S/MARt DB - S/MARbinder

AC  SB000002
XX
DT  1.1.1999 00:00:00 (created); ili
DT  11.6.2001 16:17:00 (updated); ili
XX
NA  lamin A
XX
OS  rat, Rattus norvegicus
OC  eukaryota; animalia; metazoa; chordata; vertebrata;
OC  tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae;
OC  murinae
XX
DE  G002526 
XX
SZ  665 AA; 74.3 kDa (cDNA)
XX
SQ  METPSQRRPTRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLR
SQ  LRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARN
SQ  TKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAK
SQ  KQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESR
SQ  LADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRID
SQ  SLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQ
SQ  ELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQSQGGGSVTKKRK
SQ  LESSESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLMT
SQ  YRFPPKFTLKAGQVVTIWASGAGATHSPPTDLVWKAQNTWGCGTSLRTALINATGEEVAM
SQ  RKLVRSLTMVEDNDDEEEDGDELLHHHRGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKA
SQ  ASGSGAQVGGSISSGSSASSVTVTRSFRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSSQ
SQ  NCSIM
SC  SwissProt #P48679
XX
SF  central alpha-helical rod domain flanked by a short
SF  nonhelical heat and a long nonhelical carboxy terminus
SF  [4] [5]; may self-assemble into long polymers in which
SF  the rod domains are dimerized to coiled-coil molecules
SF  [4]
XX
FF  observed in aggregates that bind MAR-DNA [2] [4]; does
FF  not bind MAR-DNA in Southwestern assay [2]; polymers of
FF  lamin A, B1 & C bind through single-stranded regions and
FF  minor groove contact [4]; no binding to DNA at 15 C
FF  [1]
XX
IN  SB000003; lamin B1
IN  SB000004; lamin C
XX
CP  liver [2]
CN  spermatogenic cells [3]
XX
BS  SM0000001; MOUSE$kappa-MAR [4]
MM  nitrocellulose filter binding;
SO  rl; rat
QA  6
BS  SM0000037; DROME$H1H3 [4]
MM  nitrocellulose filter binding;
SO  rl; rat
QA  6
BS  SM0000037; DROME$H1H3 [4]
MM  replacement by distamycin A;
SO  rl; rat
QA  6
BS  SM0000037; DROME$H1H3 [4]
MM  replacement by chromomycin;
SO  rl; rat
QA  6
BS  SM0000050; RAT$GDH-5MAR [4]
MM  nitrocellulose filter binding;
SO  rl; rat
QA  6
XX
DR  EMBL: X66870; RNLAMA; r 
DR  EMBL: X76297; RNLAMINA; r 
DR  SwissProt: P48679; LAMA_RAT
XX
RN  [1]
RX  MEDLINE; 91250423 PubMed; 2040622
RA  Hakes, D. J., Berezney, R.
RT  DNA binding properties of the nuclear matrix and individual
RT  nuclear matrix proteins. Evidence for salt-resistant DNA
RT  binding sites
RL  J. Biol. Chem. 266:11131-11140 (1991)
RN  [2]
RX  MEDLINE; 92405165 PubMed; 1525831
RA  Luderus, M. E. E., de Graaf, A., Mattia, E., den Blaauwen,
RA  J. L., Grande, M. A., de Jong, L., van Driel, R.
RT  Binding of matrix attachment regions to lamin B1
RL  Cell 70:949-959 (1992)
RN  [3]
RX  MEDLINE; 93280257 PubMed; 8505378
RA  Vester, B., Smith, A., Krohne, G., Benavente, R.
RT  Presence of a nuclear lamina in pachytene spermatocytes of
RT  the rat
RL  J. Cell Sci. 104:557-563 (1993)
RN  [4]
RX  MEDLINE; 94344140 PubMed; 8065361
RA  Luderus, M. E. E., den Blaauwen, J. L., de Smit, O. J. B.,
RA  Compton, D. A., van Driel, R.
RT  Binding of matrix attachment regions to lamin polymers
RT  involves single-stranded regions and the minor groove
RL  Mol. Cell. Biol. 14:6297-6305 (1994)
RN  [5]
RX  MEDLINE; 20114667 PubMed; 10651245
RA  Goldberg, M., Harel, A., Gruenbaum, Y.
RT  The nuclear lamina: molecular organization and interaction
RT  with chromatin
RL  Crit. Rev. Eukaryot. Gene Expr. 9:285-293 (1999)
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