wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase STE20 (EC 2.7.11.1) (Q6FN53)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: MAP4K component of the MAPK pathway required for the mating pheromone response and the regulation of cell polarity and cell cycle. Phosphorylates histone H2B to form H2BS10ph (By similarity). Involved in cell wall integrity, hypertonic stress adaptation and virulence.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cell division control protein 42
- Candida glabrata strain CBS138 chromosome M complete sequence
- Serine/threonine-protein kinase STE11
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Guanine nucleotide-binding protein subunit gamma
- non-specific serine/threonine protein kinase
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
Sequence:
MSNANQKENVPSLGLPRTHGTLNVNALKATDILKHKGKLNEVNSDQSTTNENDEVQEEAVFLDDPVHFTRVSSSSELSAALSVNTTEQEQDEEKGTEHAELEPAEEDTVEVDTIRNNGDKTYSTIRESASDFETTNNTLIEISKNSSTYSSTEFLNNNNNGISNSNRATIDSESKLRMNKLREGSSTSLSNDSNGFNGMISSNQASTVLSTPSQKPSSTTNTITKANNGGSTRAQKEKHTSPKLPSTVTAPSSHRKSADLSKTNKLPSTTAKRTPKQAVTSSSPKEPAKRKSSTSKMKGMFSSLVQNMKRNSSDNRKSASSLSSVSSSSSSTLKISTPYNPKHIYHVGVDARTGEYTGLPEEWERLLASSGISRKEQQQNMQAVIDIVNFYQDVADHTGEEKVIKTFDPKKQNPLVRDSLSKYEQVDDNRTSYASGGTPTLEQNGFHTSSTPRSRTSLTSPTAGYSMISTPPMATQEKYIPTRPAPKPPGQQTPSSNASLTPKMQNATMSPIKENISSPVTKSEVDDELLLSKKNASLPKLPSDDSSSHKKSATDSAPTSVETDTETVKVPPIPKTTPTVPAKASRRSNEKKKEERERNKKLLYAKLTEICSPGDPKSKYRDLIKIGQGASGGVYIAHDTESEDSVAIKQMNLEKQPKKELILNEILVMRESKHSNIVNFIDSYLAKGDLWIVMEYMEGGSLTDVVTHCLLSEGQIGAVCRETLKGLQFLHSKGVLHRDIKSDNILLSLKGNIKLTDFGFCAQINENNLKRTTMVGTPYWMAPEVVSRKEYGPKVDIWSLGIMIIEMIEGEPPYLNETPLRALYLIATNGTPKLKEPEALSDTLTKFLDWCLKVDPSERATATELLDDPFITEIAEDNSSLSPLVKLARIKKLEEQEEDAGTDETEPETTPDTTI
Protein: CBL-interacting serine/threonine-protein kinase 6 (EC 2.7.11.1) (SNF1-related kinase 3.14) (SOS2-like protein kinase PKS4) (SOS3-interacting protein 3) (O65554)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by phosphorylation the K(+) conductance and uptake of AKT1. Binds to CBL4 to modulate AKT2 activity by promoting a kinase interaction-dependent but phosphorylation-independent translocation of the channel to the plasma membrane.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:21445098}. Note=Targeted to the cell membrane when interacting with CBL4 and ATK2.
Interaction partners:
- Calcineurin B-like protein 4
- Calcineurin B-like protein 10
- Calcineurin B-like protein 1
- Calcineurin B-like protein 2
- Potassium channel AKT2/3
- Calcineurin B-like protein 3
- Calcineurin B-like protein 9
- Potassium channel AKT1
- Calcineurin B-like protein 8
- Potassium transporter 5
Sequence:
MVGAKPVENGSDGGSSTGLLHGRYELGRLLGHGTFAKVYHARNIQTGKSVAMKVVGKEKVVKVGMVDQIKREISVMRMVKHPNIVELHEVMASKSKIYFAMELVRGGELFAKVAKGRLREDVARVYFQQLISAVDFCHSRGVYHRDLKPENLLLDEEGNLKVTDFGLSAFTEHLKQDGLLHTTCGTPAYVAPEVILKKGYDGAKADLWSCGVILFVLLAGYLPFQDDNLVNMYRKIYRGDFKCPGWLSSDARRLVTKLLDPNPNTRITIEKVMDSPWFKKQATRSRNEPVAATITTTEEDVDFLVHKSKEETETLNAFHIIALSEGFDLSPLFEEKKKEEKREMRFATSRPASSVISSLEEAARVGNKFDVRKSESRVRIEGKQNGRKGKLAVEAEIFAVAPSFVVVEVKKDHGDTLEYNNFCSTALRPALKDIFWTSTPA
Protein: N-methyl-L-tryptophan oxidase (MTOX) (EC 1.5.3.-) (P40874)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidative demethylation of N-methyl-L-tryptophan. Can also use other N-methyl amino acids, including sarcosine, which, however, is a poor substrate.
Interaction partners:
- Nickel import ATP-binding protein NikD
- Uncharacterized protein YceO
Sequence:
MKYDLIIIGSGSVGAAAGYYATRAGLNVLMTDAHMPPHQHGSHHGDTRLIRHAYGEGEKYVPLVLRAQTLWDELSRHNEEDPIFVRSGVINLGPADSTFLANVAHSAEQWQLNVEKLDAQGIMARWPEIRVPDNYIGLFETDSGFLRSELAIKTWIQLAKEAGCAQLFNCPVTAIRHDDDGVTIETADGEYQAKKAIVCAGTWVKDLLPELPVQPVRKVFAWYQADGRYSVKNKFPAFTGELPNGDQYYGFPAENDALKIGKHNGGQVIHSADERVPFAEVASDGSEAFPFLRNVLPGIGCCLYGAACTYDNSPDEDFIIDTLPGHDNTLLITGLSGHGFKFASVLGEIAADFAQDKKSDFDLTPFRLSRFQ
Protein: IST1 homolog (Charged multivesicular body protein 8) (Q7ZVT1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Charged multivesicular body protein 1b
- Spastin
- Vesicle
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 5
- vesicle-fusing ATPase
- Charged multivesicular body protein 3
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 4c
- Charged multivesicular body protein 7
Sequence:
MLGGGFKSERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLSAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLTRFGLIQSMKELDPGLQEAVSTLIWAAPRLQSEVAELKIVSDQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDAMVRPEVCPGEEADLIDVDSDFKKPGAGGGGGGGGGFTAPAMGMPMPMPMPMPMPTAFNYPPPKGAEPFNGPVGTYDGFSNFQAPMRGGQPPQLPSCPPTYESIDELCIKPSDPSQVIPGPTPAGQVYDNSTLPELPSVPDTLPASSFGAKANTSEDIDFDDLSRRFEELKKKT
Protein: Eyes absent homolog (EC 3.1.3.48) (A0A8I6A077)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTPRKNFSGFLKTVCEDRRDLQSSHISVCKETAVLMEEEQDLPERPVKKAKMQEPGEQTLSQVNNPDTSDQKPETASLASNLSMSEEIMTCTDYIPRSSNDYTSQMYSAKPYAHILSVPVSETTYPGQTQYQTLQQSQPYAVYPQATQTYGLPPFASSTNASLISTSSAIANIPAAAVASISNQDYPTYTILGQNQYQACYPSSSFGVTGQTNSDTENTALAATTYQTEKPGAMGPAPATQRLPSDSSTSPPLSQTTPNKDADDQARKNMTVKNRGKRKADASSSQDSELERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLSNYSFSTDGFSGSGGSGSHGSSVGVQGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLGTALKSLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDEEIAAKQHNMPFWRITNHGDLVSLHQALELDFL
Protein: Myosin heavy chain, muscle (P05661)
Organism: Drosophila melanogaster (Fruit fly)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin light chain alkali
- Myosin regulatory light chain 2
- Tropomyosin-2
- Troponin I
- Paramyosin, long form
- Troponin T, skeletal muscle
- Actin, indirect flight muscle
- Actin-57B
- Bent, isoform F
- Titin
Sequence:
MPKPVANQEDEDPTPYLFVSLEQRRIDQSKPYDSKKSCWIPDEKEGYLLGEIKATKGDIVSVGLQGGEVRDIKSEKVEKVNPPKFEKIEDMADMTVLNTPCVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHIMFVMEQEEYKKEGINWDFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTKVFFRAGVLGQMEEFRDERLGKIMSWMQAWARGYLSRKGFKKLQEQRVALKVVQRNLRKYLQLRTWPWYKLWQKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEHDRQTCHNELNQTRTACDQLGRDKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAPRATSVRPQFDGLAFPPRFDLAPENEF
Protein: Antitoxin RnlB (P52130)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. A labile antitoxin (half-life of 2.1 minutes) that inhibits the endonuclease activity of cognate toxin RnlA but not that of non-cognate toxin LsoA.
Interaction partners:
- mRNA endoribonuclease toxin LS
- mRNA interferase toxin RelE
- Endoribonuclease toxin MazF
- Antitoxin RelB
- Antitoxin DinJ
- mRNA interferase toxin YafQ
- Antitoxin MazE
- mRNA interferase toxin YafO
- Antitoxin MqsA
- Toxin YoeB
Sequence:
MFEITGINVSGALKAVVMATGFENPLSSVNEIETKLSALLGSETTGEILFDLLCANGPEWNRFVTLEMKYGRIMLDTAKIIDEQDVPTHILSKLTFTLRNHPEYLEASVLSPDDVRQVLSMDF
Protein: (rape) hypothetical protein (SCARECROW-like protein) (Q6DLS1)
Organism: Brassica napus (Rape)
Interaction partners:
Sequence:
MKLQASSPQDNQPSNTTNNSTDSNHLSMDEHAMRSMDWDSIMKELEVDDDSAPYQLQPSSFNLPVFPDIDSSDVYPGPNQITGYGFNSLDSVDNGGFDYIEDLIRVVDCIESDELHLAHVVLSQLNQRLQTSAGRPLQRAAFYFKEALGSLLTGTNRNQLFSWSDIVQKIRAIKEFSGISPIPLFSHFTANQAILDSLSSQSSSPFVHVVDFEIGFGGQYASLMREIAEKSANGGFLRVTAVVAEDCAVETRLVKENLTQFAAEMKIRFQIEFVLMKTFEILSFKAIRFVDGERTVVLISPAIFRRVIGIAEFVNNLGRVSPNVVVFVDSEGCTETAGSGSFRREFVSAFEFYTMVLESLDAAAPPGDLVKKIVETFLLRPKISAAVETAANRRSAGQMTWREMLCAAGMRPVQLSQFADFQAECLLEKAQVRGFHVAKRQGELVLCWHGRALVATSAWRF
Protein: Mineralocorticoid receptor (MR) (Nuclear receptor subfamily 3 group C member 2) (P22199)
Organism: Rattus norvegicus (Rat)
Function: Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Cytoplasmic and nuclear in the absence of ligand; nuclear after ligand-binding. When bound to HSD11B2, it is found associated with the endoplasmic reticulum membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Glucocorticoid receptor
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Angiotensinogen
- Renin
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- 11-beta-hydroxysteroid dehydrogenase type 2
- Nuclear receptor coactivator
- peptidylprolyl isomerase
- Prostaglandin E synthase 3
Sequence:
METKGYHSLPEGLDMERRWSQVSQTLERSSLGPAERTTENNYMEIVNVSCVSGAIPNNSTQGSSKEKHELLPYIQQDNSRSGILPSDIKTELESKELSATVAESMGLYMDSVRDAEYTYDQQNQQGSLSPTKIYQNMEQLVKFYKENGHRSSTLSAMSRPLRSFMPDSAASMNGGALRAIVKSPIICHEKSSSVSSPLNMASSVCSPVGINSMSSSTTSFGSFPVHSPITQGTSLTCSPSVENRGSRSHSPTHASNVGSPLSSPLSSMKSPISSPPSHCSVKSPVSSPNNVPLRSSVSSPANLNNSRCSVSSPSNNTNNRSTLSSPTASTVGSIGSPISNAFSYATSGASAGAGAIQDVVPSPDTHEKGAHDVPFPKTEEVEKAISNGVTGPLNIVQYIKSEPDGAFSSSCLGGNSKISPSSPFSVPIKQESSKHSCSGASFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGSCEDSAFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSPRDQSFQHLSSFPPVNTLVESWKPHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGLHEEQPQQPPPPPPQSPEEGTTYIAPTKEPSVNSALVPQLTSITHALTPSPAMILENIEPETVYAGYDNSKPDTAESLLSTLNRLAAKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQLLYFAPDLVFNEEKMHQSAMYELCQGMRQISLQFVRLQLTFEEYSIMKVLLLLSTVPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNSSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESQALKVEFPAMLVEIITDQLPKVESGNAKPLYFHRK
Protein: Molybdopterin-guanine dinucleotide biosynthesis adapter protein (MGD biosynthesis adapter protein) (Molybdenum cofactor biosynthesis adapter protein) (Moco biosynthesis adapter protein) (Molybdopterin-guanine dinucleotide biosynthesis protein B) (P32125)
Organism: Escherichia coli (strain K12)
Function: GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP.
Interaction partners:
- Molybdenum cofactor guanylyltransferase
- Molybdopterin molybdenumtransferase
- Molybdopterin synthase catalytic subunit
- Cyclic pyranopterin monophosphate synthase
- Molybdopterin synthase sulfur carrier subunit
- Molybdopterin adenylyltransferase
- Molybdenum cofactor biosynthesis protein B
- Protein YihD
Sequence:
MAGKTMIPLLAFAAWSGTGKTTLLKKLIPALCARGIRPGLIKHTHHDMDVDKPGKDSYELRKAGAAQTIVASQQRWALMTETPDEEELDLQFLASRMDTSKLDLILVEGFKHEEIAKIVLFRDGAGHRPEELVIDRHVIAVASDVPLNLDVALLDINDVEGLADFVVEWMQKQNG
Protein: E3 14.7K (Q64863)
Organism: Human adenovirus F serotype 40 (HAdV-40) (Human adenovirus 40)
Interaction partners:
Sequence:
MSDQLEIDGQCTEQLILARRKLKQQNQELFNLQALHQCKKGLFCLVKQAELCYDVTQQGHELSYTLNKQRQSFMTMVGVKPIKVTQQSGPVEGSILCQCTNPECMYTMVKTLCGLRELLPFN
Protein: tRNA 5-carboxymethoxyuridine methyltransferase (EC 2.1.1.-) (cmo5U methyltransferase) (P36566)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs. Four tRNAs (tRNA(Ala1), tRNA(Ser1), tRNA(Pro3) and tRNA(Thr4)) are fully modified with mcmo5U in stationary-phase E.coli. Also present at low frequency in tRNA(Leu3) and tRNA(Val1).
Interaction partners:
- Chromosome partition protein MukF
- Chromosome partition protein MukE
- tRNA U34 carboxymethyltransferase
- Chromosome partition protein MukB
- Carboxy-S-adenosyl-L-methionine synthase
- Uncharacterized protein YafE
Sequence:
MQDRNFDDIAEKFSRNIYGTTKGQLRQAILWQDLDRVLAEMGPQKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHCAAQDVASHLETPVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLSLMFYNAHGLLMHNMVAGNFDYVQAGMPKKKKRTLSPDYPRDPAQVYLWLEEAGWQIMGKTGVRVFHDYLREKHQQRDCYEALLELETRYCRQEPYITLGRYIHVTARKPQSKDKV
Protein: AT27166p (Hale-bopp) (Q8T3W6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Male-specific sperm protein Mst84Dc
- GH14622p
- Male-specific sperm protein Mst84Dd
- Uncharacterized protein, isoform C
- Protein disconnected
- Cyclin-K
- Protein spinster
- Trivet, isoform I
- Protein suppressor of sable
- GEO11848p1
Sequence:
MFCTESCEHGCNATSSGKLIANGNGGGLQSQGNSQHQFTMSYAPLSTNDVPSKSEVEPPRLGMCLVTECPEGLSIDCNVPLPNSFNLDEYKNHMICSSCTQFNGGLDRFGQPGTAGPSASPSANPYPTPMPNPIQASPCSFHGQCCSAGGPCAGYDSQPNPSRCYRQESSLAQGAPAMPQIFCLAPPSSHGGLNQPVYLCSLIPVPPSWNLVPLAQPQHLTHQQLLTNPAQDSQLPLQQLVQYDLSFNRLLAELRKERERSCCDLQIPQPLAFQLYAPTVRFLDQPDSSSAKREPHCPPAAPCAPPAAPPQPPSSSSSPTATSASAAGLPRARSASPKRSRSCLRNKDLWDSGGSVPGPSPCSSPTQHATGNVCMKCGNCWHCPRCNCSNCFWHPGLVRAPPRDGR
Protein: Endothelial PAS domain-containing protein 1 (EPAS-1) (Basic-helix-loop-helix-PAS protein MOP2) (Class E basic helix-loop-helix protein 73) (bHLHe73) (HIF-1-alpha-like factor) (HLF) (Hypoxia-inducible factor 2-alpha) (HIF-2-alpha) (HIF2-alpha) (Member of PAS protein 2) (PAS domain-containing protein 2) (Q99814)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX1 seems to activate CTAD (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P97481, ECO:0000255|PROSITE-ProRule:PRU00981}. Nucleus speckle {ECO:0000250|UniProtKB:P97481}. Note=Colocalizes with HIF3A in the nucleus and speckles. {ECO:0000250|UniProtKB:P97481}.
Interaction partners:
- Egl nine homolog 1
- von Hippel-Lindau disease tumor suppressor
- Aryl hydrocarbon receptor nuclear translocator
- Prolyl hydroxylase EGLN3
- Histone acetyltransferase p300
- Hypoxia-inducible factor 1-alpha
- Prolyl hydroxylase EGLN2
- Aryl hydrocarbon receptor nuclear translocator 2
- Hypoxia-inducible factor 3-alpha
- Elongin-B
Sequence:
MTADKEKKRSSSERRKEKSRDAARCRRSKETEVFYELAHELPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVCSENESEAEADQQMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSLKNGSGFGKKSKDMSTERDFFMRMKCTVTNRGRTVNLKSATWKVLHCTGQVKVYNNCPPHNSLCGYKEPLLSCLIIMCEPIQHPSHMDIPLDSKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNPRNLQPQCIMCVNYVLSEIEKNDVVFSMDQTESLFKPHLMAMNSIFDSSGKGAVSEKSNFLFTKLKEEPEELAQLAPTPGDAIISLDFGNQNFEESSAYGKAILPPSQPWATELRSHSTQSEAGSLPAFTVPQAAAPGSTTPSATSSSSSCSTPNSPEDYYTSLDNDLKIEVIEKLFAMDTEAKDQCSTQTDFNELDLETLAPYIPMDGEDFQLSPICPEERLLAENPQSTPQHCFSAMTNIFQPLAPVAPHSPFLLDKFQQQLESKKTEPEHRPMSSIFFDAGSKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKWAVGDQRTEFLGAAPLGPPVSPPHVSTFKTRSAKGFGARGPDVLSPAMVALSNKLKLKRQLEYEEQAFQDLSGGDPPGGSTSHLMWKRMKNLRGGSCPLMPDKPLSANVPNDKFTQNPMRGLGHPLRHLPLPQPPSAISPGENSKSRFPPQCYATQYQDYSLSSAHKVSGMASRLLGPSFESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT
Protein: Alpha-methylacyl-CoA racemase (EC 5.1.99.4) (2-methylacyl-CoA racemase) (Q9UHK6)
Organism: Homo sapiens (Human)
Function: Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters. Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs.
Subcellular location: Peroxisome {ECO:0000269|PubMed:11060344, ECO:0000269|PubMed:11060359, ECO:0000269|PubMed:7649182}. Mitochondrion {ECO:0000269|PubMed:11060344, ECO:0000269|PubMed:11060359, ECO:0000269|PubMed:7649182}.
Interaction partners:
- Peroxisomal acyl-coenzyme A oxidase 2
- Long-chain fatty acid transport protein 5
- Olfactory receptor 51E2
- Sterol carrier protein 2
- Hydroxysteroid dehydrogenase-like protein 2
- Peroxisomal multifunctional enzyme type 2
- 3 beta-hydroxysteroid dehydrogenase type 7
- Olfactory receptor 51E1
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MALQGISVVELSGLAPGPFCAMVLADFGARVVRVDRPGSRYDVSRLGRGKRSLVLDLKQPRGAAVLRRLCKRSDVLLEPFRRGVMEKLQLGPEILQRENPRLIYARLSGFGQSGSFCRLAGHDINYLALSGVLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDANMVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGEFMAVGAIEPQFYELLIKGLGLKSDELPNQMSMDDWPEMKKKFADVFAEKTKAEWCQIFDGTDACVTPVLTFEEVVHHDHNKERGSFITSEEQDVSPRPAPLLLNTPAIPSFKRDPFIGEHTEEILEEFGFSREEIYQLNSDKIIESNKVKASL
Protein: Actinoporin-like protein (E7FCZ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nematocyst {ECO:0000256|ARBA:ARBA00004532}. Target cell membrane {ECO:0000256|ARBA:ARBA00004175}.
Interaction partners:
Sequence:
MTESAEAVAANVSSRRHATVEITNLTNNYCFLNPKVYLENGETSNPPQPTVRPLKTEVCTFSKSAAHATGSVGVLTYDLFERRRNDYTETLAIMFSVPWDYNLYKNWFAVGIYPKGKECDQALYKEMYYQKNQHGFVREEANGSGINFEGKNLDIRATMCPMGRAIVKVEVWDKLLSPMAQMDC
Protein: Alpha-actinin-2 (Alpha-actinin skeletal muscle isoform 2) (F-actin cross-linking protein) (P35609)
Organism: Homo sapiens (Human)
Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11171996, ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:30701273}. Note=Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle.
Interaction partners:
- Titin
- Myozenin-1
- Myozenin-2
- Myosin-7
- Actin, cytoplasmic 1
- LIM domain-binding protein 3
- Myosin-6
- Cysteine and glycine-rich protein 3
- Telethonin
- PDZ and LIM domain protein 3
Sequence:
MNQIEPGVQYNYVYDEDEYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLNEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERMEKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADGERQSIMAIQNEVEKVIQSYNIRISSSNPYSTVTMDELRTKWDKVKQLVPIRDQSLQEELARQHANERLRRQFAAQANAIGPWIQNKMEEIARSSIQITGALEDQMNQLKQYEHNIINYKNNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRDAKGITQEQMNEFRASFNHFDRRKNGLMDHEDFRACLISMGYDLGEAEFARIMTLVDPNGQGTVTFQSFIDFMTRETADTDTAEQVIASFRILASDKPYILAEELRRELPPDQAQYCIKRMPAYSGPGSVPGALDYAAFSSALYGESDL
Protein: Cell division control protein 45 (Q08032)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for initiation of chromosomal DNA replication. Acts at the origin of replication. Also has a role in minichromosome maintenance.
Subcellular location: Nucleus {ECO:0000269|PubMed:8901577}.
Interaction partners:
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM6
- Mitochondrial morphogenesis protein SLD7
- DNA polymerase alpha-binding protein
- DNA replication complex GINS protein PSF2
- Cell division control protein 6
- DNA replication licensing factor MCM4
- Chromosome segregation in meiosis protein 3
- DNA replication regulator DPB11
- DNA polymerase epsilon catalytic subunit A
Sequence:
MYYGISQFSEAYNKILRNSSSHSSCQLVIFVSCLNIDALCATKMLSLLFKKQLVQSQIVPIFGYSELRRHYSQLDDNINSLLLVGFGGVIDLEAFLEIDPQEYVIDTDEKSGEQSFRRDIYVLDAHRPWNLDNIFGSQIIQCFDDGTVDDTLGEQKEAYYKLLELDEESGDDELSGDENDNNGGDDEATDADEVTDEDEEDEDETISNKRGNSSIGPNDLSKRKQRKKQIHEYEGVLEEYYSQGTTVVNSISAQIYSLLSAIGETNLSNLWLNILGTTSLDIAYAQVYNRLYPLLQDEVKRLTPSSRNSVKTPDTLTLNIQPDYYLFLLRHSSLYDSFYYSNYVNAKLSLWNENGKKRLHKMFARMGIPLSTAQETWLYMDHSIKRELGIIFDKNLDRYGLQDIIRDGFVRTLGYRGSISASEFVEALTALLEVGNSTDKDSVKINNDNNDDTDGEEEEDNSAQKLTNLRKRWVSNFWLSWDALDDRKVELLNRGIQLAQDLQRAIFNTGVAILEKKLIKHLRIYRLCVLQDGPDLDLYRNPLTLLRLGNWLIECCAESEDKQLLPMVLASIDENTDTYLVAGLTPRYPRGLDTIHTKKPILNNFSMAFQQITAETDAKVRIDNFESSIIEIRREDLSPFLEKLTLSGLL
Protein: PelE (Q9HZE8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PelG
- PelF
- PelD
- PelC
- PelA
- PelB
- Uncharacterized protein
- Alanine--tRNA ligase
- Mannuronan synthase
- DNA-directed RNA polymerase subunit alpha
Sequence:
MISKWLFSGAFLFELSSWASVFADLPIGQALALYLFAHGLGSALLCVGVWLLLPRRYKFPLPWSPLFLFSLAFFVPLIGAVGVAAAVFPALYLPRQRGEQAWQAMGVPELPFRPKEKRLDMMFSDGGLQDVLRHAPDPNQRLTAIFATRRMPGKEAIPILKLALRDPADDVRLLAYSMLDQKESRINQRIEAALGRLAGATPARRGALHGTLARWYWELAYLGLAQGSVLEHILEQAREHTDQALRGTPSADLHLLAGRIALEQGRLEDAGRALQAAEEAGIDSAQLAPFRAEVAFFQRRYRDIPRLLAGMPDDMLQRPPFAALARYWT