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protein coding gene - ucp8 (SPBC83.01) - UBA/EH/EF hand domain protein Ucp8

Gene summary

Standard name
ucp8
Systematic ID
SPBC83.01
Product
UBA/EH/EF hand domain protein Ucp8
Organism
Schizosaccharomyces pombe (fission yeast)
UniProt ID
O94685
ORFeome ID
29/29F01
Characterisation status
biological role published
Feature type
mRNA gene
Genomic location
chromosome II: 1510199..1513963 forward strand

Annotation

Disease association

MONDO:0016576 - split hand-foot malformation

References:

GO biological process

GO:0006897 - endocytosis

References:

GO:0016197 - endosomal transport

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GO cellular component

GO:0005737 - cytoplasm

References:

GO:0005886 - plasma membrane

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GO molecular function

GO:0005509 - calcium ion binding

References:

GO:0031593 - polyubiquitin modification-dependent protein binding

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GO:0030674 - protein-macromolecule adaptor activity

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Modification

MOD:00046 - O-phospho-L-serine

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MOD:00047 - O-phospho-L-threonine

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MOD:00696 - phosphorylated residue

References:

MOD:01148 - ubiquitinylated lysine

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Protein features

PBO:0111761 - EF hand

PBO:0111910 - EH domains

PBO:0111815 - UBA domain protein

Quantitative gene expression

PBO:0006310 - protein level

References:

PBO:0011963 - RNA level

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Single locus phenotype

FYPO:0009092 - decreased cell population growth on lysine and serine nitrogen source

References:

Genotypes:

FYPO:0000250 - decreased cell population growth on proline nitrogen source

References:

Genotypes:

FYPO:0000763 - resistance to cadmium

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Genotypes:

FYPO:0002693 - resistance to diamide

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Genotypes:

FYPO:0009085 - resistance to lithium chloride and sodium dodecyl sulfate

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Genotypes:

FYPO:0009043 - resistance to potassium chloride and sodium dodecyl sulfate

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Genotypes:

FYPO:0000830 - resistance to vanadate

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Genotypes:

FYPO:0001097 - sensitive to amitrole

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Genotypes:

FYPO:0002060 - viable vegetative cell population

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Genotypes:

FYPO:0002177 - viable vegetative cell with normal cell morphology

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Genotypes:

Taxonomic conservation

PBO:0011065 - conserved in eukaryotes

PBO:0011071 - conserved in eukaryotes only

PBO:0011064 - conserved in fungi

PBO:0011069 - conserved in metazoa

PBO:0011070 - conserved in vertebrates

PBO:0000055 - no apparent S. cerevisiae ortholog

PBO:0006222 - predominantly single copy (one to one)

Warnings

PBO:0000070 - gene structure updated

References:

Protein features

IDNameInterPro nameDB name
PF00627UBAUBAPfam
PF12763EHEH_domPfam
cd00052EHEH_domCDD
cd14270UBACDD
PS50030UBAUBAPROSITE profiles
PS50031EHEH_domPROSITE profiles
PS50222EF_HAND_2EF_hand_domPROSITE profiles
SM00027EHEH_domSMART
SM00165UBAUBASMART
G3DSA:1.10.238.10CATH-Gene3D
G3DSA:1.10.8.10CATH-Gene3D
SSF46934UBA-like_sfSUPERFAMILY
SSF47473EF-hand-dom_pairSUPERFAMILY
PTHR11216PANTHER
CoilCOILS
mobidb-lite-Disorderdisorder_predictionMobiDB-Disorder
mobidb-lite-Low-complexitydisorder_predictionMobiDB-Low-complexity
mobidb-lite-Polardisorder_predictionMobiDB-Polar
mobidb-lite-Proline-richdisorder_predictionMobiDB-Proline-rich

Orthologs

References / Literature

PB_REF:0000003 - Disease Association Curation
PMID:20473289 - Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
Kim DU et al. Nat Biotechnol 2010 Jun;28(6):617-623
PMID:23697806 - A genome-wide resource of cell cycle and cell shape genes of fission yeast.
Hayles J et al. Open Biol 2013 May 22;3(5):130053
GO_REF:0000033 - Annotation inferences using phylogenetic trees
PMID:12672455 - UBA domain containing proteins in fission yeast.
Hartmann-Petersen R et al. Int J Biochem Cell Biol 2003 May;35(5):629-36
PMID:26412298 - A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival.
Beckley JR et al. Mol Cell Proteomics 2015 Dec;14(12):3132-41
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
PMID:39367033 - Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast Schizosaccharomyces pombe.
Sivakova B et al. Sci Rep 2024 Oct 04;14(1):23105
PMID:30726745 - Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.
Tay YD et al. Cell Rep 2019 Feb 05;26(6):1654-1667.e7
PMID:37970674 - SUMOylation regulates Lem2 function in centromere clustering and silencing.
Strachan J et al. J Cell Sci 2023 Dec 01;136(23)
PMID:24763107 - Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).
Carpy A et al. Mol Cell Proteomics 2014 Aug;13(8):1925-36
PMID:33823663 - A TOR (target of rapamycin) and nutritional phosphoproteome of fission yeast reveals novel targets in networks conserved in humans.
Halova L et al. Open Biol 2021 Apr;11(4):200405
PMID:23101633 - Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.
Marguerat S et al. Cell 2012 Oct 26;151(3):671-83
PMID:29996109 - Quantitative Phosphoproteomics Reveals the Signaling Dynamics of Cell-Cycle Kinases in the Fission Yeast Schizosaccharomyces pombe.
Swaffer MP et al. Cell Rep 2018 Jul 10;24(2):503-514
GO_REF:0000002 - Comments
PMID:21712547 - Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast.
Koch A et al. Sci Signal 2011 Jun 28;4(179):rs6
PMID:27298342 - Identification of S-phase DNA damage-response targets in fission yeast reveals conservation of damage-response networks.
Willis NA et al. Proc Natl Acad Sci U S A 2016 Jun 28;113(26):E3676-85
PMID:39705284 - Proteomic and phosphoproteomic analyses reveal that TORC1 is reactivated by pheromone signaling during sexual reproduction in fission yeast.
Bérard M et al. PLoS Biol 2024 Dec 20;22(12):e3002963
PMID:37787768 - Broad functional profiling of fission yeast proteins using phenomics and machine learning.
Rodríguez-López M et al. Elife 2023 Oct 03;12
PMID:25720772 - Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.
Kettenbach AN et al. Mol Cell Proteomics 2015 May;14(5):1275-87