CDA7L_HUMAN
ID CDA7L_HUMAN Reviewed; 454 AA.
AC Q96GN5; A4D141; A6NF50; B3KTR5; B4DUT3; C9K0Y1; Q6PIL4; Q86YT0; Q8IXN5;
AC Q96C70; Q9H9A2; Q9NPV2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cell division cycle-associated 7-like protein;
DE AltName: Full=Protein JPO2;
DE AltName: Full=Transcription factor RAM2;
GN Name=CDCA7L; Synonyms=HR1, JPO2, R1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, REGION, INTERACTION WITH MYC, AND FUNCTION.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=15654081; DOI=10.1074/jbc.m410033200;
RA Chen K., Ou X.-M., Chen G., Choi S.H., Shih J.C.;
RT "R1, a novel repressor of the human monoamine oxidase A.";
RL J. Biol. Chem. 280:11552-11559(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Cathomen T., Wang K.H., Oswald W.B., Weitzman M.D.;
RT "RAM2 augments production of recombinant adeno-associated virus.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, Lung, and Muscle;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-454 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PSIP1, AND REGION.
RX PubMed=16735438; DOI=10.1242/jcs.02995;
RA Maertens G.N., Cherepanov P., Engelman A.;
RT "Transcriptional co-activator p75 binds and tethers the Myc-interacting
RT protein JPO2 to chromatin.";
RL J. Cell Sci. 119:2563-2571(2006).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=16728402; DOI=10.1074/jbc.m600250200;
RA Ou X.-M., Chen K., Shih J.C.;
RT "Glucocorticoid and androgen activation of monoamine oxidase A is regulated
RT differently by R1 and Sp1.";
RL J. Biol. Chem. 281:21512-21525(2006).
RN [13]
RP FUNCTION, AND INTERACTION WITH MYC.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-108; SER-117 AND
RP SER-162, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-77; SER-79; SER-117;
RP SER-139 AND SER-162, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-77; SER-79; SER-105;
RP SER-108; SER-117; SER-138; SER-139; SER-162 AND SER-261, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP INTERACTION WITH PSIP1.
RX PubMed=25082813; DOI=10.1158/0008-5472.can-13-3602;
RA Cermakova K., Tesina P., Demeulemeester J., El Ashkar S., Mereau H.,
RA Schwaller J., Rezacova P., Veverka V., De Rijck J.;
RT "Validation and structural characterization of the LEDGF/p75-MLL interface
RT as a new target for the treatment of MLL-dependent leukemia.";
RL Cancer Res. 74:5139-5151(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-222 AND LYS-225, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [22] {ECO:0007744|PDB:5YI9, ECO:0007744|PDB:6EMO}
RP STRUCTURE BY NMR OF 1-32 AND 56-91 IN COMPLEX WITH PSIP1, INTERACTION WITH
RP PSIP1, DOMAIN IBM MOTIF, MUTAGENESIS OF ILE-16; PHE-17; SER-21; ILE-72;
RP PHE-73; THR-77; SER-79 AND THR-81, AND PHOSPHORYLATION AT SER-21; THR-77;
RP SER-79; THR-81 AND THR-88.
RX PubMed=29997176; DOI=10.1073/pnas.1803909115;
RA Sharma S., Cermakova K., De Rijck J., Demeulemeester J., Fabry M.,
RA El Ashkar S., Van Belle S., Lepsik M., Tesina P., Duchoslav V., Novak P.,
RA Hubalek M., Srb P., Christ F., Rezacova P., Hodges H.C., Debyser Z.,
RA Veverka V.;
RT "Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-
RT dependent phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E7053-E7062(2018).
RN [23]
RP VARIANT ASN-45.
RX PubMed=29961568; DOI=10.1016/j.ajhg.2018.06.001;
RG NIHR BioResource;
RG Care4Rare Canada Consortium;
RA Ito Y., Carss K.J., Duarte S.T., Hartley T., Keren B., Kurian M.A.,
RA Marey I., Charles P., Mendonca C., Nava C., Pfundt R., Sanchis-Juan A.,
RA van Bokhoven H., van Essen A., van Ravenswaaij-Arts C., Boycott K.M.,
RA Kernohan K.D., Dyack S., Raymond F.L.;
RT "De Novo Truncating Mutations in WASF1 Cause Intellectual Disability with
RT Seizures.";
RL Am. J. Hum. Genet. 103:144-153(2018).
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 Involved in apoptotic signaling pathways; May act downstream of P38-
CC kinase and BCL-2, but upstream of CASP3/caspase-3 as well as
CC CCND1/cyclin D1 and E2F1. {ECO:0000269|PubMed:15654081,
CC ECO:0000269|PubMed:15994933, ECO:0000269|PubMed:16829576}.
CC -!- SUBUNIT: Interacts with MYC (PubMed:15994933, PubMed:16829576).
CC Interacts (via IBM motifs) with PSIP1 (via IBD domain); phosphorylation
CC increases its affinity for PSIP1 (PubMed:16735438, PubMed:25082813,
CC PubMed:29997176). {ECO:0000269|PubMed:15994933,
CC ECO:0000269|PubMed:16735438, ECO:0000269|PubMed:16829576,
CC ECO:0000269|PubMed:25082813, ECO:0000269|PubMed:29997176}.
CC -!- INTERACTION:
CC Q96GN5; Q9ULW3: ABT1; NbExp=3; IntAct=EBI-5278764, EBI-2602396;
CC Q96GN5; Q15327: ANKRD1; NbExp=3; IntAct=EBI-5278764, EBI-5653378;
CC Q96GN5; X5D778: ANKRD11; NbExp=3; IntAct=EBI-5278764, EBI-17183751;
CC Q96GN5; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-5278764, EBI-5661893;
CC Q96GN5; Q5T686: AVPI1; NbExp=3; IntAct=EBI-5278764, EBI-8640233;
CC Q96GN5; Q9UL15: BAG5; NbExp=3; IntAct=EBI-5278764, EBI-356517;
CC Q96GN5; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-5278764, EBI-10181188;
CC Q96GN5; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-5278764, EBI-11519926;
CC Q96GN5; P55201-2: BRPF1; NbExp=3; IntAct=EBI-5278764, EBI-12065306;
CC Q96GN5; Q13895: BYSL; NbExp=5; IntAct=EBI-5278764, EBI-358049;
CC Q96GN5; Q9H257: CARD9; NbExp=4; IntAct=EBI-5278764, EBI-751319;
CC Q96GN5; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-5278764, EBI-2559016;
CC Q96GN5; Q8IYX3: CCDC116; NbExp=3; IntAct=EBI-5278764, EBI-744311;
CC Q96GN5; Q8NHQ1: CEP70; NbExp=7; IntAct=EBI-5278764, EBI-739624;
CC Q96GN5; Q8WYA6: CTNNBL1; NbExp=4; IntAct=EBI-5278764, EBI-748128;
CC Q96GN5; Q9UER7: DAXX; NbExp=3; IntAct=EBI-5278764, EBI-77321;
CC Q96GN5; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-5278764, EBI-399105;
CC Q96GN5; P38919: EIF4A3; NbExp=3; IntAct=EBI-5278764, EBI-299104;
CC Q96GN5; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-5278764, EBI-19153639;
CC Q96GN5; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-5278764, EBI-10175124;
CC Q96GN5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-5278764, EBI-618309;
CC Q96GN5; O75031: HSF2BP; NbExp=3; IntAct=EBI-5278764, EBI-7116203;
CC Q96GN5; Q8WYH8: ING5; NbExp=3; IntAct=EBI-5278764, EBI-488533;
CC Q96GN5; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-5278764, EBI-12094820;
CC Q96GN5; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-5278764, EBI-10172290;
CC Q96GN5; P25800: LMO1; NbExp=3; IntAct=EBI-5278764, EBI-8639312;
CC Q96GN5; Q96EZ8: MCRS1; NbExp=6; IntAct=EBI-5278764, EBI-348259;
CC Q96GN5; Q99750: MDFI; NbExp=6; IntAct=EBI-5278764, EBI-724076;
CC Q96GN5; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-5278764, EBI-16439278;
CC Q96GN5; P55081: MFAP1; NbExp=3; IntAct=EBI-5278764, EBI-1048159;
CC Q96GN5; P40692: MLH1; NbExp=4; IntAct=EBI-5278764, EBI-744248;
CC Q96GN5; Q6PF18: MORN3; NbExp=3; IntAct=EBI-5278764, EBI-9675802;
CC Q96GN5; Q13084: MRPL28; NbExp=3; IntAct=EBI-5278764, EBI-723426;
CC Q96GN5; P17568: NDUFB7; NbExp=3; IntAct=EBI-5278764, EBI-1246238;
CC Q96GN5; Q9UGY1: NOL12; NbExp=3; IntAct=EBI-5278764, EBI-716098;
CC Q96GN5; P46087: NOP2; NbExp=3; IntAct=EBI-5278764, EBI-356811;
CC Q96GN5; P40424: PBX1; NbExp=3; IntAct=EBI-5278764, EBI-301611;
CC Q96GN5; P40425: PBX2; NbExp=3; IntAct=EBI-5278764, EBI-348489;
CC Q96GN5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5278764, EBI-79165;
CC Q96GN5; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-5278764, EBI-357318;
CC Q96GN5; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-5278764, EBI-11532361;
CC Q96GN5; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-5278764, EBI-710402;
CC Q96GN5; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-5278764, EBI-10293968;
CC Q96GN5; Q9GZV8: PRDM14; NbExp=6; IntAct=EBI-5278764, EBI-3957793;
CC Q96GN5; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-5278764, EBI-1567797;
CC Q96GN5; Q9Y3A4: RRP7A; NbExp=3; IntAct=EBI-5278764, EBI-7223720;
CC Q96GN5; Q6IEG0: SNRNP48; NbExp=3; IntAct=EBI-5278764, EBI-2876632;
CC Q96GN5; Q16384: SSX1; NbExp=3; IntAct=EBI-5278764, EBI-10237585;
CC Q96GN5; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-5278764, EBI-2212028;
CC Q96GN5; O75558: STX11; NbExp=3; IntAct=EBI-5278764, EBI-714135;
CC Q96GN5; O75478: TADA2A; NbExp=3; IntAct=EBI-5278764, EBI-742268;
CC Q96GN5; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-5278764, EBI-10178002;
CC Q96GN5; P19237: TNNI1; NbExp=3; IntAct=EBI-5278764, EBI-746692;
CC Q96GN5; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-5278764, EBI-765817;
CC Q96GN5; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-5278764, EBI-5235829;
CC Q96GN5; P11441: UBL4A; NbExp=3; IntAct=EBI-5278764, EBI-356983;
CC Q96GN5; Q9NQZ2: UTP3; NbExp=3; IntAct=EBI-5278764, EBI-714067;
CC Q96GN5; Q8N5A5-2: ZGPAT; NbExp=9; IntAct=EBI-5278764, EBI-10183064;
CC Q96GN5; P15622-3: ZNF250; NbExp=3; IntAct=EBI-5278764, EBI-10177272;
CC Q96GN5; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-5278764, EBI-11962468;
CC Q96GN5; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-5278764, EBI-4395669;
CC Q96GN5; O75541: ZNF821; NbExp=3; IntAct=EBI-5278764, EBI-740865;
CC Q96GN5-2; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-9091443, EBI-16429430;
CC Q96GN5-2; P22607: FGFR3; NbExp=3; IntAct=EBI-9091443, EBI-348399;
CC Q96GN5-2; P01112: HRAS; NbExp=3; IntAct=EBI-9091443, EBI-350145;
CC Q96GN5-2; P02545: LMNA; NbExp=3; IntAct=EBI-9091443, EBI-351935;
CC Q96GN5-2; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-9091443, EBI-1567797;
CC Q96GN5-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-9091443, EBI-5235340;
CC Q96GN5-2; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-9091443, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Associates with
CC chromatin. Translocates from cytoplasm to nucleus under dexamethasone
CC induction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Variant C;
CC IsoId=Q96GN5-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant B;
CC IsoId=Q96GN5-2; Sequence=VSP_020398;
CC Name=3;
CC IsoId=Q96GN5-4; Sequence=VSP_043806;
CC Name=4;
CC IsoId=Q96GN5-5; Sequence=VSP_046270;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Overexpressed in medulloblastoma.
CC {ECO:0000269|PubMed:15654081, ECO:0000269|PubMed:15994933}.
CC -!- INDUCTION: By MYC overexpression in a concentration dependent manner in
CC neuroblastoma cell line.
CC -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC {ECO:0000269|PubMed:29997176}.
CC -!- MISCELLANEOUS: Cells lacking CDCA7L display a reduction of 25-30% of
CC colony formation in medulloblastoma cell lines. CDCA7L overexpression
CC induces colony formation.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14330.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY161168; AAO17570.1; -; mRNA.
DR EMBL; AY161169; AAO17571.1; -; mRNA.
DR EMBL; AK022955; BAB14330.1; ALT_FRAME; mRNA.
DR EMBL; AK095965; BAG53177.1; -; mRNA.
DR EMBL; AK300781; BAG62445.1; -; mRNA.
DR EMBL; AC074379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24271.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93741.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93743.1; -; Genomic_DNA.
DR EMBL; BC009352; AAH09352.2; -; mRNA.
DR EMBL; BC014630; AAH14630.2; -; mRNA.
DR EMBL; BC025242; AAH25242.1; -; mRNA.
DR EMBL; BC032576; AAH32576.1; -; mRNA.
DR EMBL; BC039823; AAH39823.1; -; mRNA.
DR EMBL; AL359619; CAB94887.1; -; mRNA.
DR CCDS; CCDS47558.1; -. [Q96GN5-5]
DR CCDS; CCDS47559.1; -. [Q96GN5-4]
DR CCDS; CCDS5374.1; -. [Q96GN5-1]
DR PIR; T50635; T50635.
DR RefSeq; NP_001120842.1; NM_001127370.2. [Q96GN5-4]
DR RefSeq; NP_001120843.1; NM_001127371.2. [Q96GN5-5]
DR RefSeq; NP_061189.2; NM_018719.4. [Q96GN5-1]
DR PDB; 5YI9; NMR; -; A=56-91.
DR PDB; 6EMO; NMR; -; A=1-32.
DR PDBsum; 5YI9; -.
DR PDBsum; 6EMO; -.
DR AlphaFoldDB; Q96GN5; -.
DR SMR; Q96GN5; -.
DR BioGRID; 120705; 86.
DR DIP; DIP-61218N; -.
DR IntAct; Q96GN5; 77.
DR MINT; Q96GN5; -.
DR STRING; 9606.ENSP00000383986; -.
DR iPTMnet; Q96GN5; -.
DR PhosphoSitePlus; Q96GN5; -.
DR BioMuta; CDCA7L; -.
DR DMDM; 74751890; -.
DR EPD; Q96GN5; -.
DR jPOST; Q96GN5; -.
DR MassIVE; Q96GN5; -.
DR MaxQB; Q96GN5; -.
DR PaxDb; Q96GN5; -.
DR PeptideAtlas; Q96GN5; -.
DR PRIDE; Q96GN5; -.
DR ProteomicsDB; 12602; -.
DR ProteomicsDB; 76648; -. [Q96GN5-1]
DR ProteomicsDB; 76649; -. [Q96GN5-2]
DR ProteomicsDB; 76650; -. [Q96GN5-4]
DR Antibodypedia; 11993; 257 antibodies from 25 providers.
DR DNASU; 55536; -.
DR Ensembl; ENST00000356195.9; ENSP00000348523.5; ENSG00000164649.20. [Q96GN5-4]
DR Ensembl; ENST00000373934.4; ENSP00000363045.4; ENSG00000164649.20. [Q96GN5-5]
DR Ensembl; ENST00000406877.8; ENSP00000383986.3; ENSG00000164649.20. [Q96GN5-1]
DR GeneID; 55536; -.
DR KEGG; hsa:55536; -.
DR MANE-Select; ENST00000406877.8; ENSP00000383986.3; NM_018719.5; NP_061189.2.
DR UCSC; uc003sve.5; human. [Q96GN5-1]
DR CTD; 55536; -.
DR DisGeNET; 55536; -.
DR GeneCards; CDCA7L; -.
DR HGNC; HGNC:30777; CDCA7L.
DR HPA; ENSG00000164649; Tissue enhanced (bone).
DR MalaCards; CDCA7L; -.
DR MIM; 609685; gene.
DR neXtProt; NX_Q96GN5; -.
DR OpenTargets; ENSG00000164649; -.
DR PharmGKB; PA142672139; -.
DR VEuPathDB; HostDB:ENSG00000164649; -.
DR eggNOG; ENOG502QWH1; Eukaryota.
DR GeneTree; ENSGT00940000159108; -.
DR HOGENOM; CLU_035988_0_0_1; -.
DR InParanoid; Q96GN5; -.
DR OMA; KAPCFKS; -.
DR PhylomeDB; Q96GN5; -.
DR TreeFam; TF101076; -.
DR PathwayCommons; Q96GN5; -.
DR SignaLink; Q96GN5; -.
DR SIGNOR; Q96GN5; -.
DR BioGRID-ORCS; 55536; 10 hits in 1083 CRISPR screens.
DR ChiTaRS; CDCA7L; human.
DR GeneWiki; CDCA7L; -.
DR GenomeRNAi; 55536; -.
DR Pharos; Q96GN5; Tbio.
DR PRO; PR:Q96GN5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96GN5; protein.
DR Bgee; ENSG00000164649; Expressed in germinal epithelium of ovary and 171 other tissues.
DR ExpressionAtlas; Q96GN5; baseline and differential.
DR Genevisible; Q96GN5; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA: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 3D-structure; Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..454
FT /note="Cell division cycle-associated 7-like protein"
FT /id="PRO_0000249313"
FT REGION 103..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..235
FT /note="MYC-binding"
FT MOTIF 9..33
FT /note="Integrase domain-binding motif 1 (IBM1)"
FT /evidence="ECO:0000269|PubMed:29997176"
FT MOTIF 65..91
FT /note="Integrase domain-binding motif 2 (IBM2)"
FT /evidence="ECO:0000269|PubMed:29997176"
FT COMPBIAS 154..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29997176,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29997176,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29997176,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29997176"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29997176"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922M5"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922M5"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043806"
FT VAR_SEQ 55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_020398"
FT VAR_SEQ 56..101
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046270"
FT VARIANT 45
FT /note="D -> N (in dbSNP:rs937337760)"
FT /evidence="ECO:0000269|PubMed:29961568"
FT /id="VAR_083475"
FT VARIANT 187
FT /note="R -> S (in dbSNP:rs35281045)"
FT /id="VAR_050776"
FT MUTAGEN 16
FT /note="I->A: Significant loss of interaction with PSIP1;
FT when associated with A-17. Complete loss of interaction
FT with PSIP1; when associated with A-17, A-72 and A-73."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 17
FT /note="F->A: Significant loss of interaction with PSIP1;
FT when associated with A-16. Complete loss of interaction
FT with PSIP1; when associated with A-16, A-72 and A-73."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 21
FT /note="S->D: Phosphomimetic mutant. Increased interaction
FT with PSIP1; when associated with D-77, D-79 and D-81."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 72
FT /note="I->A: Significant loss of interaction with PSIP1;
FT when associated with A-73. Complete loss of interaction
FT with PSIP1; when associated with A-16, A-17 and A-73."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 73
FT /note="F->A: Significant loss of interaction with PSIP1;
FT when associated with A-72. Complete loss of interaction
FT with PSIP1; when associated with A-16, A-17 and A-72."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 77
FT /note="T->D: Phosphomimetic mutant. Increased interaction
FT with PSIP1; when associated with D-21, D-79 and D-81."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 79
FT /note="S->D: Phosphomimetic mutant. Increased interaction
FT with PSIP1; when associated with D-21, D-77 and D-81."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 81
FT /note="T->D: Phosphomimetic mutant. Increased interaction
FT with PSIP1; when associated with D-21, D-77 and D-79."
FT /evidence="ECO:0000269|PubMed:29997176"
FT CONFLICT 46
FT /note="S -> G (in Ref. 4; BAG62445)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="V -> A (in Ref. 9; CAB94887)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="Y -> C (in Ref. 8; AAH32576)"
FT /evidence="ECO:0000305"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:6EMO"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:5YI9"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:5YI9"
SQ SEQUENCE 454 AA; 52206 MW; 1FAFEC7DBD763C85 CRC64;
MELATRYQIP KEVADIFNAP SDDEEFVGFR DDVPMETLSS EESCDSFDSL ESGKQQDVRF
HSKYFTEELR RIFIEDTDSE TEDFAGFTQS DLNGKTNPEV MVVESDLSDD GKASLVSEEE
EDEEEDKATP RRSRSRRSSI GLRVAFQFPT KKLANKPDKN SSSEQLFSSA RLQNEKKTIL
ERKKDCRQVI QREDSTSESE DDSRDESQES SDALLKRTMN IKENKAMLAQ LLAELNSMPD
FFPVRTPTSA SRKKTVRRAF SEGQITRRMN PTRSARPPEK FALENFTVSA AKFAEEFYSF
RRRKTIGGKC REYRRRHRIS SFRPVEDITE EDLENVAITV RDKIYDKVLG NTCHQCRQKT
IDTKTVCRNQ GCCGVRGQFC GPCLRNRYGE DVRSALLDPD WVCPPCRGIC NCSYCRKRDG
RCATGILIHL AKFYGYDNVK EYLESLQKEL VEDN
