S/MARt DB - S/MARbinder

AC  SB000062
XX
DT  14.8.2000 17:53:47 (created); ili
DT  9.3.2001 14:35:00 (updated); ili
XX
NA  PARP
XX
SY  poly(ADP-ribose) polymerase 
XX
OS  human, Homo sapiens
OC  eukaryota; animalia; metazoa; chordata; vertebrata;
OC  tetrapoda; mammalia; eutheria; primates
XX
DE  G001407 
XX
SZ  1013 AA; 113.0 kD (cDNA), 114 kDa (SDS) [2]
XX
SQ  AESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVG
SQ  HSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSN
SQ  RSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQL
SQ  KGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQ
SQ  NDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQ
SQ  LVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPET
SQ  SASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTG
SQ  TANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPW
SQ  GAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEH
SQ  SAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKL
SQ  EQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGT
SQ  KSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVS
SQ  QGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGG
SQ  SDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIER
SQ  EGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMV
SQ  SKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSAN
SQ  ISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW
SC  SwissProt #P09874
XX
SF  caution: not equal to p114 S/MAR-binding activity, but
SF  concluded to contribute to it [2]; copurifies with SAF-A
SF  SB000017 and DNA-PK SB000055 [2]
XX
FF  known to bind to nicks and ends of DNA in a
FF  sequence-independent manner [1] [2]; binding to ends
FF  of DNA occurs at higher concentrations than binding to base
FF  unpairing regions [1]; ADP-ribosylation circumvents
FF  binding to base unpairing regions in vitro and may modulate
FF  binding activity in vivo [1]; physical interaction with
FF  the Ku autoantigen in vivo is independent of the presence of
FF  DNA and critical for synergistic binding to S/MARs [1];
FF  associates with components of the DNA replication, repair,
FF  transcription and recombination machineries [2]; may be
FF  involved in telomere maintenance and chromosomal stability
FF  [2]; downregulated during cellular senescence [2];
FF  modifies DNA-PK SB000055 and p53 [2]
XX
IN  SB000054; Ku autoantigen
IN  SB000055; DNA-PK
XX
CP  upregulated in breast cancer [2]
XX
BS  SM0000044; MOUSE$IgHmu-5MAR [1]
MM  direct gel shift;
SO  SK-BR 3; human
QA  6
BS  SM0000044; MOUSE$IgHmu-5MAR [1]
MM  assessment of the dissociation constant;
MM  3 nM
SO  SK-BR 3; human
QA  6
BS  SM0000045; MOUSE$IgHmu-3MAR [1]
MM  direct gel shift;
SO  SK-BR 3; human
QA  6
BS  SM0000045; MOUSE$IgHmu-3MAR [1]
MM  assessment of the dissociation constant;
MM  1.8 nM
SO  SK-BR 3; human
QA  6
BS  SM0000046; AS$MAR [1]
MM  affinity chromatography;
PR  (25)7
SO  SK-BR 3; human
QA  6
BS  SM0000046; AS$MAR [1]
MM  direct gel shift;
PR  (25)7
SO  SK-BR 3; human
QA  6
XX
DR  EMBL: M32721; HSPPOL; r 
DR  EMBL: M18112; HSPOLP; r 
DR  EMBL: J03473; HSRISDAD; r 
DR  SwissProt: P09874; PPOL_HUMAN
DR  PIR: A29725; A29725 
XX
RN  [1]
RX  MEDLINE; 99329069 PubMed; 10400681
RA  Galande, S., Kohwi-Shigematsu, T.
RT  Poly(ADP-ribose) polymerase and Ku autoantigen form a
RT  complex and synergistically bind to matrix attachment
RT  sequences
RL  J. Biol. Chem. 274:20521-20528 (1999)
RN  [2]
RX  MEDLINE; 20271503 PubMed; 10813395
RA  Galande, S., Kohwi-Shigematsu, T.
RT  Caught in the act: binding of Ku and PARP to MARs reveals
RT  novel aspects of their functional interaction
RL  Crit. Rev. Eukaryot. Gene Expr. 10:63-72 (2000)
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