ID CCAR1_HUMAN Reviewed; 1150 AA. AC Q8IX12; A0JLT7; A1L4P7; A8K9D4; B4DNP8; B4DRK8; Q32NE3; Q5EBM3; Q5VUP6; AC Q6PIZ0; Q6X935; Q9H8N4; Q9NVA7; Q9NVQ0; Q9NWM6; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 04-NOV-2026, entry version 181. DE RecName: Full=Cell division cycle and apoptosis regulator protein 1; DE AltName: Full=Cell cycle and apoptosis regulatory protein 1; DE Short=CARP-1; DE AltName: Full=Death inducer with SAP domain; GN Name=CCAR1; Synonyms=CARP1, DIS; 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), FUNCTION, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RX PubMed=12816952; DOI=10.1074/jbc.m303173200; RA Rishi A.K., Zhang L., Boyanapalli M., Wali A., Mohammad R.M., Yu Y., RA Fontana J.A., Hatfield J.S., Dawson M.I., Majumdar A.P.N., Reichert U.; RT "Identification and characterization of a cell cycle and apoptosis RT regulatory protein-1 as a novel mediator of apoptosis signaling by retinoid RT CD437."; RL J. Biol. Chem. 278:33422-33435(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Tian Y., Li D., Benjamin T.; RT "TAZ binding partners identified by mass spectrometry."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-1058 (ISOFORM 2). RC TISSUE=Hepatoma, Lung, Placenta, Teratocarcinoma, and Thymus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-818 (ISOFORM 1). RC TISSUE=Cerebellum, Lung, Lymph, Muscle, and Skin; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [8] RP INTERACTION WITH CALCOCO1. RX PubMed=18722177; DOI=10.1016/j.molcel.2008.08.001; RA Kim J.H., Yang C.K., Heo K., Roeder R.G., An W., Stallcup M.R.; RT "CCAR1, a key regulator of mediator complex recruitment to nuclear receptor RT transcription complexes."; RL Mol. Cell 31:510-519(2008). RN [9] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-637, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Liver; RX PubMed=18655026; DOI=10.1002/pmic.200700887; RA Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., RA Luo Y., Qiang B., Yuan J., Sun X., Peng X.; RT "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell RT line Chang liver cells."; RL Proteomics 8:2885-2896(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685; SER-697 AND THR-861, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-861, AND IDENTIFICATION BY RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND THR-627, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 [14] RP FUNCTION, AND INTERACTION WITH AR AND GATA2. RX PubMed=23887938; DOI=10.1093/nar/gkt644; RA Seo W.Y., Jeong B.C., Yu E.J., Kim H.J., Kim S.H., Lim J.E., Kwon G.Y., RA Lee H.M., Kim J.H.; RT "CCAR1 promotes chromatin loading of androgen receptor (AR) transcription RT complex by stabilizing the association between AR and GATA2."; RL Nucleic Acids Res. 41:8526-8536(2013). RN [15] RP FUNCTION, AND INTERACTION WITH GATA1. RX PubMed=24245781; DOI=10.1111/gtc.12104; RA Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R., RA Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.; RT "CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel RT pathway for GATA1 function."; RL Genes Cells 19:28-51(2014). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012 AND LYS-1135, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012 AND LYS-1067, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012; LYS-1067 AND LYS-1135, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [21] RP REVIEW. RX PubMed=25894788; DOI=10.18632/oncotarget.3376; RA Muthu M., Cheriyan V.T., Rishi A.K.; RT "CARP-1/CCAR1: A biphasic regulator of cancer cell growth and apoptosis."; RL Oncotarget 6:6499-6510(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012 AND LYS-1067, 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 [23] RP VARIANT [LARGE SCALE ANALYSIS] LYS-607. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Associates with components of the Mediator and p160 CC coactivator complexes that play a role as intermediaries transducing CC regulatory signals from upstream transcriptional activator proteins to CC basal transcription machinery at the core promoter. Recruited to CC endogenous nuclear receptor target genes in response to the appropriate CC hormone. Also functions as a p53 coactivator. May thus play an CC important role in transcriptional regulation (By similarity). May be CC involved in apoptosis signaling in the presence of the reinoid CD437. CC Apoptosis induction involves sequestration of 14-3-3 protein(s) and CC mediated altered expression of multiple cell cycle regulatory genes CC including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression CC and/or cell proliferation (PubMed:12816952). In association with CC CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation CC from the gamma-globin promoter during erythroid differentiation of K562 CC erythroleukemia cells (PubMed:24245781). Can act as a both a CC coactivator and corepressor of AR-mediated transcription. Contributes CC to chromatin looping and AR transcription complex assembly by CC stabilizing AR-GATA2 association on chromatin and facilitating MED1 and CC RNA polymerase II recruitment to AR-binding sites. May play an CC important role in the growth and tumorigenesis of prostate cancer cells CC (PubMed:23887938). {ECO:0000250|UniProtKB:Q8CH18, CC ECO:0000269|PubMed:12816952, ECO:0000269|PubMed:23887938, CC ECO:0000269|PubMed:24245781}. CC -!- SUBUNIT: Directly interacts with ESR1, NR3C1 and p53/TP53 (By CC similarity). Interacts (via N-terminus) with CALCOCO1. Interacts with CC MED1 (By similarity). Interacts with GATA1. Interacts with AR and CC GATA2. {ECO:0000250|UniProtKB:Q8CH18, ECO:0000269|PubMed:18722177, CC ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}. CC -!- INTERACTION: CC Q8IX12; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-356265, EBI-10239299; CC Q8IX12; Q08379: GOLGA2; NbExp=6; IntAct=EBI-356265, EBI-618309; CC Q8IX12; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-356265, EBI-11522433; CC Q8IX12; P98175: RBM10; NbExp=2; IntAct=EBI-356265, EBI-721525; CC Q8IX12; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-356265, EBI-5661333; CC Q8IX12; P26368: U2AF2; NbExp=3; IntAct=EBI-356265, EBI-742339; CC Q8IX12; Q9GZV5: WWTR1; NbExp=2; IntAct=EBI-356265, EBI-747743; CC Q8IX12; Q9EPK5: Wwtr1; Xeno; NbExp=5; IntAct=EBI-356265, EBI-1211920; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:12816952}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8IX12-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IX12-2; Sequence=VSP_037736; CC -!- TISSUE SPECIFICITY: Expressed in various epithelial cancer cell lines, CC including breast, colon, prostate, pancreatic and leukemia. Expression CC is regulated by growth factors. {ECO:0000269|PubMed:12816952}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH26036.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAI08683.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA91354.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AY249140; AAP82002.1; -; mRNA. DR EMBL; AF465616; AAO17319.1; -; mRNA. DR EMBL; AK000741; BAA91354.1; ALT_INIT; mRNA. DR EMBL; AK001452; BAA91700.1; -; mRNA. DR EMBL; AK001701; BAA91847.1; -; mRNA. DR EMBL; AK023438; BAB14574.1; -; mRNA. DR EMBL; AK298004; BAG60310.1; -; mRNA. DR EMBL; AK299307; BAG61320.1; -; mRNA. DR EMBL; AK292649; BAF85338.1; -; mRNA. DR EMBL; AL513534; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391539; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471083; EAW54302.1; -; Genomic_DNA. DR EMBL; BC015475; AAH15475.1; -; mRNA. DR EMBL; BC026036; AAH26036.1; ALT_SEQ; mRNA. DR EMBL; BC089420; AAH89420.1; -; mRNA. DR EMBL; BC130626; AAI30627.1; -; mRNA. DR EMBL; BC132725; AAI32726.1; -; mRNA. DR EMBL; BC108682; AAI08683.1; ALT_SEQ; mRNA. DR CCDS; CCDS60547.1; -. [Q8IX12-2] DR CCDS; CCDS7282.1; -. [Q8IX12-1] DR RefSeq; NP_001269888.1; NM_001282959.2. [Q8IX12-2] DR RefSeq; NP_001269889.1; NM_001282960.2. [Q8IX12-2] DR RefSeq; NP_060707.2; NM_018237.4. [Q8IX12-1] DR AlphaFoldDB; Q8IX12; -. DR SMR; Q8IX12; -. DR BioGRID; 120867; 225. DR CORUM; Q8IX12; -. DR DIP; DIP-27607N; -. DR FunCoup; Q8IX12; 4535. DR IntAct; Q8IX12; 114. DR NDEx; MUSIC2-C5189-CCAR1; Osteosarcoma (U2OS) cell map - Pre-mRNA splicing and ribonucleoprotein assembly (49 proteins). DR STRING; 9606.ENSP00000265872; -. DR GlyCosmos; Q8IX12; 32 sites, 3 glycans. DR GlyGen; Q8IX12; 32 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (31 sites). DR iPTMnet; Q8IX12; -. DR MetOSite; Q8IX12; -. DR PhosphoSitePlus; Q8IX12; -. DR SwissPalm; Q8IX12; -. DR BioMuta; CCAR1; -. DR DMDM; 94707499; -. DR jPOST; Q8IX12; -. DR MassIVE; Q8IX12; -. DR PaxDb; 9606-ENSP00000265872; -. DR PeptideAtlas; Q8IX12; -. DR ProteomicsDB; 70961; -. [Q8IX12-1] DR ProteomicsDB; 70962; -. [Q8IX12-2] DR Pumba; Q8IX12; -. DR Antibodypedia; 2118; 237 antibodies from 33 providers. DR DNASU; 55749; -. DR Ensembl; ENST00000265872.11; ENSP00000265872.6; ENSG00000060339.15. [Q8IX12-1] DR Ensembl; ENST00000543719.5; ENSP00000445254.1; ENSG00000060339.15. [Q8IX12-2] DR Ensembl; ENST00000859847.1; ENSP00000529906.1; ENSG00000060339.15. [Q8IX12-1] DR Ensembl; ENST00000928525.1; ENSP00000598584.1; ENSG00000060339.15. [Q8IX12-1] DR Ensembl; ENST00000928526.1; ENSP00000598585.1; ENSG00000060339.15. [Q8IX12-2] DR Ensembl; ENST00000928528.1; ENSP00000598587.1; ENSG00000060339.15. [Q8IX12-1] DR Ensembl; ENST00000928530.1; ENSP00000598589.1; ENSG00000060339.15. [Q8IX12-1] DR Ensembl; ENST00000928531.1; ENSP00000598590.1; ENSG00000060339.15. [Q8IX12-2] DR Ensembl; ENST00000928534.1; ENSP00000598593.1; ENSG00000060339.15. [Q8IX12-1] DR Ensembl; ENST00000928535.1; ENSP00000598594.1; ENSG00000060339.15. [Q8IX12-1] DR Ensembl; ENST00000928536.1; ENSP00000598595.1; ENSG00000060339.15. [Q8IX12-1] DR Ensembl; ENST00000928537.1; ENSP00000598596.1; ENSG00000060339.15. [Q8IX12-1] DR GeneID; 55749; -. DR KEGG; hsa:55749; -. DR MANE-Select; ENST00000265872.11; ENSP00000265872.6; NM_018237.4; NP_060707.2. DR UCSC; uc001joo.5; human. [Q8IX12-1] DR AGR; HGNC:24236; -. DR ClinPGx; PA134920227; -. DR CTD; 55749; -. DR DisGeNET; 55749; -. DR GeneCards; CCAR1; -. DR HGNC; HGNC:24236; CCAR1. DR HPA; ENSG00000060339; Low tissue specificity. DR MIM; 612569; gene. DR OpenTargets; ENSG00000060339; -. DR VEuPathDB; HostDB:ENSG00000060339; -. DR eggNOG; KOG4246; Eukaryota. DR GeneTree; ENSGT00530000063672; -. DR InParanoid; Q8IX12; -. DR OMA; AAAVASX; -. DR OrthoDB; 21006at2759; -. DR PAN-GO; Q8IX12; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q8IX12; -. DR PathwayCommons; Q8IX12; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-9770562; mRNA Polyadenylation. DR Reactome; R-HSA-9918481; Dengue Virus-Host Interactions. DR SignaLink; Q8IX12; -. DR Agora; ENSG00000060339; -. DR BioGRID-ORCS; 55749; 536 hits in 1164 CRISPR screens. DR CD-CODE; B5B9A610; PML body. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; CCAR1; human. DR GeneWiki; CCAR1; -. DR GenomeRNAi; 55749; -. DR Pharos; Q8IX12; Tbio. DR PRO; PR:Q8IX12; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q8IX12; protein. DR Bgee; ENSG00000060339; Expressed in sperm and 187 other cell types or tissues. DR ExpressionAtlas; Q8IX12; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB. DR FunFam; 2.40.50.140:FF:000216; Cell division cycle and apoptosis regulator 1; 1. DR FunFam; 1.10.720.30:FF:000006; Cell division cycle and apoptosis regulator protein 1; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 1.10.720.30; SAP domain; 1. DR InterPro; IPR025224; CCAR1/CCAR2. DR InterPro; IPR025954; DBC1/CARP1_inactive_NUDIX. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR045353; LAIKA. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR025223; S1-like_RNA-bd_dom. DR InterPro; IPR003034; SAP_dom. DR InterPro; IPR036361; SAP_dom_sf. DR PANTHER; PTHR14304; CELL DIVISION CYCLE AND APOPTOSIS REGULATOR PROTEIN; 1. DR PANTHER; PTHR14304:SF14; CELL DIVISION CYCLE AND APOPTOSIS REGULATOR PROTEIN 1; 1. DR Pfam; PF14443; DBC1; 1. DR Pfam; PF19256; LAIKA; 1. DR Pfam; PF14444; S1-like; 1. DR Pfam; PF02037; SAP; 1. DR SMART; SM01122; DBC1; 1. DR SMART; SM00513; SAP; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF68906; SAP domain; 1. DR PROSITE; PS50800; SAP; 1. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Apoptosis; Cell cycle; Coiled coil; KW Cytoplasm; Isopeptide bond; Phosphoprotein; Proteomics identification; KW Reference proteome; Repressor; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..1150 FT /note="Cell division cycle and apoptosis regulator protein FT 1" FT /id="PRO_0000233148" FT DOMAIN 636..670 FT /note="SAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186" FT REGION 1..249 FT /note="Interaction with AR" FT /evidence="ECO:0000269|PubMed:23887938" FT REGION 124..146 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 203..660 FT /note="Interaction with GATA2" FT /evidence="ECO:0000269|PubMed:23887938" FT REGION 285..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 600..638 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 643..1150 FT /note="Interaction with GATA1" FT /evidence="ECO:0000269|PubMed:24245781" FT REGION 673..713 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 796..915 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 594..618 FT /evidence="ECO:0000255" FT COILED 1033..1114 FT /evidence="ECO:0000255" FT COMPBIAS 134..146 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 293..334 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 341..352 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 610..621 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 673..687 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 694..713 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 796..817 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 832..855 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 856..889 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 890..915 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 456 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 627 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 667 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 685 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 697 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 861 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT CROSSLNK 637 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:18655026" FT CROSSLNK 1012 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 1012 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 1067 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 1135 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297" FT VAR_SEQ 83..97 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037736" FT VARIANT 588 FT /note="T -> I (in dbSNP:rs1782338)" FT /id="VAR_058330" FT VARIANT 607 FT /note="E -> K (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035497" FT VARIANT 681 FT /note="E -> G (in dbSNP:rs1060145)" FT /id="VAR_058331" FT VARIANT 747 FT /note="M -> V (in dbSNP:rs11542602)" FT /id="VAR_058332" FT CONFLICT 296 FT /note="D -> Y (in Ref. 3; BAA91354)" FT /evidence="ECO:0000305" FT CONFLICT 305 FT /note="N -> S (in Ref. 3; BAG60310)" FT /evidence="ECO:0000305" FT CONFLICT 492 FT /note="K -> E (in Ref. 3; BAA91847)" FT /evidence="ECO:0000305" FT CONFLICT 618 FT /note="D -> Y (in Ref. 6; AAH15475)" FT /evidence="ECO:0000305" FT CONFLICT 650 FT /note="S -> G (in Ref. 2; AAO17319 and 3; BAA91700)" FT /evidence="ECO:0000305" FT CONFLICT 723 FT /note="L -> S (in Ref. 3; BAF85338)" FT /evidence="ECO:0000305" FT CONFLICT 801..803 FT /note="EKD -> KKK (in Ref. 6; AAH89420)" FT /evidence="ECO:0000305" FT CONFLICT 816..818 FT /note="EER -> KKK (in Ref. 6; AAH15475)" FT /evidence="ECO:0000305" FT CONFLICT 853 FT /note="D -> G (in Ref. 1, 2 and 3; BAA91700)" FT /evidence="ECO:0000305" FT CONFLICT 1104 FT /note="N -> S (in Ref. 1, 2 and 3; BAA91700)" FT /evidence="ECO:0000305" SQ SEQUENCE 1150 AA; 132821 MW; 30618DCC8097F552 CRC64; MAQFGGQKNP PWATQFTATA VSQPAALGVQ QPSLLGASPT IYTQQTALAA AGLTTQTPAN YQLTQTAALQ QQAAAAAAAL QQQYSQPQQA LYSVQQQLQQ PQQTLLTQPA VALPTSLSLS TPQPTAQITV SYPTPRSSQQ QTQPQKQRVF TGVVTKLHDT FGFVDEDVFF QLSAVKGKTP QVGDRVLVEA TYNPNMPFKW NAQRIQTLPN QNQSQTQPLL KTPPAVLQPI APQTTFGVQT QPQPQSLLQA QISAASITPL LQTQPQPLLQ QPQQKAGLLQ PPVRIVSQPQ PARRLDPPSR FSGRNDRGDQ VPNRKDDRSR ERERERRRSR ERSPQRKRSR ERSPRRERER SPRRVRRVVP RYTVQFSKFS LDCPSCDMME LRRRYQNLYI PSDFFDAQFT WVDAFPLSRP FQLGNYCNFY VMHREVESLE KNMAILDPPD ADHLYSAKVM LMASPSMEDL YHKSCALAED PQELRDGFQH PARLVKFLVG MKGKDEAMAI GGHWSPSLDG PDPEKDPSVL IKTAIRCCKA LTGIDLSVCT QWYRFAEIRY HRPEETHKGR TVPAHVETVV LFFPDVWHCL PTRSEWETLS RGYKQQLVEK LQGERKEADG EQDEEEKDDG EAKEISTPTH WSKLDPKTMK VNDLRKELES RALSSKGLKS QLIARLTKQL KVEEQKEEQK ELEKSEKEED EDDDRKSEDD KEEEERKRQE EIERQRRERR YILPDEPAII VHPNWAAKSG KFDCSIMSLS VLLDYRLEDN KEHSFEVSLF AELFNEMLQR DFGVRIYKSL LSLPEKEDKK EKDKKSKKDE RKDKKEERDD ETDEPKPKRR KSGDDKDKKE DRDERKKEDK RKDDSKDDDE TEEDNNQDEY DPMEAEEAED EEDDRDEEEM TKRDDKRDIN RYCKERPSKD KEKEKTQMIT INRDLLMAFV YFDQSHCGYL LEKDLEEILY TLGLHLSRAQ VKKLLNKVVL RESCFYRKLT DTSKDEENHE ESESLQEDML GNRLLLPTPT VKQESKDVEE NVGLIVYNGA MVDVGSLLQK LEKSEKVRAE VEQKLQLLEE KTDEDEKTIL NLENSNKSLS GELREVKKDL SQLQENLKIS ENMNLQFENQ MNKTIRNLST VMDEIHTVLK KDNVKNEDKD QKSKENGASV //