CDCA7_RAT
ID CDCA7_RAT Reviewed; 377 AA.
AC Q4KM91;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cell division cycle-associated protein 7;
GN Name=Cdca7;
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 FUNCTION.
RX PubMed=11598121; DOI=10.1074/jbc.m107357200;
RA Prescott J.E., Osthus R.C., Lee L.A., Lewis B.C., Shim H., Barrett J.F.,
RA Guo Q., Hawkins A.L., Griffin C.A., Dang C.V.;
RT "A novel c-Myc-responsive gene, JPO1, participates in neoplastic
RT transformation.";
RL J. Biol. Chem. 276:48276-48284(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-220, AND
RP IDENTIFICATION 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., 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: Participates in MYC-mediated cell transformation and
CC apoptosis; induces anchorage-independent growth and clonogenicity in
CC lymphoblastoid cells. Insufficient to induce tumorigenicity when
CC overexpressed but contributes to MYC-mediated tumorigenesis. May play a
CC role as transcriptional regulator (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11598121}.
CC -!- SUBUNIT: Interacts with MYC (via C-terminus), YWHAE and YWHAZ.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Predominantly nuclear with some expression also seen in the
CC cytoplasm. Predominantly cytoplasmic when phosphorylated at Thr-166 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation at Thr-166 promotes interaction with YWHAE and
CC YWHAZ, dissociation from MYC and sequestration in the cytoplasm.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Cdca7 expression is correlated with MYC expression in
CC fibroblasts and is much higher in attached cells tham in non-attached
CC cells.
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DR EMBL; BC098690; AAH98690.1; -; mRNA.
DR RefSeq; NP_001020864.1; NM_001025693.1.
DR AlphaFoldDB; Q4KM91; -.
DR STRING; 10116.ENSRNOP00000002066; -.
DR iPTMnet; Q4KM91; -.
DR PhosphoSitePlus; Q4KM91; -.
DR PaxDb; Q4KM91; -.
DR PRIDE; Q4KM91; -.
DR GeneID; 311742; -.
DR KEGG; rno:311742; -.
DR UCSC; RGD:1309363; rat.
DR CTD; 83879; -.
DR RGD; 1309363; Cdca7.
DR VEuPathDB; HostDB:ENSRNOG00000001514; -.
DR eggNOG; ENOG502QQPE; Eukaryota.
DR HOGENOM; CLU_035988_2_0_1; -.
DR InParanoid; Q4KM91; -.
DR OMA; NICGSAR; -.
DR OrthoDB; 1462540at2759; -.
DR PhylomeDB; Q4KM91; -.
DR TreeFam; TF101076; -.
DR PRO; PR:Q4KM91; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000001514; Expressed in thymus and 19 other tissues.
DR Genevisible; Q4KM91; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR033576; CDCA7.
DR InterPro; IPR040221; CDCA7/CDA7L.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR PANTHER; PTHR31169; PTHR31169; 1.
DR PANTHER; PTHR31169:SF2; PTHR31169:SF2; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..377
FT /note="Cell division cycle-associated protein 7"
FT /id="PRO_0000249312"
FT REGION 58..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..173
FT /note="Interaction with MYC"
FT /evidence="ECO:0000250"
FT REGION 253..377
FT /note="Mediates transcriptional activity"
FT /evidence="ECO:0000250"
FT MOTIF 163..179
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 170..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT1"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0M2"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT1"
SQ SEQUENCE 377 AA; 43024 MW; 891BD511AC76DC63 CRC64;
MEARRARQKA LKVKNLKNVR YMKLISVETS SSSDDSCDSF ASDNFANTRL QFNREGCRTR
SQCRPSGPLR VAMKFPARNT RRAANTKAAP PKPSESSAND SHSESDSEEE EDGMNFLEKR
ALNIKQNKAM LAKLMSELES FPGIFSGRHS LPGHRTKDSK SPRRRTFPGV ASRRNPERRA
RPLTRSRSRI LGSLGALPTE EEEDEEEEED KYMLVRRRKS VDGYMNDDDV SRSRRPGSMT
LPHIIRPVED VTEEEIRNIC SNSREKIYNR SLGSTCHQCR QKTTDTKTNC RNPDCWGIRG
QFCGPCLRNR YGEEVKDALL DPNWHCPPCR GICNCSFCRQ RDGRCATGVL VYLAKYHGFG
NVHAYLKSLK QEFEMQA
