CCAR1_HUMAN
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 03-AUG-2022, entry version 161.
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; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-356265, EBI-5661333;
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};
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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_001282959.1. [Q8IX12-2]
DR RefSeq; NP_001269889.1; NM_001282960.1. [Q8IX12-2]
DR RefSeq; NP_060707.2; NM_018237.3. [Q8IX12-1]
DR AlphaFoldDB; Q8IX12; -.
DR SMR; Q8IX12; -.
DR BioGRID; 120867; 116.
DR CORUM; Q8IX12; -.
DR DIP; DIP-27607N; -.
DR IntAct; Q8IX12; 61.
DR MINT; Q8IX12; -.
DR STRING; 9606.ENSP00000265872; -.
DR GlyGen; Q8IX12; 25 sites, 2 O-linked glycans (25 sites).
DR iPTMnet; Q8IX12; -.
DR MetOSite; Q8IX12; -.
DR PhosphoSitePlus; Q8IX12; -.
DR BioMuta; CCAR1; -.
DR DMDM; 94707499; -.
DR EPD; Q8IX12; -.
DR jPOST; Q8IX12; -.
DR MassIVE; Q8IX12; -.
DR MaxQB; Q8IX12; -.
DR PaxDb; Q8IX12; -.
DR PeptideAtlas; Q8IX12; -.
DR PRIDE; Q8IX12; -.
DR ProteomicsDB; 70961; -. [Q8IX12-1]
DR ProteomicsDB; 70962; -. [Q8IX12-2]
DR Antibodypedia; 2118; 218 antibodies from 31 providers.
DR DNASU; 55749; -.
DR Ensembl; ENST00000265872.11; ENSP00000265872.6; ENSG00000060339.14. [Q8IX12-1]
DR Ensembl; ENST00000543719.5; ENSP00000445254.1; ENSG00000060339.14. [Q8IX12-2]
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 CTD; 55749; -.
DR DisGeNET; 55749; -.
DR GeneCards; CCAR1; -.
DR HGNC; HGNC:24236; CCAR1.
DR HPA; ENSG00000060339; Low tissue specificity.
DR MIM; 612569; gene.
DR neXtProt; NX_Q8IX12; -.
DR OpenTargets; ENSG00000060339; -.
DR PharmGKB; PA134920227; -.
DR VEuPathDB; HostDB:ENSG00000060339; -.
DR eggNOG; KOG4246; Eukaryota.
DR GeneTree; ENSGT00530000063672; -.
DR InParanoid; Q8IX12; -.
DR OMA; LRYSDMH; -.
DR OrthoDB; 614048at2759; -.
DR PhylomeDB; Q8IX12; -.
DR TreeFam; TF316387; -.
DR PathwayCommons; Q8IX12; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q8IX12; -.
DR BioGRID-ORCS; 55749; 512 hits in 1084 CRISPR screens.
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 185 other tissues.
DR ExpressionAtlas; Q8IX12; baseline and differential.
DR Genevisible; Q8IX12; HS.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IGI:MGI.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR045354; BURAN.
DR InterPro; IPR025224; CCAR1/CCAR2.
DR InterPro; IPR025954; DBC1/CARP1_inactive_NUDIX_dom.
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; PTHR14304; 1.
DR Pfam; PF19257; BURAN; 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; SSF47473; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF68906; SSF68906; 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; Reference proteome; Repressor;
KW Transcription; Transcription regulation; 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 299..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..699
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..888
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..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
