wanglab/gogpt-training-data huggingface dataset:
Protein: MIP13269p (A1Z763)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable RNA-binding protein CG14230
- FI05230p
Sequence:
MPICKSSPGTASNKTATDISADHVTEAAQVKRTREQAYFNSYDFDAIEVLPYEEEDDEAGGTSHSRSRSRSQSRSQSRCGSSSSRSSSTRSYSAAKEPVAGHKFAYLQRLGAFFARNGGGAGESGSGEAAGIAAPSGGGASNAAPKGSSENFLLPRAMLKYQSTATASASPSSTSTAAVAMPLKNGLANGMGNAIGHDQQLEATGSAGERSKKCSIASNVSSTHSTDSGLPVAAAAVSASASASAAASATAATSAAAAAAAAQAARGGGGDGGGSHYSTDKSGSSGYYSSNVCSTYSLDEHIYCEPVIDVQEKIKSVAARQRQRPPLQLPTKVGAPQEAPSIDPPEGSSEKLSAVKSQRSDMQDAAGAAASNSHQTQSKAEAAEGLHHYSKKLRVLETSIENLDRHLKTFPSLYAQEHIVSFMQVAGARNEGPPQALDIGEKLRVYNQLPTIMEQQQQQQQEQMVDDSLLDIDLDAFLLAPNAGHRGIDNPSFLNDEQLAENNYKCAKYINSCPEDAYRLESERGGAGGPGVGVAEETYVKRYEDQLHFQNTRELLEDVRDKIRLLSRATPPTSGTPTPASTPPSDVPKELEGMIHTLKHELESYLQRMNQHSELELRQLCSGLGRQQHVVRMQNALERRRSCADLQLNAYEAVRDGVLISANGRPLSVREQIMTIRCASDPNFKMKRKSIAEIFPAAECYVESEVTTTSLSRSATPSPASTPQLELEALHPGLATTTIVTQMQRNLTFHKPILAVSNSNPGGGNVTVDGAGGNKAERDRERESLAEWHRKKPSIWEMYYGTNRLHQSLLGKQRGGGELVISSAQPTLSYPSSRPESDFTLDLPRAEQLRLKMEKEKKFRQRCRFITTFLSLVFFLLTVMVVSLVLTRGKRMFGSMI
Protein: Killer cell lectin-like receptor 7 (Lymphocyte antigen 49g) (Ly-49g) (T-cell surface glycoprotein Ly-49G) (Q60654)
Organism: Mus musculus (Mouse)
Function: Receptor on natural killer (NK) cells for class I MHC.
Subcellular location: Membrane; Single-pass type II membrane protein.
Interaction partners:
- H-2 class I histocompatibility antigen, D-B alpha chain
- Killer cell lectin-like receptor subfamily B member 1C
- Killer cell lectin-like receptor 8
- Natural cytotoxicity triggering receptor 1
- T-cell surface glycoprotein YE1/48
- Natural killer cells antigen CD94
- Killer cell lectin-like receptor subfamily E member 1
- NKG2-D type II integral membrane protein
Sequence:
MSEQEVTYSTVRFHESSRLQKLVRTEEPQRPREACYREYSVPWKLIVIACGILCFLLLVTVALLAITIFQHSQQKHELQETLNCHDNCSPTQSDVNLKDELLRNKSIECRPGNDLLESLSRDQNRWYSETKTFSDSSQHTGVHERPISKAEGKGRGFEKYWFCYGIKCYYFNMDRKTWSGCKQTCQISSLSLLKIDNEDELKFLQNLAPSDISWIGLSYDNKKKDWVWIDNGPSKLALNTTKYNIRDGLCMSLSKTRLDNGDCDKSYICICGKRLDKFPH
Protein: Homeobox protein Hox-D8 (Homeobox protein Hox-4.3) (Homeobox protein Hox-5.4) (P23463)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-D4
- Homeobox protein Hox-D9
Sequence:
MSSYFVNPLYSKYKAAAAAAAAAAAAAAGEAINPTYYDCHFAPEVSGRHAAALQLYGNSAAGFPHAHPHPHPHPSPPPGCGGGGGPGPGQDYFHAGAGSPTAAYQAAPPPPHPPPPPPPPPCGGIACHGEPAKFYGYDNLQRQPIFTTQQEAELVQYPDCKSSSGNIGEDPDHLNQSSSPSQMFPWMRPQAAPGRRRGRQTYSRFQTLELEKEFLFNPYLTRKRRIEVSHTLALTERQVKIWFQNRRMKWKKENNKDKFPASRPEAKDGDPKKEVSGLEEDGAEGCPTN
Protein: Metal-binding domain-containing protein (Q4GZE3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAMRSNFLCRLEVYRGPNECTLRSFSIEEAPSTILEMVNLLKSYDLRLQHGTFELTAAHGQDEAPRKLLSDDDVVAFFSVHSCPCFVFTAVIDHCDSGVGSSMLVDDPLVLLSIQHSDGGVPTTKRFIPPRREIWKALLVAVRGAIQQVLLPGQQLTLFSTEGNGKALTEICSEEAAALLIRSCMAQRSVCHLTYNIGRGDTGAKVVGATLAEVDKKEDKNKVPISTKNDNDQLPTCAVVNARSKNMDQNLPPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAETVKPVAVPEPAKAEIVEKPNLSLAVSVFLKDRDPNAFAMKKSPALRDSEIGSGRLLEPLFTKDVLVGEGNAASRPWNNAKVLPTGFKGGDGDAVTAKNGKGADESPLTSKNATECISGKKNCSDVEEELPNEVVVEVACSLEKKAPVRFFLTWKKASPKVFESFRNECLNALHLTDMDNIIIYDSNGVPLCNPSGVTAMVGEAIRKKRSCINVTAVRGHPCTSGLPLQCLFTWGTQQVMRALVLRPGCALEDMRSALAEECGLKEKDMGELSFRLVERGELDDMELTPDNVYKELKRVAENSCVVRIAILDRRRTSLIAFVVRTLCDAASAFAAEVEHVFGGHFTEMDVVPILTRCCDLSPLEGDVKRYVDAVISNLEGSQVLRSDNVVKAVLDPVSICGEEVALSFLNRCIAVTELMSSHRPFEVLMRFFRRLYRSIEYPERTESGVPLNVVTRQLAYAGLSDARWLLFRDQPFSSVVHEKDFVEMLQRVYAGNPSLVCRVAVACRLSGISSLKSRRVMAKEERDVRRQHCRKEIAHAFDGIRPDEVMAYIHHYRLHGKPNHCCLLGTVSTLLANCSERLSSQWFVERVTQRCSVTMETMLQNFEDAQIPLPLLYQLCWDVLRPELHHLTLLPESHVASAFAYWAMFAVQLLCINRNLEFPPVPLVDLKEFTWVVPEKASADTVTDEADGAVAIALPTPQPAGVAKKKIKYKYSYLCHDLRRDQRFLPMIR
Protein: G_PROTEIN_RECEP_F1_2 domain-containing protein (Q564X8)
Organism: Caenorhabditis elegans
Interaction partners:
- Clc-like protein
- G-protein coupled receptors family 1 profile domain-containing protein
- Serpentine receptor class r-10
- Innexin-19
Sequence:
MNIVSFTSHLCASTNEETTEKSGRKSPKSPIECRKLSKAPPLCCKNGEECKVAGNCVCKPPKPTGPNDEKPTSSRETYDVFLGGSCGTTVWRRQSVIPFLKKRGITYYDPQRSFWSENMIYEESIAKESSSLFLFVIDPATVNATSFLEIAYFAARKSPKLVVVFLGKTEWAEKAHPDDLPDRNRTCQLLDRILECHQVPMLHTIPDALEFIEEEMLGRQSLTEAMRSKNNRLPYLQIRARRVVRNVKSLAAQTIKVCKNYATKTVVTGLIDLTVLLSISFAFPALPLFYILVPLLMLNIVFFGVIYKVQELRKRYPRMIADSSAVMYHATAAIPSPRVTLKATNVNGTISSKTLVRRRSKQNFEKFFPDDSGASSFIVPSSFLPKQHETKVNIDCSVVELCSSSPDDNSWVQELAAPTLDGKGTPYSYVLATPNFQLDNRMNCLRTWFHHHKKFFYYIPSTTTFLSGMVEIAYILGHTNWEGTVCVPATSQILEGPDDMTADEKDHARAARRRRNDCYQIAFCYLKDMAKRRQCRVFTDIGVAVKALVDPAIRGV
Protein: Neuronal vesicle trafficking-associated protein 2 (Neuron-specific protein family member 2) (Protein 8.5) (Protein p19) (P47759)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q3KR51}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q3KR51}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q3KR51}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3KR51}. Endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Early endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Late endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Lysosome lumen {ECO:0000250|UniProtKB:Q3KR51}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:7829526}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:7829526}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:7829526}. Note=Endocytosed from the cell surface, thus entered into early endosomes, trafficks to late endosomes and degradates in lysosomes (By similarity). Mainly Golgi stack, but also found in small vacuolar organelles and multivesicular bodies (PubMed:7829526). Found in both stationary and motile endosomes (PubMed:28874679). {ECO:0000250|UniProtKB:Q3KR51, ECO:0000269|PubMed:28874679, ECO:0000269|PubMed:7829526}.
Interaction partners:
Sequence:
MVKLNSNPGEKGAKPPSVEDGFQTVPLITPLEVNHLQLAAPEKVIVKTRTEYQPEQRNKGKFRVPKIAEFTVTILVSLALAFLACIVFLVVYKAFTYDHSCPEGFVYKHKRCIPASLDAYYSSQDPSSRSRFYTVISHYSVAKQSTARAIGPWLSAAAVIHEPKPPKTQGH
Protein: Cellulose synthase catalytic subunit [UDP-forming] (EC 2.4.1.12) (P37653)
Organism: Escherichia coli (strain K12)
Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cellulose and thin aggregative fimbriae (curli fimbrae or fibers) leads to a hydrophobic network with tightly packed cells embedded in a highly inert matrix that confers cohesion, elasticity and tissue-like properties to colonies.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cyclic di-GMP-binding protein
- Endoglucanase
- Probable diguanylate cyclase DgcC
- Cellulose synthase operon protein C
- Probable cyclic di-GMP phosphodiesterase PdeD
- Cyclic di-GMP binding protein BcsE
- Cellulose biosynthesis protein BcsG
- UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Cellulose biosynthesis protein BcsF
Sequence:
MSILTRWLLIPPVNARLIGRYRDYRRHGASAFSATLGCFWMILAWIFIPLEHPRWQRIRAEHKNLYPHINASRPRPLDPVRYLIQTCWLLIGASRKETPKPRRRAFSGLQNIRGRYHQWMNELPERVSHKTQHLDEKKELGHLSAGARRLILGIIVTFSLILALICVTQPFNPLAQFIFLMLLWGVALIVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPSVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQNVGVKYIARTTHEHAKAGNINNALKYAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKQLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLTGKGLKFAQRLCYVNAMFHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHASLTNSKIQGKYRHSFWSEIYETVLAWYIAPPTLVALINPHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVGIWRYFYGPPTEMLTVVVSMVWVFYNLIVLGGAVAVSVESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKINGQAQILEGQKVNLLLKRGQQEYVFPTQVARVMGNEVGLKLMPLTTQQHIDFVQCTFARADTWALWQDSYPEDKPLESLLDILKLGFRGYRHLAEFAPSSVKGIFRVLTSLVSWVVSFIPRRPERSETAQPSDQALAQQ
Protein: Arogenate dehydratase 4, chloroplastic (AtADT4) (EC 4.2.1.91) (O22241)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19136569}.
Interaction partners:
- Arogenate dehydrogenase 1, chloroplastic
- Chorismate mutase 3, chloroplastic
- Chorismate mutase 1, chloroplastic
- Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
- Chorismate mutase 2
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Arogenate dehydrogenase 2, chloroplastic
- Probable aminotransferase TAT1
- Tyrosine aminotransferase
- Probable aminotransferase TAT4
Sequence:
MQAATSCDLKFRSTDPTSRNKCFSHAIPKRVAVTCGYRSESFSFPNGVSVSRSDWQSSCAILSSKVASVENTGGLADKIAAVNGHTNGSVNLGLVAVESTNGKLAPAQPLTITDLSPAPLHGSSLRVAYQGVPGAYSEAAAGKAYPNCDAIPCDQFDVAFQAVELWIADRAVLPVENSLGGSIHRNYDLLLRHRLHIVGEVQIPVHHCLLALPGVRTDCVSRVISHPQALAQTEHSLDVLTPHAAREAFHDTAAAAEYISANDLHDTAAVASARAAELYNLQILADGIQDDPGNVTRFLMLAREPIIPRTDRPFKTSIVFAAQEHKGTSVLFKVLSAFAFRDISLTKIESRPHHNRPLRVVGDGSFGTSKNFEYMFYVDFEASMAEPRAQNALAEVQEYTSFLRVLGSYPMDMTPWSMTSTEEA
Protein: 2'-5'-oligoadenylate synthase-like protein 1 (2',5'-oligoadenylate synthetase-like 9) (Q8VI94)
Organism: Mus musculus (Mouse)
Function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity via an alternative antiviral pathway independent of RNase L.
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Antiviral innate immune response receptor RIG-I
- 2'-5'-oligoadenylate synthase-like protein 2
- Ubiquitin-like protein ISG15
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon regulatory factor 7
- Antiviral innate immune response effector IFIT1
- Interferon-induced protein 44
- Ubl carboxyl-terminal hydrolase 18
- Interferon-induced protein with tetratricopeptide repeats 2
Sequence:
MAVAQELYGFPASKLDSFVAQWLQPTREWKEEVLETVQTVEQFLRQENFREDRGPARDVRVLKVLKVGCFGNGTVLRSTTDVELVVFLSCFHSFQEEAKHHQAVLRLIQKRMYYCQELMDLGLSNLSVTNRVPSSLIFTIQTRETWETITVTVVPAYRALGPSCPSSEVYANLIKANGYPGNFSPSFSELQRNFVKHRPTKLKSLLRLVKHWYQQYVRDKCPRANLPPLYALELLTVYAWEAGTREDANFRLDEGLATVMELLQDHELLCIYWTKHYTLQHPVIEACVRRQLRGQRPIILDPADPTNNVAEGYRWDIVAQRANQCLKQDCCYDNRDSPVPSWRVKRAPDIQVTVQEWGHSDLTFWVNPYEPIKKLKEKIQLSQGYLGLQRLSFQEPGGERQLIRSHCTLAYYGIFCDTHICLLDTISPEIQVFVKNPDGRSHAYAIHPLDYVLNLKQQIEDRQGLRCQEQRLEFQGHILEDWFDFKSYGIQDSVTVILSKTTEGAAPFVPS
Protein: Zinc finger protein 161 (Q8CGQ6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEFFISMSETIKYNDDDHKTLFLKTLNEQRLEGEFCDIAIVVEDVKFRAHRCVLAACSTYFKKLFKKLEVDSSSVIEIDFLRSDIFEEVLNYMYTAKISVKKEDVNLMMSSGQILGIRFLDKLCSQKRDVSSPDESNGQSKSKYCLKLNRPIGDAADAQDDDVEEIGDQDDSPSDDTVEGTPPSQEDGKSPTTTLRVQEAILKELGSEEVRKVNCYGQEVESMETPESKDLGSQTPQALTFNDGMSEVKDEQTPGWTTAASDMKFEYLLYGHHREQIACQACGKTFSDEGRLRKHEKLHTADRPFVCEMCTKGFTTQAHLKEHLKIHTGYKPYSCEVCGKSFIRAPDLKKHERVHSNERPFACHMCDKAFKHKSHFKDHERRHRGEKPFVCGSCTKAFAKASDLKRHENNMHSERKQVTPSAIQSETEQLQAAAMAAEAEQQLETIACS
Protein: UDP-glucuronosyltransferase 2B1 (UDPGT 2B1) (UGT2B1) (EC 2.4.1.17) (UDPGTr-2) (P09875)
Organism: Rattus norvegicus (Rat)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of the endogenous estrogen hormone estradiol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:3084479}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2C70
- Murinoglobulin-1
- Aldo-keto reductase family 1, member C1
- Cytochrome P450 1A1
- Complement component C9
- Alanine--glyoxylate aminotransferase
- Cytochrome P450 2E1
- Transmembrane O-methyltransferase homolog
- Beta-glucuronidase
Sequence:
MSMKQTSVFLLIQLICYFRPGACGKVLVWPTEYSHWINIKIILNELAQRGHEVTVLVSSASILIEPTKESSINFEIYSVPLSKSDLEYSFAKWIDEWTRDFETLSIWTYYSKMQKVFNEYSDVVENLCKALIWNKSLMKKLQGSQFDVILADAVGPCGELLAELLKTPLVYSLRFCPGYRCEKFSGGLPLPPSYVPVVLSELSDRMTFVERVKNMLQMLYFDFWFQPFKEKSWSQFYSDVLGRPTTLTEMMGKADIWLIRTFWDLEFPHPFLPNFDFVGGLHCKPAKPLPREMEEFVQSSGEHGVVVFSLGSMVKNLTEEKANVVASALAQIPQKVVWRFDGKKPDTLGSNTRLYKWIPQNDLLGHPKTKAFVAHGGTNGIYEAIYHGIPIVGIPLFADQPDNINHMVAKGAAVRVDFSILSTTGLLTALKIVMNDPSYKENAMRLSRIHHDQPVKPLDRAVFWIEYVMRHKGAKHLRSTLHDLSWFQYHSLDVIGFLLLCVVGVVFIITKFCLFCCRKTANMGKKKKE
Protein: Inositol polyphosphate 1-phosphatase (EC 3.1.3.57) (RE60387p) (Q9VFP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Inositol-1-monophosphatase
- Inositol-1-monophosphatase
- Inositol-1-monophosphatase
- Inositol-1-monophosphatase
- Inositol-1-monophosphatase
- inositol-phosphate phosphatase
- phosphatidylinositol-3,4-bisphosphate 4-phosphatase
- LD06095p
- Uncharacterized protein, isoform C
- Putative inositol monophosphatase 3
Sequence:
MSGVEEQASLLRVLINCAEKAANIARICRSNEQLLALLVQEKIGSEANERFEHDFKTLADVLIQETIKHEVGALFPAMKDAILGEESPNFTNQLGESVTIAVGATEEDTAACLQAVLSGHEDAASALATEVHRDVSFSSEKLGEIAQLPDELDYGNLGIWIDPIDATAEYISGDTMFTDFPGITSTGLDCVTVLIGVYERDTGVPVMGVVAQPFGEKLEENVYSSSMFWGVCLPTVRAHNCDFEARDENRRLGIFSSSEQSDILQRFLDLGYEFAFSAGAGHKALKVITHEVDVYLLSKGSTFKWDTCAPQAILRALGGDVLDYAASVAEQKAVPLKYLIEDAEADADWKRNAGGIISVRNVDVVDELLAKLAEQ
Protein: Acyl-Coenzyme A dehydrogenase family, member 12 (D3Z2B3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MWVRRLFQPSTLHWAWRTTALNHPLGRHQGGLRWTHSGGRSYRAVIFDTGGVLVPSPGTVAVGQASSATAQQSGKLTESMAELAWDFATKEGFRVFKEMPATKTLSRSYHAWAGPRSPRTPKGVRGHSTVAAASPSHEAKGGLVISPEGLSPAVRKLYEQLVQFIEQKVYPLEPELQRHQASANRWSPSPLIEDLKEKAKAEGLWNLFLPLETDPEKKYGAGLTNVEYAHLCEVMGMSLYASEIFNCSVPDMGTMEILVRYGTEEQKARWLVPLLEGRIHSCFAMTDRKVASSDASNIEASIKEEDNSYVINGHKWWTSGILHPHCKLCVFMGKTDPQAPRHQQQSMLLVPMDSPGITVIRPLSVFGLEDPPG
Protein: DUF3456 domain-containing protein (Q385Q0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQRHSSHLLLLLVAVVIPVCSEDKLDFTKLRDPFDMDEINRKLQEKVADDDPVQKAMPDPMDPKFRAPLRCSACGAVIEHAVRLLRPIIERQSERAARSGGVLPADALPKEYEMVDIFENLCGEVGRLYGLEVEKDKKRPTLRFSKSFGVSRLQGAWMPSFLTSTCEGVLDVEGEEKLAAMILGVARSEAEAGRGKVISMNPDQGIVDKVREMVCTKWEESAKGCDAYGVAIDPRETDNDDGAEEAASDL
Protein: Nucleoporin (Q383V1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MERLMEGSENVKEALLQCIAKSDTCAADGVLPLLRTFSRPVSKTPFFDVQVETEHAWPSSNLLNGGGRCKVHYRNGAHLVSSGNRLLVVRQDNHFYFPPWGSLIQDAYIQRCGADKRSLIIVGLANGIHAALLQEESPPVVLDDIFIETGRSVEKIVSFENGKLTLCYGNAQVESCRLVFRGDKVSEMVLSLNQRPRRIYDAVISLWDTKRYQDSAYDPYRGNLFVLSNTDLAVWKRTLTGEFVVAGSVAVLRNTVTVLASFETSHHAVLIAADGGRQPVLLDEAPAAGGGTACVNVRLASSRPLPSGLHVEDIRFACRDTNGTTLLYDALTHLLILITTNCAVYEGVYDEMELVSTFQLDGPITGIGYVSESVRFGTSFVVYGGSGIQCRIGALPIGLVTANLLKLGNPHDEIFSSLLKLGGRRGMEALVGANLAGVPAETLAPLLGQFLHPFPQSNNMRVAPGAEGLLYLVHRQIVVAERLWTSPFSWDLALRLEGAVKLMEEWRGSIESLLRLNGWLDYPVQHMGLVWQGFVVSSPQAFTTRTAINTQALFLYTLLKGLGDACIICKLYCMLLTACGEEALSMASSIGNQMGLEHIVWRCDTDAIISEFCTTALACNGANTLAQLEAMKHALPVKAQHAISVHSLIMKGNADEALTYACDNIVSLRDEQMVSYVEERLNVAFPDHMVPIRLLLCWLRHDKSSIGELLSLLEQNTADGSPEQVKRCLRLVMQAAARSPALSRDVVHWIVGHALEDDRLMCFAEIIEEYIDDLGEPQTLPALFYSCWKDRLRCPQVAARGFGDIAKSKQRVLLSTRLRCINLALEYGPTDSDRLTYVLLLLQDELVKVIERTGQSFNYNSSSKLPRQETQSHVDELRHFYVVESRLFELAGVYRRNGGAKVQMDILKMHPETPERVTVQVLHDLLASLVHEGGQGASEAVRCIVREYYGGYAAGLPLLPFVTFLVHNREDPGTIVDTLRSSGVPAAVVFDTFLHCLDDRCDDTVLTKSGVITALTAAVTNMVGEGRSVYATYLLERIHKLLENEHQIALLRRSDVEQLQNAEAAMMRFVSSSQSVS
Protein: MAP kinase-activating death domain protein (A0A0A0MRB5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVQKKKFCPRLLDYLVIVGARHPSSDSVAQTPELLRRYPLEDHTEFPLPPDVVFFCQPEGCLSVRQRRMSLRDDTSFVFTLTDKDTGVTRYGICVNFYRSFQKRISKEKGEGGAGSRGKEGTHATCASEEGGTESSESGSSLQPLSADSTPDVNQSPRGKRRAKAGSRSRNSTLTSLCVLSHYPFFSTFRECLYTLKRLVDCCSERLLGKKLGIPRGVQRDTMWRIFTGSLLVEEKSSALLHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQELQPALTFALPDPSRFTLVDFPLHLPLELLGVDACLQVLTCILLEHKVVLQSRDYNALSMSVMAFVAMIYPLEYMFPVIPLLPTCMASAEQLLLAPTPYIIGVPASFFLYKLDFKMPDDVWLVDLDSNRVIAPTNAEVLPILPEPESLELKKHLKQALASMSLNTQPILNLEKFHEGQEIPLLLGRPSNDLQSTPSTEFNPLIYGNDVDSVDVATRVAMVRFFNSANVLQGFQMHTRTLRLFPRPVVAFQAGSFLASRPRQTPFAEKLARTQAVEYFGEWILNPTNYAFQRIHNNMFDPALIGDKPKWYAHQLQPIHYRVYDSNSQLAEALSVPPERDSDSEPTDDSGSDSMDYDDSSSSYSSLGDFVSEMMKCDINGDTPNVDPLTHAALGDASEVEIDELQNQKEAEEPGPDSENSQENPPLRSSSSTTASSSPSTVIHGANSEPADSTEMDDKAAVGVSKPLPSVPPSIGKSNVDRRQAEIGEGSVRRRIYDNPYFEPQYGFPPEEDEDEQGESYTPRFSQHVSGNRAQKLLRPNSLRLASDSDAESDSRASSPNSTVSNTSTEGFGGIMSFASSLYRNHSTSFSLSNLTLPTKGAREKATPFPSLKGNRRALVDQKSSVIKHSPTVKREPPSPQGRSSNSSENQQFLKEVVHSVLDGQGVGWLNMKKVRRLLESEQLRVFVLSKLNRMVQSEDDARQDIIPDVEISRKVYKGMLDLLKCTVLSLEQSYAHAGLGGMASIFGLLEIAQTHYYSKEPDKRKRSPTESVNTPVGKDPGLAGRGDPKAMAQLRVPQLGPRAPSATGKGPKELDTRSLKEENFIASIGPEVIKPVFDLGETEEKKSQISADSGVSLTSSSQRTDQDSVIGVSPAVMIRSSSQDSEVSTVVSNSSGETLGADSDLSSNAGDGPGGEGSVHLASSRGTLSDSEIETNSATSTIFGKAHSLKPSIKEKLAGSPIRTSEDVSQRVYLYEGLLGKERSTLWDQMQFWEDAFLDAVMLEREGMGMDQGPQEMIDRYLSLGEHDRKRLEDDEDRLLATLLHNLISYMLLMKVNKNDIRKKVRRLMGKSHIGLVYSQQINEVLDQLANLNGRDLSIWSSGSRHMKKQTFVVHAGTDTNGDIFFMEVCDDCVVLRSNIGTVYERWWYEKLINMTYCPKTKVLCLWRRNGSETQLNKFYTKKCRELYYCVKDSMERAAARQQSIKPGPELGGEFPVQDLKTGEGGLLQVTLEGINLKFMHNQVFIELNHIKKCNTVRGVFVLEEFVPEIKEVVSHKYKTPMAHEICYSVLCLFSYVAAVHSSEEDLRTPPRPVSS
Protein: Phosphocarrier protein HPr (Histidine-containing protein) (O50515)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain.
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphoenolpyruvate-protein phosphotransferase
- Fructose-specific permease
- PTS system sugar phosphotransferase component IIA
- PTS system N-acetylglucosamine-specific EIIC component
- PTS transmembrane component
- Sugar phosphotransferase
- Ascorbate-specific PTS system EIIA component
- Ascorbate-specific PTS system EIIC component
- 1-phosphofructokinase
- Small ribosomal subunit protein uS7
Sequence:
MAERRVNVGWAEGLHARPASIFVRAATATGVPVTIAKADGSPVNAASMLAVLGLGAQGGEEIVLASDAEGAEAALERLAKLVAEGLEELPETV
Protein: Pyruvate dehydrogenase E1 component subunit alpha (EC 1.2.4.1) (Q5JPU2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MRKMLAAVSRVLSGASQKPFAGSPPPRHLTVGRKLSSRYEVTFESAQASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS
Protein: Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A (EC 2.8.3.5) (Succinyl-CoA:3-oxoacid CoA-transferase) (OXCT A) (P56006)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Succinyl-CoA:3-ketoacid coenzyme A transferase subunit B
- Acetyl coenzyme A acetyltransferase
- Conserved hypothetical integral membrane protein
Sequence:
MNKVITDLDKALSALKDGDTILVGGFGLCGIPEYAIDYIYKKGIKDLIVVSNNCGVDDFGLGILLEKKQIKKIIASYVGENKIFESQMLNGEIEVVLTPQGTLAENLHAGGAGIPAYYTPTGVGTLIAQGKESREFNGKEYILERAITGDYGLIKAYKSDTLGNLVFRKTARNFNPLCAMAAKICVAEVEEIVPAGELDPDEIHLPGIYVQHIYKGEKFEKRIEKITTRSTK
Protein: Beta-caryophyllene synthase (EC 4.2.3.57) (Q8SA63)
Organism: Artemisia annua (Sweet wormwood)
Function: Sesquiterpene synthase involved in the biosynthesis of beta-caryophyllene, a sesquiterpene with anti-inflammatory and anti-carcinogenic activities. Can use farnesyl diphosphate and (+)-chrysanthemyl diphosphate as substrates, but not geranylgeranyl diphosphate. Produces two irregular monoterpenes, yomogi alcohol and artemisia alcohol from (+)-chrysanthemyl diphosphate. Limited activity with geranyl diphosphate, leading to the production of limonene, terpinolene, beta-pinene, gamma-terpinene, alpha-terpinene and other minor products.
Interaction partners:
Sequence:
MSVKEEKVIRPIVHFPPSVWADQFLIFDDKQAEQANVEQVVNELREDVRKDLVSSLDVQTEHTNLLKLIDAIQRLGIAYHFEEEIEQALQHIYDTYGDDWKGRSPSLWFRILRQQGFYVSCDIFKNYKKEDGSFKESLTNDVEGLLELYEATYLRVQGEGVLDDALVFTRTCLEKIAKDLVHTNPTLSTYIQEALKQPLHKRLTRLEALRYIPMYEQQASHNESLLKLAKLGFNLLQSLHRKELSEVSRWWKGLDVPNNLPYARDRMVECYFWALGVYFEPKYSQARIFLAKVISLATVLDDTYDAYGTYEELKIFTEAIQRWSITCIDMLPEYLKLLYQGVLDIYIEMEEIMGKEGKAHHLSYAKESMKEFIRSYMMEAKWANEGYVPTAEEHMSVAFVSSGYSMLATTCFVGMGDIVTDEAFKWALTKPPIIKASCAIARLMDDIHSQKEEKERIHVASSVESYMKQYDVTEEHVLKVFNKKIEDAWKDITRESLVRKDIPMPLMMRVINLAQVMDVLYKHKDGFTNVGEELKDHIKSLLVHPIPI
Protein: Apoptosis inhibitor 5 (API-5) (AAC-11) (O35841)
Organism: Mus musculus (Mouse)
Function: Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly nuclear.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB2
- Fibroblast growth factor 2
Sequence:
MPTVEELYRNYGILADATEQVGQHKDAYQVILDGVKGGTKEKRLAAQFIPKFFKHFPELADSAINAQLDLCEDEDVSIRRQAIKELPQFATGENLPRVADILTQLLQTDDSAEFNLVNNALLSIFKMDAKGTLGGLFSQILQGEDIVRERAIKFLSTKLKTLPDEVLTKEVEELILTESKKVLEDVTGEEFVLFMKILSGLKSLQTVSGRQQLVELVAEQADLEQAFSPSDPDCVDRLLQCTRQAVPLFSKNVHSTRFVTYFCEQVLPNLSTLTTPVEGLDIQLEVLKLLAEMSSFCGDMEKLETNLRKLFDKLLEYMPLPPEEAENGENAGNEEPKLQFSYVECLLYSFHQLGRKLPDFLTAKLNAEKLKDFKIRLQYFARGLQVYIRQLRLALQGKTGEALKTEENKIKVVALKITNNINVLIKDLFHIPPSYKSTVTLSWKPVQKVEIGQKRTSEDTSSGSPPKKSPGGPKRDARQIYNPPSGKYSSNLSNFNYERSLQGK