wanglab/gogpt-training-data huggingface dataset:
Protein: Rab-GAP TBC domain-containing protein (Q17491)
Organism: Caenorhabditis elegans
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Tubby protein homolog 1
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26
- Cationic amino acid transporter C-terminal domain-containing protein
- Trafficking protein particle complex subunit 11 domain-containing protein
- LiPid Depleted
- Bridge-like lipid transfer protein family member 1 C-terminal domain-containing protein
Sequence:
MNSPGVSANFFIPLSFDATSLIKYKLSDDLLARVAASGSLRSSSCRSAVWRLVLRCLPYETSDWEISLSRSRNLYRAHKENHLIDPHDTKFSQDPEFNNPLASIEQNPWNTFFEDNDLRDIIGKDVSRTFPEIEFFQNTSIRQMMSDILLVYAKEHPFVNYRQGMHEILAPLIFVIYSDNEAFQHAKENDELKMLTVEEEDILNCLFCKEYLEQDSYNLFCSVMLEVSRWYEEPTVTESPKRPIPKEPYMRVQDSAPASRLMEDLIDIGNLLHEIDPTLAKHLSTLDIPPQLYGIRWLRLLFGRELPLHDLLFLWDVLLIDRPIAPLAKCMFVSLLVQIRHLLLSSDYGGCLQYLMRYPPIADIDSFVKLARHYRNPKKNAKPMIKSNNFSHITVAGSSHPNRTQRPQRPPAAVNSKNDGAESPSTILALAPVFQKVKNTIRDRSNTVSGPSSPRRSNEPLREPLRTPQKKDNWANEVQMMEEQVSTLQTRLNEQDMMCCQVSKALEIYAEDVRNAKSSELCAVLSQNLLELSKTLMSIKTVPVGTSPPKHSRNGISDIQPKPRDSQPIRQHNEMVDMATKRPPL
Protein: Cytochrome P450 6g1 (EC 1.14.-.-) (CYPVIG1) (Cyp6-like protein) (Q9V674)
Organism: Drosophila melanogaster (Fruit fly)
Function: Necessary and sufficient for resistance to insecticides DDT and imidacloprid. May be involved in the metabolism of insect hormones.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- CHK domain ov1
- Ecdysone 20-monooxygenase
- Glutathione S transferase E2
Sequence:
MVLTEVLFVVVAALVALYTWFQRNHSYWQRKGIPYIPPTPIIGNTKVVFKMENSFGMHLSEIYNDPRLKDEAVVGIYSMNKPGLIIRDIELIKSILIKDFNRFHNRYARCDPHGDPLGYNNLFFVRDAHWKGIRTKLTPVFTSGKVKQMYTLMQEIGKDLELALQRRGEKNSGSFITEIKEICAQFSTDSIATIAFGIRANSLENPNAEFRNYGRKMFTFTVARAKDFFVAFFLPKLVSLMRIQFFTADFSHFMRSTIGHVMEERERSGLLRNDLIDVLVSLRKEAAAEPSKPHYAKNQDFLVAQAGVFFTAGFETSSSTMSFALYEMAKHPEMQKRLRDEINEALVEGGGSLSYEKIQSLEYLAMVVDEVLRMYPVLPFLDREYESVEGQPDLSLKPFYDYTLENGTPVFIPIYALHHDPKYWTNPSQFDPERFSPANRKNIVAMAYQPFGSGPHNCIGSRIGLLQSKLGLVSLLKNHSVRNCEATMKDMKFDPKGFVLQADGGIHLEIVNDRLYDQSAPSLQ
Protein: Alkyl transferase (EC 2.5.1.-) (B9W9M1)
Organism: Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
Interaction partners:
Sequence:
MSSGPFYRSYSFNALWALVFKFPLFAYFVGFIEDFVISIIKTGPIPKHIAMIMDGNRTYAKKHRLPLKEGHFAGANALVKVLEVCYKVGIEQVTIYAFSLENFNRSKEEVDTLFALLRDKLKVMSEHEDSYARYNKVRIRIIGNRSFIPEDILKDLENVEETTKDFGSKKTLNVCFPYTARDEITYAVKSIASKRVSGELNNRNKITTKTIEKNFYFGDDVPPLDILIRTSGHTRLSDFLLWQCTTECTIEFPDVLWPDFGFISIMSILFKWSYYRTIQIEEEAIRGKEPRVQEVIPPVLLKELPNPPPATSVI
Protein: Auxin efflux carrier component 5 (AtPIN5) (Q9FFD0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin transporter regulating intracellular auxin homeostasis and metabolism. Mediates the auxin transport from the cytosol into the lumen of the endoplasmic reticulum. May also act as an auxin efflux carrier when located to the cell membrane. PIN5 and PIN8 may have an antagonistic/compensatory activity. Involved in unfolded protein response (UPR) activation. Involved in the control of vein patterning. Promotes vein formation. PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19506555, ECO:0000269|PubMed:20439545, ECO:0000269|PubMed:24692422}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:24692422}; Multi-pass membrane protein {ECO:0000305}. Note=Along the root developmental zones, the localization gradually shifted from cell membrane localization in the meristematic epidermal cells to internal localization in the older elongating epidermal cells. Localizes to the cell membrane in the pavement and guard cells of the cotyledon and to internal compartments in the vascular tissues. {ECO:0000269|PubMed:24692422}.
Interaction partners:
- Protein PIN-LIKES 2
- Auxin transporter protein 1
- Protein PIN-LIKES 5
- Auxin transporter-like protein 3
- ABC transporter B family member 1
- ABC transporter B family member 19
- ABC transporter B family member 4
- Auxin transporter-like protein 2
- Protein WALLS ARE THIN 1
- Auxin-binding protein 1
Sequence:
MINCGDVYKVIEAMVPLYVALILGYGSVKWWHIFTRDQCDAINRLVCYFTLPLFTIEFTAHVDPFNMNYRFIAADVLSKVIIVTVLALWAKYSNKGSYCWSITSFSLCTLTNSLVVGVPLAKAMYGQQAVDLVVQSSVFQAIVWLTLLLFVLEFRKAGFSSNNISDVQVDNINIESGKRETVVVGEKSFLEVMSLVWLKLATNPNCYSCILGIAWAFISNRWHLELPGILEGSILIMSKAGTGTAMFNMGIFMALQEKLIVCGTSLTVMGMVLKFIAGPAAMAIGSIVLGLHGDVLRVAIIQAALPQSITSFIFAKEYGLHADVLSTAVIFGMLVSLPVLVAYYAALEFIH
Protein: Cytochrome P450 4A22 (CYPIVA22) (Fatty acid omega-hydroxylase) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) (Q5TCH4)
Organism: Homo sapiens (Human)
Function: Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate and palmitate. Shows no activity towards arachidonic acid and prostaglandin A1. Lacks functional activity in the kidney and does not contribute to renal 20-hydroxyeicosatetraenoic acid (20-HETE) biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Cytochrome P450 4A11
- Cytochrome P450 2J2))
- Cytochrome P450 2E1
- Cytochrome P450 1A2
- Cytochrome P450 2U1
- Cytochrome P450 2B6
- Cytochrome P450 2A6
- Cytochrome P450 2C9
- Cytochrome P450 1A1
- Cytochrome P450 2S1
Sequence:
MSVSVLSPSRRLGGVSGILQVTSLLILLLLLIKAAQLYLHRQWLLKALQQFPCPPSHWLFGHIQEFQHDQELQRIQERVKTFPSACPYWIWGGKVRVQLYDPDYMKVILGRSDPKSHGSYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFHNDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKSAFSHQGSIQVDRNSQSYIQAISDLNSLVFCCMRNAFHENDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHGLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNLEVFDPSRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNQLKVARALTLLRFELLPDPTRIPIPMARLVLKSKNGIHLRLRRLPNPCEDKDQL
Protein: YopE regulator (P31491)
Organism: Yersinia pestis
Function: Positive regulator of YopE.
Interaction partners:
Sequence:
MYSFEQAITQLFQQLSLSIPDTIEPVIGVKVGEFACHITEHPVGQILMFTLPSLDNNDEKETLLSHNIFSQDILKPILSWDEVGGHPVLWNRQPLNSLDNNSLYTQLEMLVQGAERLQTSSLISPPRSFS
Protein: Galectin (G5EFI4)
Organism: Caenorhabditis elegans
Interaction partners:
- Galectin
- Galectin
Sequence:
MITRTIVCLSLAALVSCQGDASDPKETNYKKFIGEQEYKLPFKTRVSEPLAVGQTIHAVGTLSEKPTRVDFNFHKGSAKDADLPLHFSIRFNEGLLGSGKLIYNTFENGNWSEDEQRISNPFKAGQEFDLRVRILEGKFQVFANRLEVGVFTQRLPLDGIDHVSIRGDLSKLRLFHYGGRIFPNPYMAVAGLTPGKRLDISALPKGKRVNVNLYRENKEYALQVSIRYNEGAVVRNAMTSNVWGKEEREGKMPLDKKQVFDITIINEEYSFQIFLNNERFTTFSHRGSPSDIKTLEIDGDVEIQTVTINDAPGV
Protein: Volume-regulated anion channel subunit LRRC8E (Leucine-rich repeat-containing protein 8E) (Q6NSJ5)
Organism: Homo sapiens (Human)
Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine. Mediates efflux of amino acids, such as aspartate, in response to osmotic stress. The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition. Also plays a role in lysosome homeostasis by forming functional lysosomal VRAC channels in response to low cytoplasmic ionic strength condition: lysosomal VRAC channels are necessary for the formation of large lysosome-derived vacuoles, which store and then expel excess water to maintain cytosolic water homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24790029, ECO:0000269|PubMed:26824658, ECO:0000269|PubMed:28193731}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:24790029}. Lysosome membrane {ECO:0000269|PubMed:33139539}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:33139539}; Multi-pass membrane protein {ECO:0000305}. Note=In the absence of LRRC8A, resides primarily in the endoplasmic reticulum (PubMed:24790029, PubMed:33139539). Requires LRRC8A for localization at the cell membrane or lysosome membrane (PubMed:24790029, PubMed:33139539). {ECO:0000269|PubMed:24790029, ECO:0000269|PubMed:33139539}.
Interaction partners:
- Volume-regulated anion channel subunit LRRC8A
Sequence:
MIPVAEFKQFTEQQPAFKVLKPWWDVLAEYLTVAMLMIGVFGCTLQVTQDKIICLPNHELQENLSEAPCQQLLPRGIPEQIGALQEVKGLKNNLDLQQYSFINQLCYETALHWYAKYFPYLVVIHTLIFMVCTSFWFKFPGTSSKIEHFISILGKCFDSPWTTRALSEVSGENQKGPAATERAAATIVAMAGTGPGKAGEGEKEKVLAEPEKVVTEPPVVTLLDKKEGEQAKALFEKVKKFRMHVEEGDILYTMYIRQTVLKVCKFLAILVYNLVYVEKISFLVACRVETSEVTGYASFCCNHTKAHLFSKLAFCYISFVCIYGLTCIYTLYWLFHRPLKEYSFRSVREETGMGDIPDVKNDFAFMLHLIDQYDSLYSKRFAVFLSEVSESRLKQLNLNHEWTPEKLRQKLQRNAAGRLELALCMLPGLPDTVFELSEVESLRLEAICDITFPPGLSQLVHLQELSLLHSPARLPFSLQVFLRDHLKVMRVKCEELREVPLWVFGLRGLEELHLEGLFPQELARAATLESLRELKQLKVLSLRSNAGKVPASVTDVAGHLQRLSLHNDGARLVALNSLKKLAALRELELVACGLERIPHAVFSLGALQELDLKDNHLRSIEEILSFQHCRKLVTLRLWHNQIAYVPEHVRKLRSLEQLYLSYNKLETLPSQLGLCSGLRLLDVSHNGLHSLPPEVGLLQNLQHLALSYNALEALPEELFFCRKLRTLLLGDNQLSQLSPHVGALRALSRLELKGNRLEALPEELGNCGGLKKAGLLVEDTLYQGLPAEVRDKMEEE
Protein: Zinc finger protein jing (Zinc finger protein rhumba) (Q7KHG2)
Organism: Drosophila melanogaster (Fruit fly)
Function: May functionally interact with Polycomb group (PcG) and trithorax group (trxG) proteins to repress transcription (Probable). Required for Egfr pathway function and MAPK activity in CNS midline and tracheal placodes and for CNS axon development and tracheal tubule development. Required to establish the primary axon scaffold in the brain and for lateral positioning of longitudinal glia, longitudinal axons and neurons. Required for glial survival. Required to establish the proximo-distal axis of the developing leg and for wing vein and alula development. Required for regenerative growth in leg imaginal disks. Required for the initiation of anterior migration of border cells of the ovary.
Subcellular location: Nucleus {ECO:0000269|PubMed:11152631, ECO:0000269|PubMed:12015288}.
Interaction partners:
- Polycomb protein Su
- Histone-lysine N-methyltransferase E
- Chromatin assembly factor 1 p55 subunit
- Polycomb protein esc
- Polycomb protein esc
- Jing interacting gene regulatory 1, isoform A
- Pipsqueak, isoform M
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MPPHILGSASGSSSTAAASPPTSSASQTPPSPAIHHSHLSQHNATSAMSKPTTPQRHGNPSLLPTLQWPWNTSLGSTSTAVPAASANKNKRTAAGSGAALGLSGEGSCLTGGGAASAKKARSDLPGSFDASKRLKVAAMEESQTKITGFFKSQMKPSPGGGKLSPQPGQQSNPANTLTMSTPATTASLNKYFNILSQLKEQKAQQQQQQQQASKTLPTPAPVAPVPSAPPVAPVVVTPSPSLPVPALKKIERSNKQPAKIAQVAPNLRKTPSSGSSGSSSSSSSSSSNGSNTGKSPTKKHVAIAPRTPEMKQQQQQGKAAMVYRPPVTSTALKQKQISPPAPVAAHTPAPAPALNPTPAPANPTLYQLPVQLPNLVQLPPQLAAAANIMQLNNVAKAAVAAAATNNAAAQAAQAAQAAAAQYFLNGTVFKLQQVTTATTTTATTATAAAAPAGNPFGLLNLATAGNPFGLPNANGQFPIEAIPGAGSYLHHQLLLARQNNMSLNETMASNSCGNMNFVNPLNNQQVGLKDNKLYIVNSAEYLGYLMSLQIALNNQQHQQQQIISATQPPPLAATNNNSTNTATQPPPLAATNNTNSNTANNSTASNSINHNASNNLSNINNTAIQPQRAIVKPPLHSSTQPPPLVTISSMPACSPAAASSPAAKRSLPAAKPYQKRLTAKGRVGTAPIIATPTTPPPLVPTSATKELGQLRKSTGTTGTPTGTPTPTPPLVSIAPSKLTPTLSVSKQGPTMKLANSAPDLFDLVKNSKLVAKVSQPLTPLPFSSPSSSSNGSHGSHGMRSSPALSTSNSCTLSAFSKIKVETTELASQTGSLTSSSIPTISLKPQSFAGQLPKREPESETDTLKHDLLPDCTNSNSNSNSCSSSTYSHSVSSAADLSLEASTPAPSPSPSASPSGLGSPSPAASNLSASSRRAASQTDMLSELVTSSCISSGGDDCSQATDSPPMPALPLAKSEDATTPISTVSGGSSSGSSNYDEEDDKSVASLETHQTHKRLRDLPTPESGIGGSLSNSESSNSIADAISSKSASVGPPTTAASSASSSASDSNSLASNAPSPASPEDCSAAPSPACSASTTGSIPPSTVVDIAMVEATSKSLPKSAISPILSQPKTIRFPAGAGASGKGGKRHDGVCYWDKCNKKHESNSKLLDHMQTHHVNTQTGPFACLWVGCKVYNKESCSRRWLERHVLSHGGSKQFKCIVEGCGLRFGSQLALQKHVNNHFNATDNARESTSKRTSDPPVPKQLRKNGKKLRYRRQPFSARMFDFFDTGIMEGLQHRLRQISTLTNGAQAIEFQGQCMMRRRNSQGGYECFVRWSPREIISDEWLPECLNRTRQHTKVLHIKQMRPAEKTRVDSLLSTAFRLRYDSHLFADDYNVNEQQVGEASGSDCDEDGDGDQEEEDLEDQDEDEEEDGSSSSRSASCETVSSYQQVLSIAKLQMQQRRKHPRKPPKVTPPAREKLVPTDALVPI
Protein: Putative SPATULA (Q948F6)
Organism: Oryza sativa (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGLDRCESEEALGSSESEQPTRPARPRGKRSRAAEVHNLSEKRRRSRINEKMKALQSLIPNSSKTDKASMLDDAIEYLKQLQLQVQMLSMRNGLYLPPVNLSGAPEHLPIPQMSAALDQNSAKASDPSVVLQPVNQTSGALLPFELASQHKPLFLPGVPNATALEPRFLVESSRSNLQSLRFTEPAEMIYPDEMMLKHRLTSASESTIVPGTDEKSVRQNTYMMNADRFDRYALSKDQLQHIMPKNTESVLDMPHLQRILTKVLIVSDYKLTIQLPILDRLQTSDTKVRVEGRIKVNP
Protein: Sterol regulatory element-binding protein 1 (Sterol regulatory element-binding transcription factor 1) (Q90ZM5)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004557}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004557}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004394}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSALGFDDAALEGLALELRAASDIDTALLSDIDDMLQLINTPDNDFSGLFDAPFAAPDSTVSPGLPPAPTTYLGPSKPPPTGNVFPAPPVLPTFTPQPPAPLLPAPGPPAAPGVKEEPVAVPSSQPQPGVMLTPSFVPASPGQFSSQPVVGFQNQHSFPAVQPGGAAQSPLPTPQPAQPVALPGPVQSVAPQQLLAPGPAATTQPVSPQIQPVPVLLQPHFIKADSLLLTAVKTDAGGAKTSSITSLATSSTAAPLQVPALVSGGTILATVPLVVDAEKLPINRLAPSGKAALLQSKGEKRTAHNAIEKRYRSSINDKIVELKDLVVGTEAKLNKSAILRKAIEYIRFLQQSNQKLKQENLSLKMAVQKSKSLKDLVASCGAGPKAEASMEVAKAEVMEMPTPPPSDVGSPSRGSPLSLSGGSSNSSSDSEPDSPLCNHGKVKQENPPPSPGSQGMLDRSRMALCAFVFLCLSFNPLASLLRGSSAPAPSGSLGTAGPGRSIMAESGTAEEPWGWSQWLWPTLVFWGLNVALVLGAVVRLFVYGEPVTPPHSESSVLFWRHRRQADLDLDRGDFAQGAQHLRTALGALGRPLPASHGDLACSLLWSLLRHLLQRLWVGRWLAARAGGLRPDPPPRAHVRQSARNAAMAYHRLHQLHLAGKQAGGHLLAINLALSAVNLAECAGDAVSVAALAEIYVAAALRVKASLHRCFHFLARPFLCSARRVALSHGGAVPPAMQWLCHPLGHRFFVDGDWAVKGVPRETIYSSAGDPVDPLAQVTQLFREHLLEKALYCVAMPEPGRPAAQGEGCFSDALEYLQLLNGCSHASSMPGPMPSISSGLAAVTGTDPVSKWWASLIGTVIHWLKGDEEGAERLYPLVEAMPRALQSSEKPLPRAALHSFKAVRAMLSKQDGSQASLSHCEKASSCLRESLELCSPPKCTIDKAVQLLLCDLLLVTRTNLWQQQMSASQQLRGTYQASALELRGFSRTSASLRRLAQTLRPAMRRVFLHEATARLMARASPTRTHQLLDRSLRRRGVQGSKAAGEPESHPTPREHAEALLLACCYLPPSFLSAPGQRVGMLAEAARTLEKLGDRRTLHDCQQMIIKLGSGTTVTSG
Protein: Transposon Ty1-ML2 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q03434)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDRSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Type 1 encapsulin shell protein (C0ZVK4)
Organism: Rhodococcus erythropolis (strain PR4 / NBRC 100887)
Function: Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells 21-24 nm in diameter. Empty organelles can be expressed in E.coli. Cargo proteins (DypB) are targeted to the interior via their C-terminal extensions.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:24981030}.
Interaction partners:
Sequence:
MTNLHRDLAPISAAAWAEIEEEASRTFKRHVAGRRVVDVEGPSGDDLAAIPLGHQVPINPLADGVIAHARQSQPVIELRVPFTVSRQAIDDVERGAKDSDWQPVKDAAKQIAFAEDRAIFEGYPAASITGVRASGSNPELKLPIDAKDYPEAISQAITSLRLAGVNGPYSLLLNADAFTAINETSDHGYPIREHLRRVLDGEIIWAPAIDGAFLLSTRGGDYELHLGQDLSIGYLSHDANSVELYFQESMTFLMYTSEAVVSLA
Protein: alanine transaminase (EC 2.6.1.2) (Q4GYI2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Aspartate aminotransferase
- aspartate transaminase
- NAD-specific glutamate dehydrogenase
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Isocitrate dehydrogenase
- Isocitrate dehydrogenase
- oxoglutarate dehydrogenase
- 2-oxoglutarate dehydrogenase subunit, putative
- Succinate dehydrogenase, putative
- fumarate hydratase
Sequence:
MDIYLFSVWFIQNEEKCLDFLNISKKNKAKSSVQHIGGLARKQNPEPTKSIFVSRYGARSLKTSTMKGNQEFFQKGGAHVSKGVHINPRVKKAQYAVRGLVPMRADEIREEIRSGTGKSKFSFNELVYCNIGNPQALEQKPLTFHRQVMSLIDAPFLLEDNAVVSRYPSDAVSRARLYLGHIGQRTGAYTDSAGYAFVRDIVAQYVNERDAYVKPLQEASSIVLTDGASTGVRIILQTLVGDEKDAVMIPIPQYPLYTAQIALLGGTPAMYYLRESEGWALNVGELEAVYKDCVANGNATPRVLVVINPGNPTGGVLERTVMEEVAKFCCDHGVVLMADEVYQENIYTATKRFESFRKIVLELPPPYNTDTVLVSLHSVSKGIIGECGRRGGYFTLTNAPPELVEQVMKLCSINLCSNVNGQLMTALMCSPPKPGDASFDHYTAEYSGIFESLKRRADLLAKELNNIRGFKSQSVEGAMYAFPTIELPPKYVKHNDEMNSKEGRQLAPDARWALELLESTGIVVVPGSGFGQQPGTLHFRTTILPPEAHMERVVKALRQFQEGIWAKYA
Protein: Dithiol glutaredoxin (Q5ABB1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Thioredoxin
Sequence:
MFRTLLTKRLFNTSTMVSSQVKNKVEQLIKTKPVFIASKSYCPYCKATKSTIEAITKDAYILELDEVDDGAEIQEALLEITGQRTVPNVFIGGQHIGGNSDVQALKSSDKLDDKIKAAL
Protein: Tumor necrosis factor receptor superfamily member 21 (Death receptor 6) (CD antigen CD358) (O75509)
Organism: Homo sapiens (Human)
Function: Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Negatively regulates oligodendrocyte survival, maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19654028}; Single-pass type I membrane protein {ECO:0000269|PubMed:19654028}. Note=Endocytosed following oxidation in response to reactive oxygen species (ROS). {ECO:0000269|PubMed:34012073}.
Interaction partners:
- Amyloid-beta precursor protein
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Tumor necrosis factor receptor superfamily member 10B
- Caspase-6
- Tumor necrosis factor receptor superfamily member 10A
- Amyloid beta precursor like protein 2
- Tumor necrosis factor ligand superfamily member 6
- Tumor necrosis factor receptor superfamily member 25
- Tumor necrosis factor ligand superfamily member 10
- Tumor necrosis factor ligand superfamily member 15
Sequence:
MGTSPSSSTALASCSRIARRATATMIAGSLLLLGFLSTTTAQPEQKASNLIGTYRHVDRATGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPVGTFTRHENGIEKCHDCSQPCPWPMIEKLPCAALTDRECTCPPGMFQSNATCAPHTVCPVGWGVRKKGTETEDVRCKQCARGTFSDVPSSVMKCKAYTDCLSQNLVVIKPGTKETDNVCGTLPSFSSSTSPSPGTAIFPRPEHMETHEVPSSTYVPKGMNSTESNSSASVRPKVLSSIQEGTVPDNTSSARGKEDVNKTLPNLQVVNHQQGPHHRHILKLLPSMEATGGEKSSTPIKGPKRGHPRQNLHKHFDINEHLPWMIVLFLLLVLVVIVVCSIRKSSRTLKKGPRQDPSAIVEKAGLKKSMTPTQNREKWIYYCNGHGIDILKLVAAQVGSQWKDIYQFLCNASEREVAAFSNGYTADHERAYAALQHWTIRGPEASLAQLISALRQHRRNDVVEKIRGLMEDTTQLETDKLALPMSPSPLSPSPIPSPNAKLENSALLTVEPSPQDKNKGFFVDESEPLLRCDSTSSGSSALSRNGSFITKEKKDTVLRQVRLDPCDLQPIFDDMLHFLNPEELRVIEEIPQAEDKLDRLFEIIGVKSQEASQTLLDSVYSHLPDLL
Protein: Trans-3-hydroxy-L-proline dehydratase (T3LHyp dehydratase) (t3HypD) (EC 4.2.1.77) (Trans-L-3-hydroxyproline dehydratase) (Q6HMS9)
Organism: Bacillus thuringiensis subsp. konkukian (strain 97-27)
Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline. Can also catalyze the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) in vitro. Displays no proline racemase activity.
Interaction partners:
Sequence:
MKVSKVYTTIDAHVAGEPLRIITGGVPEIKGDTQLERRAYCMEHLDHLREVLMYEPRGHHGMYGCIITPPASAHADFGVLFMHNEGWSTMCGHGIIAVITVGIETGMFEVTGEKQNFIIDSPAGEVIAYAKYNGSEVESVSFENVPSFVYKKDVPIIIDDYEFQVDIAFGGAFYAVVDSKEFGLKVDFKDLSAIQMWGGKIKHYIESKMEVKHPLEEGLKGIYGVIFSDEPKGEDATLRNVTIFADGQVDRSPCGTGTSARIATLFEKDALQKGEIFVHECITDGKFEGEVLSVTAVDTYEAVVPKVTGHAFITGFHQFVVDPRDDLKRGFLLG
Protein: TGF-beta receptor type-1 (EC 2.7.11.30) (Transforming growth factor-beta receptor type I) (B4DY26)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}.
Interaction partners:
Sequence:
MCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM