AC T19187
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ID T19187
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DT 13.03.2006 (created); res.
DT 30.07.2014 (updated); mkl.
CO Copyright (C), QIAGEN.
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FA PML-4
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SY MYL; PML; PML-X; probable transcription factor PML; promyelocytic leukemia; RING finger protein 71; RNF71; TRIM19; tripartite motif protein 19.
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OS human, Homo sapiens
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates
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GE G013657 PML; HGNC: PML.
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SZ 633 AA; 70.0 kDa (cDNA) (calc.).
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SQ MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQC
SQ QAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYR
SQ QIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDG
SQ TRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEEL
SQ DAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEA
SQ VDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLR
SQ QEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPE
SQ EAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCS
SQ QTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLP
SQ NSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENL
SQ ADPQAEDRPLVFFDLKIDNESGFSWGYPHPFLI
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SC translated from EMBL:X63131
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FT 57 91 PF00097; Zinc finger, C3HC4 type (RING finger).
FT 57 91 SM00184; ring_2.
FT 57 92 PS50089; ZF_RING_2.
FT 124 166 PS50119; ZF_BBOX.
FT 124 166 SM00336; bboxneu5.
FT 126 166 PF00643; zf-B_box.
FT 137 382 PF00478; IMP dehydrogenase / GMP reductase domain.
FT 184 222 PS50119; ZF_BBOX.
FT 186 232 PF00643; zf-B_box.
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IN T21852 HDAC1; Mammalia.
IN T04110 HDAC3; human, Homo sapiens.
IN T14535 TBX2; Mammalia.
IN T14536 Tbx3; Mammalia.
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DR TRANSPATH: MO000079043.
DR EMBL: X63131;
DR UniProtKB: P29590-5;
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RN [1]; RE0025265.
RX PUBMED: 15195100.
RA Bernardi R., Scaglioni P. P., Bergmann S., Horn H. F., Vousden K. H., Pandolfi P. P.
RT PML regulates p53 stability by sequestering Mdm2 to the nucleolus.
RL Nat. Cell Biol. 6:665-672 (2004).
RN [2]; RE0052675.
RX PUBMED: 11259576.
RA Wu W. S., Vallian S., Seto E., Yang W. M., Edmondson D., Roth S., Chang K. S.
RT The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases.
RL Mol. Cell. Biol. 21:2259-2268 (2001).
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