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. 1999 Mar;10(3):597–608. doi: 10.1091/mbc.10.3.597

Figure 1.

Figure 1

Cloning and sequencing of p220 cDNA. (A) Alignment of the predicted amino acid sequence of p220 with human MAP4 (West et al., 1991). Identical residues are shaded in black, and similar residues are shaded in gray. The dashed line above the sequence indicates an internal peptide sequence from XMAP230. Potential phosphorylation sites for p34cdc2 kinase are indicated by black circles; MAP kinase is indicated by lines; and MARK is indicated by white circles. (B) Structural comparison of Xenopus and human MAP4. The domains are N, highly conserved amino terminus; a, acidic region; RPT, repetitive domain; b, acidic region; P, highly conserved proline-rich domain; SP, serine- and proline-rich domain; PGGG, highly conserved domain containing the MT-binding domain; and C, acidic tail (see West et al., 1991). Potential phosphorylation sites for p34cdc2 kinase are indicated by black circles; MAP kinase is indicated by squares; and MARK is indicated by white circles. Overall XMAP4 and human MAP4 are 30% identical and 65% similar.