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InterPro: IPR004274 NLI interacting factor

Protein matches Help

UniProtKB

Matches:

1393 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

IPR004274 NIF

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03031	NIF	1256
PROSITE profile	PS50969	FCP1	1356
SMART	SM00577	CPDc	1290
Signatures in BioMart

InterPro Relationships Help

Children

IPR011943 HAD-superfamily hydrolase, subfamily IIID
IPR011947 FCP1-like phosphatase, phosphatase domain
IPR011948 Dullard-like phosphatase domain

InterPro annotation

Entry Details in BioMart

Abstract

The function of this domain is unclear. It is found in proteins of diverse function including phosphatases some of which may be active in active in ternary elongation complexes and a number of NLI interacting factors. In the phospatases this domain is often present N-terminal to the BRCT domain (IPR001357).

Structural links Help

PDB - click here

SCOP: c.108.1.16

CATH: 3.40.50.1000

Database links Help

PROSITE doc: PDOC50969

PANDIT: PF03031

Blocks: IPB004274

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004274

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

Q20432 Serine/threonine-protein phosphatase dullard homolog

Q8BGR9 Ubiquitin-like domain-containing CTD phosphatase 1

Q9V9P3 Mitochondrial import inner membrane translocase subunit TIM50-A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011943	HAD-superfamily hydrolase, subfamily IIID
IPR000626	Ubiquitin
IPR004274	NLI interacting factor
IPR019955	Ubiquitin supergroup
IPR011948	Dullard-like phosphatase domain
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Archambault J, Chambers RS, Kobor MS, Ho Y, Cartier M, Bolotin D, Andrews B, Kane CM, Greenblatt J. An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 94 1997 14300-5 [PubMed: 9405607] http://dx.doi.org/10.1073/pnas.94.26.14300
	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
	Cho H, Kim TK, Mancebo H, Lane WS, Flores O, Reinberg D. A protein phosphatase functions to recycle RNA polymerase II. Genes Dev. 13 1999 1540-52 [PubMed: 10385623] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=10385623&action=stream&blobtype=pdf
	Hausmann S, Shuman S. Defining the active site of Schizosaccharomyces pombe C-terminal domain phosphatase Fcp1. J. Biol. Chem. 278 2003 13627-32 [PubMed: 12556522] http://dx.doi.org/10.1074/jbc.M213191200
	Kobor MS, Archambault J, Lester W, Holstege FC, Gileadi O, Jansma DB, Jennings EG, Kouyoumdjian F, Davidson AR, Young RA, Greenblatt J. An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae. Mol. Cell 4 1999 55-62 [PubMed: 10445027] http://dx.doi.org/10.1016/S1097-2765(00)80187-2
	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

InterPro 23.1