM; CLU_058140_1_0_1; -.
DR InParanoid; Q3MHS2; -.
DR OMA; EQIECYK; -.
DR OrthoDB; 1458826at2759; -.
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; Expressed in thymus and 20 other tissues.
DR Genevisible; Q3MHS2; RN.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; ISO:RGD.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0033260; P:nuclear DNA replication; ISO:RGD.
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 GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR040050; ZNF830-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR13278; PTHR13278; 1.
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 Developmental protein; Metal-binding; Mitosis; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96NB3"
FT CHAIN 2..370
FT /note="Zinc finger protein 830"
FT /id="PRO_0000076195"
FT ZN_FING 53..75
FT /note="C2H2-type"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..40
FT /evidence="ECO:0000255"
FT COILED 310..338
FT /evidence="ECO:0000255"
FT COMPBIAS 120..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96NB3"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NB3"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NB3"
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
