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CAAP1_MOUSE
ID   CAAP1_MOUSE             Reviewed;         356 AA.
AC   Q8VDY9; Q3USG8;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Caspase activity and apoptosis inhibitor 1;
DE   AltName: Full=Conserved anti-apoptotic protein;
DE            Short=CAAP;
GN   Name=Caap1; Synonyms=Caap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-307, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Anti-apoptotic protein that modulates a caspase-10 dependent
CC       mitochondrial caspase-3/9 feedback amplification loop. {ECO:0000250}.
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DR   EMBL; AK140382; BAE24364.1; -; mRNA.
DR   EMBL; AL807252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020067; AAH20067.1; -; mRNA.
DR   CCDS; CCDS18358.1; -.
DR   RefSeq; NP_080644.2; NM_026368.2.
DR   AlphaFoldDB; Q8VDY9; -.
DR   BioGRID; 212430; 1.
DR   STRING; 10090.ENSMUSP00000030313; -.
DR   iPTMnet; Q8VDY9; -.
DR   PhosphoSitePlus; Q8VDY9; -.
DR   EPD; Q8VDY9; -.
DR   jPOST; Q8VDY9; -.
DR   MaxQB; Q8VDY9; -.
DR   PaxDb; Q8VDY9; -.
DR   PeptideAtlas; Q8VDY9; -.
DR   PRIDE; Q8VDY9; -.
DR   ProteomicsDB; 265483; -.
DR   Antibodypedia; 10518; 27 antibodies from 9 providers.
DR   DNASU; 67770; -.
DR   Ensembl; ENSMUST00000030313; ENSMUSP00000030313; ENSMUSG00000028578.
DR   GeneID; 67770; -.
DR   KEGG; mmu:67770; -.
DR   UCSC; uc008tsa.2; mouse.
DR   CTD; 79886; -.
DR   MGI; MGI:1915020; Caap1.
DR   VEuPathDB; HostDB:ENSMUSG00000028578; -.
DR   eggNOG; ENOG502RN9N; Eukaryota.
DR   GeneTree; ENSGT00390000017010; -.
DR   HOGENOM; CLU_078683_0_0_1; -.
DR   InParanoid; Q8VDY9; -.
DR   OMA; CQPSIQQ; -.
DR   OrthoDB; 1443498at2759; -.
DR   TreeFam; TF332850; -.
DR   BioGRID-ORCS; 67770; 5 hits in 72 CRISPR screens.
DR   PRO; PR:Q8VDY9; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8VDY9; protein.
DR   Bgee; ENSMUSG00000028578; Expressed in pharyngeal arch 2 and 236 other tissues.
DR   Genevisible; Q8VDY9; MM.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR038991; CAAP1.
DR   PANTHER; PTHR14740; PTHR14740; 1.
DR   Pfam; PF15335; CAAP1; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Coiled coil; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..356
FT                   /note="Caspase activity and apoptosis inhibitor 1"
FT                   /id="PRO_0000089718"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          276..306
FT                   /evidence="ECO:0000255"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8G2"
FT   MOD_RES         69
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8G2"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8G2"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   CROSSLNK        84
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8G2"
FT   CONFLICT        22
FT                   /note="S -> A (in Ref. 3; AAH20067)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="V -> G (in Ref. 3; AAH20067)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="A -> T (in Ref. 3; AAH20067)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="A -> P (in Ref. 3; AAH20067)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   356 AA;  37825 MW;  B545CADE48A36A25 CRC64;
     MTGKKSSREK RRKRSGQEAA ASLAAPDLVP VLSGSAGGCG SGGCCGVAGG GTSVAGGAER
     SERRKRRSTD SSSSVSGSLQ QETKYLLPSL EKELFLAEHS DLEEGGLDLN VSLKPVSFYI
     SDKKEMLQQC FCIIGEKKLQ KMLPDVLKNC SVEEIKKLCQ EQLELLSEKQ ILKILEGDNG
     LDSDMEEEAD DGCKVAPDLI SQQDTCVDST SSLRENKQPE VLESKQGKGE DSDVLSINAD
     AYDSDIEGPS IDEAAAAATA TPAATAVATA ASEVPENTVQ SEAGQIDDLE RDIEKSVNEI
     LGLAESSPKE PKVATLTVPP AEDVQPSAQQ LELLELEMRA RAIKALMKAG DIKKPV
 
 
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