query: gene_exact:Spcs2 AND organism_id:10090

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Microsomal signal peptidase 25 kDa subunit

value: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity)

value: Component of the signal peptidase complex paralog A (SPC-A) composed of a catalytic subunit SEC11A and three accessory subunits SPCS1, SPCS2 and SPCS3. Component of the signal peptidase complex paralog C (SPC-C) composed of a catalytic subunit SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex, interacts with SEC11A or SEC11C and SPCS1. The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids

description: Removed

description: Signal peptidase complex subunit 2

description: Cytoplasmic

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Disordered

description: Gly residues

description: N-acetylalanine

description: in Ref. 2; AAH50150

description: in Ref. 1; BAB29262

authors:
Carninci P.
Kasukawa T.
Katayama S.
Gough J.
Frith M.C.
Maeda N.
Oyama R.
Ravasi T.
Lenhard B.
Wells C.
Kodzius R.
Shimokawa K.
Bajic V.B.
Brenner S.E.
Batalov S.
Forrest A.R.
Zavolan M.
Davis M.J.
Wilming L.G.
Aidinis V.
Allen J.E.
Ambesi-Impiombato A.
Apweiler R.
Aturaliya R.N.
Bailey T.L.
Bansal M.
Baxter L.
Beisel K.W.
Bersano T.
Bono H.
Chalk A.M.
Chiu K.P.
Choudhary V.
Christoffels A.
Clutterbuck D.R.
Crowe M.L.
Dalla E.
Dalrymple B.P.
de Bono B.
Della Gatta G.
di Bernardo D.
Down T.
Engstrom P.
Fagiolini M.
Faulkner G.
Fletcher C.F.
Fukushima T.
Furuno M.
Futaki S.
Gariboldi M.
Georgii-Hemming P.
Gingeras T.R.
Gojobori T.
Green R.E.
Gustincich S.
Harbers M.
Hayashi Y.
Hensch T.K.
Hirokawa N.
Hill D.
Huminiecki L.
Iacono M.
Ikeo K.
Iwama A.
Ishikawa T.
Jakt M.
Kanapin A.
Katoh M.
Kawasawa Y.
Kelso J.
Kitamura H.
Kitano H.
Kollias G.
Krishnan S.P.
Kruger A.
Kummerfeld S.K.
Kurochkin I.V.
Lareau L.F.
Lazarevic D.
Lipovich L.
Liu J.
Liuni S.
McWilliam S.
Madan Babu M.
Madera M.
Marchionni L.
Matsuda H.
Matsuzawa S.
Miki H.
Mignone F.
Miyake S.
Morris K.
Mottagui-Tabar S.
Mulder N.
Nakano N.
Nakauchi H.
Ng P.
Nilsson R.
Nishiguchi S.
Nishikawa S.
Nori F.
Ohara O.
Okazaki Y.
Orlando V.
Pang K.C.
Pavan W.J.
Pavesi G.
Pesole G.
Petrovsky N.
Piazza S.
Reed J.
Reid J.F.
Ring B.Z.
Ringwald M.
Rost B.
Ruan Y.
Salzberg S.L.
Sandelin A.
Schneider C.
Schoenbach C.
Sekiguchi K.
Semple C.A.
Seno S.
Sessa L.
Sheng Y.
Shibata Y.
Shimada H.
Shimada K.
Silva D.
Sinclair B.
Sperling S.
Stupka E.
Sugiura K.
Sultana R.
Takenaka Y.
Taki K.
Tammoja K.
Tan S.L.
Tang S.
Taylor M.S.
Tegner J.
Teichmann S.A.
Ueda H.R.
van Nimwegen E.
Verardo R.
Wei C.L.
Yagi K.
Yamanishi H.
Zabarovsky E.
Zhu S.
Zimmer A.
Hide W.
Bult C.
Grimmond S.M.
Teasdale R.D.
Liu E.T.
Brusic V.
Quackenbush J.
Wahlestedt C.
Mattick J.S.
Hume D.A.
Kai C.
Sasaki D.
Tomaru Y.
Fukuda S.
Kanamori-Katayama M.
Suzuki M.
Aoki J.
Arakawa T.
Iida J.
Imamura K.
Itoh M.
Kato T.
Kawaji H.
Kawagashira N.
Kawashima T.
Kojima M.
Kondo S.
Konno H.
Nakano K.
Ninomiya N.
Nishio T.
Okada M.
Plessy C.
Shibata K.
Shiraki T.
Suzuki S.
Tagami M.
Waki K.
Watahiki A.
Okamura-Oho Y.
Suzuki H.
Kawai J.
Hayashizaki Y.

title: The transcriptional landscape of the mammalian genome.

title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

authors:
Trinidad J.C.
Specht C.G.
Thalhammer A.
Schoepfer R.
Burlingame A.L.

title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.

referencePositions: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2

referencePositions: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Huttlin E.L.
Jedrychowski M.P.
Elias J.E.
Goswami T.
Rad R.
Beausoleil S.A.
Villen J.
Haas W.
Sowa M.E.
Gygi S.P.

title: A tissue-specific atlas of mouse protein phosphorylation and expression.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

value: Synthesis, secretion, and deacylation of Ghrelin

value: Regulation of CDH1 posttranslational processing and trafficking to plasma membrane

value: Expressed in lacrimal gland and 260 other cell types or tissues

value: MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site

value: Component of the signal peptidase complex paralog A (SPC-A) composed of a catalytic subunit SEC11A and three accessory subunits SPCS1, SPCS2 and SPCS3. Component of the signal peptidase complex paralog C (SPC-C) composed of a catalytic subunit SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex, interacts with SEC11A or SEC11C and SPCS1. The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids

value: Lacks conserved residue(s) required for the propagation of feature annotation

description: Helical

authors:
Church D.M.
Goodstadt L.
Hillier L.W.
Zody M.C.
Goldstein S.
She X.
Bult C.J.
Agarwala R.
Cherry J.L.
DiCuccio M.
Hlavina W.
Kapustin Y.
Meric P.
Maglott D.
Birtle Z.
Marques A.C.
Graves T.
Zhou S.
Teague B.
Potamousis K.
Churas C.
Place M.
Herschleb J.
Runnheim R.
Forrest D.
Amos-Landgraf J.
Schwartz D.C.
Cheng Z.
Lindblad-Toh K.
Eichler E.E.
Ponting C.P.

title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Huttlin E.L.
Jedrychowski M.P.
Elias J.E.
Goswami T.
Rad R.
Beausoleil S.A.
Villen J.
Haas W.
Sowa M.E.
Gygi S.P.

title: A tissue-specific atlas of mouse protein phosphorylation and expression.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Church D.M.
Schneider V.A.
Graves T.
Auger K.
Cunningham F.
Bouk N.
Chen H.C.
Agarwala R.
McLaren W.M.
Ritchie G.R.
Albracht D.
Kremitzki M.
Rock S.
Kotkiewicz H.
Kremitzki C.
Wollam A.
Trani L.
Fulton L.
Fulton R.
Matthews L.
Whitehead S.
Chow W.
Torrance J.
Dunn M.
Harden G.
Threadgold G.
Wood J.
Collins J.
Heath P.
Griffiths G.
Pelan S.
Grafham D.
Eichler E.E.
Weinstock G.
Mardis E.R.
Wilson R.K.
Howe K.
Flicek P.
Hubbard T.

title: Modernizing reference genome assemblies.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

value: Expressed in lacrimal gland and 260 other cell types or tissues

value: MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site

value: Component of the signal peptidase complex paralog A (SPC-A) composed of a catalytic subunit SEC11A and three accessory subunits SPCS1, SPCS2 and SPCS3. Component of the signal peptidase complex paralog C (SPC-C) composed of a catalytic subunit SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex, interacts with SEC11A or SEC11C and SPCS1. The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids

description: Helical

description: Helical

description: Disordered

description: Gly residues

authors:
Trinidad J.C.
Specht C.G.
Thalhammer A.
Schoepfer R.
Burlingame A.L.

title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Church D.M.
Goodstadt L.
Hillier L.W.
Zody M.C.
Goldstein S.
She X.
Bult C.J.
Agarwala R.
Cherry J.L.
DiCuccio M.
Hlavina W.
Kapustin Y.
Meric P.
Maglott D.
Birtle Z.
Marques A.C.
Graves T.
Zhou S.
Teague B.
Potamousis K.
Churas C.
Place M.
Herschleb J.
Runnheim R.
Forrest D.
Amos-Landgraf J.
Schwartz D.C.
Cheng Z.
Lindblad-Toh K.
Eichler E.E.
Ponting C.P.

title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Huttlin E.L.
Jedrychowski M.P.
Elias J.E.
Goswami T.
Rad R.
Beausoleil S.A.
Villen J.
Haas W.
Sowa M.E.
Gygi S.P.

title: A tissue-specific atlas of mouse protein phosphorylation and expression.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Church D.M.
Schneider V.A.
Graves T.
Auger K.
Cunningham F.
Bouk N.
Chen H.C.
Agarwala R.
McLaren W.M.
Ritchie G.R.
Albracht D.
Kremitzki M.
Rock S.
Kotkiewicz H.
Kremitzki C.
Wollam A.
Trani L.
Fulton L.
Fulton R.
Matthews L.
Whitehead S.
Chow W.
Torrance J.
Dunn M.
Harden G.
Threadgold G.
Wood J.
Collins J.
Heath P.
Griffiths G.
Pelan S.
Grafham D.
Eichler E.E.
Weinstock G.
Mardis E.R.
Wilson R.K.
Howe K.
Flicek P.
Hubbard T.

title: Modernizing reference genome assemblies.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

value: Expressed in lacrimal gland and 260 other cell types or tissues

value: MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site

value: Component of the signal peptidase complex paralog A (SPC-A) composed of a catalytic subunit SEC11A and three accessory subunits SPCS1, SPCS2 and SPCS3. Component of the signal peptidase complex paralog C (SPC-C) composed of a catalytic subunit SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex, interacts with SEC11A or SEC11C and SPCS1. The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids

description: Helical

description: Helical

description: Disordered

description: Gly residues

authors:
Trinidad J.C.
Specht C.G.
Thalhammer A.
Schoepfer R.
Burlingame A.L.

title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Church D.M.
Goodstadt L.
Hillier L.W.
Zody M.C.
Goldstein S.
She X.
Bult C.J.
Agarwala R.
Cherry J.L.
DiCuccio M.
Hlavina W.
Kapustin Y.
Meric P.
Maglott D.
Birtle Z.
Marques A.C.
Graves T.
Zhou S.
Teague B.
Potamousis K.
Churas C.
Place M.
Herschleb J.
Runnheim R.
Forrest D.
Amos-Landgraf J.
Schwartz D.C.
Cheng Z.
Lindblad-Toh K.
Eichler E.E.
Ponting C.P.

title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Huttlin E.L.
Jedrychowski M.P.
Elias J.E.
Goswami T.
Rad R.
Beausoleil S.A.
Villen J.
Haas W.
Sowa M.E.
Gygi S.P.

title: A tissue-specific atlas of mouse protein phosphorylation and expression.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Church D.M.
Schneider V.A.
Graves T.
Auger K.
Cunningham F.
Bouk N.
Chen H.C.
Agarwala R.
McLaren W.M.
Ritchie G.R.
Albracht D.
Kremitzki M.
Rock S.
Kotkiewicz H.
Kremitzki C.
Wollam A.
Trani L.
Fulton L.
Fulton R.
Matthews L.
Whitehead S.
Chow W.
Torrance J.
Dunn M.
Harden G.
Threadgold G.
Wood J.
Collins J.
Heath P.
Griffiths G.
Pelan S.
Grafham D.
Eichler E.E.
Weinstock G.
Mardis E.R.
Wilson R.K.
Howe K.
Flicek P.
Hubbard T.

title: Modernizing reference genome assemblies.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

value: Expressed in lacrimal gland and 260 other cell types or tissues

value: MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site

value: Component of the signal peptidase complex paralog A (SPC-A) composed of a catalytic subunit SEC11A and three accessory subunits SPCS1, SPCS2 and SPCS3. Component of the signal peptidase complex paralog C (SPC-C) composed of a catalytic subunit SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex, interacts with SEC11A or SEC11C and SPCS1. The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids

description: Helical

description: Helical

authors:
Church D.M.
Goodstadt L.
Hillier L.W.
Zody M.C.
Goldstein S.
She X.
Bult C.J.
Agarwala R.
Cherry J.L.
DiCuccio M.
Hlavina W.
Kapustin Y.
Meric P.
Maglott D.
Birtle Z.
Marques A.C.
Graves T.
Zhou S.
Teague B.
Potamousis K.
Churas C.
Place M.
Herschleb J.
Runnheim R.
Forrest D.
Amos-Landgraf J.
Schwartz D.C.
Cheng Z.
Lindblad-Toh K.
Eichler E.E.
Ponting C.P.

title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Huttlin E.L.
Jedrychowski M.P.
Elias J.E.
Goswami T.
Rad R.
Beausoleil S.A.
Villen J.
Haas W.
Sowa M.E.
Gygi S.P.

title: A tissue-specific atlas of mouse protein phosphorylation and expression.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Church D.M.
Schneider V.A.
Graves T.
Auger K.
Cunningham F.
Bouk N.
Chen H.C.
Agarwala R.
McLaren W.M.
Ritchie G.R.
Albracht D.
Kremitzki M.
Rock S.
Kotkiewicz H.
Kremitzki C.
Wollam A.
Trani L.
Fulton L.
Fulton R.
Matthews L.
Whitehead S.
Chow W.
Torrance J.
Dunn M.
Harden G.
Threadgold G.
Wood J.
Collins J.
Heath P.
Griffiths G.
Pelan S.
Grafham D.
Eichler E.E.
Weinstock G.
Mardis E.R.
Wilson R.K.
Howe K.
Flicek P.
Hubbard T.

title: Modernizing reference genome assemblies.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

value: Expressed in lacrimal gland and 260 other cell types or tissues

value: MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site

value: Component of the signal peptidase complex paralog A (SPC-A) composed of a catalytic subunit SEC11A and three accessory subunits SPCS1, SPCS2 and SPCS3. Component of the signal peptidase complex paralog C (SPC-C) composed of a catalytic subunit SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex, interacts with SEC11A or SEC11C and SPCS1. The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids

description: Helical

description: Helical

description: Disordered

description: Gly residues

authors:
Church D.M.
Goodstadt L.
Hillier L.W.
Zody M.C.
Goldstein S.
She X.
Bult C.J.
Agarwala R.
Cherry J.L.
DiCuccio M.
Hlavina W.
Kapustin Y.
Meric P.
Maglott D.
Birtle Z.
Marques A.C.
Graves T.
Zhou S.
Teague B.
Potamousis K.
Churas C.
Place M.
Herschleb J.
Runnheim R.
Forrest D.
Amos-Landgraf J.
Schwartz D.C.
Cheng Z.
Lindblad-Toh K.
Eichler E.E.
Ponting C.P.

title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Huttlin E.L.
Jedrychowski M.P.
Elias J.E.
Goswami T.
Rad R.
Beausoleil S.A.
Villen J.
Haas W.
Sowa M.E.
Gygi S.P.

title: A tissue-specific atlas of mouse protein phosphorylation and expression.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Church D.M.
Schneider V.A.
Graves T.
Auger K.
Cunningham F.
Bouk N.
Chen H.C.
Agarwala R.
McLaren W.M.
Ritchie G.R.
Albracht D.
Kremitzki M.
Rock S.
Kotkiewicz H.
Kremitzki C.
Wollam A.
Trani L.
Fulton L.
Fulton R.
Matthews L.
Whitehead S.
Chow W.
Torrance J.
Dunn M.
Harden G.
Threadgold G.
Wood J.
Collins J.
Heath P.
Griffiths G.
Pelan S.
Grafham D.
Eichler E.E.
Weinstock G.
Mardis E.R.
Wilson R.K.
Howe K.
Flicek P.
Hubbard T.

title: Modernizing reference genome assemblies.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

value: Expressed in lacrimal gland and 260 other cell types or tissues

value: MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus

value: Signal peptidase complex subunit 2 homolog (S. cerevisiae)

description: Disordered

description: Gly residues

description: Basic and acidic residues

description: Basic residues

authors:
Trinidad J.C.
Specht C.G.
Thalhammer A.
Schoepfer R.
Burlingame A.L.

title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Church D.M.
Goodstadt L.
Hillier L.W.
Zody M.C.
Goldstein S.
She X.
Bult C.J.
Agarwala R.
Cherry J.L.
DiCuccio M.
Hlavina W.
Kapustin Y.
Meric P.
Maglott D.
Birtle Z.
Marques A.C.
Graves T.
Zhou S.
Teague B.
Potamousis K.
Churas C.
Place M.
Herschleb J.
Runnheim R.
Forrest D.
Amos-Landgraf J.
Schwartz D.C.
Cheng Z.
Lindblad-Toh K.
Eichler E.E.
Ponting C.P.

title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Church D.M.
Schneider V.A.
Graves T.
Auger K.
Cunningham F.
Bouk N.
Chen H.C.
Agarwala R.
McLaren W.M.
Ritchie G.R.
Albracht D.
Kremitzki M.
Rock S.
Kotkiewicz H.
Kremitzki C.
Wollam A.
Trani L.
Fulton L.
Fulton R.
Matthews L.
Whitehead S.
Chow W.
Torrance J.
Dunn M.
Harden G.
Threadgold G.
Wood J.
Collins J.
Heath P.
Griffiths G.
Pelan S.
Grafham D.
Eichler E.E.
Weinstock G.
Mardis E.R.
Wilson R.K.
Howe K.
Flicek P.
Hubbard T.

title: Modernizing reference genome assemblies.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

value: Expressed in lacrimal gland and 260 other cell types or tissues


query: gene_exact:C28G1.2 AND organism_id:6239

lineage: Eukaryota Metazoa Ecdysozoa Nematoda Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis

description: Serpin

title: Genome sequence of the nematode C. elegans: a platform for investigating biology.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

value: Collagen biosynthesis and modifying enzymes

value: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)

value: Regulation of FXIIa and plasma kallikrein activity


query: gene_exact:vps13b AND organism_id:284812

scientificName: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

lineage: Eukaryota Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces

value: Intermembrane lipid transfer protein vps1302

value: Vacuolar protein sorting-associated protein 13b

value: Mediates the transfer of lipids between membranes at organelle contact sites (By similarity). May play a role in mitochondrial lipid homeostasis, Golgi vesicle transport, reticulophagy, actin cytoskeleton organization and formation of the forespore membrane (By similarity)

description: Intermembrane lipid transfer protein vps1302

description: Chorein N-terminal

description: SHR-BD

description: Disordered

description: Basic and acidic residues

description: in Ref. 2; BAA13854

description: in Ref. 2; BAA13854

description: in Ref. 2; BAA13854

authors:
Wood V.
Gwilliam R.
Rajandream M.A.
Lyne M.H.
Lyne R.
Stewart A.
Sgouros J.G.
Peat N.
Hayles J.
Baker S.G.
Basham D.
Bowman S.
Brooks K.
Brown D.
Brown S.
Chillingworth T.
Churcher C.M.
Collins M.
Connor R.
Cronin A.
Davis P.
Feltwell T.
Fraser A.
Gentles S.
Goble A.
Hamlin N.
Harris D.E.
Hidalgo J.
Hodgson G.
Holroyd S.
Hornsby T.
Howarth S.
Huckle E.J.
Hunt S.
Jagels K.
James K.D.
Jones L.
Jones M.
Leather S.
McDonald S.
McLean J.
Mooney P.
Moule S.
Mungall K.L.
Murphy L.D.
Niblett D.
Odell C.
Oliver K.
O'Neil S.
Pearson D.
Quail M.A.
Rabbinowitsch E.
Rutherford K.M.
Rutter S.
Saunders D.
Seeger K.
Sharp S.
Skelton J.
Simmonds M.N.
Squares R.
Squares S.
Stevens K.
Taylor K.
Taylor R.G.
Tivey A.
Walsh S.V.
Warren T.
Whitehead S.
Woodward J.R.
Volckaert G.
Aert R.
Robben J.
Grymonprez B.
Weltjens I.
Vanstreels E.
Rieger M.
Schaefer M.
Mueller-Auer S.
Gabel C.
Fuchs M.
Duesterhoeft A.
Fritzc C.
Holzer E.
Moestl D.
Hilbert H.
Borzym K.
Langer I.
Beck A.
Lehrach H.
Reinhardt R.
Pohl T.M.
Eger P.
Zimmermann W.
Wedler H.
Wambutt R.
Purnelle B.
Goffeau A.
Cadieu E.
Dreano S.
Gloux S.
Lelaure V.
Mottier S.
Galibert F.
Aves S.J.
Xiang Z.
Hunt C.
Moore K.
Hurst S.M.
Lucas M.
Rochet M.
Gaillardin C.
Tallada V.A.
Garzon A.
Thode G.
Daga R.R.
Cruzado L.
Jimenez J.
Sanchez M.
del Rey F.
Benito J.
Dominguez A.
Revuelta J.L.
Moreno S.
Armstrong J.
Forsburg S.L.
Cerutti L.
Lowe T.
McCombie W.R.
Paulsen I.
Potashkin J.
Shpakovski G.V.
Ussery D.
Barrell B.G.
Nurse P.

title: The genome sequence of Schizosaccharomyces pombe.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

authors:
Yoshioka S.
Kato K.
Nakai K.
Okayama H.
Nojima H.

title: Identification of open reading frames in Schizosaccharomyces pombe cDNAs.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2999-3131

value: INTERMEMBRANE LIPID TRANSFER PROTEIN VPS13

value: VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS13


title: Meiotic spindle pole bodies acquire the ability to assemble the spore plasma membrane by sequential recruitment of sporulation-specific components in fission yeast.

authorString: Nakase Y, Nakamura-Kubo M, Ye Y, Hirata A, Shimoda C, Nakamura T.

affiliation: Department of Biology, Graduate School of Science, Osaka City University, Osaka 558-8585, Japan.

title: Molecular biology of the cell

abstractText: The spindle pole body (SPB) of Schizosaccharomyces pombe is required for assembly of the forespore membrane (FSM) during meiosis. Before de novo biogenesis of the FSM, the meiotic SPB forms outer plaques, an event referred to as SPB modification. A constitutive SPB component, Spo15, plays an indispensable role in SPB modification and sporulation. Here, we analyzed two sporulation-specific genes, spo13(+) and spo2(+), which are not required for progression of meiotic nuclear divisions, but are essential for sporulation. Spo13 is a 16-kDa coiled-coil protein, and Spo2 is a 15-kDa nonconserved protein. Both Spo13 and Spo2 specifically associated with the meiotic SPB. The respective deletion mutants are viable, but defective in SPB modification and in the onset of FSM formation. Spo13 and Spo2 localized on the cytoplasmic side of the SPB in close contact with the nascent FSM. Localization of Spo13 to the SPB was dependent on Spo15 and Spo2; that of Spo2 depended only on Spo15, suggesting that their recruitment to the SPB is strictly controlled. Spo2 physically associated with both Spo15 and Spo13, but Spo13 and Spo15 did not interact directly. Taken together, these observations indicate that Spo2 is recruited to the SPB during meiosis and then assists in the localization of Spo13 to the outer surface of the SPB.

affiliation: Department of Biology, Graduate School of Science, Osaka City University, Osaka 558-8585, Japan.

pubType:
Research Support, Non-U.S. Gov't
research-article
Journal Article


title: E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification.

authorString: Huang DT, Ayrault O, Hunt HW, Taherbhoy AM, Duda DM, Scott DC, Borg LA, Neale G, Murray PJ, Roussel MF, Schulman BA.

affiliation: Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.

title: Molecular cell

abstractText: Ubiquitin and ubiquitin-like proteins (UBLs) are directed to targets by cascades of E1, E2, and E3 enzymes. The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, -2, -3, -4, or -5) and RING proteins (RBX1 or -2). CRLs are activated by ligation of the UBL NEDD8 to a conserved cullin lysine. How is cullin NEDD8ylation specificity established? Here we report that, like UBE2M (also known as UBC12), the previously uncharacterized E2 UBE2F is a NEDD8-conjugating enzyme in vitro and in vivo. Biochemical and structural analyses indicate how plasticity of hydrophobic E1-E2 interactions and E1 conformational flexibility allow one E1 to charge multiple E2s. The E2s have distinct functions, with UBE2M/RBX1 and UBE2F/RBX2 displaying different target cullin specificities. Together, these studies reveal the molecular basis for and functional importance of hierarchical expansion of the NEDD8 conjugation system in establishing selective CRL activation.

affiliation: Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.

pubType: Research Support, U.S. Gov't, Non-P.H.S.


title: Inhibition of a NEDD8 Cascade Restores Restriction of HIV by APOBEC3G.

authorString: Stanley DJ, Bartholomeeusen K, Crosby DC, Kim DY, Kwon E, Yen L, Cartozo NC, Li M, Jäger S, Mason-Herr J, Hayashi F, Yokoyama S, Krogan NJ, Harris RS, Peterlin BM, Gross JD.

affiliation: Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, United States of America.

title: PLoS pathogens

abstractText: Cellular restriction factors help to defend humans against human immunodeficiency virus (HIV). HIV accessory proteins hijack at least three different Cullin-RING ubiquitin ligases, which must be activated by the small ubiquitin-like protein NEDD8, in order to counteract host cellular restriction factors. We found that conjugation of NEDD8 to Cullin-5 by the NEDD8-conjugating enzyme UBE2F is required for HIV Vif-mediated degradation of the host restriction factor APOBEC3G (A3G). Pharmacological inhibition of the NEDD8 E1 by MLN4924 or knockdown of either UBE2F or its RING-protein binding partner RBX2 bypasses the effect of Vif, restoring the restriction of HIV by A3G. NMR mapping and mutational analyses define specificity determinants of the UBE2F NEDD8 cascade. These studies demonstrate that disrupting host NEDD8 cascades presents a novel antiretroviral therapeutic approach enhancing the ability of the immune system to combat HIV.

affiliation: Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, United States of America.

pubType:
Research Support, Non-U.S. Gov't
research-article
Journal Article
Research Support, N.I.H., Extramural

descriptorName: vif Gene Products, Human Immunodeficiency Virus

name: vif Gene Products, Human Immunodeficiency Virus