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PDCD2_MOUSE
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   03-AUG-2022, entry version 137.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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 lymphoid
RT   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., 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).
CC   -!- FUNCTION: May be a DNA-binding protein with a regulatory function. May
CC       play an important role in cell death and/or in regulation of cell
CC       proliferation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during apoptosis of lymphoid and myeloid
CC       cells.
CC   -!- PTM: Ubiquitinated by PRKN, promoting proteasomal degradation.
CC       {ECO:0000250}.
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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   AlphaFoldDB; 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   ProteomicsDB; 287900; -.
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   InParanoid; P46718; -.
DR   OrthoDB; 1181470at2759; -.
DR   PhylomeDB; P46718; -.
DR   TreeFam; TF313722; -.
DR   BioGRID-ORCS; 18567; 13 hits in 44 CRISPR screens.
DR   ChiTaRS; Pdcd2; mouse.
DR   PRO; PR:P46718; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P46718; protein.
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; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..343
FT                   /note="Programmed cell death protein 2"
FT                   /id="PRO_0000218305"
FT   ZN_FING         134..171
FT                   /note="MYND-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   CONFLICT        88
FT                   /note="L -> P (in Ref. 2; BAC32560)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="A -> P (in Ref. 1; AAA83433)"
FT                   /evidence="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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