wanglab/gogpt-training-data huggingface dataset:
Protein: Inner capsid protein VP2 (A2T3R5)
Organism: Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Function: Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles (By similarity). May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04127}. Note=Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04127}.
Interaction partners:
Sequence:
MAYRKRGARRETNLKQDERMQEKEDSKNINNDSPKSQLSEKVLSKKEEIITDNQEEVKISDEVKKSNKEESKQLLEVLKTKEEHQKEVQYEILQKTIPTFEPKESILKKLEDIKPEQAKKQTKLFRIFEPKQLPIYRANGERELRNRWYWKLKRDTLPDGDYDVREYFLNLYDQVLMEMPDYLLLKDMAVENKNSRDAGKVVDSETAAICDAIFQDEETEGAVRRFIAEMRQRVQADRNVVNYPSILHPIDHAFNEYFLQHQLVEPLNNDIIFNYIPERIRNDVNYILNMDRNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLKELVSTEAQIQKMSQDLQLEALTIQSETQFLTGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVIPNDMFIRESLVACQLAIINTIVYPAFGMQRMHYRNGDPQTPFQIAEQQIQNFQVANWLHFVNYNQFRQVVIDGVLNQVLNDNIRNGHVVNQLMEALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLSYNYETLMACITMNMQHVQTLTTEKLQLTSVTSLCMLIGNATVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKSIVEDFLKRLQIFDVARVPDDQMYRLRDRLRLLPVEIRRLDIFNLIAMNMEQIERASDKIAQGVIIAYRDMQLERDEMYGYVNIARNLDGFQQINLEELMRSGDYAQITNMLLNNQPVALVGALPFITDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWIPTSTTKVYKQVPQQFDFRASMHMLTSNLTFTVYSDLLAFVSADTVEPINAVAFDNMRIMNEL
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FMP9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Sulfiredoxin
- Thioredoxin reductase
- Candida glabrata strain CBS138 chromosome M complete sequence
- Thioredoxin
- Catalase
- Candida glabrata strain CBS138 chromosome E complete sequence
Sequence:
MVAQVQKPAPTFKKTAVIDGMFEEVSLDKYKGKYVVLAFVPLAFTFVCPTEIVAFSEAAKRFEALDAQVLFASTDSEYSLLAWTNVARKDGGLGPVDIPLLADTNHKLSRDYGVLIEDEGIALRGLFIIDPKGIVRHITINDLPVGRNVEESLRLVEGFQWTDKNGTVLPCNWTPGSATIKPTVEDSKEYFKEANSKN
Protein: Uncharacterized protein YGL041C-B (Q3E750)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MFDSSIERVTLELCFHITLSIMCGCSIYFLLLVFILTFYSSVLLHLKLYFFSSDRAIFNA
Protein: Exosome complex component RRP46 (Ribosomal RNA-processing protein 46) (P53256)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP46 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Superkiller protein 7
- ATP-dependent RNA helicase DOB1
- Exosome complex component RRP40
- Exosome complex component CSL4
- Exosome complex exonuclease RRP6
- Exosome complex component RRP4
- Exosome complex exonuclease DIS3
- Exosome complex component RRP42
- Exosome complex protein LRP1
- Pre-rRNA-processing protein PNO1
Sequence:
MSVQAEIGILDHVDGSSEFVSQDTKVICSVTGPIEPKARQELPTQLALEIIVRPAKGVATTREKVLEDKLRAVLTPLITRHCYPRQLCQITCQILESGEDEAEFSLRELSCCINAAFLALVDAGIALNSMCASIPIAIIKDTSDIIVDPTAEQLKISLSVHTLALEFVNGGKVVKNVLLLDSNGDFNEDQLFSLLELGEQKCQELVTNIRRIIQDNISPRLVV
Protein: Zinc finger protein 92 (Zinc finger protein HTF12) (Q03936)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Tumor-associated calcium signal transducer 2
Sequence:
MGPLTFRDVKIEFSLEEWQCLDTAQRNLYRDVMLENYRNLVFLGIAVSKPDLITWLEQGKEPWNLKRHEMVDKTPVMCSHFAQDVWPEHSIKDSFQKVILRTYGKYGHENLQLRKDHKSVDACKVYKGGYNGLNQCLTTTDSKIFQCDKYVKVFHKFPNVNRNKIRHTGKKPFKCKNRGKSFCMLSQLTQHKKIHTREYSYKCEECGKAFNWSSTLTKHKIIHTGEKPYKCEECGKAFNRSSNLTKHKIIHTGEKPYKCEECGKAFNRSSTLTKHKRIHTEEKPYKCEECGKAFNQFSILNKHKRIHMEDKPYKCEECGKAFRVFSILKKHKIIHTGEKPYKCEECGKAFNQFSNLTKHKIIHTGEKPYKCDECGKAFNQSSTLTKHKRIHTGEKPYKCEECGKAFKQSSTLTEHKIIHTGEKPYKCEKCGKAFSWSSAFTKHKRNHMEDKPYKCEECGKAFSVFSTLTKHKIIHTREKPYKCEECGKAFNQSSIFTKHKIIHTEGKSYKCEKCGNAFNQSSNLTARKIIYTGEKPYKYEECDKAFNKFSTLITHQIIYTGEKPCKHECGRAFNKSSNYTKEKLQT
Protein: Proactivator polypeptide-like 1 [Cleaved into: Saposin A-like; Saposin B-Val-like; Saposin B-like; Saposin C-like; Saposin D-like] (Q6NUJ1)
Organism: Homo sapiens (Human)
Function: May activate the lysosomal degradation of sphingolipids.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Prosaposin
- Protein canopy homolog 1
- Granulysin
- Protein canopy homolog 2
- Mesencephalic astrocyte-derived neurotrophic factor
Sequence:
MLCALLLLPSLLGATRASPTSGPQECAKGSTVWCQDLQTAARCGAVGYCQGAVWNKPTAKSLPCDVCQDIAAAAGNGLNPDATESDILALVMKTCEWLPSQESSAGCKWMVDAHSSAILSMLRGAPDSAPAQVCTALSLCEPLQRHLATLRPLSKEDTFEAVAPFMANGPLTFHPRQAPEGALCQDCVRQVSRLQEAVRSNLTLADLNIQEQCESLGPGLAVLCKNYLFQFFVPADQALRLLPPQELCRKGGFCEELGAPARLTQVVAMDGVPSLELGLPRKQSEMQMKAGVTCEVCMNVVQKLDHWLMSNSSELMITHALERVCSVMPASITKECIILVDTYSPSLVQLVAKITPEKVCKFIRLCGNRRRARAVHDAYAIVPSPEWDAENQGSFCNGCKRLLTVSSHNLESKSTKRDILVAFKGGCSILPLPYMIQCKHFVTQYEPVLIESLKDMMDPVAVCKKVGACHGPRTPLLGTDQCALGPSFWCRSQEAAKLCNAVQHCQKHVWKEMHLHAGEHA
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q9XU13)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.
Interaction partners:
Sequence:
MEDAHAKDANEVCKFFGTGPEGLTPQQVETLRNKYGENEMPAEEGKSLWELILEQFDDLLVKILLLAAIISFVLALFEEHEDQTEAVTAFVEPFVILLILIANATVGVWQERNAESAIEALKEYEPEMAKVIRSGHHGIQMVRAKELVPGDLVEVSVGDKIPADLRLVKIYSTTIRIDQSILTGESVSVIKHTDSVPDPRAVNQDKKNCLFSGTNVASGKARGIVFGTGLTTEIGKIRTEMAETENEKTPLQQKLDEFGEQLSKVISVICVAVWAINIGHFNDPAHGGSWVKGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVSKMFIAGQASGDNINFTEFAISGSTYEPVGKVSTNGREINPAAGEFESLTELAMICAMCNDSSVDYNETKKIYEKVGEATETALIVLAEKMNVFGTSKAGLSPKELGGVCNRVIQQKWKKEFTLEFSRDRKSMSAYCFPASGGSGAKMFVKGAPEGVLGRCTHVRVNGQKVPLTSAMTQKIVDQCVQYGTGRDTLRCLALGTIDTPVSVSNMNLEDSTQFVKYEQDITFVGVVGMLDPPRTEVSDSIKACNHAGIRVIMITGDNKNTAEAIGRRIGLFGENEDTTGKAYTGREFDDLPPEQQSEACRRAKLFARVEPSHKSKIVDILQSQGEITAMTGDGVNDAPALKKAEIGISMGSGTAVAKSASEMVLADDNFASIVSAVEEGRAIYNNMKQFIRYLISSNVGEVVSIFMVAALGIPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRHPRSANDGLISGWLFFRYLAVGTYVGVATVGASMWWFLLYEEGPQITYYQLTHWMRCEIEPDNFADLDCAVFEDNHPNAMALSVLVTIEMLNAINSLSENQSLLVMPPWKNIWLMAAISLSMSLHFVILYVDIMATIFQITPLNWVEWIAVLKISLPVLLLDEILKFIARNYIDVEAPIKDKRD
Protein: Prostamide/prostaglandin F synthase (Prostamide/PG F synthase) (Prostamide/PGF synthase) (EC 1.11.1.20) (Peroxiredoxin-like 2B) (Protein FAM213B) (Q8TBF2)
Organism: Homo sapiens (Human)
Function: Catalyzes the reduction of prostaglandin-ethanolamide H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor. Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha) (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9DB60}.
Interaction partners:
Sequence:
MSTVDLARVGACILKHAVTGEAVELRSLWREHACVVAGLRRFGCVVCRWIAQDLSSLAGLLDQHGVRLVGVGPEALGLQEFLDGDYFAGELYLDESKQLYKELGFKRYNSLSILPAALGKPVRDVAAKAKAVGIQGNLSGDLLQSGGLLVVSKGGDKVLLHFVQKSPGDYVPKEHILQVLGISAEVCASDPPQCDREV
Protein: Leucine-rich repeat and fibronectin type-III domain-containing protein 4 (Q80XU8)
Organism: Mus musculus (Mouse)
Function: Promotes neurite outgrowth in hippocampal neurons. May play a role in redistributing DLG4 to the cell periphery.
Subcellular location: Membrane {ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18227064}; Single-pass type I membrane protein {ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18227064}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase S
- Disks large homolog 4
- Interleukin-1 receptor accessory protein-like 1
- Receptor-type tyrosine-protein phosphatase F
- Disks large homolog 1
- Interleukin-1 receptor accessory protein
Sequence:
MAPPLLLLLLASGAAACPLPCVCQNLSESLSTLCAHRGLLFVPPNVDRRTVELRLADNFIQALGPPDFRNMTGLVDLTLSRNAITRIGARSFGDLESLRSLHLDGNRLVELGSSSLRGPVNLQHLILSGNQLGRIAPGAFDDFLDSLEDLDVSYNNLRQVPWAGIGSMPALHTLNLDHNLIDALPPGVFAQLSQLSRLDLTSNRLATLAPDPLFSRGRDAEASPSPLVLSFSGNPLHCNCELLWLRRLARPDDLETCASPPTLAGRYFWAVPEGEFSCEPPLIARHTQRLWVLEGQRATLRCRALGDPVPTMHWVGPDDRLVGNSSRAWAFPNGTLEIGVTGAGDAGAYTCIATNPAGEATARVELRVLALPHGGNTSAEGGRPGPSDIAASARTAAEGEGTLESEPAVQVTEVTATSGLVSWGLGRPADPVWMFQIQYNSSEDETLIYRIVPASSHHFLLKHLVPGADYDLCLLALSPAAGPSDLTATRLLGCAHFSTLPATPLCHALQAHVLGGTLTVAVGGVLVAALLVFTVALLVRGRGAGNGRLPLKLSHVQSQTNGGTSPMPKSHPPRSPPPRPQRSCSLDLGDTGGCYGYARRLGGAWARRSHSVHGGLLGAGCRGVGGSAERLEESVV
Protein: Tubulin alpha-4 chain (EC 3.6.5.-) (P06606)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-3 chain
- Tubulin beta chain
- Tubulin beta-2 chain
- beta-Tubulin at 65B
- Protein matrimony
- Serine/threonine-protein kinase CG17528
- Maternal effect protein oskar
- non-specific serine/threonine protein kinase
- Deubiquitinase otu
- Vitellogenin receptor Yl
Sequence:
MREVVSIQIGQCGIQIGNACWELYLLEHGINLDGSLKTKEELTASGSSASVGHDTSANDARTFFTETGNGKQVPRSIFVDLEPTVIDDVRNGCMRELYHPEQLISGKEDAANNYARGRYSIGKEVIDRVTSRLQKIAEQCDSLQGFLIFHSLGGGTGSGFTSLLVERLSTDYSKKCKLDFAVYPSPKVSTAVVEPYNALLTTHSTMDHSDCVFMVDNEAIYDICNNSLGVDRPAYRNLNRLIAQIVSSTTASLRFSGSMNVDLNEFQTNLVPFPRIHFPLVAYAPLMSAERSAHEQHAITTLTNACFESSNMMVKCDPRAGKFMACCMLYRGDVVPKDVNAAVSAIKSKRHIQFVDWCPTGFKIGINYEKPAFVPDGDLAKTSRACCMLSNTTAISVAFSNLSYKFDLMFKKRAFVHWYVGEGMEEGEFTEARENIAVLERDFEEVGLDNAEEGGDEDFDEF
Protein: GDP-fucose protein O-fucosyltransferase 3 (EC 2.4.1.221) (Alpha-(1,3)-fucosyltransferase 10) (EC 2.4.1.-) (Fucosyltransferase X) (Fuc-TX) (FucT-X) (Galactoside 3-L-fucosyltransferase 10) (Fucosyltransferase 10) (Q6P4F1)
Organism: Homo sapiens (Human)
Function: Predominantly fucosylates the innermost N-acetyl glucosamine (GlcNAc) residue in biantennary N-glycan acceptors. Postulated to generate core alpha(1->3)-fucose epitope within the chitobiose unit of biantennary N-glycans, providing for a recognition signal to reorient aberrantly folded glycoproteins for degradation. Involved in biosynthesis of Lewis X-carrying biantennary N-glycans that regulate neuron stem cell self-renewal during brain development (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:39775168}; Single-pass type II membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000305|PubMed:19088067}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000305|PubMed:12370785, ECO:0000305|PubMed:19088067}; Single-pass type II membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 4]: Golgi apparatus {ECO:0000269|PubMed:19088067}. Lysosome {ECO:0000269|PubMed:19088067}.; SUBCELLULAR LOCATION: [Isoform 5]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19088067}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000305|PubMed:19088067}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVRIQRRKLLASCLCVTATVFLLVTLQVMVELGKFERKEFKSSSLQDGHTKMEEAPTHLNSFLKKEGLTFNRKRKWELDSYPIMLWWSPLTGETGRLGQCGADACFFTINRTYLHHHMTKAFLFYGTDFNIDSLPLPRKAHHDWAVFHEESPKNNYKLFHKPVITLFNYTATFSRHSHLPLTTQYLESIEVLKSLRYLVPLQSKNKLRKRLAPLVYVQSDCDPPSDRDSYVRELMTYIEVDSYGECLRNKDLPQQLKNPASMDADGFYRIIAQYKFILAFENAVCDDYITEKFWRPLKLGVVPVYYGSPSITDWLPSNKSAILVSEFSHPRELASYIRRLDSDDRLYEAYVEWKLKGEISNQRLLTALRERKWGVQDVNQDNYIDAFECMVCTKVWANIRLQEKGLPPKRWEAEDTHLSCPEPTVFAFSPLRTPPLSSLREMWISSFEQSKKEAQALRWLVDRNQNFSSQEFWGLVFKD
Protein: General secretion pathway protein GspJ (Hypothetical type II secretion protein GspJ) (Q8VRM4)
Organism: Escherichia coli
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004377}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004377}.
Interaction partners:
Sequence:
MLVAIAIFASLALMAQQVTNGVTRVNSAVAGHDQKLNLMQQTMSFLTHDLTQMMPRPVRGDQGQREPALLAGAGVLASESEGMRFVRGGVVNPLMRLPRSNLLTVGYRIHDGYLERLAWPLTDAAGSVKPTMQKLIPADSLRLQFYDGTRWQESWSSVQAIPVAVRMTLHSPQWGEIERIWLLRGPQ
Protein: Probable transcriptional regulatory protein YebC (P0A8A0)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00693}.
Interaction partners:
- Dihydroneopterin triphosphate diphosphatase
- Crossover junction endodeoxyribonuclease RuvC
- Aspartate--tRNA ligase
- Holliday junction branch migration complex subunit RuvA
- Large ribosomal subunit protein bL19
Sequence:
MAGHSKWANTRHRKAAQDAKRGKIFTKIIRELVTAAKLGGGDPDANPRLRAAVDKALSNNMTRDTLNRAIARGVGGDDDANMETIIYEGYGPGGTAIMIECLSDNRNRTVAEVRHAFSKCGGNLGTDGSVAYLFSKKGVISFEKGDEDTIMEAALEAGAEDVVTYDDGAIDVYTAWEEMGKVRDALEAAGLKADSAEVSMIPSTKADMDAETAPKLMRLIDMLEDCDDVQEVYHNGEISDEVAATL
Protein: StAR-related lipid transfer protein 4 (START domain-containing protein 4) (StARD4) (Q99JV5)
Organism: Mus musculus (Mouse)
Function: Involved in the intracellular transport of cholesterol. Binds cholesterol or other sterols.
Interaction partners:
- Phosphatidylcholine transfer protein
Sequence:
MADPESPWSQIGRKIKLEGLSDVASISTKLQNTLIQYHSIKEDEWRVAKKVKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRPGPWRLDWDRLMTSLDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYEEGLLSCGVSVEWSETRPEFVRGYNHPCGWFCVPLKDSPSQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRKGLRKA
Protein: LIM domain-binding protein 1-A (LDB-1-A) (LIM domain-binding protein 4) (LDB-4) (zLdb4) (O73715)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:16815859}.
Interaction partners:
- T-cell acute lymphocytic leukemia protein 1 homolog
- Rhombotin-2
- Rhombotin-1
- Endothelial transcription factor GATA-2a
- Single-stranded DNA-binding protein 2
- Single-stranded DNA-binding protein 4
- BHLH domain-containing protein.
- LIM/homeobox protein Lhx3
Sequence:
MLDRDVGPTPMYPPSYMEPGIGRHTPYGNQTDYRIFELNKRLQNWTEQDCDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELFYVLKHPKESFHNNFVSLDCDQCTMVTQNGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHREVVPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQAPNKRRKRKMSGGSTMSSGGGNNNNSNSKKKSPASSFALSSQDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNSSPTMGTNSPWNSKAPSSQQGKNDNPSSQSSQ
Protein: Uncharacterized GPI-anchored protein C212.08c (Q9HGP7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Uncharacterized but2-like protein C27D7.11c
- Truncated RecQ DNA helicase-like protein C212.06c
- Uncharacterized but2-like protein C27D7.09c
- ATP-dependent DNA helicase tlh1
- UPF0591 membrane protein C15E1.02c
- UPF0300 protein C737.04
- Uncharacterized oxidoreductase C663.06c
Sequence:
MSPLIVGTLIIILLSGLATAFYVTWQGRLICAGVGLILEQAYEGGQMFNTLMAHCFETYNGVEKSGTQCVADWLKVGLLAVTFGAGGPRLVNTLGGTFLTSPTAKRSNLYCDDFTGADYFSCELETLRPYTLMRKSLPYGNIHDVWINTTDTHQMIGVHMTLNGTDMIHYYNKTYVINYSGLKLNSSAINKRSYFYPQDSFLVSHAEWQDGNGIWTDTDYFAAMADCDFLGQNLGFWLASSYPNAYKWETQLWRTVGINLNGNIIYPGQLIMQTFNGS
Protein: 2,3-dihydroxybenzoate-AMP ligase, chrysobactin biosynthesis (EC 2.7.7.58, EC 4.2.1.-) (E0SLE4)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- isochorismatase
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
- isochorismate synthase
- Dimodular nonribosomal peptide synthetase
- Chrysobactin synthetase cbsF
- Indigoidine synthase
- MbtH-like protein
- Nonribosomal peptide synthetase
- Iron
- Enterobactin synthase component D
Sequence:
MMIEFTRWPPELEQRYRDRGYWQDLPLGDILARHADSDDTALICGERTLSYRQMNQQVAQLAGALQRRGLKPGQTALVQLGNVAEFYLTYFALLRAGIVPVNALFSHQRSELCAYADQIAPTLLIADRGHLLFADDSFIDELRQRCPSLQQVILRGDADSAQALSQLLQEDGDPQAATPTPADQVAFFQLSGGSTGTPKLIPRTHNDYYYSIRGSVEICRVDAHTRFLCALPAAHNYPLSSPGALGVFYAGGTVVLAGDPSPTCCFPLIAQHRITLTALVPPAVTLWLEAVALSGDRSALASLLVLQVGGARLSEALARRVPAELGCQLQQVFGMAEGLVNYTRLDDDDIHRFTTQGCPISDDDEVWVADAYGNPLPHGEPGRLMTRGPYTFRGYYRSPAHNRQVFNDDGFYCSGDLVIQQADGYLQVVGREKDQINRGGEKIAAEEIENLLLRHPAVINAALVAVPDTMMGEKSCAFLVTREPLKAAALRRHLREQGIADYKLPDRFEQLPTLPETAVGKVDKQRLRQLAQQRVAAPTAGE
Protein: Chromatin modification-related protein EAF7 (ESA1-associated factor 7) (P53911)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Chromatin modification-related protein EAF5
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- Enhancer of polycomb-like protein 1
- SWR1-complex protein 4
- Chromatin modification-related protein EAF3
- Protein AF-9 homolog
- Chromatin modification-related protein EAF6
- Chromatin modification-related protein YNG2
- Chromatin modification-related protein EAF1
- Histone acetyltransferase ESA1
Sequence:
MVVHWTIVDEIRLLRWASEFKPAGIHKHFHMFCIVERMNSPDKYPVTLLQKETMKLGKVFTAKDIWDKLSQSYNLEKIDEMENTYSLEATTESSRNGNGNGDDAEIHEETLLELNNRIRVRKQDFTLPWEEYGELILENARKSPNSNEEYPRVEDMNEKDSTIPKESPSTDLKNDNNKQEKNATIKVKELPEYHTEENDSPIDVQKEPIKEVQSDEKELQREHMSEEEQKMKSTNKTAAPVRKSQRLKRSKEVKFEDEEKEEIEEDNTKDEEQKEKKEEIQEPKITHNEEVDKEKNENEEGDDEREKSTSYENTNGSESEGVDEGVDEELGYESEREAEGKGKQIESEGGNLKKKTENKKGDDQQDDTKKDSKDKNEPLAKRTRHSSSTGNTSNETSPKRKRRKAGSRKNSPPATRVSSRLRNKK
Protein: Leucine-rich repeat protein (LRRP) (Q38EE5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGSDLSIVLRTCVAAPDCTKEENQSTPAADGGRDSEELKWYTELRLADRSSPEAPESILRSDFGVEPEVLIPECTLTALSELDTRDPKAFLRLKKVLCCPKCAGRVGLAVDSSASIGRRLHVAEHRRVFTQCLSALLSKLVLAMKDNVSDEGREDQLARVKRESTPLDAECTLPIGRYELFLLDLQHCLLDDASGPWIVRDFLEHVGNSRHQHSAVSLVHDEQRSRSSSIMSFCLSPSARERLSTNYTSLQFLMAENDSNPPVSQAAEAAEQTFCKSLCYIRLSENNMSQIGMRKCVEELVGCKDKEKMRCLRSLRLIDVRQNEETVAAQRAVANLSSTSNIHILVGDSGLRWRYQSGVRYSVGLASRLGRSLSHTTDVHRSMLSEERLRAPSQLTMSNARFSIPMASHIGFDQRTRQYEDEGSAVPVGVVTDVLPNTPLETRLAELEEDVEEPFPRSLHGHIEDTRGNDNRCLHSYQQDKQHQSKTASAALATAVPENDAEFFQDSDAADACSEGGAMLREPQTFLAAPHPELLAATQMKREKRGLADGGQSSVAPRISARRTIATRDTANQNKARFLRTDKPTVGRSTSSRTPTSERATARTARPQPDSNRTNKTKGVATVAAGGGSLKHLSREPPKRVK
Protein: AICARFT/IMPCHase bienzyme family protein (Putative phosphoribosylaminoimidazolecarboxamide formyltransferase) (Q8RWT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- Adenylosuccinate synthetase, chloroplastic
- Phosphoribosylglycinamide formyltransferase, chloroplastic
- Inosine-5'-monophosphate dehydrogenase 2
- Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- Inosine-5'-monophosphate dehydrogenase 1
- Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic
- Formate--tetrahydrofolate ligase
- Serine hydroxymethyltransferase 3, chloroplastic
Sequence:
MLSSAATATSVSARSGDILCGLFRKKSVAPFRFTQPVYRTSLCPSFVAVRAMAESQTAQRNQPQSSGSSGEKQALISLSDKRDLASLGNGLQELGYTIVSTGGTASTLENAGVSVTKVEKLTHFPEMLDGRVKTLHPNIHGGILARRDVEHHMEALNEHGIGTFDVVVVNLYPFYEKVTAPGGISFEDGIENIDIGGPAMIRAAAKNHKDVLIVVDSGDYQAVLEYLKGGQSDQQFRRKLAWKAFQHVAAYDSAVSEWLWKQTEGKEKFPPSFTVPLVLKSSLRYGENPHQKAAFYVDKSLAEVNAGGIATAIQHHGKEMSYNNYLDADAAWNCVSEFENPTCVVVKHTNPCGVASRDDILEAYRLAVKADPVSAFGGIVAFNVEVDEVLAREIREFRSPTDGETRMFYEIVVAPKYTAKGLEVLKGKSKTLRILEAKKNDQGKLSLRQVGGGWLAQDSDDLTPEDISFNSVSDKTPTESELADAKFAWLCVKHVKSNAIVIAKNNCMLGMGSGQPNRVESLRIAFKKAGEEAKGAALASDAFFPFAWKDAVEEACQMGIGVIAEPGGSIRDQDAIDCCKKYGVSLLFTNVRHFRH
Protein: Poly(rC) binding protein 2 (Q6AYU2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLESPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWAGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS
Protein: Uncharacterized protein C5H10.12c (Q09680)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized alpha-1,2-galactosyltransferase C1289.13c
- Probable alpha-1,2-galactosyltransferase gmh2
- Probable alpha-1,2-galactosyltransferase gmh1
- Alpha-1,2-galactosyltransferase
- Alpha-1,2-galactosyltransferase gmh3
Sequence:
MSRISLSNFLSLPRYKFLLFSVVLIIVMTTLVFNGHDYKQTLNDRLTSLKNNFVEENDNAVLKEEPGKYTYMSLFTMPSTEEDYYFNATRVLIHRLKYHPTTKSKYPIHILALRGVDEWKIERFRKDGASVIVIDPIASSDIVYDTSSFSQEISARYEQMFSKLRIFEQIQFDKICVIDSDILIMKNIDDIFDTPYMYQQINTLNYTRLPSYTKPDDDTVYHFNEDFKEYGASRSEFYPYLLAAVSDRGEHHSIPPEDTPYFNAGLMLIRPSELHFNRILKIGRFPYMYENAKMMEQSLLNLAFSLDGWFPWTRLDPYYNGVWPSIDERPLLKTAHGKFWNIGSSEFAPVYLADWYAAYGEMLSFHKYETH