CDA7L_MOUSE
ID CDA7L_MOUSE Reviewed; 438 AA.
AC Q922M5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cell division cycle-associated 7-like protein;
DE AltName: Full=Transcription factor RAM2;
GN Name=Cdca7l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=15994933; DOI=10.1158/0008-5472.can-05-0500;
RA Huang A., Ho C.S.W., Ponzielli R., Barsyte-Lovejoy D., Bouffet E.,
RA Picard D., Hawkins C.E., Penn L.Z.;
RT "Identification of a novel c-Myc protein interactor, JPO2, with
RT transforming activity in medulloblastoma cells.";
RL Cancer Res. 65:5607-5619(2005).
RN [4]
RP FUNCTION.
RX PubMed=16829576; DOI=10.1073/pnas.0601515103;
RA Ou X.-M., Chen K., Shih J.C.;
RT "Monoamine oxidase A and repressor R1 are involved in apoptotic signaling
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10923-10928(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-185, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in transcriptional regulation as a repressor
CC that inhibits monoamine oxidase A (MAOA) activity and gene expression
CC by binding to the promoter. Plays an important oncogenic role in
CC mediating the full transforming effect of MYC in medulloblastoma cells
CC (By similarity). Involved in apoptotic signaling pathways; May act
CC downstream of P38-kinase and BCL-2, but upstream of CASP3/caspase-3 as
CC well as CCND1/cyclin D1 and E2F1. {ECO:0000250,
CC ECO:0000269|PubMed:16829576}.
CC -!- SUBUNIT: Interacts with MYC (By similarity). Interacts (via IBM motifs)
CC with PSIP1 (via IBD domain); phosphorylation increases its affinity for
CC PSIP1 (By similarity). {ECO:0000250|UniProtKB:Q96GN5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Associates with chromatin. Translocates from cytoplasm to nucleus
CC under dexamethasone induction (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues but not detected in total
CC brain. {ECO:0000269|PubMed:15994933}.
CC -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC {ECO:0000250|UniProtKB:Q96GN5}.
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; AK149673; BAE29017.1; -; mRNA.
DR EMBL; BC006933; AAH06933.1; -; mRNA.
DR CCDS; CCDS49197.1; -.
DR RefSeq; NP_666152.1; NM_146040.1.
DR AlphaFoldDB; Q922M5; -.
DR BioGRID; 229982; 3.
DR STRING; 10090.ENSMUSP00000021592; -.
DR iPTMnet; Q922M5; -.
DR PhosphoSitePlus; Q922M5; -.
DR EPD; Q922M5; -.
DR MaxQB; Q922M5; -.
DR PaxDb; Q922M5; -.
DR PeptideAtlas; Q922M5; -.
DR PRIDE; Q922M5; -.
DR ProteomicsDB; 265637; -.
DR Antibodypedia; 11993; 257 antibodies from 25 providers.
DR DNASU; 217946; -.
DR Ensembl; ENSMUST00000021592; ENSMUSP00000021592; ENSMUSG00000021175.
DR GeneID; 217946; -.
DR KEGG; mmu:217946; -.
DR UCSC; uc007pid.1; mouse.
DR CTD; 55536; -.
DR MGI; MGI:2384982; Cdca7l.
DR VEuPathDB; HostDB:ENSMUSG00000021175; -.
DR eggNOG; ENOG502QWH1; Eukaryota.
DR GeneTree; ENSGT00940000159108; -.
DR HOGENOM; CLU_035988_0_0_1; -.
DR InParanoid; Q922M5; -.
DR OMA; KAPCFKS; -.
DR OrthoDB; 1462540at2759; -.
DR PhylomeDB; Q922M5; -.
DR TreeFam; TF101076; -.
DR BioGRID-ORCS; 217946; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cdca7l; mouse.
DR PRO; PR:Q922M5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q922M5; protein.
DR Bgee; ENSMUSG00000021175; Expressed in glomerular capsule and 212 other tissues.
DR ExpressionAtlas; Q922M5; baseline and differential.
DR Genevisible; Q922M5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR040221; CDCA7/CDA7L.
DR InterPro; IPR033578; CDCA7L.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR PANTHER; PTHR31169; PTHR31169; 1.
DR PANTHER; PTHR31169:SF4; PTHR31169:SF4; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..438
FT /note="Cell division cycle-associated 7-like protein"
FT /id="PRO_0000249314"
FT REGION 56..115
FT /note="PSIP1-binding"
FT /evidence="ECO:0000250"
FT REGION 74..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..223
FT /note="MYC-binding"
FT /evidence="ECO:0000250"
FT MOTIF 9..33
FT /note="Integrase domain-binding motif 1 (IBM1)"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOTIF 63..89
FT /note="Integrase domain-binding motif 2 (IBM2)"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT COMPBIAS 150..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
SQ SEQUENCE 438 AA; 50248 MW; D0BB5A15A0321ABA CRC64;
MELATRSQIP KEVADIFSAP SDDEEFVGFQ DDVPMQNLSE SCGSLDSREL EKQQNVCFRS
KYFTEELRRI FKEDTDSEME DFEGFTESEL NMSSNPELME SELSDSDKAY PVMNDAEEDD
EEEAAPRRGR STRRSSFGLR VAFQFPTKKL ARTPDKDSSH LLDSKTDLRR KKSSRQPKGK
EDSASDAEDE SRAESQENSD ALLKRAMNIK ENKAMLAQLL AELNSVPDFF PVRTPPSASR
RRTPRRAFSE GQITRRMNPT RSARPPEKFA LENFTFSATK LTEELYSFRR RKTISGGKCQ
TYRRHRISSF RSVKDITEED LENIAITVRD KVYDKVLGNT CHQCRQKTID TKTVCRNQSC
GGVRGQFCGP CLRNRYGEDV RTALLDPKWT CPPCRGICNC SYCRRRDGRC ATGILIHLAK
FYGYDNVKEY LESLQKQL
