wanglab/gogpt-training-data huggingface dataset:
Protein: Scribble planar cell polarity protein (A0A8I6ABB5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLKCIPLWRCNRHVESVDKRHCSLQVVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPVELGGLALLTDLLLSQNLLQRLPEGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLTALPRSLGKLTKLTNLNVDRNHLEVLPPEIGGCVALSVLSLRDNRLAVLPPELAHTAELHVLDVAGNRLRSLPFALTHLNLKALWLAENQAQPMLRFQTEDDAQTGEKVLTCYLLPQQPLPSLEDPGQQSSPSESCSDAPLSRVSVIQFEDPLEGEEDAEEAAAEKRGLQRRATPHPSELKVMKRGIEERRNEAFVCKPDPSPPSPSEEERRLSAESALSGNSVPSASTASDGEPETLPAEVQGLGQQEAMPGQEEYPEEDYNEPTVHFAEDTLIPREDGEGEEGQPEAPWPLPSGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGVQTDREGPTAGWHNGPHTPWAPRAHEEEEEEENRDEEEGEASMEEDDKEEAVASAPSVKGVSFDQANNLLIEPARIEEEELTLTIVRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAAHAGVRVGDKLLEVNGVALQDAEHHEAVEALRGAGAAVQMRVWRERMVEPENAVTITPLRPEDDYSPREWRGGGLRLPLLQPETPVPLRQRHAACLVRSEKGLGFSIAGGKGSTPYRAGDAGIFISRIAEGGAAHRAGTLQVGDRVLSINGVDMTEARHDHAVSLLTAASTTISLLLERETGGAYPPSPPPHSSSTPTATVAATMTTAIPGEPLLPRLSPSLLATALEGPYPVEEICLPRAGGPLGLSIVGGSDHSSHPFGVQDPGVFISKVLPRGLAARCGLRVGDRILAVNGQDVREATHQEAVSALLRPCLELCLLVRRDPPPPGMRELCIQKAPGEKLGISIRGGAKGHAGNPCDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHAEAVQLLRSVGDTLTVLVCDGFDTSTTTALEVSPGVIANPFAAGLGHRNSLESISSIDRELSPEGPGKEKELASQTLPWEPESAETTGRNQEPLKLDYRVLAAVPSAGSLQRPPSPDELPANVKQAYRAFAAVPTVHPPENSATQPPTPGPAASPEQLSFRERQKYFELEVRVPQAEGPPKRVSLVGADDLRKMQEEEARKLQQKRAQMLREEAVTSGPDTGLASDRESLDDEQEAEQPWAGPSHAGGLSPSSPTPLGGSAPVRTAKAERRHQERLRMQSPELPAPERALSPAERRALEAEKRALWRAARMKSLEQDALRAQMVLSKSQEGRGKRGPLERLAEAPSPAPTPSPTPLEDFGLQTSTSPGRLSPDFVEELRTLDPSPSPGPQEEDGEVALVLLGRPSPGTVGPEDMTLCSSRRAMRPGRRGLGPVPS
Protein: Histone H3.1 (P68433)
Organism: Mus musculus (Mouse)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Chromobox protein homolog 5
- Histone H4
- V
- WD repeat-containing protein 5
- DNA
- DNA
- Histone H3.3
- Chromobox protein homolog 3
- Histone-arginine methyltransferase CARM1
- Histone H3.2
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Leucine-rich repeat-containing protein 56 homolog (Q387Y5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Required for the assembly of dynein arms in the distal portion of flagellum axoneme.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:30388400}. Note=Localizes to the distal portion of the flagellum. {ECO:0000269|PubMed:30388400}.
Interaction partners:
Sequence:
MKKSTVLDARPTGPLPRRPQQPSPVEVRNSSQVEKNNARGSWRKLSPLGRQQEEQGGLIHSQSQSLDTSFAPNTNTTLGSTDVNLNSGVRDRPSPRHSIMHRRETRPLLPSNPTDSGVYASEDCGSSSAGFPRFSSMGNIDKSRDNGQLPDGLCTGGSEVTHSSAVHGEAITDELLRRLTRCSDLKSVSSAQFQLDFGTLRCVESISARMPQLNSLKLNNSRITELRVLGTNYANLRRLWISNCLVSSVSGVGACAPVLEELYASFNSISDIDALTEVSSTLQVVDLEGNDIRDTDMLKRTLPQLKKMKHLVLKGNPVASSETIVELSHSSEEKGTRQRKVSYSKLIGHLMPDLQYLDDAEISNTSLQKSARVQKKHHSAHVDPLEICIRDEYLFVQECIRECGFDALGASGADEMHGSCSRSNVSLISSRSHQLKQNRPSYDRNRPSVAVRSLRKNSQSTASSGDSTNQGCDGGKPRPSCQRWGPTQRTSRLFTGRVTSVGAPKARCRQLPPLKETPASPSTEGLGNEPGNDGQRQQESGAMMQLALKPVPPDANSTRGERKQQNTTSPICGLTAAKGNVYAFDVCDDDDDELEKSKESLMHRVRLGNSATSQQATFMGSGTAKSTNSELADSGLSFLLHRLSTCTHPSGADPPDQRNEQQQEQPTTAGATSRCLDDLETPGDGPLESLNGTPEKDWEWRRELMQSVVDIRKMTSEAALKERVQGSKEVDGGGLEKVESEDEEDVSPVVF
Protein: Suppressor of cytokine signaling at 36E, isoform D (Q8INY1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Elongin-C
- Elongin-B
- Cullin-5
- Signal transducer and transcription activator
- Tyrosine-protein kinase hopscotch
- Cytokine receptor
- Cullin-2
- FI03911p
- Unpaired 2
- Suppressor of variegation 2-10, isoform I
Sequence:
MGHHLSKFSARANSQEKRNPTASSSPREAAALVETISLDEEELQVEEILTEATVSAATSPAEVRQIIIKIQLAKMENGNPVAAGQVESFAEVVEQEEEQQRQCADGATDDDAAALSADSLNANGQIVNVTLEGGYGEVGVVTNRTAGSSPEAAKTERQPVNNNGLAGSVGAAISTLQLHDNHGGNANCPLEADDDDDLDESLLRRRRSNSNSRSNIHHHHHHHQQQQQQQHEAEVVEYCEVLESLPVSNMLSAGTQHSSKPVSRSNNSNSCCRSRSSKALSMGAATSSASGSASTSVSTSTSSKRRCCKCKCRDAIRGLRDMLPSSSSSVSNKKDAAAVVAMVPRKSRTADRRSTPPTLGTSSGGSQRRMQSQRIRNSVAVPDASHHHHQLIIRITSPGFVVESPNGGRVTVVTEPAPQSPQTPPRPRPLATVAPAGGAGHAGIGAARNMTVHSQIDFMHCLVPDLEKITNSSFYWGKMDRYEAEHLLEGKPEGTFLLRDSAQEEFLFSVTFRKYGRSLHARIEQSGHKFSFDCHDPCVFTAPTVTGLLEHYKDPACVMFFEPCLTIPLHRRQTFSLQQLSRATIVSNTSYDGINQMELPGRLKSYLKEYHYKQKLRVKPIDQNTPMPYYGNVXREEQQVGFTYYEDVESGSEVDEDDDEGVNIRVSYVQHAEVVAQLQQVTTASGPSAPSSSRSSNLQEHLSRLPNRMAAAFGRMSANLNCYQKTVATPERHSNSS
Protein: Laccase-2 (EC 1.10.3.2) (FpLCC2) (S8FGV1)
Organism: Fomitopsis schrenkii (Brown rot fungus)
Function: In vitro, has activity towards 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), 2,6-dimethoxy-phenol, and guaiacol. Although brown rot fungi preferentially degrade hemicellulose and cellulose, the enzyme may contribute to generating small amounts of lignin breakdown products required for catalytic reactions.
Subcellular location: Secreted {ECO:0000269|PubMed:34116754}.
Interaction partners:
- Nitrate reductase
- Solute carrier family 40 member
- Uncharacterized protein
Sequence:
MLLSSAFVGSCLAILNFAAAVSAQGGLSRTTLNIVNKVISPDGYSRDSVLANGIHPGPLISGNKGDTFQINVNNQLHDNSMNTSTTVHWHGIDQHHTNWADGPAFVTQCPIVPEHSFLYNFTVPDQAGTFWYHSHESVQYCDGLRGPLVVYDPEDPHKDLYDVDDDTTIISLSDWYHSPAHELLPGPIPPNSTLINSLGRPDGSDLPVTIIEVDPTKRYRFRLISMACHPYFDFSIDGHNMTIIEADGSNTEPLSDIDQIRIYPAQRYSFVLEPNQTPGDYWIRAAPLQLGNTSNPDTTTSLGLAILRYTNRSGYAQAASVDPYDISQTPIPVNPLLEQNLHAYGDVPELDEECDDCKLTFDFAFNFTAVDFTVNGTSYVNPTVPVLLQILNGTYTAQELLPHHSVYTLPRNKTIEITMPGAVTGGPHPMHLHGHSFYVIQSMGSDTTNTVNPVLRDTVAVGGATGDNVVIRFRTDNPGPWIMHCHIDFHLALGFAVVLAEAPQDVAEYVSPIPTWDELCPIWDNAPSHN
Protein: G1/S-specific cyclin CLN2 (P20438)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the control of the cell cycle at the G1/S (start) transition. Interacts with the CDC28 protein kinase to form MPF.
Interaction partners:
- Regulatory protein SWI4
- SCF E3 ubiquitin ligase complex F-box protein GRR1
- Cyclin-dependent kinase 1
- G1/S-specific cyclin CLN1
- Regulatory protein SWI6
- G1/S-specific cyclin CLN3
- Protein SIC1
- Protein BCK2
- Transcription factor MBP1
- Cyclin-dependent kinase inhibitor FAR1
Sequence:
MASAEPRPRMGLVINAKPDYYPIELSNAELLSHFEMLQEYHQEISTNVIAQSCKFKPNPKLIDQQPEMNPVETRSNIITFLFELSVVTRVTNGIFFHSVRLYDRYCSKRIVLRDQAKLVVATCLWLAAKTWGGCNHIINNVVIPTGGRFYGPNPRARIPRLSELVHYCGDGQVFDESMFLQMERHILDTLNWNIYEPMINDYVLNVDENCLMQYELYENQVTYDKQCSEKRQSQLSQDSDATVDERPYQNEEEEEEDLKLKIKLINLKKFLIDVSAWQYDLLRYELFEVSHGIFSIINQFTNQDHGPFLMTPMTSESKNGEILSTLMNGIVSIPNSLMEVYKTVNGVLPFINQVKEYHLDLQRKLQIASNLNISRKLTISTPSCSFENSNSTSIPSPASSSQSHTPMRNMSSLSDNSVFSRNMEQSSPITPSMYQFGQQQSNSICGSTVSVNSLVNTNNKQRIYEQITGPNSNNATNDYIDLLNLNESNKENQNPATAHYLNGGPPKTSFINHGMFPSPTGTINSGKSSSASSLISFGMGNTQVI
Protein: Fructose-bisphosphate aldolase B (EC 4.1.2.13) (Liver-type aldolase) (P07341)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}.
Interaction partners:
- Triosephosphate isomerase
- Transketolase
- Uncharacterized protein.
- ATP-dependent 6-phosphofructokinase
- 6-phosphofructokinase
- Glyceraldehyde-3-phosphate dehydrogenase
- FBPase domain-containing protein
- Fructose-bisphosphatase 2
- Glucose-6-phosphate isomerase
- Transaldolase
Sequence:
MTHQFPALSPEQKKALSDIAQRIVASGKGILAADESVGTMGNRLQRINVENTEENRRAFREILFSSDASISKSIGGVILFHETLYQKDSSGKPFPAIIKEKGMVVGIKLDAGTAPLAGTNGETTIQGLDKLAERCAQYKKDGADFGKWRAVLKISSTTPSQLAIQENANTLARYASICQQNGLVPIVEPEVLPDGDHDLQRCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHSCPKKYTPQDVAVATVTTLLRTVPAAVPGICFLSGGQSEEEASLNLNAMNQSPLPKPWKLTFSYGRALQASALAAWLGKSENKKAAQEAFCKRAQINSLACRGQYVTSGKTDTAATQSLFTASYTY
Protein: Neuropeptide F receptor (DmNPFR1) (Q9VNM1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for NPF. Integral part of the sensory system that mediates food signaling, providing the neural basis for the regulation of food response; coordinates larval foraging and social behavior changes during development. Required in dopaminergic (DA) neurons that innervate the mushroom body for satiety to suppress appetitive memory performance; a key factor in the internal state of hunger in the brain. NPF neurons coordinately modulate diverse sensory and motor neurons important for feeding, flight, and locomotion. NPF/NPFR pathway exerts its suppressive effect on larval aversion to diverse stressful stimuli (chemical stress and noxious heat) through attenuation of TRP channel-induced neuronal excitation. NPF neural signaling system plays a physiological role in acute modulation of alcohol sensitivity in adults, rather than a general response to intoxication by sedative agents. Activation and inhibition of the NPF system reduces and enhances ethanol preference, respectively. Sexual experience, the NPF system activity and ethanol consumption are all linked; sexual deprivation is a major contributor to enhanced ethanol preference.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuropeptide F
- Short neuropeptide F
- Proctolin receptor, isoform A
Sequence:
MIISMNQTEPAQLADGEHLSGYASSSNSVRYLDDRHPLDYLDLGTVHALNTTAINTSDLNETGSRPLDPVLIDRFLSNRAVDSPWYHMLISMYGVLIVFGALGNTLVVIAVIRKPIMRTARNLFILNLAISDLLLCLVTMPLTLMEILSKYWPYGSCSILCKTIAMLQALCIFVSTISITAIAFDRYQVIVYPTRDSLQFVGAVTILAGIWALALLLASPLFVYKELINTDTPALLQQIGLQDTIPYCIEDWPSRNGRFYYSIFSLCVQYLVPILIVSVAYFGIYNKLKSRITVVAVQASSAQRKVERGRRMKRTNCLLISIAIIFGVSWLPLNFFNLYADMERSPVTQSMLVRYAICHMIGMSSACSNPLLYGWLNDNFRKEFQELLCRCSDTNVALNGHTTGCNVQAAARRRRKLGAELSKGELKLLGPGGAQSGTAGGEGGLAATDFMTGHHEGGLRSAITESVALTDHNPVPSEVTKLMPR
Protein: Putative pectinesterase/pectinesterase inhibitor 43 [Includes: Pectinesterase inhibitor 43 (Pectin methylesterase inhibitor 43); Pectinesterase 43 (PE 43) (EC 3.1.1.11) (Pectin methylesterase 43) (AtPME43)] (O23447)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Pectin lyase-like superfamily protein
- Mannan endo-1,4-beta-mannosidase 1
- Protein IQ-DOMAIN 14
- Mannan endo-1,4-beta-mannosidase 2
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- UDP-glycosyltransferase 88A1
Sequence:
MNKYVLLGVTALIMAMVICVEANDGNSPSRKMEEVHRESKLMITKTTVSIICASTDYKQDCTTSLATVRSPDPRNLIRSAFDLAIISIRSGIDRGMIDLKSRADADMHTREALNTCRELMDDAIDDLRKTRDKFRGFLFTRLSDFVEDLCVWLSGSITYQQTCIDGFEGIDSEAAVMMERVMRKGQHLTSNGLAIAANLDKLLKAFRIPFPFLRSRRGRLGILGSGSSRDESVGSSQDSPPNEDSSDDSPSTVDSSENQPVDSSSENQSSDSSNNRPLDSSKNQQMESSEDTPKKSAFSGNQPLDDSSDKLPQKSTSSENQPLDSSENPPQKSTSSENRPLDPLRKLNPLNKLDSLKDRHLSEEGEFPPWVTPHSRRLLARRPRNNGIKANVVVAKDGSGKCKTIAQALAMVPMKNTKKFVIHIKEGVYKEKVEVTKKMLHVMFVGDGPTKTVITGDIAFLPDQVGTYRTASVAVNGDYFMAKDIGFENTAGAARHQAVALRVSADFAVFFNCHMNGYQDTLYVHTHRQFYRNCRVSGTIDFVFGDAKAVFQNCEFVIRRPMEHQQCIVTAQGRKDRRETTGIVIHNSRITGDASYLPVKAKNRAFLGRPWKEFSRTIIMNTEIDDVIDPEGWLKWNETFALNTLFYTEYRNRGRGSGQGRRVRWRGIKRISDRAAREFAPGNFLRGNTWIPQTRIPYNAN
Protein: U3 snoRNA-associated protein UTP11, putative (Q387X5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- DDB1- and CUL4-associated factor 13
- CCAAT-binding factor domain-containing protein
- Nop14-like protein
- Nucleolar RNA binding protein, putative
- U3 small nucleolar ribonucleoprotein protein MPP10, putative
- Periodic tryptophan protein 2, putative
- Sas10 C-terminal domain-containing protein
- U3 small nucleolar RNA-associated protein 14
- Bms1-type G domain-containing protein
- PIN domain-containing protein
Sequence:
MTKGKGRNPGMGNLDKHVKRKVHKERSQPAARKHLGPLEKHKDHVVRSRRRKAKVQRLLELKRAAAQRNPDEFHINMTKTVLDVESGKMRRRRLSKEDNRKKMEKTLRHNTRNLHYLKYKAHADWSRAKELIEEDALGALTAAPPKNKHIIFAEDEDEYHHFNPLKQLDATPEMLKQHPAVRGRLSVLRETVLPEEILLSGYRMLSTAQKRKERREIQRKLQKSGLKSEEERAEFVKRLHAKKEVKMHRFSSLVANALESTDAEAEGEDADDPCDVDRLLEYKKIKEKEEALLAASRVKEIQQRVHRSKKLDTLARAIKKQNDGIRCSLENKRNARFKPNSKRRAR
Protein: Sll0314 protein (Q55648)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Sll0350 protein
- Slr0217 protein
- Slr1194 protein
- Thylakoid membrane protein slr0575
- Slr1273 protein
- Slr1122 protein
- Ssl3829 protein
- Slr0287 protein
- Slr1546 protein
- Slr0872 protein
Sequence:
MLVFLTRFTPMNLIRNRWAQIFTQSILGVLIAGGTAWAGDPFRPNNPHNIGDQTEAAFEAIFRDGNYRGAEEILAGAIQAEPNEPLVYAMQASFAYDANDMEGMRKYAQQTLESAQRLAPSDPLRGNLYIAVGHFLEGSYLLKKGSYLQAVGKTGTVFEHLDKASAINPNDPELNLLRGYLDLFLSRYTPFSQSEQVISRFEQYAAPDYLRYRALATTYRDLEKYDLAMANIDRALAITPDNPELQYLKGQFLRNEGRRSMDLGKLQQAQQYYAMALQKQDQLSRALVVQLNHENNAVVDEIQKLAQNPSLKGF
Protein: Glycerol-3-phosphate dehydrogenase [NAD(+)] 2 (EC 1.1.1.8) (Q6FWJ7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Glycerol-3-phosphate dehydrogenase
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Glycerol-3-phosphate dehydrogenase [NAD
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
Sequence:
MFVRLARIPRITRHYRLGLFSTQPKPKPNEYLYYRNKHKSKMEAPIKRSSSAVSLVELEREPFKVTVIGSGNWGTTIAKVVAENTKANPQVFQERVDMWVFDENIDGTMLTEIINTKHQNVKYLPNIDLPENLVANPDLLKSVEGADILVFNIPHQFLPKIVDQLRGHVEPHVRAISCLKGFEVGKKGVQLLSTYITEELGIECGALSGANLAPEVAKEHWSETTVAYHIPKDYQGDGMDVDHKVLKLLFHRPYFHVSVIDDVAGISIAGALKNVVALGCGFVEGLGWGNNAAAAIQRVGLGEIIKFGQMFFPESRVETYYQESAGVADLITTCSGGRNVRVATHMAKTGKSAEDSEKELLNGQSAQGVITCKEVHEWLSTCEMIEEFPLFEAVYKIVYEDVPMHKLPEMIEELDDIVVAGQ
Protein: Uncharacterized protein (Q5AUE4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MKLTAAVVTGLLATSTSAAFDKWAPWGKRDYSCINAYSGPTENSTLTTGTPLEIKFNRNSGRCDSLNDYPTGNYSLWLHNNPVRNMGFVNSDYQVKIQDGISSDATSVTFTLPDDLPEVADDTVWYLRLDTYLPTAPQMPSLFNALGPFRIVQ
Protein: Vacuolar protein sorting-associated protein 9A (AtVPS9a) (Q9LT31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as guanine nucleotide exchange factor (GEF) for Rab small GTPases. Activates specifically RABF1, RABF2A and RABF2B proteins. Required for early stages of embryogenesis, cytokinesis, embryogenesis, and organ development. Is essential for the establishment or maintenance of the polar localization of the auxin efflux carrier PIN1.
Interaction partners:
- Ras-related protein RABF2b
- Ras-related protein RABF1
- Ras-related protein RABF2a
- Vesicle-associated membrane protein 727
- Guanosine nucleotide diphosphate dissociation inhibitor At5g09550
- Brefeldin A-inhibited guanine nucleotide-exchange protein 5
- Vacuolar protein sorting-associated protein 29
- Ras-related protein RABG3b
- Ras-related protein RABA1b
- Vacuolar fusion protein CCZ1 homolog A
Sequence:
MENTDVFLGLHDFLERMRKPSAGDFVKSIKSFIVSFSNNAPDPEKDCAMVQEFFSKMEAAFRAHPLWSGCSEEELDSAGDGLEKYVMTKLFTRVFASNTEEVIADEKLFQKMSLVQQFISPENLDIQPTFQNESSWLLAQKELQKINMYKAPRDKLVCILNCCKVINNLLLNASIASNENAPGADEFLPVLIYVTIKANPPQLHSNLLYIQRYRRESKLVGEAAYFFTNILSAESFISNIDAKSISLDEAEFEKNMESARARISGLDSQTYQTGHGSAPPPRDESTLQKTQSLNPKRENTLFQSKSSDSLSGTNELLNINSETPMKKAESISDLENKGATLLKDTEPSKVFQEYPYIFASAGDLRIGDVEGLLNSYKQLVFKYVCLTKGLGDGTSLAPSSSPLQASSGFNTSKESEDHRRSSSDVQMTKETDRSVDDLIRALHGEGEDVNNLSDVKHEEYGAMLVEGKDEERDSKVQGEVDAKDIELMKQIPKREGDNSSSRPAEDEDVGSKQPVTEASE
Protein: Carbonic anhydrase (EC 4.2.1.1) (A0A8I6A5P9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPHCSLHATVVLLLVILKEQPSSSAPLNGKSLLGPAGEKNWSKKYPSCGGLLQSPIDLHSDILQYDASLAPLQFQGYNVSVEKLLNLTNDGHSVRLNLNSDMYIQGLQPHQYRAEQLHLHWGNRNDPHGSEHTVSGKHFAAELHIVHYNSDLYSDFGSASDKSEGLAVLAVLIEIGSVNPSYDKIFSHLQHVKYKGQQVLIPGFNIEELLPESPGEYYRYEGSLTTPPCYPTVLWTVFRNPVQISQEQLLALETALYFTHMDDPSPREMVNNFRQVQKFDERLVYISFRQGLLTDTGLSLGIILSVALAGVLGISIVLAVSVWLFKRKKSKKGDNKGVIYKPAIKKEAEVHA
Protein: FMN-dependent NADH:quinone oxidoreductase 2 (EC 1.6.5.-) (Azo-dye reductase 2) (FMN-dependent NADH-azo compound oxidoreductase 2) (FMN-dependent NADH-azoreductase 2) (EC 1.7.1.17) (Q9I2E2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Reduces both benzoquinones and naphthoquinones efficiently.
Interaction partners:
- Probable NAD
- Probable nitroreductase
- NAD
- FMN reductase
Sequence:
MKLLHIDSSILGDASASRQLSAELVQAWRQNEDGLDVTYRDLAADAVAHFSALTLAAGSTPAELRDAALKHEVAVGEEVLEEFLAADVVVIGAPMYNFTISSQLKAWIDRIAVAGKTFRYTENGPVGLAGDKKVVIVSTAGGVHAGQPTGAAHEGYLRTVLGFFGITDIEVVRAEGLAYGEEPRTQAIAAARRQIAGQFAAA
Protein: Transmembrane protein 201 (Spindle-associated membrane protein 1) (A2A8U2)
Organism: Mus musculus (Mouse)
Function: Involved in nuclear movement during fibroblast polarization and migration. May recruit Ran GTPase to the nuclear periphery (By similarity).
Subcellular location: [Isoform 2]: Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5SNT2}. Note=The C-terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle (By similarity). {ECO:0000250|UniProtKB:Q5SNT2}.
Interaction partners:
- SUN domain-containing protein 1
- SUN domain-containing protein 2
- Prelamin-A/C
- Emerin
Sequence:
MEGVSALLASCPTAGLAGGLGVTACAAAGVVLYRIARRVKPTHTMVNCWFCNHDTLVPYGNRNCWDCPHCEQYNGFQENGDYNKPIPAQYMEHLNHVVSSVPSPRDPAQPQQWVSSQVLLCRRCSHHQTTKIKQLAAFTPREEGRYDEEIEVYRHHLEQMYKLCRPCQAAVEYYIKHQNRQLRALLLSHQFRRREADQAHGQSFSSSAVKAPFQVILLRALAFLACAFLLFTTLYGPSEPFTPGAALPPALPPGGNSSAASDNTTSQAEGWQQLLGLLPEHATEKLHEAWAFGQSHQTSIVAVGLLTCLLAMLLAGRIRLRRIDAFSTCLWALLLGLHLAEHYLQAASPGWLDTLKFSTTSLCCLVGFTAAVATRKSTGPRRFRPRRYFSGDSASLFPSSPSLAVPYPSVTSSPASLFIPTPPGFLPLTKQQLFRSPRRVSPSSLPGRLSRALSLGTIPPLTRTDSGYLFSGSRPPSRVSPAGEVSLSDYFSLLSSSFPASPLPSPAPSVASSVASSSGSLRHRRPLISPARLNLKGQKLLLFSSPGEAPNTPSSSEEFSPPNGSLFIESPQLPQRNHTRDTKHTMEMRSMLARDSARSSHSIKKEDESSQSSTCVVDTTTKGCSEETTPWKARVSPSLVRGLLAVSLAVNALFTSAYLYQSLR
Protein: Trans-Golgi network integral membrane protein 1 (TGN38A) (Q62313)
Organism: Mus musculus (Mouse)
Function: May be involved in regulating membrane traffic to and from trans-Golgi network.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes (By similarity). {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit alpha-2
- Vesicle-associated membrane protein 4
- AP-2 complex subunit beta
- AP-1 complex subunit mu-2
- AP-1 complex subunit beta-1
- AP-1 complex subunit gamma-1
- Syntaxin-6
- Golgin subfamily A member 1
- AP-2 complex subunit sigma
Sequence:
MRFQVALLLLSVAVARALPSVYKRDADSGDSQNPPNQPSKQSSTPLPSSNQVKTTRPTDGQGQKSDKKDQDKTTLAAVSSKAESGPRTAATDHSLGDSRRQPEKTDAELNETARPLSPVNPKLEKSDQSSTEDSGKPTGGNSGKPTGGDSGKPTEAGSNKATEDDSGKSTKVDLDKPTSKISPDTETSKTDKVQPTEKGQKPTLTSKTESGETLAGDSDFSLKPEKGDKSSEPTEDVETKEIEEGDTEPEEGSPLEEENEKVPGPSSSENQEGTLTDSMKNEKDDLYKDSSGNTSAESSHFFAYLVTAAVLVAVLYIAYHNKRKIIAFALEGKRSKVTRRPKASDYQRLNLKL
Protein: Pyridoxal 5'-phosphate synthase subunit PdxT (EC 4.3.3.6) (Pdx2) (Pyridoxal 5'-phosphate synthase glutaminase subunit) (EC 3.5.1.2) (P9WII7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit PdxS
- Pyridoxine 5'-phosphate oxidase
- Probable acyl-CoA thioesterase II TesB2
- Probable transcriptional regulatory protein Rv2603c
- Ribokinase
- Transaldolase
- Transketolase
- Ribose-phosphate pyrophosphokinase
- Probable phosphoglucomutase PgmA
- Ribose-5-phosphate isomerase B
Sequence:
MSVPRVGVLALQGDTREHLAALRECGAEPMTVRRRDELDAVDALVIPGGESTTMSHLLLDLDLLGPLRARLADGLPAYGSCAGMILLASEILDAGAAGRQALPLRAMNMTVRRNAFGSQVDSFEGDIEFAGLDDPVRAVFIRAPWVERVGDGVQVLARAAGHIVAVRQGAVLATAFHPEMTGDRRIHQLFVDIVTSAA
Protein: Fanconi-associated nuclease (EC 3.1.4.1) (Q38AL0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU365033}.
Interaction partners:
- Mismatch repair protein MLH1
- Crossover junction endonuclease MUS81
- DNA repair protein, putative
- Structure-specific endonuclease subunit SLX1 homolog
- asparagine--tRNA ligase
Sequence:
MTGDVCPSSRDLERALSLPMVEAFHVSAWYVLQYYEKAIDSSDLLSLRGLITLSLNNLCRSEEAADGIEAFELLLRMALRDAKWLRVRCIETQYSCFIRVASALEELNITPIAKYVISDTRSEGEQLVRVLDGKAIFRPPLGCREEIREILRTARVHELQQLDRCVRYEDGPPSHNHSAVHYTLAGNHSYGGESITGVQTAGRSSWNAKGCSSRLLPEKEDLIDRILSVSDEEGQLASAWDRTVGPICCVHQLFRDSILKISELIHEVTAPSIRDDICKYPGSAPAGCRSSDTTILKIVSKLMLRQSSDLRGPWMLWPQACRIVGGESSGGVVPLLASSPKALVSFREAIELCQRLCELRHAKTLKQCSADIVLEYHSTIEKKLALLDSRPLTADDCADETARRKRTYSVTTSADVSDGCALSVEELLHHGGLLYEHLLHFLPKYRWFACAELLVPLLQAHKRWDLVNMWLRKLLDEPVYVVSTSFGTPTFPMYYRYEKRGKWWNLLAQGHAHLGDKEGAFQLLEKRQSAWREQDSPQRYLRMERAEELPVSIQRRARLLCALFRVGRGRNSGSQKAVALYNAVGEHHRLHFYRRSDRIAIERTLLSLQSFLRRWTPTSPNLSSFTAHMLSAPETTIPGDKDHSDATFWGDTKPSTGCFSAEKCVLRWFGLPKVHESGDGTCRPSSWTGLHCKGRWVNYLGRLLLWDAFHFDPDALPRGNESMTGSVPEFVWLSPVQETPLDLETSSISFQQRRRHIIEKSLRFFERCSRDVLIYYVRQRCVSENSGACEDNSKQKSNSSSLKEPLHANDVGADFISGDENFVPLGQPVRSPNSQEKDGPTASFIPAEQLLDPEEFPLFDLLQAVPQGALCALLRCLYLPPPEDGYSVHFDSFPDLVLWREVPSQPDGYEFKLVEVLGPNESLSEKQISTIDTLLRCKFDVTVAHVTDVDEGKKKSNRSKGRHDGTEHGRGRNRQDGAHPPV