1XM2

Crystal structure of Human PRL-1

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1xm2a_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1xm2b_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1xm2c_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1xm2d_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d1xm2e_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d1xm2f_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8042325	3000304	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8042325	3000304	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8042325	3000304	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8042325	3000304	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8042325	3000304	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8042325	3000304	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	DSPc	e1xm2A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)
B	DSPc	e1xm2B1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)
C	DSPc	e1xm2C1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)
D	DSPc	e1xm2D1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)
E	DSPc	e1xm2E1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)
F	DSPc	e1xm2F1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
B	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
C	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
D	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
E	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
F	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00782	Dual specificity phosphatase, catalytic domain (DSPc)	Dual specificity phosphatase, catalytic domain	Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Tyrosine Phosphatase	phosphoric ester hydrolase activity phosphoprotein phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds phosphatase activity hydrolase activity catalytic activity protein tyrosine/serine/threonine phosphatase activity protein tyrosine phosphatase activity	cellular process cell cycle positive regulation of locomotion regulation of biological process regulation of cell motility regulation of cellular process biological regulation positive regulation of biological process positive regulation of cell migration regulation of locomotion positive regulation of cell motility regulation of cell migration cell migration cell motility cellular process cell cycle positive regulation of locomotion regulation of biological process regulation of cell motility regulation of cellular process biological regulation positive regulation of biological process positive regulation of cell migration regulation of locomotion positive regulation of cell motility regulation of cell migration cell migration cell motility locomotion positive regulation of cellular process dephosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process phosphorus metabolic process	membrane-bounded organelle intracellular anatomical structure early endosome endosome intracellular vesicle cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle cytoplasmic vesicle organelle cytoplasm vesicle cytoskeleton membrane-bounded organelle intracellular anatomical structure early endosome endosome intracellular vesicle cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle cytoplasmic vesicle organelle cytoplasm vesicle cytoskeleton spindle intracellular non-membrane-bounded organelle microtubule cytoskeleton non-membrane-bounded organelle cell periphery cytoplasmic side of plasma membrane cytoplasmic side of membrane membrane plasma membrane side of membrane nucleus endoplasmic reticulum

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR029021	Protein-tyrosine phosphatase-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR003595	Protein-tyrosine phosphatase, catalytic	Domain
A, B, C, D, E A, B, C, D, E, F	IPR000387	Tyrosine-specific protein phosphatases domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR020422	Dual specificity protein phosphatase domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR000340	Dual specificity phosphatase, catalytic domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: Q93096	lung cancer medulloblastoma pancreatic ductal adenocarcinoma Pneumocystis Carinii Pneumonia Prevention psoriasis transitional cell carcinoma breast cancer dermatomyositis gastric cancer hereditary spastic paraplegia interstitial lung disease limb-girdle muscular dystrophy malignant colon neoplasm osteosarcoma Pick disease lung cancer medulloblastoma pancreatic ductal adenocarcinoma Pneumocystis Carinii Pneumonia Prevention psoriasis transitional cell carcinoma breast cancer dermatomyositis gastric cancer hereditary spastic paraplegia interstitial lung disease limb-girdle muscular dystrophy malignant colon neoplasm osteosarcoma Pick disease pneumocystosis Sjogren syndrome Alzheimer disease breast carcinoma Duchenne muscular dystrophy gastric carcinoma human African trypanosomiasis invasive ductal breast carcinoma lung adenocarcinoma malignant pancreatic neoplasm ovarian cancer plasma cell myeloma progressive supranuclear palsy Tourette syndrome astrocytic tumor cutaneous lupus erythematosus exocrine pancreatic carcinoma hepatocellular carcinoma IgA glomerulonephritis juvenile dermatomyositis

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.