GenomeNet

Database: UniProt
Entry: P46718
LinkDB: P46718
Original site: P46718 
ID   PDCD2_MOUSE             Reviewed;         343 AA.
AC   P46718; Q8BR06;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAY-2019, entry version 125.
DE   RecName: Full=Programmed cell death protein 2;
DE   AltName: Full=Zinc finger protein Rp-8;
GN   Name=Pdcd2; Synonyms=Rp8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Thymus;
RX   PubMed=7880439; DOI=10.1089/dna.1995.14.189;
RA   Vaux D.L., Haecker G.;
RT   "Cloning of mouse RP-8 cDNA and its expression during apoptosis of
RT   lymphoid and myeloid cells.";
RL   DNA Cell Biol. 14:189-193(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May be a DNA-binding protein with a regulatory function.
CC       May play an important role in cell death and/or in regulation of
CC       cell proliferation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during apoptosis of lymphoid and
CC       myeloid cells.
CC   -!- PTM: Ubiquitinated by PRKN, promoting proteasomal degradation.
CC       {ECO:0000250}.
DR   EMBL; U10903; AAA83433.1; -; mRNA.
DR   EMBL; AK045985; BAC32560.1; -; mRNA.
DR   CCDS; CCDS28413.1; -.
DR   PIR; I49067; I49067.
DR   RefSeq; NP_032825.2; NM_008799.2.
DR   SMR; P46718; -.
DR   IntAct; P46718; 1.
DR   STRING; 10090.ENSMUSP00000052523; -.
DR   PhosphoSitePlus; P46718; -.
DR   EPD; P46718; -.
DR   MaxQB; P46718; -.
DR   PaxDb; P46718; -.
DR   PeptideAtlas; P46718; -.
DR   PRIDE; P46718; -.
DR   DNASU; 18567; -.
DR   GeneID; 18567; -.
DR   KEGG; mmu:18567; -.
DR   UCSC; uc008aoq.1; mouse.
DR   CTD; 5134; -.
DR   MGI; MGI:104643; Pdcd2.
DR   eggNOG; KOG2061; Eukaryota.
DR   eggNOG; ENOG410XRI4; LUCA.
DR   HOGENOM; HOG000237274; -.
DR   InParanoid; P46718; -.
DR   KO; K14801; -.
DR   OrthoDB; 1181470at2759; -.
DR   PhylomeDB; P46718; -.
DR   TreeFam; TF313722; -.
DR   PRO; PR:P46718; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; ISO:MGI.
DR   GO; GO:1901532; P:regulation of hematopoietic progenitor cell differentiation; ISO:MGI.
DR   InterPro; IPR007320; PDCD2_C.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF04194; PDCD2_C; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    343       Programmed cell death protein 2.
FT                                /FTId=PRO_0000218305.
FT   ZN_FING     134    171       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   CONFLICT     88     88       L -> P (in Ref. 2; BAC32560).
FT                                {ECO:0000305}.
FT   CONFLICT    248    248       A -> P (in Ref. 1; AAA83433).
FT                                {ECO:0000305}.
SQ   SEQUENCE   343 AA;  38342 MW;  6D67243B0EA16BAC CRC64;
     MAAAAPGPVE LGFAEEAPAW RLRSEQFPSK VGGRPAWLGL AELPGPGALA CARCGRPLAF
     LLQVYAPLPG RDDAFHRSLF LFCCREPLCC AGLRVFRNQL PRNNAFYSYE PPSETEALGT
     ECVCLQLKSG AHLCRVCGCL APMTCSRCKQ AHYCSKEHQT LDWRLGHKQA CTQSDKIDHM
     VPDHNFLFPE FEIVTETEDE ILPEVVEMED YSEVTGSMGG IPEEELDSMA KHESKEDHIF
     QKFKSKIALE PEQILRYGRG IKPIWISGEN IPQEKDIPDC PCGAKRIFEF QVMPQLLNHL
     KADRLGRSID WGVLAVFTCA ESCSLGSGYT EEFVWKQDVT DTP
//
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