commentType: FUNCTION

source: PubMed

value: Involved in sporulation. Plays a significant role in modification of the spindle pole body prior to spore formation and is required for initiating forespore membrane formation. Assists in the localization of spo13 to the outer surface of the SPB

commentType: SUBUNIT

value: Interacts with spo13 and spo15

commentType: SUBCELLULAR LOCATION

value: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body

commentType: INDUCTION

value: Induced during meiosis by the transcription factor mei4. Protein levels rapidly increase during meiosis and then decline

commentType: MISCELLANEOUS

value: The sequence is 100 percent identical to the C-terminus of vps13b

commentType: SIMILARITY

value: Belongs to the VPS13 family

entryType: UniProtKB reviewed (Swiss-Prot)

description: Sporulation-specific protein 2

modifier: EXACT

type: Chain

Cytoplasm

category: Cellular component

Meiosis

category: Biological process

Reference proteome

category: Technical term

commonName: Fission yeast

lineage: Eukaryota Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces

scientificName: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

value: Sporulation-specific protein 2

proteinExistence: 1: Evidence at protein level

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.

database: PubMed

database: DOI

citationType: journal article

journal: Nature

title: The genome sequence of Schizosaccharomyces pombe.

type: STRAIN

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

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

journal: Mol. Biol. Cell

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

referencePositions:
FUNCTION
INDUCTION
SUBCELLULAR LOCATION
INTERACTION WITH SPO13 AND SPO15

database: EMBL

key: ProteinId

key: Status

key: MoleculeType

database: AlphaFoldDB

key: Description

database: SMR

database: BioGRID

key: Interactions

database: STRING

database: PaxDb

database: PomBase

key: GeneName

database: VEuPathDB

database: eggNOG

key: ToxonomicScope

value: Eukaryota

database: HOGENOM

database: InParanoid

database: OMA

key: Fingerprint

database: PRO

database: Proteomes

key: Component

value: Chromosome II

database: GO

key: GoTerm

value: C:meiotic spindle pole body

key: GoEvidenceType

value: P:ascospore formation

value: P:ascospore-type prospore-specific spindle pole body remodeling


value: Nucleus

value: Belongs to the peptidase C48 family

description: Ubiquitin-like-specific protease 2

description: Disordered

source: SAM

type: Region

description: Disordered

description: Disordered

description: Basic and acidic residues

type: Compositional bias

description: Polar residues

description: Low complexity

description: Polar residues

description: Polar residues

description: Acidic residues

type: Active site

description: Phosphothreonine

type: Modified residue

Hydrolase

category: Molecular function

Phosphoprotein

category: PTM

value: Ubiquitin-like-specific protease 2

database: PubMed

authors:
Rhind N.
Chen Z.
Yassour M.
Thompson D.A.
Haas B.J.
Habib N.
Wapinski I.
Roy S.
Lin M.F.
Heiman D.I.
Young S.K.
Furuya K.
Guo Y.
Pidoux A.
Chen H.M.
Robbertse B.
Goldberg J.M.
Aoki K.
Bayne E.H.
Berlin A.M.
Desjardins C.A.
Dobbs E.
Dukaj L.
Fan L.
FitzGerald M.G.
French C.
Gujja S.
Hansen K.
Keifenheim D.
Levin J.Z.
Mosher R.A.
Mueller C.A.
Pfiffner J.
Priest M.
Russ C.
Smialowska A.
Swoboda P.
Sykes S.M.
Vaughn M.
Vengrova S.
Yoder R.
Zeng Q.
Allshire R.
Baulcombe D.
Birren B.W.
Brown W.
Ekwall K.
Kellis M.
Leatherwood J.
Levin H.
Margalit H.
Martienssen R.
Nieduszynski C.A.
Spatafora J.W.
Friedman N.
Dalgaard J.Z.
Baumann P.
Niki H.
Regev A.
Nusbaum C.

journal: Science

title: Comparative functional genomics of the fission yeasts.

citationType: submission

submissionDatabase: UniProtKB

authors:
Matsuyama A.
Arai R.
Yashiroda Y.
Shirai A.
Kamata A.
Sekido S.
Kobayashi Y.
Hashimoto A.
Hamamoto M.
Hiraoka Y.
Horinouchi S.
Yoshida M.

journal: Nat. Biotechnol.

title: ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.

referencePositions: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]

authors:
Wilson-Grady J.T.
Villen J.
Gygi S.P.

journal: J. Proteome Res.

title: Phosphoproteome analysis of fission yeast.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526

database: PIR

key: EntryName

database: RefSeq

key: NucleotideSequenceId


value: tRNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in tRNAs at position 49 and 50 (PubMed:30646830). Trm4a and trm4b methylate different sets of tRNAs (PubMed:30646830). Also methylates cytosine to m5C at positions (60, 61 and 62) in tRNA(Asp) (PubMed:23074192)

commentType: CATALYTIC ACTIVITY

directionType: left-to-right

database: Rhea

name: cytidine(49) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(49) in tRNA precursor + S-adenosyl-L-homocysteine + H(+)

database: ChEBI

name: cytidine(50) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(50) in tRNA + S-adenosyl-L-homocysteine + H(+)

name: cytidine(60) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(60) in tRNA(Asp) + S-adenosyl-L-homocysteine + H(+)

name: cytidine(61) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(61) in tRNA(Asp) + S-adenosyl-L-homocysteine + H(+)

name: cytidine(62) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(62) in tRNA(Asp) + S-adenosyl-L-homocysteine + H(+)

commentType: DISRUPTION PHENOTYPE

value: Cells lacking both trm4a and trm4b show a mild resistance to calcium chloride

source: PROSITE-ProRule

value: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. TRM4 subfamily

description: Multisite-specific tRNA:(cytosine-C(5))-methyltransferase trm4b

description: Nucleophile

type: Binding site

authors:
Becker M.
Muller S.
Nellen W.
Jurkowski T.P.
Jeltsch A.
Ehrenhofer-Murray A.E.

title: Pmt1, a Dnmt2 homolog in Schizosaccharomyces pombe, mediates tRNA methylation in response to nutrient signaling.

authors:
Mueller M.
Samel-Pommerencke A.
Legrand C.
Tuorto F.
Lyko F.
Ehrenhofer-Murray A.E.

title: Division of labour: tRNA methylation by the NSun2 tRNA methyltransferases Trm4a and Trm4b in fission yeast.

referencePositions:
FUNCTION
CATALYTIC ACTIVITY
DISRUPTION PHENOTYPE

value: NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING


value: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Combines in the mitochondrion with mitochondrial transcription factor mtf1 as a holoenzyme to recognize and initiate transcription at the core mitochondrial promoters

name: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate

value: Mitochondrion

value: Belongs to the phage and mitochondrial RNA polymerase family

description: Mitochondrion

type: Transit peptide

description: DNA-directed RNA polymerase, mitochondrial

description: Disordered

description: Basic and acidic residues

Transit peptide

category: Domain

flag: Precursor

proteinExistence: 3: Inferred from homology

database: DOI

authors:
Jiang H.
Sun W.
Wang Z.
Zhang J.
Chen D.
Murchie A.I.

journal: Nucleic Acids Res.

title: Identification and characterization of the mitochondrial RNA polymerase and transcription factor in the fission yeast Schizosaccharomyces pombe.

database: EMBL

database: AlphaFoldDB

database: SMR

database: BioGRID

database: FunCoup

key: Number of interactors

database: iPTMnet

database: GeneID

database: KEGG

value: C:mitochondrial DNA-directed RNA polymerase complex

value: F:mitochondrial promoter sequence-specific DNA binding

value: P:transcription initiation at mitochondrial promoter

value: 5' to 3' exonuclease, C-terminal subdomain

value: DNA-directed RNA polymerase, N-terminal domain

value: DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL


value: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 3 binds ATP. Also involved in replication and DNA damage checkpoint controls, probably functioning as a checkpoint sensor

value: Heteropentamer of subunits rfc1, rfc2, rfc3, rfc4 and rfc5 that forms a complex (RFC) with PCNA in the presence of ATP. Two other complexes exist where rfc1 can be replaced by either ctf18 or elg1 to form the ctf18-RFC or the elg1-RFC complexes respectively

value: Belongs to the activator 1 small subunits family

description: Replication factor C subunit 3

originalSequence: R

description: Defective DNA replication.

type: Mutagenesis

ATP-binding

category: Ligand

value: Replication factor C subunit 3

value: Replication factor C3

authors:
Shimada M.
Okuzaki D.
Tanaka S.
Tougan T.
Tamai K.K.
Shimoda C.
Nojima H.

title: Replication factor C3 of Schizosaccharomyces pombe, a small subunit of replication factor C complex, plays a role in both replication and damage checkpoints.

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]

authors:
Gray F.C.
MacNeill S.A.

journal: Curr. Genet.

title: The Schizosaccharomyces pombe rfc3+ gene encodes a homologue of the human hRFC36 and Saccharomyces cerevisiae Rfc3 subunits of replication factor C.

authors:
Kim J.
Robertson K.
Mylonas K.J.L.
Gray F.C.
Charapitsa I.
MacNeill S.A.

title: Contrasting effects of Elg1-RFC and Ctf18-RFC inactivation in the absence of fully functional RFC in fission yeast.

value: mRNA

database: ComplexPortal

value: DNA replication factor C complex, rad17 variant

value: DNA replication factor C complex, ctf18 variant

value: DNA replication factor C complex, elg1 variant

value: DNA replication factor C complex, RFC1 variant

database: STRING

database: PaxDb

database: PomBase

database: VEuPathDB

database: eggNOG

value: Eukaryota

database: HOGENOM

database: InParanoid

value: Recognition of DNA damage by PCNA-containing replication complex

value: Activation of ATR in response to replication stress

value: PCNA-Dependent Long Patch Base Excision Repair

value: Termination of translesion DNA synthesis

value: Gap-filling DNA repair synthesis and ligation in GG-NER

value: Gap-filling DNA repair synthesis and ligation in TC-NER

value: P:DNA strand elongation involved in mitotic DNA replication

value: P:mitotic DNA replication leading strand elongation

value: P-loop containing nucleotide triphosphate hydrolases

value: REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT

value: P-loop containing nucleoside triphosphate hydrolases


value: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors

value: Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits

value: Nucleus, nucleolus

value: Belongs to the eukaryotic RPA49/POLR1E RNA polymerase subunit family

description: DNA-directed RNA polymerase I subunit rpa49

description: Disordered

description: Basic and acidic residues

value: DNA-directed RNA polymerase I 49 kDa polypeptide

value: RNA polymerase I subunit A49

proteinExistence: 2: Evidence at transcript level

authors:
Shematorova E.K.
Shpakovski G.V.

submissionDatabase: EMBL/GenBank/DDBJ databases

title: Molecular cloning and complementation studies of the fission yeast genes encoding subunits Rpa12 and Rpa49 specific for nuclear RNA polymerase I.

database: PubMed

database: DOI

value: mRNA

database: PIR

database: RefSeq

database: OMA

database: PhylomeDB

database: Reactome

key: PathwayName

value: RNA Polymerase I Transcription Initiation

value: RNA Polymerase I Promoter Escape

database: PRO

database: Proteomes

value: Chromosome I

database: GO

value: P:RNA polymerase I preinitiation complex assembly

value: P:transcription elongation by RNA polymerase I

value: DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA49


value: Binds to centromeric K-type repeat DNA and ARS3002 DNA. The CBH-binding consensus sequence is Py-Pu-A-T-A-T-Py-Pu-T-A

value: Nucleus

value: Chromosome, centromere

description: CENP-B homolog protein 1

description: HTH CENPB-type

type: Domain

originalSequence: I

description: in Ref. 1; AAB80698

type: Sequence conflict

value: cbh

value: CENP-B homolog protein 1

authors:
Lee J.-K.
Huberman J.A.
Hurwitz J.

journal: Proc. Natl. Acad. Sci. U.S.A.

title: Purification and characterization of a CENP-B homologue protein that binds to the centromeric K-type repeat DNA of Schizosaccharomyces pombe.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA]
PARTIAL PROTEIN SEQUENCE
FUNCTION

database: EMBL

database: AlphaFoldDB

database: SMR

database: BioGRID

database: FunCoup

database: IntAct

database: STRING

database: iPTMnet

database: GeneID

database: KEGG

value: Eukaryota

value: C:condensed chromosome, centromeric region


value: Cytoplasm

commentType: SEQUENCE CAUTION

sequenceCautionType: Erroneous gene model prediction

description: Uncharacterized WD repeat-containing protein C27B12.05

description: WD 1

type: Repeat

description: WD 2

proteinExistence: 4: Predicted

authors:
Machida M.
Yamazaki S.
Kunihiro S.
Tanaka T.
Kushida N.
Jinno K.
Haikawa Y.
Yamazaki J.
Yamamoto S.
Sekine M.
Oguchi A.
Nagai Y.
Sakai M.
Aoki K.
Ogura K.
Kudoh Y.
Kikuchi H.
Zhang M.Q.
Yanagida M.

database: PubMed

database: DOI

journal: Yeast

title: A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment.

database: PIR

database: PaxDb

database: PomBase

database: VEuPathDB

database: eggNOG

database: HOGENOM

database: InParanoid

value: Chromosome II

value: P:nonfunctional rRNA decay

database: FunFam

value: YVTN repeat-like/Quinoprotein amine dehydrogenase


source: UniProtKB

value: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane

value: Component of the mitochondrial small ribosomal subunit (mt-SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and at least 32 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and at least 45 different proteins

value: Mitochondrion

value: Belongs to the universal ribosomal protein uS13 family

description: Small ribosomal subunit protein uS13m

value: 37S ribosomal protein subunit sws2, mitochondrial

value: Small ribosomal subunit protein uS13m

database: EMBL

database: RefSeq

database: AlphaFoldDB

database: SMR

database: BioGRID

database: ComplexPortal

value: 37S mitochondrial small ribosomal subunit

database: OMA

database: PhylomeDB

database: PRO

database: Proteomes

value: Chromosome III

database: GO

value: C:mitochondrial small ribosomal subunit

value: C:small ribosomal subunit

value: F:RNA binding

value: F:structural constituent of ribosome

value: P:mitochondrial translation

value: 30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18


value: Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and at least 32 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and at least 45 different proteins

value: Belongs to the universal ribosomal protein uL4 family

description: Mitochondrion

description: Large ribosomal subunit protein uL4m

description: Disordered

value: 54S ribosomal protein yml6, mitochondrial

value: Large ribosomal subunit protein uL4m

database: PubMed

database: DOI

source: EMBL

database: PIR

value: 54S mitochondrial large ribosomal subunit

database: FunCoup

database: STRING

database: PaxDb

database: GeneID

database: KEGG

database: PomBase

value: Eukaryota

value: Chromosome II

value: C:mitochondrial large ribosomal subunit


value: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure (By similarity). It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (PubMed:28218250)

value: Forms a stable heterodimer with pob3 (By similarity). The spt16-pob3 dimer weakly associates with multiple molecules of nhp6 to form the FACT complex (By similarity). Interacts with abo1 (PubMed:26582768). Interacts with chromatin remodeling protein fft3; to mediate nucleosome disassembly at transcribing regions and promote the efficient passage of RNAPII through chromatin (PubMed:28218250)

commentType: INTERACTION

value: Nucleus

value: Chromosome

value: Belongs to the peptidase M24 family. SPT16 subfamily

commentType: CAUTION

value: Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity

description: FACT complex subunit spt16

description: Disordered

description: Disordered

type: Coiled coil

description: Basic and acidic residues

description: Acidic residues

description: Basic and acidic residues

description: Phosphoserine

description: Phosphoserine

source: PDB

type: Helix

type: Beta strand

type: Turn

value: Facilitates chromatin transcription complex subunit spt16

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444 AND SER-445

authors:
Gal C.
Murton H.E.
Subramanian L.
Whale A.J.
Moore K.M.
Paszkiewicz K.
Codlin S.
Baehler J.
Creamer K.M.
Partridge J.F.
Allshire R.C.
Kent N.A.
Whitehall S.K.

title: Abo1, a conserved bromodomain AAA-ATPase, maintains global nucleosome occupancy and organisation.

authors:
Lee J.
Choi E.S.
Seo H.D.
Kang K.
Gilmore J.M.
Florens L.
Washburn M.P.
Choe J.
Workman J.L.
Lee D.

title: Chromatin remodeller Fun30Fft3 induces nucleosome disassembly to facilitate RNA polymerase II elongation.

value: RNA Polymerase II Pre-transcription Events

value: TP53 Regulates Transcription of DNA Repair Genes

value: Regulation of TP53 Activity through Phosphorylation

value: F:H2A-H2B histone complex chaperone activity

value: P:DNA replication-dependent chromatin assembly

value: P:regulation of DNA-templated transcription elongation

value: P:transcription elongation-coupled chromatin remodeling

value: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)


value: May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function

database: Rhea

name: a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP] + holo-[ACP] + CO2

database: ChEBI

name: butanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxohexanoyl-[ACP] + holo-[ACP] + CO2

name: hexanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxooctanoyl-[ACP] + holo-[ACP] + CO2

name: octanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxodecanoyl-[ACP] + holo-[ACP] + CO2

name: decanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxododecanoyl-[ACP] + holo-[ACP] + CO2

name: dodecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxotetradecanoyl-[ACP] + holo-[ACP] + CO2

name: tetradecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxohexadecanoyl-[ACP] + holo-[ACP] + CO2

value: Lipid metabolism; fatty acid biosynthesis

value: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family

description: Mitochondrion

description: Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial

description: Ketosynthase family 3 (KS3)

description: For beta-ketoacyl synthase activity

description: For beta-ketoacyl synthase activity

description: For beta-ketoacyl synthase activity


value: Component of the GPI transamidase complex. Involved in transfer of GPI to proteins (By similarity)

commentType: PATHWAY

value: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis

value: Forms a complex with PIG-S homolog, PIG-U homolog and GPI8

value: Endoplasmic reticulum membrane

value: Single-pass type I membrane protein

commentType: PTM

value: The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity

value: Belongs to the PIGT family

type: Signal

description: GPI transamidase component PIG-T homolog

description: Lumenal

type: Topological domain

description: Helical

type: Transmembrane

description: Cytoplasmic

description: N-linked (GlcNAc...) asparagine

type: Glycosylation

description: N-linked (GlcNAc...) asparagine

description: N-linked (GlcNAc...) asparagine

description: N-linked (GlcNAc...) asparagine

description: N-linked (GlcNAc...) asparagine

description: Interchain (with C-73 in PIGK/GPI8)

type: Disulfide bond

database: EMBL

database: RefSeq

database: AlphaFoldDB

database: SMR

database: ComplexPortal

value: GPI-anchor transamidase complex

database: GlyCosmos

key: glycosylation

value: 5 sites, No reported glycans

database: VEuPathDB

database: eggNOG

value: C:lumenal side of endoplasmic reticulum membrane

value: GPI TRANSAMIDASE COMPONENT PIG-T-RELATED


value: Cytoplasm

value: Nucleus

description: PHD and RING finger domain-containing protein C126.07c

type: Chain

description: RING-type 1; atypical

type: Zinc finger

description: PHD-type

description: RING-type 2; degenerate

description: Disordered

type: Region

description: Polar residues

type: Compositional bias

description: Basic residues

description: Polar residues

database: PubMed

database: DOI

type: STRAIN

database: PIR

database: BioGRID

database: iPTMnet

value: Eukaryota

database: HOGENOM

database: InParanoid

database: OMA

database: PhylomeDB

database: PRO

database: Proteomes

value: Chromosome III

database: GO

value: Zinc/RING finger domain, C3HC4 (zinc finger)

value: PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1


value: Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:15654094, PubMed:22705791, PubMed:23080121, PubMed:7885834). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (By similarity). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). Within the MRN complex, rad32 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (Probable) (PubMed:22705791). Rad32 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (By similarity). It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination (By similarity)

database: ChEBI

commentType: COFACTOR

value: Forms a multisubunit endonuclease complex, MRN, together with nbn and rad50

value: Localizes to discrete nuclear foci after treatment with genotoxic agents

value: Chromosome, telomere

value: Chromosome

value: Belongs to the MRE11/RAD32 family

description: Double-strand break repair protein rad32

description: Disordered

description: Polar residues

description: Polar residues

description: Acidic residues

description: Proton donor

source: PIRSR

type: Active site

type: Binding site

description: Decreased repair of double strand breaks (DSBs).

authors:
Tavassoli M.
Shayeghi M.
Nasim A.
Watts F.Z.

title: Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene: a gene required for repair of double strand breaks and recombination.

referencePositions:
NUCLEOTIDE SEQUENCE [GENOMIC DNA]
FUNCTION

authors:
Chahwan C.
Nakamura T.M.
Sivakumar S.
Russell P.
Rhind N.

title: The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint.

authors:
Farah J.A.
Cromie G.
Steiner W.W.
Smith G.R.

title: A novel recombination pathway initiated by the Mre11/Rad50/Nbs1 complex eliminates palindromes during meiosis in Schizosaccharomyces pombe.

authors:
Limbo O.
Moiani D.
Kertokalio A.
Wyman C.
Tainer J.A.
Russell P.

title: Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
MUTAGENESIS OF TRP-248

authors:
Schiller C.B.
Lammens K.
Guerini I.
Coordes B.
Feldmann H.
Schlauderer F.
Moeckel C.
Schele A.
Straesser K.
Jackson S.P.
Hopfner K.P.

title: Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 7-413 IN COMPLEX WITH MANGANESE AND NBS1

value: Cytosolic sensors of pathogen-associated DNA

value: DNA Damage/Telomere Stress Induced Senescence

value: Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks

value: F:double-stranded DNA 3'-5' DNA exonuclease activity

value: F:single-stranded DNA endonuclease activity

value: P:double-strand break repair involved in meiotic recombination

value: P:double-strand break repair via homologous recombination

value: P:double-strand break repair via nonhomologous end joining

value: P:meiotic DNA double-strand break formation

value: P:mitochondrial double-strand break repair via homologous recombination

value: P:mitotic G2 DNA damage checkpoint signaling

value: P:mitotic intra-S DNA damage checkpoint signaling

value: DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11


value: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB

value: Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of cft1, cft2, ysh1, pta1, swd2, pfs2, dis2, yth1, ssu72, and fip1

value: Nucleus

value: To yeast PTA1

description: mRNA cleavage and polyadenylation specificity factor complex subunit pta1

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.

authors:
Roguev A.
Shevchenko A.
Schaft D.
Thomas H.
Stewart A.F.
Shevchenko A.

journal: Mol. Cell. Proteomics

title: A comparative analysis of an orthologous proteomic environment in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.

authors:
Matsuyama A.
Arai R.
Yashiroda Y.
Shirai A.
Kamata A.
Sekido S.
Kobayashi Y.
Hashimoto A.
Hamamoto M.
Hiraoka Y.
Horinouchi S.
Yoshida M.

title: ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.

authors:
Hu W.
Suo F.
Du L.L.

journal: Genome Biol. Evol.

title: Bulk segregant analysis reveals the genetic basis of a natural trait variation in fission yeast.

database: EMBL

database: RefSeq

database: AlphaFoldDB

database: SMR

database: ComplexPortal

value: Cleavage and polyadenylation specificity factor complex

database: FunCoup

database: STRING

database: PaxDb

database: GeneID

database: KEGG

database: PomBase

value: Eukaryota

database: Reactome

value: Transport of Mature mRNA Derived from an Intronless Transcript

value: Processing of Intronless Pre-mRNAs

value: mRNA Polyadenylation

value: Chromosome I

value: C:mRNA cleavage and polyadenylation specificity factor complex

value: P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway

value: P:termination of RNA polymerase II transcription, poly(A)-coupled


value: Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly

value: Interacts with pre-ribosome complex

value: Cytoplasm

value: Nucleus, nucleolus

value: Belongs to the NIP7 family

description: 60S ribosome subunit biogenesis protein nip7

description: PUA

type: Domain

value: P:assembly of large subunit precursor of preribosome

value: 60S ribosome subunit biogenesis protein NIP7 homolog

value: CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT/60S RIBOSOME SUBUNIT BIOGENESIS PROTEIN NIP7


value: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body (By similarity)

value: tRNA splicing endonuclease is a heterotetramer composed of sen2, sen15, sen34 and sen54. Interacts directly with sen34 (By similarity)

value: Belongs to the SEN15 family

description: Probable tRNA-splicing endonuclease subunit sen15

value: tRNA-intron endonuclease sen15

database: PubMed

database: DOI

database: BioGRID

database: VEuPathDB

database: eggNOG

database: HOGENOM

database: InParanoid

database: OMA

database: PhylomeDB

value: C:tRNA-intron endonuclease complex

value: F:nucleic acid binding

value: P:tRNA-type intron splice site recognition and cleavage

key: MatchStatus

database: InterPro

database: PANTHER

value: TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN15

database: Pfam

database: SUPFAM

value: tRNA-intron endonuclease catalytic domain-like


value: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs). Within the SAGA complex, participates in a subcomplex with SGF11, SGF73 and UBP8 required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery

value: Component of the 1.8 MDa SAGA (Spt-Ada-Gcn5 acetyltransferase) complex, which is composed of 19 subunits tra1, spt7, taf5, ngg1/ada3, sgf73, spt20, spt8, taf12, taf6, hfi1/ada1, ubp8, gcn5, ada2, spt3, sgf29, taf10, taf9, sgf11 and sus1 (PubMed:19056896). The SAGA complex is composed of 4 modules, namely the HAT (histone acetyltransferase) module (gcn5, ada2, ngg1/ada3 and sgf29), the DUB (deubiquitinating) module (ubp8, sgf11, sgf73 and sus1), the core or TAF (TBP-associated factor) module (taf5, taf6, taf9, taf10 and taf12), and the Tra1 or SPT (Suppressor of Ty) module (tra1, hfi1/ada1, spt3, spt7, spt8 and spt20). The Tra1/SPT module binds activators, the core module recruits TBP (TATA-binding protein), the HAT module contains the histone H3 acetyltransferase gcn5, and the DUB module comprises the histone H2B deubiquitinase ubp8 (By similarity). Component of the nuclear pore complex (NPC)-associated TREX-2 complex (transcription and export complex 2), composed of at least sus1, sac3, thp1, sem1, and cdc31. TREX-2 contains 2 sus1 chains. The TREX-2 complex interacts with the mRNA export factors mex67, mtr2 and sub2, and the nucleoporin nup1 (By similarity)

source: HAMAP-Rule

value: Nucleus, nucleoplasm

value: Cytoplasm, P-body

value: Belongs to the ENY2 family

description: SAGA complex subunit Sus1

value: Transcription and mRNA export factor sus1

value: SAGA complex subunit Sus1

authors:
Helmlinger D.
Marguerat S.
Villen J.
Gygi S.P.
Bahler J.
Winston F.

journal: Genes Dev.

title: The S. pombe SAGA complex controls the switch from proliferation to sexual differentiation through the opposing roles of its subunits Gcn5 and Spt8.

referencePositions:
IDENTIFICATION IN THE SAGA COMPLEX
IDENTIFICATION BY MASS SPECTROMETRY

database: EMBL

key: ProteinId

database: RefSeq

database: AlphaFoldDB

database: SMR

database: ComplexPortal

value: SAGA complex

database: FunCoup

database: IntAct

database: MINT

database: STRING

database: iPTMnet

database: PaxDb

database: GeneID

database: PRO

database: Proteomes

value: Chromosome II

database: GO

value: C:DUBm complex

value: C:nuclear pore

value: P:positive regulation of transcription by RNA polymerase II

value: P:regulation of transcription by RNA polymerase II

value: P:transcription elongation by RNA polymerase II

value: P:transcription initiation-coupled chromatin remodeling

value: ENHANCER OF YELLOW 2 TRANSCRIPTION FACTOR


value: Probable zinc transporter involved in Golgi membrane trafficking through the regulation of zinc homeostasis

value: Interacts with zrg17

value: Endoplasmic reticulum membrane

value: Multi-pass membrane protein

value: Golgi apparatus, cis-Golgi network membrane

value: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily

description: Probable zinc transporter cis4

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Disordered

originalSequence: G

description: In cis4-1; confers sensitivities to the calcineurin inhibitor FK506 and to a high concentration of MgCl2.

type: Mutagenesis

description: In cis4-2; confers sensitivities to the calcineurin inhibitor FK506 and to a high concentration of MgCl2.

originalSequence: L

description: in Ref. 2; BAA13900

type: Sequence conflict

originalSequence: N

description: in Ref. 2; BAA13900

description: in Ref. 2; BAA13900

value: Probable zinc transporter cis4

database: PubMed

database: DOI

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 377-732

authors:
Fang Y.
Sugiura R.
Ma Y.
Yada-Matsushima T.
Umeno H.
Kuno T.

title: Cation diffusion facilitator Cis4 is implicated in Golgi membrane trafficking via regulating zinc homeostasis in fission yeast.

referencePositions:
FUNCTION
MUTAGENESIS OF GLY-375 AND GLY-393
SUBCELLULAR LOCATION
INTERACTION WITH ZRG17

value: Zinc efflux and compartmentalization by the SLC30 family

value: F:zinc ion transmembrane transporter activity

value: Cation efflux protein transmembrane domain-like


value: Component of the 90S pre-ribosome involved in the maturation of rRNAs. Required for early cleavages of the pre-RNAs in the 40S ribosomal subunit maturation pathway (By similarity)

value: Associates with 90S and pre-40S pre-ribosomal particles

value: Nucleus, nucleolus

value: Belongs to the RRP36 family

description: rRNA biogenesis protein rrp36

description: Disordered

description: Disordered

type: Coiled coil

description: Polar residues

description: Acidic residues

description: Basic and acidic residues

description: Basic residues

value: Ribosomal RNA-processing protein 36

value: rRNA biogenesis protein rrp36

authors:
Bitton D.A.
Wood V.
Scutt P.J.
Grallert A.
Yates T.
Smith D.L.
Hagan I.M.
Miller C.J.

journal: Genetics

title: Augmented annotation of the Schizosaccharomyces pombe genome reveals additional genes required for growth and viability.

referencePositions:
REVISION OF GENE MODEL
IDENTIFICATION BY MASS SPECTROMETRY

database: EMBL

key: Status

database: BioGRID

database: PomBase

database: VEuPathDB

database: eggNOG

value: Eukaryota

database: HOGENOM

database: InParanoid

database: OMA

database: Reactome

value: Major pathway of rRNA processing in the nucleolus and cytosol

value: P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

value: RIBOSOMAL RNA PROCESSING PROTEIN 36 HOMOLOG


value: Metalloendopeptidase that acts selectively on DNA-binding proteins. DNA is needed to bring the protease and substrates together to enable proteolysis. Involved in the repair of toxic DNA-protein cross-links (DPCs) such as covalently trapped topoisomerase 1 (top1) adducts on DNA lesions or DPCs induced by reactive compounds such as formaldehyde. Involved in DNA damage response and processing of stalled or collapsed replication forks by removing the covalently trapped top1 from chromatin. DPC proteolysis enables the repair of the lesions via downstream DNA repair pathways. May be recruited to DPCs via the SUMOylation of substrate proteins at damaged DNA sites (By similarity)

database: ChEBI

value: Binds to DNA. Interacts with pmt3/smt3

value: Nucleus

commentType: DOMAIN

value: The SUMO interaction motif (SIM) is important for binding to pmt3/smt3 (SUMO)

value: Belongs to the peptidase M3 family. WSS1-like metalloprotease (WLM) subfamily

description: DNA-dependent metalloprotease WSS1 homolog

description: WLM

description: Disordered

description: SUMO interaction motif (SIM)

type: Motif

description: Basic residues

note: catalytic

source: PomBase

value: DNA damage response protein WSS1 homolog

key: MoleculeType

database: RefSeq

database: AlphaFoldDB

database: SMR

database: FunCoup

database: STRING

database: MEROPS

database: KEGG

value: P:protein-DNA covalent cross-linking repair


value: Copper amine oxidase involved in the metabolism of xenobiotic and biogenic amines. Capable of catalyzing the oxidative deamination of primary amines such as ethylamine as alternate sources of nitrogen to support growth

name: a primary methyl amine + O2 + H2O = an aldehyde + H2O2 + NH4(+)

database: Rhea

value: Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity).

value: Contains 1 topaquinone per subunit.

value: Binds 1 Mn(2+) ion per subunit.

value: Homodimer

value: Cytoplasm

value: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue

value: Belongs to the copper/topaquinone oxidase family

description: Copper amine oxidase 1

description: Proton acceptor

description: Schiff-base intermediate with substrate; via topaquinone

type: Modified residue

originalSequence: H

description: Decreases copper amine oxidase activity.

description: Impairs copper amine oxidase activity.

description: Impairs copper amine oxidase activity.

description: Impairs copper amine oxidase activity.

title: Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine oxidase 1 expressed in Saccharomyces cerevisiae.

authors:
Peter C.
Laliberte J.
Beaudoin J.
Labbe S.

title: Copper distributed by Atx1 is available to copper amine oxidase 1 in Schizosaccharomyces pombe.

referencePositions: MUTAGENESIS OF HIS-456; HIS-458; HIS-460 AND HIS-627


value: Component of the AP-1 complex which links clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration

value: Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit apl4 and beta-type subunit apl2), a medium adaptin (mu-type subunit apm1) and a small adaptin (sigma-type subunit aps1). AP-1 interacts with clathrin (By similarity)

value: Cytoplasmic vesicle, clathrin-coated vesicle membrane

value: Endosome

value: Golgi apparatus

value: Leads to hypersensitivity to valproic acid

value: Belongs to the adaptor complexes small subunit family

description: AP-1 complex subunit sigma-1

value: Valproic acid-sensitive protein 2

value: AP-1 complex subunit sigma-1

database: PubMed

database: DOI

authors:
Ma Y.
Takeuchi M.
Sugiura R.
Sio S.O.
Kuno T.

journal: Genes Cells

title: Deletion mutants of AP-1 adaptin subunits display distinct phenotypes in fission yeast.

referencePositions:
DISRUPTION PHENOTYPE
IDENTIFICATION IN THE AP-1 COMPLEX
SUBCELLULAR LOCATION
FUNCTION

database: EMBL

key: Description

database: BioGRID

database: ComplexPortal

value: Adaptor complex AP-1

database: PaxDb

database: GeneID

value: Eukaryota

database: PhylomeDB

value: Lysosome Vesicle Biogenesis

database: PRO

database: Proteomes

value: Chromosome I

database: GO

value: C:AP-1 adaptor complex

value: P:endosome to plasma membrane protein transport

value: P:retrograde transport, endosome to Golgi

value: P:vesicle targeting, trans-Golgi to endosome


value: Probable methyltransferase

value: Cytoplasm

value: Nucleus

value: Belongs to the methyltransferase superfamily

description: Uncharacterized methyltransferase C25B8.09

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

database: PIR

database: RefSeq

database: AlphaFoldDB

database: SMR

key: Interactions

database: iPTMnet

database: PomBase

database: VEuPathDB

database: eggNOG

database: HOGENOM

database: InParanoid

value: F:methyltransferase activity

value: P:cellular detoxification

value: P:cellular response to amino acid starvation

database: CDD

database: FunFam

value: Vaccinia Virus protein VP39

value: METHYLTRANSFERASE TYPE 11 DOMAIN-CONTAINING PROTEIN


value: Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin

name: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

value: Component of the 26S proteasome. Interacts with rpn10

value: Belongs to the peptidase C12 family

description: Ubiquitin carboxyl-terminal hydrolase 2

description: UCH catalytic

description: ULD

description: Nucleophile

description: Proton donor

description: Transition state stabilizer

type: Site

description: Important for enzyme activity

value: Ubiquitin carboxyl-terminal hydrolase 2

database: PubMed

database: DOI

authors:
Stone M.
Hartmann-Petersen R.
Seeger M.
Bech-Otschir D.
Wallace M.
Gordon C.

journal: J. Mol. Biol.

title: Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast.

referencePositions:
FUNCTION
INTERACTION WITH RPN10
SUBCELLULAR LOCATION

authors:
Li T.
Naqvi N.I.
Yang H.
Teo T.S.

journal: Biochem. Biophys. Res. Commun.

title: Identification of a 26S proteasome-associated UCH in fission yeast.

database: EMBL

database: BioGRID

database: ComplexPortal

value: 26S proteasome complex

database: FunCoup

database: IntAct

database: STRING

database: MEROPS

database: PaxDb

database: GeneID

database: KEGG

key: GeneName

value: P:cytoplasm protein quality control by the ubiquitin-proteasome system

value: Peptidase C12, ubiquitin carboxyl-terminal hydrolase

value: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5


value: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner (PubMed:22615807, PubMed:32518066). Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step (PubMed:32518066). The LSM1-LSM7 complex loads onto the 3'-end of single stranded RNA (PubMed:32518066). Component of the nuclear LSM2-LSM8 complex, which is involved in spliceosome assembly (PubMed:32518066). The LSM2-LSM8 complex plays a role in the biogenesis of the spliceosomal U4/U6-U5 tri-snRNP complex by accelerating prp24-mediated annealing of U4/U6 di-snRNA (By similarity). The LSM2-LSM8 complex binds U6 snRNA terminating with a cyclic 2',3' phosphate group; RNA with an unmodified 3' hydroxyl or non-cyclic 3' phosphate is bound less tightly (PubMed:32518066)

value: Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a donut shape (Probable) (PubMed:32518066). The LSm subunits are arranged in the order lsm1, lsm2, lsm3, lsm6, lsm5, lsm7 and lsm4 (PubMed:22001694, PubMed:22615807, PubMed:32518066). Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a donut shape (Probable) (PubMed:32518066). The LSm subunits are arranged in the order lsm8, lsm2, lsm3, lsm6, lsm5, lsm7 and lsm4 (PubMed:22001694, PubMed:22615807, PubMed:32518066)

value: LSM1 and LSM8 act competitively with respect to the localization of LSM1-LSM7 to the cytoplasm and LSM2-LSM8 to the nucleus. LSm proteins shift to the cytoplasm under conditions of stress

value: Nucleus, nucleolus

value: Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily

description: LSM complex subunit lsm6

description: Sm

type: Helix

type: Beta strand

value: LSM complex subunit lsm6

authors:
Mund M.
Neu A.
Ullmann J.
Neu U.
Sprangers R.

title: Structure of the LSm657 complex: an assembly intermediate of the LSm1-7 and LSm2-8 rings.

referencePositions: IDENTIFICATION IN THE LSM1-LSM7 AND LSM2-LSM8 COMPLEXES

authors:
Wu D.
Jiang S.
Bowler M.W.
Song H.

journal: PLoS ONE

title: Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe.

authors:
Montemayor E.J.
Virta J.M.
Hayes S.M.
Nomura Y.
Brow D.A.
Butcher S.E.

journal: RNA

title: Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH RNA

database: PIR

database: RefSeq

database: PDB

value: U6 small nuclear ribonucleoprotein complex

value: P:telomerase holoenzyme complex assembly

value: Probable U6 snRNA-associated Sm-like protein LSm6

value: SMALL NUCLEAR RIBONUCLEOPROTEIN F SNRNP-F

value: U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM6


value: Catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate (Dol-P) biosynthesis. Dol-P is a lipid carrier essential for the synthesis of N-linked and O-linked oligosaccharides and for GPI anchors

database: Rhea

name: a di-trans,poly-cis-dolichol + CTP = a di-trans,poly-cis-dolichyl phosphate + CDP + H(+)

database: ChEBI

value: Protein modification; protein glycosylation

value: Endoplasmic reticulum membrane

value: Multi-pass membrane protein

value: Belongs to the polyprenol kinase family

description: Dolichol kinase sec59

description: Cytoplasmic

type: Topological domain

description: Helical

type: Transmembrane

description: Lumenal

description: Helical

description: Cytoplasmic

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Helical

description: Lumenal

authors:
Rhind N.
Chen Z.
Yassour M.
Thompson D.A.
Haas B.J.
Habib N.
Wapinski I.
Roy S.
Lin M.F.
Heiman D.I.
Young S.K.
Furuya K.
Guo Y.
Pidoux A.
Chen H.M.
Robbertse B.
Goldberg J.M.
Aoki K.
Bayne E.H.
Berlin A.M.
Desjardins C.A.
Dobbs E.
Dukaj L.
Fan L.
FitzGerald M.G.
French C.
Gujja S.
Hansen K.
Keifenheim D.
Levin J.Z.
Mosher R.A.
Mueller C.A.
Pfiffner J.
Priest M.
Russ C.
Smialowska A.
Swoboda P.
Sykes S.M.
Vaughn M.
Vengrova S.
Yoder R.
Zeng Q.
Allshire R.
Baulcombe D.
Birren B.W.
Brown W.
Ekwall K.
Kellis M.
Leatherwood J.
Levin H.
Margalit H.
Martienssen R.
Nieduszynski C.A.
Spatafora J.W.
Friedman N.
Dalgaard J.Z.
Baumann P.
Niki H.
Regev A.
Nusbaum C.

title: Comparative functional genomics of the fission yeasts.

referencePositions: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]

value: P:dolichol phosphate mannose biosynthetic process

value: P:dolichyl monophosphate biosynthetic process