wanglab/gogpt-training-data huggingface dataset:
Protein: Kinetoplast ribosomal PPR-repeat containing protein 3 (Q4GZA2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Ribosomal protein L9 domain-containing protein
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL29m
- Mitochondrial carrier protein, putative
- 50S ribosomal protein L13, putative
- Ribosomal protein L11, putative
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein mL43
Sequence:
MRPLRCSFGRRHRVTSAAFGVSQFPSSSSTFSASCRWVVIPPVEPITSASASASSSSSSSRKGECRTSYRFAVKDEERGLYDHGVTPDARTLAAEAEAQYRASSEFLHAPAGGLPAPELHMEVDGTSVSCIAAPFGEEYVPSSKERFAHRGHVGDLSRQRTSDRKYLLDARSHLNIRKERQLSELLSAPMPLLQKSNEIQQMLLSDFYPQNLVVSSRNVEAVIALWAQCSLEQCIAGLNSQRPENLLAPSADTTCHEVDAVDSVPFLNHMKRLYFHSRQTHVAPTPLVLEYVMTALGNVTTADSRVFHLANRLLLDADKYVILPTRTTYAAFFTICSLHNAMPFALSRFKDAVVNLHVAVDATMASAILEGLVQNGLVEEAVLLLARLQHVPMDVQLLNTALEVLLLSKQPQSCFSAFEAVRHSGVEPTADTYTLLLLACERSGLWGNTTAILADMQMRRVKGDGRTLNLLLKGLLTERLHGYSRQLYETMVNKNVEVWPALESHMKSRTAGGEQLKRGSTIKTSKSSQPS
Protein: L-lactate dehydrogenase A-like 6B (EC 1.1.1.27) (Q9BYZ2)
Organism: Homo sapiens (Human)
Interaction partners:
- Pyruvate kinase PKLR
- Putative aspartate aminotransferase, cytoplasmic 2
- Pyruvate kinase PKM
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Probable D-lactate dehydrogenase, mitochondrial
- Pyruvate carboxylase, mitochondrial
- NADP-dependent malic enzyme, mitochondrial
- NADP-dependent malic enzyme
- NAD-dependent malic enzyme, mitochondrial
Sequence:
MSWTVPVVRASQRVSSVGANFLCLGMALCPRQATRIPLNGTWLFTPVSKMATVKSELIERFTSEKPVHHSKVSIIGTGSVGMACAISILLKGLSDELALVDLDEDKLKGETMDLQHGSPFTKMPNIVCSKDYFVTANSNLVIITAGARQEKGETRLNLVQRNVAIFKLMISSIVQYSPHCKLIIVSNPVDILTYVAWKLSAFPKNRIIGSGCNLDTARFRFLIGQKLGIHSESCHGWILGEHGDSSVPVWSGVNIAGVPLKDLNSDIGTDKDPEQWKNVHKEVTATAYEIIKMKGYTSWAIGLSVADLTESILKNLRRIHPVSTIIKGLYGIDEEVFLSIPCILGENGITNLIKIKLTPEEEAHLKKSAKTLWEIQNKLKL
Protein: Ornithine aminotransferase (PfOAT) (EC 2.6.1.13) (Ornithine--oxo-acid aminotransferase) (Q6LFH8)
Organism: Plasmodium falciparum (isolate 3D7)
Function: The enzyme has a very narrow substrate specificity and can only catalyze the transamination of alpha-ketoglutarate with ornithine or N-acetylornithine and, to a lesser extent, of glutamate-5-semialdehyde with glutamate and alanine.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Arginase
- Pyrroline-5-carboxylate reductase, putative
- S-adenosylmethionine decarboxylase/ornithine decarboxylase
- Delta-aminolevulinic acid dehydratase
- Glutamate dehydrogenase, putative
- asparagine synthase
- Asparagine synthase
- Glutamate dehydrogenase
- Glutamate dehydrogenase
- DNA-directed RNA polymerase subunit
Sequence:
MDFVKELKSSQDYMNNELTYGAHNYDPIPVVLKRGKGVFVYDIEDRRYYDFLSAYSSVNQGHCHPDILNAMINQAKKLTICSRAFFSDSLGVCERYLTNLFGYDKVLMMNTGAEASETAYKLCRKWGYEVKKIPENSAKIIVCNNNFSGRTLGCVSASTDKKCKNNFGPFVPNFLKVPYDDLEALEKELQDPNVCAFIVEPVQGEAGVIVPSDSYFPGVASLCKKYNVLFVADEVQTGLGRTGKLLCTHHYGVKPDVILLGKALSGGHYPISAILANDDVMLVLKPGEHGSTYGGNPLAAAICVEALKVLINEKLCENADKLGAPFLQNLKEQLKDSKVVREVRGKGLLCAIEFKNDLVNVWDICLKFKENGLITRSVHDKTVRLTPPLCITKEQLDECTEIIVKTVKFFDDNL
Protein: Amidophosphoribosyltransferase 1, chloroplastic (AtATase1) (PRPP1) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase 1) (AtGPRAT1) (Q9SI61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the first committed step of 'de novo' purine biosynthesis from glutamine. Involved in plastid biogenesis and cell division.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:15266056}.
Interaction partners:
- Phosphoribosylamine--glycine ligase, chloroplastic
- Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
- Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- Glutamine synthetase cytosolic isozyme 1-3
- Glutamine synthetase cytosolic isozyme 1-5
- Glutamine synthetase cytosolic isozyme 1-4
- Glutamine synthetase, chloroplastic/mitochondrial
- Glutamine synthetase cytosolic isozyme 1-2
Sequence:
MAATTSFSSSLSLITKPNNSSYTNQPLPLFPKPFLKPPHLSLLPSPLSSPPPSLIHGVSSYFSSPSPSEDNSHTPFDYHNDEDDEKPREECGVVGIYGDPEASRLCYLALHALQHRGQEGAGIVTVSPEKVLQTITGVGLVSEVFNESKLDQLPGEFAIGHVRYSTAGASMLKNVQPFVAGYRFGSIGVAHNGNLVNYKTLRAMLEENGSIFNTSSDTEVVLHLIAISKARPFFMRIIDACEKLQGAYSMVFVTEDKLVAVRDPYGFRPLVMGRRSNGAVVFASETCALDLIEATYEREVYPGEVLVVDKDGVKSQCLMPKFEPKQCIFEHIYFSLPNSIVFGRSVYESRHVFGEILATESPVECDVVIAVPDSGVVAALGYAAKSGVPFQQGLIRSHYVGRTFIEPSQKIRDFGVKLKLSPVRGVLEGKRVVVVDDSIVRGTTSSKIVRLLREAGAKEVHMRIASPPIVASCYYGVDTPSSEELISNRLSVEEINEFIGSDSLAFLSFDTLKKHLGKDSKSFCYACFTGDYPVKPTEVKVKRGGGDFIDDGLVGSFENIEAGWVR
Protein: Uncharacterized protein ycf73 (ORF249) (Q37066)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MTKDETLLVFTLVVSSVSVFLFGILLFMVLISATRDFRERTKSKLVKIMIWAGIVVITFAIAVRIYPIFIFLLKERIKPLVEALYDKLPWIWEVSLSRYWDRLIDFLDRYLWACAQRIQTGIRKQKGEFVVTFSCRVKKRLYARAIEVGIHLSLLSNLFWILKTTLAVGYRLLWVLYYIISFEGFLGSFRLYLVYFGFYCLLFSGKWLRTSEDRGERQAQISGILLRGMLIECAFSVLCLEEDSNLHAL
Protein: Farnesyl diphosphate synthase (Q9KWR7)
Organism: Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Interaction partners:
Sequence:
MFSERLKEVQDGVEAAMAAAIGRLPAGDLRDAMAYAAQGGKRLRAFLAIESAAIHGISMEQAMPAALAVEALHAYSLVHDDMPCMDNDDLRRGLPTVHRKWDEATAVLAGDALQTLAFELCTDPVLGSAENRVALVAALAQASGAEGMVYGQALDIAAETAAVPLTLDEIIRLQAGKTGALISFAAQAGAIIAGADRALLAAYATALGLAFQIADDILDVEGDEEAAGKRLGKDAEAHKATFVSLLGLPGAKARAADLVAEAEAALAPYGEAAATLRACARYVIERDK
Protein: Phosphoinositol dihydroceramide synthase (PI-DHC synthase) (Q8A7K2)
Organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Function: Catalyzes the addition of a phosphorylinositol group onto dihydroceramide to form phosphoinositol dihydroceramide (PI-DHC), an essential step in sphingolipid biosynthesis.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylinositol phosphate synthase
- GtrA/DPMS transmembrane domain-containing protein
- Putative phosphatidylinositol-3-phosphatase
- Inositol-3-phosphate synthase 1
- Membrane protein
- TonB-dependent Receptor Plug Domain
Sequence:
MPSKKETLTVIVIMALFLLLTAACIGLRSEHLLMAALYLVLFFAGLPTRKLAVALLPFAIFGISYDWMRICPNYEVNPIDVAGLYNLEKSLFGVMDNGVLVTPCEYFAVHHWAVADVFAGIFYLCWVPVPILFGLCLYFKKERKTYLRFALVFLFVNLIGFAGYYIHPAAPPWYAINYGFEPILNTPGNVAGLGRFDEIFGVTIFDSIYGRNANVFAAVPSLHAAYMVVALVYAIIGKCRWYVIALFSVIMAGIWGTAIYSCHHYIIDVLLGISCALLGWLFFEYGLMKIRGFRNFFDRYYQYIK
Protein: phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC 3.1.3.95) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Q9W1Q6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
Sequence:
MDEIKLAKVENVRMIDRYNTKNPTVGTLYLTATHLIFVEPDSNKETWILHMHVASIEKLPLSTTGSPLLIRCKTFLSVTFVIPKDSECHDVYTSLLKLFQPVSINKLYCFNYQPNKDDFPKNAGWDYFKLEAEFKHMLVPNEAWTLCSMNEKYELCDTYPRQIYVPKEATTLMLISSSRFRSKGRLPVLTYLHNNKASICRCSQPLSGFSARCLEDEQMLEAIRKTNSNTDYMYVVDTRPRINAMANRAAGKGYENEAFYENIKFHFLGIENIHVQRASLQKVLEACEQKSPTMSAFINALESSGWLKHIRSILDTSSFIANAVDKGVSVVVHCSDGWDRTAQVCSLAQLMLNPYYRTIKGFQALIEKDWLAFGHKFSERCGHIQTDAREVSPIFTQFLDCTWQLMSQRSEAFEFNERFLLILHDHVHSCQFGTFVGNCEKDRLDLKLAERTFSLWGYMANHLNEYINPLYKPNVDEAIKANLAPQCIKFWRGMYSRFESGIHPREPLGDVLLDSKEHCNSLEDHVQHLTKRIASFKNYISKSAKKLQDATSAPGKVNKELSSNEINDNKYNYDKKLSELSAADDDHPLKASNMSFASLSLSAEQSSPPQALPEEINSVAVDWKPMRNVTTCSCSTPFDQFSKKTHCWRCGDIFCERCIDKNVALPGHDSGKPVPVCRGCFRQMQKQSP
Protein: NUBP iron-sulfur cluster assembly factor, mitochondrial (F8W061)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRGLPKQKPIEGVKQVIVVASGKGGVGKSTTAVNLALALAANDSSKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPLLNYGIACMSMGFLVEESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMP
Protein: RNA helicase (EC 3.6.4.13) (Q9W4W2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable RNA helicase armi
- Protein vreteno
- Splicing factor 3A subunit 2
- Splicing factor 3B subunit 4
- PHD finger-like domain-containing protein 5A
- LD45152p
- Splicing factor 3B subunit 1
- LD21442p
- Inactive peptidyl-prolyl cis-trans isomerase shutdown
- Splicing factor 3B subunit 5
Sequence:
MEPIGDLQVPSFKVVSGGTTFTYASPKSGAASLDFLAHTLRKREANTEKTILICQQNFEAERLKFELAERDVNTILLPPHGAMVGQVLLLWSKGYINQALILCDGMLEHLGVVEANLVIHTTLPELNKFEERLKWLSISARNAEMLVITPCDEENEKEGKGETEPEIVQQRMPLKVDALNSMQLYEIKENTPPTSSEDYKAEADVLLSAATPATIPNDNKEQEINLSVEDATVKLLASFELGSTDSAAVDESSPAAAKFNAPVYSPFVTENPTKSLDAEFQELVKSFKVQNVFKNMNLPPPPSVSIEEPVSSASASDYRHQIDTTSLDSIRTVKDSPASLAVVPFSAGGITYNNYGVLGWSRHAVVPCYGLTEAPDISTIIRRAMQQMGVARSRARAVQRFAWPHVSLGKSVLVVGNLQIGKTWSYLPTVCQRSHEDLQRRPDVGRGPTCIFVCPNQGQGKQIERWMSTLLCLLGSASGFEDVVTHWDKTQLVDIVRRLKKPVGILLTSVDLLLQLLNHNPVGSIFDAQAVKCIALDNLNDMVRVLPNDTMKLLQRLPEMFQLTQNKCQLLVSGRIWHTDLMVQHILPLMPDVLVLFDDALEASVYGGVQLDVRVVADEPEKIEHLKALIAERRNFANEPAVMVCSNSTEVLLLRRSLQAIGVNAHICVSEACYSNVAEWLRQSPSGLLLVTDDVVPRLKCGKIPLLIHYSFASMWARFKNRFSLFYANLKSPTTRPVGQSVVFAKPTDLENIWKLCDFYMKHKLPRPGHLLGILSQRRLEEQPTSRSLCHQMAAFGDCLRHKCMYRHVMWRDEVLPPDHYPKNGLIRFLVLVCYSPAALAVRLSDQFPTAIRFLNFPMSDLGERVQRHYELEANRHMHPNPVPGEMAVVKNINRYERVHIVSVESNVMVLVQLLDTSTECFSYKTSQLYSCDKIFKDSPREAMDLRILGLQPESLDRIWPDDARNLVRKDFFRRTHNKRNRQFHAVVQSAIHRTIFVRNIYDDEGNDLLSFVINRFRSHQDECCQLKLDAMVMSSKDCPYM
Protein: Zinc transporter ZIP13 (Solute carrier family 39 member 13) (Zrt- and Irt-like protein 13) (ZIP-13) (Q8BZH0)
Organism: Mus musculus (Mouse)
Function: Acts as a zinc-influx transporter.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:18985159}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96H72}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q96H72}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96H72}.
Interaction partners:
- Zinc transporter ZIP9
- Proton-coupled zinc antiporter SLC30A2
- Proton-coupled zinc antiporter SLC30A5
- Zinc transporter ZIP1
- Probable proton-coupled zinc antiporter SLC30A4
- Zinc transporter ZIP11
- Zinc transporter 7
- Zinc transporter 6
- Proton-coupled zinc antiporter SLC30A1
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
Sequence:
MPGCPCPGCGMAGQRLLFLTVLALELLERAGGSQPALRSLGAAAACRLDNKESESWGALLSGERLDTWICSLLGSLMVGLSGVFPLLVIPLEMGTLLQSEAGAWRLRQLLSFALGGLLGNVFLHLLPEAWAYTCNITPGGEGQSLQRQQQLGLWVIAGFLTFLALEKMFLNSKEDPSQAPSKDPTAAALNGGHCLAQPAAEPGLRAVVRNLKVSGYLNLLANTIDNFTHGLAVAASFLVSKKIGLLTTMAILLHEIPHEVGDFAILLRAGFDRWTAAKLQFSTALGGLLGACFAICTQSPKGVEETVVWILPFTSGGFLYIALVNVLPDLLEEDDPWHSLQQVLLLCSGVLVMVLLSLFVE
Protein: Protein snail (P08044)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for the correct specification of ventral-dorsal patterns.
Subcellular location: Nucleus.
Interaction partners:
- DE-cadherin
- C-terminal-binding protein
- Protein twist
- Dorsal-ventral patterning protein Sog
- G9a, isoform B
- Histone deacetylase HDAC1
- RAC serine/threonine-protein kinase
- Partner of paired, isoform B
- Mothers against decapentaplegic homolog
- Scalloped, isoform Q
Sequence:
MAANYKSCPLKKRPIVFVEERLPQTEALALTKDSQFAQDQPQDLSLKRGRDEETQDYQQPEPKRDYVLNLSKTPERNSSSSSNSCLLSPPVEAQDYLPTEIHMRGLTAGTTGYTTATPTTINPFQSAFVMAAGCNPISALWSSYQPHLAAFPSPASSMASPQSVYSYQQMTPPSSPGSDLETGSEPEDLSVRNDIPLPALFHLFDEAKSSSSGASVSSSSGYSYTPAMSASSASVAANHAKNYRFKCDECQKMYSTSMGLSKHRQFHCPAAECNQEKKTHSCEECGKLYTTIGALKMHIRTHTLPCKCPICGKAFSRPWLLQGHIRTHTGEKPFQCPDCPRSFADRSNLRAHQQTHVDVKKYACQVCHKSFSRMSLLNKHSSSNCTITIA
Protein: Aminoglycoside N(6')-acetyltransferase type 1 (EC 2.3.1.82) (AAC(6')-I) (Aminoglycoside resistance protein) (P20092)
Organism: Serratia marcescens
Function: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin and kanamycin.
Interaction partners:
Sequence:
MSIQHFQRKLGITKYSIVTNSNDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDGWWEEETDPGVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPDGPAVYMVQTRQAFERTRRFA
Protein: Inward rectifier potassium channel 2 (Cardiac inward rectifier potassium channel) (Inward rectifier K(+) channel Kir2.1) (IRK-1) (hIRK1) (Potassium channel, inwardly rectifying subfamily J member 2) (P63252)
Organism: Homo sapiens (Human)
Function: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium or cesium.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16571646, ECO:0000269|PubMed:9533862}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q64273}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 1
- ATP-sensitive inward rectifier potassium channel 12
- Inward rectifier potassium channel 4
- Potassium voltage-gated channel subfamily KQT member 2
- Potassium voltage-gated channel subfamily KQT member 3
- Voltage-gated inwardly rectifying potassium channel KCNH2
- Potassium voltage-gated channel subfamily KQT member 5
- Potassium voltage-gated channel subfamily KQT member 4
- Inward rectifier potassium channel 18
- Endothelin-1 receptor
Sequence:
MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKEGKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDIDLHNQASVPLEPRPLRRESEI
Protein: Putative metabotropic GABA-B receptor subtype 3 (Q9BML5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRIIQPVQGTRYGPWPAVGLRLVLALAWATSAAAAMESSAELQALGHEAIRPGAASISTSSPSSSPPGESASTVTAGGTPIPPRSDWKYKRTKVKRRQQRLNSHSNLPGSTNASHAHHLLNLPPRQRYLKVNQVFESERRMSPAEMQRNHGKIVLLGLFELSTSRGPRPDGLSELGAATMAVEHINRKRLLPGYTLELVTNDTQCDPGVGVDRFFHAIYTQPSTRMVMLLGSACSEVTESLAKVVPYWNIVQVSFGSTSPALSDRREFPYFYRTVAPDSSHNPARIAFIRKFGWGTVTTFSQNEEVHSLAVNNLVTELEAANISCAATITFAATDFKEQLLLLRETDTRIIIGSFSQELAPQILCEAYRLRMFGADYAWILHESMGAPWWPDQRTACSNHELQLAVENLIVVSTHNSIVGNNVSYSGLNNHMFNSQLRKQSAQFHGQDGFGSGYGPRISIAATQSDSRRRRRRGVVGTSGGHLFPEAISQYAPQTYDAVWAIALALRAAEEHWRRNEEQSKLDGFDYTRSDMAWEFLQQMGKLHFLGVSGPVSFSGPDRVGTTAFYQIQRGLLEPVALYYPATDALDFRCPRCRPVKWHSGQVPIAKRVFKLRVATIAPLAFYTIATLSSVGIALAITFLAFNLHFRKLKAIKLSSPKLSNITAVGCIFVYATVILLGLDHSTLPSAEDSFATVCTARVYLLSAGFSLAFGSMFAKTYRVHRIFTRTGSVFKDKMLQDIQLILLVGGLLLVDALLVTLWVVTDPMERHLHNLTLEISATDRSVVYQPQVEVCRSQHTQTWLSVLYAYKGLLLVVGVYMAWETRHVKIPALNDSQYIGVSVYSVVITSAIVVVLANLISERVTLAFITITALILTSTTATLCLLFIPKLHDIWARNDIIDPVIHSMGLKMECNTRRFVVDDRRELQYRVEVQNRVYKKEIQALDAEIRKLERLLESGLTTTSTTTSSSTSLLTGGGHLKPELTVTSGISQTPAASKNRTPSISGILPNLLLSVLPPVIPRASWPSAEYMQIPMRRSVTFASQPQLEEACLPAQDLINLRLAHQQATEAKTGLINRLRGIFSRTTSSNKGSTASLADQKGLKAAFKSHMGLFTRLIPSSQTASCNAIYNNPNQDSIPSEASSHPNGNHLKPIHRGSLTKSGTHLDHLTKDPNFLPIPTISGGEQGDQTLGGKYVKLLETKVNFQLPSNRRPSVVQQPPSLRERVRGSPRFPHRILPPTCSLSALAESEDRPGDSTSILGSCKSIPRISLQQVTSGGTWKSMETVGKSRLSLGDSQEEEQQAPANGTE
Protein: Variant surface glycoprotein (VSG), putative (Q38CQ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MHTALICAVLLTMAMVLRQQAQGAVKDNEHGGDCAALCGLIQFAEPNTPAISLPQEITEIADELLAVNLSMSEAALQQLVTKHKDKSWDDIPASDKPAAQPYKEHWQHWQKLAADPKPETVKFKLEQFRKVSQNTMAKNKFHLIADAALELATEAKMLLQKKTKTDIDTKLTKALNGNNAPTNTFTFSGKTRSQLCGTGTTTPGEQAGKALLVDLLCICAGANTDTTAGKSCCKGCETNPNHDEWQPATNAKLRAEHIAKQCPTTRATADKSTTKLHHLLGDFYTQVNTAKGTGQEMKYALGTVGGNGNDGCTGKVGSTNNGRCVKYTDNSILKGTPQLDWVQNLIDAAADYDARTDNMNKIQRIADKMEVLNKTATALLWEQQPVPILQTKAATTTTHQTAEETKQECKAITKAADCNSNGNCKWTKPDVKTGTHCELNTTTSEQAAQTGGGAAGATTTVKCSDYGTKDKCEEVNKGKDKPVCGWRIGKDNEDDKGTEKCRDSSILPNKHFALSVVSAAFAALLF
Protein: Very low-density lipoprotein receptor (VLDL receptor) (VLDL-R) (P98156)
Organism: Mus musculus (Mouse)
Function: Multifunctional cell surface receptor that binds VLDL and transports it into cells by endocytosis and therefore plays an important role in energy metabolism. Binds also to a wide range of other molecules including Reelin/RELN or apolipoprotein E/APOE-containing ligands as well as clusterin/CLU. In the off-state of the pathway LRP8 and VLDLR form homo or heterooligomers (By similarity). Upon binding to ligands, homooligomers are rearranged to higher order receptor clusters that transmit the extracellular RELN signal to intracellular signaling processes by binding to DAB1 on its cytoplasmic tail (By similarity). This interaction results in phosphorylation of DAB1 leading to the ultimate cell responses required for the correct positioning of newly generated neurons. Later, mediates a stop signal for migrating neurons, preventing them from entering the marginal zone.
Subcellular location: Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit; Single-pass type I membrane protein.
Interaction partners:
- Reelin
- Apolipoprotein E
- Disabled homolog 1
- Proprotein convertase subtilisin/kexin type 9
- Low-density lipoprotein receptor-related protein 8
- Clusterin
- Lipoprotein lipase
- Thrombospondin-1
- Apolipoprotein B-100
- Hepatic triacylglycerol lipase
Sequence:
MGTSARWALWLLLALCWAPRDSGATASGKKAKCDSSQFQCTNGRCITLLWKCDGDEDCADGSDEKNCVKKTCAESDFVCKNGQCVPNRWQCDGDPDCEDGSDESPEQCHMRTCRINEISCGARSTQCIPVSWRCDGENDCDNGEDEENCGNITCSADEFTCSSGRCVSRNFVCNGQDDCDDGSDELDCAPPTCGAHEFQCSTSSCIPLSWVCDDDADCSDQSDESLEQCGRQPVIHTKCPTSEIQCGSGECIHKKWRCDGDPDCKDGSDEVNCPSRTCRPDQFECEDGSCIHGSRQCNGIRDCVDGSDEVNCKNVNQCLGPGKFKCRSGECIDMSKVCDQEQDCRDWSDEPLKECHINECLVNNGGCSHICKDLVIGYECDCAAGFELIDRKTCGDIDECQNPGICSQICINLKGGYKCECSRGYQMDLATGVCKAVGKEPSLIFTNRRDIRKIGLERKEYIQLVEQLRNTVALDADIAAQKLFWADLSQKAIFSASIDDKVGRHFKMIDNVYNPAAIAVDWVYKTIYWTDAASKTISVATLDGAKRKFLFNSDLREPASIAVDPLSGFVYWSDWGEPAKIEKAGMNGFDRRPLVTEDIQWPNGITLDLVKSRLYWLDSKLHMLSSVDLNGQDRRIVLKSLEFLAHPLALTIFEDRVYWIDGENEAVYGANKFTGSELATLVNNLNDAQDIIVYHELVQPSGKNWCEDDMENGGCEYLCLPAPQINDHSPKYTCSCPNGYNLEENGRECQSTSTPVTYSETKDINTTDILRTSGLVPGGINVTTAVSEVSVPPKGTSAAWAILPLLLLVMAAVGGYLMWRNWQHKNMKSMNFDNPVYLKTTEEDLSIDIGRHSASVGHTYPAISVVSTDDDLA
Protein: Target of Myb1 membrane trafficking protein (Target of Myb protein 1) (O88746)
Organism: Mus musculus (Mouse)
Function: Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (By similarity). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (By similarity). Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes (By similarity). MYO6 links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). Binds to polyubiquitinated proteins via its GAT domain (By similarity). In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin (By similarity). Mediates clathrin recruitment to early endosomes by ZFYVE16 (By similarity). Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition; the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking (By similarity). Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation. PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation. Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25588840}. Endosome membrane {ECO:0000269|PubMed:25588840}; Peripheral membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:O60784}; Peripheral membrane protein {ECO:0000305}. Note=Localized to endo/exosomal vesicles (PubMed:25588840). Enriched on signaling endosomes (PubMed:25588840). Recruited to early endosomes by TOLLIP and by PtdIns(5)P (By similarity). {ECO:0000250|UniProtKB:O60784, ECO:0000269|PubMed:25588840}.
Interaction partners:
- Toll-interacting protein
- Unconventional myosin-VI
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
Sequence:
MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDAFRAVKKRIMGNKNFHEVMLALTVLETCVKNCGHRFHVLVANQDFVENVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETPSRQNSVSSNTSQRGDLSQHATPLPTPAVLPGDSPITPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQVEPADLELLQELNRTCRAMQQRILELIPRISNEQLTEELLMINDNLNNVFLRHERFERFRTGQTAKASSEAELATDLIDMGPDPAATNNLSSQLAGMNLGSRSVRAGLQSLETSGHLEDDFDMFALTRGSSLADQRKGVKYEAPQTTDGLAGALDARQQSTGAIPATQARIMEDIEQWLSTDVGNSAEEPSGVTSEEFDKFLEERAKAADRLPNLASPSAEGPPRPSPGTAPRRKTQEKDDDMLFAL
Protein: Dynein regulatory complex subunit 7 (Coiled-coil domain-containing protein 135) (Coiled-coil domain-containing protein lobo homolog) (Spermatogenesis-related gene in late stages of spermatogenesis cells protein) (Q6V3W6)
Organism: Mus musculus (Mouse)
Function: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (By similarity). Essential for male fertility, sperm head morphogenesis and sperm flagellum formation. Not required for ciliogenesis in the brain and trachea.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A8JAM0}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8JAM0}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8JAM0}. Note=Associated with the outer doublet microtubules (OD). {ECO:0000250|UniProtKB:A8JAM0}.
Interaction partners:
- Dynein regulatory complex protein 1
- Dynein regulatory complex subunit 4
- Outer dynein arm-docking complex subunit 4
- Dynein regulatory complex subunit 2
- Dynein regulatory complex subunit 3
- Dynein regulatory complex subunit 5
Sequence:
MEVLREKVEEEEEAEREEAAERAERTEKLERVTKSAEVSREGTILSQDELRDLEGKLMAIEIPTQADHSVISQAPVDVTKLPPSYTTNSLKEEHLLLVADNFSRQYSHLCPDRVPLFLHPLNECNVPKFVSTTLRPTLMPYPELYNWDSCAQFVSDFLTMVPLVDPLKPPTHLYSSTTVLKCQKGNCFDFSTLLCSMLIGSGYDAYCVNGYGSLDLCLMDLTREVCPLTVKAKEIVKKKEKTVPKKYSIKPPRDLTSKFEQEQEEKRIQEIKDLEQRRLKEEEDRILEAEKAKPDPLHGLRVHSWVLVLAGKREVPESFFIDPLTARSYSTKDEHFLGIESLWNHKNYWINMQDCWNCCKDLIFDLGDPVRWEYMLLGTDKPHLSLTEEDEEGLDDDDDDVEDLGKEEEDKSFDMPSSWVSQIEITPEEFETRCPSGKKVIQYKKAQLEKWSPYLNNNGLVCRLTTYEDQQCTKVLEIKEWYQNREDMLELKHINKTTGLHVDYFKPGHPQALCVHSYKSMLPEMDRVMEFYKKIRVDGLVKREETPMTMTEYYEGRSDFLAYRHVNFGPRVKKLSQSSVESNPRPMVKITERFSRNPEKPADEDVAERLFLIVEERIQLRYHCRDDYITASKREFLRRMEVDSKGNKIIMTPEMCISYEVEPMEHTKKLLYQYETMNQLKNEEKLSRHQAWESELEVLEILKLREEEEEAHTLTISIYDTKRNEKSKEYREAMERVLHEEHLRQVEAQLDYLAPFLAQLPPGEKLTRWQAVRLKDECLSDFKQRLIDKANLIQARFEKETQELQKKQQWYQENQVTLTPEDENLYLSYCSQAMFRIRILEQRLNRHKELAPLKYLALEEKLYKDPRLIDFVKVFV