wanglab/gogpt-training-data huggingface dataset:
Protein: UDP-galactose translocator (Solute carrier family 35 member A2) (UDP-galactose transporter) (UDP-Gal-Tr) (UGT) (P78381)
Organism: Homo sapiens (Human)
Function: Transports uridine diphosphate galactose (UDP-galactose) from the cytosol into the Golgi apparatus, functioning as an antiporter that exchanges UDP-galactose for UMP. It is also able to exchange UDP-galactose for AMP and CMP, and to transport UDP-N-acetylgalactosamine (UDP-GalNAc) and other nucleotide sugars. As a provider of UDP-galactose to galactosyltransferases present in the Golgi apparatus, it is necessary for globotriaosylceramide/globoside (Gb3Cer) synthesis from lactosylceramide.
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15932921}. Golgi apparatus membrane {ECO:0000269|PubMed:15932921, ECO:0000269|PubMed:24115232, ECO:0000269|PubMed:28167211}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane {ECO:0000269|PubMed:15932921}.
Interaction partners:
- UDP-glucuronosyltransferase 1A4
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 1A10
- UDP-glucuronosyltransferase 1A7
- UDP-glucuronosyltransferase 1A8
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 1A9
- UDP-glucuronosyltransferase 3A1
- UDP-glucuronosyltransferase 3A2
- UDP-glucuronosyltransferase 2B4
Sequence:
MAAVGAGGSTAAPGPGAVSAGALEPGTASAAHRRLKYISLAVLVVQNASLILSIRYARTLPGDRFFATTAVVMAEVLKGLTCLLLLFAQKRGNVKHLVLFLHEAVLVQYVDTLKLAVPSLIYTLQNNLQYVAISNLPAATFQVTYQLKILTTALFSVLMLNRSLSRLQWASLLLLFTGVAIVQAQQAGGGGPRPLDQNPGAGLAAVVASCLSSGFAGVYFEKILKGSSGSVWLRNLQLGLFGTALGLVGLWWAEGTAVATRGFFFGYTPAVWGVVLNQAFGGLLVAVVVKYADNILKGFATSLSIVLSTVASIRLFGFHVDPLFALGAGLVIGAVYLYSLPRGAAKAIASASASASGPCVHQQPPGQPPPPQLSSHRGDLITEPFLPKLLTKVKGS
Protein: Phosphopantetheine adenylyltransferase (PPAT) (EC 2.7.7.3) (Coenzyme A biosynthesis protein 4) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (P53332)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity). Plays a role in the physiological regulation of the intracellular CoA concentration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14690591}. Nucleus {ECO:0000269|PubMed:14690591}.
Interaction partners:
- Dephospho-CoA kinase CAB5
- Phosphopantothenate--cysteine ligase CAB2
- Coenzyme A biosynthesis protein 3
- Pantothenate kinase CAB1
- Phosphopantothenoylcysteine decarboxylase subunit VHS3
- Phosphopantothenoylcysteine decarboxylase subunit SIS2
- Oxysterol-binding protein homolog 4
- Uncharacterized protein YGR273C
Sequence:
MVEENSRVLIVLPYTPPSATLQRIIGQTIPFLRECQSQLDIVIVPEFKTSFQLDSALGKMYSITRDVLLGYGMINSGINIIFNNIHFVESNLQWKVVLLPQESTFETWKLELGQGQYHSIEHYALHDNIMEEIEGPKDANKFHVTALGGTFDHIHDGHKILLSVSTFITSQRLICGITCDELLQNKKYKELIEPYDTRCRHVHQFIKLLKPDLSVELVPLRDVCGPTGKVPEIECLVVSRETVSGAETVNKTRIEKGMSPLAVHVVNVLGGREEDGWSEKLSSTEIRRLLKSSASPTCTPQNPCV
Protein: Apolipoprotein B (A8MUN2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Lipid droplet {ECO:0000256|ARBA:ARBA00004502}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDPPRPALLALLALPALLLLLLAGARAEEEMLENVSLVCPKDATRFKHLRKYTYNYEAESSSGVPGTADSRSATRINCKVELEVPQLCSFILKTSQCTLKEVYGFNPEGKALLKKTKNSEEFAAAMSRYELKLAIPEGKQVFLYPEKDEPTYILNIKRGIISALLVPPETEEAKQVLFLDTVYGNCSTHFTVKTRKGNVATEISTERDLGQCDRFKPIRTGISPLALIKGMTRPLSTLISSSQSCQYTLDAKRKHVAEAICKEQHLFLPFSYKNKYGMVAQVTQTLKLEDTPKINSRFFGEGTKKMGLAFESTKSTSPPKQAEAVLKTLQELKKLTISEQNIQRANLFNKLVTELRGLSDEAVTSLLPQLIEVSSPITLQALVQCGQPQCSTHILQWLKRVHANPLLIDVVTYLVALIPEPSAQQLREIFNMARDQRSRATLYALSHAVNNYHKTNPTGTQELLDIANYLMEQIQDDCTGDEDYTYLILRVIGNMGQTMEQLTPELKSSILKCVQSTKPSLMIQKAAIQALRKMEPKDKDQEVLLQTFLDDASPGDKRLAAYLMLMRSPSQADINKIVQILPWEQNEQVKNFVASHIANILNSEELDIQDLKKLVKEALKESQLPTVMDFRKFSRNYQLYKSVSLPSLDPASAKIEGNLIFDPNNYLPKESMLKTTLTAFGFASADLIEIGLEGKGFEPTLEALFGKQGFFPDSVNKALYWVNGQVPDGVSKVLVDHFGYTKDDKHEQDMVNGIMLSVEKLIKDLKSKEVPEARAYLRILGEELGFASLHDLQLLGKLLLMDRPDSLTIPAAQARKDACTFFRDGGLP
Protein: WD repeat domain-containing protein 83 (Mitogen-activated protein kinase organizer 1) (Q19986)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Splicing factor 3B subunit 4
- G patch domain-containing protein 1 homolog
- Pre-mRNA-splicing factor 8 homolog
- LUC7-related splicing factor homolog
- Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
- RRM domain-containing protein
- Ragulator complex protein LAMTOR2 homolog
- Serine/threonine-protein phosphatase Pgam5, mitochondrial
Sequence:
MSKCPTVRARAIDCKQGAVRAVRYNVDGNYCVTCGSDKTVKLWNPLKSSLLKTYSGTGNEVLDAASSSDNSQIAAGGADRACTVFDVETGKQLRRWRTHGAQVNAVAFNEESSVVFSGSMDCTMQAFDCRSRSEKPIQIFNESTDGILSIDVNGHEIVAGSADGNYRVYSIRDGNMTVDYMGDSVNSVSFTPDSNCLLAGVMGGIVRLIDKSSGKLLASYKGHQNTEYKLDCRVLQSIEHVASGSEDGFVYVYSLLDSHIVSKLEHPSKVIHSLTAHPKKERLMTAAGQMIYLWVAEDDAEVLGE
Protein: DNA polymerase alpha catalytic subunit (EC 2.7.7.7) (3'-5' exodeoxyribonuclease) (EC 3.1.11.-) (P26019)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit PolA1, an accessory subunit PolA2 and two primase subunits, the catalytic subunit Prim1 and the regulatory subunit Prim2) is recruited to DNA at the replicative forks. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity). These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity). In addition to polymerase activity, exhibits 3' to 5' exonuclease activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:1429896, ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:9858578}.
Interaction partners:
- Chromosome transmission fidelity 4
- DNA polymerase alpha subunit B
- DNA primase large subunit
- DNA primase small subunit
- DNA polymerase epsilon catalytic subunit 1
- DNA polymerase delta subunit 2
- DNA polymerase delta catalytic subunit
- DNA replication licensing factor Mcm2
- DNA polymerase epsilon subunit 2
- CDC45L
Sequence:
MSESPSEPRAKRQRVDKNGRFAAMERLRQLKGTKNKCKVEDQVDDVYDVVDEREYAKRAQEKYGDDWIEEDGTGYAEDLRDFFEDEDEYSDGEEDRKDSKKKKGVAPNSKKRPRENEKPVTGKASIKNLFSNAVPKKMDVKTSVKDDDILADILGEIKEEPAATSEKAEKVIAPAKISVTSRKFDAAAAKEYMNSFLNNIKVQEQERKKAEASSDNEMLERILKPKAAVPNTKVAFFSSPTIKKEPMPEKTPAKKATEDPFSDNEMDFSCLDDDENQFDVEKTQQTEKVSQTKTAAEKTSQSKVAEKSAPKKETTGSPKESESEDISRLLNNWESICQMDDDFEKSVLTTEQDSTISSDQQLRFWYWEAYEDPVKMPGEVFLFGRTADGKSVCLRVQNINRVLYLLPRQFLLDPISKEPTKQKVTVADIYKEFDSEVANQLKLEFFRSRKVTKSFAHHAIGIEVPQSCDYLEVHYDGKKPLPNLSADKKYNSIAHIFGATTNALERFLLDRKIKGPCWLQVTGFKVSPTPMSWCNTEVTLTEPKNVELVQDKGKPAPPPPLTLLSLNVRTSMNPKTSRNEICMISMLTHNRFHIDRPAPQPAFNRHMCALTRPAVVSWPLDLNFEMAKYKSTTVHKHDSERALLSWFLAQYQKIDADLIVTFDSMDCQLNVITDQIVALKIPQWSRMGRLRLSQSFGKRLLEHFVGRMVCDVKRSAEECIRARSYDLQTLCKQVLKLKESERMEVNADDLLEMYEKGESITKLISLTMQDNSYLLRLMCELNIMPLALQITNICGNTMTRTLQGGRSERNEFLLLHAFHEKNYIVPDKKPVSKRSGAGDTDATLSGADATMQTKKKAAYAGGLVLEPMRGLYEKYVLLMDFNSLYPSIIQEYNICFTTVQQPVDADELPTLPDSKTEPGILPLQLKRLVESRKEVKKLMAAPDLSPELQMQYHIRQMALKLTANSMYGCLGFAHSRFFAQHLAALVTHKGREILTNTQQLVQKMNYDVVYGDTDSLMINTNITDYDQVYKIGHNIKQSVNKLYKQLELDIDGVFGCLLLLKKKKYAAIKLSKDSKGNLRREQEHKGLDIVRRDWSQLAVMVGKAVLDEVLSEKPLEEKLDAVHAQLEKIKTQIAEGVVPLPLFVITKQLTRTPQEYANSASLPHVQVALRMNRERNRRYKKGDMVDYVICLDGTTNAAMQRAYHLDELKTSEDKKLQLDTNYYLGHQIHPVVTRMVEVLEGTDASRIAECLGMDPTKFRQNAQRTQRENTEQSEGESLLKTTLQLYRLCEPFRFQCVTCKTEQLMASAYRPGPSNSHIAVLQQCAKSECQTAPIQYLASVRNQLQLSMRQYVQRFYKNWLVCDHPDCNFNTRTHSLRKKSHRPLCQKCRSGSLLRQYTERDLYNQLCYLRFMFDLGKQTLQQKPTLTPELEQAYQLLYETVDQQLQSSSYVIISLSKLFARSLAQMSLQPSVAQPQIEAIPSALADVV
Protein: Cytochrome b-c1 complex subunit 7-1, mitochondrial (Complex III subunit 7-1) (Complex III subunit VII) (Ubiquinol-cytochrome c oxidoreductase subunit 7-1) (Q9SUU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18189341}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00128}; Matrix side {ECO:0000250|UniProtKB:P00128}.
Interaction partners:
- Cytochrome b-c1 complex subunit 6-1, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-2, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit 6-2, mitochondrial
- Cytochrome c1 2, heme protein, mitochondrial
- Cytochrome c1 1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 6a, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
Sequence:
MASLLKAFIDPKKNFLARMHMKAISTRLRRYGLRYDDLYDQYYSMDIKEAMNRLPREVVDARNQRLKRAMDLSMKHEYLPKDLQAVQTPFRGYLQDMLALVERESKEREALGALPLYQRTLP
Protein: SCF E3 ubiquitin ligase complex F-box protein pof2 (F-box and leucine-rich repeat protein pof2) (F-box/LRR-repeat protein pof2) (F-box protein pof2) (O74783)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in substrate recognition in ubiquitin-dependent degradation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Suppressor of kinetochore protein 1
- Protein phosphatase PP2A regulatory subunit B
- Cullin-1
- RING-box protein pip1
- Cullin-3
- Protein phosphatase PP2A regulatory subunit A
- Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
Sequence:
MRVPNEVCFNILSYLEADELRCKSTVCTSWRNFIIPTLWEKVVFQNEAQLNNFFDTLQYSKDVSYYFRYLRKLNCSRVRKFLTDKHLMLMTLATGISRLNLSGCTRISEPLIGKLLYQNLNLVTINFSNIFSLPANILEYISDNCPNLKALNIGNCGLVEDTGMVQIIKRCPYLNRLIIPNCRKLTDVSLQILSEKEDLIELDISGCEGFHNADTLSRLVSRNRGLKELSMDGCTELSHFITFLNLNCELDAMRALSLNNLPDLKDSDIELITCKFSKLNSLFLSKCIGLTDSSLLSLTKLSQSLTTLHLGHCYEITDIGVQCLLKSCKNITYIDFGGCLRLSDIAVSAIAKLPYLQRVGLVKCICLTDLSVILLSGSFSRNLERVHLSYCIGLTAKSVSYLMYNCKTLKHLSVTGINSILCTELRSFSRPIPDGINPSQVPVFCAFTKVEIDLFREFIRNRI
Protein: Uncharacterized protein YPL068C (Q02749)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MHMQLRKRKRVDYSGRNQTSDPPSTTTAAVPSIIVPKKRKVVAQNMVSPAIRATTTTLGTSNIIIPKPLQRPKFHNSASLSSPDDDPEKISVLEVQKNLSNLIKRQQRLFYKDIHKPTLAGLKNFEMLRLPNDLKLLQNIVNLLYSFEQLNSDSKTRPVTTSKLKASSQAHSDKLKKMLAERKPPFSHPSHSGTAYHNDIIHEIANLHSINLVDLINLEVYNNNCHTNNTALQTTANSLTLNSIIKKLDKPILKERNNSLVWPHKSRFKAKRNQPSPGQSLINNTDITLYNDV
Protein: Nuclear receptor corepressor 1 (E7EVU5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSSGYPPNQGAFSTEQSRYPPHSVQYTFPNTRHQQEFAVPDYRSSHLEVSQASQLLQQQQQQQLRRRPSLLSEFHPGSDRPQERRTSYEPFHPGPSPVDHDSLESKRPRLEQVSDSHFQRVSAAVLPLVHPLPEGLRASADAKKDPAFGGKHEAPSSPISGQPCGDDQNASPSKLSKEELIQSMDRVDREIAKVEQQILKLKKKQQQLEEEAAKPPEPEKPVSPPPVEQKHRSIVQIIYDENRKKAEEAHKIFEGLGPKVELPLYNQPSDTKVYHENIKTGVPARRMMKNQVMRKKLILFFKRRNHARKQREQKICQRYDQLMEAWEKKVDRIENNPRRKAKESKTREYYEKQFPEIRKQREQQERFQRVGQRGAGLSATIARSEHEISEIIDGLSEQENNEKQMRQLSVIPPMMFDAEQRRVKFINMNGLMEDPMKVYKDRQFMNVWTDHEKEIFKDKFIQHPKNFGLIASYLERKSVPDCVLYYYLTKKNENYKALVRRNYGKRRGRNQQIARPSQEEKVEEKEEDKAEKTEKK
Protein: Os05g0337200 protein (cDNA clone:001-112-C09, full insert sequence) (Q5WMQ1)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVSREQKRASLHEKLQILRTLTHSHAVNKMSIISDASTYIKDLKQKIAALNKELGCAKNMNICEEPSPVVRVQVLDKGFLINVFMDKSSPGLLSSILQAFDELGLTVIEARASCSNSFRLEAVGGEHEEADGGIDANAVELAVMQAIKSTPGK
Protein: Vesicle-associated membrane protein 7 (VAMP-7) (Synaptobrevin-like protein 1) (Q9JHW5)
Organism: Rattus norvegicus (Rat)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein. Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Note=In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region. Colocalizes with LAMP1 in kidney cells. Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney.
Interaction partners:
- Synaptosomal-associated protein 29
- Syntaxin-7
- Syntaxin-4
- Syntaxin-8
- Syntaxin-17
- BET1 homolog
- Vesicle transport through interaction with t-SNAREs homolog 1B
- Syntaxin-7
- Ankyrin repeat domain-containing protein 27
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MAILFAVVARGTTILAKHAWCGGNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFGFLNEVKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKHHSENQSLDRVTETQAQVDELKGIMVRNIDLVAQRGERLELLIDKTENLVDSSVTFKTTSRNLARAMCVKNVKLTAIIVVVSIVFIYIIVSPLCGGFTWPSCVKK
Protein: Transcription factor bHLH84 (Basic helix-loop-helix protein 84) (AtbHLH84) (bHLH 84) (bHLH transcription factor bHLH084) (Q7XHI9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1
- Topless-related protein 1
Sequence:
MEAMGEWSTGLGGIYTEEADFMNQLLASYEQPCGGSSSETTATLTAYHHQGSQWNGGFCFSQESSSYSGYCAAMPRQEEDNNGMEDATINTNLYLVGEETSECDATEYSGKSLLPLETVAENHDHSMLQPENSLTTTTDEKMFNQCESSKKRTRATTTDKNKRANKARRSQKCVEMSGENENSGEEEYTEKAAGKRKTKPLKPQKTCCSDDESNGGDTFLSKEDGEDSKALNLNGKTRASRGAATDPQSLYARKRRERINERLRILQHLVPNGTKVDISTMLEEAVQYVKFLQLQIKLLSSDDLWMYAPIAYNGMDIGLDLKLNALTR
Protein: Myosin-1 (Myosin heavy chain D) (MHC D) (P02567)
Organism: Caenorhabditis elegans
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin-2
- Myosin, essential light chain
- Myosin regulatory light chain 1
- Troponin T, skeletal muscle
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- Myosin regulatory light chain 2
- Tropomyosin isoforms a/b/d/f
- Troponin I 3
- Protein atz-1
Sequence:
MSLEHEKDPGWQYLKRSREQQLADQSRPYDSKKNVWIPDAEEGYIEGVIKGPGPKADTVIVTAGGKDVTLKKDIVQEVNPPKFEKTEDMSNLTFLNDASVLWNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDQAYRYMLQDHENQSMLITGESGAGKTENTKKVICYFATVGASQKAALKEGEKEVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGTLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFKPQLRDELLLNHPISNYWFVAQAELLIDGIDDTEEFQLTDEAFDVLKFSPTEKMDCYRLMSAHMHMGNMKFKQRPREEQAEPDGQDEAERACNMYGIDVDQFLKALVSPRVKVGTEWVSKGQNVDQVHWAIGAMAKGLYARVFHWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDMTLAQKLTDQHLGKHPNFEKPKPPKGKQGEAHFAMRHYAGTVRYNVLNWLEKNKDPLNDTVVSVMKASKKNDLLVEIWQDYTTQEEAAAAAKAGGGRKGGKSGSFMTVSMMYRESLNKLMTMLHKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTQHPDFVQRYAILAAKEAKSSDDMKTCAGAILQALINQKQLNDEQFRIGHTKVFFKAGVVAHIEDLRDDKLNQIITGFQSAIRWYTATADAGARRKQLNSYIILQRNIRSWCVLRTWDWFLLFGKLRPQLKCGKMAEEMIKMAEEQKVLEAEAKKAESARKSQEEAYAKLSAERSKLLEALELTQGGSAAIEEKLTRLNSARQEVEKSLNDANDRLSEHEEKNADLEKQRRKAQQEVENLKKSIEAVDGNLAKSLEEKAAKENQIHSLQDEMNSQDETIGKINKEKKLLEENNRQLVDDLQAEEAKQAQANRLRGKLEQTLDEMEEAVEREKRIRAETEKSKRKVEGELKGAQETIDELSAIKLETDASLKKKEADIHALGVRIEDEQALANRLTRQSKENAQRIIEIEDELEHERQSRSKADRARAELQRELDELNERLDEQNKQLEIQQDNNKKKDSEIIKFRRDLDEKNMANEDQMAMIRRKNNDQISALTNTLDALQKSKAKIEKEKGVLQKELDDINAQVDQETKSRVEQERLAKQYEIQVAELQQKVDEQSRQIGEYTSTKGRLSNDNSDLARQVEELEIHLATINRAKTAFSSQLVEAKKAAEDELHERQEFHAACKNLEHELDQCHELLEEQINGKDDIQRQLSRINSEISQWKARYEGEGLVGSEELEELKRKQMNRVMDLQEALSAAQNKVISLEKAKGKLLAETEDARSDVDRHLTVIASLEKKQRAFDKIVDDWKRKVDDIQKEIDATTRDSRNTSTEVFKLRSSMDNLSEQIETLRRENKIFSQEIRDINEQITQGGRTYQEVHKSVRRLEQEKDELQHALDEAEAALEAEESKVLRLQIEVQQIRSEIEKRIQEKEEEFENTRKNHQRALESIQASLETEAKSKAELARAKKKLETDINQLEIALDHANKANVDAQKNLKKLFDQVKELQGQVDDEQRRREEIRENYLAAEKRLAIALSESEDLAHRIEASDKHKKQLEIEQAELKSSNTELIGNNAALSAMKRKVENEVQIARNELDEYLNELKASEERARKAAADADRLAEEVRQEQEHAVHVDRQRKSLELNAKELQAKIDDAERAMIQFGAKALAKVEDRVRSLEAELHSEQRRHQESIKGYTKQERRARELQFQVEEDKKAFDRLQENVEKLQQKIRVQKRQIEEAEEVATQNLSKFRQIQLALENAEERAEVAENSLVRMRGQVVRSATNK
Protein: Palmitoyltransferase pfa3 (EC 2.3.1.225) (Protein fatty acyltransferase 3) (O14345)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Vacuolar protein 8
Sequence:
MNLIHKVSTICQCVLVILAKYCMQIIALSLMSGVQWLAWGIYKINKNRVGIIILFLYIMIVTCYVLTNLTPPGSPSETSFDPNSTRQYMTLQNGKSRFCEKCQEYKCDRSHHCSQCNKCILRMDHHCMWFKNCVGFRNHKFFFLECFYLNLYSICVLYSTFVAITKTFTAEGANISAIYLVFWGFLFAFAVGMSIVMTAFTFYHTSLLIHNLSTLESMSSSWSRYTHSTQPFNVGWYENWCQIMGKSPFLWLLPFPNSIGEGVEYPLNANALPYLPQTEEKNDKLYKSSVPASIAGAEGWSSDEEQYAMKNRRWNPHMGQYEWIEDFLV
Protein: Interferon-activable protein 204 (Ifi-204) (Interferon-inducible protein p204) (P0DOV2)
Organism: Mus musculus (Mouse)
Function: Interferon-stimulated protein that plays a role in several biological processes including cell differentiation, autophagy and innate immunity. Cooperates with CGAS to sense dsDNA and activates the STING-dependent type I IFN pathway. Mechanistically, gets acteylated upon bacterial infection and then translocates from nucleus into cytoplasm to recruit STING for activation of TBK1-dependent IRF3 nuclear translocation and IFN-beta release. Inhibits the transcription of ribosomal RNA. May inhibit DNA binding by UBTF. Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways. Acts as a coactivator of RUNX2 during osteogenesis. May be involved in macrophage differentiation. Enables skeletal muscle and cardiac myocyte differentiation by sequestring Id proteins in the cytosol and promoting their ubiquitination and subsequent degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:28529930}. Nucleus, nucleolus. Cytoplasm {ECO:0000269|PubMed:28529930}. Note=Nuclear in proliferating cells, translocates to cytosol during cell differentiation or bacterial infection. {ECO:0000269|PubMed:28529930}.
Interaction partners:
- Apoptosis-associated speck-like protein containing a CARD
- Interferon-inducible protein AIM2
- Stimulator of interferon genes protein
- Interferon activated gene 207
- Cellular tumor antigen p53
- Cyclic GMP-AMP synthase
- Interferon activated gene 206
- Caspase-1
- NLR family CARD domain-containing protein 4
- Pyrin
Sequence:
MVNEYKRIVLLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIAFCEEVPALRKRAEILKKERSEVTGETSLEKNGQEAGPATPTSTTSHMLASERGETSATQEETSTAQAGTSTAQARTSTAQAGTSTAQKRKIMREEETGVKKSKAAKEPDQPPCCEEPTARCQSPILHSSSSASSNIPSAKNQKSQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMLHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVLEAAPDQMIEVPNSIIRNANASPKICDIQKGTSGAVFYGVFTLHKKTVNRKNTIYEIKDGSGSIEVVGSGKWHNINCKEGDKLHLFCFHLKTIDRQPKLVCGEHSFIKISKRGNVPKEPAKEEDHHHGPKQVMVLKVTEPFTYDLKEDKRMFHATVATETEFFRVKVFDTALKSKFIPRNIIAISDYFGCNGFLEIYRASCVSDVNVNPTMVISNTLRQRANATPKISYLFSQARGTFVSGEYLVNKKTERNKFIYYGIGDDTGKMEVVVYGRLTNVRCEPGSKLRLVCFELTSTEDGWQLRSVRHSYMQVINARK
Protein: Histone H2A [Cleaved into: Buforin-1 (Buforin I); Buforin-2 (Buforin II)] (P55897)
Organism: Bufo gargarizans (Asian toad) (Bufo bufo gargarizans)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
Sequence:
AGRGKQGGKVRAKAKTRSSRAGLQFPVGRVHRLLRKGNY
Protein: Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 4, mitochondrial (UDP-3-O-acyl-GlcNAc deacetylase 4) (EC 3.5.1.108) (Protein LIPID X C4) (AtLpxC4) (UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase 4) (P0DKB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21709257, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial
Sequence:
MRLPVTVKATKPSFLVIWIRYSSAASSPTVSLNPSGRLQQTLAGSVEVKGKSLHSGKFSTVKLNPEIAGAGRFFEFRSRFIPASIEFAQESPLCTTLLKDELKIRTVEHLLSALEAKGVDNCRIQIESESSDDREVEVPIFDGSAKEWVDAIQGVGINAAQNHDGESVEKMVAHVNKPVYVCKNDTFVAAFPALETRITCGIDFPQVPAIGCQWFSWRPIHESSFAKDIASSRTFCVYEEVERMREAGLIKGGSLDNAIVCSAEHGWMNPPLRFDDEACRHKILDLIGDLSLVSRGGNGGLPVAHIVAYKAGHALHTDLARHLTMD