wanglab/gogpt-training-data huggingface dataset:
Protein: Auxin transporter-like protein 3 (AUX1-like protein 3) (Q9CA25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carrier protein involved in proton-driven auxin influx. Mediates the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips by contributing to the loading of auxin in vascular tissues and facilitating acropetal (base to tip) auxin transport within inner tissues of the root apex, and basipetal (tip to base) auxin transport within outer tissues of the root apex (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Auxin efflux carrier component 3
- Auxin efflux carrier component 7
- Auxin efflux carrier component 4
- ABC transporter B family member 19
- Auxin efflux carrier component 2
- Auxin response factor 7
- LOB domain-containing protein 16
- Auxin response factor 19
- Auxin efflux carrier component 5
- Auxin efflux carrier component 8
Sequence:
MAAEKIETVVAGNYLEMEREEENISGNKKSSTKTKLSNFFWHGGSVYDAWFSCASNQVAQVLLTLPYSFSQLGMMSGILFQLFYGLMGSWTAYLISVLYVEYRTRKEREKFDFRNHVIQWFEVLDGLLGKHWRNLGLIFNCTFLLFGSVIQLIACASNIYYINDKLDKRTWTYIFGACCATTVFIPSFHNYRIWSFLGLAMTTYTSWYLTIASLLHGQAEDVKHSGPTTMVLYFTGATNILYTFGGHAVTVEIMHAMWKPQKFKAIYLLATIYVLTLTLPSASAVYWAFGDKLLTHSNALSLLPKTGFRDTAVILMLIHQFITFGFASTPLYFVWEKLIGVHETKSMFKRAMARLPVVVPIWFLAIIFPFFGPINSAVGSLLVSFTVYIIPALAHMLTFAPAPSRENAVERPPRVVGGWMGTYCINIFVVVWVFVVGFGFGGWASMVNFVRQIDTFGLFTKCYQCPPHKP
Protein: Nucleolar protein 56 (Nucleolar protein 5A) (Q6DRE5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- WD repeat domain 43.
- WD repeat domain 36
- H/ACA ribonucleoprotein complex subunit 2-like protein
- U3 small nucleolar RNA-interacting protein 2
- rRNA 2'-O-methyltransferase fibrillarin
- BMS1 ribosome biogenesis factor
- WD repeat domain 46.
- H/ACA ribonucleoprotein complex subunit DKC1
- Nucleolar protein 58
- NHP2-like protein 1
Sequence:
MVLLHVLFEHAAGYALLAVKEVEEIGMLLPQVEESVLNVGKFSSVVKLSAFFPFKSAQGALENINAVSEGVVHADLKLFLETNLPSGGKKKPMLGVSDAKLGAALQEELNLSIQTGGVVAEIIRGVRLHFHSLVKGLTAQAASKAQLGLGHSYSRAKVKFNVNRADNMIIQSIALLDQLDKDINTFSMRVREWYGYHFPELIKIVSDNSTYCKLAKLIGNRKELSEEMLEAMEEITMDSAKAQAILDASRSSMGMDISPIDLINIECFSSRVVSLTDYRQELQEYLRSKMGQVAPNLAALIGEVVGARLISHAGSLTNLAKYPASTVQILGAEKALFRALKTRGNTPKYGLIFHSTFIGRAAAKNKGRISRYLANKCTIASRIDCFSEVPTSVFGDKLRDQVEERLAFYETGEAPRKNLDVMKEAVAQASEVAAEIKRKLEKKEKKKKKRQKKLEALSTAEGDEETNGDVEENEVATKKKKKKQAAEEMEVKEDEEVTTNGVEETPGKKKKKRKIEAVEAEPEVQEEADETQVEKKKKKKKKKAQEDE
Protein: KRR1 small subunit processome component homolog (KRR-R motif-containing protein 1) (Ribosomal RNA assembly protein mis3) (O74777)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10947840, ECO:0000269|PubMed:16823372}.
Interaction partners:
- rRNA-processing protein fcf1
- U3 small nucleolar RNA-associated protein 6
- Uncharacterized protein C3B8.09
- Ribosome biogenesis protein enp2 homolog
- Uncharacterized protein C13G1.09
- Uncharacterized WD repeat-containing protein C2E1P5.05
- Probable U3 small nucleolar RNA-associated protein 7
- Probable U3 small nucleolar RNA-associated protein 18
- Probable nucleolar complex protein 14
- U3 small nucleolar RNA-associated protein 21 homolog
Sequence:
MTEVESSTENNVIVNKNKRYRRDKPWDTDDIDHWKIEPFTKDDSKESFLEESSFATLFPKYREKYLREVWPHVTRALDKFGITCVLDLVEGSMTVKTTRKTFDPYSILDARDLIKLLARSVPFPQAVKIMQDGVACDIIKIGNILRNKERFVKRRQRLIGTNGQTLKALELLTQCYILVQGTTVAVMGGYKGLKEVRRIVEDCMHNIHPIYHIKELMIKRELAKDPTLANESWDRFLPQFKKRNVARRKPAKIRETKEYTPFPPAQPPSKLDLEIESGEYFLKKEEKERKKRAEKKEQQKEKKKEKEKERMKAFIPPEESSKKRKRD
Protein: Amine oxidase (EC 1.4.3.-) (Q2U8B9)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Aromatic-L-amino-acid/L-histidine decarboxylase
- Amine oxidase
- Amine oxidase domain-containing protein
- VOC domain-containing protein
- D-lactate dehydratase
- Lactoylglutathione lyase
- D-amino-acid oxidase
- 4-aminobutyrate aminotransferase
- aldehyde dehydrogenase
- Aldehyde dehydrogenase domain-containing protein
Sequence:
MAPHPLAILSEEETNIAREVVVAAHPNTVLHFREIYLSEPPKEQLQEFLAIEHAGRLSPTTPRPPRLALCQYDVISGDRIPVYQEAEVDVNTRKRVQHKIIGKEHHAALTLAEFEVLVERCFASPLFQKAMEDFDLPKGFEVVIEPWPYGGRDHSDPNRRFFQALCFATNTTKNNEDANFYSYPLPIIPVMDATTQEIVRIDRPATGGKGEGLHEQTFSRDIIGHCKDSDYVPELLPNGSRKDLKPLNVVQPEGPSFKITNESLVEWQKWRFRVAFNPREGATIHDVWYDGRSVMYRLAISEMTVPYADPRPPYHRKQAFDFGDGGGGNMANNLSIGCDCLGVIKYFDAVITGADGKAQKLPNAICLHEQDNGIGWKHSNWRTGRAVVTRHRELVVQFIITLANYEYIFAYKFDQAGGITVESRATGILNVVNIDPGKTSDYGNVVSGGVLAQNHQHIFCVRMDPAVDGANNSVVIEESHPVPMNEATNPNGNYYKVTNQTIERATYLDAAPQLNRVVKMVNPNKTNPISQKPVAYKFTPLATQTLLADPNSIQARRAQFAQHHVWVTKYRDAELYAGGRYTLQSQVEVDGVADAVKRGDAVDNTDVVVWSTFGITHNPRVEDWPVMPVEIFQLMIRPSDFFTENPAIDVPSGKNAASRVVQSECCRNSHI
Protein: Myosin-3 (Muscle embryonic myosin heavy chain) (Myosin heavy chain 3) (Myosin heavy chain, fast skeletal muscle, embryonic) (SMHCE) (P11055)
Organism: Homo sapiens (Human)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Troponin I, fast skeletal muscle
- Troponin T, fast skeletal muscle
- Tropomyosin beta chain
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin regulatory light chain 11
- Troponin I, slow skeletal muscle
- Alpha-actinin-2
- Myosin-4
- Myosin-6
- Myosin light chain 3
Sequence:
MSSDTEMEVFGIAAPFLRKSEKERIEAQNQPFDAKTYCFVVDSKEEYAKGKIKSSQDGKVTVETEDNRTLVVKPEDVYAMNPPKFDRIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDDRLAKLITRTQAVCRGFLMRVEFQKMVQRRESIFCIQYNIRSFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVHESEE
Protein: ATP-grasp domain-containing protein (Q384P9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Biotin--acetyl-CoA-carboxylase ligase, putative
- Fatty acid desaturase, putative
Sequence:
MPKEEQCSHCDKLLQTSPTVDNEDYARLINYLVDNFGCSWESAQCTVRRHWPNVDACVADLRRKERPCLVAVEVYLLQREHMQDLAKSLLPIDSSQLPCFSKANLNGRSKGYPLLTWAEVAEKINSGPGIEVHFVDTDAADVLDGPAAYEDFYQRKVVTEGFSDIVAFVTAVDGVVPLVDYLHRRHFGDPDTRRLAYPYGGSGRCCRVPRSISETYARAHAQVPCCADAALSTARRTRILLGNDPATSVSKRQDKSSMQNTLKEHGLLYIKGFSGRDVGEMKRQMRRERIMFPVIVKPVSGAGSEFVTLCYDENDVDIAFAVSSEVQTTQQTDASHMLLQEYIEGPEYVVNVVSYMGIHVVSDVWKSWKYPYPVKSTRLRPSVEKKLMQSYLTSGRGREPVPHTTTVLMYDRIEFVHELSKLPASSEERRVVAYTLKCLDALGLQQGCSHCEVRVDNRPGSSTKGMPVLIELNARMLGDVPRATSFVGYDQYKLMMYLLLCASSIPEDEFSRLDVSGEHCGGDSRDALPWPPAPQLYNSLKVDVTLHVVFVRAAESSYLCIPGFRAIQALPTYKNLTRNSTLEDLKPGMLLAVCKTFDLLTSPGAIVMEGTDDDIRRDTAYIRRVENKDMREWKDMIDAAVGILNSVYVPLSSTQVHTPLLASAPAASNARMELCVAASSLIQSYERARLRVFDYFETMEPPLFIPMEYGEKLRRLDATQLICGV
Protein: Tudor staphylococcal nuclease (EC 3.1.31.1) (Q8II01)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Apoptosis-related protein
Sequence:
MERLNGIVKQVISADTYVLIGAKKGGVSQERQINLACLQCPRLFMKSQNTEKVEEPLAWESREFIRKMIIGKNVSFCLEYTYNNRQFCSVFYEEQNLGILLLEKGYATLVSNKNVKSSVYADLEPYYVQAKERKVGIFGNNIKSYVRNIVYCYNDKNENKKVYDLFVNRRLKCVVEHIRDGANFRVYAEKEAANEKREVLVSTNNNNNNNNNNNSGEKNKKNKKNKNNNNNNNIDNTELNGMIEEDTGNSKKKMKNKNKKKTNEDENAESNLNPNEKYLTMYYFSFSLCGIIVDMFKKEMVDNEETVKEELYAMETKRFVESRLLNRDIEIEIKHIDNNFNLYANIYYKLGNICTLLLKSGYAYINEYTIKFVPNPIEYKKALDEAIQLRKKKWTNYTEKEIDYEKEYFSRVIEVLYGDVIIIDYKNEERRLYLASIKCEKHNNTDIKLNTLCLMAKDCLKSQIAGEQIKIVTEYVKTPQSNSDGYIPQCSDDKGRMHFVSIYKIQKKKNKNDKNKNHINDDVYDGLTNKWNEKKNTKGNTKRTLAHNNNNNNNNSNNSTSKLNNISKKKNVKKNSKKLNTPLGNNEKGLDYDDTDDDDDEEEEYINLNEELVAKGLAKVLNHRQDDDKASNYFRLQELEKEAEEKKLGRFNPHLEIIKINNISGNENALRARSFENTLNKYNNLNAYVDFIYGANKYKLYIPSQNLLINFILLGITVEKINLKDLNNMELKIKNKNNMNGMENNEKNNILNGDADFEKNNSKKEKLEYKEIAVQAYKYTRKMLMQRMVQISIITCDKGGNFIGLLKYQNKDFSMHLLSLGYGVLNEVGLNNTSERNNFVKAAEEAKIQKKNIWSLEKSEYTDNLLKTENDLTAYDNIYYCSYVEDINNISLQLKNRKEELLTLQRELNKKSNLDSSNLNEINKNTLVLAKYNDNCYYRAIVLQVNKNKKKVLVKYIDFGNEYELDFVDIKKLNEQFNLKNYPPFSFKVSLAGLKIPTENKTDLIIYIKKFLLDKFLYVKFEKKEANLFHVVFYDYEQFNTNKNIKSVNEEIVYNGICYVDNNSDTKIFEKLKKEEILAKKNKHVIWSYGDIDYDDEN
Protein: Protein transport protein sec31 (O13637)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Protein transport protein sec13
- Protein transport protein sec24
- Protein transport protein sec23-1
- COPII coat assembly protein sec16
- Protein transport protein sec23-2
- Small COPII coat GTPase sar1
- Uncharacterized protein C4.03c
- Probable coatomer subunit beta'
- Transport protein particle subunit bet3
- Uncharacterized protein C1259.08
Sequence:
MRLKDISKTATLAWSPRGVNDNQALLALGGYTGTEGSKNSDTLLELWNENPESQKPVGSIDVKTRFYDLAWEKSLDKPMGVIAGSLEDGGIGFWDPAAILKSDEASASIATYKSENGSILGPLDFNRLQPNLLASGDNKGDVWVWDIKHPQQPFALPKQNRSSEVHVVSWNNKVSHILASGNATEYTTVWDVKLKRQVLNLSYLGAAGVSAATGAVNSIAWHPNNATRLATAIDDNRNPIILTWDLRQPTVPQNILTGHQKAALSLSWCPEDPTFLLSSGKDGRAMVWNVETGESLGSFPRSGNWYTKSSWCPSNSNRVAVASLEGKVSIFSIQSTNTDKSQEASIKGATSIDDNEFFNNLPSIAGSQEPSFSLPLAPKWFKVPVGARFGFPNKIVSFSPNSKEVTITSAPDEVEQDEAKSFHSSAKFQTEKEITDFCQKGVEESASEEEAINWKLLMAVSKRASRSKFAELLGYKTLKPKNDEDDSKVDESVAKDSTTPNELSKNANNENYDDDSSFYGKLAESVQEVSIADKKDAEIVKDSFKIFNPEDSDLEKNITEALLTGDVLSAVKACLEEKKISEALFLSTFGGKECRKCVRDAFYELQEHKPSYMRLSACIADNDLQNVVDNAEVSEWKDIFVFICTYATDDEFAPLCSTLGQRLEDLEDEKSIRSAEFCYIASKSLQSYANLWLKQLATSTKTSKAASAYGAYVEQLTKLMDKVSMFRSIVVYKDDELSATKDWKLAGLYEVYIAYAKILSASGKFDDAMSYLNLVPTEFPGAKEEIQRLTMLLEPHAVPPIHQIKQTGYAPVQPKTSQASSILPTVPRTTSYTSPYATTSSHITPADVHPLPPPSTSTTAGWNDAPMLGQLPMRRAAPSMAPVRSPFPGASSAQPAAMSRTSSVSTLPPPPPTASMTASAPAIASPPPPKVGETYHPPTASGTRVPPVQQPSHPNPYTPVAPQSPVAAASRISSSPNMPPSNPYTPIAVASSTVNPAHTYKPHGGSQIVPPPKQPANRVVPLPPTASQRASAYEPPTVSVPSPSALSPSVTPQLPPVSSRLPPVSATRPQIPQPPPVSTALPSSSAVSRPPIATSAGRSSTAASTSAPLTYPAGDRSHIPGNLRPIYEMLNAELQRVSQSLPPQMSRVVHDTEKRLNMLFDRLNSNVLSKPLTDELLALATSLNAHDYQTASNIQTNIVTTLGDQCEHWIVGVTRLITLSKSTT
Protein: 26S proteasome regulatory subunit 7 (26S proteasome AAA-ATPase subunit rpt-1) (Proteasome 26S subunit ATPase 2) (Q18787)
Organism: Caenorhabditis elegans
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 14
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 2
- Proteasome subunit alpha type-2
- 26S proteasome non-ATPase regulatory subunit 7
- Probable 26S proteasome regulatory subunit 10B
- 26S protease regulatory subunit 6A
- Ubiquitin carboxyl-terminal hydrolase 14
Sequence:
MPDHLGDDMRKTKKDDTKEEEKNFQALDEGDIAVLKRYGQGPYAEQLKTLDADIENCLKKVNELSGVKESDTGLAPPALWDIAADKQAMQQEQPLQVARCTKIITSDKHDPRYLINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRNKYQIHLPLPAKIDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAINKVVKGYAKFSATPRYLTHN
Protein: Protein-arginine rhamnosyltransferase (EC 2.4.1.-) (EF-P arginine rhamnosyltransferase) (Q9HZZ1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Protein-arginine rhamnosyltransferase that catalyzes the transfer of a single rhamnose to elongation factor P (EF-P) on 'Lys-32', a modification required for EF-P-dependent rescue of polyproline stalled ribosomes.
Interaction partners:
- Elongation factor P
- FixH family protein
- Dehydrogenase
- Nudix hydrolase domain-containing protein
Sequence:
MASWDIFCSVVDNYGDIGVTWRLARQLAAEHGQAVRLWVDEPQAFARICPRADPVAHVQCLDGVEVRAWGRPWAPVAAADVVIEAFACELPEAHRQAMRERKRPSLWLNLEYLSAEEWIGSCHALPSLQACGLSKYFFFPGFREPSGGLLREAGLLERRRRFQASVSAQDEFLASLGVRRKVGERLISLFAYENPALPGWLEQLRDARQPSLLLVPEGRVLADVADWLRVATLAVGDVHVRDALRVQVLPFMAQDDYDRLLWCCDLNAVRGEDSFVRAQWAGRPLLWHIYRQEEETHLAKLEAFLELYCAGLPADLAENLRTFWLAWNAGGGLAGAWEGLERQLPEWRREAQRWADEQGMRPDLAARLVQFYADWL
Protein: Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-) (Q38AK7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- pyruvate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoamide dehydrogenase, putative
- Citrate synthase
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- 3-methyl-2-oxobutanoate dehydrogenase
Sequence:
MFRRPVAQHIFPVCFARFLTVTPIPMPALSPTMEKGKISEWVKKVGDAVETGDTWCKVETDKAVVSYDNVSEDGFVARILVQVGEEATVGDAVCLIVDEASGVNSDEVKNWQAAGSSPAATQSKVQEVPSPTQVAPLPAGGKEAGGRVKASPLARKTAAELNVSLDTIEGTGGGVGRIVRKDVEAAASKREHAAPAAAPAAKPVVPVIATTPSTQNYTDIPVTNMRSTIAKRLTQSKNVEIPHYYLFEECCAENMMALVQQLNSKGDGKYKITLNDYIIKAVARANMLVPEANSSWQGDFIRQYRTVDVSVAVATPTGLITPIIKDAQARGLVDISNEMKVLAKKAREGTLQPHEFIGGTVSVSNLGASGIPGFTAIINPPQALIVAVGSAKPRPRMSLDPDTGKYTVGAEAEMFVRFTASFDHRVVDGAVASQWCKHFKDAVENPLSLLL
Protein: Nonsense-mediated mRNA decay protein 2 (Up-frameshift suppressor 2) (O13824)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in nonsense-mediated decay of mRNAs containing premature stop codons. It interacts, via its C-terminus, with NAM7/UPF1. Could be involved in determining the efficiency of translational termination or reinitiation or factors involved in the initial assembly of an initiation- and termination-competent mRNP.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11073994}.
Interaction partners:
- Nonsense-mediated mRNA decay protein 3
- ATP-dependent helicase upf1
- Uncharacterized RNA-binding protein C23A1.09
- PWI domain-containing protein C825.05c
- Eukaryotic peptide chain release factor GTP-binding subunit
- Nuclear cap-binding protein subunit 1
- ATP-dependent RNA helicase fal1
- Eukaryotic translation initiation factor 4 gamma
- Uncharacterized serine-rich protein C2F12.03c
- Polyadenylate-binding protein 2
Sequence:
MSREEQIKKLNQYLDNRELAFRAKDGDKNIFHTESQLDSSLKKNTAFMKRCKSSLTSENYDSFIKEIKTLSLKKFIPEITAAIVEGMMKCKATKDILSSVKIVWALNLRFSTAFTGPMLANLYCALYPNPGYSLCHESYFELKQNENEVSEKDRSSHLLKVRPLLRFLIEFWLNGVVGTPEDFVSYLPSTDSNDKKFRKPWFEEQNLKKPLVVLLFNDLMDTRFGFLLLPVLTSLVRTFSCELFTTEDFEDKETLELVNRLNPVVWRTYLRKSLNSYVDKLEVYCQKRKSLFEELNKQYQEQSIIRADPNNEKFQRLANFSKSIESEFSSYASLSEVLNRKASEDLLELNFMEKASSGTNSVFNASGERSESANVETAQVWDDREQYFFYEVFPNFNEGSIAEMKSSIYESSQEGIRSSSENNKKEDDLKDSTGDLNTTQVSSRVDNFLLKLPSMVSLELTNEMALEFYDLNTKASRNRLIKALCTIPRTSSFLVPYYVRLARILSQLSSEFSTSLVDHARHSFKRMIHRKAKHEYDTRLLIVRYISELTKFQLMPFHMVFECYKLCINEFTPFDLEVLALLLESCGRFLLRYPETKLQMQSFLEAIQKKKLASALASQDQLVLENALHFVNPPKRGIIVSKKKSLKEEFLYDLIQIRLKDDNVFPTLLLLRKFDWKDDYQILYNTIMEVWNIKYNSLNALARLLSALYKFHPEFCIHVIDDTLESLFSAVNNSDHVEKQKRLAQARFISELCVIHMLDVRAITNFLFHLLPLEKFESFLTMKASTLTNINNDMFRLRLIVVVLQTCGPSIIRSKTKKTMLTYLLAYQCYFLIQPEMPLDMLYEFEDVIGYVRPSMKVYMHYEEARNALTERLQAISDDWEEDDTRPVFQGANDGDISSNEESVYLPEDISDESETDEESSGLEESDLLDSEDEDIDNEMQLSRELDEEFERLTNESLLTRMHEKNPGFDVPLPLRASSLGSPYVTRNEESASESSHVMFTLLTKRGNKQRSQYLEIPSHSSLVRSTKNQQTEEIMERKRVKEMVLNFE
Protein: Phosphoethanolamine N-methyltransferase 1 (PEAMT-1) (PMT-1) (EC 2.1.1.103) (Methyltransf_25 domain-containing protein) (S-adenosyl-L-methionine:phosphoethanolamine N-methyltransferase) (Q23552)
Organism: Caenorhabditis elegans
Function: Catalyzes the first step in the synthesis of phosphocholine by converting phosphoethanolamine into phospho-monomethylethanolamine (N-methylethanolamine phosphate). Phosphocholine is a precursor for phosphatidylcholine, a major component in membranes and a precursor itself in the production of glycoconjugates secreted by parasitic nematodes to avoid host immune responses.
Interaction partners:
Sequence:
MSTDQQSSVEDQTVAMVNVRRANFKSFWDKYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPSTGRSKAKSMHDTANANPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAEDGAKGTSFNELVELIKNTWQNEQEAWDAKLDDEKYVWTDKVFSSALTSLPSNSTFFLYTPRTVSPYCHINAHTLAETFNANVWNTEIIPEYYRTSLTKSNNLKDQRVRFGWNQSLTDSVTYWQQKDALFDVFVATEFLSTVDDETIRQLPNVMSDGAKFITLEPVDEVNEAEMKQRIQELGYTLKSFTDVTDQCIEAQEQYFKDHEQLRDEKVIRKNWVLLELTH
Protein: Pilin (Pili structural subunit) (P9WI87)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Structural subunit of M.tuberculosis pili (MTP), which are thin (2- to 3-nm wide), flexible, coiled-coil, aggregative fibers. Has a strong affinity for laminin but lacks significant binding affinity for fibronectin or type IV collagen. Mediates adhesion to the extracellular matrix, an event that would facilitate direct interaction with the host epithelium during infection in the lung or other tissues.
Subcellular location: Fimbrium {ECO:0000269|PubMed:17360408}. Note=Part of the pili surface structure.
Interaction partners:
- Uncharacterized protein Rv1824
- Thymidine phosphorylase
Sequence:
MYRFACRTLMLAACILATGVAGLGVGAQSAAQTAPVPDYYWCPGQPFDPAWGPNWDPYTCHDDFHRDSDGPDHSRDYPGPILEGPVLDDPGAAPPPPAAGGGA
Protein: Vacuolar protein sorting 20, isoform A (Vacuolar protein sorting 20, isoform C) (Q9W236)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004608}.
Interaction partners:
- Charged multivesicular body protein 4
- RH72336p
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein-sorting-associated protein 25
- GH14561p
- vesicle-fusing ATPase
- Charged multivesicular body protein 5
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar-sorting protein SNF8
- IST1 homolog
Sequence:
MGALFGKTSKKTAPSRITDQDKAVLQLKQQRDRLKQYQKRIETQLENDRLLARKCLQQGRKDRAKLLLRKKKYQESLLTNADKQLENLEKLAADIEFAQVEMKVLDGLKAGNAALKKVHEMLDIDEVERIMDETREGIEKQQEIDAILTDVLTTQDEEDVLAELDALEAEEEQQKGAQLPDVPTEDLPIPAEIESVEEPAKTKATKKVLVEA
Protein: Cation-transporting ATPase, putative (EC 3.6.3.-) (Q57YG5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MITKNSIIKEIKLLRHRHWSAWPIIWPFVPLYAVIFTLHLNPEIAWDRTTYLVHGTYINFFHAVCIPIVIFFHGLLSLFTIWSVRFRSLVQFHCVPPKEVDTATHVYVCTKEFKGESEIVPLVHASSDHPCCFVFQQRKWKLDAVTEQFVKPRFPTKDNLSMYFAWEGLATTADRSKQLDMFGRNETEVVIPDFQTLLVDHALAPFFVFQMFCVLLWCLDQYWYYSLFTAVMLVAMECTIVMQRIRNMKTLRSMAEVPVRQVTVLRAGREVSVKTTELLPMDLMVVDNNAPCPADVILVRGTCIVNEAMLTGESTPQLKEAIDAANLPLEMKKHARHLLYSGTQLLLSNGPHGQSDTERGRALAVVLKTGFETKQGKLLRTILHSQERASENNGEAFGFIGLLLVFALMASGYLLKRGLEDPNRDRWKLFLACIQIITAVVPPELPMELTLAVNTALLGLVKQNVFCTEPFRIPYAGKVDTCCFDKTGTLTTDEMLFSGVDMADGKGLLNTLKTVPPKAELVLVTCHSLLQLEGTDTVAGDAMEKASLGALGYRVNIDDTVVYDPPAQKEDVKGKSTTGSSKNETSGSSKSQNRKNNSGFEKQYKILVRFPFLANLRRMPCIVSAPDGKYVVAKGSPEAIAQLCESIPPDFHSVANAHAIKGYRVIALAYRPLKEEERSKEAIHNMDREDCEKNLIFAGLAVFQCPLKKDAKDTIEMLQSGSHRCVIITGDSVQTAISVGRDVTILKCRQQLVASSMKKKGNGEDEVDDCIVWTDAATGKEVNLDRRSILAKTFVQTRRHKVPSDDEWDLCVNAESIPTTTLATLIAQYSEHIAVWARCAPTHKEDIVTDLKQKEHMVLMAGDGTNDVGALKQAHAGIAVLNATSMDASQNVGGSGEHNSNEPHNEPDVPKDHKIPPGFKLTVVPPAPSADAPFMEQVRHKMAQARRRAEIVQIARWNKQLEESKKSRKTAEAGKVASQPEMNAPASDFLMESIFNADDADMGGAPQVKLGDASIAAPFTCRSRALTSVCDIVRLGRSTLVTTLQMYKILALNCLTSAYSMSVLQMDGVKHGESQMILSGIILTVCFLCMSKSQPMPTLCPQRPITKVFHPYMMCTIFMQFGLHLYSMVETVRLVEEADAEGVATMRQAGAEGEFKPTLLNSAMFLLTTLIGGVTFAVNYRGEPFMQSIRKNRPMFYSLVVLALAVFYFASEMDPTLNQSFEIVAFPSKEFRERFLQILLMDALGCFVIEGLSLKLLTEYD
Protein: CLIM2 (Q05KH5)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKYPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ
Protein: tRNA-dihydrouridine(47) synthase [NAD(P)(+)] (EC 1.3.1.89) (mRNA-dihydrouridine synthase DUS3) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 3) (Q06053)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs. Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA pseudouridine synthase 1
- tRNA
- tRNA
- Ribosome biogenesis protein ERB1
- tRNA
- tRNA
- Multisite-specific tRNA:
- tRNA
- tRNA
- Multisubstrate pseudouridine synthase 7
Sequence:
MEQNAEKRSIVGDDNSTVKRQDTSPSKGIAHIKPEYIVPLKQNENQKVAIYDEEMSSDRMTNEFAGGTNKKNKNGRGKKRGQNKNRDNRQVKEQNVLCPRLIHGDISKCSFGDNCRFVHDINLYLSTKKPEVESNIFPSCPVFNSLGFCPMGFKCRFLSSHLNKEDNILISKKEIDPDAQTIWSVKGEVNHISPERKLDLIKRRFPFTKSNEILEIIDSFQQECRDSMKPEEEVESTPQLKKQDPDVEQPVAPQVEQRNKELSEHRMKQREVYLKYKDTRYFAQEKKPLDLYHKKIVSPLTTVGNLPYRRLMRKLGADVTYSEMALAVPLIQGTNSEWALPKAHTSEFPGFGVQVACSKAWQAAKAAEALANSVSEISEINLNSGCPIDLLYRQGSGSALLDNPARMIRCLNAMNYVSKDIPITVKIRTGTKEGHPIAEGLVKRLVNETDVAAITLHGRSRQQRYTKSADWDYVSQVADTLRSAEADFIETEQGKEGRDSKNRIQFVGNGDVNNFEDWYRYLNGNENIDSVMVARGALIKPWIFEEVESQQYLDKTSTERLDILRDYAQFSMEHWGTDEYGISQCRRFFCEFMSFFHRYVPMGICERYPVKLNERPPNWCGRDELETLMGSTDVNDWIKLSDLFFGKTDENFVFVPKHKSSSYANRDS