wanglab/gogpt-training-data huggingface dataset:
Protein: CCR4-NOT transcription complex subunit 4, isoform K (M9PB92)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CCR4-NOT transcription complex subunit 3
- poly
- CCR4-NOT transcription complex subunit 9
- Not1, isoform H
- Regulator of gene activity
- Protein associated with topo II related - 1, isoform A
- ATP-dependent RNA helicase me31b
- CCR4-NOT transcription complex subunit 11
- poly
- CCR4-NOT transcription complex subunit 10
Sequence:
MNGLSSNDDAVECPLCMEPLEVDDLTFFPCTCGYQICRFCWHRIRTDENKLCPACRKEYPENPADFKPLSQEEMIAFKSQKRQRDQQRKQKITENRKHLANVRVVQKNLVFVVGLPPRLADADILKKHEYFGKYGKIHKVVINPSTTYAGVQVRVGPSASAYVTYVNNSDALRAIQSVNNIMIDGRLIKTSLGTTKYCSHFMKNQQCPKGDCMYLHELGDPEASFTKEEMHQGKHLEYEKRLHDTLIASLGPNATGIVNGNGASKANVAIPSSSSASSSSSGSGTNGSSASGNAQQKEAWPSLSVSPINGKEAAATATSSSGKSKREKLRNEKRHEKNKAKNKNGSNTNANASNKENYVPETRSSTSTETFAEATADAPASTKAEPPQASSNRTRADRGKDRTTASAKEQKKSKEAAPAPAASKPAERVETSESTIRQKKAEVTESCEDNLPQKRLAGTNVQRSVSSCSENSEGHVSESSLSEKSLTGDYVEEKCNSVNSESQQESVKFQEELEKSNEAIVEAETILPTAESSEDISPAAVAPGNGEVEGCLPVVDPVEPPSLADNGSRVTDALSKLNIFDDTPSFFTSPSFQQAPILKNKLDLEMRQSHLPDLVNDIDGIQKASNTNEWEEAFKNVMMGNTQHMEEQLLQQQHLQQHQNLRHQLVLQQEEFLRMQELQKRNNFATQINGPANDFLRAYELRAQANAIIQQQLLQQHAGENLFGGNMSKFFDFHKSQPQSHHQYLNGHPPQINGNGAVPEPQRVAASLESNRLNSPFVENGLINSQQQQQQQQQQQKQRMMGMYEFMPPNTQSQQNRFTQNSIVDDDLGFDPFVETQKGLAELMENEVVQKQSINNENPLPKLPPQPQVPPHPQLVDNLQRARMPPPGFNHVNTLGLGGASRLQLTSKIIPFMNMPVNGVGNSGAQGQHQMPMGVNWNAPMGMHQNPGQPVGDSQLQHPMAHNKVYNNSDWTSMDPAILSFRQYSSFPQNQIPPHPQQQQDLFLQHLAQQQNSQSGGFNNQAQQMLPMGMPNSLLNGQQTQPPQVNANVQGMLEFLKSRQFV
Protein: Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase (EC 4.2.1.134) (H3BS72)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363109}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363109}.
Interaction partners:
Sequence:
MENQVLTPHVYWAQRHRELYLRVELSDVQGLTLLPRLECSSVIIAHRSLELLGLSSPPGSAYQVGLQNPAISITENVLHFKAQGHGAKGDNVYEFHLEFLDLVKPEPVYKLTQRQVNITVQKKVSQWWERLTKQEKRPLFLAPDFDRWLDESDAEMELRAKEEERLNKLRLESEGSPETLTNLRKGYLFMYNLVQFLGFSWIFVNLTVRFCILGKESFYDTFHTVADMMYFCQMLAVVETINAAIGVTTSPVLPSLIQLLGRNFILFIIFGTMEEMQNKAVVFFVFYLWSAIEIFRYSFYMLTCIDMDWKVLTWLRYTLWIPLYPLGCLAEAVSVIQSIPIFNETGRFSFTLPYPVKIKVRFSFFLQIYLIMIFLGLYINFRHLYKQRRRRYGQKKKKIH
Protein: Protein RTA1 (P53047)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in 7-aminocholesterol resistance.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Citrinin resistance protein, mitochondrial
Sequence:
MAKDGFELYRYTPELGASILFTVLFAVSGVAFVILLFHYSVKSKRRVGSLMKSQPVLRYYGTVNLAGAYIPFIFGCFVECVGFAFRCKSSKDTTLLNPYIIQTVFLLVSPTLYAASIYMIFGRMATLLFAENLMIMPARFNTTIFVIGDVGSLLLQAIGGAMMSKVTSASSGSHLVTAGLFIQIAFFGLFIINEVLFIFKMSKKPTNVSVRYGSWKYLNIALLVNSFLILIRSIVRAVEFIQGYDGEIASHEWYLYIFDGLPMFLLVLIFIVAFPLINIFRIHEESIQAQQSARFDGTDYPDVEVTSIEEDLASKSE
Protein: Vacuolar protein sorting-associated protein 39 homolog (Q1ZXS5)
Organism: Caenorhabditis elegans
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways (By similarity). Believed to act in part as a component of the putative HOPS endosomal tethering complex which is proposed to be involved in the rab-5-to-rab-7 endosome conversion probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to rab-7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes (By similarity). Required for fusion of endosomes (By similarity). In association with lgg-2 mediates the tethering of autophagosomes with lysosomes to form autolysosomes. Within the HOPS complex, contributes to the normal development of gut granules in embryonic and adult intestinal cells.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96JC1}. Lysosome membrane {ECO:0000250|UniProtKB:Q96JC1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96JC1}. Late endosome membrane {ECO:0000250|UniProtKB:Q96JC1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96JC1}. Late endosome {ECO:0000250|UniProtKB:Q96JC1}. Lysosome {ECO:0000250|UniProtKB:Q96JC1}.
Interaction partners:
- Vps8 domain-containing protein
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 33A
- Vacuolar fusion protein CCZ1 homolog
- V-SNARE coiled-coil homology domain-containing protein
- Ras-related protein Rab-7a
- t-SNARE coiled-coil homology domain-containing protein
Sequence:
MYDAYTPCEVALRLPVEVTCLAFQESNQTLLAGGRAGHLYAYTISANRRGFELTNICKSFHKKAVMELKVCQREDLLLCVSDGQLMAHKLSDPEYKVETLIHKVKPVQTFARFSPKTSGDLYVIVSSRKKLYLFKWGEKDGHKEFIEVALDYNPVFLDTPTSIRCVGEMVFFSVRNEYFSMTMQKDKTTTSPSEGSTPEGWNGFVTRLLNFNCQPGIVPMIDRRRVAFVRNEIVVTTDIWGQRPANVLSDEYKFSEVPMQIVYDSPYLVGMLSKGRVEVRSIFDGQLVQTMSLPKAMTLCSGARGQVFVAALSDIWILDTSQNLRKNVSHLIQERHFELAIQLAENSNLFAEEQKLEIKKKAALNLFNQKKFDESFALFGEIKTDISEVLSIIRMFPELLPDGFQSMTGVVSDMPANDRMRALLALGSYLSEIRTEHAKHIELYNRLYSSGAAKKTDEDEKAKLLLTLRVVDTTLLKCYIKTKPMLVDSLIRLQSNACTFEDAKKILESEGRLRSLFILYETRKKHEMALDLFIDQSSRPDADPFFDDAIQQIVEYLQSLGNSNLPLILKYAKWVLAKNLEAGVQIFTSDETEMARNLNRKAVVEFLKSECPDALIPYLEHVIFKWEEPSSYFHETLLEFYVARVNTLFKDYVHAFPDAFSDENITRAGDEDGELGLYRKRLLKFLEVSHSYSPQTVLLQLAPHAFYEERALILGRLKQHEQALAIYVNTLKNVPAAEEYCRLYYNAHDETNSQVYLMLFRTLVHPNQQQLHSIPYHADSTPFGSYRDDVSEASTLVNSTSSYQPDVNTAIKILAKHADKIDTVGALNMLPATTPLRVVFSAINAVIQTTGRQASTRKMEKSVSQCAMSKKLERKNKAQSTKIIVNFSSECVVCEKKIAVSAFVRYPDGRLAHLYCHNDSQGGNRN
Protein: Oleosin H2 (Oleosin 15.5 kDa) (O04925)
Organism: Sesamum indicum (Oriental sesame) (Sesamum orientale)
Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Subcellular location: Lipid droplet {ECO:0000255|RuleBase:RU000540, ECO:0000269|PubMed:12450125, ECO:0000269|PubMed:9399587}. Membrane {ECO:0000255|RuleBase:RU000540}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU000540}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}.
Interaction partners:
Sequence:
MADEPHDQRPTDVIKSYLPEKGPSTSQVLAVVTLFPLGAVLLCLAGLILTGTIIGLAVATPLFVIFSPILVPAALTIALAVTGFLTSGAFGITALSSISWLLNYVRRMRGSLPEQLDHARRRVQETVGQKTREAGQRSQDVIRP
Protein: Protein SCAR3 (AtSCAR3) (Protein WAVE2) (Q9LP46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. Regulates trichome branch positioning and expansion.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Protein BRICK 1
- Protein SCAR4
- Protein SCAR1
- Microtubule-associated protein 70-4
- Protein SCAR2
- Protein ABIL1
- Transcription initiation factor IIF subunit alpha
- Protein SPIRRIG
- Zinc finger protein GIS
Sequence:
MPRNVYGMNQSEVYRNVDREDPKAILNGVAVTGLVGVLRQLGDLAEFAAEIFHGIQEEVMATASRSNQLKIRLQHIEATVPPLEKAMLAQTTHIHFAYTGGLEWHPRIPITQNHLIYDDLPHIIMDPYEECRGPPRLHLLDKFDINGPGSCLKRYSDPTYFRRASSNLSQGNKKFQKDKKHCKMKKKKTSSRSRDMSRLASLANQNARKTFASFSFSGQTSSTKTTSTSDMEKRYDFQDHHSRSFESRSGSGYNECLSTATSSLKTGERPKGVFVSSSLTPGSCTIASVLSECETEDAHDNFQFSPSQGQAARGSSCVSWDEKAEIVESLGLQTDEASEMVEANSVVDTLDEKPSYGEGIGGVDFHSKDNENDKSESGLRKRAGIDEVREIKNGREIVGEPRDSEQETESEGECFVDALNTIESESENNQGLQTSQVSSSCGVADERLEKSVCEQETEQNSYSVEDSCRSMDGLMANSFKNEENASSENVSVEMHQQNLQAGSDINRLQKNDLCANKDMRNDSGGKDTITFTFVPGLENSLVDSSNPLIHHGLQENQETEAESSGDLEAFKIWTNGGLLGLKPSKPPVLAMPSSLSPDCKTEERTVGFAEAEKDKADDLVENASHRHVLNNSSLATPGTQNPGSSNGIVMGIVDQRESHETSSGVFGLSHKFLTSGFRRKDSFAHDRKTVPATIPENDEVTTERRRFCDQDINEKTFMDPFRDEAPIDWITSSPPLQHMKISLNPADTLQASRLKLKFSDGDNTYNTFSSFQLLPETGTSLPDSYSDDDTFCRSSPYMSDTDYLSDNHSLSNSEPWEESSDSHGRKEQELYDSFHESRHVDNNAEASPLGIKSESSCVAVNLSYLQNPAEPLPPPFPPMQWMVSKTPSEKMEDKTQSLQLQEALRFAFEKHISLPTAKNELPSMVTSAPKPEIKAHLKNNVREEKQSANAKETETGDFLQQIRTQQFNLRPVVMTTTSSATATTDPIINTKISAILEKANSIRQAVASKDGDESDTWSDT
Protein: Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain] (P00742)
Organism: Homo sapiens (Human)
Function: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
Subcellular location: Secreted.
Interaction partners:
- Prothrombin
- Tissue factor pathway inhibitor
- Tissue factor
- Antithrombin-III
- Coagulation factor VIII
- Coagulation factor V
- Coagulation factor VII
- von Willebrand factor
- Endothelial protein C receptor
- Coagulation factor IX
Sequence:
MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK
Protein: Soluble inorganic pyrophosphatase 5 (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase 5) (PPase 5) (O82597)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q93V56}.
Interaction partners:
- Putative ATPase, plasma membrane-like
- ATP synthase subunit b, chloroplastic
- Pyrophosphate-energized vacuolar membrane proton pump 1
- ATPase 6, plasma membrane-type
- ATPase 9, plasma membrane-type
- ATPase 8, plasma membrane-type
- ATPase 11, plasma membrane-type
- ATPase 4, plasma membrane-type
- ATPase 7, plasma membrane-type
- V-type proton ATPase subunit c''1
Sequence:
MNGEEVKTSQPQKKLQNPTPRLNERILSSLSKRSVAAHPWHDLEIGPGAPVIFNVVIEISKGSKVKYELDKKTGLIKVDRILYSSVVYPHNYGFVPRTLCEDNDPIDVLVIMQEPVLPGCFLRARAIGLMPMIDQGEKDDKIIAVCVDDPEYKHITNINELPPHRLSEIRRFFEDYKKNENKEVAVNDFLQPGPAIEAIQYSMDLYAEYILHTLRR
Protein: N-acetyl-D-glucosamine kinase (N-acetylglucosamine kinase) (EC 2.7.1.59) (GlcNAc kinase) (Muramyl dipeptide kinase) (EC 2.7.1.-) (N-acetyl-D-mannosamine kinase) (EC 2.7.1.60) (Q9UJ70)
Organism: Homo sapiens (Human)
Function: Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity.
Interaction partners:
- N-acetylglucosamine-6-phosphate deacetylase
- Glucosamine 6-phosphate N-acetyltransferase
- Phosphoacetylglucosamine mutase
- N-acylglucosamine 2-epimerase
- Beta-hexosaminidase subunit beta
- Beta-hexosaminidase subunit alpha
- Chitotriosidase-1
- Acidic mammalian chitinase
- N-acetylglucosamine-6-phosphate deacetylase
- Glucosamine-6-phosphate deaminase 1
Sequence:
MAAIYGGVEGGGTRSEVLLVSEDGKILAEADGLSTNHWLIGTDKCVERINEMVNRAKRKAGVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGGVVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGYVKQAMFHYFQVPDRLGILTHLYRDFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTQGREIQAQNFFSSFTLMKLRHSSALGGASLGARHIGHLLPMDYSANAIAFYSYTFS
Protein: O-acyltransferase (F1MIW3)
Organism: Bos taurus (Bovine)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}.
Interaction partners:
Sequence:
MGDRGGAGGSRRRRTGSRPSIQGGSGPAAAEEEVRDVGAGGDAPVRDTDKDGDVDVGSGHWDLRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPALCLVIVANIFAVAAFQVEKRLAVGALTEQAGLLLHGVNLATILCFPAAVAFLLESITPVGSVLALMVYTILFLKLFSYRDVNLWCRERRAGAKAKAALAGKAANGGAAQRTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRLLEMLFLTQLQVGLIQQWMVPAIQNSMKPFKDMDYSRIVERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESITYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWAARTAVFLASAFFHEYLVSIPLRMFRLWAFTGMMAQIPLAWIVGRFFRGNYGNAAVWLSLIIGQPVAVLMYVHDYYVLNREAPAAGT
Protein: Atrophin-1 (Dentatorubral-pallidoluysian atrophy protein homolog) (O35126)
Organism: Mus musculus (Mouse)
Function: Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats (By similarity). Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P54258}. Cell junction {ECO:0000250|UniProtKB:P54258}. Nucleus {ECO:0000250|UniProtKB:P54258}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells. Colocalizes with MTG8 in discrete nuclear dots (By similarity). {ECO:0000250|UniProtKB:P54258}.
Interaction partners:
- Nuclear receptor subfamily 2 group E member 1
- Angiotensinogen
- Ataxin-1
- Ataxin-3
- Ataxin-2
- Ataxin-7
Sequence:
MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGGAAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLNNASASPPGMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSSSSSAAASSSSSSSSASQYPASQALPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANNNTHPGPFPPTGGQSTAHPAAPTHHHHQQQPQQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHGQVSYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGASYPFPPVPPVTTSSATLSTVIATVASSPAGYKTASPPGPPQYSKRAPSPGSYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYEPPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL
Protein: DNA nucleotidylexotransferase (EC 2.7.7.31) (A0A8I6AFP2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR000817}.
Interaction partners:
Sequence:
MDPLQAVHLGPRKKRPRQTGASGASTPHDIRFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSEFELLDISWLIECMGAGKPVEMAGRHQLVVRRNPSLSPVPGSQTVPPPPMQKISQYACQRRTTLNNHNQLFTDAFDILAENYEFRENEVSCLPFMRAASVLKSLSFPIVSMKDIEGIPCLGDKVKCVIEGIIEDGESSEVKAVLNDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIKSDKSLRFTHMQKAGFLYYEDLVSCVNRAEAEAVSMLVKEAVVAFLPDALVTMTGGFRRGKMTGHDVDFLITSPEATEEEEQQLLHKVTNFWRQQGLLLYCDIIESTFEKFKLPSRKVDALDHFQKCFLILKLHRGLVRSEESGQQEGKDWKAIRVDLVMCPYERRAFALLGWTGSRQFERDLRRYATHERKMMLDNHALYDKTKTVTVSPLYGKMSKPQEALRVFLEAESEEEIFAHLGLDYIEPWERNA
Protein: Serine/threonine kinase 38 like (F5GY51)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAMTAGTTTTFPMSNHTRERVTVAKLTLENFYSNLILQHEERETRQKKLEVAMEEEGLADEEKKLRRSQHARKETEFLRLKRTRLGLDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKSDMLEKEQ
Protein: L-tryptophan--pyruvate aminotransferase 1 (EC 2.6.1.27) (EC 2.6.1.99) (Protein CYTOKININ INDUCED ROOT CURLING 1) (Protein SHADE AVOIDANCE 3) (Protein TRANSPORT INHIBITOR RESPONSE 2) (Protein TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS 1) (Protein WEAK ETHYLENE INSENSITIVE 8) (Tryptophan transaminase) (Q9S7N2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: L-tryptophan aminotransferase involved in auxin (IAA) biosynthesis. Can convert L-tryptophan and pyruvate to indole-3-pyruvic acid (IPA) and alanine. Catalyzes the first step in IPA branch of the auxin biosynthetic pathway. Required for auxin production to initiate multiple change in growth in response to environmental and developmental cues. It is also active with phenylalanine, tyrosine, leucine, alanine, methionine and glutamine. Both TAA1 and TAR2 are required for maintaining proper auxin levels in roots, while TAA1, TAR1 and TAR2 are required for proper embryo patterning. Involved in the maintenance of the root stem cell niches and required for shade avoidance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18394996}.
Interaction partners:
- Tryptophan N-monooxygenase 1
- Aromatic aminotransferase ISS1
- Probable indole-3-pyruvate monooxygenase YUCCA1
- Tryptophan N-monooxygenase 2
- Probable indole-3-pyruvate monooxygenase YUCCA8
- Probable indole-3-pyruvate monooxygenase YUCCA4
- Indole-3-pyruvate monooxygenase YUCCA2
- Probable indole-3-pyruvate monooxygenase YUCCA5
- Probable indole-3-pyruvate monooxygenase YUCCA3
- Indole-3-pyruvate monooxygenase YUCCA6
Sequence:
MVKLENSRKPEKISNKNIPMSDFVVNLDHGDPTAYEEYWRKMGDRCTVTIRGCDLMSYFSDMTNLCWFLEPELEDAIKDLHGVVGNAATEDRYIVVGTGSTQLCQAAVHALSSLARSQPVSVVAAAPFYSTYVEETTYVRSGMYKWEGDAWGFDKKGPYIELVTSPNNPDGTIRETVVNRPDDDEAKVIHDFAYYWPHYTPITRRQDHDIMLFTFSKITGHAGSRIGWALVKDKEVAKKMVEYIIVNSIGVSKESQVRTAKILNVLKETCKSESESENFFKYGREMMKNRWEKLREVVKESDAFTLPKYPEAFCNYFGKSLESYPAFAWLGTKEETDLVSELRRHKVMSRAGERCGSDKKHVRVSMLSREDVFNVFLERLANMKLIKSIDL
Protein: Polyadenylate-binding protein 1-A (PABP-1-A) (Poly(A)-binding protein, cytoplasmic 1-A) (Q54BM2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Polyadenylate-binding protein 1-B
- Eukaryotic peptide chain release factor GTP-binding subunit
- PAN2-PAN3 deadenylation complex subunit pan3
- PAN2-PAN3 deadenylation complex catalytic subunit PAN2
- Eukaryotic translation initiation factor 4 gamma
- Nuclear cap-binding protein subunit 2
- Uncharacterized protein
- Eukaryotic translation initiation factor 4E
- Myb domain-containing protein
- Ataxin-2 homolog
Sequence:
MATNFTPISSSLYVGDLLPEVSEQHLFEIFNQVGLVSNIRVCRDTNTRRSLSYAYVNYYNGADAERALDTLNNTPIRGKACRIMWSQRDPSLRKSGVGNVFIKNLDKGIDHKALYDTFSAFGNILSCKVVTDDGNSSKGFGFVHYETQESADKAIAKVNGMMINGQKVFVGPFKSSKERGQPTEVKFTNVFFKNLSEDVGPDQLKELLQQYGEITNITIMADDKGKSKGFGFANFESAEAAKNVVENENGKIFHGKPIYAGRAQKKIEREAELKHTFETKYQGVNLYIKNIDDSIDNDKLREVFSQFGTITSAIVMKDDKATTSKGFGFVCYTAPDEATRAVTEMNGRMIGTKPLYVALAQRKDIRRAQLEMQHQQKFKTGIRQQMPPTYGSGPVFFTPAPVNPQVVYQQMMPRPRNWNGQPVGVPQGQYANMNYARGQPRQNGPRQNGGQPRQNGPRPDVSGAQPIPVQQQTTLDVAQTQQAASSAESALNLQSIINLPSRDQQNVALGEHLYPLIHNSQPDLAGKITGMLLDSLPVEELFTLTQRQDLLADKIREALEVLGSN
Protein: Folylpolyglutamate synthase (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (Tetrahydrofolylpolyglutamate synthase) (A0A8I6AA44)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MMKSTRCLPVSWPVAEKFWWDLAMEWKGLPSACEAKTASFQDAVRTLNTLQTNASCLEEVKRQRSDPQAQLEAMEVYLARSGLQVEDLNQLKIIHVTGTKGKGSTCAFTERILRNYGLKTGFFSSPHLVQVRERIRINGKPISPELFTKYFWHLYQQLEEFKDDSHISMPSYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAFDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIAWQKGGIFKPGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPPLEALEQVGLPLSLGLEGEHQRHNAALALQLARCWLEQQNYHDIQELKASKPSIRWQLPLAPVFRPTPHMRRGLRDTEWPGRTQVLQRGPVTWYLDGAHTTSSVQACVHWYCQSLERSRRTDGGHEVHILLFNSTGDRDSAALLKLLQPCHFDYAVFCPNVTEISSIGNADQQNFTVTLDQVLLRCLQHQKHWNCLAEKQASSNLWGSCGPESARPGSLLLAPHPPQPTSTSSLVFSCISHALQWISQGRDPIFQPESPPRNLLNHPTANSGASILREAAAIHVLVTGSLHLVGGALRLLDPSMSQ
Protein: Bidirectional sugar transporter SWEET3 (AtSWEET3) (Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 3) (Q6NQN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8L9J7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8L9J7}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 2B
Sequence:
MGDKLRLSIGILGNGASLLLYTAPIVTFSRVFKKKSTEEFSCFPYVMTLFNCLIYTWYGLPIVSHLWENLPLVTINGVGILLESIFIFIYFYYASPKEKIKVGVTFVPVIVGFGLTTAISALVFDDHRHRKSFVGSVGLVASISMYGSPLVVMKKVIETRSVEYMPFYLSFFSFLASSLWLAYGLLSHDLFLASPNMVATPLGILQLILYFKYKNKKDLAPTTMVITKRNDHDDKNKATLEFVVDVDRNSDTNEKNSNNASSI
Protein: Pinin, isoform A (RE29832p) (Q9VH84)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVNDSGLSTVDDLEQKLNSAKQSLVILNENIRRIAGRVPKESLQRSEKFKYTQDGKKNEHNGDRPFPRNATPGGVFKDKRRMYESKNPISRFPIEENEGRPPRINSRVIREMPTKKEIVEAQGTDSESRARNRRMFGSLLGTLQKFCQEESRLKSKEDKKAEIDRKVEKQELQERAMLRKQRETLFLDRKKKQFEIRRLEYKMARMKDFKVWEATMLNAKNNIRTKTKPHLFFRPKVHSPRTEKLLSKSKSEADVFIEFRREELEVELKNLENMNFGKMEDDTAIDESFYEEPDDEEQLDKCK
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform E) (Q9VHC4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004283}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004283}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004283}.
Interaction partners:
Sequence:
MTVDFNDYFWGEKNNGYDVLYHNMKFGLIASKELSEFLREKSNIEEQNSKMMSKLAHKAGTLNSTFAPVWTILRTSAEKLSTLHLQMVQKLTELVKDVAKYADELHKKHKSVKEEESQTLECVQAIQTSTVAVQKLRDLYASKVQELEKLRKDNGSHKDAEKLESKLKKLQEEYKALLDKHNPIKNEFERRMTQTCKRFQEIEEVHLRQMKEFLSTYLEMLQNNHDMVGQVHSDFKRQFVDMSVDKLLEQFVLNKYTGLEKPEMPELEYVALSSGSRLQQPQVSASASNSNSATSIQAALRAGNAATTASGSAVSMDQRGDALAAISLGSGSAASGSIPFAEDPILGAMGSPRPTSPDMLAGANASGIQSQPTGGATSTVKSLRSWFLPTAKQQPSAGAGNFGMAGSGSTNNTTTTTTASNNSNNLNTNNTTATTTTTTGTNNLTTNITKNSPNSEDTSNQVSGILRSRRDKTKTKKAKKKKDNEAAENIQEERLTSLDRGNNTLLDYDDHGRSMKTQNSSGSSAGGGLAALSVTSAQGSVDSAGASSMGGSGGAAVASGSLPNAGALTNSASITAPGAASGTGTGYEVDEEGFSIQPAKEIAWEEGQDKSGSFYSDSDTDSDNDKQERRIHVSIKPLKNGQAPMSASVDELRATVENISLSPTGVFSHHSQQLQAARGAPASRQQSPEISNASTPTASVHPYAPLQSPTLSNNNNANNTTNSRYADLGDIFSELGDMSMSAPSSATLGKPPGRQIPTPTSASTGGSIAIPRPPSRRSDMIAIGPAATGTAPGRGRMSPAPVTAMNRAESIGSLEFRTAIGGVGSSRGPSPLTIGISDTIPLAVAFHEIIHAYFRGSDESRCQVKVSGDMMLSFPAGIAGLLANNPNPAKLGFRIKHVQNLENLVPNGKLVQIDRQQSSSVSTMLEFNMGALTALLRRQAENNPTASYFNVDILKYQVRTKPGASSCPFQLVSYWKCESSYTALKVDYKYNNHAMASASPLLNVTLSVPVNGSVRNVQSKPHSAWLGESNRLVWNFTDISQNSQDGGVGTLRARLELNDGPSTPALLATQFNCEGTTLSGIEFELQGSGYRLSLVKRRFVSGKYVCEGDGIRSGATPTPPSVGSTSPYSAKSN
Protein: Alpha-ketoglutarate dehydrogenase subunit 4, mitochondrial (alpha-KGDH subunit 4) (2-oxoglutarate dehydrogenase complex component 4) (OGDHC subunit 4) (P19955)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:25165143}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
Sequence:
MIATPIRLAKSAYEPMIKFVGTRHPLVKHATEVVVHPCATNGMLPGSKECIPVSKFMENYKPFRVVPIKHSANAGLSSSKTSVFVNRPLQKDELASIFELPARFRYKPINEHELESINSGGAW
Protein: Bruno 3, isoform M (M9MS39)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVHIIELVGQPKVEFAQQVTMNRALQLKPAENESRSGCAFVKFGSQQEAQSAITNLHGSQTMPGASSSLVVKYADTEKERQIRRMQQMAGHMNLLNPFVFNQFSPYGAYAQQQQQAALMAAAATAPGSAAAYMNPMAALATQIPHGLNGTGQPPSLPSPTMPNFNMGANTPNGQPGGAAAAAAAAAAADGVFTNGIPQTAFPGPTELFVADPLHLTIPPQGLPNGDAATLQHAFPGLPPFPGVAFPAVYGQFPQALPPPLAAVAPTQREDFLMFPGCSISGPEGCNLFIYHLPQEFGDAELMQMFLPFGNVISSKVFIDRATNQSKCFGFVSFDNPASAQAAIQAMNGFQIGMKRLKVQLKRPKDASRPY