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InterPro: IPR011948 Dullard-like phosphatase domain

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UniProtKB

Matches:

517 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR011948 Dullard

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR02251	HIF-SF_euk	517
Signatures in BioMart

InterPro Relationships Help

Parent

IPR004274 NLI interacting factor

GO Term annotation Help

Function

GO:0016791 phosphatase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard" [1], and the NLI interacting factor (NIF)-like phosphatases [2].

Structural links Help

PDB - click here

SCOP: c.108.1.16

CATH: 3.40.50.1000

Database links Help

Enzyme: EC:3.1.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011948

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14595 Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2

P38757 Nuclear envelope morphology protein 1

P58465 CTD small phosphatase-like protein

Q20432 Serine/threonine-protein phosphatase dullard homolog

Q9VRG7 Serine/threonine-protein phosphatase dullard homolog

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004274	NLI interacting factor
IPR011948	Dullard-like phosphatase domain
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Satow R, Chan TC, Asashima M. Molecular cloning and characterization of dullard: a novel gene required for neural development. Biochem. Biophys. Res. Commun. 295 85-91 2002 [PubMed: 12083771] http://dx.doi.org/10.1016/S0006-291X(02)00641-1
2.	Kashuba VI, Li J, Wang F, Senchenko VN, Protopopov A, Malyukova A, Kutsenko AS, Kadyrova E, Zabarovska VI, Muravenko OV, Zelenin AV, Kisselev LL, Kuzmin I, Minna JD, Winberg G, Ernberg I, Braga E, Lerman MI, Klein G, Zabarovsky ER. RBSP3 (HYA22) is a tumor suppressor gene implicated in major epithelial malignancies. Proc. Natl. Acad. Sci. U.S.A. 101 4906-11 2004 [PubMed: 15051889] http://dx.doi.org/10.1073/pnas.0401238101

Additional Reading Open in usermanual
	Kamenski T, Heilmeier S, Meinhart A, Cramer P. Structure and mechanism of RNA polymerase II CTD phosphatases. Mol. Cell 15 2004 399-407 [PubMed: 15304220] http://dx.doi.org/10.1016/j.molcel.2004.06.035
	Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK. Structural genomics of protein phosphatases. J. Struct. Funct. Genomics 8 2007 121-40 [PubMed: 18058037] http://dx.doi.org/10.1007/s10969-007-9036-1
	Koonin EV, Tatusov RL. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 244 1994 125-32 [PubMed: 7966317] http://dx.doi.org/10.1006/jmbi.1994.1711
	Zhang Y, Kim Y, Genoud N, Gao J, Kelly JW, Pfaff SL, Gill GN, Dixon JE, Noel JP. Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1. Mol. Cell 24 2006 759-70 [PubMed: 17157258] http://dx.doi.org/10.1016/j.molcel.2006.10.027
	Selengut JD. MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases. Biochemistry 40 2001 12704-11 [PubMed: 11601995] http://dx.doi.org/10.1021/bi011405e

InterPro 23.1