wanglab/gogpt-training-data huggingface dataset:
Protein: Meiotic recombination protein rec11 (Q92380)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Meiotic recombination protein rec8
- Structural maintenance of chromosomes protein 1
- Structural maintenance of chromosomes protein 3
- Cohesin subunit rad21
- Linear element protein rec10
- Sister chromatid cohesion protein pds5
- Sister chromatid cohesion protein mis4
- Cohesin subunit psc3
- Meiotic recombination protein rec12
- Linear element protein Mug20
Sequence:
MRFEFESDASSHLNEVLTELESVELENVEYEGPSLQNVSICASPSEKKRKWGTQDEFSLTENEENNEIETNEEMHVNSHDYAFPQEFFLKLLDIDMPLEQLSQHYFEDYKSNSADFMLTFINFALVASGCQPFVTNFDVQDVDSIPETLSQVNRSSFQKSSCAYTDYLYTSNSKEAKTVRIRFQLFLVEFISKVYVEDAFLGDSFMETTKAWIFTMTTSPWMLVRHTATTICCDIMRCLCLIVNKLSEKSNQTAEILVLRDLTSRFIDMIHDICDSVLFSRIHDIRASIRIVCVTALYDCCQLLPTYLINRNLIRHSGWGLSDAESQIRKISLKIIDYLSSHEPEKDQDFVVDFLDRFSLRIVEICRYDIDSVRSVALKTCEKLMEKISLNGKCINIVSSCIFDGKPQNRISTMRILVAHTNERYANYCEAKTATISLSKLLRREKIPLLVSSFESLFKMNALLFILEQGFESWFRDSSDHIFSRVKDDDKFVYQSQENNFYDADFIREYDMNNHRQQLIEESMHSIHTNSQLLASWEDVAKLLLYDRFDAKDTNSVLNPCIPSNAVIEFSSIYLHYFATHISKRSKKPGKRLEDEVVNQQQAMLRNLPLLLQKYRESCVSSYFFIKCVEQIPDELLYKREFHKDFSKLYKEILDIFNSTTVNFLMILCSRFFHRLAVNKVVQEDILFAIDNVYNDLAESLHEQLNAYIQRKKINKKNQLNGNDETQNLVLALNKFGCFAKEMVCLRDVNDWNIKLSEKLCEICSLEVGPIVCYSSLKVLFLLLLSDMRDRNCIFTNIFLKAAKVAKQKNGNSFLSKVFITITMLTLFLGSKANNWDINFSDDDLKLMNEEEIMEQIETFKAWSMKFKEKSSGNPSYFFSPEDTEEKELWNNLFEDWYPNRARDPGTLSHLVKGLKETADHLS
Protein: Actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit) (p34-ARC) (P85970)
Organism: Rattus norvegicus (Rat)
Function: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the mother actin filament. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19343716}. Cell projection {ECO:0000250|UniProtKB:O15144}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9CVB6}. Nucleus {ECO:0000250|UniProtKB:O15144}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 3
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 5-like protein
- Actin-related protein 2/3 complex subunit 1A
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
Sequence:
MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSISLKFYKELQAHGADELLKRVYGSFLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNCFASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKVFMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNATARDNTINLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITRKTFSST
Protein: Sodium channel protein type 7 subunit alpha (Glial sodium channel alpha subunit) (Na-G) (Nax channel) (Voltage-gated sodium channel-like protein) (SCL-11) (F1LQQ7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q01118}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium channel regulatory subunit beta-1
- Sodium channel regulatory subunit beta-4
- Calcium/calmodulin-dependent protein kinase type II subunit delta
- Sodium channel protein type 5 subunit alpha
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Sodium channel regulatory subunit beta-2
- Sodium channel regulatory subunit beta-3
- Unc-79 homolog, NALCN channel complex subunit
Sequence:
MLTSPEPKGLVPFTAESLELIKNHIAKKCNEEHEEEDLKPSWGLEAGKKLPFAYGTLPQGTVSEPLEDVDPYYYVKRNTFMVLNRNRVIFRFNAVSILCTLSPLSSLRRAVIKVLVHPLFRLLILISVLTDSILMCMSNLPEWILAVENTLLGIYTFEILVKVIARGIWAGSFSFLGDLWNWLDFSVTLFELITRSSPLSSLPMFKTIRTLRILKIIPLNHGLQSIVVTLVQCLKKLLGAIALALFFLTVSSLFGMGLFMGNLKHKCVRWPQEDGNDVMYNGTGSQYHILERENFYYMEGARYALLCGNKTDAGLCPEGYMCVKEGSNPDNGFTSFDNFGWALLAMFRLMTQDYPELLYHQILYASGKIYMIFFVLISFWFAFYMASLFLGILTMAYEQEKQRASEESRDMDSKCHQTVKEFEEEHEGAEMETTQIEMKKRSPTSINTTLDILEDTALGHKEEPETSRKECPLCWYKFTKTCFIWKCSPCWIKLNEFADRIITHPLFDLFLVICIILNICFLALEHFPMSEELMSLLAIGNLVFIGIYTIEMILKIIAMHPYGYFQISWHIFDSILVVLGLTEMLLADIEEITVFILVPLIFIKLGKYAPPFKNLMRILGRALVALKDLVLLVSIFIYFSAVFGMKLFGRSYKDCVCHVDQDCQRQRWHMSDFLHAYVTVFRILCGEWIETLWECMEVAGEAWCIPFYMMVILIGNLLILYLFVALVSSFASYDATTEVSKEAKNLQLAVAWIKMVINCVLLKILCKEKTVSTEATDQTCDPSVKENISGHTLSELSNTQTFLRYKDQSSGTEKTPVTESESQSLIASPSVSETVPIASGESDIENLDNKETRSKSANGSSKEKMKQSSSSECSTVDIAISEEEEMVYEHEKSKLHKNGYERKSSAGQVSRESRNGKIWRNIRKTCCKIVENSWFECFIGLVTLLCTGTLALEDIYIDQRKTIKIFLEYGDMIFAYIFILEMLLKWVAYGFKAYFSNNWYKLDFMVVIVLCLSLIGKTREDLNPLASIKFLRALRVLSQFERMKVVLRALIKTTLPAVSVFLVCLMIWLLFSVMGVFLFAGKFYECIDPTRGERFSVFEVMNKSQCENLVFNESMPWENAKLNFDNVGNGFLSLFQVATFNGWISIMNSAIDSVGVYMQPSFEHSLHMYTYFIIFVVFGLFLPLCMLIGVIIRNFNKQKIKQGGSNIFITVKQKKQYRALKKLLYADSQKPAARPRNKFQGFICDVVTHRVFNVIIILLICFQATTIMIQNDEQSPQIETAVFWMNSLFTMLFTLECILKLTAFRCHYFTSAWNVHDFMVVVFSITGLLLPLSIGQYFVPPSLVQLLLLSRIIHVLRPGKGPKVFHDLMLPLMLSLPALLNIALLIFLVMFIYAIFGMYNFAYVKKEAGINDVSNFETFGSSMLCLFQVTTFSGWDGMLDAIFNSQWSDCDPDKINPGTQVRGDCGSPSVGIFYFVSYILISWLIIVNMYVVLIMEFLSIPSKRKNRTLSEDDFRRFFKVWNRFDPDRTQYIDSTKLSDFAAALDPPLFMAKPNKGQLVAMDLPMAAGDRIHCLDILLAFTKRVMGKDERVEKILSEIESGFMLANPFKITYEPITTTLKRKQEAVSATIIQRAYKSYRLRQSDKKIQDIPEIDDGREDPNSKGVHSGQIEEKASIQTQI
Protein: Dexamethasone-induced Ras-related protein 1 (Q9JKF8)
Organism: Rattus norvegicus (Rat)
Function: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18922798}. Nucleus {ECO:0000269|PubMed:18922798}.
Interaction partners:
- Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein
- Nitric oxide synthase 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
Sequence:
MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLKQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVEQREIEQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGDHGDAFGILAPFARRPSVHSDLMYIREKTSVSSQAKDKERCVIS
Protein: Monocarboxylate transporter 1 (MCT 1) (Solute carrier family 16 member 1) (P53987)
Organism: Rattus norvegicus (Rat)
Function: Bidirectional proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH. The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart. Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 302-Asp is essential for the conformational transition (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11719518, ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:8526936, ECO:0000269|PubMed:9169423}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Basolateral cell membrane {ECO:0000269|PubMed:10564700}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Apical cell membrane {ECO:0000250|UniProtKB:P53985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Note=Expression at the cell surface requires the ancillary proteins BSG and EMB. {ECO:0000250|UniProtKB:P53985}.
Interaction partners:
- Basigin
- Embigin
- L-lactate dehydrogenase A chain
- Sodium-coupled monocarboxylate transporter 1
Sequence:
MPPAIGGPVGYTPPDGGWGWAVVVGAFISIGFSYAFPKSITVFFKEIEIIFSATTSEVSWISSIMLAVMYAGGPISSILVNKYGSRPVMIAGGCLSGCGLIAASFCNTVQELYFCIGVIGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFLSTLAPLNQAFFGIFGWRGSFLILGGLLLNCCVAGSLMRPIGPQQGKVEKLKSKESLQEAGKSDANTDLIGGSPKGEKLSVFQTVNKFLDLSLFTHRGFLLYLSGNVVMFFGLFTPLVFLSNYGKSKHFSSEKSAFLLSILAFVDMVARPSMGLAANTRWIRPRVQYFFAASVVANGVCHLLAPLSTTYVGFCIYAGVFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVILIIAGLYLFIGMGINYRLVAKEQKAEEKKRDGKEDETSTDVDEKPKKTMKETQSPAPLQNSSGDPAEEESPV
Protein: Signal transducer and activator of transcription (A0A669KB68)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
Sequence:
MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV
Protein: Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPAT) (P28173)
Organism: Gallus gallus (Chicken)
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Interaction partners:
- Multifunctional protein ADE2
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional purine biosynthesis protein ATIC
- Uncharacterized protein.
- Trifunctional purine biosynthetic protein adenosine-3
- Adenylosuccinate lyase
- Ribose-phosphate pyrophosphokinase 2
- Pribosyltran_N domain-containing protein.
- Glutamine synthetase
- Glutamine synthetase
Sequence:
MELEELGIREECGVFGCIAAGVWPTELDVPHVITLGLVGLQHRGQESAGIVTSDGESSQAFKVHKGMGLINHVFNADSLKKLYVSNLGIGHTRYSTSGISELQNCQPFVVETLHGKIAVAHNGELTNAVRLRRKLMRHGVGLSTSSDSELITQLLAFTPPLENDDTADWVARIKNLMNETPTSYSLLIMHKDIIYAVRDPYGNRPLCIGRLIPVGDINGKGKDNSETEGWVVSSESCSFLSIGAEYYREVLPGEIVKISRYDVQTLDVVPRPEGDPSAFCIFEYVYFARPDSIFEGQMVYSVRRRCGQQLAIEAPVEADLVSTVPESATPAALGYAQKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRVVIIDDSIVRGNTISPIIKLLRESGAKEVHIRVASPPIRFPCYMGINIPTKEELIANRPEFHDLANYIGADSVVYLSVEGLVSSVQESIKARKENENSLKTQKSRVGKIGHCTACLTGDYPVELEW
Protein: Protein OXIDATIVE STRESS 3 LIKE 2 (AtO3L2) (A0A1I9LQ12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9LVB9}.
Interaction partners:
Sequence:
MFTAIDKIDRTFTVDQEFACLSSSTSSDSIGENSDDDEGGENEIESSYNGPLDMMESLEEALPIKRAISKFYKGKSKSFMSLSETSSLPVKDLTKPENLYSRRRRNLLSHRICSRGGISKKPFKSVLAMSQREGDSSSSGDDSLPTLRQHHKTLTPRLRKGSFGNCVPVVDSPRCFQTAAGRNIHNIIC
Protein: Craniofacial development protein 1 (Bucentaur) (A3KPL8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|RuleBase:RU363092}.
Interaction partners:
- RuvB-like 1
- DNA methyltransferase 1-associated protein 1.
- Helicase SRCAP isoform X2
- RuvB-like 2
- E1A-binding protein p400.
- Zgc:112524
- Actin-related protein 6
- Histone H2A.V
- Histone H2A
- YEATS domain-containing protein 4
Sequence:
MNYSDYDSDGYSSNEDEDYVPSDDNLSEDDINDCVKEDALEGEDHDRQTPENLTKKKKKSKADVHMRKRKKGGLKLVEDGEASTADQQKDEDEPKEDDFVTKSVGDIEERQKKKADDLWASFLSDIPRPKAEVPSASSQKFTSAAATDEPSKLSTASSQKEDKPKDSSKITITKVFDFAGEEVRVTKEVDARSREAKSFLKNEEKLLEDTKEPSVSSEPQPPHPLSSGSSAKRPAGMGSILNRIGAKKQKMSTLEKSKMDWDAFKSEEGITDELAIHNRGKEGYVERKNFLERVDQRQFELEKTVRLNNMKR
Protein: Polycomb protein mes-3 (Maternal-effect sterile protein 3) (Q10665)
Organism: Caenorhabditis elegans
Function: Component of a Polycomb group (PcG) complex. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. In association with the nfya-1-NF-Y complex, may play a role in repressing the expression of the homeobox protein egl-5 in tissues such as the head. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. The mes-2/mes-3/mes-6 complex may participate in the global inactivation of the X chromosomes in germline cells. The complex may act via methylation of histone H3 'Lys-27', rendering chromatin heritably changed in its expressibility. This complex is required to exclude mes-4 from the inactivated X-chromosomes in germline cells.
Subcellular location: Nucleus.
Interaction partners:
- Polycomb protein mes-6
- Histone-lysine N-methyltransferase mes-2
- Histone-lysine N-methyltransferase mes-4
- Probable histone-binding protein lin-53
- Mortality factor related protein 1
Sequence:
MTPATAEVKVGGRKRKNDEPVFIKTKQSRSARREEEKENLLNKSLPSTPTSSEAGSSRESSNPVTSSSRRKNPPTKLENIQKTLPTCSDGLEIRNYVKKYGLPEDNKFLVRNVFDKQLLFGKKYVCRRRVIKSIDEFFPRLKTDAHRENGLYNFCTLQFMKISSWGSSMDEKIYVTSAAIVQSYVIIVDDNDSVTCIENGISVIPMANRTLPSISYNSSNVKNITLTGPELKKAKNVYLAVIVKRKTPKLGENRVGTRGKSTRASFETAASSENFQQLVRFGCTLMYDKDAEINCLNDGVQRIILLDREEKPAYLKIFGKADEPELENAWMNNVKHLEFISDTNYNKEDSHLARLIFSSNTHNYFDRPDISKFSPWQPRSRRTTLKSGISVEPGTSCDEDCGSQYEDTITLKQLLLGTKKLCGRRKRHLTRLTSRWPCFSVDPTKINSYFNETGVTLLENSCSYRPGTQRSIPIKPTRVIRVREETPVSVPIEVITIEDDSDDSPCFSARNRAPGGTRKYGLDFIQSSGHMPYIRYVYMNRANDLVPQLNGEENGKIEGLMEAYPMNNAHMYSDIEFLRKEKLNLPKNAQKYGEMTILDYPLTKTETDEYNKKMSVMNVKDFAVKPRKPIPTVGNTTLSLDLEGCPISTFSEIFFPSGKTELFNILCRHFYSEAGQRPGCFSAQWKSRVLTGFINKYHQYIFDMKLNSLFEKQINLIAMVSPDWKLEDFELPMVRYKQLKKEWKNRQRDIPSSN
Protein: enoyl-CoA hydratase (EC 4.2.1.17) (A0A2R8Y4F5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSKVNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLSQEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYLEEVAITFAKGLADKKISPKRDKGLVETFYFTELTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPAPLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKDVKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSFERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALPISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVKDGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVAEDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLKLPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Protein: Guanine nucleotide-binding protein subunit beta-4 (Transducin beta chain 4) (Q9HAV0)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MSELEQLRQEAEQLRNQIQDARKACNDATLVQITSNMDSVGRIQMRTRRTLRGHLAKIYAMHWGYDSRLLVSASQDGKLIIWDSYTTNKMHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELPGHTGYLSCCRFLDDSQIVTSSGDTTCALWDIETAQQTTTFTGHSGDVMSLSLSPDMRTFVSGACDASSKLWDIRDGMCRQSFTGHVSDINAVSFFPNGYAFATGSDDATCRLFDLRADQELLLYSHDNIICGITSVAFSKSGRLLLAGYDDFNCNVWDTLKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLRIWN
Protein: Uncharacterized protein (Q57Y72)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNLAKKIIVCLFIAILCNVGGVRGFSLVEKKGGYCTKLKATVEELGKRFTDTWNVFEDALHKVENVKENCERFVKLSEEKEVSDAANSDKMKLVNEYYNAIMYNERQISDYEKKIHDLLIGLGKHCGFWLSFTPVSSFLRDITKRHLEEASELISKVESLSENAKSYASHASGEWCSAPATDTQEEVTRSEAEPQSGGDSLQDTTPTVGTRELDRATSTTSSETREEHAGTESAN
Protein: Callose synthase 10 (EC 2.4.1.34) (1,3-beta-glucan synthase) (Protein CHORUS) (Protein GLUCAN SYNTHASE-LIKE 8) (Q9SJM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in sporophytic and gametophytic development. Required for normal plant development and for the proper accumulation of callose at cell plates, cll walls and plasmodesmata. During pollen formation, required for the entry of microspores into mitosis. During plant growth and development, callose is found as a transitory component of the cell plate in dividing cells, is a major component of pollen mother cell walls and pollen tubes, and is found as a structural component of plasmodesmatal canals. Required for proper cell division and tissue patterning throughout plant organs, including stomatal patterning.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Plasmodesmata-located protein 5
- Glucan endo-1,3-beta-glucosidase 10
- Protein EFFECTOR OF TRANSCRIPTION 2
- PLASMODESMATA CALLOSE-BINDING PROTEIN 1
- Maternal effect embryo arrest 18
- Translocon-associated protein subunit alpha
Sequence:
MARVYSNWDRLVRATLRREQLRNTGQGHERVSSGLAGAVPPSLGRATNIDAILQAADEIQSEDPSVARILCEQAYSMAQNLDPNSDGRGVLQFKTGLMSVIKQKLAKRDGASIDRDRDIERLWEFYKLYKRRHRVDDIQKEEQKWRESGTTFSSNVGEILKMRKVFATLRALIEVLEVLSRDADPNGVGRSIRDELGRIKKADATLSAELTPYNIVPLEAQSMTNAIGVFPEVRGAVQAIRYTEHFPRLPVDFEISGQRDADMFDLLEYIFGFQRDNVRNQREHLVLTLSNAQSQLSIPGQNDPKIDENAVNEVFLKVLDNYIKWCKYLRIRVVYNKLEAIDRDRKLFLVSLYFLIWGEAANVRFLPECICYIFHNMAKELDAKLDHGEAVRADSCLTGTDTGSVSFLERIICPIYETISAETVRNNGGKAAHSEWRNYDDFNEYFWTPACFELSWPMKTESRFLSKPKGRKRTAKSSFVEHRTYLHLFRSFIRLWIFMFIMFQSLTIIAFRNEHLNIETFKILLSAGPTYAIMNFIECLLDVVLMYGAYSMARGMAISRLVIRFLWWGLGSAFVVYYYVKVLDERNKPNQNEFFFHLYILVLGCYAAVRLIFGLLVKLPACHALSEMSDQSFFQFFKWIYQERYFVGRGLFENLSDYCRYVAFWLVVLASKFTFAYFLQIKPLVKPTNTIIHLPPFQYSWHDIVSKSNDHALTIVSLWAPVLAIYLMDIHIWYTLLSAIIGGVMGAKARLGEIRTIEMVHKRFESFPEAFAQNLVSPVVKRVPLGQHASQDGQDMNKAYAAMFSPFWNEIIKSLREEDYLSNREMDLLSIPSNTGSLRLVQWPLFLLCSKILVAIDLAMECKETQEVLWRQICDDEYMAYAVQECYYSVEKILNSMVNDEGRRWVERIFLEISNSIEQGSLAITLNLKKLQLVVSRFTALTGLLIRNETPDLAKGAAKAMFDFYEVVTHDLLSHDLREQLDTWNILARARNEGRLFSRIAWPRDPEIIEQVKRLHLLLTVKDAAANVPKNLEARRRLEFFTNSLFMDMPQARPVAEMVPFSVFTPYYSETVLYSSSELRSENEDGISILFYLQKIFPDEWENFLERIGRSESTGDADLQASSTDALELRFWVSYRGQTLARTVRGMMYYRRALMLQSFLERRGLGVDDASLTNMPRGFESSIEARAQADLKFTYVVSCQIYGQQKQQKKPEATDIGLLLQRYEALRVAFIHSEDVGNGDGGSGGKKEFYSKLVKADIHGKDEEIYSIKLPGDPKLGEGKPENQNHAIVFTRGEAIQTIDMNQDNYLEEAIKMRNLLEEFHGKHGIRRPTILGVREHVFTGSVSSLAWFMSNQETSFVTLGQRVLAYPLKVRMHYGHPDVFDRIFHITRGGISKASRVINISEDIYAGFNSTLRQGNITHHEYIQVGKGRDVGLNQIALFEGKVAGGNGEQVLSRDVYRIGQLFDFFRMMSFYFTTVGFYVCTMMTVLTVYVFLYGRVYLAFSGADRAISRVAKLSGNTALDAALNAQFLVQIGIFTAVPMVMGFILELGLLKAIFSFITMQFQLCSVFFTFSLGTRTHYFGRTILHGGAKYRATGRGFVVQHIKFADNYRLYSRSHFVKAFEVALLLIIYIAYGYTDGGASSFVLLTISSWFLVISWLFAPYIFNPSGFEWQKTVEDFEDWVSWLMYKGGVGVKGELSWESWWEEEQAHIQTLRGRILETILSLRFFMFQYGIVYKLDLTRKNTSLALYGYSWVVLVVIVFLFKLFWYSPRKSSNILLALRFLQGVASITFIALIVVAIAMTDLSIPDMFACVLGFIPTGWALLSLAITWKQVLRVLGLWETVREFGRIYDAAMGMLIFSPIALLSWFPFISTFQSRLLFNQAFSRGLEISIILAGNRANVET
Protein: ADP ribosylation factor-like 4, isoform A (AT26185p) (Q9V4B2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGATMVKPLVKNGNILDALPSQATLHVVMLGLDSAGKTTALYRLKFDQYLNTVPTIGFNCEKVQCTLGKAKGVHFLVWDVGGQEKLRPLWRSYTRCTDGILFVIDSVDTERMEEAKMELMRTAKCPDNQGVPVLILANKQDLPNACGAMELEKLLGLNELYNPVPNISMPSSSDSSPTINLIGCRVSNQSITDKSLEEKKESHLHSSMIHIKPALESKDHNSTLSGGALTAFIYPQSHNNSAVLDQKNPQDVKNGFHNKKMNRSSSNSVQFRGWYIQPTCAITGEGLQEGLDALYDMILKRRKINKSNKRNL
Protein: Probable polygalacturonase At1g80170 (PG) (EC 3.2.1.15) (Pectinase At1g80170) (Q94AJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Probable pectinesterase 55
- Probable pectinesterase/pectinesterase inhibitor 16
- Protein STRICTOSIDINE SYNTHASE-LIKE 9
- Probable pectinesterase/pectinesterase inhibitor 32
- Protein trichome birefringence-like 38
- Protein STRICTOSIDINE SYNTHASE-LIKE 4
- Protein STRICTOSIDINE SYNTHASE-LIKE 3
- Arabinogalactan protein 13
- glucan endo-1,3-beta-D-glucosidase
- Pectin acetylesterase 11
Sequence:
MSYSRGGTLVTLLLLLVVASSLALTANANSFESLLQLPRRQSRSTRPRSERLLHVGNFGAKGNGVTDDTKAFADAWKTACSSKVKTRILVPENYTCLLRPIDLSGPCKARLTLQISGTIIAPNDPDVWEGLNRRKWLYFHGLSRLTVEGGGTVNGMGQEWWERSCKHNHSNPCRGAPTALTFHKCKNMRVENLNVIDSQQMHIALTSCRRVTISGLKVIAPATSPNTDGIHISVSRGIVIDNTTVSTGDDCISIVKNSTQISISNIICGPGHGISIGSLGKSKSWEEVRDITVDTAIISDTANGVRIKTWQGGSGLVSKIIFRNIKMNNVSNPIIIDQYYCDSRKPCANQTSAISIENISFVHVRGTSASKEAIKISCSDSSPCRNILLQDIDLEPSNGDGFTESFCWEAYGSSSGQVYPPPCLSDDTSFLEQSVQSGITSAYL
Protein: Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Q5XJN2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P13284}. Lysosome {ECO:0000250|UniProtKB:P13284}.
Interaction partners:
- Alpha-aminoadipic semialdehyde synthase, mitochondrial
- SH2 domain-containing 4A.
- WD repeat-containing protein 90
Sequence:
MFGFNLCVVLVAVFSLSKCSARFVYSCKYPPSQWCSSEDIAAECGVLEQCMKYNSTKAADKVKVSLYYESLCPGCRMFLTSQLVPTLIMLQDIMEIDLVPYGNAQETQAQGKYIFTCQHGEDECLGNMIETCMLNKLGLDAVMVIFCMESGNDVLKSAQPCLGVYRPDVTWDSIMQCVKGDQGNKLMHENAVKTDALNPPHQYVPWITVNGEHTDDLQDKAMGSLFSLVCSLYKGQKPAACTLGLKKNTNNYCMN