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Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain)

 CCAR1_HUMAN             Reviewed;        1150 AA.
Q8IX12; A0JLT7; A1L4P7; A8K9D4; B4DNP8; B4DRK8; Q32NE3; Q5EBM3; Q5VUP6;
Q6PIZ0; Q6X935; Q9H8N4; Q9NVA7; Q9NVQ0; Q9NWM6;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 2.
12-AUG-2020, entry version 152.
RecName: Full=Cell division cycle and apoptosis regulator protein 1;
AltName: Full=Cell cycle and apoptosis regulatory protein 1;
Short=CARP-1;
AltName: Full=Death inducer with SAP domain;
Name=CCAR1; Synonyms=CARP1, DIS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=12816952; DOI=10.1074/jbc.m303173200;
Rishi A.K., Zhang L., Boyanapalli M., Wali A., Mohammad R.M., Yu Y.,
Fontana J.A., Hatfield J.S., Dawson M.I., Majumdar A.P.N., Reichert U.;
"Identification and characterization of a cell cycle and apoptosis
regulatory protein-1 as a novel mediator of apoptosis signaling by retinoid
CD437.";
J. Biol. Chem. 278:33422-33435(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tian Y., Li D., Benjamin T.;
"TAZ binding partners identified by mass spectrometry.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 1-1058 (ISOFORM 2).
TISSUE=Hepatoma, Lung, Placenta, Teratocarcinoma, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-818 (ISOFORM 1).
TISSUE=Cerebellum, Lung, Lymph, Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[8]
INTERACTION WITH CALCOCO1.
PubMed=18722177; DOI=10.1016/j.molcel.2008.08.001;
Kim J.H., Yang C.K., Heo K., Roeder R.G., An W., Stallcup M.R.;
"CCAR1, a key regulator of mediator complex recruitment to nuclear receptor
transcription complexes.";
Mol. Cell 31:510-519(2008).
[9]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-637, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=18655026; DOI=10.1002/pmic.200700887;
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J.,
Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell
line Chang liver cells.";
Proteomics 8:2885-2896(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685; SER-697 AND THR-861, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-861, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND THR-627, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
FUNCTION, AND INTERACTION WITH AR AND GATA2.
PubMed=23887938; DOI=10.1093/nar/gkt644;
Seo W.Y., Jeong B.C., Yu E.J., Kim H.J., Kim S.H., Lim J.E., Kwon G.Y.,
Lee H.M., Kim J.H.;
"CCAR1 promotes chromatin loading of androgen receptor (AR) transcription
complex by stabilizing the association between AR and GATA2.";
Nucleic Acids Res. 41:8526-8536(2013).
[15]
FUNCTION, AND INTERACTION WITH GATA1.
PubMed=24245781; DOI=10.1111/gtc.12104;
Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R.,
Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.;
"CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel
pathway for GATA1 function.";
Genes Cells 19:28-51(2014).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012 AND LYS-1135, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012 AND LYS-1067, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012; LYS-1067 AND LYS-1135, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.o114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to replication
stress reveals novel small ubiquitin-like modified target proteins and
acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[21]
REVIEW.
PubMed=25894788; DOI=10.18632/oncotarget.3376;
Muthu M., Cheriyan V.T., Rishi A.K.;
"CARP-1/CCAR1: A biphasic regulator of cancer cell growth and apoptosis.";
Oncotarget 6:6499-6510(2015).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1012 AND LYS-1067, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
VARIANT [LARGE SCALE ANALYSIS] LYS-607.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Associates with components of the Mediator and p160
coactivator complexes that play a role as intermediaries transducing
regulatory signals from upstream transcriptional activator proteins to
basal transcription machinery at the core promoter. Recruited to
endogenous nuclear receptor target genes in response to the appropriate
hormone. Also functions as a p53 coactivator. May thus play an
important role in transcriptional regulation (By similarity). May be
involved in apoptosis signaling in the presence of the reinoid CD437.
Apoptosis induction involves sequestration of 14-3-3 protein(s) and
mediated altered expression of multiple cell cycle regulatory genes
including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression
and/or cell proliferation (PubMed:12816952). In association with
CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation
from the gamma-globin promoter during erythroid differentiation of K562
erythroleukemia cells (PubMed:24245781). Can act as a both a
coactivator and corepressor of AR-mediated transcription. Contributes
to chromatin looping and AR transcription complex assembly by
stabilizing AR-GATA2 association on chromatin and facilitating MED1 and
RNA polymerase II recruitment to AR-binding sites. May play an
important role in the growth and tumorigenesis of prostate cancer cells
(PubMed:23887938). {ECO:0000250|UniProtKB:Q8CH18,
ECO:0000269|PubMed:12816952, ECO:0000269|PubMed:23887938,
ECO:0000269|PubMed:24245781}.
-!- SUBUNIT: Directly interacts with ESR1, NR3C1 and p53/TP53 (By
similarity). Interacts (via N-terminus) with CALCOCO1. Interacts with
MED1 (By similarity). Interacts with GATA1. Interacts with AR and
GATA2. {ECO:0000250|UniProtKB:Q8CH18, ECO:0000269|PubMed:18722177,
ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}.
-!- INTERACTION:
Q8IX12; Q08379: GOLGA2; NbExp=6; IntAct=EBI-356265, EBI-618309;
Q8IX12; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-356265, EBI-11522433;
Q8IX12; Q9NQM4: PIH1D3; NbExp=3; IntAct=EBI-356265, EBI-10239299;
Q8IX12; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-356265, EBI-5661333;
Q8IX12; Q9GZV5: WWTR1; NbExp=2; IntAct=EBI-356265, EBI-747743;
Q8IX12; Q9EPK5: Wwtr1; Xeno; NbExp=5; IntAct=EBI-356265, EBI-1211920;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:12816952}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IX12-1; Sequence=Displayed;
Name=2;
IsoId=Q8IX12-2; Sequence=VSP_037736;
-!- TISSUE SPECIFICITY: Expressed in various epithelial cancer cell lines,
including breast, colon, prostate, pancreatic and leukemia. Expression
is regulated by growth factors. {ECO:0000269|PubMed:12816952}.
-!- SEQUENCE CAUTION:
Sequence=AAH26036.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAI08683.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA91354.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY249140; AAP82002.1; -; mRNA.
EMBL; AF465616; AAO17319.1; -; mRNA.
EMBL; AK000741; BAA91354.1; ALT_INIT; mRNA.
EMBL; AK001452; BAA91700.1; -; mRNA.
EMBL; AK001701; BAA91847.1; -; mRNA.
EMBL; AK023438; BAB14574.1; -; mRNA.
EMBL; AK298004; BAG60310.1; -; mRNA.
EMBL; AK299307; BAG61320.1; -; mRNA.
EMBL; AK292649; BAF85338.1; -; mRNA.
EMBL; AL513534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL391539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54302.1; -; Genomic_DNA.
EMBL; BC015475; AAH15475.1; -; mRNA.
EMBL; BC026036; AAH26036.1; ALT_SEQ; mRNA.
EMBL; BC089420; AAH89420.1; -; mRNA.
EMBL; BC130626; AAI30627.1; -; mRNA.
EMBL; BC132725; AAI32726.1; -; mRNA.
EMBL; BC108682; AAI08683.1; ALT_SEQ; mRNA.
CCDS; CCDS60547.1; -. [Q8IX12-2]
CCDS; CCDS7282.1; -. [Q8IX12-1]
RefSeq; NP_001269888.1; NM_001282959.1. [Q8IX12-2]
RefSeq; NP_001269889.1; NM_001282960.1. [Q8IX12-2]
RefSeq; NP_060707.2; NM_018237.3. [Q8IX12-1]
SMR; Q8IX12; -.
BioGRID; 120867; 75.
CORUM; Q8IX12; -.
DIP; DIP-27607N; -.
IntAct; Q8IX12; 49.
MINT; Q8IX12; -.
STRING; 9606.ENSP00000265872; -.
GlyGen; Q8IX12; 5 sites, 1 O-linked glycan (5 sites).
iPTMnet; Q8IX12; -.
MetOSite; Q8IX12; -.
PhosphoSitePlus; Q8IX12; -.
BioMuta; CCAR1; -.
DMDM; 94707499; -.
EPD; Q8IX12; -.
jPOST; Q8IX12; -.
MassIVE; Q8IX12; -.
MaxQB; Q8IX12; -.
PaxDb; Q8IX12; -.
PeptideAtlas; Q8IX12; -.
PRIDE; Q8IX12; -.
ProteomicsDB; 70961; -. [Q8IX12-1]
ProteomicsDB; 70962; -. [Q8IX12-2]
Antibodypedia; 2118; 192 antibodies.
Ensembl; ENST00000265872; ENSP00000265872; ENSG00000060339. [Q8IX12-1]
Ensembl; ENST00000543719; ENSP00000445254; ENSG00000060339. [Q8IX12-2]
GeneID; 55749; -.
KEGG; hsa:55749; -.
UCSC; uc001joo.5; human. [Q8IX12-1]
CTD; 55749; -.
DisGeNET; 55749; -.
EuPathDB; HostDB:ENSG00000060339.13; -.
GeneCards; CCAR1; -.
HGNC; HGNC:24236; CCAR1.
HPA; ENSG00000060339; Low tissue specificity.
MIM; 612569; gene.
neXtProt; NX_Q8IX12; -.
OpenTargets; ENSG00000060339; -.
PharmGKB; PA134920227; -.
eggNOG; KOG4246; Eukaryota.
GeneTree; ENSGT00530000063672; -.
InParanoid; Q8IX12; -.
OMA; LRYSDMH; -.
OrthoDB; 614048at2759; -.
PhylomeDB; Q8IX12; -.
TreeFam; TF316387; -.
PathwayCommons; Q8IX12; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
BioGRID-ORCS; 55749; 471 hits in 875 CRISPR screens.
ChiTaRS; CCAR1; human.
GeneWiki; CCAR1; -.
GenomeRNAi; 55749; -.
Pharos; Q8IX12; Tbio.
PRO; PR:Q8IX12; -.
Proteomes; UP000005640; Chromosome 10.
RNAct; Q8IX12; protein.
Bgee; ENSG00000060339; Expressed in testis and 216 other tissues.
ExpressionAtlas; Q8IX12; baseline and differential.
Genevisible; Q8IX12; HS.
GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030374; F:nuclear receptor transcription coactivator activity; IGI:MGI.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
Gene3D; 1.10.720.30; -; 1.
InterPro; IPR025224; CCAR1/CCAR2.
InterPro; IPR025954; DBC1/CARP1_inactive_NUDIX_dom.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR025223; S1-like_RNA-bd_dom.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
PANTHER; PTHR14304; PTHR14304; 1.
Pfam; PF14443; DBC1; 1.
Pfam; PF14444; S1-like; 1.
Pfam; PF02037; SAP; 1.
SMART; SM01122; DBC1; 1.
SMART; SM00513; SAP; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF68906; SSF68906; 1.
PROSITE; PS50800; SAP; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Apoptosis; Cell cycle; Coiled coil;
Cytoplasm; Isopeptide bond; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1..1150
/note="Cell division cycle and apoptosis regulator protein
1"
/id="PRO_0000233148"
DOMAIN 636..670
/note="SAP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
REGION 1..249
/note="Interaction with AR"
/evidence="ECO:0000269|PubMed:23887938"
REGION 203..660
/note="Interaction with GATA2"
/evidence="ECO:0000269|PubMed:23887938"
REGION 643..1150
/note="Interaction with GATA1"
/evidence="ECO:0000269|PubMed:24245781"
COILED 594..618
/evidence="ECO:0000255"
COILED 1033..1114
/evidence="ECO:0000255"
COMPBIAS 73..79
/note="Poly-Ala"
COMPBIAS 293..361
/note="Arg-rich"
COMPBIAS 673..889
/note="Glu-rich"
MOD_RES 456
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 627
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 667
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 685
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231"
MOD_RES 697
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231"
MOD_RES 861
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692"
CROSSLNK 637
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:18655026"
CROSSLNK 1012
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1); alternate"
/evidence="ECO:0000244|PubMed:25114211"
CROSSLNK 1012
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364, ECO:0000244|PubMed:28112733"
CROSSLNK 1067
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733"
CROSSLNK 1135
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297"
VAR_SEQ 83..97
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_037736"
VARIANT 588
/note="T -> I (in dbSNP:rs1782338)"
/id="VAR_058330"
VARIANT 607
/note="E -> K (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_035497"
VARIANT 681
/note="E -> G (in dbSNP:rs1060145)"
/id="VAR_058331"
VARIANT 747
/note="M -> V (in dbSNP:rs11542602)"
/id="VAR_058332"
CONFLICT 296
/note="D -> Y (in Ref. 3; BAA91354)"
/evidence="ECO:0000305"
CONFLICT 305
/note="N -> S (in Ref. 3; BAG60310)"
/evidence="ECO:0000305"
CONFLICT 492
/note="K -> E (in Ref. 3; BAA91847)"
/evidence="ECO:0000305"
CONFLICT 618
/note="D -> Y (in Ref. 6; AAH15475)"
/evidence="ECO:0000305"
CONFLICT 650
/note="S -> G (in Ref. 2; AAO17319 and 3; BAA91700)"
/evidence="ECO:0000305"
CONFLICT 723
/note="L -> S (in Ref. 3; BAF85338)"
/evidence="ECO:0000305"
CONFLICT 801..803
/note="EKD -> KKK (in Ref. 6; AAH89420)"
/evidence="ECO:0000305"
CONFLICT 816..818
/note="EER -> KKK (in Ref. 6; AAH15475)"
/evidence="ECO:0000305"
CONFLICT 853
/note="D -> G (in Ref. 1, 2 and 3; BAA91700)"
/evidence="ECO:0000305"
CONFLICT 1104
/note="N -> S (in Ref. 1, 2 and 3; BAA91700)"
/evidence="ECO:0000305"
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


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Pathways :
WP414: Cell Cycle and Cell Division
WP1195: G1 to S cell cycle control
WP844: Cell cycle
WP1775: Cell Cycle Checkpoints
WP31: Cell cycle
WP1078: G1 to S cell cycle control
WP179: Cell cycle
WP348: G1 to S cell cycle control
WP1689: Porphyrin and chlorophyll metabolism
WP2414: Quercetin and Nf-kB/ AP-1 induced cell apoptosis
WP2152: BDNF
WP413: G1 to S cell cycle control
WP1200: Cell cycle
WP2272: Pathogenic Escherichia coli infection
WP429: Cell cycle
WP45: G1 to S cell cycle control
WP1900: Regulation of mitotic cell cycle
WP2328: Allograft rejection
WP959: G1 to S cell cycle control
WP1083: Cell cycle
WP840: G1 to S cell cycle control
WP2435: Quercetin and Nf-kB/ AP-1 induced cell apoptosis
WP445: G1 to S cell cycle control
WP1566: Citrate cycle (TCA cycle)
WP1782: APC/C-mediated degradation of cell cycle proteins

Related Genes :
[CCAR1 CARP1 DIS] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain)
[Ccar1 Carp1] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1)
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[Aifm1 Aif Pdcd8] Apoptosis-inducing factor 1, mitochondrial (EC 1.6.99.-) (Programmed cell death protein 8)
[AIFM1 AIF PDCD8] Apoptosis-inducing factor 1, mitochondrial (EC 1.6.99.-) (Programmed cell death protein 8)
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[CDCA7 JPO1] Cell division cycle-associated protein 7 (Protein JPO1)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
[Aifm1 Aif Pdcd8] Apoptosis-inducing factor 1, mitochondrial (EC 1.6.99.-) (Programmed cell death protein 8)
[CDK11A CDC2L2 CDC2L3 PITSLREB] Cyclin-dependent kinase 11A (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 2) (Cell division protein kinase 11A) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L2)
[AIFM2 AMID PRG3] Ferroptosis suppressor protein 1 (FSP1) (EC 1.6.5.-) (Apoptosis-inducing factor homologous mitochondrion-associated inducer of death) (AMID) (p53-responsive gene 3 protein)
[ced-9 T07C4.8] Apoptosis regulator ced-9 (Cell death protein 9)
[cdc-48.1 C06A1.1] Transitional endoplasmic reticulum ATPase homolog 1 (EC 3.6.4.6) (Cell division cycle-related protein 48.1) (p97/CDC48 homolog 1)
[SEPTIN4 ARTS PNUTL2 SEP4 SEPT4 hucep-7] Septin-4 (Apoptosis-related protein in the TGF-beta signaling pathway) (ARTS) (Bradeion beta) (Brain protein H5) (CE5B3 beta) (Cell division control-related protein 2) (hCDCREL-2) (Cerebral protein 7) (Peanut-like protein 2)
[RCC1 CHC1] Regulator of chromosome condensation (Cell cycle regulatory protein) (Chromosome condensation protein 1)
[CDC43 CAL1 YGL155W G1864] Geranylgeranyl transferase type-1 subunit beta (GGTase-I-beta) (EC 2.5.1.59) (Cell division cycle protein 43) (Geranylgeranyl transferase type I subunit beta) (RAS proteins geranylgeranyltransferase subunit beta) (Type I protein geranyl-geranyltransferase subunit beta) (PGGTase I beta)
[Pdcd6 Alg2] Programmed cell death protein 6 (Apoptosis-linked gene 2 protein homolog) (ALG-2)
[tax] Protein Tax-1 (Protein X-LOR) (Protein PX) (Trans-activating transcriptional regulatory protein of HTLV-1)
[TRIAP1 15E1.1 HSPC132] TP53-regulated inhibitor of apoptosis 1 (Protein 15E1.1) (WF-1) (p53-inducible cell-survival factor) (p53CSV)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[BIRC2 API1 MIHB RNF48] Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (IAP homolog B) (Inhibitor of apoptosis protein 2) (hIAP-2) (hIAP2) (RING finger protein 48) (RING-type E3 ubiquitin transferase BIRC2) (TNFR2-TRAF-signaling complex protein 2)
[AIFM2] Ferroptosis suppressor protein 1 (FSP1) (EC 1.6.5.-) (Apoptosis-inducing factor homologous mitochondrion-associated inducer of death) (AMID) (p53-responsive gene 3 protein)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[RIPK1 RIP RIP1] Receptor-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (Cell death protein RIP) (Receptor-interacting protein 1) (RIP-1)
[BIK NBK] Bcl-2-interacting killer (Apoptosis inducer NBK) (BIP1) (BP4)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Pdcd6 Alg2] Programmed cell death protein 6 (ALG-257) (Apoptosis-linked gene 2 protein) (ALG-2) (PMP41)

Bibliography :