DB code: D00493

CATH domain 2.20.70.10 : Ubiquitin Ligase Nedd4; Chain
3.10.50.40 : Chitinase A; domain 3 Catalytic domain
E.C. 5.2.1.8
CSA 1nmw
M-CSA 1nmw
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q13526 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
EC 5.2.1.8
Rotamase Pin1
PPIase Pin1
NP_006212.1 (Protein)
NM_006221.3 (DNA/RNA sequence)
PF00639 (Rotamase)
PF00397 (WW)
[Graphical View]

KEGG enzyme name
peptidylprolyl isomerase
PPIase
cyclophilin [misleading, see comments]
peptide bond isomerase
peptidyl-prolyl cis-trans isomerase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q13526 PIN1_HUMAN Peptidylproline (omega=180) = peptidylproline (omega=0). Interacts with STIL (By similarity). Interacts with MPHOSPH1. Nucleus.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C03798 C03633
E.C.
Compound Peptidylproline (omega=180, trans) Peptidylproline (omega=0, cis)
Type amino acids,peptide/protein amino acids,peptide/protein
ChEBI
PubChem
1f8aB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1nmvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1pinA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1f8aB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1nmvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1nmwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1pinA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ALA-PRO (chain B)

Reference for Active-site residues
resource references E.C.
literature [1]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1f8aB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1nmvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pinA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f8aB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 63;CYS 117;SER 158;HIS 161
1nmvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 59;CYS 113;SER 154;HIS 157
1nmwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 59;CYS 113;SER 154;HIS 157
1pinA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 59;CYS 113;SER 154;HIS 157

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Fig.7, p.880-883
[3]
[28]

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS)
Medline ID 97344079
PubMed ID 9200606
Journal Cell
Year 1997
Volume 89
Pages 875-86
Authors Ranganathan R, Lu KP, Hunter T, Noel JP
Title Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.
Related PDB 1pin
Related UniProtKB Q13526
[2]
Resource
Comments
Medline ID
PubMed ID 9548941
Journal Biochemistry
Year 1998
Volume 37
Pages 5566-75
Authors Schutkowski M, Bernhardt A, Zhou XZ, Shen M, Reimer U, Rahfeld JU, Lu KP, Fischer G
Title Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin1 substrate recognition.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 11212339
Journal Cell Mol Life Sci
Year 1999
Volume 56
Pages 788-806
Authors Zhou XZ, Lu PJ, Wulf G, Lu KP
Title Phosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11163176
Journal Cell
Year 2000
Volume 103
Pages 1001-4
Authors Sudol M, Hunter T
Title NeW wrinkles for an old domain.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10899126
Journal EMBO J
Year 2000
Volume 19
Pages 3727-38
Authors Wu X, Wilcox CB, Devasahayam G, Hackett RL, Arevalo-Rodriguez M, Cardenas ME, Heitman J, Hanes SD
Title The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10744752
Journal J Biol Chem
Year 2000
Volume 275
Pages 10577-81
Authors Landrieu I, De Veylder L, Fruchart JS, Odaert B, Casteels P, Portetelle D, Van Montagu M, Inze D, Lippens G
Title The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10966801
Journal J Mol Biol
Year 2000
Volume 301
Pages 1003-17
Authors Sekerina E, Rahfeld JU, Muller J, Fanghanel J, Rascher C, Fischer G, Bayer P
Title NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10932246
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 639-43
Authors Verdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP
Title Structural basis for phosphoserine-proline recognition by group IV WW domains.
Related PDB 1f8a
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10932238
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 611-3
Authors Zarrinpar A, Lim WA
Title Converging on proline: the mechanism of WW domain peptide recognition.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11456485
Journal Biochemistry
Year 2001
Volume 40
Pages 8479-86
Authors Myers JK, Morris DP, Greenleaf AL, Oas TG
Title Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11795843
Journal Curr Genet
Year 2001
Volume 40
Pages 234-42
Authors Wu X, Chang A, Sudol M, Hanes SD
Title Genetic interactions between the ESS1 prolyl-isomerase and the RSP5 ubiquitin ligase reveal opposing effects on RNA polymerase II function.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11223034
Journal FEBS Lett
Year 2001
Volume 490
Pages 190-5
Authors Sudol M, Sliwa K, Russo T
Title Functions of WW domains in the nucleus.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11470801
Journal J Biol Chem
Year 2001
Volume 276
Pages 37520-8
Authors Kamimoto T, Zama T, Aoki R, Muro Y, Hagiwara M
Title Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11013245
Journal J Biol Chem
Year 2001
Volume 276
Pages 1434-8
Authors Landrieu I, Odaert B, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Inze D, Lippens G
Title p13(SUC1) and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11118437
Journal J Biol Chem
Year 2001
Volume 276
Pages 13524-9
Authors Metzner M, Stoller G, Rucknagel KP, Lu KP, Fischer G, Luckner M, Kullertz G
Title Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11313338
Journal J Biol Chem
Year 2001
Volume 276
Pages 25150-6
Authors Wintjens R, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Buee L, Lippens G, Landrieu I
Title 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 11118438
Journal J Biol Chem
Year 2001
Volume 276
Pages 13517-23
Authors Yao JL, Kops O, Lu PJ, Lu KP
Title Functional conservation of phosphorylation-specific prolyl isomerases in plants.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 11389853
Journal Mol Cell
Year 2001
Volume 7
Pages 1071-83
Authors Stukenberg PT, Kirschner MW
Title Pin1 acts catalytically to promote a conformational change in Cdc25.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 11786999
Journal Biopolymers
Year 2002
Volume 63
Pages 111-21
Authors Kowalski JA, Liu K, Kelly JW
Title NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 11904169
Journal FEBS Lett
Year 2002
Volume 513
Pages 305-11
Authors Kops O, Zhou XZ, Lu KP
Title Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 11982361
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 4980-6
Authors Deechongkit S, Kelly JW
Title The effect of backbone cyclization on the thermodynamics of beta-sheet unfolding: stability optimization of the PIN WW domain.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 12358534
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 11900-7
Authors Kaul R, Deechongkit S, Kelly JW
Title Synthesis of a negatively charged dibenzofuran-based beta-turn mimetic and its incorporation into the WW miniprotein-enhanced solubility without a loss of thermodynamic stability.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 11751914
Journal J Biol Chem
Year 2002
Volume 277
Pages 10173-7
Authors Kato Y, Ito M, Kawai K, Nagata K, Tanokura M
Title Determinants of ligand specificity in groups I and IV WW domains as studied by surface plasmon resonance and model building.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 11723108
Journal J Biol Chem
Year 2002
Volume 277
Pages 2381-4
Authors Lu PJ, Zhou XZ, Liou YC, Noel JP, Lu KP
Title Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 12153046
Journal J Biomol NMR
Year 2002
Volume 23
Pages 163-4
Authors Jacobs DM, Saxena K, Grimme S, Vogtherr M, Pescatore B, Langer T, Elshorst B, Fiebig KM
Title 1H, 13C and 15N backbone resonance assignment of the peptidyl-prolyl cis-trans isomerase Pin1.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 12079389
Journal J Mol Biol
Year 2002
Volume 320
Pages 321-32
Authors Landrieu I, Wieruszeski JM, Wintjens R, Inze D, Lippens G
Title Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana.
Related PDB 1j6y
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 12397361
Journal Nature
Year 2002
Volume 419
Pages 849-53
Authors Zheng H, You H, Zhou XZ, Murray SA, Uchida T, Wulf G, Gu L, Tang X, Lu KP, Xiao ZX
Title The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response.
Related PDB
Related UniProtKB
[28]
Resource
Comments NMR structure
Medline ID
PubMed ID 12721297
Journal J Biol Chem
Year 2003
Volume 278
Pages 26183-93
Authors Bayer E, Goettsch S, Mueller JW, Griewel B, Guiberman E, Mayr LM, Bayer P
Title Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding.
Related PDB 1nmv 1nmw
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 12686540
Journal J Biol Chem
Year 2003
Volume 278
Pages 26174-82
Authors Jacobs DM, Saxena K, Vogtherr M, Bernado P, Pons M, Fiebig KM
Title Peptide binding induces large scale changes in inter-domain mobility in human Pin1.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 12471608
Journal Proteins
Year 2003
Volume 50
Pages 158-69
Authors Wang T, Wade RC
Title Implicit solvent models for flexible protein-protein docking by molecular dynamics simulation.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 15229605
Journal Nature
Year 2004
Volume 430
Pages 101-5
Authors Deechongkit S, Nguyen H, Powers ET, Dawson PE, Gruebele M, Kelly JW
Title Context-dependent contributions of backbone hydrogen bonding to beta-sheet folding energetics.
Related PDB
Related UniProtKB

Comments
According to the literature [1], this enzyme catalyzes the following reactions:
(A) Addition of Cys to carbonyl carbon of substrate, leading to a formation of tetrahedral intermediate.
(B) Elimination of Cys from the tetrahedral intermediate.

Created Updated
2005-05-06 2009-02-26