wanglab/gogpt-training-data huggingface dataset:
Protein: Rab GDP dissociation inhibitor (Q24349)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU363124}.
Interaction partners:
Sequence:
MDEEYDVDVLGTGLKECILSGIMLSVSGKKVLHIDRNKYYGGESASITPLEELFQRYRTGAARPRFGRGRDWNVDLIPKFLMANGQLVKLLIHTGVTRYLEFKSIEGSYVYKGGKIAKVPVDQKRPWHPDLMGMFEKRRFRNFLIYVQDFREDDPKTWKDFDPTKANMQGLYDKFGLDKNTQDFTGHALALFRDDEYLNEPAVNTIRRIKLYSDSLARYGKSPYLYPMYGLGELPQGFARLSAIYGGTYMLDKPIDEIVLGEGGKVVGVRSGEEVAKCKQVYCDPSYVPRRLRKRGKVIRCICIQDHPGASTKDGLSTQIIIPQKQVGRKSDIYVSLVSSTHQVAAKGWFVGMVSTTVETENPEVEIKPGLDLLEPIAQKFVTISDYLEPIDDGSESQIFISESYDATTHFETTCWDVLNIFKRGTGETFDFSKDQGTSWVTRSSKRE
Protein: 2-aminoethanethiol dioxygenase (EC 1.13.11.19) (Cysteamine dioxygenase) (Q96SZ5)
Organism: Homo sapiens (Human)
Function: Plays a vital role in regulating thiol metabolism and preserving oxygen homeostasis by oxidizing the sulfur of cysteamine and N-terminal cysteine-containing proteins to their corresponding sulfinic acids using O2 as a cosubstrate. Catalyzes the oxidation of cysteamine (2-aminoethanethiol) to hypotaurine. Catalyzes the oxidation of regulators of G-protein signaling 4 (RGS4) and 5 (RGS5) and interleukin-32 (IL32).
Interaction partners:
- Cysteine dioxygenase type 1
- Cysteine sulfinic acid decarboxylase
- Acidic amino acid decarboxylase GADL1
- Glutamate decarboxylase 2
- Glutamate decarboxylase 1
Sequence:
MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQLRAEDLNIAPRKATLQPLPPNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGMLKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPREREAVRPGVLRSRAEYTEASGPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACDLPREVWLLETPQADDFWCEGEPYPGPKVFP
Protein: Glutathione S-transferase U11 (AtGSTU11) (EC 2.5.1.18) (GST class-tau member 11) (Q9CAS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase L1
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase F12
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Glutathione S-transferase F14
- Glutathione reductase, chloroplastic
- Glutathione S-transferase DHAR2
- Glutathione S-transferase F8, chloroplastic
- Probable glutathione peroxidase 5
- Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
Sequence:
MGLMNRSKNDEYVKLLGAWPSPFVLRTRIALNLKNVAYEYLEEEDTLSSESVLNYNPVHKQIPILIHGNKPIRESLNIVMYVDETWLSGPPILPSDPFDRAVARFWDVYIDEHCFTSINGVAVAKGEENINAAIAKLEQCMALLEETFQECSKGRGFFGGENIGFIDIGFGSMLGPLTVLEKFTGVKFIHPENTPGLFHWADRFYAHEAVKPVMPDIEKLVQFARLKFNTSIFK
Protein: Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit) (Q6DRG7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Regulates myosin phosphatase activity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase
- Protein phosphatase 1 regulatory subunit 14A
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Protein phosphatase 1, regulatory
- cGMP-dependent protein kinase
- cGMP-dependent protein kinase
- Protein phosphatase 1 regulatory subunit 12C
Sequence:
MKMADAKQKRNEQLKRWIGSETDLEPPLLKKKKTKVKFDDGAVFLAACSSGDTEEVLRMLDRGADINYANVDGLTALHQACIDDNVDMVTFLVEHGACINQPDNEGWIPLHAAASCGYLDIAEYLISQGASVGVVNSEGETPLDIAEEEAMEELLQNEINRQGVDIEAARKEEERIMLRDARQWLNSGQINDVRHTKSGGTALHVAAAKGYAEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVEHLCDMDVVNKVGQTAFDVADEDILGYLEELQKKQNLLLSEKKDVKKSPLIETTTTGDNNQSVKPLKSKETLLLEPEKTAPRIETLEPEKVDEEEGEGKKDESSCSSEEEEEEDSESENEADKTKSSVPSSVSNSTPTTAPSSITVTSPTTPSNQVTTPTSPTKKVSTPAGKLSPKEEDRKDESPASWRLGLRKTGSYGALAEISTTKEAQKEKDTAGVMRSASSPRLSSSLDNKDKEKEKEKTRLAYVAPTIPRRHVSTSDIDEKENRDSAASLVRSGSYTRRRWEEDLKNSDGTASTNRTSSYQRSTSHTLALGRTSSSRDLPAKSSSASSLEPNNSKAWQPSSYYQSYSIHRSGSFGRRHEDPLSSTSSSTTTTTTTSSVTSPTGHRSLLSRYWAEESAEKEKEKEKESATVIPTINTAGTTTTTSTTGTVLGSDGRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRPTRPREDEKEEKEKQDKEKQEEKKETETKEDDYRSRYRSFEEKYRTSLASSTTASSTIPSSSSSSSSSLYSTSSLNRPNSLTGLTSTYSRSTRDTDRESDRKEKDEDRDGDDKSQPRSIRDRRRPREKRRSTGVSFWTQDSDENEPDHPSDSEGSTKGEPQSDRLSSNDPLSTSTSSTDRYESLSSRGIGESRRPYSRFEKDDSTDYKKLYEQILAENEKLKAQLRDTELELSDLKLQLEKATQRQERFADRSQLEMEKRERRALERKISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK
Protein: Exocrine gland secreted peptide 16 (Exocrine gland-secreting peptide 16) (A8R0U9)
Organism: Mus musculus (Mouse)
Interaction partners:
- Exocrine gland secreted peptide 15
Sequence:
MASFPLMYFLIFLVFPTILPEGMALKRTEKEPNISADLNDDFEISFCQTIRDRLDLMRMSRGSVVGKISLNYVVLMYCREYSLTM
Protein: Uncharacterized protein (Q4GYI3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MATPRQGPTRPPSAVAGMTEDEIAAGENAGKSMTCQGGLYATSERCRELLDDVANKERALSQLRCVLEEMAGAYEQLQRHSQRIETELETLTARYNVQQEELIAAKSKVSMQESKLQQADEDYQRRTQQLRWELKSAREERDEVTADRESLWTQIRSLRADVEEHRRVQQAAEAAWESKLADARKEATEKAHAVLREREEILSIREAELQRALSKLEGRFDETAAETRRLELLNESLRDRVGEMQECVQREAEMRHRLEAARGTQQQENKLLSECMELERRGRREQQKAIEGGYEAQLREMKRSYELLERERRRQEEESCRALRESRLATQLARDEWLAQQQHLELTISGLRGEVDRGRLRFDQVDELKQRAESELLRAQRELQFVQQRETTLQETVETLQGTVARHRATEVRLEGEIQRLLAVVAEREREVERWKCAAERLEWKRYVGAEEVPSLSSHGTCHFHQQCGHQDGRDVGGMCGPTTELPFSPESAVPAQPTVVGSLAPACSGPSTPSRPLPSFLTPCLRQYKRCQQPYHSQHIESIDRTPNCLLNDVSRFDCTQSSEEVQAELLRSIVQDVLWEHLQPGDGVSINLMGANGHPYSSASPTGARVGGQGVPHISPWHHESRRGPPVPTRPMGEQRKSVKASQERSQTAHDATRAQGNSSPLRNPLVELPNACATPLQGPMPRDCTIQLNIRDRSGGAEHHRCGSLSTSSAIAGSAVAASETAVSPKATPTPPFVAVTSTPNSSTLCSGAFLASTPNNLSVGSSATSHRRRSTLSTHFCNKEKSKRRSNVQGYFSKQRRQPPHDVVPAPVSYEGVNELGAGYGFESNPNNSNQRFSKQGRDSRSGRSPSEGSVKRLPSSASDIRCTSNVLSIGSDVTSSTCVSATPPAPLLQLTALQERFATMSIL
Protein: NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) (Flavoprotein WrbA) (NAD(P)H:quinone oxidoreductase) (NQO) (Q9I509)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable NAD
- NAD
- Probable NAD
- Dihydroneopterin triphosphate 2'-epimerase
- Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE
- NADPH:quinone reductase
- Quinone oxidoreductase
- NAD
- Arsenate reductase
- DUF2069 domain-containing protein
Sequence:
MSSPYILVLYYSRHGATAEMARQIARGVEQGGFEARVRTVPAVSTECEAVAPDIPAEGALYATLEDLKNCAGLALGSPTRFGNMASPLKYFLDGTSSLWLTGSLVGKPAAVFTSTASLHGGQETTQLSMLLPLLHHGMLVLGIPYSEPALLETRGGGTPYGASHFAGADGKRSLDEHELTLCRALGKRLAETAGKLGS
Protein: Ribonuclease MRP protein subunit rmp1 (RNA-processing protein rmp1) (Q9UT91)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as part of ribonuclease MRP (RNase MRP), which is involved in rRNA processing in mitochondria.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable ribonuclease P protein subunit 3
- Ribonuclease P/MRP protein subunit POP5
- Ribonucleases P/MRP protein subunit pop1
- Probable ribonuclease P protein subunit 1
- Ribonucleases P/MRP protein subunit pop3
- Uncharacterized protein C16C4.19
- Probable ribonucleases P protein subunit pop8
- Ribonucleases P/MRP protein subunit POP7
- Uncharacterized protein C6C3.09
- Ribonuclease P protein subunit rpr2
Sequence:
MQELQYDVVLLQKIVYRNRNQHRLSVWWRHVRMLLRRLKQSLDGNEKAKIAILEQLPKSYFYFTNLIAHGQYPALGLVLLGILARVWFVMGGIEYEAKIQSEIVFSQKEQKKLELQSQDDIDTGTVVARDELLATEPISLSINPASTSYEKLTVSSPNSFLKNQDESLFLSSSPITVSQGTKRKSKNSNSTVKKKKKRARKGRDEIDDIFG
Protein: Acyl-CoA ligase 891, peroxisomal (ACL891) (EC 6.2.1.-) (P9WEY3)
Organism: Penicillium brevicompactum
Function: Acyl-CoA ligase involved in the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893. The peroxisomal acyl-CoA ligase 891 converts the intermediate MFDHMP-3C into MFDHMP-3C-CoA which impairs its diffusion from the peroxisome. The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable).
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:31209052}.
Interaction partners:
Sequence:
MFFTQPPHLVKAEELKQEPPKGTAYSVAIPGTEQPGRSRVYRAWNAQKELLTTLDPQVTTAHDMFESTANRQPKNHCLGWRPYNSTTKTWDPYQWLTYETVQKRRAAFGAGLVELHQKHNCHRPGQYGVGLWAQNRPEWQITDLACISQSLYSVSIYDVLAPDATEYIINHAELNCVVTSLPHIPTLLKLKSSLPNLKMIVSLDPLDGPEQNGHSKRALLESMAAGLDLAIYTIDQVEELGLASKRGYNAPSASDIVTINYTSGTTGPPKGVVLTHGNAVAATSCGLTTIGQARGDTMCSYLPLAHIYARLAEHTAFWGGARIGYFHGNIVELVDDLKLLKPTGFMSVPRLYSRFGTAIRAATVEQPGFKGALSRHIVAAKMANMKNPDPSKATIKHALYDRIWAKKVAAALGLERAKYMISGSAPLDPTLHNFLRVATGTDVVQGYGLTESYASATAQSTQDLSSGNCGRLAPCTEACLVSLPDMEYSVEDKPFPRGELLLRGNNMFREYYKNDDETSKAVTEDGWFRTGDVCTVDAQGRFIIIDRRKNVLKLAQGEYISPERLEGVILSELGYVAQAYVHGDSSETFLVGIFGVAPDLFAPYASKVLGKTIAPTDVEGLKEHLNDDKLRRAVLRDLERVAKKHKFAGYERVRNVSLKVDPFTVENNLLTPTLKLKRPPVVKMYRTLLDQLYGQANEEQSAPRAKL
Protein: Isoamyl alcohol oxidase, putative (AFU_orthologue AFUA_1G01180) (Q5B9Y2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MKAVWIAALLFGATATAAPAASSSNTSCHCLPGDACWPSAAKWNALNSTVGGRLIATVPIGSVCHEPTYDAEACAQLQEDWNLPQTHYVSSSSIMQQFFTNRSCDPFDEDSSCELGNYVSYAVDVASSADVVAAIKFAQQNNIRLVIKNTGHDYLGRSTGAGALSVWTHHLNSIEYLDWSDSTYSGPAYKLGSGVMGYEVLEATHAQGYVLVGGECPTVGLAGGYTQGGGHSALSTTFGLGADQTLAFEVVTANGRVVTASRTKNTDLYWALSGGGAGNWGVVLSVTVKAYKSAPVSGAYLAFTTSNLSEDVYTKALTQFHELLPAMVDAGTTVIYQILPGYFLIKPLTAYNKTTAEVKAVLAPFLSALDGLSIQYSVSYTEYETYYDHYEKYMGPLPNGNLEVGTFTYGGRLLPRSVVESDAASIAQVLYNFTSQNVVAVGVGLNVSNTNDVDNAIFAPWRKALVTMQFGITLGNEKPWSQILADQQTVTNELAPQLEALTPGSGTYENESNFLQPNWKQVFFGENYDKLAKIKKKWDPNTFFYSFKGVGSDYWTVSESGRMCKA
Protein: Leucine aminopeptidase 2 (EC 3.4.11.-) (Epoxide hydrolase) (EC 3.3.2.10) (Leucyl aminopeptidase yscIV) (AP IV) (Leukotriene A-4 hydrolase homolog) (LTA-4 hydrolase) (Q10740)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mannitol dehydrogenase DSF1
- Inner nuclear membrane protein SRC1
- Inner nuclear membrane protein HEH2
- Transcription initiation factor TFIID subunit 2
- Uncharacterized protein YJL049W
Sequence:
MFLLPFVIRHSSSIYLPTLRFRGLLTVISRNIHISTPHKMLPLSIEQRRPSRSPEYDQSTLSNYKDFAVLHTDLNLSVSFEKSAISGSVTFQLKKLHEGKNKSDELHLDTSYLDVQEVHIDGSKADFQIEQRKEPLGSRLVINNASCNDNFTLNIQFRTTDKCTALQWLNSKQTKGGKPYVFSQLEAIHARSLFPCFDTPSVKSTFTASIESPLPVVFSGIRIEDTSKDTNIYRFEQKVPIPAYLIGIASGDLSSAPIGPRSTVYTEPFRLKDCQWEFENDVEKFIQTAEKIIFEYEWGTYDILVNVDSYPYGGMESPNMTFATPTLIAHDRSNIDVIAHELAHSWSGNLVTNCSWNHFWLNEGWTVYLERRIIGAIHGEPTRHFSALIGWSDLQNSIDSMKDPERFSTLVQNLNDNTDPDDAFSTVPYEKGFNLLFHLETILGGKAEFDPFIRHYFKKFAKKSLDTFQFLDTLYEFYPEKKEILDSVDWETWLYKPGMPPRPHFITALADNVYQLADKWVEMAQHLKTTEDFRSEFNAIDIKDFNSNQLVLFLETLTQNGHSNKKPKDFDWAKFPVASRALLDIYQDNIVKSQNAEVVFKMFKFQIFAKLQEEYKHLADWLGTVGRMKFVRPGYRLLNSVDRRLALATFDKFKDTYHPICKALVKQDLGL
Protein: GH25793p (Verprolin 1, isoform F) (Verprolin 1, isoform K) (Q8SX98)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAIPPPPGPPPPPGPPPPPAMGGLKLGGAGGADARSALLSSIQKGTKLKKTTTVDKSGPALSGKVCGGDGGAGIGAKRTLNNNTSTSNHNNSSSSSNGLGNGTPKLGGLFEGLSQMPKLKPVNGIRATPSAGSAATTTSKSTTNSSAQQRSNSPPAATSASNASNGPMDFNTELTKHLTLKRQKQQQQQQPQPPTNNTHINATEANLRTNRGPPPQPPKSANSNDSILERMNIPRTAPTPPFGNSSSVKAASPTLSDSGSNSSGSGGGSGSVKSKAANLNISLGNSFVNSSKSTVSASTASLNSSLTSSTGSVRNLAPNKSTLFGGSSGSSSGSSSGGGYASVHKSSPPSTADSTPSVTPTPPPLQLPMKPAISFGKPNFAPKPPGLNQLAMANGQQRPAVTRHHSMKSPRSPPAAGIVNGLVFPTQQHLGTLRGPLQFHGSESSSPNTSAGSMRCAPNPPKSRPSVKPPPPPTPARSFSNTNLNNIGGSTMFSAVNTALIQSSAISSQAPSPPITQPPSSSSSSNSVAALRDQFRGGAGMSNGAPSPPLPPTPAPSSNPSSASASPKSLLRDNVKPIILNGGPLNPPAPPPHRSCPPPPPPQRQSSNGGSGSGSAPVPPQRHSSIRPNAPSTPPTHMANASHQFGSSSGLSSGSGAGAAASVGRLVNDLETKFGKRFHNVTEFPKPPPFLNIQKVYPSRTFKATNGM
Protein: Proteasome activator complex subunit 2 (11S regulator complex subunit beta) (REG-beta) (Activator of multicatalytic protease subunit 2) (Proteasome activator 28 subunit beta) (PA28b) (PA28beta) (Q9UL46)
Organism: Homo sapiens (Human)
Function: Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.
Interaction partners:
- Proteasome activator complex subunit 1
- Proteasome subunit alpha type-2
- Proteasome subunit beta type-7
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-4
- Proteasome subunit beta type-9
- Proteasome subunit beta type-5
Sequence:
MAKPCGVRLSGEARKQVEVFRQNLFQEAEEFLYRFLPQKIIYLNQLLQEDSLNVADLTSLRAPLDIPIPDPPPKDDEMETDKQEKKEVHKCGFLPGNEKVLSLLALVKPEVWTLKEKCILVITWIQHLIPKIEDGNDFGVAIQEKVLERVNAVKTKVEAFQTTISKYFSERGDAVAKASKETHVMDYRALVHERDEAAYGELRAMVLDLRAFYAELYHIISSNLEKIVNPKGEEKPSMY
Protein: Uncharacterized protein (Q57Y65)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
Sequence:
MNDAAVAGHSGGFHRPNPLGEDRSPSSSIGSVTGAAANDGAAAGSERPISVEAKAAIEYGEGYRVILESMGEPGYGAMKALFYGEEGPPPSTIPAISVSFELFESVQTRFVNTELVLERTRAELHTRCQELNETNARYEQLQASYDVLEKRSLELEKNNTQLHQSIARQNISADQLRQQISRLKAELGMFEDRMAKRDEELQISNNRVAEGLVALSLKETIITNLRRQIGMASYGRRLPHQQLMHEGGEYSAEALKIIAEGVEGNSVEAEHRLYTLGLESEIRKLEDEKKYIMMRHTLYRKHVQEVTEAYETLCMAKEDAVLSHVCVGPPAEGTQEETESVPTTGDGRSTKFDSTQDRLSLGRASPKSADGATLQGAPTSVVPAQLVARRDVFTDDEGSVERTPLIASHSTLSDSEEDVPSAEEAVPKTKSKKKSNVLPPSVTSGRDSRASVSWDKLATSVDDAALPPSSKGRQSGAAQPPKTKGDLFSPLGLPRPDTGSTSSPRQSLTTRTTEKSKKKSTSKRPAKEATASKSGAAGHSGERAASDLSFLPSDNTDARVPSAGSDSTRRGAHGESRTEKQSRRDDASQRPFSGGSTRSSDTGRRRVTSASKRSLTTAEDADIRERRKTPSERRTASHSQTSRGGTATTRDLSSHALPPLGVGRGSSAGAGGEATTDDGERENSQETRSLSQTMELMARMSPLSVSVGNHVAELARHYGLLHQSVIALNELLESLSLRGSTDSTKTVKFRAPGPNTNTVVLTEHMSEVVLSDTLVLENFLRHVRGRLPSGGSASDTTGERSSLSSSNNLAPGSPRGGAAPKFPSKGTGASQGLRAPGRADDTGSPQAKGAQQARKVRAVAAASPVTSVGGGSTRSAASPSNQKASPVRGSGGQQQPATGGDGDVRTTAKPASRHGPGQVRGRESSGDISSDERYQQGGKTDLPAQVQPQSPRGRKVSSQLSRSGGGRSSPKSFQSHDSGSLADSKRRWSKGGTAHPIQPSHGTVGGGSSVFSSSAVEKVDTPPDTAPRPTAVPAKRSAPGSLRGPITDAPQFGPGTSDLPCSDDRDTKVSESTGGATFVPFLSEASGYVRERSPPPVTLTRRGVQRIPWRASVIRVDLLTDIPEVKQRDRAPPARFTGLQQNFSFIQQRGTPWYDPGTPLLEGDEDQYEPREQRLLHAYTFTPRTAEQIFAGIGRGRERGSVGAGGTGYSERTGYSERAGPGSVGYGSATGRDARTVPGSFGYGSRAGRDARTGPGSVGAGGTGYSERTGPGSVGYGPGTGHSDARAGHGSFGYGYGAGGSGGGGPGTGFAHRGAYKPLPLQRKLARTHELPQRKLKPGVTLDIGTEGFPTARTYLRPAEEAYYRSLSRMLLAHRPKSATGPVLPESPVLEPNMFKCFNPISTMSSVQSNPVVRPRPYVNMGAEGGHSNDISRRRGTSALRPVGRNLKMCSPLPCINITLGDVGVDENLWQESGLPQSWRPLSSTAKCVQRSLLRNVNRLCQSTLGRRPSNLAFCRNVVKRYVQKVQSCGSGDFSPPRLSGALIRKQILRYSANRARTLRHSAKRLPRRAFFVKQCILARRGAELCSNWVLVPLELRHLGGRHPPSVSPNSSFRMSP
Protein: LD09783p (Q8MSY0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEGDFPDDLEDIVSSMIKETSECASAAGGGFLNSLESSLPAATVATVVSTASTNTSSIGSIKLNGEHHILEHDDLIKKLTESKPPAIKVKLEEMPPLLTIKKEPVIKPMASGLKVEAKVEVKLEPKVEPKSEEKLQEKPPSESSSASLQPISIEIPAQVDGETPRIRTRASSRLESPLDAQKASPDPTTVTGVSTTAATAANASTTVKSLSRASSTASPRVVTPTPNHNNNNNKRRRQESECGSSNDGADLGENSIKRPRISSGTTSNNNATETAAEHNAGAGLPKKVEIESSDSDEPLIEVAGKVRNSKQAQVEAADAAAVGVEKHVTRRNAQQLQPPQNKTAGNHAPSSTPALGTPRSGKAQAPVGATSAANNNHNSSTANNASVVPSSVTTTTMPGGAVVTTSQVNSGTSVVHATRGATAAAASTTNNNSASSPTDEKIGTRRSVRASAAANKIIYSRSNAAAAAAAAAAAAEPKGTTGKAGAAVGANNAGNVESVAEARRKTRSAVIGESMLTEGRRRRTSRDYK
Protein: Positive alginate biosynthesis regulatory protein (P26275)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Positive regulator of the algD gene, which codes for a GDP-mannose dehydrogenase, a key step enzyme in the alginate biosynthesis pathway.
Interaction partners:
- Alginate biosynthesis protein AlgZ/FimS
- RNA polymerase sigma-H factor
- Sigma factor AlgU negative regulatory protein
- GDP-mannose 6-dehydrogenase
- Protein PilG
- Transcription factor AmrZ
- Sigma factor AlgU regulatory protein MucB
- Transcriptional regulatory protein AlgQ
- cAMP-activated global transcriptional regulator Vfr
- Phosphomannomutase/phosphoglucomutase
Sequence:
MNVLIVDDEPLARERLARLVGQLDGYRVLEPSASNGEEALTLIDSLKPDIVLLDIRMPGLDGLQVAARLCEREAPPAVIFCTAHDEFALEAFQVSAVGYLVKPVRSEDLAEALKKASRPNRVQLAALTKPPASGGSGPRSHISARTRKGIELIPLEEVIFFIADHKYVTLRHAQGEVLLDEPLKALEDEFGERFVRIHRNALVARERIERLQRTPLGHFQLYLKGLDGDALTVSRRHVAGVRRLMHQL
Protein: WD repeat-containing protein pop2 (Proteolysis factor sud1) (O14170)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in maintenance of ploidy through proteasome dependent degradation of CDK inhibitor rum1 and S-phase initiator cdc18. Functions as a recognition factor for rum1 and cdc18, which are subsequently ubiquitinated and targeted to the 26S proteasome for degradation. Together with pop1, required for cig2 instability during G2 and M phase and cig2 degradation in exponentially growing cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12167173}. Nucleus {ECO:0000269|PubMed:12167173}.
Interaction partners:
- Cell division control protein 18
- Suppressor of kinetochore protein 1
- RING-box protein pip1
- Cullin-1
- WD repeat-containing protein pop1
- Cyclin-dependent kinase inhibitor rum1
- Ubiquitin-conjugating enzyme E2 4
- Chromatin modification-related protein rik1
- Anaphase-promoting complex subunit 3
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
Sequence:
MSLSRCPTDNSSSRINSSVPLINSSSPATPPESFDPQVFPSSLIHGDNLLPQDDQIASDPRSESNSCNGNTSSSLPCTDSYQYPLKHSCTPSFLRKFNESIENVSYKCLDHSPPDSVPGDFSISLVPQRNFLYSHSSLPPKIISIDRNNRIKLDNSISSNSDNFPPSPKVDTSNTVSPGSKPISEDLEDLNLQSIVQTFEDLPEGIQSYAFFQLLRSCNRQSMRLLLNECEPLLKKDILSNLPFSIVQSILLNLDIHSFLSCRLVSPTWNRILDVHTSYWKHMFSLFGFQINENDWKYANPNLNRPPFLHNDQISDDYFPEIFKRHFLNRKRWLFPSIPPSHLSFPIHVPNFMITSLLLHKDRIITTSGSGTIQIHNAITGVLEARLEGHKEGVWAVKIHENTLVSGSIDKTVRVWNIEKAKCTHIFRGHISIIRCLEILVPSRLIRHGVEIVEPDQPYIVSGSRDHTLRVWKLPKNTDPPYLPDNTNSIDRWEKNPYFVHTLIGHTDSVRTISGYGDILVSGSYDSSIRIWRVSTGECLYHLRGHSLRIYSVLYEPERNICISGSMDKSIRVWDLSTGTCKYVLEGHDAFVTLLNVFQNRLISGSADSTIRIWDLNTGKPLMVLPSNSGYISSFVSDEHKIISGNDGSVKLWDVRTGKLLRFLLTDLTKIWHVDFDAMRCVAAVQRDDQAYLEVINFSGSRP
Protein: Uncharacterized protein YKL023W (P36103)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Antiviral protein SKI8
- Antiviral helicase SKI2
- Suppressor protein SRP40
Sequence:
MNKEELLGFLLDDSIDSQKRCVTDQQAYSNWLKNDNDERTAHEESSSQSTIAALNKKKQTEAAQEDIEELLNGLEGIIGGADPRNLKSKSKRKTKKGGSKPREENVNTEKHIVMLEVEDFSDMSTHEDVNGASPSPNLDRSKKNEKRRKNAKELSYDELKDKLEVTTRKSRLECKDLKKKVHGLERRNLELEQRLEELKIENQTLIEINNKLLKNTNEDEINKSQRNKEKDRKRRERRTARRKDERKQEKKQEKKQDNKTSQSFPSSTDMNGQPIEF
Protein: Tetraspanin-13 (Tspan-13) (Transmembrane 4 superfamily member 13) (Q9D8C2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVCGGFSCSKNCLCALNLLYTLVSLLLIGIAAWGIGFGLISSLRVVGVVIAVGIFLFLIALVGLIGAVKHHQVLLFFYMIILLLVFIVQFSVSCACLALNREQQGQLLEVGWNNTASARNDIQRNLNCCGFRSYNPNDTCPASCAKSTQKCSSCAPIIGEYAGEVLRFVGGIGLFFSFTEILGVWLTYRYRNQKDPRANPSAFL
Protein: Defensin (P36192)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responsible for the anti Gram-positive activity of immune hemolymph. Expressed in the absence of immune challenge during metamorphosis.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710, ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:8168509}.
Interaction partners:
- Dorsal-related immunity factor Dif
- Cecropin-A1
- Diptericin B
- Cecropin-C
- Cecropin-B
- Metchnikowin
- Diptericin A
- Protein immune deficiency
- Attacin-A
- Attacin-D
Sequence:
MKFFVLVAIAFALLACVAQAQPVSDVDPIPEDHVLVHEDAHQEVLQHSRQKRATCDLLSKWNWNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Protein: UspA domain-containing protein (A0A0H3LA21)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Interaction partners:
Sequence:
MSAQQTNLGIVVGVDGSPCSHTAVEWAARDAQMRNVALRVVQVVPPVITAPEGWAFEYSRFQEAQKREIVEHSYLVAQAHQIVEQAHKVALEASSSGRAAQITGEVLHGQIVPTLANISRQVAMVVLGYRGQGAVAGALLGSVSSSLVRHAHGPVAVIPEEPRPARPPHAPVVVGIDGSPTSGLAAEIAFDEASRRGVDLVALHAWSDMGPLDFPRLNWAPIEWRNLEDEQEKMLARRLSGWQDRYPDVVVHKVVVCDRPAPRLLELAQTAQLVVVGSHGRGGFPGMHLGSVSRAVVNSGQAPVIVARIPQDPAVPA
Protein: Endochitinase EP3 (EC 3.2.1.14) (Chitinase class IV) (AtchitIV) (Protein HOMOLOG OF CARROT EP3-3 CHITINASE) (AtEP3) (Q9M2U5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in hypersensitive reaction upon Xanthomonas campestris infection.
Interaction partners:
- Amino acid transporter AVT1A
- Class V chitinase
- Hevein-like preproprotein
- Kunitz trypsin inhibitor 3
- Putative cysteine-rich receptor-like protein kinase 9
Sequence:
MLTPTISKSISLVTILLVLQAFSNTTKAQNCGCSSELCCSQFGFCGNTSDYCGVGCQQGPCFAPPPANGVSVAEIVTQEFFNGIISQAASSCAGNRFYSRGAFLEALDSYSRFGRVGSTDDSRREIAAFFAHVTHETGHFCYIEEIDGASKDYCDENATQYPCNPNKGYYGRGPIQLSWNFNYGPAGTAIGFDGLNAPETVATDPVISFKTALWYWTNRVQPVISQGFGATIRAINGALECDGANTATVQARVRYYTDYCRQLGVDPGNNLTC
Protein: Mitochondrial chaperone BCS1 (h-BCS1) (EC 3.6.1.-) (BCS1-like protein) (Q9Y276)
Organism: Homo sapiens (Human)
Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:9878253}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Heme A synthase COX15
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 1
- Cytochrome b-c1 complex subunit 9
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MPLSDFILALKDNPYFGAGFGLVGVGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRHSTRTQHLSVETSYLQHESGRISTKFEFVPSPGNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFGYPRRRRPLNSVVLQQGLADRIVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVLLEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYVGYCSHWQLTQMFQRFYPGQAPSLAENFAEHVLRATNQISPAQVQGYFMLYKNDPVGAIHNAESLRR