Skip to main content
. Author manuscript; available in PMC: 2011 May 3.
Published in final edited form as: Dev Dyn. 2008 Jul;237(7):1851–1861. doi: 10.1002/dvdy.21582

Table 1.

S. purpuratus homologs of conserved Polycomb group proteins

Predicted
PcG Complex*
Gene Name Genbank
accession
Predicted
polypeptide length
Domains and function Homologs
(BLAST score)
PhoRC Sp-Pho XP_790188 400 C2H2 Zn-finger (4) transcription factor, binds Polycomb Responsive
Elements (PREs)
D. rerio (8e-112)
H. sapiens (2e-104)
Sp-Mbt1 XP_785195 1805 MBT-domain (3), Sterile α-motif (SAM) protein-protein interaction
domain
M. musculus (9e-83)
H. sapiens (4e-82)
Sp-Mbt2 XP_001202275
XP_001201293
1944 MBT-domain (4), SAM protein-protein interaction domain G. gallus (2e-142)
H. sapiens (4e-141)
Sp-L(3)mbt XP_792284 992 MBT-domain (3), C2H2 Zn-finger (2), SAM protein-protein
interaction domain
H. sapiens (1e-180)
M.musculus (3e-179)

PRC2 Sp-Ezh2 XP_790741 551 SET-domain histone methyltransferase, specific tri-methylation of
H3K27 recognized by the Polycomb (Pc) chromodomain
X. tropicalis (2e-179)
H. sapiens (5e-179)
Sp-Eed XP_786345 461 WD40-domains (5) coordinate multi-protein complex assemblies as
a scaffold for protein interactions
D. rerio (2e-157)
H. sapiens (2e-156)
Sp-Suz12 XP_788076 757 No defined domains, required for HTMase and silencing activity
of the EED-EZH2 complex
D.rerio (4e-123)
M. musculus (1e-122)
Sp-Rbbp4 XP_780271 430 WD40-domains (5) M. musculus (0.0)
H. sapiens (0.0)

PRC1 Sp-Pc1 SPU_20586 1393 Chromodomain, chromatin organization modifier domain involved
in promoting heterochromatin condensation
R. norvegicus (1e-22)
C. familiaris (2e-22)
Sp-Pc2 SPU_20946 456 Chromodomain D. melanogaster (7e-16)
R. norvegicus (2e-16)
Sp-Ph XP_789940 788 Zn-finger, SAM protein-protein interaction domain H. sapiens (5e-50)
M. musculus (9e-50)
Sp-Psc XP_783799 479 C3CH4 Zn-finger (RING-finger) domain M. musculus (3e-54)
H. sapiens (9e-54)
Sp-Ring1 XP_788976 306 C3CH4 Zn-finger (RING-finger) domain M. musculus (3e-93)
H. sapiens (4e-93)
*

The S. purpuratus polycomb group protein homologs are categorized based on genetic and biochemical evidence of complex association from their respective counterparts in various animals