SMART: Pfam domain MISS

The domain within your query sequence starts at position 1 and ends at position 166; the E-value for the MISS domain shown below is 5.5e-52.

MYPFIPPARLLPGSPAPFLPSGPSCPQPSGPYPGPAVRVPGPTRSYVSTNVPFPELPRPN
SAPTDPVGPLGTQGSMSSGPWAPGMGGQHPNVPYLFPESSPTPPLPVSGAPPVAWVTVPP
GAWEPPAQYPTPEASYPSPGLQPSPNNPYPLPPGPSAASPGPGSLH

MISS

PFAM accession number:	PF15822
Interpro abstract (IPR031653):	MAPK-interacting and spindle-stabilising protein (MISS) is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localisation signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII (meiosis metaphase II) spindle. MISS is the first example of a physiological MAPK-substrate that is stabilised in MII that specifically regulates MII spindle integrity during the cytostatic factor (CSF) arrest [ (PUBMED:12011110) ].

PFAM accession number:

PF15822

Interpro abstract (IPR031653):

MAPK-interacting and spindle-stabilising protein (MISS) is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localisation signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII (meiosis metaphase II) spindle. MISS is the first example of a physiological MAPK-substrate that is stabilised in MII that specifically regulates MII spindle integrity during the cytostatic factor (CSF) arrest [ (PUBMED:12011110) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry MISS