wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phosphatase 2C homolog 2 (PP2C-2) (EC 3.1.3.16) (Q4WTH5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P39966}. Nucleus {ECO:0000250|UniProtKB:P39966}.
Interaction partners:
- Acetyltransferase, GNAT family family
- Serine/threonine-protein phosphatase
Sequence:
MRTCGTSSEGQDECCLYGLSAMQGWRISMEDAHAAVLDLQAKSTGGSEKPTDPDKRLAFFGVYDGHGGDKVALFAGENVHKIVAKQEAFAKGDIEQALKDGFLATDRAILEDPKYEEEVSGCTAAVSVISKNKIWVANAGDSRSVLGVKGRAKPLSFDHKPQNEGEKARISAAGGFVDFGRVNGNLALSRAIGDFEFKKSPELSPEQQIVTAYPDVTVHEVTDDDEFLVIACDGIWDCQSSQSVVEFVRRGIAAKQELYRICENMMDNCLASNSETGGVGCDNMTMIIIGLLNGKTKEEWYNQISERVANGDGPCAPPEYGKSEFRGPGIRNQFEETPDNYDLENDRSRGFSVRSGRIILLGDGTELIPEQNDEELFDQREENRDVTNHLQHDKAEETSTAANLSESPSSANKNSSGSGTEATEKSASS
Protein: H-2 class II histocompatibility antigen gamma chain (Ia antigen-associated invariant chain) (Ii) (MHC class II-associated invariant chain) (CD antigen CD74) [Cleaved into: Class-II-associated invariant chain peptide (CLIP)] (P10247)
Organism: Rattus norvegicus (Rat)
Function: Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to compartments where peptide loading of class II takes place. Enhance also the stimulation of T-cell responses through interaction with CD44.
Subcellular location: [Isoform Long]: Late endosome {ECO:0000250|UniProtKB:P04441}. Lysosome {ECO:0000250|UniProtKB:P04441}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04233}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P04233}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04233}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P04233}. Endosome {ECO:0000250|UniProtKB:P04233}. Lysosome {ECO:0000250|UniProtKB:P04233}. Secreted {ECO:0000250|UniProtKB:P04233}. Note=Transits through a number of intracellular compartments in the endocytic pathway. It can either undergo proteolysis or reach the cell membrane. {ECO:0000250|UniProtKB:P04233}.
Interaction partners:
- Rano class II histocompatibility antigen, D-1 beta chain
- Macrophage migration inhibitory factor
- Rano class II histocompatibility antigen, B-1 beta chain
- Rano class II histocompatibility antigen, B alpha chain
- CD44 antigen
- Histocompatibility 2, class II antigen E alpha
- C-X-C chemokine receptor type 2
- C-X-C chemokine receptor type 4
- Ubiquitin-like protein FUBI
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
Sequence:
MDDQRDLISNHEQLPILGQRARAPESNCNRGVLYTSVSVLVALLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKSAKPVSPMRMATPLLMRPLSMDNMLQAPVKNVTKYGNMTQDHVMHLLTKSGPVNYPQLKGSFPENLKHLKNSMNGLDWKVFESWMKQWLLFEMSKNSLEEKQPTQTPPKVLTKCQEEVSHIPDVHPGAFRPKCDENGNYMPLQCHGSTGYCWCVFPNGTEVPHTKSRGRHNCSEPLDMEDPSSGLGVTKQDMGQMFL
Protein: Protein SCO2 homolog, mitochondrial (Q8VCL2)
Organism: Mus musculus (Mouse)
Function: Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/COX2.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O43819}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cellular tumor antigen p53
- Cytochrome c oxidase assembly protein COX11
- Cytochrome c oxidase subunit 2
- Heme A synthase COX15
- Cytochrome c oxidase copper chaperone
- Surfeit locus protein 1
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase assembly factor 6 homolog
- Fructose-2,6-bisphosphatase TIGAR
- Cytochrome c oxidase subunit 1
Sequence:
MLLALGPKAWPKLSQFKPLLRISGGETLHRNSRHWAGQGQRQGPGLRTRLLITALFGAGLGWAWLAARAEKEQWRQQQRTEALRQAAVGQGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRKLEAEPDLPLVQPVFITVDPERDDVAAMARYVQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQIVESIRRHIAAFHSVLP
Protein: Synapse differentiation-inducing gene protein 1 (SynDIG1) (Dispanin subfamily C member 2) (DSPC2) (Transmembrane protein 90B) (A2ANU3)
Organism: Mus musculus (Mouse)
Function: May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20152115}; Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}. Early endosome membrane {ECO:0000269|PubMed:20152115}; Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}. Postsynaptic density membrane {ECO:0000269|PubMed:20152115}. Synapse {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Shuttles between the cell surface and early endosome membrane.
Interaction partners:
- Protein cornichon homolog 2
- Germ cell-specific gene 1-like protein
- Protein shisa-9
Sequence:
MDGIIEQKSVLVHSKISDAGKRNGLINTRNFMAESRDGLVSVYPAPQYQSHRLVASAAPGSLEGGRSEPVQQLLDPNTLQQSVESHYRPNIILYSDGVLRSWGDGVATDCCETTFIEDRSPTKDSLEYPDGKFIDLSGDDIKIHTLSYDVEEEEELQELESDYSSDTESEDNFLMMPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVAKGDFHQASTSSRRALFLAVLSITIGTGIYVGVAVALIAYLSKNNHL
Protein: Multidrug efflux pump subunit AcrB (AcrAB-TolC multidrug efflux pump subunit AcrB) (Acridine resistance protein B) (P31224)
Organism: Escherichia coli (strain K12)
Function: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137}.
Interaction partners:
- Outer membrane protein TolC
- Multidrug efflux pump subunit AcrA
- Multidrug efflux pump accessory protein AcrZ
- Sec translocon accessory complex subunit YajC
- Cation efflux system protein CusC
- Multidrug resistance protein MdtA
- Multidrug resistance protein MdtE
- Multidrug export protein AcrE
- Probable multidrug resistance protein EmrK
- Macrolide export protein MacA
Sequence:
MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQEVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGSQYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRLTSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANALDTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQNFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMALSVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGRYLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLTKEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKDAMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNGLEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYRMLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEAMELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFSVMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGLIEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIFFVPVFFVVVRRRFSRKNEDIEHSHTVDHH
Protein: Viral CASP8 and FADD-like apoptosis regulator (v-CFLAR) (Viral FLICE-inhibitory protein) (v-FLIP) (Q98325)
Organism: Molluscum contagiosum virus subtype 1 (MOCV) (MCVI)
Function: Inhibits TNFRSF1A, TNFRSF6/FAS and TNFRSF12 induced apoptosis. Directs the degradation of host NFKBIB but not NFKBIA. Suppresses also host NF-kappa-B activation by interacting with and preventing ubiquitination of host NEMO/IKBKG, the NF-kappa-B essential modulator subunit of the IKK complex. Interferes with host CASP8/caspase-8 recruitment and activation at the death-inducing signaling complex (DISC). May lead to higher virus production and contribute to virus persistence and oncogenicity. Participates also in the inhibition of host autophagy by interacting with host SH3BP4.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:30842330}. Host nucleus {ECO:0000269|PubMed:30842330}.
Interaction partners:
Sequence:
MSDSKEVPSLPFLRHLLEELDSHEDSLLLFLCHDAAPGCTTVTQALCSLSQQRKLTLAALVEMLYVLQRMDLLKSRFGLSKEGAEQLLGTSFLTRYRKLMVCVGEELDSSELRALRLFACNLNPSLSTALSESSRFVELVLALENVGLVSPSSVSVLADMLRTLRRLDLCQQLVEYEQQEQARYRYCYAASPSLPVRTLRRGHGASEHEQLCMPVQESSDSPELLRTPVQESSSDSPEQTT
Protein: Late embryogenesis abundant domain-containing protein / LEA domain-containing protein (Q9C7H3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Late embryogenesis abundant protein 6
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Late embryogenesis abundant protein 32
- Gb|AAF18257.1 hydroxyproline-rich glycoprotein family)
- F6D8.10
- Late embryogenesis abundant protein M17
- Agamous-like MADS-box protein AGL81
- Late embryogenesis abundant
- Late embryogenesis abundant
- At5g54370 protein-like protein)
Sequence:
MTNLLALCLVLSTLLAAEVWSPSPAMTTHNTAVASEGEVIVKDGHHVVVVEYDRDGKTNTRVSISPPSADQGEEKENEVEMGTSMFRNVKEKAKETASYLPHVGQGISQPVMTDEARDHHATAGEVICDAFGKCRQKIASVVGRAKDRTVDSVGETASDVREAAAHKAHDVKETVTHAARDVEDTVADQAQYAKGRVTEKAHDPKEGVAHKAHDAKESVADKAHDAKESVAQKAHDAKEKVREKAHDVKETVAQKAHESKERAKDRVREKAQELKETATHKSKNAWERVKNGAREFGSATAATLSPTKVASIVGLTGIAAAFGTSVWVTFVSSYVLASVLGRQQFGVVQSKLYPVYFKATSVGILVGLFGHVLSRRRKLLTDATEMWQGVNLLSSFFMIEANKSFVEPRATKAMFERMKAEKEEGRGGERTSEQELRRKLEQLSERLSKLNTYSSWLNILTLMSLTWHFVYLGQRLGAAC
Protein: IC97/Casc1 N-terminal domain-containing protein (Q57ZZ4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPPKTVKVIGRGGKDDRKDDKPKKLKPAQIAINKAVETADKLYKLHERERLKMEQTDRVALQKFSLDKAAEKERLRLDQDVYTAFEDELVEQEQLAYKECEKHRLWSLIPEASRLPPIRSQSAINTFLSVWRDSEEHYSHYSPPVEVNIKRDNSNSSLRVHRFHQGELGIPPAARRKMLNEELNRCVMAYDLVETIRLEADRCLTLGKTEDLKFFGENIGNVYEQVMFAFDFVTIHTLLNYDVILDGPDSEFLTVAVPSANPVAKFGLWVKVKETTRSFASLVFPVVSMRLDPKSSALPKLPKALGLSKENVALRVIQLRFDPYGCRGSGGREYYALPCVIKIDLLSFTERPKQSGDWLYRSETEEAHKLHVVPYPPPVLEATDENPALRVSFEVPSTIVMRQPTLLIGKWVEKTKEWEPCSHTSSSPDSTGPERMCSFATGEFGTFTILQGKGFDVPYEQWRLQPVSFDQVMMVLEGRHRGEGSDREFRILICDAKCKLISPGDPELAALRADWLEPATLVRLLSQAGFNFMLRDEDAEFIEDIVPKSSELEEKVYADIAQFCLFYIIASSRHNKCGEDADLALFRMSKQVYLGTEDSPDLTAEADGEWHSIRYQTHCCAFSAFRERDDVPDLRILEDHETHLNLYTLLLKEKGEEVRLMALHRTNFLLRRCVYQLLRLIRPLTWG
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1 (EC 2.4.1.198) (C6KT29)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MSGVNYDVKLNECLSIFFPQNIATINPDTKYYLYGFSNDNIYIIVHITDKYIENFKLKKKHEKYSEWKIFRIVGELTFIENFNELNKNMCTTKNEDNNKVNYLYLIYYNNIPIFKKKSGNEQNISALFILYDVKKYVYNMVHDHVNTLVLEAFRREDIIKKIKVKEKQNNNDKNKESNIEKDKNEQTKFTDIYDTNSKSDKDIQKNNMNDGDSNNKNSSLFIDPFESDSYEKNNFSNEKCALQNVDKSKKDKEHIYSENITPSSSNNNNDNNKENDCDKEQLDKYNKDKENKLKLNDKDEYISFNFIEDKLTESFHMNQIIHLINKKCVFTKCLENYENRYFVLKKEEILKKKKKQKKMSIFSYIVSIILFFTYIISLINSCLYYVICTPKLFSEYIFSKKKINTFILIKHKFIFHSEWHNIFRSFMKNKQNPSEYYKYREILLIRIINLIIDIFLGFLIFLLLYFNVINLHYISEKAQIFYGTSTLTSILGTLLQNPLGFKLNNNFTSFIGSILVSILDKWDLFTNTIPVNNSTVLNFVGYTSLLGFSFFLSFVIDYLRFVTAHVTIIYLFLKKICTLFHKNMYSLYLLFNGKKWNILKLRVDTNYYSNEEVLLGTILFTILIFLYPTIFVLVLVFGLIYLIINRIIYLLCVMEKIILYTPFYIFFIQPNCNKYISKGFKFTKYEVGEHELLKRYPTNSYLLLENIHFLFFDKIKLFINIFLYFKNLE
Protein: Zinc finger protein ZAT18 (Q9LFG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in stress responses (Probable). Positive regulator of the jasmonic acid (JA)- mediated signaling pathway. Triggers the up-regulation of LOX3, VSP2, PAL1 and PAL2 in a JA-dependent manner. Promotes drought and osmotic stress tolerance by preventing reactive oxygen species (ROS) production (e.g. H(2)O(2)).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:28586434}.
Interaction partners:
- C2H2 and C2HC zinc fingers superfamily protein
- Glycosyltransferase
- Protein RESPONSE TO ABA AND SALT 1
- HAT family dimerization domain-containing protein
- Ac-like transposase
- C2H2-type zinc finger family protein
- Small ribosomal subunit protein eS12z
- Late embryogenesis abundant protein 6
Sequence:
MKRDRSDYEESMKHIDIVESLMMLSRSFVVKQIDVKQSTGSKTNHNNHFECKTCNRKFDSFQALGGHRASHKKPKLIVDQEQVKHRNKENDMHKCTICDQMFGTGQALGGHMRKHRTSMITEQSIVPSVVYSRPVFNRCSSSKEILDLNLTPLENDLVLIFGKNLVPQIDLKFVN
Protein: Tubulin alpha-1B chain (EC 3.6.5.-) (Alpha-tubulin 2) (Alpha-tubulin isotype M-alpha-2) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain] (P05213)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-5 chain
- Tubulin beta-3 chain
- Tubulin beta-2A chain
- Tubulin beta-4B chain
- Tubulin beta-4A chain
- Tubulin beta-6 chain
- Tubulin alpha-1A chain
- Tubulin beta-2B chain
- Tubulin beta-1 chain
- Microtubule-associated protein
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Protein: Tetraspanin (Q8WUV1)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}.
Interaction partners:
Sequence:
MEGDCLSCMKYLMFVFNFFIFLGGACLLAIGIWVMVDPTGFREIVAANPLLLTGAYILLAMGGLLFLLGFLGCCGAVRENKCLLLFFFLFILIIFLAELSAAILAFIFRENLTREFFTKELTKHYQGNNDTDVFSATWNSVMITFGCCGVNGPEDFKFASVFRLLTLDSEEVPEACCRREPQSRDGVLLSREECLLGRSLFLNKQGCYTVILNTFETYVYLAGALAIGVLAIEEERAHSVSQATGILYQLPASPQAFQSPGTLGATA
Protein: Glycerate kinase (EC 2.7.1.31) (Q0VGK3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8IVS8}.
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- 4-trimethylaminobutyraldehyde dehydrogenase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Phosphoglycerate mutase 1
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- Aldehyde dehydrogenase X, mitochondrial
- Phosphoglycerate mutase 2
- Alpha-enolase
- Gamma-enolase
Sequence:
MAAALQVLPCLLRAPSRPFLWGPPVARMTSGMALAEQARQLFDSAVGAVQPGPMLQRTLSLDPSGKQLKVRDRTFQLQENLYLVGFGKAVLGMAAAADELLGQHLVQGVISVPKGIRAAVELAGKQEMLLKPHSHIQVFEGAEDNLPDRDALRAAQAIQQLAERLTADDLLLVLISGGGSALLPAPIPPVTLEEKQTLTKLLAARGATIQELNTIRKALSQLKGGGLAQAAYPAQVVSLILSDVIGDPLEVIASGPTVASTHSVQDCLHILNHYGLRAALPRSVKTVLSRADSDPHGPHTCGHVLNVIIGSNSLALAEAQRQAEVLGYHAMVLSTAMQGDVRRVAQFYGLLARVAAACLTSSTAERPLEEEAKLHQLAAELQLPDLQLEEALEAVAKAKGPVCLLAGGEPTVQLQGSGKGGRNQELALRVGAELGKQPLGPVDVLFLSGGTDGQDGPTKVAGAWVMSDLVSQASAENLDFATFLDNNDSYTFFCSFQGGTHLLHTGLTGTNVMDVHLLVFHPQ
Protein: Glucose-1-phosphate thymidylyltransferase 1 (G1P-TT 1) (EC 2.7.7.24) (dTDP-glucose pyrophosphorylase 1) (dTDP-glucose synthase 1) (P37744)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
Interaction partners:
- dTDP-4-dehydrorhamnose 3,5-epimerase
- dTDP-glucose 4,6-dehydratase 1
- dTDP-4-dehydrorhamnose reductase
- dTDP-glucose 4,6-dehydratase 2
- Putative O-antigen transporter
- UDP-galactopyranose mutase
- Putative O-antigen polymerase
- Putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ
- Putative glycosyltransferase WbbK
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MKMRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDKNGTAISLEEKPLEPKSNYAVTGLYFYDNDVVQMAKNLKPSARGELEITDINRIYLEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKVSCPEEIAFRKGFIDVEQVRKLAVPLIKNNYGQYLYKMTKDSN
Protein: Cyclin D binding myb like transcription factor 1 (H7C388)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTAAAPASPEQIIVHALSPEHLLNTSDNVTVQCHTPRVIIQTVATEDITSSISQAELTVDSDIQSSDFPEPPDALEADTFPDEIHHPKMTVEPSFNDAHVSKFSDQNSTELMNSVMVRTEEEISDTDLKQEESPSDLASAYVTEIPYSNIIRKNQISLDHPWAVLFQKIQRMSKIW
Protein: Defensin D2 (Ns-D2) (P86973)
Organism: Nigella sativa (Black cumin)
Function: Antimicrobial peptide active against fungi, Gram-positive and Gram-negative bacteria. Inhibits growth of hyphae in the fungi A.niger (IC(50)=3.5 ug/ml), B.sorokiniana (IC(50)=1.8 ug/ml), F.oxysporum (IC(50)=5.3 ug/ml), F.graminearum (IC(50)=6.9 ug/ml), F.culmorum (IC(50)=6.9 ug/ml) and B.cinerea (IC(50)=13.7 ug/ml). Has no effect on spore germination. Destroys spores in germinated conidia by disruption of cell walls and membranes in A.niger and B.sorokiniana. Causes vacuolization of germinated macro- and microconidia in F.oxysporum, F.graminearum and F.culmorum. Strongly inhibits growth of P.infestans on potato tubers above concentrations of 3.4 ug/ml. Inhibits growth of Gram-positive bacteria C.michiganensis and B.subtilis and of Gram-negative bacteria P.syringae, E.carotovora and E.coli.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P69241}.
Interaction partners:
Sequence:
KFCEKPSGTWSGVCGNSGACKDQCIRLEGAKHGSCNYKLPAHRCICYYEC
Protein: Pumilio homolog 1 (Q5T1Z4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
MSVACVLKRKAVLWQDSFSPHLKHHPQEPANPNMPVVLTSGTGSQAQPQPAANQALAAGTHSSPVPGSIGVAGRSQDDAMVDYFFQRQHGEQLGGGGSGGGGYNNSKHRWPTGDNIHAEHQVRSMDELNHDFQALALEGRAMGEQLLPGKKFWETDESSKDGPKGIFLGDQWRDSAWGTSDHSVSQPIMVQRRPGQSFHVNSEVNSVLSPRSESGGLGVSMVEYVLSSSPGDSCLRKGGFGPRDADSDENDKGEKKNKGTFDGDKLGDLKEEGDVMDKTNGLPVQNGIDADVKDFSRTPGNCQNSANEVDLLGPNQNGSEGLAQLTSTNGAKPVEDFSNMESQSVPLDPMEHVGMEPLQFDYSGTQVPVDSAAATVGLFDYNSQQQLFQRPNALAVQQLTAAQQQQYALAAAHQPHIAGLAPAAFVPNPYIISAAPPGTDPYTAGLAAAATLGPAVVPHQYYGVTPWGVYPASLFQQQAAAAAAATNSANQQTTPQAQQGQQQVLRGGASQRPLTPNQNQQGQQTDPLVAAAAVNSALAFGQGLAAGMPGYPVLAPAAYYDQTGALVVNAGARNGLGAPVRLVAPAPVIISSSAAQAAVAAAAASANGAAGGLAGTTNGPFRPLGTQQPQPQPQQQPNNNLASSSFYGNNSLNSNSQSSSLFSQGSAQPANTSLGFGSSSSLGATLGSALGGFGTAVANSNTGSGSRRDSLTGSSDLYKRTSSSLTPIGHSFYNGLSFSSSPGPVGMPLPSQGPGHSQTPPPSLSSHGSSSSLNLGGLTNGSGRYISAAPGAEAKYRSASSASSLFSPSSTLFSSSRLRYGMSDVMPSGRSRLLEDFRNNRYPNLQLREIAGHIMEFSQDQHGSRFIQLKLERATPAERQLVFNEILQAAYQLMVDVFGNYVIQKFFEFGSLEQKLALAERIRGHVLSLALQMYGCRVIQKALEFIPSDQQVINEMVRELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFALSTHPYGCRVIQRILEHCLPDQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVAEIRGNVLVLSQHKFASNVVEKCVTHASRTERAVLIDEVCTMNDGPHSALYTMMKDQYANYVVQKMIDVAEPGQRKIVMHKIRPHIATLRKYTYGKHILAKLEKYYMKNGVDLGPICGPPNGII
Protein: AT3g53950/F5K20_250 (Glyoxal oxidase-related protein) (Q9M332)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Expressed protein
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Nicotinamide adenine dinucleotide transporter 1, chloroplastic
- DNA repair endonuclease UVH1
- Calcium-dependent lipid-binding family protein
- Ricin B-like lectin EULS3
- Haloacid dehalogenase-like hydrolase
- FAD/NAD
- DEAD-box ATP-dependent RNA helicase FANCM
- DEAD/DEAH-box RNA helicase family protein
Sequence:
MAELIPWYYTSGSGIVLVLQTIFLFSIVRADLPGSWELIVQDAGIASMHTAVTRFNTVILLDRTNIGPSRKALDRHRCRRDPKDAALKRDCYAHSVLFDLGTNQIRPLMIQTDTWCSSGQFLSDGSLLQTGGDKDGFKKIRKFEPCDPNETCDWVELQDTELITGRWYASNQILPDGSVIIVGGRGTNTVEYYPPRENGAVPFQFLADVEDKQMDNLYPYVHLLPDDDGGNLFIFANSRAVKYDHRINAVVKEYPPLDGGPRNYPSGGSSAMLAIQGDFTTAEILICGGAQSGAFTARAIDAPAHGTCGRIVATAADPVWVTEEMPFGRIMGDMVNLPTGEILIINGAQAGSQGFEMGSDPCLYPLLYRPDQPIGLRFMTLNPGTVPRMYHSTANLLPDGRILLAGSNPHYFYKFNAEFPTELRIEAFSPEYLSPDRANLRPEIQEIPQIIRYGEVFDVFVTVPLPVVGIIQMNWGSAPFATHSFSQGQRLVKLTVAPSVPDGVGRYRIQCTAPPNGAVSPPGYYMAFAVNQGVPSIARWIRIVS
Protein: Solute carrier family 12 member 2 (A0A8I5ZP25)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEPGPAAPSSGAPRPARDGDAPLTAAGVDLPGTAVLSGREDATAGSQAGGGVRGEGTPAAGDGLGKPLGPTPSQSRFQVDPVSENAGRAAAAAAAAAAAAAAGAAGKETPAAGKAGTESGVAKGSEEAKGRFRVNFVDPAASSSADDSLSDAAGVGGDGPNVSFQNGGDTVLSEGSSLHSGGGSGHHQQYYYDTHTNTYYLRTFGHNTMDAVPRIDHYRHTAAQLGEKLLRPSLAELHDELEKEPFEDGFANGEESTPTRDAVVTYTAESKGVVKFGWIKGVLVRCMLNIWGVMLFIRLSWIVGQAGIGLSVLVIAMATVVTTITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGAIGLIFAFANAVAVAMYVVGFAETVVELLKEHSILMIDEINDIRIIGAITVVVLLGISVAGMEWEAKAQIVLLVILLLAIADFVIGTFISLDSKKPKGFFGYKSEIFSENFGPDFREEETFFSVFAIFFPAATGILAGANISGDLADPQSAIPKGTLLAILITTVVYIGIAVSVGSCVVRDATGNVNDTITTELTNCTSAACKLNFDFSYCESNTCSYGLMNNFQVMSMVSGFAPLISAGIFSATLSSALASLVSAPKIFQALCKDNIYPAFQMFAKGYGKNNEPLRGYILTFLIALGFILIAELNVIAPIISNFFLASYALINFSVFHASLAKSPGWRPAFKYYNMWISLTGAILCCIVMFVINWWAALLTYVIVLGLYIYVTYKKPDVNWGSSTQALTYLSALQHSIRLSGVEDHVKNFRPQCLVMTGSPNSRPALLHLVHDFTKNVGLMICGHVHMGPRRQAMKEMSIDQAKYQRWLIKNKMKAFYAPVHADDLREGAQYLMQAAGLGRMKPNTLVLGFKKDWLQADMRDVDMYINLFHDAFDIQYGVVVIRLKEGLDISHLQGQEELLSSQEKSPGTKDVVVNVDYSKKSDQDAFKASGEKPITQKESKGPVAPLNVADQKLLEASTQFQKKQGKNTIDVWWLFDDGGLTLLIPYLLTTKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDIMVLGDINTKPKKENIVAFDDMIEPYRLHEDDKEQDIADKMKEDEPWRITDNELELYKTKTYRQIRLNELLKEHSSTANIIVMSLPVARKGAVSSALYMAWLEALSKDLPPILLVRGNHQSVLTFYS
Protein: 3-octaprenyl-4-hydroxybenzoate carboxy-lyase (EC 4.1.1.98) (Polyprenyl p-hydroxybenzoate decarboxylase) (P0AAB4)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000305|PubMed:782527}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000305|PubMed:782527}.
Interaction partners:
- Flavin prenyltransferase UbiX
- 4-hydroxybenzoate octaprenyltransferase
- 2-octaprenylphenol hydroxylase
- Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE
- NAD
- Trk system potassium uptake protein TrkH
- Ubiquinone biosynthesis accessory factor UbiJ
- Ubiquinone biosynthesis O-methyltransferase
- 3-demethoxyubiquinol 3-hydroxylase
- Chorismate pyruvate-lyase
Sequence:
MDAMKYNDLRDFLTLLEQQGELKRITLPVDPHLEITEIADRTLRAGGPALLFENPKGYSMPVLCNLFGTPKRVAMGMGQEDVSALREVGKLLAFLKEPEPPKGFRDLFDKLPQFKQVLNMPTKRLRGAPCQQKIVSGDDVDLNRIPIMTCWPEDAAPLITWGLTVTRGPHKERQNLGIYRQQLIGKNKLIMRWLSHRGGALDYQEWCAAHPGERFPVSVALGADPATILGAVTPVPDTLSEYAFAGLLRGTKTEVVKCISNDLEVPASAEIVLEGYIEQGETAPEGPYGDHTGYYNEVDSFPVFTVTHITQREDAIYHSTYTGRPPDEPAVLGVALNEVFVPILQKQFPEIVDFYLPPEGCSYRLAVVTIKKQYAGHAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWNDVIWAITTRMDPARDTVLVENTPIDYLDFASPVSGLGSKMGLDATNKWPGETQREWGRPIKKDPDVVAHIDAIWDELAIFNNGKSA
Protein: Formyltransferase/hydrolase complex Fhc subunit B (C5B138)
Organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens)
Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Formyltransferase/hydrolase complex subunit D
- Formyltransferase/hydrolase complex Fhc subunit C
- Formyltransferase/hydrolase complex Fhc subunit A
- Methenyltetrahydromethanopterin cyclohydrolase
- NAD
- Ribofuranosylaminobenzene 5'-phosphate
- Tetrahydromethanopterin C1 transfer protein
- Tetrahydromethanopterin synthesis protein
- Formamidase
- Tetrahydromethanopterin synthesis protein
Sequence:
MAAWVKGGAADVDAAVEAAADLLAASRVPVLAGLSAEVSALRAAYRLAETLGASLDPVSGPSVYAELGALSAGGAMSTTRAETIGRADVILIVGNRPWDGELIAEIAAAAPSRGRAAGSERALLSLGGPQNGAIRHVAYAADAGGLTISLGHLRAFAKGHLAGEAAFADLAKRLFAAQYGVIVYDPEEVGELGAEMLQGLIRDLNESTRFFALTLADPFQGRAAVQLSAWTTGQAPRVGFGRHQPEHDSWRFDSARQIAAGEADAALWLASLPAPRPAWLGSLPTIAIVGEGSQEAAGETAEVVITVGVPGQSVGGALWNDRRGVIAYAEASDPAKTPAETETAAGVLTRIRDRLIEKGVSC