Structural Classification of Proteins
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Fold: (Phosphotyrosine protein) phosphatases II

core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1432

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b)
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: (Phosphotyrosine protein) phosphatases II
    core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1432

Superfamilies:

  1. (Phosphotyrosine protein) phosphatases II (3)
    share with the family I the common active site structure with a circularly permuted topology
    1. Dual-specificity phosphatases (2)
      1. VH1-related dual-specificity phosphatase, VHR
        1. Human (Homo sapiens) (2)
      2. Mapk phosphotase Pyst1 (mkp3)
        1. Human (Homo sapiens) (1)
    2. Higher-molecular-weight phosphotyrosine protein phosphatases (8)
      have an extension to the beta-sheet of 3 antiparallel strands before strand 4
      1. Tyrosine phosphatase
        1. Human (Homo sapiens), 1B (24) pic
        2. Human (Homo sapiens), mu (1)
          receptor protein tyrosine phosphatase mu, domain 1
        3. Mouse (Mus musculus) (1)
          receptor protein tyrosine phosphatase alpha, domain 1
        4. Human (Homo sapiens), shp-2 (1)
        5. Human (Homo sapiens), shp-1 (1)
        6. Yersinia enterocolitica (4)
      2. SptP tyrosine phosphatase, catalytic domain
        1. Salmonella typhimurium (2)
      3. RPTP Lar
        duplication: tandem repeat of the phosphatase domain
        1. Human (Homo sapiens) (1)
    3. Phoshphoinositide phosphatase Pten (Pten tumor suppressor), N-terminal domain (1)
      1. Phoshphoinositide phosphatase Pten (Pten tumor suppressor), N-terminal domain
        1. Human (Homo sapiens) (1)

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Generated from scop database 1.55 with scopm 1.095 on Mon Jul 9 18:35:50 2001
Copyright © 1994-2001 The scop authors / scop@mrc-lmb.cam.ac.uk