wanglab/gogpt-training-data huggingface dataset:
Protein: Lysyl oxidase homolog 4 (EC 1.4.3.13) (Lysyl oxidase-like protein 4) (Lysyl oxidase-related protein C) (Q96JB6)
Organism: Homo sapiens (Human)
Function: May modulate the formation of a collagenous extracellular matrix.
Subcellular location: Secreted, extracellular space {ECO:0000305}.
Interaction partners:
- Elastin
- Fibulin-5
Sequence:
MAWSPPATLFLFLLLLGQPPPSRPQSLGTTKLRLVGPESKPEEGRLEVLHQGQWGTVCDDNFAIQEATVACRQLGFEAALTWAHSAKYGQGEGPIWLDNVRCVGTESSLDQCGSNGWGVSDCSHSEDVGVICHPRRHRGYLSETVSNALGPQGRRLEEVRLKPILASAKQHSPVTEGAVEVKYEGHWRQVCDQGWTMNNSRVVCGMLGFPSEVPVDSHYYRKVWDLKMRDPKSRLKSLTNKNSFWIHQVTCLGTEPHMANCQVQVAPARGKLRPACPGGMHAVVSCVAGPHFRPPKTKPQRKGSWAEEPRVRLRSGAQVGEGRVEVLMNRQWGTVCDHRWNLISASVVCRQLGFGSAREALFGARLGQGLGPIHLSEVRCRGYERTLSDCPALEGSQNGCQHENDAAVRCNVPNMGFQNQVRLAGGRIPEEGLLEVQVEVNGVPRWGSVCSENWGLTEAMVACRQLGLGFAIHAYKETWFWSGTPRAQEVVMSGVRCSGTELALQQCQRHGPVHCSHGGGRFLAGVSCMDSAPDLVMNAQLVQETAYLEDRPLSQLYCAHEENCLSKSADHMDWPYGYRRLLRFSTQIYNLGRTDFRPKTGRDSWVWHQCHRHYHSIEVFTHYDLLTLNGSKVAEGHKASFCLEDTNCPTGLQRRYACANFGEQGVTVGCWDTYRHDIDCQWVDITDVGPGNYIFQVIVNPHYEVAESDFSNNMLQCRCKYDGHRVWLHNCHTGNSYPANAELSLEQEQRLRNNLI
Protein: Disintegrin and metalloproteinase domain-containing protein 8 (ADAM 8) (EC 3.4.24.-) (Cell surface antigen MS2) (Macrophage cysteine-rich glycoprotein) (CD antigen CD156a) (Q05910)
Organism: Mus musculus (Mouse)
Function: Possible involvement in extravasation of leukocytes.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-3
Sequence:
MLGLWLLSVLWTPAVAPGPPLPHVKQYEVVWPRRLAASRSRRALPSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAGLRGFFRVGSTVHLIEPLDADEEGQHAMYQAKHLQQKAGTCGVKDTNLNDLGPRALEIYRAQPRNWLIPRETRYVELYVVADSQEFQKLGSREAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWNKDKFYISRYANVTLENFLSWREQNLQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSRHSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPEPREGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVPDVNRFVGGPVCGNLFVEHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAFQQNGTPCPGGYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPGCNGRMYSGRINRCGALYCEGGQKPLERSFCTFSSNHGVCHALGTGSNIDTFELVLQGTKCEEGKVCMDGSCQDLRVYRSENCSAKCNNHGVCNHKRECHCHKGWAPPNCVQRLADVSDEQAASTSLPVSVVVVLVILVAAMVIVAGIVIYRKAPRQIQRRSVAPKPISGLSNPLFYTRDSSLPAKNRPPDPSETVSTNQPPRPIVKPKRPPPAPPGAVSSSPLPVPVYAPKIPNQFRPDPPTKPLPELKPKQVKPTFAPPTPPVKPGTGGTVPGATQGAGEPKVALKVPIQKR
Protein: Acidic phospholipase A2 1 (svPLA2) (EC 3.1.1.4) (LM-PLA2-I) (Phosphatidylcholine 2-acylhydrolase) (P0C932)
Organism: Lachesis muta muta (Bushmaster)
Function: Snake venom phospholipase A2 (PLA2) that displays a potent enzymatic activity as measured by indirect hemolysis of red blood cells. Is neither lethal when injected into mice nor does it present anticoagulant activity. Displays a moderate inhibitory activity on the aggregation of platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, strongly inhibits platelet aggregation induced by high doses of collagen. Shows myotoxic activity, increases the plasma creatine-kinase activity and induces edema and myonecrosis of mouse skeletal muscles. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted.
Interaction partners:
Sequence:
HLLQFGDLIDKIAGRSGFWYYGFYGCYCGLGGRGRPQDATDRCCFVHDCC
Protein: JAB1/MPN/MOV34 metalloenzyme domain-containing protein (Q4QIM7)
Organism: Leishmania major
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit 7-like protein
- Uncharacterized protein
- Eukaryotic translation initiation factor 3 subunit E
- JAB1/MPN/MOV34 metalloenzyme domain-containing protein
- Putative eukaryotic translation initiation factor 3 subunit 8
- CSN8/PSMD8/EIF3K domain-containing protein
- Eukaryotic translation initiation factor 3 subunit L
Sequence:
MYAGFPRLNVTEAQETVDLDFELTNEKGCVKVTEFPVPKVVNLSFPAVCALLYNARTATSSRNIFGSVIGLQLQDTVEVTDVKTNPSIDIEEDDRMTEEERMERVRKERKLLDADKAIFENMYNQENLDTNVIGQFVVSSARFNPFSTRTMRKLQELHRESLPAILLTYDPFRTGLLGRPHIRAYTPTAAYYKYDSLVSTERGYQRRRSLAQYAKESGITKEGVLHEIPVKLEVDAFHKLNLMNVPPTAVGDSFKAIQSMAVSNYIEALLSSIRNNTDQLKQKLDYEGNVKDNGNVPVGQDAETMLLMKHVRDQTDHLDALCDSALLYSSLLRDL
Protein: Protein KRI1 homolog (Q6DRJ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Zona pellucida glycoprotein d.
- KRR1 small subunit processome component homolog.
- NOP14 nucleolar protein homolog
- BMS1 ribosome biogenesis factor
- NOC2-like nucleolar-associated transcriptional repressor
- PWP2 small subunit processome component.
- rRNA-processing protein UTP23 homolog
- Protein LTV1 homolog
- ESF1 homolog)
- U3 small nucleolar ribonucleoprotein protein MPP10
Sequence:
MSDLKINKKFAEKYEKYRQKEELQRLKDRYGDQEEENSSNSSESDSDDSEVELDPKLDRDFYRTLSLLKKKDPKIYQKDAKFYTEETSGSGSDEQPSTSKQSEKPMFLKDYERKVILERGGKYEDDDSADEEISAKMQERAASPTYIQEQKEIQESLRKFVQDSDDEDSDGDGQFLTRRTKTQEEKDKEEADYVEWLKGQTELDEKEELKDMKYLRDYWNNPQLDEKESFLRDFMLNKGYMEEEDEERIPTYNELMQDDVDDSEDEGESFLHKQEDFERHYNFRFEEPDAGKVKTYPRNIATSVRSKDDRRKRKREEVKERKEKEKEQKQQQLKELKNLKRAEIMDKLKKLQELTGNEQLAFNDVDLDGDFDPQQHDQLMQKVFGDEYYEENEEEKPQFEGDEEFEENWNWDTWVGKQQNEEEYDHKEDYTAEEHYQPNCDDPDFIMDADYDPSQQAVSKKKRKKEREEKKKKSKEDVPLMGKKRKKSHFAEIISKSKPVFDPNEKSFEQYLDEYYKLDFEDIIDDLPCRFRYREVVANDFGLSTDEILNAGDKELNRWCSLRKTCMYRSEREELCDLKNFQIKARNVKKKQQVFVSLFNENDGQEEQKDTKGKVGKKRRDRLKKAELTEKSDTTVTEETAEPPPAEQADVQDLKATIANDEEEDDEEFLVPKKKMKTAETVVTKRKEADVERTEKPKRPRKKMRRSGGRRLLKSMTVKMAGREFSRQRLQAYGLNPKRLHFRELYRQKRKEREKQEKQQKKSKQ
Protein: N-acetylmuramic acid 6-phosphate phosphatase (MurNAc 6-phosphate phosphatase) (MurNAc-6P phosphatase) (EC 3.1.3.105) (Q88M11)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Specifically catalyzes the dephosphorylation of N-acetylmuramate 6-phosphate (MurNAc-6P) to MurNac. Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc. Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc. Shows a very low activity on GlcNAc-6P, and neither alpha-1-phosphorylated MurNAc, GlcNAc, or glucose nor glucosamine-6P or glucose-6P can be used as a substrate.
Interaction partners:
- N-acetylmuramate/N-acetylglucosamine kinase
- N-acetylmuramate alpha-1-phosphate uridylyltransferase
- Ubiquinone biosynthesis O-methyltransferase
- Anhydro-N-acetylmuramic acid kinase
- Histidinol-phosphatase
- Ribulose-phosphate 3-epimerase
- Beta-hexosaminidase
Sequence:
MRLRAVLFDMDGTLLDTAPDFIAICQAMLAERGLPAVDDNLIRGVISGGARAMVATAFAMDPEADGFEALRLEFLERYQRDCAVHSKLFEGMAELLADIEKGNLLWGVVTNKPVRFAEPIMQQLGLAERSALLICPDHVKNSKPDPEPLILACKTLNLDPASVLFVGDDLRDIESGRDAGTRTAAVRYGYIHPEDNPNNWGADVVVDHPLELRKVIDSALCGC
Protein: Matrix metalloproteinase 1, isoform C (EC 3.4.24.-) (RE19818p) (RE62222p) (Q9W122)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tissue inhibitor of metalloproteinase
- Matrix metalloproteinase-2
- Furin-like protease 1, isoforms 1/1-X/2
- Low-density lipoprotein receptor-related protein
- Protein kinase C, brain isozyme
- Peptidase S1 domain-containing protein
- Neurogenic locus Notch protein
- protein-tyrosine-phosphatase
- palmitoyl-protein hydrolase
Sequence:
MTNCQSSVFIVVGTLFSIMAAAQSAPVSTTTQAEIYLSQFGYLPASARNPASSGLHDQRTWVSAIEEFQSFAGLNITGELDAETMKLMSLPRCGVRDRVGTGDSRSKRYALQGSRWRVKNLTYKISKYPKRLKRVDVDAEIGRAFAVWSEDTDLTFTRKTSGPVHIEIKFVESEHGDGDAFDGQGGTLAHAFFPVFGGDAHFDDAELWTIGSPRGTNLFQVAAHEFGHSLGLSHSDQSSALMAPFYRGFEPVFKLDEDDKAAIQSLYGRKTNQLRPTNVYPATTQRPYSPPKVPLDDSICKDSKVDTLFNSAQGETYAFKGDKYYKLTTDSVEEGYPQLISKGWPGLPGNIDAAFTYKNGKTYFFKGTQYWRYQGRQMDGVYPKEISEGFTGIPDHLDAAMVWGGNGKIYFFKGSKFWRFDPAKRPPVKASYPKPISNWEGVPNNLDAALKYTNGYTYFFKGDKYYRFHDARFAVDSATPPFPRPTAHWWFGCKNTPSSTGNIVEGSDNEFEQHSMIPHADDGNGDDFDAAVGDHQSNDEPIVPEVAERTGNGAMSQSKLTSSSAVSTVITTILMCLVSKLIVS
Protein: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB (Glycosyltransferase chaperone Gtf2) (Glycosyltransferase stabilizing protein GtfB) (Glycosyltransferase-stabilizing protein Gtf2) (A1C3M0)
Organism: Streptococcus parasanguinis
Function: Required for the polymorphic O-glycosylation of the serine-rich repeat protein Fap1. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export Fap1, a serine-rich fimbrial adhesin encoded upstream in the same operon. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-GlcNAc to Fap1, attaching the first sugar residue. Cannot use not UDP-Glc as substrate. Stabilizes the glycosylation activity of GtfA, causing it to partially localize to the cellular membrane where it is more protease resistant.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21862581}; Peripheral membrane protein {ECO:0000305|PubMed:21862581}.
Interaction partners:
Sequence:
MIRLFEWLTQESLDLHYSLEESGIHGTSIVLNDDGFLPEGIISPYTFFCEVEMDGSPLYFNQLEVPYLWQITGTNIEGEIWNRSSKRGVIHYHEPKYLRFVQSVDWLYPDGSIYMTDHYNKYGWAFARTYFFSDQQVSHKKYYTKSGQEVLSENILTGDILLNWKGKVYHFTKKVDFFLFYFKKSGLDLSSIWYNSLGMPFLISYYLGGEGRDILFWQENLADQLPGNMQIIFSGRTSRTKKVIVQDRSVYKKLLHLVEEKNKEMISFLNIIYPKLRENYSRKEILIVTNSDQIEGIETLTDNLSAYTFHIGALTSMSDKLQNIGQKENVLLYPNMSPKTMLDLLEQCDIYLDINHGNEVLSIVRLAFERSLLILAYDNTVHSPIFHHESGIFNHSKPQTLSDWLLNLDDYSQTVSCWRSDLFPMTYRDYKQVLVSNVD
Protein: Zinc finger X-linked protein ZXDB (P98169)
Organism: Homo sapiens (Human)
Function: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEIPKLLPARGTLQGGGGGGIPAGGGRVHRGPDSPAGQVPTRRLLLLRGPQDGGPGRRREEASTASRGPGPSLLAPRTDQPSGGGGGGGDDFFLVLLDPVGGDVETAGSGQAAGPVLREEAEEGPGLQGGESGANPAGPTALGPRCLSAVPTPAPISAPGPAAAFAGTVTIHNQDLLLRFENGVLTLATPPPHAWEPGAAPAQQPGCLIAPQAGFPHAAHPGDCPELPPDLLLAEPAEPAPAPAPEEEAEGPAAALGPRGPLGSGPGVVLYLCPEAQCGQTFAKKHQLKVHLLTHSSSQGQRPFKCPLGGCGWTFTTSYKLKRHLQSHDKLRPFGCPAEGCGKSFTTVYNLKAHMKGHEQENSFKCEVCEESFPTQAKLSAHQRSHFEPERPYQCAFSGCKKTFITVSALFSHNRAHFREQELFSCSFPGCSKQYDKACRLKIHLRSHTGERPFLCDFDGCGWNFTSMSKLLRHKRKHDDDRRFMCPVEGCGKSFTRAEHLKGHSITHLGTKPFVCPVAGCCARFSARSSLYIHSKKHLQDVDTWKSRCPISSCNKLFTSKHSMKTHMVKRHKVGQDLLAQLEAANSLTPSSELTSQRQNDLSDAEIVSLFSDVPDSTSAALLDTALVNSGILTIDVASVSSTLAGHLPANNNNSVGQAVDPPSLMATSDPPQSLDTSLFFGTAATGFQQSSLNMDEVSSVSVGPLGSLDSLAMKNSSPEPQALTPSSKLTVDTDALTPSSTLCENSVSELLTPTKAEWNVHPDSDFFGQEGETQFGFPNAAGNHGSQKETDLITVTGSSFLV
Protein: 75b (Tegument protein/FGARAT) (O41977)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Subcellular location: Virion tegument {ECO:0000256|ARBA:ARBA00004535}.
Interaction partners:
Sequence:
MDEDVWAIQVYARARTTLEEHVLNRLILSRTIHFPLRSTSICGVLTLTIRNSRTRNGRASSRRIRRWIQVAARLTCSDLTLDSTREPPDDGHGDAQRLDFIYGPFPGQRPLTWCNELTELLGYILPMGTTRMDYSRRICGIYTQPNAAILVMIELLYWFIYGRERTQLEYDHLSTFEPSSRLTSPTVLSSEPDAVHANIMLAQGLGRTTYANSLSTFPEAVPTMIKLTGSEMATCHHTTITGPGNFLHANLSSISNMPGVIPVAINGGSYLICNQTVGDNPLAPCILTMLLKARSDHLRASGVPVTGGFIRPISSNQLTFPTEVNFVNFISKLSKDDYVSHNRPADPCNTFIVAVGSFCPLYRPDGPPYGYDSSPLTVRKLTRVLQEWTKDLSHACYIRSMMPQVRCSIQEILTELLSPMGALIDINDLPDPVCHGLRNRTQEELERGIRTKFLNVTTDQVFLLVQNETGTIQETQESVGTIEHLINLCAKYEVACSIVGKCCTEPNLHIISSTSNPVAVTYDTADIMLTIPLDYDHGQTGGLAASAPRPSREDGALNWASLNLRQVWSDIITHPAVESKEYILTHIRRVANGRVVQQPGCGPFDFPVADHSLVSLNSIHNTKSWTSDLTVVTSSEMVNRIMSDPDIWFCDPSTSDVPRLECVASAIGEQHYKVKEDPILGSTYGLVEALLNLNTCPGATLEKTIITCSVTCSQADVAHSELYDAIAECKNMCTMMGCTFMCDMAAKNPRNCDINSPLIVFSAKCIVDFPWRGRIGPNLKEHHNTLLWLPIHSQPTLAGSIFKTFNPHVPIHRLPQISVNALFKLLTNTQKLFEQDKIRSIHDVSDGGLLTCVAEMAMSGGKSVVMTLPDHIANPKAMLLSETPGYVIEVDNDSTDAILTFLQENSCVAMPIGRVVPLTESSTFSVFHKSENLLSVPFFNVVGCWRRRHVDESTLLCTHLGPRRSIYAIEYGHNQFNFPGVSRYFLTSPVRSFRAPPHAQKRVCVIEFNGQTSLEGTLFMLQYAGFLPEIVHSSCLHDFETSLDRFCGIVFTGSMCTLHEHGGVLAAATRFTESHTVVSKLSAFCRRPDTFMLGFDQLGMQILLNLNILNITADKTMYDCKIDPLECMPLKKNASCTYESRWLNFYIPESNSLFFKPIQQNVFPSWIQGSNLGLPLDQHQESFWRNTRQICTYYQTEQPTPGIAAINYPRNPVAGSPVAGICSLDGRITGCLIDPAESFFPWTWQFVPGNRALASTPWQLCFQQLLIWTLSTDGL
Protein: Probable cationic amino acid transport integral membrane protein RocE (P71892)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Probable ornithine aminotransferase
- N
- Universal stress protein Rv2319c
- Probable ornithine aminotransferase
- Probable alpha-glucosidase AglA
- Trehalose synthase/amylase TreS
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
Sequence:
MPTTSMSLRELMLRRRPVSGAPVASGASGNLKRSFGTFQLTMFGVGATIGTGIFFVLAQAVPEAGPGVIVSFIIAGIAAGLAAICYAELASAVPISGSAYSYAYTTLGEAVAMVVAACLLLEYGVATAAVAVGWSGYVNKLLSNLFGFQMPHVLSAAPWDTHPGWVNLPAVILIGLCALLLIRGASESARVNAIMVLIKLGVLGMFMIIAFSAYSADHLKDFVPFGVAGIGSAAGTIFFSYIGLDAVSTAGDEVKDPQKTMPRALIAALVVVTGVYVLVALAALGTQPWQDFAEQETAGLAIILDNVTHGEWASTILAAGAVVSIFTVTLVTMYGQTRILFAMGRDGLLPARFAKVNPRTMTPVHNTVIVAIFASTLAAFIPLDSLADMVSIGTLTAFSVVAVGVIVLRVREPDLPRGFKVPGYPVTPVLSVLACGYILASLHWYTWLAFSGWVAVAVIFYLMWGRHHSALNEEVP
Protein: Spectrin repeat containing, nuclear envelope 2 (Syne2 protein) (Q6DFZ2)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus outer membrane {ECO:0000256|ARBA:ARBA00046312}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046312}.
Interaction partners:
Sequence:
GKGKLAADPLQHAKSKAALQAQLQDHKAFFQKLVADMLLIQTYSATMFPPSLQKGEGFGAEQVAEVRALEEEACLRGAQLQSMLQKWEEFDDNYASLEKDLEALISSLPSVSLVEETEERLLERISFYQQIKRNIDGKHARLCQTLNEGRQLAASVSCPEPEGQIARLEEQWLSLNKRIDQELHRLQTLLKHLLSYSRDSDELTRWLETSQQTLNYWKEQSLNVSQDLNTIRSNIDRFFKFSKEVDERSSLKSAVMSTGNQLLHLKEADTATLRASLAQFEQKWTVLITQLPDIQEKLHQLQMEKLPSREAISEMISWMNAVEPQAAGKDTELSKSSASQVKHLLQKLKEFRMEMDYKQWVVDFVNQSLLQLSTCDVESKRYERTEFAEHLGEMNRQWQRVHGTLNRKIQHLEQLLESITENENKVQNLNSWLEAQEERLKMLQKPESAVSMEKLLLDCQDIENQLALKSKALDELRQSSLTMDGGDVPLLEDMASGIVELFQKKNNVTSQVHQLRASVQSVLQEWKACDKLYDEATMRTTQLTYSMEHSKPAVLSLQALACQVQNLEALQDEAENGERSWEKLQEVIGRLKASCPSMAGIIEEKCQDAHSRWTQVNQDLADQLQEARGQLQLWKAPHNAHAEAAAWLQQQEAKFQQLANTNLSGDNLADILPRALKDIKGLQSDLQKTKEAFLENSTLSDQLPQPEERSTPGLHSGQRHSLQTAAYLEKMLLAKSNEFEIVLAQFKDFTDRLAYSKDLIVHKEENLNKLYHEEKEEVPDLFLNHVLALTAQSPDIERLNEESLRLPLSDVTIKTLQSLNRQWIRATATALDHYSELQGNGLNEKFLHYCERWIQVLEKIQESLSVEVAHSLPALLEQQKTYEILEAEVSTNQAVADAYVTQSLQLLDTAEIEKRPEFVSEFSKLSDQWQRAARGVRQRKCDISRLVTQWRFFTTSVEDLLRFLADTSQLLSAVKEQDCYSLCQTRRLVHELKSKEIHLQRWRTTYALALEAGEKLRNTPSPETREFVDGQISRLQESWKDTELSLGEVISRLQSTAETWDQCKKKIKKLKKRLQALKAQSEDPLPELHEALHEEKELIKEVEKSLANWTHSLKELQTMKADLSQHILAEDVTVLKEQIQLLHRQWEDLCLRVAIRKQEIEDRLNSWIVFNEKNKELCAWLVQMENKVLQTADVSIEEMIEKLQKDCMEEISLFTENKLQLKQMGDQLIKASSKAKAAELEEKLSKINDRWQHLFDVIGSRVKKLKETFAFIQQLDKNMSNLRTWLARIESELSKPVVYDVCDNQEIQKRLAEQQDLQRDIEQHSAGVESVFNICDVLLHDSDACANETECDSIQQTTRSLDRRWRNICAMSMERRMKIEETWRLWQKFLDDYSRFEDWLKSAERTAACPNSSEVLYTNAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDTASKLKQMVHEGNQRWDNLQKRVTAILRRLRYFTNQREEFEGTRESILVWLTEMDLQLTNVEHFSESDAEDKMRQLNGFQQEITLNTNKIDQLIVFGEQLIQKSEPLDAVLIEDELEELHRYCQEVFGRVSRFHRRLTSHTPGLDDEKEASENETDIEDPREIQADSWRKRRESEEPTSPQSLCHLVPPALGHERSGCETPVSVDSIPLEWDHTGDVGGSSSHEDDEEGPFYSALSDVEIPENPEAYLKMTTKSLQASSGKSISEGHPWHVPDSPSHSKHHYKHMEGDRTEAPVPTDASTPFKSDYVKLLLRQGTDDSKEGLKEAQQEDEQLATLTGQQPGAFDRWELIQAQELHSKLRLKQTVQQLKSDIGSIAAWLGKTEAELEALKLAEPPSDIQEIALRVKRLQEILKAFDTYKALMVSVNVSHKEYLPSQSPEATELQNRLHQLSLSWDSVQGVLDSWRGDLRQSLMQCQDFHQLSQDLLLWLATAESRRQKAHVTSPEADRQVLLECQKDLMRLEKELVARQPQVSSLREISSSLLVKGQGEDYIEAEEKVHVIEKKLKQLQEQVAQDLMSLQRSLDPDASLTSFDEVDSGEQLPAAFAKFGVEEEEEEEETDSRMPHLDSPGSSQPRRSFLSRVIRAALPLQLLLLLLLLLACLLPASEDDYSCTQANNFARSFYPMLRYTNGPPPT
Protein: Ecdysone-induced protein 63E, isoform G (Ecdysone-induced protein 63E, isoform I) (Ecdysone-induced protein 63E, isoform K (EC 2.7.11.22)) (Ecdysone-induced protein 63E, isoform L) (Serine/threonine protein kinase variant L63B1) (Serine/threonine protein kinase variant L63B4) (Serine/threonine protein kinase variant L63C1) (Serine/threonine protein kinase variant L63C2) (Q7KM03)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAELISQPTKINNNNFGAGVTMREKKGGALQKLKKRLSHSFGRLTISREDGDESTHHHHHHHHHRGGHGGHHNHGNKVPYNGYNSEEYLDRLEPNGNIPADKTNCRYGAQESAKNDNNKPQDWRSTDSTDHHDRVQRQLSVSSDSKLLDEDIREEMKYHSHVVMRPKKPPRPKSEVFLNKQETHPRRKRFSAFGGDSPFGKQEAYVKLEPLGEGSYATVYKGFSKLTYQRVALKEIRLQEEEGAPFTAIREASLLKELKHSNIVTLHDIVHTRETLTFVFEYVNTDLSQYMEKHPGGLDHRNVRLFLFQLLRGLSYCHKRRVLHRDVKPQNLLISDCGELKLADFGLARAKSVPSHTYSHEVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFVEMVTGMPTFPGIRDTYDQLDKIFKLLGTPTEDTWPGVTHFPGYKPHKLGFYRPRKLGHNFPRLYDIIEGETIANGFLQLNPEQRLGADDALQHPYFAQLPKKLYELPDETSIFTVEGVQLYTEPNRQNK
Protein: DNA-directed RNA polymerases II, IV and V subunit 3 (DNA-directed RNA polymerase II 36 kDa polypeptide A) (DNA-directed RNA polymerase II subunit RPB3-A) (RNA polymerase II subunit 3-A) (RNA polymerase II subunit B3-A) (Q39211)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. NRPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements.
Subcellular location: Nucleus.
Interaction partners:
- DNA-directed RNA polymerase II subunit 2
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerases II, IV and V subunit 9A
- DNA-directed RNA polymerases II and IV subunit 5A
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerases II, IV and V subunit 12
- DNA-directed RNA polymerase IV subunit 1
Sequence:
MDGATYQRFPKIKIRELKDDYAKFELRETDVSMANALRRVMISEVPTVAIDLVEIEVNSSVLNDEFIAHRLGLIPLTSERAMSMRFSRDCDACDGDGQCEFCSVEFRLSSKCVTDQTLDVTSRDLYSADPTVTPVDFTIDSSVSDSSEHKGIIIVKLRRGQELKLRAIARKGIGKDHAKWSPAATVTFMYEPDIIINEDMMDTLSDEEKIDLIESSPTKVFGMDPVTRQVVVVDPEAYTYDEEVIKKAEAMGKPGLIEISPKDDSFIFTVESTGAVKASQLVLNAIDLLKQKLDAVRLSDDTVEADDQFGELGAHMRGG
Protein: DnaJ homolog subfamily C member 30, mitochondrial (Williams-Beuren syndrome chromosomal region 18 protein homolog) (P59041)
Organism: Mus musculus (Mouse)
Function: Mitochondrial protein enriched in neurons that acts as a regulator of mitochondrial respiration. Associates with the ATP synthase complex and facilitates ATP synthesis. May be a chaperone protein involved in the turnover of the subunits of mitochondrial complex I N-module. It facilitates the degradation of N-module subunits damaged by oxidative stress, and contributes to complex I functional efficiency (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96LL9}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAAARCLGWTLSPLWRWWQVRGLPPSSATGLCSRGRTYSRTALYELLGVPSTATQAQIKAAYYRQSFLYHPDRNPGSAEAAERFTRVSEAYLVLGSTILRRKYDRGLLSDQDLRGPGVKPSKTPVADPAPPRPPPYTPRAPGGSRASPGDGRTMFDFDAFYQAHYGEQLERERRLRARREALRKKQENQANKGTSWDDTRDATFFVVLFLIFVFVGFRI
Protein: Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform (Phosphorylase kinase alpha M subunit) (P46020)
Organism: Homo sapiens (Human)
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Phosphorylase b kinase gamma catalytic chain, liver/testis isoform
- Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
- Calmodulin-1
- Phosphorylase b kinase regulatory subunit alpha, liver isoform
- Phosphorylase b kinase regulatory subunit beta
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 6
- Calmodulin-like protein 4
Sequence:
MRSRSNSGVRLDGYARLVQQTILCHQNPVTGLLPASYDQKDAWVRDNVYSILAVWGLGLAYRKNADRDEDKAKAYELEQSVVKLMRGLLHCMIRQVDKVESFKYSQSTKDSLHAKYNTKTCATVVGDDQWGHLQLDATSVYLLFLAQMTASGLHIIHSLDEVNFIQNLVFYIEAAYKTADFGIWERGDKTNQGISELNASSVGMAKAALEALDELDLFGVKGGPQSVIHVLADEVQHCQSILNSLLPRASTSKEVDASLLSVVSFPAFAVEDSQLVELTKQEIITKLQGRYGCCRFLRDGYKTPKEDPNRLYYEPAELKLFENIECEWPLFWTYFILDGVFSGNAEQVQEYKEALEAVLIKGKNGVPLLPELYSVPPDRVDEEYQNPHTVDRVPMGKLPHMWGQSLYILGSLMAEGFLAPGEIDPLNRRFSTVPKPDVVVQVSILAETEEIKTILKDKGIYVETIAEVYPIRVQPARILSHIYSSLGCNNRMKLSGRPYRHMGVLGTSKLYDIRKTIFTFTPQFIDQQQFYLALDNKMIVEMLRTDLSYLCSRWRMTGQPTITFPISHSMLDEDGTSLNSSILAALRKMQDGYFGGARVQTGKLSEFLTTSCCTHLSFMDPGPEGKLYSEDYDDNYDYLESGNWMNDYDSTSHARCGDEVARYLDHLLAHTAPHPKLAPTSQKGGLDRFQAAVQTTCDLMSLVTKAKELHVQNVHMYLPTKLFQASRPSFNLLDSPHPRQENQVPSVRVEIHLPRDQSGEVDFKALVLQLKETSSLQEQADILYMLYTMKGPDWNTELYNERSATVRELLTELYGKVGEIRHWGLIRYISGILRKKVEALDEACTDLLSHQKHLTVGLPPEPREKTISAPLPYEALTQLIDEASEGDMSISILTQEIMVYLAMYMRTQPGLFAEMFRLRIGLIIQVMATELAHSLRCSAEEATEGLMNLSPSAMKNLLHHILSGKEFGVERSVRPTDSNVSPAISIHEIGAVGATKTERTGIMQLKSEIKQVEFRRLSISAESQSPGTSMTPSSGSFPSAYDQQSSKDSRQGQWQRRRRLDGALNRVPVGFYQKVWKVLQKCHGLSVEGFVLPSSTTREMTPGEIKFSVHVESVLNRVPQPEYRQLLVEAILVLTMLADIEIHSIGSIIAVEKIVHIANDLFLQEQKTLGADDTMLAKDPASGICTLLYDSAPSGRFGTMTYLSKAAATYVQEFLPHSICAMQ
Protein: AMP deaminase, putative (EC 3.5.4.6) (Q381L1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Inosine-5'-monophosphate dehydrogenase
- Adenylosuccinate lyase
- Adenylosuccinate synthetase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Adenosine kinase
- Adenosine kinase
- Hypoxanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
Sequence:
MSDPTPLPMSGPVASPRDRSPTSIKTGPQPELSRTEQSAWQREKTAFNADAGRKNIRKNPSSRYQRVIIGEDDGDRDFAKCAEMIANVILARQKYKQRDKGEFDSLTKEGDEEESSDITPGDDETTLVFDRGVYRFGGMKTHVIPWETYVRDVRLVYSVIESGPCLSAARSRLLTLERKSQLFALLNWKIESNVDRPVCGDNMYVQCTRVDNALQLNTSVIAQVVLEFIISTATEQPRTPLFREKGKTVLLHEYLESHGVKDPRQLTVQGLGMHPPKYHNKFQQYDAFDSALNPGGRFATDLLQSFLSTNGSRDGDLLGSIIRPEFEQREFRGRQTFATEMQLKVYGHNAEELEKLAAWVSRQGFNSFTLNSWTICIPRTAPPEGPNMQPITCDTFSDQLKNIFYPMFMATLHPSEQRWVDVALLLKKTGSISILTGSQTQSQSITLDAVSPEQVKYTASISDCYFFYYIWSNLLALNCLRARYDLNTLNFSPSVFERAPMYEQLISSFLLGDVVYHANTLQSSWIMQYLFMYCRIGIVMSPLRDNALSMSYFDHPIVRYFLRGLVVSITTSDPLYVHHSINPLLEEYATLMKLFSMTPMAVYELSRNSVLNSNFPDAVKQKWLGDIFQHLEFGGGDVRRLGACDSRLQFRQECLVHEEAVLNLVLSQVAKKGEQPTRINMVTVTGAARTLDDDLQQLRNAKRANHTDWRVVFSRIDVTDGPTGFREREAVELLREIIVLRSKYVNPRVKYVDVKVEDVFNDSNFDESLWEYNNYYGVFLTCRSGLAPQWPSFIPPVKEFIRDVYTVRGAVMGHQKLRNLATQRLNLLERKFHLHLALNISKEAGKKEEKEWNNRDFFTAHKVDTNVQTAAGMNARTLLEFFVEKALHHGHDVVFEEDNQPVTLRQVLERHKINPTRITVDELNHLLNTNPQLRTTFLDPDNFMKGRYFAELTKRTLELYQEDAFSFSENRLVIGGKSKSEWALLAHWFDRYGMASRQNRWMISLPRCYRRLRQQGIVRNFGEYLDNIFQPLWEVSLHPAKDTRFHYFLTHVSGMDCVDDETKIDLPLTCKYPHDWNSELNPPYNMYLYYYWANITTLNQFRASRGLSTFAFRPQCGELGDIEHLIGGFLLADGINHGVTLRNNPVLEYMYYITQVGVAMSPLSNTAAASEYLLNPFPLFFRRGLNVSLATNQPLYFHFTREPLIEEYSIAAKLWKFEFNDLSEIARNSVLQSGFPHAWKKNALGNLYYLNSTLGNDARKSRVSDIRVAYRYEAYHEEMNFLSEQLDRDEKIPRAMTLLEEEIAVYEKETGKRVDMPSLLKLDDGSLPKDPPKTVARLREEVEYLQRKILHSNSVISTYRKENNCIVEHFNRIRSRLASSSFVVMGNLSRKYEQMDIESSDERGNVASLCNDESRDS
Protein: Ectonucleotide pyrophosphatase/phosphodiesterase family member 5 (E-NPP 5) (NPP-5) (EC 3.1.-.-) (Q9UJA9)
Organism: Homo sapiens (Human)
Function: Can hydrolyze NAD but cannot hydrolyze nucleotide di- and triphosphates. Lacks lysopholipase D activity. May play a role in neuronal cell communication.
Subcellular location: Secreted {ECO:0000305}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTSKFLLVSFILAALSLSTTFSLQPDQQKVLLVSFDGFRWDYLYKVPTPHFHYIMKYGVHVKQVTNVFITKTYPNHYTLVTGLFAENHGIVANDMFDPIRNKSFSLDHMNIYDSKFWEEATPIWITNQRAGHTSGAAMWPGTDVKIHKRFPTHYMPYNESVSFEDRVAKIIEWFTSKEPINLGLLYWEDPDDMGHHLGPDSPLMGPVISDIDKKLGYLIQMLKKAKLWNTLNLIITSDHGMTQCSEERLIELDQYLDKDHYTLIDQSPVAAILPKEGKFDEVYEALTHAHPNLTVYKKEDVPERWHYKYNSRIQPIIAVADEGWHILQNKSDDFLLGNHGYDNALADMHPIFLAHGPAFRKNFSKEAMNSTDLYPLLCHLLNITAMPHNGSFWNVQDLLNSAMPRVVPYTQSTILLPGSVKPAEYDQEGSYPYFIGVSLGSIIVIVFFVIFIKHLIHSQIPALQDMHAEIAQPLLQA