wanglab/gogpt-training-data huggingface dataset:
Protein: Secretory 16, isoform F (M9PHF1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MLHNNAPWLPPHQQQQQQAPQQHPTPQQQHAMPQQQQTLPAQQQQQQVYASQMFQQHQPNYWPEDQHQQQQQPQSLNYNNYFPGQQQQHPMQQQQLPPQQQLPPQQQQPTQQQHTIQQQLYYPTQQQPQVPAPAEPALDSFDNNNSGGGGGGGRSDGWGDWGDWNDNSNNNNSNGTDGLLEPTGQLLEDSFNVQSSQGSWQAFATSNNVNNNGELPPPANPQSTSLQQQPLNQQSIPLLHQQPQSPPELGQEPELDAIVPPQAFQNQPPTAAPPPTSLTSFSAQMTAVGSPIYAVGASSAHSAGVGASPAPPTGVVAPPAHLAGIGAPPAHLAGVGASPAPSALVGASPAPIIGVGAPPVGAPPVGAPPADATTIAPPAALPPSIVPSSGSNPFKRSTGLNKRVNIMADPAAGAPSPPAPAAAIAPVAPVAPIPPPADQLFGMPAEAHGEGFNLIAAPPVEASLGTPLSAPIPAPIPVPNASLYASPAVPQAFAHLEPDNQEVLSAPNDERAQYLQTSHLSEQLGEGEADQDAGLLPPPGLSRLVLGQPELDSQQQRQVTGATEQPPLNVAQAAALHMQERRADGEDTSDGEQQVRNIQTPPRRVVTGVETNAPSLREQREVVLDGENLEDREAIPPPTLAELPTTSVHHNILPDEAEQLHHNNPPQAMTPLNAQQPHQQQSTLQQQHQQHSTTQQEKKRAAVGRRTTASLDLESDESDEFLQSERERDRERERRDLMEERHSRGRSHSHYPYEGETEDSVRGAAHHETKSLRETHHKRNHDSARSRRHQDPKVERERERDRERDRTWRRRSNKYHSGGEDPDRSYDHSRRYNNSNYEGESDNPEYNHMGDAELDGSGGRSSKTSRHRRSAAEEDFDDYERERNRSRRSTKPQSSAEKSRSSGGRRNYENSGRSARADDGRRRYQDQRNPGAQYPVSATGYVPYGMYEQMSRNPQVYADMYAKFYGQMINSMNAAVSAAASKGGVPAGAGVIPGLMPSAVPVSAAQLVAATSGGSVSGSSEAAMLRERERYTHAYITQANEFHRHQYKELIYQQQQQQQQQQQQQQQREDHLNSSFSVAEDNASFYGSHGGGSIYNQYQSYPLSSARSLSNLNGDGRNSRCGPYYAGSECGLDIRAAADAAPSTYGGVAGTAGPVTNTAVARPPRRRTPLQFSRPHLVASYAMSLLLKVKPKYAGRGRLRNDVEVAPPRIRDGTSSLLRMYPGPLQGRKLHKDKIISFCKEQIRLGPTKGCTALYATQKKPQGSVTKYRASHALMWHLLILLLRQNGYIADTDVGDLLLENQQEYPYDPSEFEAENEPDADAEQDAAAPADKTVDSDLDSESAAGVTPAEPLAAGAATSSINGADAANAATPLSEQAATDKFRSYVLRGNVEEALQWATDNGLWTHAFFLALYEDRYALTDVAQKFLNRAIKANDPLQTLYQMKSCHTPACVSQLRDEQWGDWRSHLSILVTNKSRQPEYDRSSVVALGDTLFQRGDIYAAHFCYLVAQEEFGRYDSSATELTTLTANVPRLILLGSSHYKHFNEFASNEAIIMTEIYEYARSLFDPKFSIAHFQHYKFLLATRILDYGQHFRCTNYLEQIARHIELKPESYDSNFIQRVCGLAERLRYHDPILINRVSFASPPNATSKDSAAAEEKAWLRQLRSLAYVQPQQEQLQQLQQNQQVQQEQNDIDQQFAEVNKQFRELNMQYESNSNMENTLQPQLPPVDQQPPQQQQQVLSESYQQPTQQYYEPPPQAPTESDPYGQGQPSYYDPNAGQLHYDPNAAQHQYDQQQPQPQPTPSYGQIEPGTEAYQPGQATADPAAVPSGYGYDYWSGTQQPPYGDEPNENQAALKDEEEEDEEQDEQQILQYAKQQILQQTKQQQLQQEQHTRSNGAASINNRFKSNALKQERSSGSLRKRQEASRTATIAAAAAAIAQITPATVAAAATPPAASAKAFNLNDLQQQTRPAISMPKSKSYGDEDDGGSGGVADPGQKTKPVGSSEAAGKQQASGKQANSGSDLGIYHFEHSAPGNKNAGWFGGLWNKLSLKPKNQMILPDDKNPAIVWDKERKCWTNTEGNGDEAESFKPPPKMSDLGMALGGPPAAPIGNAGLGMGLMPVANNAPGSHQSAPLMDQQTPSQPQTYGSPIDYTAAPAPELIPTVPSPAPLSVPSSAPAALAAPNPAAVPGGPQPKLQSNMFKMQRNRTLKNSYVDVFNPSGAPMSAAPENVLAPMMAPAAVPQGGYFVPQQ
Protein: Tgm6 protein (Q14CG3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVNSNNDRGVVQGQWQGKYGGGTNPLNWRGSVAILQKWFKGRYKPVKYGQCWVFAGVMCTVLRCLGIATRVVSNFNSAHDTDGNLSVDKYVDSYGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYDGWQVLDATPQEESEGMFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDKRRERVYSDTKKIGRCISTKAVGSDSRVDITGLYKYPEGSRKERQVYSKAVKKLLSVEAWGRRRRIRRASVRGVWRDDLLEPVTKPSITGKFKVLEPPVLGQDLKLALCLTNLTARAQRVRVNVSGATILYTRKPVAEILRESHTVKLGPLEEKKIPVTISYSQYKGDLTEDKKILLAAMCLVSKGEKLLVEKDITLEDFITIKVLGPAVVGVTVTVEVLVINPLSESVKDCVLMVEGSGLLQGQLSIEVPSLQPQEKALIQFNITPSKSGPRQLQVDLVSSQFPDIKGFVIIHVATAK
Protein: Putative phosphatidate cytidylyltransferase (EC 2.7.7.41) (CDP-DAG synthase) (CDP-DG synthase) (CDP-diacylglycerol synthase) (CDS) (CDP-diglyceride pyrophosphorylase) (CDP-diglyceride synthase) (CTP:phosphatidate cytidylyltransferase) (Q9P381)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Supplies CDP-diacylglycerol, which may play an important role as both a precursor to phosphoinositide biosynthesis in the plasma membrane and as a negative effector of phosphatidylinositol 4-kinase activity, thereby exerting an effect on cell proliferation via a lipid-dependent signal transduction cascade.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Uncharacterized acyltransferase C1851.02
- Triacylglycerol lipase ptl3
- Lysophospholipid acyltransferase
- Phospholipase D1
- Putative lysophosphatidic acid:oleoyl-CoA acyltransferase
- Nuclear elongation and deformation protein 1
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- CTP-dependent diacylglycerol kinase 1
Sequence:
MARKRTNKRNNSDKENGNVGVVQNKDSASSKTTEPARLTKHKSLARKPSQNFITRTIWTFLLLGIFFTALAMGHFWVVLLVTIVQIGVYKEVIAIASVPSREKDLPWTRFINWYFLMTTLYYAYGESIYAYFHHLFIMDSFMLPLVLHHRFISFMLYIIGFVLFVASLKKGNYKFQFSQFCWTHMTLLLVVGQSHFMINNLFEGLFWFFVPVCYVVCNDVFAYLCGKMFGKHPLIQVSPKKTVEGFLGGWICTVVIGSLISYVLMHFKYFICPTRDLSTSAFSGLNCTPNSVFLPHTYTIPAVFVDTFRLPETITLAPIYFHLAIFATFSSLIAPFGGFFASGLKRAFKIKDFGASIPGHGGLTDRMDCQFLNGVFVYMYFQSFIAEKSTSVADLLDTAVYSLTTTQQVQLVEDLQNYLISHGKTSVQAICSKLLQNSK
Protein: Protein N-lysine methyltransferase METTL21A (EC 2.1.1.-) (HSPA lysine methyltransferase) (HSPA-KMT) (Hepatocellular carcinoma-associated antigen 557b) (Methyltransferase-like protein 21A) (Q8WXB1)
Organism: Homo sapiens (Human)
Function: Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members. Contributes to the in vivo trimethylation of Lys residues in HSPA1 and HSPA8. In vitro methylates 'Lys-561' in HSPA1, 'Lys-564' in HSPA2, 'Lys-585' in HSPA5, 'Lys-563' in HSPA6 and 'Lys-561' in HSPA8.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23349634}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 4
- Methyltransferase-like protein 22
- EEF1A lysine methyltransferase 2
- Histidine protein methyltransferase 1 homolog
- Protein FAM200C
- Hsp70-binding protein 1
- Electron transfer flavoprotein beta subunit lysine methyltransferase
Sequence:
MALVPYEETTEFGLQKFHKPLATFSFANHTIQIRQDWRHLGVAAVVWDAAIVLSTYLEMGAVELRGRSAVELGAGTGLVGIVAALLGAHVTITDRKVALEFLKSNVQANLPPHIQTKTVVKELTWGQNLGSFSPGEFDLILGADIIYLEETFTDLLQTLEHLCSNHSVILLACRIRYERDNNFLAMLERQFTVRKVHYDPEKDVHIYEAQKRNQKEDL
Protein: Protein suppressor of forked (P25991)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential protein, may play a role in mRNA production or stability.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cleavage stimulation factor 64 kD subunit
- Symplekin
- Cleavage stimulation factor subunit 1
- Pre-mRNA cleavage complex 2 protein Pcf11
- Factor interacting with poly
- Cleavage and polyadenylation specificity factor 73
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 4
- Probable cleavage and polyadenylation specificity factor subunit 2
- LD24014p
Sequence:
MSSARDLIKVDIEWGMERLVRAQQVVELRPYDIESWSVMIREAQTRPIHEVRSLYESLVNVFPTTARYWKLYIEMEMRSRYYERVEKLFQRCLVKILNIDLWKLYLTYVKETKSGLSTHKEKMAQAYDFALEKIGMDLHSFSIWQDYIYFLRGVEAVGNYAENQKITAVRRVYQKAVVTPIVGIEQLWKDYIAFEQNINPIISEKMSLERSKDYMNARRVAKELEYHTKGLNRNLPAVPPTLTKEEVKQVELWKRFITYEKSNPLRTEDTALVTRRVMFATEQCLLVLTHHPAVWHQASQFLDTSARVLTEKGVRTSVENISPILCVPVVNQIEWVMAFAWWWAKDVQAAKIFADECANILERSINGVLNRNALLYFAYADFEEGRLKYEKVHTMYNKLLQLPDIDPTLVYVQYMKFARRAEGIKSARSIFKKAREDVRSRYHIFVAAALMEYYCSKDKEIAFRIFELGLKRFGGSPEYVMCYIDYLSHLNEDNNTRVLFERVLSSGGLSPHKSVEVWNRFLEFESNIGDLSSIVKVERRRSAVFENLKEYEGKETAQLVDRYKFLDLYPCTSTELKSIGYAENVGIILNKVGGGAQSQNTGEVETDSEATPPLPRPDFSQMIPFKPRPCAHPGAHPLAGGVFPQPPALAALCATLPPPNSFRGPFVSVELLFDIFMRLNLPDSAPQPNGDNELSPKIFDLAKSVHWIVDTSTYTGVQHSVTAVPPRRRRLLPGGDDSDDELQTAVPPSHDIYRLRQLKRFAKSN
Protein: Protein TRC8 homolog (Q7KRW1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in growth inhibition that is dependent upon COP9 signalosome subunits CSN5 and CSN6. May modulate signalosome levels or compartmentalization. Probably functions in the same or a related pathway to VHL during early midline development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12032852}; Multi-pass membrane protein {ECO:0000269|PubMed:12032852}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 G2
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Endoplasmic reticulum lectin 1
- Derlin
- Nuclear protein localization protein 4 homolog
- Derlin-1
- Eukaryotic translation initiation factor 3 subunit F-2
- RING-type E3 ubiquitin transferase
- SD07518p
- COP9 signalosome complex subunit 5
Sequence:
MSVRTKVLGLVDVMMRVPPVMVIDEILKMDMGMQSWLYPDKDKASGALATPTEAPAVPSGQDPFTSIKELFSHMTTSAQSVLEQSIEKASEAAKTHGMLSSGFNSLMNELSKDQTLADVLSTTTVKFVLCVFAFLSAACIFMLWTRHLVMVYMFLTSLGLTFLSYWSNVSALALTERSPSMVEDLMSLNTTRLLDSGGVVMSLAPHLMAQWFMGMLFAYIHLGPRFEHVQRSMPIIFASPILLAMLPLPAKVVQHLPVVAVFTPIILTKITLMQSAMEASRTVYNGYQYAMNFVSNFGLSALIENEWQRLNVPNVLRVFWTIRLIQGGYALATTESDEPLDLMTATQKLLVDGCETMTAVLGMTGVISMFCHYIGRGFQWYLLTYDDEEKSLGTVSAVLFYILALQTGLTSLSPDKRFIRLCRNLCLLMTALLHFLHNIVSPILMSLSAARNPSRKRHVRALSVCAFLVVLSVSLLYHLWSQQSISTWLLAVTAFSVEVVVKVLVSLATYTLFLLDARRQFFWEKLDDYLYYVRAFGNSVEFCFGILLFINGAWILIFESAQNATGGGIRAIMMCIHAYFNIWCEARAGWSVFMKRRSAVHKISALPEATPAQLQAFDDVCAICYQEMYSAKITRCRHFFHGVCLRKWLYVQDRCPLCHEIMMYTDKADENAPEAEPAPAAQAEQPMRIYPRDDANNAAAQRRSPERAPVEASEQAPATSSSSAAATIGAEAVSAIVESAAAVGEARSLVSVASSSSATHRISASGSSDSSYMTASAQSPPPTATSAAAVATAAASNTTHMFRMSQDQQ
Protein: Type IV secretion system protein VirB9 (Q2GI58)
Organism: Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas)
Interaction partners:
- Type IV secretion system protein VirB10
- Type IV secretion system protein VirB8
- Type IV secretion system protein
- Type IV secretion system protein VirD4
- Type IV secretion system protein VirB6
- Type IV secretion system protein virB4
- Type IV secretion system protein VirB3
- Type IV secretion system protein VirB4
- Type IV secretion system protein,VirB6 family
- Type IV secretion system protein, VirB6 family
Sequence:
MMNFYKIYTILLLVLVMMFNSSAYAINRVDNPVTVDSRIKTFVYSNNEIYNVVFNYGYHSYIEFSKGETIKMLAMGNTVSWKVKPVGNKLFIMPLEKNGRTNMLIETNKGRSYAFDLICRSANESSDDNNDQAGYSDLIDLTYIVRFYYPKTEEDFELNQVKLPDISVPSAVQKIKKHVVIKPNNTSNHYILETKSENQNILPVELFDDGKLTYFKFSNDNQIIPQIFIYNNSEKKVPCKMLLLQNYVIIKGVHKNLYLEYKSESVKITNKKL
Protein: Fidgetin (Q9ERZ6)
Organism: Mus musculus (Mouse)
Function: ATP-dependent microtubule severing protein. Severs microtubules along their length and depolymerizes their ends, primarily the minus-end, suppressing microtubule growth from and attachment to centrosomes. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome (By similarity).
Subcellular location: Nucleus matrix {ECO:0000269|PubMed:16751186}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes to centrosomes throughout mitosis and to the spindle midzone during telophase. {ECO:0000250}.
Interaction partners:
- UBX domain-containing protein 7
Sequence:
MISSTSVYGLKMQWTPEHAQWPEQHFDITSTTRSPAHKVEAYRGHLQRTYQYAWANDDISALTASNLLKKYAEKYSGILEGPVDRPVLSNYSDTPSGLVNGRKNDSEPWQPSLNSEAVYPMNCVPDVITASKAGVSSALPPVDVSASIGSSPGVASNLTEPSYSSSTCGSHTVPSLHAGLPSQEYAPGYNGSYLHSTYSSQATPALPSPHPSPLHSSGLLQPPPPPPPPPALVPGYNGTSNLSSYSYPSASYPPQTAVGSGYSPGGAPPPPSAYLPSGIPAPTPLPPTTVPGYTYQGHGLTPIAPSALTNNSASSLKRKAFYMAGQGDMDSSYGNYSYGQQRSTQSPMYRMPDNSISNSNRGNGFDRNAETSSLAFKPTKQLMPSEQQRKFSSQSSRALTPPSYSTAKNSLGSRSSESFGKYTSPVMSEHGDDHRQLLAHPIQGPGLRAATSSNHSVDEQLKNTDTHLIDLVTNEIITQGPPVDWSDIAGLDLVKAVIKEEVLWPVLRSDAFSGLTALPRSILLFGPRGTGKTLLGRCIASQLGATFFKIAGSGLVAKWIGEAEKIIHASFLVARCRQPSVIFVSDIDMLLSSQVSEEHSPVSRMRTEFLMQLDTVLTSAEDQIVVICATSKPEEIDESLRRYFMKRLLIPLPDSTARHQIIVQLLTQHNYCLNDKEFALLVQRTEGFSGLDVAHLCQEAAVGPLHAMPATDLSAIMPSQLRPVTYQDFENAFCKIQPSISQKELDMYVEWNKMFGCSQ
Protein: Transmembrane protein RAM-5 (ZP domain-containing protein) (G5EC82)
Organism: Caenorhabditis elegans
Interaction partners:
- ZP domain-containing protein
- ZP domain-containing protein
- Protein lon-8
- Cuticle collagen 34
Sequence:
MQYSTKHVIGYIFSFVVLATSTDFDNAHVMGVPQVTCSAKLITVSFNTNIPFQGRISVFDKLFIPACNHDYSTNIQKNATFQMDILKCANPMFLKNGSRLLRAYVEIGFHPLVMTNSDRTFLVECLDNTIMPIVNRAQSFADCTHLVRMASEWSSMSEFQVGDAIVHEWSCKLPNPAKTQTFLTNCNALSQNGQIIHLIDENGCVIDSELMGDIVYSDHVPKLYARARIFKFLTDDKYRIECTLEFCNNGSPCKDRVFPPKCAFTKEEITSRSTKNQLEQSGMTTMPGIPSSAYDSRLKISSAWLTIKLNQYTETKGLHPRYHLKTFLDPTLHETISPNDADHFLMGISYREPIPKLSSQSELSHPDNNRVEGARILHSSAFQPIISPPIDSHEEFIETITFGSNLNSEPIVNVQKEMHLQKEPVHKVFTHKDPLKTEKTEKFMKLVQIENEDRNHGAALETTQQSRMFTTTMPSTMISTTTTPMTSSSRTDKLPSEHFNHPELDTFEKPKKSFEKSHSLVQMTETTTAPAANLKFYSTTASTKKLTPTTPYASAPPESSTQTPNSTKPTSIRNVTHSVPTVKKYDKFVNNNADWRFDDKAINDSDIVSEKQTSACYNATIISSQRQCKWSGVEHLLLIWSFASLIVWMMLIALFLYRYSSRKPQWIGFREQELRRVAQSRVLSQDHPWLHADAFEERNQSKNEIEINHFT
Protein: Tartrate-resistant acid phosphatase type 5 (EC 3.1.3.2) (Q6DHF5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Low molecular weight phosphotyrosine protein phosphatase
- Riboflavin kinase
- Acid phosphatase 2
- Biliverdin reductase B.
- Tartrate-resistant acid phosphatase type 5
- Ectonucleotide pyrophosphatase/phosphodiesterase 1
- FAD synthase
- Nudix-type motif 12.
- Phosphate-regulating endopeptidase homolog, X-linked
Sequence:
MAKKLAFLLISCLQTFSTASQTNQQASSLRFVGIGDWGGRPSYPFYTPHEADTAKELARVAQSSGLDFVLSLGDNFYYDGVKDVDDTRFKFSYEQVFSHPALMTIPWYLIAGNHDHRGNVSAQIAYSSRSERWIYPDLYYELNFKVPHSNTSLTILMTDTVVVCGNTYDGLDPVGPEDLAAANKQLAWIEQRLQSTKADFVIVVGHYPIWSIGHHGPTKCLISKLRPLLKKYNVSLYLSGHDHSLQFIREDDGSSFVVSGAGVEEDSSTDHRKSFPSAWQLFSSPVNQTSGSFVYFEVNKSEMLINYLQPDGKCVYQTSVHKHKVQL
Protein: Protein arginine N-methyltransferase 1 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT1) (Q63009)
Organism: Rattus norvegicus (Rat)
Function: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP and MAP3K5/ASK1. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway (By similarity). Methylates RBM15, promoting ubiquitination and degradation of RBM15 (By similarity). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity (By similarity). Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (By similarity). Methylates MAP3K5/ASK1 at 'Arg-85' and 'Arg-87' which promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5-induced activation of JNK. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Plays a role in regulating alternative splicing in the heart (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9JIF0}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm, cytosol {ECO:0000269|PubMed:15837430}. Cytoplasm {ECO:0000250|UniProtKB:Q99873}. Lysosome membrane {ECO:0000250|UniProtKB:Q99873}. Note=Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity). Upon methionine stimulation, localizes to the lysosome in an NPRL2-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q99873, ECO:0000250|UniProtKB:Q9JIF0}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Protein BTG2
- Forkhead box protein O1
- Forkhead box O6
- Forkhead box O3
- Forkhead box O4
- Histone H4
- Methylosome protein WDR77
- Small nuclear ribonucleoprotein-associated protein B
- Runt-related transcription factor 1
Sequence:
MAAAEAANCIMEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR
Protein: Vacuole morphology and inheritance protein 14 (Swollen vacuole phenotype 2 protein) (Q06708)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Regulates the synthesis of PtdIns(3,5)P2 by positive activation of FAB1 and by controlling FIG4 localization. Required for FIG4-mediated turnover of PtdIns(3,5)P2 after hyperosmotic shock. Essential for the control of trafficking of some proteins to the vacuole lumen via the multivesicular body (MVB), and for maintenance of vacuole size and acidity.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:11889142, ECO:0000269|PubMed:14528018, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18653468, ECO:0000269|PubMed:19037259}; Peripheral membrane protein {ECO:0000269|PubMed:11889142, ECO:0000269|PubMed:14528018, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18653468, ECO:0000269|PubMed:19037259}. Note=Limiting membrane of the vacuole. Localization requires FAB1 and FIG4.
Interaction partners:
- 1-phosphatidylinositol 3-phosphate 5-kinase FAB1
- Polyphosphoinositide phosphatase
- Vacuolar segregation protein 7
- Autophagy-related protein 18
- Phosphatidylinositol 3-kinase VPS34
- Vacuolar protein sorting-associated protein 30
- Serine/threonine-protein kinase VPS15
- DNA repair and recombination protein RAD54
- Vacuolar protein sorting-associated protein 38
- PtdIns3K complex I subunit atg38
Sequence:
MEKSIAKGLSDKLYEKRKAAALELEKLVKQCVLEGDYDRIDKIIDELCRDYAYALHQPMARNAGLMGLAATAIALGINDVGRYLRNILPPVLACFGDQNDQVRFYACESLYNIAKIAKGEILVYFNEIFDVLCKISADTENSVRGAAELLDRLIKDIVAERASNYISIVNNGSHGLLPAIKTDPISGDVYQEEYEQDNQLAFSLPKFIPLLTERIYAINPDTRVFLVDWLKVLLNTPGLELISYLPSFLGGLFTFLGDSHKDVRTVTHTLMDSLLHEVDRISKLQTEIKMKRLERLKMLEDKYNNSSTPTKKADGALIAEKKKTLMTALGGLSKPLSMETDDTKLSNTNETDDERHLTSQEQLLDSEATSQEPLRDGEEYIPGQDINLNFPEVITVLVNNLASSEAEIQLIALHWIQVILSISPNVFIPFLSKILSVLLKLLSDSDPHITEIAQLVNGQLLSLCSSYVGKETDGKIAYGPIVNSLTLQFFDSRIDAKIACLDWLILIYHKAPNQILKHNDSMFLTLLKSLSNRDSVLIEKALSLLQSLCSDSNDNYLRQFLQDLLTLFKRDTKLVKTRANFIMRQISSRLSPERVYKVISSILDNYNDTTFVKMMIQILSTNLITSPEMSSLRNKLRTCEDGMFFNSLFKSWCPNPVSVISLCFVAENYELAYTVLQTYANYELKLNDLVQLDILIQLFESPVFTRMRLQLLEQQKHPFLHKCLFGILMIIPQSKAFETLNRRLNSLNIWTSQSYVMNNYIRQRENSNFCDSNSDISQRSVSQSKLHFQELINHFKAVSEEDEYSSDMIRLDHGANNKSLLLGSFLDGIDEDKQEIVTPISPMNEAINEEMESPNDNSSVILKDSGSLPFNRNVSDKLKK
Protein: Rifin (C6KTF8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYINILLFELPLNILIYNQRNHYITRTPKATTRSLSECELYAPSNYDNDPQMKEVMDNFNRQTQQRFHEYDHRMKTTRQKCKEQCDKEIQKIILKDKLEKELMDKFATLHTDIQNDAIPTCVCEKSVADKVEKNCMKCTQNLGGIVAPSSGVLAGIAEGALYVWRDAEIVAAIAAAKEAGAAKGAAVGIKEGIKVLLNRLNTDFGLSPVRIKELESVINGTNYTDVTFIYEAIYTTYKRSCVPVDVSVRFTVADTDLTFCESVWNQTLAVSQRNMGTSPLPIIQKTAQKIVSDANFTAAATAETATEEATTTLTAKNTGEVNATYMGYQTPIIASIVAILVIVLVMIIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Thioredoxin domain-containing protein C13F5.05, mitochondrial (O13704)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative protein disulfide-isomerase C1F5.02
- ERO1-like protein 2
- Thioredoxin domain-containing protein C959.05c
- Uncharacterized protein C3D6.13c
- Protein disulfide-isomerase C17H9.14c
- Tryptophan synthase
Sequence:
MLFRIPTLFTLFLACFSLVSGVFGYSPMFGSNTIELNSKNFRKFVKAKGPSLVVFYAPWCGYCKKLVPTYQKLASNLHSLLPVTAVDCDADQNRAVCSQYQVQGFPTIKLVYPSSKGSSLSSTDYNGDRSYKSLQKFVSDSIPSKVKILTSEAKTQKFIQDAQNSSKVILISQKMKPTLLYKSLSNEFSSLPFSFMPAKANVNDLFNISAYVDTSDLPILFIKHPNNGTSFFSNSLNRDSIVEFLQSSIKDNNFSEYLATFCSKKSCIITIQDKDSDSGIDESIRKKYPKLHFVRLGRNTTVAERLEDTLDLGYSDTFLLSLKKSHYNAKPYGKPLRRWLEDIQVQQAGPSVSLPNDLLSKIK
Protein: UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase) (P17952)
Organism: Escherichia coli (strain K12)
Function: Cell wall formation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- D-alanine--D-alanine ligase B
- UDP-N-acetylenolpyruvoylglucosamine reductase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- Probable peptidoglycan glycosyltransferase FtsW
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- D-alanine--D-alanine ligase A
- Cell division protein FtsQ
Sequence:
MNTQQLAKLRSIVPEMRRVRHIHFVGIGGAGMGGIAEVLANEGYQISGSDLAPNPVTQQLMNLGATIYFNHRPENVRDASVVVVSSAISADNPEIVAAHEARIPVIRRAEMLAELMRFRHGIAIAGTHGKTTTTAMVSSIYAEAGLDPTFVNGGLVKAAGVHARLGHGRYLIAEADESDASFLHLQPMVAIVTNIEADHMDTYQGDFENLKQTFINFLHNLPFYGRAVMCVDDPVIRELLPRVGRQTTTYGFSEDADVRVEDYQQIGPQGHFTLLRQDKEPMRVTLNAPGRHNALNAAAAVAVATEEGIDDEAILRALESFQGTGRRFDFLGEFPLEPVNGKSGTAMLVDDYGHHPTEVDATIKAARAGWPDKNLVMLFQPHRFTRTRDLYDDFANVLTQVDTLLMLEVYPAGEAPIPGADSRSLCRTIRGRGKIDPILVPDPARVAEMLAPVLTGNDLILVQGAGNIGKIARSLAEIKLKPQTPEEEQHD
Protein: Urea transporter 1 (Solute carrier family 14 member 1) (Urea transporter B) (UT-B) (Urea transporter, erythrocyte) (Q5QF96)
Organism: Bos taurus (Bovine)
Function: Mediates the transport of urea driven by a concentration gradient across the cell membrane. Mediates the transport of urea across the cell membranes of erythrocytes and the renal inner medullary collecting duct which is critical to the urinary concentrating mechanism (By similarity). Facilitates water transport in erythrocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15845882, ECO:0000269|PubMed:22733730}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8VHL0}; Multi-pass membrane protein {ECO:0000255}. Note=Restricted to the basolateral membrane in various portions of the urothelium. {ECO:0000250|UniProtKB:Q8VHL0}.
Interaction partners:
- Aquaporin-3
Sequence:
MDDNPTAVKLDQGGNQAPQGRGRRCLPKALGYITGDMKEFANWLKDKPQALQFVDWVLRGISQVVFVSNPISGILILVGLLVQNPWCALNGCVGTVVSTLTALLLSQDRSAITAGLQGYNATLVGILMAIYSDKGNYFWWLLFPVSAMSMTCPVFSSALNSVLSKWDLPVFTLPFNMALSMYLSATGHYNPFFPSTLITPVTSVPNVTWPDLSALQLLKSLPVGVGQIYGCDNPWTGGIFLGAILLSSPLMCLHAAIGSLLGIIAGLSLSAPFEDIYAGLWGFNSSLACIAIGGTFMALTWQTHLLALACALFTAYLGASMSHVMAVVGLPSGTWPFCLATLLFLLLTTKNPNIYKMPISKVTYPEENRIFYLQSRKRTVQGPL
Protein: Catalase (EC 1.11.1.6) (P17336)
Organism: Drosophila melanogaster (Fruit fly)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular location: Peroxisome matrix {ECO:0000250|UniProtKB:P04040}.
Interaction partners:
- (S)-2-hydroxy-acid oxidase
- Peroxisomal multifunctional enzyme type 2
- catalase
- Sterol carrier protein 2
- 2-hydroxyacyl-CoA lyase
- Acyl-coenzyme A oxidase 1
- Hydroxysteroid dehydrogenase-like protein 2
- Trehalase
- Trehalase
- Glutathione peroxidase
Sequence:
MAGRDAASNQLIDYKNSQTVSPGAITTGNGAPIGIKDASQTVGPRGPILLQDVNFLDEMSHFDRERIPERVVHAKGAGAFGYFEVTHDITQYCAAKIFDKVKKRTPLAVRFSTVGGESGSADTARDPRGFAVKFYTEDGVWDLVGNNTPVFFIRDPILFPSFIHTQKRNPQTHLKDPDMFWDFLTLRPESAHQVCILFSDRGTPDGYCHMNGYGSHTFKLINAKGEPIYAKFHFKTDQGIKNLDVKTADQLASTDPDYSIRDLYNRIKTCKFPSWTMYIQVMTYEQAKKFKYNPFDVTKVWSQKEYPLIPVGKMVLDRNPKNYFAEVEQIAFSPAHLVPGVEPSPDKMLHGRLFSYSDTHRHRLGPNYLQIPVNCPYKVKIENFQRDGAMNVTDNQDGAPNYFPNSFNGPQECPRARALSSCCPVTGDVYRYSSGDTEDNFGQVTDFWVHVLDKCAKKRLVQNIAGHLSNASQFLQERAVKNFTQVHADFGRMLTEELNLAKSSKF