5C16

Myotubularin-related proetin 1

External Resource: Annotation

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5c16a1	All beta proteins	PH domain-like barrel	PH domain-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d5c16a2	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Myotubularin-like phosphatases	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d5c16b1	All beta proteins	PH domain-like barrel	PH domain-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d5c16b2	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Myotubularin-like phosphatases	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d5c16c1	All beta proteins	PH domain-like barrel	PH domain-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d5c16c2	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Myotubularin-like phosphatases	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d5c16d1	All beta proteins	PH domain-like barrel	PH domain-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d5c16d2	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Myotubularin-like phosphatases	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF02893	e5c16A2	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: PF02893	ECOD (1.6)
A	PF06602	e5c16A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF06602	ECOD (1.6)
B	PF02893	e5c16B2	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: PF02893	ECOD (1.6)
B	PF06602	e5c16B1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF06602	ECOD (1.6)
C	PF02893	e5c16C2	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: PF02893	ECOD (1.6)
C	PF06602	e5c16C1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF06602	ECOD (1.6)
D	PF02893	e5c16D2	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: PF02893	ECOD (1.6)
D	PF06602	e5c16D1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF06602	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
B	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
C	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
D	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02893	GRAM domain (GRAM)	GRAM domain	The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.	Domain
A, B, C, D	PF06602	Myotubularin-like phosphatase domain (Myotub-related)	Myotubularin-like phosphatase domain	This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate [1]. M ...	This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate [1]. Mutations in gene encoding myotubularin-related proteins have been associated with disease [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Myotubularin-related protein 1	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity phosphoric ester hydrolase activity phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity hydrolase activity, acting on ester bonds phosphatidylinositol bisphosphate phosphatase activity phosphatase activity hydrolase activity phosphatidylinositol-3,5-bisphosphate phosphatase activity phosphatidylinositol phosphate phosphatase activity catalytic activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity phosphoric ester hydrolase activity phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity hydrolase activity, acting on ester bonds phosphatidylinositol bisphosphate phosphatase activity phosphatase activity hydrolase activity phosphatidylinositol-3,5-bisphosphate phosphatase activity phosphatidylinositol phosphate phosphatase activity catalytic activity phosphatidylinositol-3-phosphate phosphatase activity phosphatidylinositol monophosphate phosphatase activity	phosphatidylinositol metabolic process dephosphorylation cellular metabolic process glycerophospholipid metabolic process lipid modification primary metabolic process phospholipid metabolic process organic substance metabolic process organophosphate metabolic process phosphatidylinositol dephosphorylation phospholipid dephosphorylation phosphate-containing compound metabolic process cellular lipid metabolic process metabolic process phosphatidylinositol metabolic process dephosphorylation cellular metabolic process glycerophospholipid metabolic process lipid modification primary metabolic process phospholipid metabolic process organic substance metabolic process organophosphate metabolic process phosphatidylinositol dephosphorylation phospholipid dephosphorylation phosphate-containing compound metabolic process cellular lipid metabolic process metabolic process cellular process glycerolipid metabolic process phosphorus metabolic process lipid metabolic process regulation of cellular process regulation of lipid metabolic process regulation of primary metabolic process regulation of phosphate metabolic process regulation of biological process regulation of dephosphorylation biological regulation regulation of phospholipid metabolic process regulation of cellular metabolic process regulation of macromolecule metabolic process regulation of phosphatidylinositol dephosphorylation regulation of phosphorus metabolic process macromolecule metabolic process regulation of metabolic process cellular biosynthetic process lipid biosynthetic process organic substance biosynthetic process glycerophospholipid biosynthetic process phospholipid biosynthetic process phosphatidylinositol biosynthetic process biosynthetic process glycerolipid biosynthetic process organophosphate biosynthetic process	membrane cellular anatomical entity intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR029021	Protein-tyrosine phosphatase-like	Homologous Superfamily
A, B, C, D	IPR010569	Myotubularin-like, phosphatase domain	Domain
A, B, C, D	IPR003595	Protein-tyrosine phosphatase, catalytic	Domain
A, B, C, D	IPR000387	Tyrosine-specific protein phosphatases domain	Domain
A, B, C, D	IPR011993	PH-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR030564	Myotubularin family	Family
A, B, C, D	IPR004182	GRAM domain	Domain
A, B, C, D	IPR016130	Protein-tyrosine phosphatase, active site	Active Site
A, B, C, D	IPR037857	MTMR1, PH-GRAM	Domain
A, B, C, D	IPR030587	Myotubularin-related protein 1, protein tyrosine phosphatase domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: Q13613	adenoma atypical teratoid rhabdoid tumor intellectual disability medulloblastoma osteosarcoma psoriasis adrenal cortex carcinoma dermatomyositis large cell medulloblastoma myopathy ovarian cancer Sjogren syndrome arthrogryposis Gaucher disease lung cancer adenoma atypical teratoid rhabdoid tumor intellectual disability medulloblastoma osteosarcoma psoriasis adrenal cortex carcinoma dermatomyositis large cell medulloblastoma myopathy ovarian cancer Sjogren syndrome arthrogryposis Gaucher disease lung cancer oligodendroglioma Pick disease spina bifida

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D	OPM	Monotopic/peripheral	Alpha/Beta monotopic/peripheral	Phosphotyrosine protein phosphatases II	Myotubularin-like phosphatases

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.