wanglab/gogpt-training-data huggingface dataset:
Protein: RE62293p (Q8MT34)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046278}; Lipid-anchor {ECO:0000256|ARBA:ARBA00046278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00046278}.
Interaction partners:
Sequence:
MAGDMSIGCAALKRSSKLRSCTSAADTDSMRVPSDHRDNGSLIKPPPVPPQNMRGGLRVYKIVILGDGGVGKSAVTLQFVSHSFLDYHDPTIEDSYQRQAVIDNEAALLDILDTAGQVEFTAMRDQYMRCGEGFIICYSVTDRHSFQEASEYRKLITRVRLSEDIPLVLIANKVDLESQRRVTTEEGRNLSTSSAARFLRHRLHCVITSTRHSTRWSARFDARKCTRPWARTPIRKRFTRGDEVAGGASDPFSHWFSGADETLTRPGGGFLEMSAILTTKTK
Protein: Inositol-3-phosphate synthase (EC 5.5.1.4) (Myo-inositol-1-phosphate synthase) (MIP synthase) (TbINO1) (Q5QQ46)
Organism: Trypanosoma brucei brucei
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). De novo-synthesized myo-inositol is essential for incorporation into GPI (glycosylphosphatidylinositol) glycolipids in the bloodstream form.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16824097}.
Interaction partners:
Sequence:
MPAVRTKSGHGVEYTDEAITATYSYNTTRVEKEANGDVTVQPIQLHLKFRTQRKVQRTGVMLIGWGGNNGTTVTAALMAHKHRXSWRTKTGTKQPDYLGSITQSSTMSVGLTSEMEEVFVPMKALVPMINPAELVIGGWDCSGMNIADAMRRAQVLDVTLQDALYNYLKDMHPLPAAFDLDFVAENQLSRADNIMQTKNKWESVEQLRADIRNFREKNSLEEVIVLWTANTERFSEHITGVHDTADHLIDAIRRNENEIAPSVLYATAAIMEGCSYVNGAPQNTLCAGLIELARRHGVFVVGDDFKSGQTKVKSGLVEFFMDAGIKPECIASYNHLGNNDGYNLAAPKQFRSKEVTKGGVLDDMVSSNSILYPPGSRGPDHCIVIKYLPYVGDSKRALDEYNFSIFMGGEQTVVLHNTCQDSLLAAPLIIDLVVLTELMHRVTVTQCDGEDCCDKKEKMTSYTHMETVLSLLSYLLKAPRVPEGTPVVNGLNRQGQAIKNVLRALVGLPPDNNMQLECRLPFLRGVGS
Protein: Zinc finger and BTB domain-containing protein 10 (Zinc finger protein RIN ZF) (Q9WTY8)
Organism: Rattus norvegicus (Rat)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MGPGRRGNGIGGPGAPRLGGLRRGGRRGGRQGVAAPLGHGRPRLAGRRRGGPPASGKEPSDSGLPRGRRRGSRQQWQQSRPPGDLGVAPQAFQWARAGGRGSGAGRAGGEGVDAGRGVPELQHRGGGGEPGRWQWGGRRQRSSSRRSGGEGGEEAEGSGVGAGEGETVQHFPLARPKSLMQKLQCSFQTSWLKDFPWLRYSNDTGLMFCGWCQTTPEDVGSVDLPQVGHDELSRGTRNYKKTLLLRHHVSTEHKLHEANAQVLGSQACVTVDGSAVDKPDASEGCLLVGNESEIPSEEGYCDFNSRPNENSYCYQLLRQLDEQRKKDILCDVSIVVSGKIFKAHKNILVAGSRFFKTLYCVSNKESPNQNNTTHLDIAAVQGFSVILDFLYSGNLVLTSQNAIEVMTVASYLQMSEVVQTCRNFIKDALNISIKSEAPESVVVDYNNRKPVSRDGLTSSRDQKIASFWATRNLTNLASNIKIENDGCNVDEGQIENYQMNDSNWVQDGSPELAENESQGKTKVFIWNNMASQETGKARRKNQTTKRFVYNIPPNSETIVEDCSVLQPPVAYPEENKALLIKEEPVSDLDGALLSGPDGDRTMNTNLLAEACSSQDAGDAAGASHDFKYGLMPGTSSDFKYGLLPSTSNDFKYGLLPGAPNDFKYGLLPESWPTQEPWENGDSSLIMNKLKCPHCSYVAKYRRTLKRHLLIHSGVRSFKCEICGKMFTRREHVKRHSLVHKKDKKYKCMVCKKIFMLAASVGIKHGSRRYGVCMDCVDKSQPGGQESIDQGQDTEFPRDEEYEENEGVEPDEELAEDGQDQSDAPRWDEPGGAYVSG
Protein: Sec14 cytosolic factor (Phosphatidylinositol/phosphatidyl-choline transfer protein) (PI/PC TP) (Sporulation-specific protein 20) (Q10137)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro. Essential for viability and secretion.
Subcellular location: Nucleus {ECO:0000269|PubMed:11294895}. Prospore membrane {ECO:0000269|PubMed:11294895}. Note=Nuclear, during meiosis. Associated with the forespore membrane during sporulation. During interphase found at the cell poles and during M-phase is located at both the cell poles and the medial region.
Interaction partners:
- Probable prefoldin subunit 3
- Membrane glycoprotein spo14
- Sporulation-specific protein 2
- Sporulation-specific protein 13
- Sporulation-specific protein 15
- Sporulation-specific protein 3
Sequence:
MSETISDPYPLTNPNAPLGHPGHLNSTQQATLDSMRLELQKLGYTERLDDATLLRFLRARKFNLQQSLEMFIKCEKWRKEFGVDDLIKNFHYDEKEAVSKYYPQFYHKTDIDGRPVYVEQLGNIDLKKLYQITTPERMMQNLVYEYEMLALKRFPACSRKAGGLIETSCTIMDLKGVGITSIHSVYSYIRQASSISQDYYPERMGKFYVINAPWGFSSAFNLIKGFLDEATVKKIHILGSNYKSALLEQIPADNLPAKLGGNCQCPGGCELSDAGPWHEEQWMNKN
Protein: Trem-like transcript 4 protein (TLT-4) (Triggering receptor expressed on myeloid cells-like protein 4) (Q6UXN2)
Organism: Homo sapiens (Human)
Function: Positively regulates Toll-like receptor TLR7 signaling in macrophages.
Subcellular location: Secreted {ECO:0000305|PubMed:24975946}.
Interaction partners:
- CMRF35-like molecule 2
- Triggering receptor expressed on myeloid cells 1
- Trem-like transcript 1 protein
Sequence:
MAWGGVHTCCFHLCCCCSWPQGAVPEELHKHPGQTLLLQCQYSPKRGPYQPKSWCQQTSPSRCTLLVTSSKPWTAVQKSHYTIWDKPNAGFFNITMIQLTQNDSGFYWCGIYNASENIITVLRNISLVVSPAPTTSPMWTLPWLPTSTVLITSPEGTSGHPSINGSETRKSRAPACLGSGGPRFLVLVLCGLLLAKGLML
Protein: Electrogenic sodium bicarbonate cotransporter 1 (Sodium bicarbonate cotransporter) (Na(+)/HCO3(-) cotransporter) (Solute carrier family 4 member 4) (kNBC1) (Q9Y6R1)
Organism: Homo sapiens (Human)
Function: Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:12907161, ECO:0000269|PubMed:15273250, ECO:0000269|PubMed:15713912, ECO:0000269|PubMed:17661077}; Multi-pass membrane protein {ECO:0000269|PubMed:12534288, ECO:0000305|PubMed:29500354}. Cell membrane {ECO:0000269|PubMed:12534288, ECO:0000269|PubMed:15817634, ECO:0000269|PubMed:15930088, ECO:0000269|PubMed:16636648, ECO:0000269|PubMed:23324180, ECO:0000269|PubMed:23636456, ECO:0000269|PubMed:29500354}; Multi-pass membrane protein {ECO:0000269|PubMed:12534288, ECO:0000305|PubMed:29500354}.
Interaction partners:
- S-adenosylhomocysteine hydrolase-like protein 1
- Carbonic anhydrase 2
- Carbonic anhydrase 4
- Sodium/hydrogen exchanger 3
- Sodium/hydrogen exchanger 1
- Solute carrier family 26 member 6
Sequence:
MEDEAVLDRGASFLKHVCDEEEVEGHHTIYIGVHVPKSYRRRRRHKRKTGHKEKKEKERISENYSDKSDIENADESSSSILKPLISPAAERIRFILGEEDDSPAPPQLFTELDELLAVDGQEMEWKETARWIKFEEKVEQGGERWSKPHVATLSLHSLFELRTCMEKGSIMLDREASSLPQLVEMIVDHQIETGLLKPELKDKVTYTLLRKHRHQTKKSNLRSLADIGKTVSSASRMFTNPDNGSPAMTHRNLTSSSLNDISDKPEKDQLKNKFMKKLPRDAEASNVLVGEVDFLDTPFIAFVRLQQAVMLGALTEVPVPTRFLFILLGPKGKAKSYHEIGRAIATLMSDEVFHDIAYKAKDRHDLIAGIDEFLDEVIVLPPGEWDPAIRIEPPKSLPSSDKRKNMYSGGENVQMNGDTPHDGGHGGGGHGDCEELQRTGRFCGGLIKDIKRKAPFFASDFYDALNIQALSAILFIYLATVTNAITFGGLLGDATDNMQGVLESFLGTAVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDNNFDYLEFRLWIGLWSAFLCLILVATDASFLVQYFTRFTEEGFSSLISFIFIYDAFKKMIKLADYYPINSNFKVGYNTLFSCTCVPPDPANISISNDTTLAPEYLPTMSSTDMYHNTTFDWAFLSKKECSKYGGNLVGNNCNFVPDITLMSFILFLGTYTSSMALKKFKTSPYFPTTARKLISDFAIILSILIFCVIDALVGVDTPKLIVPSEFKPTSPNRGWFVPPFGENPWWVCLAAAIPALLVTILIFMDQQITAVIVNRKEHKLKKGAGYHLDLFWVAILMVICSLMALPWYVAATVISIAHIDSLKMETETSAPGEQPKFLGVREQRVTGTLVFILTGLSVFMAPILKFIPMPVLYGVFLYMGVASLNGVQFMDRLKLLLMPLKHQPDFIYLRHVPLRRVHLFTFLQVLCLALLWILKSTVAAIIFPVMILALVAVRKGMDYLFSQHDLSFLDDVIPEKDKKKKEDEKKKKKKKGSLDSDNDDSDCPYSEKVPSIKIPMDIMEQQPFLSDSKPSDRERSPTFLERHTSC
Protein: Myocyte enhancer factor 2C (D6RJG6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGQNLFLLLETVPPPLRDTHNTRATRRGDLLLTA
Protein: Cell cycle checkpoint control protein (A8JNV5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKYTLEGSNARVIAKAVQSLSKVGKEMFIEIDQQSLQMRAINATQSAVGSISFKRSMFEVYDMPPHSDFYCKISMKGCLAVFRNMNEVEYCELNLLDNQTNLQVNLRCKLETTKEATISIIDDQNINTNINTDQMPNIIRGDHKLLTDISNNFNSSEEELTLEANSGSVVAKNYIEGARVNDKFMRTQLKLKPSEFEQYQVTKETVITFCIKEFRAFLLFAECLNASLTLEFDEAGMPFLLKIKKHGEIECLLIMSTLSPDDISFSEDYCQKDLTVQDEDVRAAAAKRKSSVSKPNVTNKRKGSSSEPAAVQPKRRVEETQLESSLDNPLFQFRDSEAPSVQHPRILAEVDTVVLIEDEAEQEALMLAAADAALEASMAPAPEPPNSTEVCFINTDDSQQPKPAKSSSDEDETIPQSPERPNKVRTIFSRCFQRTYVPREPSPNTQVYAPNSDTED
Protein: Secreted protein (Q19591)
Organism: Caenorhabditis elegans
Interaction partners:
- DUF19 domain-containing protein
- DUF19 domain-containing protein
- DUF19 domain-containing protein
- DUF19 domain-containing protein
- C-type LECtin
Sequence:
MKFAIVFAALYGAAVAQFGTDNCVSAQFQACNSKLGDFWRTDTTSAWKDLASLDRITQSLIVSPYVIDSWVNVCNGYAAFYGCLGQAQIRNCLGTVGLVGSGLDLNTAYAYQGFLADWDFKCGAGFWTMYERKTLTTCVESTYVNYQQETSAAMNTYMTATAQDPNGACKYAQNLMNAWQNTYTKGPCRTVMPAQAGWFGCQSAREWSNAQFRHCKHTTQCASPTSNEAVTRFNTETGKVEYETLPTYQIVDNKAVVLNEASWISE
Protein: Protocadherin-17 (Protocadherin-17 precursor) (C4P342)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Ca2+-dependent activator protein for secretion b.
Sequence:
MHLSVFLFLLLWAQALTLKNLNYSIPEEKIQGVIGNIAKDAELELGEQGKKSNFRVLENSAPHLIDVDPESGLLYTKQRIDRETLCRQNSKCQLSMEVFANDKEICMIKVEIQDINDNAPSFPSEQIDIDISENAAPGTRFPLAAAYDPDTKENGLKTYQITRDDYSIFSLDVKSRGDGTKFPELVVQRSLDREERSHHTLIITATDGGEYPKSGTMQINVKVTDSNDNSPVFEQPSYVVEIPENAPLGTVIIDLNATDSDEGINGQVTYSFSCYVPDRIKELFSIDPRTGVIKIQGKIDFEENPIIEIDVQAKDQGPNPIPGHCKVTVKVLDRNDNWPSIGFVAVRQGAVSEAATPGTVIALVRVTDKDSGRNGQLQCRILGNVPFKLEENYDNFYTVVTDRPLDREVKDEYNITIVAKDNGNPPLNSTKSFTVKILDENDNAPRFTKMVYLLQVPENNIPGEYLGSVLAHDPDLGQNGTVSYSLLPSNVSEESITTYVNIKPTDGAIYALRSFNYEQTKYFDFKVQAKDSGNPHLESNTTVRVSVLDVNDNIPVIVLPLLQNDTAEIHVPRNVGVGHIITTVRAVDNDFGESGRLTYEISDGNEEHLFEIDSVTGEVRTAQPLWEEVTPVVELIIKVTDHGKPSLSAMAKLIVKAYSGPLPEGEPRINAEHHNWDMSLPLIVTLSIISIMLLAAMITIAVKCKRENKEIRTYNCRIAEYSHPQLGKSKKKKINKNDIMLVQSEVEERDTMNVMNVVSSPSLATSPMYFDYQTRLPLSSPRSEVMYLKPTANNLSVPQGHVGCHTSFTGPVTNTTETPVNRMSIIQTDNFPAEPNYMGNRQQFVQSSSTFKDPERASLRDSGHGDSDQADSDQDTNKGSCCDMSAKEALKMKATGLKPQPLEQEEDCLNCTEECRVLGHSDRCWMPQFPAGAGGAGTPQAEGSDYRTNLFVPAGMEAVAVETETYETVCNPNGKKTFCTFGKERRDHTILVANVKPYLKTKRALSPLLQEVPSASCSPTKGCSTGSPCSSAKGMGDGAEGKPSTSHYGPPDGQYISPNKQNKEQGYSTLPPSDPVAKVLAEARSRISQETAVEMDCVLEQGGGEMGRSTMDADQVVRDIDKLLQDCRGNENTPIRK
Protein: Phosphatase NudJ (EC 3.6.1.-) (P0AEI6)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of 4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate (HMP-P), and hydrolysis of thiamine pyrophosphate (TPP) to thiamine monophosphate (TMP). Can hydrolyze other substrates such as MeO-HMP-PP, CF(3)-HMP-PP and MeO-TPP. Is also a non-specific nucleoside tri- and diphosphatase that releases inorganic orthophosphate.
Interaction partners:
- Ribosomal large subunit pseudouridine synthase E
- Nucleoside triphosphatase NudI
- tRNA-specific 2-thiouridylase MnmA
- Sulfur carrier protein ThiS
Sequence:
MFKPHVTVACVVHAEGKFLVVEETINGKALWNQPAGHLEADETLVEAAARELWEETGISAQPQHFIRMHQWIAPDKTPFLRFLFAIELEQICPTQPHDSDIDCCRWVSAEEILQASNLRSPLVAESIRCYQSGQRYPLEMIGDFNWPFTKGVI
Protein: Heat shock protein, putative (Q38F93)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- Uncharacterized protein
- Protein disulfide isomerase
- Lipophosphoglycan biosynthetic protein, putative
- Ribosomal protein L7Ae/L30e/S12e/Gadd45 domain-containing protein
- Chaperone protein DNAJ, putative
- Chaperone protein DNAJ, putative
- Chaperone protein DnaJ, putative
- Chaperone protein DNAJ, putative
- Chaperone protein DNAJ, putative
- Nucleotide exchange factor Fes1 domain-containing protein
Sequence:
MLCLAQWALLLVLCLVGCCCTVSGGSEVLAVDIGADWAKGATRVIGGSTAPRASIVLNDQTNRKSPQCIAFRIVPNAGNDTLRSVERLFAEEARSLEPRFPQQSICGPSLLAGLIVSKEISAGQKHHEQTGNQRSEREGVISFSDTDRFTYVVVPQIRRKSAVVRITPGGSSEGTTTAPIEFTVEELIGMILGHMKRSAERSLDGAPVRHLVLVVPTSSSLAYRQAMVDAAAVVGLRTIRLVHGSAAAATQLAHLNTETLFRGHPSNTTERKYAMIYDMGSSKTEVAVFRFTPATARDDFGTVTLVASATNHTLGGRSFDRCLARYVERNLFPAAKPTPVTPVLDRKPVTATTRRAVVSLLRAVNAARERLSVNQNVPFVVPGVREDGGDFIANISRAQFEEACGELFNEAVRLRDHAITQTNGTVRSLNELVRLELIGGATRMPKLQERLSEGYGKPADRTLNSDEAVVSGAALMIHDTLSRIRVMESLTNDIYFTASPPIKESNETKPHRNLLFAKRNTTVPAARSLIFPNRTADFTLTLHDGNGRYSRSVLVSGVSGSMNAAREKEKEMSTERANKVTKTSVVLRQVEVVVEVVLSRSGLPYVAGSYVHARYAEQVTVLPSVKKTGDNETTAQKDENNNPSQNETDTTSTISPGREKRSGGSPSAANSNSAKMQNSRADEAKENETPTGDEILEVNERDAGTGGKNNNAKVRHFALRFPLNNTPAPSSTSQGGVNMNKEEALAARNRLRALQRLDDERLRRSGLLNDVESLLLHYKSLDAWSAQQSDDNSNDWRSVVKDVSRWFEEVGGDVNVTELQKQYQRLKDLKLGE
Protein: Protein TusB (tRNA 2-thiouridine synthesizing protein B) (P45530)
Organism: Escherichia coli (strain K12)
Function: Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sulfurtransferase TusD
- Protein TusC
- Sulfurtransferase TusE
- Sulfur carrier protein TusA
- tRNA-specific 2-thiouridylase MnmA
- Uncharacterized protein YheO
- Cysteine desulfurase IscS
- tRNA sulfurtransferase
- Iron-sulfur cluster assembly scaffold protein IscU
Sequence:
MLHTLHRSPWLTDFAALLRLLSEGDELLLLQDGVTAAVDGNRYLESLRNAPIKVYALNEDLIARGLTGQISNDIILIDYTDFVRLTVKHPSQMAW
Protein: Glycine betaine uptake system permease protein YehW (P33359)
Organism: Escherichia coli (strain K12)
Function: Part of an ABC transporter complex involved in low-affinity glycine betaine uptake. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glycine betaine-binding protein YehZ
- Glycine betaine uptake system ATP-binding protein YehX
- Glycine betaine uptake system permease protein YehY
- Glycine betaine/proline betaine transport system ATP-binding protein ProV
- Uncharacterized lipoprotein YehR
- Uncharacterized protein YehS
- Glycine betaine/proline betaine-binding periplasmic protein
Sequence:
MKMLRDPLFWLIALFVALIFWLPYSQPLFAALFPQLPRPVYQQESFAALALAHFWLVGISSLFAVIIGTGAGIAVTRPWGAEFRPLVETIAAVGQTFPPVAVLAIAVPVIGFGLQPAIIALILYGVLPVLQATLAGLGAIDASVTEVAKGMGMSRGQRVRKVELPLAAPVILAGVRTSVIINIGTATIASTVGASTLGTPIIIGLSGFNTAYVIQGALLVALAAIIADRLFERLVQALSQHAK
Protein: choloylglycine hydrolase (EC 3.5.1.24) (Bile salt hydrolase) (Choloylglycine hydrolase) (Q6J264)
Organism: Bifidobacterium bifidum
Interaction partners:
Sequence:
MCTGVRFSDDEGNMYFGRNLDWSFSYGETILVTPRGYQYDYVYGAEGKSEPNAVIGVGVVMVDRPMYFDCANEHGLAIAGLNFPGYASFAHEPVEGTENVATFEFPLWVTRNFDTVDEVEEALKNVTLVSQVVPGQQESLLHWFIGDGTRSIVVEQMADGMHVHHDDVDVLTNQPTFDFHMENLRNYMCVSNEMAEPTTWGKAELSAWGAGVSMHGIPGDVSSPSRFVRVAYTNTHYPQQNNEAANVSRLFHTLVSVQMVDGMSKMGNGQFERTLFTSGYSGKTNTYYMNTYEDPAIRSFAMSDFDMDSSELITAD
Protein: Nudix hydrolase DR_1184 (EC 3.6.1.77) (Coenzyme A pyrophosphatase) (DR-CoAse) (MutT/nudix family protein) (Q9RV46)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Interaction partners:
- MazG protein
- Nudix hydrolase DR_1025
Sequence:
MTAPHDPLDDIQADPWALWLSGRTRTALELPHYRRAAVLVALTREADPRVLLTVRSSELPTHKGQIAFPGGSLDAGETPTQAALREAQEEVALDPAAVTLLGELDDVFTPVGFHVTPVLGRIAPEALDTLRVTPEVAQIITPTLAELRAVPLVRERRTLPDGTEVPLYRYPWRGLDIWGMTARVLHDLLEQGPG
Protein: Regulator of G-protein signaling 16 (RGS16) (A28-RGS14P) (Retinal-specific RGS) (RGS-r) (Retinally abundant regulator of G-protein signaling) (P97428)
Organism: Mus musculus (Mouse)
Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Plays an important role in the phototransduction cascade by regulating the lifetime and effective concentration of activated transducin alpha. May regulate extra and intracellular mitogenic signals.
Subcellular location: Membrane {ECO:0000269|PubMed:10373502}; Lipid-anchor {ECO:0000269|PubMed:10373502}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MCRTLATFPNTCLERAKEFKTRLGIFLHKSELSSDTGGISKFEWASKHNKERSFSEDVLGWRESFDLLLNSKNGVAAFHAFLKTEFSEENLEFWLACEEFKKIRSATKLASRAHHIFDEYIRSEAPKEVNIDHETRELTKTNLQAATTSCFDVAQGKTRTLMEKDSYPRFLKSPAYRDLAAQASATSTSAPSGSPAEPSHT
Protein: Ubiquitin-activating enzyme E1, putative (Q57UC3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- SUMO-conjugating enzyme UBC9
- Ubiquitin activating enzyme, putative
- Small ubiquitin protein, putative
- Ubiquitin-conjugating enzyme E2, putative
Sequence:
MHVNVGHIVFPVPILSQEAQTVSVKRVKREGAQGVAADDARFVRESVVAAVRVALREAVDGTSVDDVFIDVHVHEGGKGVSFSFVKGFLSLSLSTPAGTEVCIPAGLTFDEIQNATGFPSFTQVRLHFSDEVGGMELPVYWEKRVVCAATPTALVAVEGRIKTPGTNIQYAADKDIVLLDSRVLVVGAGGIGCELLKVLVLYGFSDIDVFDLDTVDATNLNRQFLFNRDDVGQSKSATARQAIMNWFTPANPRRPPNIRAHHANIKDEAYGKAFFAQFAVVLNALDNVSARQCVNRMCKQAGVPLVESGTMGYNGQVQPIVYGRYECYDCHPKASGKQTLAVCTVHARPTTMVHCVHYAKELYERLFGDGQQDAGDELTFVDDLLNQEKERQGINTENGKLNLHNLAVSLGCCLFVSKIEELLSIKSAWPTQPPSPLEPTAIHGAAEQLKAACDNPQGVVPRVTRDCLMSLNETALLFVDAFVRCASRGQRVAFRKEDDDAVDFVAGVSNLRALIFHISPQQSVEEIRSIAGAIVPAIATTNAVIAAGVVQQAVRVLFVSRGGNQPPEPKMIYVRKVPQVRRRRLSANPSAVLGGNGKLGLVRWVSDMYLVHSAPPNPASDKCLVCRDRHPTVDVYLNAKQVTFELFVHRVLQQHLNMHEPTIFHGASILYEKGDYEALNSTPLLSQMKDDHRPLDLLVDDLDHDVEWRVVVHHCEELKEQVPQSGVVVEGLEEALKFESSLLAMPISTADPAAIDAGDAVGEANVPAGGCTLSKAAVPVLIDSGDEDSDEVVEID
Protein: Leucine-rich repeat-containing protein 4 (Brain tumor-associated protein MBAG1) (Netrin-G2 ligand) (NGL-2) (Q99PH1)
Organism: Mus musculus (Mouse)
Function: Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays an important role for auditory synaptic responses. Involved in the suppression of glioma.
Subcellular location: Membrane; Single-pass type I membrane protein. Postsynaptic cell membrane {ECO:0000250}. Note=LRRC4 and DLG4 are interdependent for synaptic localization. {ECO:0000250}.
Interaction partners:
- Netrin-G2
- Netrin-G1
- Disks large homolog 4
Sequence:
MKLLWQVTVHHTWNAVLLPVVYLTAQVWILCAAIAAAASAGPQNCPSVCSCSNQFSKVVCTRRGLSEVPQGIPSNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDNWLTVIPSGAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLMRLDLGELKKLEYISEGAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWLAWWLREYIPTNSTCCGRCHAPMHMRGRYLVEVDQAAFQCSAPFIMDAPRDLNISEDRMAELKCRTPPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNVSSAELNTPNFSFFTTVTVETTEISPEDITRKYKPVPTTSTGYQPAYTTSTTVLIQTTRVPKQVPVPSTDTTDKMQTSLDEVMKTTKIIIGCFVAVTLLAAAMLIVFYKLRKRHQQRSTVTAARTVEIIQVDEDIPAAAPAAATAAPSGVSGEGAVVLPTIHDHINYNTYKPAHGAHWTENSLGNSLHPTVTTISEPYIIQTHTKDKVQETQI
Protein: RNA demethylase ALKBH5 (EC 1.14.11.53) (Alkylated DNA repair protein alkB homolog 5) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5) (Q6P6C2)
Organism: Homo sapiens (Human)
Function: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro). Requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA processing and export. Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells (By similarity).
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:21264265, ECO:0000269|PubMed:23177736, ECO:0000269|PubMed:37474102}. Note=Promotes formation and localizes to paraspeckles, a nuclear membraneless organelle. {ECO:0000269|PubMed:37474102}.
Interaction partners:
- Alpha-ketoglutarate-dependent dioxygenase FTO-)-demethylase FTO)
- Probable ATP-dependent RNA helicase DDX46
- Nucleic acid dioxygenase ALKBH1
- YTH domain-containing family protein 1
- N
- Pre-mRNA-splicing regulator WTAP
- N
- 3'-5' RNA helicase YTHDC2
- YTH domain-containing protein 1
- YTH domain-containing family protein 2
Sequence:
MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYPVSGAKRKYQEDSDPERSDYEEQQLQKEEEARKVKSGIRQMRLFSQDECAKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPEWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSVLPPSYASDRLSGNNRDPALKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPTHRRRGSFSSENYWRKSYESSEDCSEAAGSPARKVKMRRH
Protein: DNA repair protein rad60 (Q9USX3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for repair of DNA double strand breaks which occur during replication, or induced by UV or gamma radiation, via recombination between sister chromatids. This has a subsequent role in the maintenance of chromosome structure. May work in conjunction with the Smc5-Smc6 complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:11971984}.
Interaction partners:
- SUMO-conjugating enzyme ubc9
- Structural maintenance of chromosomes protein 6
- Ubiquitin-like protein pmt3/smt3
- E3 SUMO-protein ligase pli1
- E3 SUMO-protein ligase nse2
- Ubiquitin-activating enzyme E1-like
- E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8
- Ubiquitin-like-specific protease 1
- Asteroid homolog 1
- Serine/threonine-protein kinase cds1
Sequence:
MDNLDEDDLAFFSKPIKKPPLNYAKQLIASSSDSEEESELDTNKQALEHINAQKNITHNENKSAEPLSRQSTILDADEGNQDVSDTTPNACLNEGRHSPKSAISCVTQPVSPVYNTRAAANLRNNSINSEAALSTTSSLLDDDFARRLEEIDRQVQEFEKSSSDMDVQIHTHKREIEEDDDNTSADVPLLKHSKSDHSTLYHSKSEFSTNEPVISVVLQLAVIGQRIPNSNISLPRDWEAPLFFKVKSNQQFRRVRIAYSERKKVDNVVLVFQNQRLWDYGTPKGAGMLKVDTRLVVHAYCHSDFISLKRIKELEVEKLSSVTEDSTAQTCKLITLLLRSSKSEDLRLSIPVDFTVKDLIKRYCTEVKISFHERIRLEFEGEWLDPNDQVQSTELEDEDQVSVVLD
Protein: DNA-directed RNA polymerase subunit alpha (RNAP subunit alpha) (EC 2.7.7.6) (RNA polymerase subunit alpha) (Transcriptase subunit alpha) (P20429)
Organism: Bacillus subtilis (strain 168)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit beta'
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS8
- DNA-directed RNA polymerase subunit beta
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein bL17
- Small ribosomal subunit protein uS10
- Translation initiation factor IF-1
Sequence:
MIEIEKPKIETVEISDDAKFGKFVVEPLERGYGTTLGNSLRRILLSSLPGAAVTSIQIDGVLHEFSTIEGVVEDVTTIILHIKKLALKIYSDEEKTLEIDVQGEGTVTAADITHDSDVEILNPDLHIATLGENASFRVRLTAQRGRGYTPADANKRDDQPIGVIPIDSIYTPVSRVSYQVENTRVGQVANYDKLTLDVWTDGSTGPKEAIALGSKILTEHLNIFVGLTDEAQHAEIMVEKEEDQKEKVLEMTIEELDLSVRSYNCLKRAGINTVQELANKTEEDMMKVRNLGRKSLEEVKAKLEELGLGLRKDD
Protein: Creatinine amidohydrolase (EC 3.5.2.10) (Creatininase) (P83772)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.
Interaction partners:
Sequence:
MSKSVFVGELTWKEYEARVAAGDCVLMLPVGALEQHGHHMCMNVDVLLPTAVCKRVAERIGALVMPGLQYGYKSQQKSGGGNHFPGTTSLDGATLTGTVQDIIRELARHGARRLVLMNGHYENSMFIVEGIDLALRELRYAGIQDFKVVVLSYWDFVKDPAVIQQLYPEGFLGWDIEHGGVFETSLMLALYPDLVDLDRVVDHPPATFPPYDVFPVDPARTPAPGTLSSAKTASREKGELILEVCVQGIADAIREEFPPT