wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha/beta hydrolase nvfD (EC 3.1.1.-) (Novofumigatonin biosynthesis cluster protein D) (A0A2I1BT15)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: Alpha/beta hydrolase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Interaction partners:
Sequence:
MLKPAIIIVPGALHRPEHYQGIVSRLHKLQYEAVAVSMPSLSSSPPQPTWTEDVEAIRKAIFKFSESGQDVVLVGHSYSGILISEASKGLSRKDLPHGEGAVVRLIYMCAIAVPVGESLTGQLEPRTPQEVEAFREEGSISLLDADKVRDVLYNKCEPKVADWAISLLGKQPVTTMSTPATHAAWLEIPSTYLICEDDLAVPECVQLRMAKQGNGAFDIVRCQEGHAPCLSNPDLVVRMIRNAAGEAIEI
Protein: Coronatine-insensitive 1 (Q6TDU2)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Interaction partners:
- Protein TIFY
- Protein JAZ7
- Protein TIFY
- Protein TIFY
- Protein TIFY
- Transcription factor MYC2
- Tify domain-containing protein
- Protein TIFY
- Protein TIFY
- Cullin family profile domain-containing protein
Sequence:
MEERNSTRLSSSTNDTVWECVIPYIQESRDRDAVSLVCKRWWQIDAITRKHITMALCYTAKPEQLSRRFPHLESVKLKGKPRAAMFNLIPEDWGGYVTPWVMEITKSFSKLKALHFRRMIVRDSDLELLANRRGRVLQVLKLDKCSGFSTDGLLHISRSCKNLRTLLMEESYIIEKDGEWAHELALNNTVLENLNFYMTDLLQVRAEDLELIARNCKSLVSMKISECEITNLLGFFRAAAALEEFGGGAFNDQPELVVENGYNEHSGKYAALVFPPRLCQLGLTYLGRNEMSILFPIASRLRKLDLLYALLDTAAHCFLLQRCPNLEILETRNVVGDRGLEVLGQYCKRLKRLRIERGADDQEMEDEEGAVTHRGLIDLAKGCLELEYMAVYVSDITNEALEVIGTYLKNLSDFRLVLLDREERITDLPLDNGVRALLRGCHNLRRFALYVRPGGLTDVGLSYVGQYSPNVRWMLLGYVGESDHGLLEFSKGCPSLQKLEVRGCCFSERALALATLQLKSLRYLWVQGYRASSAGRDLLAMARPFWNIELIPARRVIANDGNNAETVVSEHPAHILAYYSLAGQRTDFPDTVKPLDPTYLLAE
Protein: Probable 3-phenylpropionic acid transporter (Q47142)
Organism: Escherichia coli (strain K12)
Function: Probable permease involved in the uptake of 3-phenylpropionic acid.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Siroheme synthase
- Gnt-II system L-idonate transporter
Sequence:
MVLQSTRWLALGYFTYFFSYGIFLPFWSVWLKGIGLTPETIGLLLGAGLVARFLGSLLIAPRVSDPSRLISALRVLALLTLLFAVAFWAGAHVAWLMLVMIGFNLFFSPLVPLTDALANTWQKQFPLDYGKVRLWGSVAFVIGSALTGKLVTMFDYRVILALLTLGVASMLLGFLIRPTIQPQGASRQQESTGWSAWLALVRQNWRFLACVCLLQGAHAAYYGFSAIYWQAAGYSASAVGYLWSLGVVAEVIIFALSNKLFRRCSARDMLLISAICGVVRWGIMGATTALPWLIVVQILHCGTFTVCHLAAMRYIAARQGSEVIRLQAVYSAVAMGGSIAIMTVFAGFLYQYLGHGVFWVMALVALPAMFLRPKVVPSC
Protein: beta-Tubulin at 65B (Q9VRX3)
Organism: Drosophila melanogaster (Fruit fly)
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 {ECO:0000250}.
Interaction partners:
- AT04270p
- Tubulin alpha-2 chain
- Tubulin alpha-4 chain
- Tubulin alpha-3 chain
- Tubulin alpha-1 chain
- Serine/threonine-protein kinase CG17528
- non-specific serine/threonine protein kinase
- Echinoderm microtubule-associated protein-like CG42247
- Protein mini spindles
- Sperm-specific dynein intermediate chain 1, isoform A
Sequence:
MREIVTLQIGGAGNAIGDSFWHVISHEHGVDYASGRFGGTSPLQLERINVFFNATASKRFYARTILIDTEASTIQRLNASSQLYRPENFVAGSESAGNNFARGYHTDGAAILDQVLENTRREVESVDSLQGFQLLHSIGGGTGSGLTSLIMEALVEQYPDNLLCNYVTIPSPNMSQVVVEPYNALLSTPALVNNSHLTFCLDNEALFQICNRNLKLKMSGYEHINHIVALTMSGITTCLRFPGQLNAGLRKIYVNMVPFPRLHFLIPGFAPLVTCKQQQFSKGTVSELVQQIFYSNNLLCAIDLRKGKLLTAAGIFRGRMSPREVDQLMTGVRNKNINNFVDWIPNNIKTAICDIPPRGLKMSATFIGNTTAIQTLFQRLLDASMSMLRRKAHLHWYTGEGMEEQEFQDAQQELQAIIDDYRSSAEGEDSGGGGGGGGGRSGSAESGEEEATPEAHCQYCTE
Protein: C-C motif chemokine 20 (Beta-chemokine exodus-1) (CC chemokine LARC) (Liver and activation-regulated chemokine) (Macrophage inflammatory protein 3 alpha) (MIP-3-alpha) (Small-inducible cytokine A20) [Cleaved into: CCL20(1-67); CCL20(1-64); CCL20(2-70)] (P78556)
Organism: Homo sapiens (Human)
Function: Acts as a ligand for C-C chemokine receptor CCR6. Signals through binding and activation of CCR6 and induces a strong chemotactic response and mobilization of intracellular calcium ions. The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases. CCL20 acts as a chemotactic factor that attracts lymphocytes and, slightly, neutrophils, but not monocytes. Involved in the recruitment of both the pro-inflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation. Required for optimal migration of thymic natural regulatory T cells (nTregs) and DN1 early thymocyte progenitor cells (By similarity). C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. Positively regulates sperm motility and chemotaxis via its binding to CCR6 which triggers Ca2+ mobilization in the sperm which is important for its motility. Inhibits proliferation of myeloid progenitors in colony formation assays. May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells (By similarity). Possesses antibacterial activity towards E.coli ATCC 25922 and S.aureus ATCC 29213.
Subcellular location: Secreted {ECO:0000269|PubMed:11035086}.
Interaction partners:
- C-C chemokine receptor-like 2
- C-C motif chemokine 5
- Stromal cell-derived factor 1
- C-C chemokine receptor type 6
- C-X-C motif chemokine 11
- C-X-C motif chemokine 5
- Platelet factor 4
- C-X-C motif chemokine 17
- Cytokine SCM-1 beta
- C-C chemokine receptor type 2
Sequence:
MCCTKSLLLAALMSVLLLHLCGESEAASNFDCCLGYTDRILHPKFIVGFTRQLANEGCDINAIIFHTKKKLSVCANPKQTWVKYIVRLLSKKVKNM
Protein: Period circadian regulator 1 (J3KRL7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGPLEGADGGGDPRPGESFCPGGVPSPGPPQHRPCPGPSLADDTDANSNGSSGNESNGHESRGASQRSSHSSSSGNGKDSALLETTESSKSTNSQSPSPPSSSIAYSLLSASSEQDNPSTSGCSSEQSARARTQKELMTALRELKLRLPPERRGKGRSGTLATLQYALACVKQVQANQEYYQQWSLEEGEPCSMDMSTYTLEELEHITSEYTLQNQAAVLLRCKRDVFRGTRFSELLAPQDVGVFYGSTAPSRLPTWGTGASAGSGLRDFTQEKSVFCRIRGGPDRDPGPRYQPFRLTPYVTKIRVSDGAPAQPCCLLIAERIHSGYEAPRIPPDKRIFTTRHTPSCLFQDVDERAAPLLGYLPQDLLGAPVLLFLHPEDRPLMLAIHKKILQLAGQPFDHSPIRFCARNGEYVTMDTSWAGFVHPWSRKVAFVLGRHKVRTAPLNEDVFTPPAPSPAPSLDTDIQELSEQIHRLLLQPVHSPSPTGLCGVGAVTSPGPLHSPGSSSDSNGGDAEGPGPPAPVTFQQICKDVHLVKHQGQQLFIESRARPQSRPRLPATGTFKAKALPCQSPDPELEAGSAPVQAPLALVPEEAERKEASSCSYQQINCLDSILRYLESCNLPSTTKRKCASSSSYTTSSASDDDRQRTGPVSVGTKKDPPSAALSGEGATPRKEPVVGGTLSPLALANKAESVVSVTSQCSFSSTIVHVGDKKPPESDIIMMEDLPGLAPGPAPSPAPSPTVAPDPAPDAYRPVGLTKAVLSLHTQKEEQAFLSRFRDLGRLRGLDSSSTAPSALGCHHGPAPPSRRHHCRSKAKRSRHHQNPRAEAPCYVSHPSPVPPSTPWPTPPATTPFPAVVQPYPLPVFSPRGGPQPLPPAPTSVPPAAFPAPLVTPMVALVLPNYLFPTPSSYPYGALQTPAEGPPTPASHSPSPSLPALAPSPPHRPDSPLFNSRCSSPLQLNLLQLEELPRAEGAAVAGGPGSSAGPPPPSAEAAEPEARLAEVTESSNQDALSGSSDLLELLLQEDSRSGTGSAASGSLGSGLGSGSGSGSHEGGSTSASITRSSQSSHTSKYFGSIDSSEAEAGAARGGAEPGDQVIKYVLQDPIWLLMANADQRVMMTYQVPSRDMTSVLKQDRERLRAMQKQQPRFSEDQRRELGAVHSWVRKGQLPRALDVMACVDCGSSTQDPGHPDDPLFSELDGLGLEPMEEGGGEQGSSGGGSGEGEGCEEAQGGAKASSSQDLAMEEEEEGRSSSSPALPTAGNCTS
Protein: ELM2 domain-containing protein (Putative MYB family transcription factor) (Q9ZQ83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Trihelix transcription factor ENAP1
- Tubby-like F-box protein 2
- Transcription factor HHO5
- NAC domain-containing protein 1
Sequence:
MGLKRPYDAEEMQKCNAKHARQLSYKNHNQFDEAIPYHHASMEKKTNVLVEDLIGLCENPTWTNDANHVDKGFETTGLCQEDSQSGVTTQSDLSHQSSGSDFTWKPVEDVYTCLMNQPPRKQVLVGSNHQADIPEFVKEEILDQSEARTKEDLEGKLMRKCVIPMSDSDLCGTGQGRKECLCLDKGSIRCVRRHIIEARESLVETIGYERFMELGLCEMGEEVASLWTEEEEDLFHKVVYSNPFSAGRDFWKQLKGTFPSRTMKELVSYYFNVFILRRRGIQNRFKALDVDSDDDEWQVEYNIFNSTKSLDEEDNNGNRSSYEDNEEEEETSSNDDDEEEEEEDDSSSNDAHCVDTDKASRDGFGEEVNVEDDSCMSFELQDSNLIFSHNPIKNRECHRSGEDSYSFDDQRFTSDCWNKNNDLLPTSNIIEEIFGQDDWGDKDDNNLKEK
Protein: Serine/threonine-protein kinase PknG (EC 2.7.11.1) (P9WI73)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Phosphorylates GarA. May play a role in metabolic regulation via control of the phosphorylation status of GarA. Plays a crucial role in the survival of mycobacteria within host macrophages, by blocking the intracellular degradation of mycobacteria in lysosomes. Required for intrinsic antibiotic resistance.
Subcellular location: Cytoplasm. Cell membrane. Note=Also detected in growth media, suggesting that it can be translocated into host macrophages under specific conditions.
Interaction partners:
- Probable glutamine-binding lipoprotein GlnH
- Glycogen accumulation regulator GarA
- Possible conserved membrane protein
- Serine/threonine-protein kinase PknF
- Serine/threonine protein phosphatase PstP
- Serine/threonine-protein kinase PknB
- Serine/threonine-protein kinase PknL
- Putative 8-oxo-dGTP diphosphatase 3
- UDP-N-acetylmuramate--L-alanine ligase
- FHA domain-containing protein FhaB
Sequence:
MAKASETERSGPGTQPADAQTATSATVRPLSTQAVFRPDFGDEDNFPHPTLGPDTEPQDRMATTSRVRPPVRRLGGGLVEIPRAPDIDPLEALMTNPVVPESKRFCWNCGRPVGRSDSETKGASEGWCPYCGSPYSFLPQLNPGDIVAGQYEVKGCIAHGGLGWIYLALDRNVNGRPVVLKGLVHSGDAEAQAMAMAERQFLAEVVHPSIVQIFNFVEHTDRHGDPVGYIVMEYVGGQSLKRSKGQKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEEQLKLIDLGAVSRINSFGYLYGTPGFQAPEIVRTGPTVATDIYTVGRTLAALTLDLPTRNGRYVDGLPEDDPVLKTYDSYGRLLRRAIDPDPRQRFTTAEEMSAQLTGVLREVVAQDTGVPRPGLSTIFSPSRSTFGVDLLVAHTDVYLDGQVHAEKLTANEIVTALSVPLVDPTDVAASVLQATVLSQPVQTLDSLRAARHGALDADGVDFSESVELPLMEVRALLDLGDVAKATRKLDDLAERVGWRWRLVWYRAVAELLTGDYDSATKHFTEVLDTFPGELAPKLALAATAELAGNTDEHKFYQTVWSTNDGVISAAFGLARARSAEGDRVGAVRTLDEVPPTSRHFTTARLTSAVTLLSGRSTSEVTEEQIRDAARRVEALPPTEPRVLQIRALVLGGALDWLKDNKASTNHILGFPFTSHGLRLGVEASLRSLARVAPTQRHRYTLVDMANKVRPTSTF
Protein: Protein FAR1-RELATED SEQUENCE 5 (Q9SZL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription activator involved in regulating light control of development.
Subcellular location: Nucleus {ECO:0000269|PubMed:15591448}. Note=The nuclear localization is independent of the light treatment.
Interaction partners:
- Protein EMBRYO DEFECTIVE 1674
- Histone acetyltransferase subunit NuA4-domain protein
Sequence:
MMDNEVLDFDIGVGVSSGGDVDDDAIDIEHHALDDDDMLDSPIMPCGNGLVGNSGNYFPNQEEEACDLLDLEPYDGLEFESEEAAKAFYNSYARRIGFSTRVSSSRRSRRDGAIIQRQFVCAKEGFRNMNEKRTKDREIKRPRTITRVGCKASLSVKMQDSGKWLVSGFVKDHNHELVPPDQVHCLRSHRQISGPAKTLIDTLQAAGMGPRRIMSALIKEYGGISKVGFTEVDCRNYMRNNRQKSIEGEIQLLLDYLRQMNADNPNFFYSVQGSEDQSVGNVFWADPKAIMDFTHFGDTVTFDTTYRSNRYRLPFAPFTGVNHHGQPILFGCAFIINETEASFVWLFNTWLAAMSAHPPVSITTDHDAVIRAAIMHVFPGARHRFCKWHILKKCQEKLSHVFLKHPSFESDFHKCVNLTESVEDFERCWFSLLDKYELRDHEWLQAIYSDRRQWVPVYLRDTFFADMSLTHRSDSINSYFDGYINASTNLSQFFKLYEKALESRLEKEVKADYDTMNSPPVLKTPSPMEKQASELYTRKLFMRFQEELVGTLTFMASKADDDGDLVTYQVAKYGEAHKAHFVKFNVLEMRANCSCQMFEFSGIICRHILAVFRVTNLLTLPPYYILKRWTRNAKSSVIFDDYNLHAYANYLESHTVRYNTLRHKASNFVQEAGKSLYTCDVAVVALQEAAKTVSLAMNKEVRRTMANRHFKASSVTGGKHQQEVLAQPEPEDEMDKKINQLRNELELANRKCEAYRTNLLSVLKEMEDQKLQVSIKVQNIKISLKDNL
Protein: Anaphase-promoting complex subunit 2 (B2RYJ1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Anaphase-promoting complex subunit 5
- Fizzy-related protein homolog
- Anaphase-promoting complex subunit 11
- Cell division cycle 16
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 10
- Cell division cycle protein 20 homolog
- Cell division cycle protein 23 homolog
- Cell division cycle protein 27 homolog
Sequence:
MEAEGVAVSVAAAAAATTTIVATDDCDSRPGQELVVAWNTVSTGLVPPAALGLASSRTSGAVPPKEEELRAAVEVLRAHGLHSVLEEWFVEVLQNDLQGNIATEFWNAISLRENSVDEPQCLVLLLDAFGLLESRLDPYLHSLELLEKWTRLGLLMGAGAQGLREKVHTMLRGVLFFSTPRTFQEMVQRLYGRFLRVYMQSKRKGEGGTDPELEGELDSRYARRRYYRLLQSPLCAGCGSDKQQCWCRQALEQFNQLSQVLHRLSLLERVSAEAVTTTLHQVTRERMEDRCRGEYERSFLREFHKWIERVVGWLGKVFLQDNPSRPTSPEAGNTLRRWRCHVQRFFYRIYASLRIEELFSIIRDFPDSRPAIEDLKYCLERTDQRQQLLVSLKVALETRLLHPGVNTCDIITLYISAIKALRVLDPSMVILEVACEPIRRYLRTREDTVRQIVAGLTGDSDGTGDLAVELSKTDPACLETGQDSEDDSGEPEDWVPDPVDADPAKSSSKRRSSDIISLLVSIYGSKDLFINEYRSLLADRLLHQFSFSPEREIRNVELLKLRFGEAPMHFCEVMLKDMADSRRINANIREEDEKRPVEEQPPFGVYAVILSSEFWPPFKDEKLEVPEDIRAALDVYCKKYEKLKAMRTLSWKHTLGLVTMDVELADRTLSVAVTPVQAVVLLYFQDQASWTLEELSKVVKMPVALLRRRMSVWLQQGVLREEPPGTFSVIEEERPQDRDNMVLIDSDDESDSGMASQADQKEEELLLFWTYIQAMLTNLESLSLERIYSMLRMFVMTGPALAEIDLQELQGYLQKKVRDQQLIYSAGVYRLPKNCN
Protein: Beta-myrcene/(E)-beta-ocimene synthase 2, chloroplastic (EC 4.2.3.15) (Terpenoid synthase 24) (AtTPS24) (Q9LRZ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in monoterpene (C10) biosynthesis. The major products are alpha- and beta-pinene, sabinene, beta-myrcene, (E)-beta-ocimene and limonene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- S-
- Tricyclene synthase, chloroplastic
- 1,8-cineole synthase 1, chloroplastic
- Solanesyl diphosphate synthase 2, chloroplastic
- Solanesyl diphosphate synthase 1, chloroplastic
- Camelliol C synthase
- Probable alpha,alpha-trehalose-phosphate synthase 11
- Probable alpha,alpha-trehalose-phosphate synthase 7
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2
- Squalene epoxidase 6
Sequence:
MATLCIGSAPIYQNACIHNFRLQRPRRFISKSMTKTMPDANPLDLRRRSGNYQPSSWDHSYLLSIENKYVNEKEVITRHVLKKKVKKMLEEVETKSRLEKLELIDDLQKLGVSYHFEQEINNILTNFHLENGKNIWKCDKEEDLHATALEFRLLRQHGFGVSEDIFDVIIDKIESNTFKSDNITSIITLYEASYLSTKSDTKLHKVIRPFATEQIRNFVDDESETYNIMLREMAIHALEIPYHWRMRRLETRWYIDAYEKKHDMNLFLAEFAKIDFNIVQTAHQEDVKYVSCWWKETGLGSQLHFVRDRIVENYFWTVGMIYEPQFGYIRRIVAIVAALITVIDDIYDIYGTPEELELFTAMVQNWDINRLDELPEYMKLCFLTLFNEINAMGCDVLKCKNIDVIPYFKKSWADLCKAYLVEAKWYKGGYKPSVEEYMQNAWISISAPTMLIHFYCAFSGQISVQILESLVQQQQDVVRCSATVLRLANDLATSPDELARGDVLKSVQCYMHETGVSEEEARTHVQQMISHTWDEMNYEARTAARSSSLLSRRFVETAMNLARMSQCMYQHGDGHGCPDKAKIVDRVQTLLVDPIPLD
Protein: Subtilisin-like serine protease Cla h 9.0101 (EC 3.4.21.-) (Vacuolar serine protease) (allergen Cla h 9.0101) (B7ZK61)
Organism: Davidiella tassiana (Mycosphaerella tassiana) (Cladosporium herbarum)
Function: Serine protease.
Interaction partners:
Sequence:
MRGALAGLSLATLATASPVLVNSIHNDAAPIISASNAKEIADNYMIKFKDHVTQNLAAEHHGWVQDLHEKTQVAKTELRKRSQSPMVDDIFNGLKHTYNIAGGLMGYAGHFDEDVIEQIRRHPDVELVERDQEVHVLGSESEVEKNAPWGLARISHRDSLSFGTFNKYLYTEDGGEGVDVYVVDTGTNVDHVDFEGRASWGKTIPQGDADEDGNGHGTHCSGTVAGKKYGVAKKAHVKAVKVLRSNGSGSMSDVVKGVEYAAESHLEQVSITKKGKRKGFKGSTANMSLGGGKSPILDKAVNAAVDAGIHFAVAAGNDNADSCNYSPAAAENAVTVGASTLADERAYFSNYGKCNDIFAPGLNIQSTWIGSKYAVNTISGTSMASPHVAGLLAYLLSLQPAKDSAFAVADISPKKLKANLISIATVGALTDVPSNTANILAWNGGGESNYSAIVEKGGYKATHRPTMLEEIESEAKVASKKVYSEGDELAHKVAELTEKVEDLIAGELKDMFRELKRE
Protein: Uncharacterized protein (Q580L7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLQLTVEDLTPEAIAALEVQCKAQAEKVNQLEEAMGLLQKELDDARKKYRSTSKAVQWRRLMAEVENDEDIANITVMMQEALADFYKTMQPPDDYDESREGISFCDTDDYADLTSVETKVDEFLLAIRRLVGENCASPEDDGDRRHQRRRALLMLLVLTINAARITDTPTEDAASLMEEQQDNIASLWQTLLHTDSGLVEAEKSEWKDIVSSFLGPPYDTST
Protein: ATP synthase subunit alpha, mitochondrial (Q1G1M7)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}. Plastid, chloroplast thylakoid membrane {ECO:0000256|RuleBase:RU000341}; Peripheral membrane protein {ECO:0000256|RuleBase:RU000341}.
Interaction partners:
Sequence:
RDAYSGDVFYLHSRLLERAAKLNSLLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELQAFAQFASALDKTSQNQLARGRRLRELLKQSQANPLPVEEQIATIYIGTRGYLDSLEIGQVKKFLDELRKHLKDTKPQFQEIISSSKTFTEEAEILLKEAIQEQLERFSLQEQT
Protein: Serpin B13 (HaCaT UV-repressible serpin) (Hurpin) (Headpin) (Peptidase inhibitor 13) (PI-13) (Proteinase inhibitor 13) (Q9UIV8)
Organism: Homo sapiens (Human)
Function: May play a role in the proliferation or differentiation of keratinocytes.
Subcellular location: Cytoplasm.
Interaction partners:
- Cathepsin G
- Cathepsin K
- Procathepsin L
- Serpin B3
- Runt-related transcription factor 1
- Cathepsin L2
- Core-binding factor subunit beta
Sequence:
MDSLGAVSTRLGFDLFKELKKTNDGNIFFSPVGILTAIGMVLLGTRGATASQLEEVFHSEKETKSSRIKAEEKEVIENTEAVHQQFQKFLTEISKLTNDYELNITNRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESKTNEKIKDLFPDGSISSSTKLVLVNMVYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTEEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP
Protein: Probable serine/threonine-protein kinase fhkA (EC 2.7.11.1) (Forkhead-associated kinase protein A) (Q54BF0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- 32 kDa heat shock protein
- Protein BUD31 homolog
- Probable serine/threonine-protein kinase atr1
- Eukaryotic translation initiation factor 6
Sequence:
MSQTNYIPSTPNKSTPPSELSSTPIDENDIGLLVSLNQEISSNIHVKIKIEENITIGRSKTCNIVVPELIVSGKHCIITRADAIENGNTNYGLLMIQDQSTNGTFINGKLIGKGKSRLLKNGDKLCLGKSTKEIDISFLYKSNYSNQLLLSSSTNNLNNSGTAQYIWERKDIKDDILKDYDFIKELGSGNFSVVYEGVNKNTGKRVAIKHLNLSKINTHTPKFKSQLNREIEILKFINHENVVEIYDIFYTKDQQLFFILELANGGELYNKIGFNEPLLNENQSKFIFKQILNAVSYLHSKGIAHRDLKPENILFDSYGDDYLKIKITDFGLARFIHEGELAKTLCGSPLYVAPEVILSLHHKNKYGTNSSSSSQSPTKDINSVGYGKSCDAWSLGAILYIVLCGTPPFDDDDDEEMSTPQLFEKIVSGNYRVEKLEKSLISSSAADLVKGLLTVDPDKRLTVEQALNHPWITEINNNSNNNNNNINNNSSNINIIKKSPLKTVNTNNNNNNCKLSSPIKNSSKLKRNLSNEPLNNNISNNNNTQTSFTGSLLNQLQLNEGELLKKRKTFLSNNDQKENINPVINNPFLKSSQ
Protein: Oligopeptide transporter 2 (Q06593)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transports tetra- and pentapeptides. Does not transport glutathione.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Peptide transporter PTR2
- Allantoate permease
Sequence:
MSETVKDKVIIDEKVSTKGTVDYAEGAEYSERLSNHSSDFSQWYTDEQILHFMKKLGYENRTLYDIPEDVAYILKKMPELTLEDSFKILKDSIIYFKDDENIPHDQYEEWKRLVDLEDLDSKEGIDEYDSFDIRAFASAIKFHSPYQEVRAVVDPEDDPTIPVETFRAYFLAIIWSVIGSGFNEFFSHRVVSISLNTPIIQMFLYICGKAWAKTIPCWTITIRGRKYGINIDKPWTQKEQMFSTLLYAICQGAFYTHYNILTQKLFYHSAFSFGYQFLLSLSVQFIGFGFAGILRKFVVYPARALWPTVMPTIAINKALLGKEKHESGMSRYKFFFLTFFIMFIYNWFPTYIINILNTFNWMTWIKPSNINLANITGGVTGLGINPISSFDWNVISFNSPLVYPFWSYLTQYLGCILAALIVIAVYYSNYMSCQYLPIFTNSLYTNTGHSFKVTEVLDSDNKLDVKKYQSYSPPYYSAGNLVSYGAFICAYPLMITWSFIVHSKLLFNAFKDWALNLWAMRKLKSWVTMFKSDYRALDDYDDPHSNAMKNYKEVPDWWYFAILIGSLVVGIAVVEHYPTNTPVWGLFVCLGFNFVFLIPTTILQATTGYSFGLNLLIEMVMGYALPGNPIAIMILKAFGYNIDGQADNYVSNLKIAHYCKIPPMALFRGQCVIVFIQIFVNLGVLNWQISNIKDFCTPHQNAKFTCPDAVTYYNASVVWGAIGPKRIFNYIYPIFKWCWLIGACIGIFFGVWKRWGKFYPRYFDPMLFVGGMLNMSPPYNLMYYTSGMIVSYISQYYMKRHHLNLWEKYNYVLSAGFSTGLVLSAIIIFFAVQYKDTAFNWWGNTVPYAGADGVGYPLKNITDTANGYFGYAPGHYP
Protein: Syntaxin, putative (Q38FF1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Syntaxin, putative
- Syntaxin, putative
- Vesicle transport v-SNARE N-terminal domain-containing protein
- SNARE protein, putative
- Gamma-soluble NSF attachment protein
- Syntaxin, putative
Sequence:
MSDVKGALTRLERLHEACGGAGLSTVGALPADGGANMSVNEVGSYEKGQYHVACLMKRARESMTILAETGESMDIARRAEISNSIRRDMSAVKKECTALNRVAMKEGKRGDYMQLLSFVNKTEQFQRRLHNGPVLGEASGAIGDGSTHVGGTTPGVPEANAVTADSENREVGSFISASEVEGFLQFFEETRKRDAEIDQVLERISAGVTRLQENALTLRSELCTQQRLLDDTEEKVDGIHAKLDSLNIKLRRTLEQVDKDRMSVYILCCLLLLGIYGAIYNMSR
Protein: UDP-N-acetylbacillosamine N-acetyltransferase (EC 2.3.1.203) (Protein glycosylation D) (UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase) (Q0P9D1)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation pathway.
Interaction partners:
- Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase
- UDP-N-acetylbacillosamine transaminase
- N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
- N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase
- GalNAc
- GalNAc-alpha-
- Protein glycosylation K
- Undecaprenyl-diphosphooligosaccharide--protein glycotransferase
- UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase
- UDP-glucose 4-epimerase
Sequence:
MARTEKIYIYGASGHGLVCEDVAKNMGYKECIFLDDFKGMKFESTLPKYDFFIAIGNNEIRKKIYQKISENGFKIVNLIHKSALISPSAIVEENAGILIMPYVVINAKAKIEKGVILNTSSVIEHECVIGEFSHVSVGAKCAGNVKIGKNCFLGINSCVLPNLSLADDSILGGGATLVKNQDEKGVFVGVPAKRM
Protein: Anaphase-promoting complex subunit 4 (Cyclosome subunit 4) (O65418)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 2
- Mitotic spindle checkpoint protein MAD2
- Ubiquitin-conjugating enzyme E2 22
Sequence:
MSEMASDEEENIIPFQLQFDKPIPFQIKIAEWNPEKDLLAMVTEDSKILLHRFNWQRLWTISPGKPVTSLCWRPDGKAIAVGLEDGTISLHDVENGKLLRNLKPHDVAVVCLNWEEDGQSNTDESGNFSVYEDRTSRFFPPAPRPPKMPGLVAGDSSFMDDGEDSLAELSNTSFRKFNILCTGDRDGNICFSIFGIFQIGKINIHELSLPVPHLDEHASCKLFNASIYKVALSKDLCRLVVMCTGELKDCDIKPREEKINVQDLPGLHCLAMDTSIFWKRKYELHQVAQQASNIEDLTEVIRASLSVMNKQWADAMKTFHEKFHSLSTLIIDNGLESSPQEEFLSLLGGARISPALNQFLVNSLGEVGVKRVLKSVCGTGKELQQVVLDHLQPAAEIIGFRIGELRGLSRWRARYQGIGLDEMLLNEATENTGLLLVQVQRFMMVLSSVVQQFSNFFNWLVRSIKYLMQEPNDQLLSYNSELLVVFLKFLYDQDPVKDLLELSEAGDDIEIDLKTIGRVKELLQFGGFSECDFLQRTLAKEFQHMESSFKMAFQMPFTTISRKISCMKLLPLCPLQLSTTQTPTTIPMSLSFYKNELSDDTPCQSGYTDYISFQVPDETFPEISNCIGIAKGYKQNSNNEKNGYTSLEAVLLSVPNGYTCVDLSLYKDKELVLLLNKTNTDSEGSGEACMMVVQTGDLAFISISGSSSLNQWELEDLKGSIVNLEMENEKVRKVPHSVIAPLAVSASRGVACVFAERRRALVYILEEDEDEEISDEK