wanglab/gogpt-training-data huggingface dataset:
Protein: Hsp90 co-chaperone Cdc37-like 1 (Hsp90-associating relative of Cdc37) (Q7L3B6)
Organism: Homo sapiens (Human)
Function: Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11413142}.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Stress-induced-phosphoprotein 1
- Prostaglandin E synthase 3
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Secreted phosphoprotein 24
- Endoplasmin
- Heat shock 70 kDa protein 4
- Tyrosine-protein kinase HCK
Sequence:
MEQPWPPPGPWSLPRAEGEAEEESDFDVFPSSPRCPQLPGGGAQMYSHGIELACQKQKEFVKSSVACKWNLAEAQQKLGSLALHNSESLDQEHAKAQTAVSELRQREEEWRQKEEALVQREKMCLWSTDAISKDVFNKSFINQDKRKDTEDEDKSESFMQKYEQKIRHFGMLSRWDDSQRFLSDHPYLVCEETAKYLILWCFHLEAEKKGALMEQIAHQAVVMQFIMEMAKNCNVDPRGCFRLFFQKAKAEEEGYFEAFKNELEAFKSRVRLYSQSQSFQPMTVQNHVPHSGVGSIGLLESLPQNPDYLQYSISTALCSLNSVVHKEDDEPKMMDTV
Protein: Zinc finger protein VAR3, chloroplastic (Organelle Zinc finger 1) (Protein VARIEGATED 3) (Q8S9K3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of some protein complex required for chloroplast and palisade cell development. Involved in C-to-U editing of chloroplastic RNA. Controls a large number of chloroplastic editing sites. Binds the editing recognition trans-factors PCMP-H51/CRR28 and PCMP-H12/OTP82.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15340011, ECO:0000269|PubMed:25768119, ECO:0000269|PubMed:28213559}. Note=Localizes at punctuate loci in chloroplasts. {ECO:0000269|PubMed:25768119}.
Interaction partners:
- Protoporphyrinogen oxidase 1, chloroplastic
- Organelle RRM domain-containing protein 1
- Organelle RRM domain-containing protein 2
- ATP-dependent zinc metalloprotease FTSH 5, chloroplastic
- Glycine-rich RNA-binding protein 5, mitochondrial
- ATP-dependent zinc metalloprotease FTSH 2, chloroplastic
- Multiple organellar RNA editing factor 1, mitochondrial
- Glycine-rich RNA-binding protein 3, mitochondrial
- Pentatricopeptide repeat-containing protein At1g08070, chloroplastic
- Multiple organellar RNA editing factor 9, chloroplastic
Sequence:
MNNSTRLISLFSPHPPPLFLLRGLYISRIANLRRFHRRAFPPSSVASTNLCSFRPLVSLPPLIPTFPIGRFYNHQVRVSAADFVPSYHNQQLPEWTELLQSLSKAGYFSDSGSISGLESEFFPGFPDELLRPALACLALARERPELLEMLSRRDVEVLVENGKPFLFKTGPDSLKRMSLYLRSGLQGIGKLMDMEKASTVDLMRLILSYVVDVASSEESKQHNKEIMESSVRSLLSQIAKMSLRPPESNVHDTMQNQYSDRDGQGVRSFQNNVEMKRGDWICSRCSGMNFARNVKCFQCDEARPKRQLTGSEWECPQCDFYNYGRNVACLRCDCKRPRDSSLNSANSDYSSDPELERRLVENEKKAQRWLSKVAQGGSDANSVDTDEDFPEIMPLRKGVNRYVVSTRKPPLERRLANTENRVATDGNSKRSDDNALGSKTTRSLNEILGSSSSLTSRSDDKNVSSRRFESSQGINTDFVPFVPLPSDMFAKKPKEETQIGLIDNIQVDGFSGGNQNVYQEDKSDANHSGKETDRLEKEDHKSEEPARWFKRVTELHNVSDLESAIPQEISPEKMPMRKGENRFVVSRKKDRSLTSPAYKRPEDSDFVPFVPFPPDYFAKEKQPKESIDTLPAPATENVSQVVQQEPREPSINKSDTVAVKIRNGKSLEGSLVKESDLLDMSEEAKAERWFKRVAEIKNISELSEIPDEDFPSIMPMRKGVNRFVVSKRKTPLERRLTSQRHQRNPHITNSDPTGKGDK
Protein: Alpha-L-arabinofuranosidase A (ABF A) (Arabinosidase A) (EC 3.2.1.55) (Q8NK90)
Organism: Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Function: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides.
Subcellular location: Secreted {ECO:0000269|PubMed:16233515}.
Interaction partners:
- Alpha-L-arabinofuranosidase B
- Alpha-L-arabinofuranosidase.
- Exopolygalacturonase X
- NADP
- Alcohol dehydrogenase GroES-like domain-containing protein.
- Endo-polygalacturonase D
- Alcohol dehydrogenase.
- Polygalacturonase
- Polygalacturonase
- Kinesin-like protein
Sequence:
MVAFSALSGVSALSLLLCLVQHAHGVSLKVSTQGGNSSSPILYGFMFEDINHSGDGGIYGQLLQNPGLQGTTPNLTAWAAVGDATIAIDGDSPLTSAIPSTIKLDVADDATGAVGLTNEGYWGIPVDGSEFQSSFWIKGDYSGDITVRLVGNYTGTEYGSATITHTSTADNFTQASVKFPTTKAPDGNVLYELTVDGSVAAGSSLNFGYLTLFGETYKSRENGLKPQLANVLADMKGSFLRFPGGNNLEGNSAENRWKWNETIGDLWDRPGREGTWTYYNTDGLGLHEYFYWCEDLGLVPVLGVWDGFALESGGNTPITGDALTPYIDDVLNELEYILGDTSTTYGAWRAANGQEEPWNLTMVEIGNEDMLGGGCESYAERFTAFYDAIHAAYPDLILIASTSEADCLPESMPEGSWVDYHDYSTPDGLVGQFNYFDNLDRSVPYFIGEYSRWEIDWPNMKGSVSEAVFMIGFERNSDVVKMAAYAPLLQLVNSTQWTPDLIGYTQSPDDIFLSTSYYVQEMFSRNRGDTIKEVTSDSDFGPLYWVASSAGDSYYVKLANYGSETQDLTVSIPGTSTGKLTVLADNDPDAYNSDTQTLVTPSESTVQASNGTFTFSLPAWAVAVLAAN
Protein: Transcription factor E2F6 (E2F-6) (O75461)
Organism: Homo sapiens (Human)
Function: Inhibitor of E2F-dependent transcription. Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Has a preference for the 5'-TTTCCCGC-3' E2F recognition site. E2F6 lacks the transcriptional activation and pocket protein binding domains. Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression. Represses expression of some meiosis-specific genes, including SLC25A31/ANT4 (By similarity). May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase.
Subcellular location: Nucleus {ECO:0000269|PubMed:9689056, ECO:0000269|PubMed:9704927}.
Interaction partners:
- Transcription factor Dp-1
- Polycomb group RING finger protein 6
- Chromobox protein homolog 3
- Transcription factor Dp-2
- E3 ubiquitin-protein ligase RING2
- Lethal
- WD repeat-containing protein 5
- MAX gene-associated protein
- RING1 and YY1-binding protein
- E3 ubiquitin-protein ligase RING1
Sequence:
MSQQRPARKLPSLLLDPTEETVRRRCRDPINVEGLLPSKIRINLEDNVQYVSMRKALKVKRPRFDVSLVYLTRKFMDLVRSAPGGILDLNKVATKLGVRKRRVYDITNVLDGIDLVEKKSKNHIRWIGSDLSNFGAVPQQKKLQEELSDLSAMEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAPREDSITVHIRSTNGPIDVYLCEVEQGQTSNKRSEGVGTSSSESTHPEGPEEEENPQQSEELLEVSN
Protein: Integrin subunit alpha 2 (A0A0G2K470)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
- Integrin beta-1
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Integrin beta-3
- Integrin beta-4
- Integrin beta-6
- Focal adhesion kinase 1
- Paxillin
- Basement membrane-specific heparan sulfate proteoglycan core protein
Sequence:
MGPGQAGGALLLQLLLLTQGLLSCLAYNVGLPGAKIFSGSSSEQFGYSVQQLTTPQGNWLLVGSPWSGFPDNRMGDVYKCPVDLPTATCEKLNLQNSASISNVTEIKTNMSLGLTLTRNPGTGGFLTCGPLWAHQCGNQYYATGICSDVSPDFQSLTSFSPAVQACPSLVDVVVVCDESNSIYPWEAVKNFLEKFVQGLDIGPKKTQVALIQYANDPRVVFNLTTYKNKEDMVQATSETRQYGGDLTNTFKAIQFARDIAYLPESGGRPGATKVMVVVTDGESHDGSKLQTVIQQCNDDEILRFGIAVLGYLNRNALDTKNLIKEIKAIASTPTERYFFNVADEAALLEKAGTLGEHIFSIEGTVQGGDNFQMEMAQVGFSADYSPQNDILMLGAVGAFDWSGTVVQETSYEHLIFPKQAFDQVLQDRNHSSFLGYSVAAISTENGVHFVAGAPRANYTGQIVLYSVNKHGNVTVIQSHRGDQIGSYFGSVLCSVDVDKDTITDVLLVGAPMYMNDLKKEEGKVYLFTITKGVLNQHQFLEGPEGTGNARFGSAIAALSDINMDGFNDVIVGSPVENENSGAVYIYNGHQGTIRTKYSQKILGSDGAFKSHLQFFGRSLDGYGDLNGDSITDVSIGALGQVVQLWSQSVADVATEASFTPDKIILLNKEAKITLKLCFRAKFRPPGQNHQVAILFNMTLDADQYSSRVTSRGIFRENSERFLQKTMVVSEVENCSEYHISIQKPSDVVNPLDLRVDISLEKPGTSPALEAYSETVKVFSIPFYKECGSDGICISDLILDVRQLPALRNQPFIVSNQNKRLTFSVTLKNRGESAYNTAVLAEFSENLFFASFSMPVDGTEVTCQIGSSQKSVTCDVGYPALKSEQQVTFTINFDFNLQNLQNQAAINFQAFSESQETNKADNSVSLIVPLLYDAELHLTRSTNINFYEISSDENAPSVINSVEDIGPEFIFSLKITAGSAPVSMASVTIHIPLHTKEKNPLLYLTGIQTDKAGDISCRAEINPLNLPHTASPVSFKSENFRHMKELDCKTTSCSNVSCWLKDLHMKAEYFINVTTRVWNRTFAASTFQTVQLTAAAEIDTHNPQLFVIEENAVTIPLMIMKPTEKAEVPTGVIIGSIIAGILLLLAMVAGLWKLGFFKRQYKKMGQNPDETDETTELNS
Protein: Selenide, water dikinase 2 (EC 2.7.9.3) (Selenium donor protein 2) (Selenophosphate synthase 2) (P97364)
Organism: Mus musculus (Mouse)
Function: Synthesizes selenophosphate from selenide and ATP.
Interaction partners:
- O-phosphoseryl-tRNA
- Thioredoxin reductase 3
- Selenocysteine lyase
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin reductase 1, cytoplasmic
- L-seryl-tRNA
- Selenide, water dikinase 1
- Protein adenylyltransferase SelO, mitochondrial
- Thioredoxin reductase-like selenoprotein T
- tRNA selenocysteine 1-associated protein 1
Sequence:
MAEAAAAGASGETMAALVAAEGSLGPAGWSAGRSFSNYRPFEPQTLGFSPSWRLTSFSGMKGUGCKVPQETLLKLLEGLTRPALQPPLTSGLVGGQEETVQEGGLSTRPGPGSAFPSLSIGMDSCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVSQSMSEKEREKVTPLMIKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQQNEFIMPDSAVVGDVLVLTKPLGTQVAANAHQWLDNPEKWNKIKMVVSREEVELAYQEAMFNMATLNRTAAGLMHTFNAHAATDITGFGILGHSQNLAKQQKNEVSFVIHNLPIIAKMAAISKASGRFGLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKPRVIEVLPRGASAAAAAAPDNSNAASEPSS
Protein: Dynamin-like GTPase OPA1, mitochondrial (EC 3.6.5.5) (Optic atrophy protein 1) [Cleaved into: Dynamin-like GTPase OPA1, long form (L-OPA1); Dynamin-like GTPase OPA1, short form (S-OPA1)] (O60313)
Organism: Homo sapiens (Human)
Function: Dynamin-related GTPase that is essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Coexpression of isoform 1 with shorter alternative products is required for optimal activity in promoting mitochondrial fusion. Binds lipid membranes enriched in negatively charged phospholipids, such as cardiolipin, and promotes membrane tubulation. The intrinsic GTPase activity is low, and is strongly increased by interaction with lipid membranes. Plays a role in remodeling cristae and the release of cytochrome c during apoptosis (By similarity). Proteolytic processing in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space (By similarity). Plays a role in mitochondrial genome maintenance.
Subcellular location: [Dynamin-like GTPase OPA1, long form]: Mitochondrion inner membrane {ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:20974897, ECO:0000269|PubMed:28746876, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}; Single-pass membrane protein {ECO:0000255}. Note=Detected at contact sites between endoplasmic reticulum and mitochondrion membranes. {ECO:0000269|PubMed:24616225}.; SUBCELLULAR LOCATION: [Dynamin-like GTPase OPA1, short form]: Mitochondrion intermembrane space {ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.
Interaction partners:
- Mitofusin-1
- Metalloendopeptidase OMA1, mitochondrial
- Mitofusin-2
- Mitochondrial fission 1 protein
- Prohibitin-2
- Presenilin-associated rhomboid-like protein, mitochondrial
- Presenilin-associated rhomboid-like protein, mitochondrial
- Serine/threonine-protein kinase PINK1, mitochondrial
- Outer mitochondrial transmembrane helix translocase
- Mitochondrial outer membrane protein SLC25A46
Sequence:
MWRLRRAAVACEVCQSLVKHSSGIKGSLPLQKLHLVSRSIYHSHHPTLKLQRPQLRTSFQQFSSLTNLPLRKLKFSPIKYGYQPRRNFWPARLATRLLKLRYLILGSAVGGGYTAKKTFDQWKDMIPDLSEYKWIVPDIVWEIDEYIDFEKIRKALPSSEDLVKLAPDFDKIVESLSLLKDFFTSGSPEETAFRATDRGSESDKHFRKVSDKEKIDQLQEELLHTQLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFPMKALGYFAVVTGKGNSSESIEAIREYEEEFFQNSKLLKTSMLKAHQVTTRNLSLAVSDCFWKMVRESVEQQADSFKATRFNLETEWKNNYPRLRELDRNELFEKAKNEILDEVISLSQVTPKHWEEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPKGKEHDDIFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRWLYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNLCRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQLAEDLKKVREIQEKLDAFIEALHQEK
Protein: D-dopachrome decarboxylase (EC 4.1.1.84) (D-dopachrome tautomerase) (P80254)
Organism: Rattus norvegicus (Rat)
Function: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8267597}.
Interaction partners:
- H-2 class II histocompatibility antigen gamma chain
Sequence:
MPFVELETNLPASRIPAGLENRLCAATATILDKPEDRVSVTIRPGMTLLMNKSTEPCAHLLISSIGVVGTAEQNRSHSSSFFKFLTEELSLDQDRIIIRFFPLEPWQIGKKGTVMTFL
Protein: Thyrotropin-releasing hormone receptor (Thyroliberin receptor) (Q86RL0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLPQIPSYIRTTAMFFCIVIMLLGVVGNVMVPIVIVKTKDMRNSTNIFLTNLSIADLLVLLVCTPTVLVEVNTRPETWVLGHEMCKAVPFVELTVAHASVLTILAISFERYYAICEPLKAGYVCTKGRAILICVLAWGIAALFTSPILWVAEYKLAEYIDGSSVAVCLTQAISDWTLAFFLMTISVFFVVPFVTLVVLYGIIARNLVSNRAAMLRARPTKPELSLKARKQVVLMLGAVVLSFFVCLLPFRVLTLWIILSTDQTLHDLGLVRYYSLLYFCRIMLYLNSAMNPILYNLMSTKFRRGFKRLCQDAGRLLLELVTLGRRKEDSSRGRRGTLSLGMGTNTNTNTNSSNATGATSSSILSRSSNRRCSEDISRTRLKIEMQMPCGSDLEAMAMLQHSTLGKGIARRVSDSRLMPLRNHQPRRHKPQISFDEESLEENKRSEGKIPTKCREKLPGIAREIVNLTENTL
Protein: Cytochrome P450 2K6 (EC 1.14.14.-) (F1Q8C3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Metabolizes aflatoxin B1 (AFB1) to the cytotoxic derivative AFB1 exo-8,9-epoxide. Does not show activity towards lauric acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15907766}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:15907766}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- HemK methyltransferase family member 1.
- Tripartite motif-containing 35-9.
- MICOS complex subunit
- Aspartate dehydrogenase domain-containing protein
- Arachidonate 12-lipoxygenase
- Si:dkey-174n20.1
- Retinol dehydrogenase 14a.
- Retinol dehydrogenase 14b
Sequence:
MALIEAFLLQGSPTGTILGALLLFLVIYLFSSSSSSQDKEKYPPGPKPLPLLGNLHILDLKKTYLSLLELSKKYGPIYTVYLGPKKVVILSGYKIVKEALVNLSEEFGDRDISPIFHDFNRGYGIAFSNGENWREMRRFALSTLRDFGMGRKRSEELIIEEIKYVKEEFEKFGGNPFETKLPLALAISNIIASIVFSVRFEYSNTKLHRMVGRAYENMKLTGSPSVQIYNMFPWLRPIVANRNQIVKNLRDTFKQNEELINGVMKTLDPFNPRGIVDSFLIRQQKDEESGKTDSLYNSNNLYCTVNNLFGAGTDTTVTTLRWGLLLMAKYPEIQAKVQDEIERVIGGRQPVVEDRKNLPYTDAVIHEIQRFADISPIGAPRQTTCDVHLNGYFIKKGTPVFPLLVSVLRDENEWETPDSFNPKHFLNKQGQFVKKDAFMPFGAGRRVCIGESLARMELFLFFTSLLQYFRFTPPPGVSEDDLDLTPVVGFTLNPKPHQLCAVKRS
Protein: Alcohol dehydrogenase (EC 1.1.1.1) (Q5V676)
Organism: Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Interaction partners:
Sequence:
MFLYLYSIFGNCFHPITRPGGCDRRHENGFPQPTRNGSMRAAIYRGPGDITVEEVPRPEIESPTDAIVRVTHTAVCGSDLWFYRGQSDREEGSRVGHEPMGIVEEVGDDVRSVEPGDRVFAPFVVSCGRCEFCRKGLHTSCVNGDSWGGDNGGGQGEYVRATEADGTLVRVPDRHADDEDTLEAILPLTDVMGTGHHAAVSAGVSEGDTCIVVGDGAVGLCGVLAARRLGAERIIAMGHHEDRLELAESFGATETVAARGQDAVDAADDLTNGGANHVLECVGAASAMETAIDVCRPGGTVGYVGVPHGLDDSGLDMFSLFGDNIGLNGGIAPVRAYADELLADVLQGTLDPSPIFTKTVDLNGVPEGYQAMDEREAIKVLVKL
Protein: Ion-translocating oxidoreductase complex subunit E (EC 7.-.-.-) (Rsx electron transport complex subunit E) (P77179)
Organism: Escherichia coli (strain K12)
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000269|PubMed:10411911, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Ion-translocating oxidoreductase complex subunit C
- Ion-translocating oxidoreductase complex subunit D
- Ion-translocating oxidoreductase complex subunit G
- Ion-translocating oxidoreductase complex subunit B
- Endonuclease III lyase)
- Ion-translocating oxidoreductase complex subunit A
- FAD:protein FMN transferase
- Probable pyruvate-flavodoxin oxidoreductase
Sequence:
MSEIKDVIVQGLWKNNSALVQLLGLCPLLAVTSTATNALGLGLATTLVLTLTNLTISTLRHWTPAEIRIPIYVMIIASVVSAVQMLINAYAFGLYQSLGIFIPLIVTNCIVVGRAEAFAAKKGPALSALDGFSIGMGATCAMFVLGSLREIIGNGTLFDGADALLGSWAKVLRVEIFHTDSPFLLAMLPPGAFIGLGLMLAGKYLIDERMKKRRAEAAAERALPNGETGNV
Protein: Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form] (Q06599)
Organism: Bos taurus (Bovine)
Function: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000250}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Receptor-interacting serine/threonine-protein kinase 1
- TNF alpha induced protein 3.
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- NF-kappa-B essential modulator
- Serine/threonine-protein kinase TBK1
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
Sequence:
MSTKSMIRDVELAEEVLSEKAGGPQGSRSCLCLSLFSFLLVAGATTLFCLLHFGVIGPQREEQSPGGPSINSPLVQTLRSSSQASSNKPVAHVVADINSPGQLRWWDSYANALMANGVKLEDNQLVVPADGLYLIYSQVLFRGQGCPSTPLFLTHTISRIAVSYQTKVNILSAIKSPCHRETPEWAEAKPWYEPIYQGGVFQLEKGDRLSAEINLPDYLDYAESGQVYFGIIAL
Protein: PRNP (D6PZR1)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MARLLTTCCLLALLLAACTDVALSKKGKGKPSGGGWGAGSHRQPSYPRQPGYPHNPGYPHNPGYPHNPGYPHNPGYPHNPGYPQNPGYPHNPGYPGWGQGYNPSSGGSYHNQKPWKPHKTNFKHVAGAAAAGAVVGGLGGYAMGRVMSGMNYHFDSPDEYRWWSENSARYPNRVYYRDYSSPVPQDVFVADCFNITVTEYSIGPAAKKNTSEAVAAANQTEVEMENKVVTKVIREMCVQQYREYRLASGIQLHPADTWLAVLLLLLTTLFAMH
Protein: WT1 transcription factor (J3KNN9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MDFLLLQDPASTCVPEPASQHTLRSGPGCLQQPEQQGVRDPGGIWAKLGAAEASAERLQGRRSRGASGSEPQQMGSDVRDLNALLPAVPSLGGGGGCALPVSGAAQWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYGPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTPTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGHSTGYESDNHTTPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL
Protein: Thioredoxin Y2, chloroplastic (AtTrxy2) (Q8L7S9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase that poorly activates chloroplastic malate dehydrogenase (NADP-MDH) and fructose-1,6-bisphosphatase. Provides reducing equivalents for peroxiredoxin Q.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:15531707, ECO:0000269|PubMed:19259774}.
Interaction partners:
- 2-Cys peroxiredoxin BAS1, chloroplastic
- FAD/NAD
- Protein SHORT HYPOCOTYL IN WHITE LIGHT 1
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- Probable RNA-dependent RNA polymerase 3
- Uncharacterized protein
Sequence:
MAISLATAYISPCFTPESSNSASPSRTLSSVRLPSQIRRFGSVQSPSSSTRFAPLTVRAAKKQTFNSFDDLLQNSDKPVLVDFYATWCGPCQLMVPILNEVSETLKDIIAVVKIDTEKYPSLANKYQIEALPTFILFKDGKLWDRFEGALPANQLVERIENSLQVKQ
Protein: ATP-binding cassette sub-family C member 9 (ATP-binding cassette, sub-family C (CFTR/MRP), member 9) (Q5RH87)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 8
- ATP-sensitive inward rectifier potassium channel 11
- Kir6.3 protein
Sequence:
MALSFCGNDRDSNAYSVDNGVLDNGCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNMRWILTFTLLFVHVCEIAEGIVSNTWMESNHLHLFMPAFMGFIAATTSVVYYHNIETANFPKLLLALFIYWILAFITKMIKLWKFAEASLGVQHLRFCITALLVVLYGLLMAVEINVIRVRKYVFFANPQRVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNPLIIGAHKRPIELKKIGKLPIAMRALTNYLRLKDSYEEQRQNTEDPEKSPSIWKSMYRAFGGSILLSSTFRYMADLLGFAGPLCISGIVEHLHNSTEIDRTNKTGNMTFGVYFMSSTELLQNTSVLAVLLFLALVLQRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNMSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYYLLGNSALIGAGVILLLAPVQYLIATKLADIQKSTLDYSTDRLKKTTEILKGIKLLKLYAWENIFCDRVEETRGKELTSLKTFALHTSMSIFMNAAIPIAAVLATFVTHAYIEEDRLSPAKAFASLALFHILVTPLFLLSTVVRFAVKALVSVQKLSEFLQSDEIGDDSWRNGDMCMSLEVGKKYKYQGDTKAINRKGRYRMDNYEQPVRRQLRPSETEDVAVQVNDGFFTWGSNLSTLSDINIRIPTGQLTMIVGQVGCGKSSLLLAMLGEMQTISGKVYWSNKNRYSVAYATQKSWLLNATVEENITFGSPFNKQRYKAVIDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTVVLVTHKLQYLIHADWIIAMKDGSVLREGTLKDIQTHDVELYEHWKTLMNRQDQELEKDTDLESQTTLERKTLRRAFYSREAKNHVDDEDEEEEVEEEDDDNMSTTTSRRSKIPWKMCCCYLSSGGFLMVFLMVSSKLAKHSVMVAIDYWLAAWTSSNPHNQSFVNSSFNHTLNDDATQIAEHRSYVPVFIILCAAAIALCLITSLTVEFLGVAAATNLHHNLLNKIIHAPIRFFDVTPLGQILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGVIAFVTPAFLIALVPLAVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHEARFKQRMLELTDTNNTAYLFLSAANRWLEVRTDYLGAVIVLTAAVAAIWSTSPSGLVGLGLTYALTLTNYLNWVVRNLADLEVQMAAVKKVNSFLSTESENYEGSMDVSQVPEDWPQHGEITIHDLCVRYDSMLKPVLKHVNAHINPGQKVGICGRTGSGKSSLSLAFFNMVDVFEGKIVIDGIDICKLPLQTLRSRLSIILQDPVLFSGSIRLNLDPERTCTDDRLWEALEIAQLKNMVKALPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHLVSSILEAEQVLVFSSGILVENDSAINLLAQEDSLFGILVRTHK
Protein: Conserved domain protein (A0A0H2UQB9)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MNEIKCPNCGEVFTVNESQYAELLSQVRTAEFDKELHDRMKQELALAEQKAMNEQQTKLAQKDQEIAQLQSQIQNFDTEKELAKKEVEQTSHEALLAKDKEVQLLENQLATLRLEHENQLQKTLSDLEKERDQVKNQLLLQEKENELSLASVKQNYEAQLKAASEQVEFYKNFKAQQSTKAIGESLEQYAESEFNKVRSFAFPNAYFEKDNKVSSRGSKGDFIFRECDENGVEIISIMFEMKNEADGTEKKHKNADFYKELDKDRREKNCEYAVLVTMLEADNDYFNTGIVDVSHEYEKMYVVRPQFFIQLIGLLRNAALNSLKYKQELALVREQNIDITHFEEDLDAFKLAFAKNYNSASTNFGKAIDEIDKAIKRMEEVKKFLTTSENQLRLANNKLEDVSVKKLTRKNPTMKAKFEALKGE
Protein: RE22242p (Q86P23)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAKLFVVFAVLALAAFNEASASDPLLRYKRQATTEETKKEESFEKELCKDKDAGEWFRLVAGEGDNCRDVIQCTSSGLQAIRCPAGLYFDIEKQTCDWKKSVKNCKSKNKERRVKPLLHTDEPLCQDGFLACGDGNCIERGLFCNGEKDCSDGSDENTCDIDNDPNRAPPCDPAVCVLPDCFCSEDGTSIPGDLPAKDVPMMITITFDDAINNNNIELYKEIFKDRKNPNGCSIKATYFVSHKYTNYSAVQETARKGHEIAVHSITHNDEERFWSNATVDDWAKEMAGMRIITEKFANITDNSVVGVRAPYLRVGGNNQFTMMEEQAFLYDSTITAPLSNPPLWPYTMYFRMPHRCHGNLQSCPTRSHAVWEMVMNELDRREDPVNDEYLPGCAMVDSCSNILTGDQFYNFLNHNFDRHYDQNRAPLGLYFHAAWLKNNPEFLDAFLYWIDEILANHNDVYFVTMTQVIQWMQNPRTISEVKNFEPWREKCVVEGKPACWVPNTCKLTSKEVPGETINLQTCVRCPNNYPWVSDPTGDGFF