wanglab/gogpt-training-data huggingface dataset:
Protein: Copper chaperone for superoxide dismutase (Superoxide dismutase copper chaperone) (Q9WU84)
Organism: Mus musculus (Mouse)
Function: Delivers copper to copper zinc superoxide dismutase (SOD1).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Copper-transporting ATPase 2
- Superoxide dismutase
- Copper-transporting ATPase 1
- Extracellular superoxide dismutase
- Copper transport protein ATOX1
- Cytochrome c oxidase copper chaperone
- High affinity copper uptake protein 1
- Protein SLC31A2
- Cytochrome c oxidase assembly protein COX11
Sequence:
MASKSGDGGTVCALEFAVQMSCQSCVDAVHKTLKGVAGVQNVDVQLENQMVLVQTTLPSQEVQALLESTGRQAVLKGMGSSQLQNLGAAVAILEGCGSIQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTRDCNSCGDHFNPDGASHGGPQDTDRHRGDLGNVRAEAGGRATFRIEDKQLKVWDVIGRSLVIDEGEDDLGRGGHPLSKITGNSGKRLACGIIARSAGLFQNPKQICSCDGLTIWEERGRPIAGQGRKDSAQPPAHL
Protein: Homeobox protein ceh-10 (P41935)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Required for larval development and for cell fate specification and migration of CAN neurons. Required for generation, or placement, and differentiation of the ALA neuron, and may play a role in ALA axon migration. Involved in development and function of the AIY interneurons, acting by regulating expression of LIM/homeobox protein ttx-3. Also acts in an autoregulatory feedback loop to maintain its own expression. Modulates lifespan, perhaps acting in the AIY interneurons. Plays a role in fertility and egg-laying behavior.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- LIM/homeobox protein ttx-3
- Transcription factor unc-86
- Transcriptional coregulator psa-3
- Serpentine receptor class alpha-11
- Transcription factor unc-3
- Homeobox protein ceh-32
Sequence:
MAVDEMQLAASMQMSNQMSNSQRMSFAIHEILGIQGNAYLSHGYCPQGTFLSNQPNFMDIGSCGVSGFDRQLCGTDSIGNAPAPLMYRMPISTSEVITSEPQTHVSSSSILSSATTSNSSGGGSSGGGGKASKRKKRRHRTIFTQYQIDELEKAFQDSHYPDIYAREVLAGKTELQEDRIQVWFQNRRAKWRKTEKTWGKSTIMAEYGLYGAMVRHSLPLPETITKSAEAADPQQSAAPWLLGMHKKSMEAAAHLESVEKCDMSDSDDDDRPVTPPVQRQVKNEYKPRIIEHVQQQAPQHQSSLNFDTSLVVSSSLSQLHFQDSQMIPNNNASLKLYHDYNNPM
Protein: Conserved Edge Expressed protein (Q19824)
Organism: Caenorhabditis elegans
Interaction partners:
- ATPase asna-1
- Uncharacterized protein ZK688.5
- SGTA homodimerisation domain-containing protein
- UV excision repair protein RAD23
- Sodium/calcium exchanger membrane region domain-containing protein
- Sodium/calcium exchanger membrane region domain-containing protein
- Guided entry of tail-anchored proteins factor 1
Sequence:
MDATTLSRLSEFEKEKKFYDALQFYRTKVTRSFRLKNANEVAIPLVKHALEFFFREKQYQCAIDITTQYAECLSKNNVDLGEEAFNILADSVSKFANFAEIENEAGNSEPEQLLNTARCKCVDLAIQWTKQKATTPIEKKYGSAAFHTVLAKKLVAVDHVELAKNHFLLSDDFKSFANFLHQEYESFKQKESEPEVIIVEAVFQSLCLDRFPFAVSLFTEYVAPAKYPFTKPLLNFQHILFDVIETENQPQYSELTSSYQTELKRSLAFIGYLTRIGKLYFGIRDNQCMSGGLGGLFSGLLGGQKEEETATSHITSRTPARQKPAAMSQPSPFGPFGALAGAPAPAPVPKKIQKVEMEEDLD
Protein: Guanidinium exporter (Quaternary ammonium compound-resistance protein SugE) (P69937)
Organism: Escherichia coli (strain K12)
Function: Guanidinium ion exporter. Couples guanidinium export to the proton motive force, exchanging one guanidinium ion for two protons. Overexpression leads to resistance to a subset of toxic quaternary ammonium compounds such as cetylpyridinium, cetyldimethylethyl ammonium and cetrimide cations.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:14728684, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:14728684}.
Interaction partners:
- Spermidine export protein MdtJ
- Outer membrane lipoprotein Blc
- Beta-lactamase
- Multidrug transporter MdfA
Sequence:
MSWIILVIAGLLEVVWAVGLKYTHGFSRLTPSVITVTAMIVSMALLAWAMKSLPVGTAYAVWTGIGAVGAAITGIVLLGESANPMRLASLALIVLGIIGLKLSTH
Protein: Copine 1 (Q5JX45)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAHCVTLVQLSISCDHLIDKDIGSKSDPLCVLLQDVGGGSWAELGRTERVRNCSSPEFSKTLQLEYRFETVQKLRFGIYDIDNKTPELRDDDFLGGAECSLGQIVSSQVLTLPLMLKPGKPAGRGTITDFLGKSDPFLEFFRQGDGKWHLVYRSEVIKNNLNPTWKRFSVPVQHFCGGNPSTPIQVQCSDYDSDGSHDLIGTFHTSLAQLQAVPAEFECIHPEKQQKKKSYKNSGTIRVKICRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPSSPDSLHYLSPTGVNEYLMALWSVGSVVQDYDSDKLFPAFGFGAQVPPDWQVSHEFALNFNPSNPYCAGIQGIVDAYRQALPQVRLYGPTNFAPIINHVARFAAQAAHQGT
Protein: Methionine-S-oxide reductase (Q6RF46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- ABC transporter I family member 17
Sequence:
MASTIYTCKECGSDLNLNPNDLFPPDFYFEAGNKGTLSFAAVDAEKFRFEKEDKIMPFFETLNYWGIQRKRTKIKCTSCNHLIGYIYDDGPPLTGGIGQYGFGPSQVIPRAPRYRFKTKAVQVSSQT
Protein: Peroxisomal ATPase PEX1 (EC 3.6.4.-) (Peroxin-1) (Peroxisome biogenesis disorder protein 1) (Peroxisome biogenesis factor 1) (O43933)
Organism: Homo sapiens (Human)
Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16854980}. Peroxisome membrane {ECO:0000269|PubMed:11439091, ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:16854980, ECO:0000269|PubMed:21362118}. Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes. {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:16854980}.
Interaction partners:
- Peroxisomal ATPase PEX6
- Peroxisome assembly protein 26
- Peroxisomal targeting signal 1 receptor
- Peroxisomal membrane protein PEX13
- Peroxisome biogenesis factor 10
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 2
- Peroxisomal targeting signal 2 receptor
- PEX5-related protein
Sequence:
MWGSDRLAGAGGGGAAVTVAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSHQPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLKPCSHVVSCQQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAASYGRLETDTKLLIQPKTRRAKENTFSKADAEYKKLHSYGRDQKGMMKELQTKQLQSNTVGITESNENESEIPVDSSSVASLWTMIGSIFSFQSEKKQETSWGLTEINAFKNMQSKVVPLDNIFRVCKSQPPSIYNASATSVFHKHCAIHVFPWDQEYFDVEPSFTVTYGKLVKLLSPKQQQSKTKQNVLSPEKEKQMSEPLDQKKIRSDHNEEDEKACVLQVVWNGLEELNNAIKYTKNVEVLHLGKVWIPDDLRKRLNIEMHAVVRITPVEVTPKIPRSLKLQPRENLPKDISEEDIKTVFYSWLQQSTTTMLPLVISEEEFIKLETKDGLKEFSLSIVHSWEKEKDKNIFLLSPNLLQKTTIQVLLDPMVKEENSEEIDFILPFLKLSSLGGVNSLGVSSLEHITHSLLGRPLSRQLMSLVAGLRNGALLLTGGKGSGKSTLAKAICKEAFDKLDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAGLPAVPEHEHSPDAVQSQRLAHALNDMIKEFISMGSLVALIATSQSQQSLHPLLVSAQGVHIFQCVQHIQPPNQEQRCEILCNVIKNKLDCDINKFTDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGMLLSSGLQDGSSSSDSDLSLSSMVFLNHSSGSDDSAGDGECGLDQSLVSLEMSEILPDESKFNMYRLYFGSSYESELGNGTSSDLSSQCLSAPSSMTQDLPGVPGKDQLFSQPPVLRTASQEGCQELTQEQRDQLRADISIIKGRYRSQSGEDESMNQPGPIKTRLAISQSHLMTALGHTRPSISEDDWKNFAELYESFQNPKRRKNQSGTMFRPGQKVTLA
Protein: Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein) (SPHK1-binding protein) (Q96S38)
Organism: Homo sapiens (Human)
Function: May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell. Plays a role in the recruitment of PRDX3 to early endosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12077123, ECO:0000269|PubMed:15750338}. Membrane {ECO:0000269|PubMed:12077123}. Early endosome {ECO:0000269|PubMed:15750338}.
Interaction partners:
Sequence:
MTSYRERSADLARFYTVTEPQRHPRGYTVYKVTARVVSRRNPEDVQEIIVWKRYSDFKKLHKELWQIHKNLFRHSELFPPFAKGIVFGRFDETVIEERRQCAEDLLQFSANIPALYNSKQLEDFFKGGIINDSSELIGPAEAHSDSLIDTFPECSTEGFSSDSDLVSLTVDVDSLAELDDGMASNQNSPIRTFGLNLSSDSSALGAVASDSEQSKTEEERESRSLFPGSLKPKLGKRDYLEKAGELIKLALKKEEEDDYEAASDFYRKGVDLLLEGVQGESSPTRREAVKRRTAEYLMRAESISSLYGKPQLDDVSQPPGSLSSRPLWNLRSPAEELKAFRVLGVIDKVLLVMDTRTEQTFILKGLRKSSEYSRNRKTIIPRCVPNMVCLHKYIISEESVFLVLQHAEGGKLWSYISKFLNRSPEESFDIKEVKKPTLAKVHLQQPTSSPQDSSSFESRGSDGGSMLKALPLKSSLTPSSQDDSNQEDDGQDSSPKWPDSGSSSEEECTTSYLTLCNEYGQEKIEPGSLNEEPFMKTEGNGVDTKAIKSFPAHLAADSDSPSTQLRAHELKFFPNDDPEAVSSPRTSDSLSRSKNSPMEFFRIDSKDSASELLGLDFGEKLYSLKSEPLKPFFTLPDGDSASRSFNTSESKVEFKAQDTISRGSDDSVPVISFKDAAFDDVSGTDEGRPDLLVNLPGELESTREAAAMGPTKFTQTNIGIIENKLLEAPDVLCLRLSTEQCQAHEEKGIEELSDPSGPKSYSITEKHYAQEDPRMLFVAAVDHSSSGDMSLLPSSDPKFQGLGVVESAVTANNTEESLFRICSPLSGANEYIASTDTLKTEEVLLFTDQTDDLAKEEPTSLFQRDSETKGESGLVLEGDKEIHQIFEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKSHPFFTPVDWAELMR
Protein: Albumin (BSA) (allergen Bos d 6) (P02769)
Organism: Bos taurus (Bovine)
Function: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (Probable). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner. The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (Probable). The rank order of affinity is zinc > calcium > magnesium (Probable). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli. Does not prevent iron uptake by the bacterial siderophore aerobactin.
Subcellular location: Secreted.
Interaction partners:
- Beta-lactoglobulin
- Alpha-lactalbumin
- Lactotransferrin
- Insulin
- Myoglobin
- SPARC
- Serpin domain-containing protein
- Cytochrome c
- Alpha-2-HS-glycoprotein
- Lactoperoxidase
Sequence:
MKWVTFISLLLLFSSAYSRGVFRRDTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA
Protein: Peptide ABC transporter, ATP-binding protein, putative (O69631)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MSVPAAPLLSVEGLEVTFGTDAPAVCGVDLAVRSGQTVAVVGESGSGKSTTAAAILGLLPAGGRITAGRVVFDGRDITGADAKRLRSIRGREIGYVPQDPMTNLNPVWKVGFQVTEALRANTDGRAARRRAVELLAEAGLPDPAKQAGRYPHQLSGGMCQRALIAIGLAGRPRLLIADEPTSALDVTVQRQVLDHLQGLTDELGTALLLITHDLALAAQRAEAVVVVRRGVVVESGAAQSILQSPQHEYTRRLVAAAPSLTARSRRPPESRSRATTQAGDILVVSELTKIYRESRGAPWRRVESRAVDGVSFRLPRASTLAIVGESGSGKSTLARMVLGLLQPTSGTVVFDGTYDVGALARDQVLAFRRRVQPVFQNPYSSLDPMYSVFRAIEEPLRVHHVGDRRQRQRAVRELVDQVALPSSILGRRPRELSGGQRQRVAIARALALRPEVLVCDEAVSALDVLVQAQILDLLADLQADLGLTYLFISHDLAVIRQIADDVLVMRAGRVVEHASTEEVFSRPRHEYTRQLLQAIPGAPSAPRKVGNL
Protein: Inositol monophosphatase 2 (IMP 2) (IMPase 2) (EC 3.1.3.25) (Inositol-1(or 4)-monophosphatase 2) (Myo-inositol monophosphatase A2) (Q91UZ5)
Organism: Mus musculus (Mouse)
Function: Can use myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14732}.
Interaction partners:
- Inositol monophosphatase 1
- Inositol-3-phosphate synthase 1
- Inositol polyphosphate 1-phosphatase
- Inositol oxygenase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- Inositol polyphosphate-4-phosphatase type I A
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Myotubularin
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
Sequence:
MKPSSEEEGELVQGVGPWDECFEVAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHRVEDLIVSELRKRFPSHRFIAEEATASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVHQELEFGVIHHCTEERLYTGRRGQGAFCNGQRLQVSRETDLAKALVLTEIGPKRDPDTLKVFLSNMERLLHAKAHGVRVIGSSTLALCYLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPLDLMSCRVVAAGTREMAVLIAQALQTINYGRDDEK
Protein: Over compensating males, isoform A (Over compensating males, isoform B) (Over compensating males, isoform C) (Q9W198)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTYELPPIILKGKELIKYRHIKRKYPVSKDFLHSNWWNVERFIVYALSPRCVIRNYAWRRRRTRSVCIIRRVRILLFDPRLKRMIKRRLQNVRHWSKGLVNYYKKMGRIEEHEETEVYRVAEPLAAEELSKQMKQQLELLKTGKRSLSLIEETTAIAEVPPKKPKQFPDITEEARVINDSDDRLDAAPSKQAAERTPTKSPAQVAASEDVPTPATPSKEQSGQTSTCSSAEKTDKVEKVGGGSKFLDMLISKVRVKNFARENNMPAEPSAVTFCTSEDEGSADFVGFDESVHQPGMLLTPLVPNNCKTTEGNSAFVSESLDAYMREHHINDSDSQDDKDKLLEPMGHDGQVTSHSMPPPMDMPAVPEALQRLRTVAERRQYLQRCKNHKMGIINNEANVYRELQRKQRQRKVKIGAMQALQASDSQMPFTRQGWQAASYVATEHSKYYYQVIQVDGEMVRLPGAQGNNLKREKSPYLSRLSRKEQEELKCSEQCLDARIQQELKVIPTRVSPPRNPKILNQYPLPAIFRPCPLSKKPLQRPLDDDTAALLLAGGSMAVVSMPNVELDVMPQLGRPLDEIAKRYLQHILPHHDITREWAEFSVSTLQAPPATMKDAEEQASQTPAGRRKSFTFVIPYLNDRNHILVRRVVDRSEHLDRSFKEEPNKLQEFTFREMLPPQPDAEIVACAEMISDMINTVAISCSENSFISEDPDALDASSVPKSSDLCPAKEETGKDTDKSGAKPKNLPNKQKRLANELRRLNATIIDAAARKADANKPCSKDYCHLGCICASLAGTELPVRDHCGRAECVLDCRCLSAEESRVMRLEAADGRGISNEDAFNLRRKATARLAKMEKDFTSTLVLTDNETLLINESQGDKKRRCTKAPKRYEDFDDSIYDEEEKDVVSPTTRKQKKHAAAAAAAAAAAAAAAAASAKISAPALSEPCFVKDTDLAKLKHCFVGLRRLSNVENLATFCMTHQLYKCFCGGDSPDGKPVVIEKDQWNAPVTHFNPDLAVRAHYSFERPPEETSTKKKGKEKKPKHKLESKSSNDVADQKPQTQAVETLPLKTESKQEPPPANSLFKDESPLKRSNELNKIFNYFRSRPDVCRRAISIPKNSYQRLNQRRADRVRHQIAREESLKTNEMLKMRIQGAVVYYRKEIDRQRKRELSKKPVIEVRNESDASDASVRQKKIETPAEGPTPGKRIKLKADEPPAQEKKAHMLDIQVPRIAACYSLNTASVDVLAPDMAKEATTSAAATGSTHGSTDTNSANVCTFYNDVVKNMNTLVSKKMQDIDLALQRESKIIPSPNEEILCIIKWTNFLAAFESGFVFIWDVQMKTHNFLAATTTNLMPSVCGAIAVVNTKFAPDPQALPLMARMLMNSMRNEKTNRLAVVMQGRQSFWLVKGFLRHMQGNACTKPTPMTHPLLTKKINVLCSLLVKQRVRENEKKTLGDGSGAPYEVLAGDVSPQTSLLMKNRSRDLKRKSQADERLLPSGPSMTKSSKPSAGGYPIAASVATSTTSAFASSSGKSTPVCTAKTNSASTKNKSSATGIRSNIEFRKVNHNDVDELQIPELHQTDHRWVVLDIFDDFSHIFVPSFSDMISLTRIHSVMQVAEERQKVVKLQFFPNAPYDAFVTPSSKKKIYFGPLSLDMPPPVLVLLQSVDRKMMLREVYQREHSIPVQRHRRSMAFWVLQINGQVHFEIDTESTAKLAAQQKNAIGTPPGLNVLKIPSQLSVEIEKNQDEVPPVVVIDSDEEDDDGERQLVIDEQDDEQAETDVKQEVERTGFTIQTLPSSGALQITISDSAETSSHPAKDVNTCHFSGGFMPFIANVPAKFGETAPTTQFLTPQVQVTTSQSGPETLTSSSSSHLPASKSAYPKINESLQELFSSGVPPGGITITKVDSQEKTLPNETVQVVKNKKSIAITGIHKQVTKAASSTATVTAARAPVVKPQSTSVSKVAPPIRPGATTQPKTLVRLYPKPALAAGRKSLPANAKTPVATPRQSQPVACDKPPLVSGSTLPALVEPSARKSLPSKPLAAGEHLRPRQSLPAKVTANPPAAARPDAASTSAQNLTNVSKAQLAKEEICYGIMVAKDLPRFRAKVEGSDFMIKIPEHGVFRFKTFGLAASFLSRHVAKDPKLKQFLPAEWKFHPLEQFNKQVPSRSQQSPAAIVIED
Protein: Candida glabrata strain CBS138 chromosome I complete sequence (Q6FQH5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MQYKKTLAASALATSALAAYVPGQPWSTLTPSATFKGGITDYASTFGIAVQPIATPASVAKRAVSQIGDGQVQATTKTTSTLAPKAPISQIGDGQIQATTKTQAAPVSQIGDGQIQATTKTQAAPVSQIGDGQIQATTKTQAAPVSQIGDGQIQATTKTQAAPVSQIGDGQIQATTKTQAAPVSQIGDGQIQATTKTAVSQIGDGQIQATKTATAGASQIQDGQVQASNQGKAPNDPVGAVSCKVDGTLEMNLKGGILTDGKGRIGSIVANRQFQFDGPPPQAGAIFAAGWSLTPQGNLALGDNDVFYQCLSGNFYNLYDQHIGSQCTPVHLSAIDLIKC
Protein: Type IV methyl-directed restriction enzyme EcoKMcrA (EcoKMcrA) (EC 3.1.21.-) (5-methylcytosine-specific restriction enzyme A) (P24200)
Organism: Escherichia coli (strain K12)
Function: Restriction of 5-methyl and 5-hydroxymethylcytosines at the specific DNA sequence 5'-C(me)CGG-3'.
Interaction partners:
- Small ribosomal subunit protein uS12
- Type IV methyl-directed restriction enzyme EcoKMrr
- Galactokinase
- UTP--glucose-1-phosphate uridylyltransferase
- Type IV methyl-directed restriction enzyme EcoKMcrB subunit
- Type IV methyl-directed restriction enzyme EcoKMcrBC
- Protease 7
- Type I restriction enzyme EcoKI specificity subunit
- Type I restriction enzyme EcoKI endonuclease subunit
- Beta-galactosidase
Sequence:
MHVFDNNGIELKAECSIGEEDGVYGLILESWGPGDRNKDYNIALDYIIERLVDSGVSQVVVYLASSSVRKHMHSLDERKIHPGEYFTLIGNSPRDIRLKMCGYQAYFSRTGRKEIPSGNRTKRILINVPGIYSDSFWASIIRGELSELSQPTDDESLLNMRVSKLIKKTLSQPEGSRKPVEVERLQKVYVRDPMVKAWILQQSKGICENCGKNAPFYLNDGNPYLEVHHVIPLSSGGADTTDNCVALCPNCHRELHYSKNAKELIEMLYVNINRLQK
Protein: Fibroblast growth factor 7 (FGF-7) (Heparin-binding growth factor 7) (HBGF-7) (Keratinocyte growth factor) (Q02195)
Organism: Rattus norvegicus (Rat)
Function: Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation.
Interaction partners:
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 4
- Pro-epidermal growth factor
- Klotho
- Fibroblast growth factor-binding protein 1
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Platelet-derived growth factor receptor alpha
Sequence:
MRKWILTRILPTPLYRPCFHLVCLVGTISLACNDMSPEQTATSVNCSSPERHTRSYDYMEGGDIRVRRLFCRTQWYLRIDKRGKVKGTQEMRNSYNIMEIMTVAVGIVAIKGVESEYYLAMNKQGELYAKKECNEDCNFKELILENHYNTSASAKWTHSGGEMFVALNQKGLPVKGKKTKKEQKTAHFLPMAIT
Protein: Thymidylate kinase (EC 2.7.4.9) (Thymidine monophosphate kinase) (dTMP kinase) (TMPK) (P0A720)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth.
Interaction partners:
- Endolytic murein transglycosylase
- DNA polymerase III subunit delta'
- Thymidine kinase
- Aminodeoxychorismate lyase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Thymidylate synthase
- Uncharacterized metal-dependent hydrolase YcfH
- Acyl carrier protein
- Ribonucleoside-diphosphate reductase 2 subunit alpha
- Nucleoside diphosphate kinase
Sequence:
MRSKYIVIEGLEGAGKTTARNVVVETLEQLGIRDMVFTREPGGTQLAEKLRSLVLDIKSVGDEVITDKAEVLMFYAARVQLVETVIKPALANGTWVIGDRHDLSTQAYQGGGRGIDQHMLATLRDAVLGDFRPDLTLYLDVTPEVGLKRARARGELDRIEQESFDFFNRTRARYLELAAQDKSIHTIDATQPLEAVMDAIRTTVTHWVKELDA
Protein: Envelope glycoprotein E (Q6UK11)
Organism: Suid herpesvirus 1 (SuHV-1) (Pseudorabies virus)
Subcellular location: Host Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004152}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004152}. Host cell junction {ECO:0000256|ARBA:ARBA00004315}. Host cell membrane {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004402}. Host endosome membrane {ECO:0000256|ARBA:ARBA00004235}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004235}. Virion membrane {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004563}.
Interaction partners:
Sequence:
MRPFLLRAAQLLALLALALSTEAPSLSAETTPGPVTEVPSPSAEVWDLSTEAGDDDLDGDLNGDDRRAGFGSALASLREAPPAHLVNVSEGANFTLDARGDGAVVAGIWTFLPVRGCDAVAVTMVCFETACHPDLVLGRACVPEAPERGIGDYLPPEVPRLQREPPIVTPERWSPHLTVRRATPNDTGLYTLHDASGPRAVFFVAVGDRPPAPLAPVGPARHEPRFHALGFHSQLFSPGDTFDLMPRVVSDMGDSRENFTATLDWYYARAPPRCLLYYVYEPCIYHPRAPECLRPVDPACSFTSPARARLVARRAYASCSPLLGDRWLTACPFDAFGEEVHTNATADESGLYVLVMTHNGHVATWDYTLVATAAEYVTVIKELTAPARAPGTPWGPGGGDDAIYVDGVTTPAPPARPWNPYGRTTPGRLFVLALGSFVMTCVVGGAVWLCVLCSRRRAASRPFRVPTRAGTRMLSPVYTSLPTHEDYYDGDDDDEEAGDARRRPSSPGGDSGYEGPYVSLDAEDEFSSDEDDGLYVRPEEAPRSGFDVWFRDPEKPEVTNGPNYGVTASRLLNARPA
Protein: Protein phosphatase 1 regulatory subunit 3B (33 kDa glycogen-binding protein) (Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL) (Protein phosphatase 1 regulatory subunit 4) (PP1 subunit R4) (Protein phosphatase 1 subunit GL) (Q6IN01)
Organism: Rattus norvegicus (Rat)
Function: Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Glycogen [starch] synthase, liver
- Glycogen [starch] synthase, muscle
- Protein phosphatase 1 regulatory subunit 3A
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Protein phosphatase 1 regulatory subunit 3C
- Protein phosphatase 1 regulatory subunit 3E
- Protein phosphatase 1, regulatory subunit 3D
- Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
Sequence:
MAVDIEYSYSSMAPSLRRERFTFKISPKLNKPLRPCIQLGSKDEAGRMVAPTVQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDIPFNITELLDNIVSLTTAESESFVLDFPQPSADYLDFRNRLQTNHVCLENCVLKEKAIAGTVKVQNLAFEKVVKIRMTFDTWKSFTDFPCQYVKDTYAGSDRDTFSFDISLPEKIQSYERMEFAVCYECNGQSYWDSNKGKNYRITRAELRSTQGMTEPYNGPDFGISFDQFGSPRCSFGLFPEWPSYLGYEKLGPYY
Protein: Methyltransferase ausD (EC 2.1.3.-) (Austinoid biosynthesis clusters protein D) (C8VE82)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Methyltransferase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Interaction partners:
- FAD-binding monooxygenase ausB
- Non-reducing polyketide synthase ausA
- Uncharacterized protein
- Polyprenyl transferase ausN
Sequence:
MIAMQPETQLKTALKNGFDPNILYKDPLTIVKEPMCTILEKHSKIPVDKVVSHVNKVRDRAFAVFPYACIGQFSFVELSIAASPYYPEMLERVKNGHKLLDLGCAFGQELRQLIYDGAPGESLYGSDIQQEFLNLGYELFLDRATLPESHLIASNILDRQSPLFTHLTGKLNIVYISLFLHVFDFEQQITVAGNVLDLLAAEPGSLIVCRVTACRDQGVLNATAERMPYYYHDRASWEQLWEVVQKRTGVKLCVDTWEQPDELVKKHPLPGIYILGSAIRRV