DB code: D00493

CATH domain	2.20.70.10 : Ubiquitin Ligase Nedd4; Chain
CATH domain	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	Unbound	Unbound
1nmvA01	Unbound	Unbound
1pinA01	Unbound	Unbound
1f8aB02	Unbound	Unbound
1nmvA02	Unbound	Unbound
1nmwA	Unbound	Unbound
1pinA02	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
1nmvA01
1pinA01
1f8aB02	HIS 63;CYS 117;SER 158;HIS 161
1nmvA02	HIS 59;CYS 113;SER 154;HIS 157
1nmwA	HIS 59;CYS 113;SER 154;HIS 157
1pinA02	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