wanglab/gogpt-training-data huggingface dataset:
Protein: L-serine dehydratase (SDH) (EC 4.3.1.17) (L-serine deaminase) (L-SD) (P9WGT5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Serine hydroxymethyltransferase 2
- Phosphoserine phosphatase SerB2
- Serine hydroxymethyltransferase 1
- L-threonine dehydratase biosynthetic IlvA
- Serine acetyltransferase
- Probable cystathionine beta-synthase Rv1077
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Probable glycine dehydrogenase
Sequence:
MTISVFDLFTIGIGPSSSHTVGPMRAANQFVVALRRRGHLDDLEAMRVDLFGSLAATGAGHGTMSAILLGLEGCQPETITTEHKERRLAEIAASGVTRIGGVIPVPLTERDIDLHPDIVLPTHPNGMTFTAAGPHGRVLATETYFSVGGGFIVTEQTSGNSGQHPCSVALPYVSAQELLDICDRLDVSISEAALRNETCCRTENEVRAALLHLRDVMVECEQRSIAREGLLPGGLRVRRRAKVWYDRLNAEDPTRKPEFAEDWVNLVALAVNEENASGGRVVTAPTNGAAGIVPAVLHYAIHYTSAGAGDPDDVTVRFLLTAGAIGSLFKERASISGAEVGCQGEVGSAAAMAAAGLAEILGGTPRQVENAAEIAMEHSLGLTCDPIAGLVQIPCIERNAISAGKAINAARMALRGDGIHRVTLDQVIDTMRATGADMHTKYKETSAGGLAINVAVNIVEC
Protein: CKII alpha subunit interactor 1 (Q24161)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTEAEICKLCKDNLAIEIDLEKPKFKSANKLLQRLFDWYKIDAAILGENYCICEPCFGETLRISESLEKWGTAQDEFHRRPIEIDDSTAFQIKLEVTSNKEEVETEKNDEENSFDQHIAEPVKEDPLEKNEHMEIVVEESLKTASVDFFSVGLSRDGLAVTKFFKDKTQATRMLCTCCGHVLEILTHIRMHSCKPRPNPVYYCRDCGSEFHKLHELHEHMKTMKHNKTMCGAKDLEFLCLRCNQIFPRYFDVIRHENSVHNVSDFICVECNMSFANQGSYRRHTRSHKVKFTQQRFYECPYKDCTSSYRVWARLMSHMSSHGLFSGFKSKVPSTQQERRLLEGKFMTLDPMKRVEPDRRKLPYRKKSFYAKADFPESPTKCTNGGEFISLPKKISLQKGKYINLSDNSRP
Protein: Spectrin beta chain (A0A0G2K677)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Ankyrin-3
- Spectrin alpha chain, non-erythrocytic 1
- Spectrin alpha chain, erythrocytic 1
- Ankyrin 2
- Ankyrin 1
- Spectrin beta chain, non-erythrocytic 2
- Protein kinase C beta type
Sequence:
MAQVPGEVDNMEGPAASNNNNPAARWESPDRGWDREPPAAANAAASLFECSRIKALADEREAVQKKTFTKWVNSHLARVGCHIGDLYADLRDGFVLTRLLEVLSGEQLPRPTRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLVWTIILRFQIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLVDLSKLTKSNANYNLQRAFRTAEQHLGLARLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKALAVEGKRIGKVLDQVLEVDKIIERYEELAAELLAWIHRTVDLISNQKFANSLSGVQQQLQAFTAYCTLEKPVKFQEKGNLEVLLFSIQSKLRAHNRRLFVPREGCGIWDIDKAWGELEKAEHEREAALRAELIRQEKLELLAQRFDHKVAMRESWLNENQRLVSQDNFGYELPAVEAAMKKHEAIEADIAAYEERVQGVAELAQALAAEGYYDARRVAAQRDSVLRQWALLTGLVGARRTRLEQNLALQKVFQEMVYMVDWMEEMQTQLLSRECGQHLVEADDLLQKHGLLEGDIAAQSERVEALNAAALRFSQLQGYQPCDPQVICNRVNHVHGCLSELQEQAARRRAELEASRSLWALLQELEEAESWARDKERLLEATSGSGGAAGTAGGAHDLSSTARLLAQHKILQGELGGRRALLQQALRRGEELAAAGGSVGPGAEPLHLAGLAERAASARRRWQRLEEAAARRERRLQEARALHQFGADLDGLLDWLRDAYRLAAAGDFGHDEASSRRLARQHRALTGEVEAHRGPVGGLRRQLATLGGASGAGPLVVALQVRVVEAEQLFAEVTEVAALRRQWLRDALAVYRMFGEVHACELWIGEKEQWLLAMRVPDSLDDVEVVQHRFESLDQEMNSLMGRVLDVNQTVQELVEGGHPSSDEVRSCQDHLNSRWNRIVELVEQRKEEMSAVLLVENHVLEVAEVRAQVREKRRAVESAPRAGGALQWRLSGLEAALQALEPRQAALLEEAALLAERFPAQATRLHQGAEELGAEWGALAGAAQACGEAVAAAGRLQRFLRDLDTFLDWLVRAQEAAGAVEGPLPRSLEEADGLLARHAALKEEVDQREEDYARIVAASEALLASDGAELGPGLALDEWLPHLEVGWHKLLGLWEERREALVQAHVYQLFLRDLCQALAVLRNQEVALSGAELPCTVESVEEAMKRHRDFLTTMELNQQKMQVAVQAAEGLLRQGNAYGEQAQEAVARLLEKSQENQLRAQQWMQKLLDQLVLQHFLRDCHELDGWIHEKMLMARDGTREDSHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQLFEASKADQLVQSFAELDKRLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWCREVGELQAQTAALPLEQASKELVGERQSAVGERLVRLLEPLQERRRLLLASKELHQVAHDLDDELAWVQERLPLAMLTERGTGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGVLASLRSPEAEAVRRGQEQLQSAWTGLREATERRQQTLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRRQSQVDRLYVALKELGEERRVSLEQQYWLYQLSRQVDELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETGTAGRERLAAVNQMVDELIECGHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASRELHKFFSDARELQGQIEEKRRRLPRLTAPPEPRPSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTVYAGEHAEAIASREQEVLQGWKELLAACEDARLHVSSTADALRFHSQARDLLSWMDGIAGQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELTACQELGRSLLLNKSAMADEIQAQLDKLGSRKEEVSEKWDRHWEWLQQMLEVHQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEAFRKAAAAWEERFSSLRRLTTIEKLKAEQSKQPPTPLLGRKFFGDPTELAAKAAPLLRPGGYDRGLEPLARRASDTLSAEVRTRVGYVRQELKPERLQPRIDRLPETSGKVEPAAPTAAALDTTDTPGTPAVTEQVRPRPERQELADRAEELPRRRRSERQESTDQPEEAARRRRPERQESADHEGPHSLTLGRYEQMERRRERRERRIERQESSEQETPTRGELVKGKATLADIVEQLQEKEAGPGLPAAVPSLPQPRELPPGRLPNGLEPPERTPRPDRPRARDRPKPRRRPRPREGGEGGGSRRSRSAPAQGGSAPAPPPPPTHTVQHEGFLLRKRELDANRKSSNRSWVNLYCVLSKGELGFYKDSKGPASGGTHGGEPLLSLHKATSEVASDYKKKKHVFKLQTQDGSEFLLQAKDEEEMNGWLEAVANSVAEHAEIARWGQTLPTTSSTDEGNPKREGGERRASGRRK
Protein: E3 SUMO-protein ligase SIZ2 (EC 2.3.2.-) (E3 SUMO-protein transferase SIZ2) (Q6ASW7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable SUMO E3 ligase that may regulate Pi starvation responses.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Os10g0536000 protein
- Os03g0123100 protein
- Small ubiquitin-related modifier
- Os04g0580400 protein
- Small ubiquitin-related modifier 1
- Os01g0372300 protein
- Os07g0574600 protein
- Os07g0574550 protein
- Os05g0534100 protein
- Os01g0852300 protein
Sequence:
MALDPADDPLLADCKYKLNHFRIKELKDVLHQLGLPKQGRKQELVDKIIAVLSDQQEQDSRLNGLPNKKMVGKETVAKIVDDTFAKMNGSTNAVPASRNQTDSGHIVKPKRKSDDSAQLDVKVRCPCGYSMANDSMIKCEGPQCNTQQHVGCVIISEKPADSVPPELPPHFYCDMCRITRADPFWVTVNHPVLPVSITPCKVASDGSYAVQYFEKTFPLSRANWEMLQKDEYDLQVWCILFNDSVPFRMQWPLHSDIQINGIPIRVVNRQPTQQLGVNGRDDGPVLTAYVREGSNKIVLSRSDSRTFCLGVRIAKRRSVEQVLSLVPKEQDGENFDNALARVRRCVGGGTEADNADSDSDIEVVADSVSVNLRCPMTGSRIKIAGRFKPCVHMGCFDLEAFVELNQRSRKWQCPICLKNYSLDNIIIDPYFNRITALVQSCGDDVSEIDVKPDGSWRVKGGAELKGLAQWHLPDGTLCMPTDTRSKPNIRIVKQEIKEEPLSEETGGRLKLGIRRNNNGQWEINKRLDSNNGQNGYIEDENCVVSASNTDDENSKNGIYNPEPGQFDQLTSNIYDLDSSPMDAHFPPAPTEQDVIVLSDSDDDNVMVLSPGDVNFSSAHDNGNAFPPNPPEASGICGEQPRGAGPDVTSFLDGFDDLELPFWESSSSQDAAGTQVTDNQCEMQNFIVNHQFLHEPILGVNLGGTAASNTLECEHDGALQACQSSDQDGDQNQTCHDGHSGDLTNLSIISTQDSLTNGKNASQKRTNCEDGTAGLDGSVVRSANGLRGEMPPLGQEQDRTVRQKLILTIESDSD
Protein: KQT-1 potassium channel (Potassium voltage-gated channel subfamily KQT member 5) (G5EDN5)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDEESGSSTDQAAPSDEQQEAGSSSAIGQESRKTVVFQEPDIGFPSEHDQLTTLHDSEEGNRKMSLVGKPLTYKNYRTDQRFRRMQNKMHNFLERPRGWKAATYHLAVLFMVLMCLALSVFSTMPDFEVNATIVLYYLEIVFVIWLATEYICRVWSAGCRSRYRGISGRIRFATSAYCVIDIIVILASITVLCIGATGQVFAASAIRGLRFFQILRMLRIDRRAGTWKLLGSVVWAHRQELLTTVYIGFLGLIFSSFLVYLCEKNTNDKYQTFADALWWGVITLSTVGYGDKTPETWPGKIIAAFCALLGISFFALPAGILGSGFALKVQQHQRQKHLIRRRVPAAKLIQCLWRHYSAAPESTSLATWKIHLARELPPIVKLTPNGSNNATGLINRLRQSTKRTPNLNNQNLAVNSQATSKNLSVPRVHDTISLVSTSDISEIEQLGALGFSLGWKSKSKYGGSKKATDDSVLQSRMLAPSNAHLDEEEAVGYQPQTIEEFTPALKNCVRAIRRIQLLVARKKFKEALKPYDVKDVIEQYSAGHVDLQSRVKTVQAKLDFICGKNIEKIEPKISMFTRIATLETTVGKMDKKLDLMVEMLMGRQASQRVFSQNTSPRGEFSEPTSARQDLTRSRRSMVSTDMEMYTARSHSPGYHGDARPIIAQIDADDDDEDENVFDDSTPLNNGPGTSSC
Protein: GTP-binding protein REM 2 (Rad and Gem-like GTP-binding protein 2) (Q9WTY2)
Organism: Rattus norvegicus (Rat)
Function: Binds GTP saturably and exhibits a low intrinsic rate of GTP hydrolysis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10727423}.
Interaction partners:
Sequence:
MHTDLDTDMDADTETVALCSSSSRQASPSGTPTPEADTTLLKQKPEKLLAELDRGGPPPAPGVPRRRGSMPVPYKHQLRRAQAVDELDWPPQASSSGSSDSLGSGEAALAQKDGVFKVMLLGESGVGKSTLAGTFGGLQGDNAHEMENSEDTYERRIMVDKEEVTLIVYDIWEQGDAGGWLQDHCLQTGDAFLIVFSVTDRRSFSKVPETLLRLRAGRPHHDLPVILVGNKSDLARSREVSLEEGRHLAGTLSCKHIETSAALHHNTRELFEGAVRQIRLRRGRGHAGGQRPEPSSPDGPAPPTRRESLTKKAKRFLANLVPRNAKFFKQRSRSCHDLSVL
Protein: Probable tetraspanin tspC (Q55CV7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- GH84 domain-containing protein
- Probable serine/threonine-protein kinase samkB
- Lipocalin/cytosolic fatty-acid binding domain-containing protein
Sequence:
MVNTRDFLPKTTHYLKVPIIGLNAILWLLGLVLIVVGSVCISFFSNFKEFTKESGYKNALSNLTTSAPTGVLVIGIFFILLTLVGCFVAYKEKLVGLVLYTMLMLILLVVLIGIGGKALTLDKEDAVSIIGTSWVQISNSLKNSTITKLEDFLECCCWSESYSNQTYKDLCPKDDDGNIKYEDTYCEGIFTKQVSSKLVLVGIAGVVIGCIEFVAMALSLFLIIRICRSPRSRAYDQY
Protein: 40S ribosomal protein S24 (Q6TEN7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNDTVTVRTRKFMTNRLLQRKQMIVDVLHPGKATVPKTEIREKLAKMYKTTPDVVFVFGFKTQFGGGKTTGFGMIYDSLDYAKKNEPKYRLQRVCHSLMLIVLHD
Protein: Bud site selection protein 14 (P27637)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Important for bud site selection. Seems to be a regulatory subunit of the BUD14-GLC7 type-I phosphatase complex. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex.
Interaction partners:
- Kelch repeat-containing protein 1
- Kelch repeat-containing protein 2
- Serine/threonine-protein phosphatase PP1-2
- BNI1-related protein 1
- Protein BNI1
- GTPase-activating protein BEM2/IPL2
- Kinesin-related protein SMY1
- Bud site selection protein 6
- RNA end formation protein 2
- Serine/threonine-protein kinase KIN2
Sequence:
MSNKEEHVDETSASGVKEVSSIAARHDNGYAPSLITSTSGMDSFQSHALLNDPTLIEDYSDIINNRPTSGSKLTLGNEDSESMGGSVVVTPTSNKSSPFNSKLNILSNAAEKGHDVLRNRDDDKELEEENVEKHMHSNSKRDQRHYKENSSELPDSYDYSDSEFEDNLERRLQEIETDSVDSADKDEVHFSVNNTMNPDVDDFSDGLKYAISEDEDEEENYSDDDDFDRKFQDSGFQGEKDDLEEENDDYQPLSPPRELDPDKLYALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRITDGKIGFAPAEILETFPERLARLNCWKNENMSSQSVASSDSKDDSISSGNKNQSDAESIIPTPALNGYGKGNKSVSFNDVVGYADRFIDDAIEDTSLDSNDDGGEGNGQSYDDDVDNDKETKVTHRDEYTEAKLNFGKFQDDDTSDVVSDVSFSTSLNTPLNVKKVRRQDNKNESEPKTSSSKDREDDYNANRYVGQEKSEPVDSDYDTDLKKVFEAPRMPFANGMAKSDSQNSLSTIGEFSPSSSEWTNESPSTPIVEESSSIPSSRAIKDISQYIHAKSKIEETTNVENTEGQIQASLGSSGGMANQTDAEQPKEELEKHHSTPEEEKQSTLSLHSSSEEDFYMDEQRAVSSASINSSLSGSRALSNTNMSDPASKPNSLVQHLYAPVFDRMDVLMKQLDEIIRK
Protein: Thermosome subunit beta (Chaperonin subunit beta) (Thermophilic factor 55 beta) (TF55-beta) (Thermosome subunit 2) (Q9V2T8)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
Interaction partners:
- Thermosome subunit alpha
- TATA-box-binding protein
- Translation initiation factor 5A
- Prefoldin subunit alpha
- Proteasome subunit beta 1
- Large ribosomal subunit protein uL4
- Probable translation initiation factor IF-2
- Prefoldin subunit beta
- Proteasome subunit alpha
- GTPase
Sequence:
MATATVATTPEGIPVIILKEGSSRTYGKEALRANIAAVKAIEEALKSTYGPRGMDKMLVDSLGDITITNDGATILDKMDLQHPTGKLLVQIAKGQDEETADGTKTAVILAGELAKKAEDLLYKEIHPTIIVSGYKKAEEIALKTIQEIAQPVTINDTDVLRKVALTSLGSKAVAGAREYLADLVVKAVAQVAELRGDKWYVDLDNVQIVKKHGGSVNDTQLVYGIVVDKEVVHPGMPKRIENAKIALLDASLEVEKPELDAEIRINDPTQMHKFLEEEENILKEKVDKIAATGANVVICQKGIDEVAQHYLAKKGILAVRRAKKSDLEKLARATGGRVISNIDELTSQDLGYAALVEERKVGEDKMVFVEGAKNPKSVSILIRGGLERVVDETERALRDALGTVADVIRDGRAVAGGGAVEIEIAKRLRKYAPQVGGKEQLAIEAYANAIEGLIMILAENAGLDPIDKLMQLRSLHENETNKWYGLNLFTGNPEDMWKLGVIEPALVKMNAVKAATEAVTLVLRIDDIVAAGKKSGSEPSGKKEKDKEEKSSED
Protein: FI03664p (Formin homology 2 domain containing, isoform B) (Q9VSQ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIVKMEPDELITFRVQYLVDSDPLSACTAFPIPVRAPTYAFATTMPLANQLGTILRLLNAPQSIDDAAIQVYKDGDYGAYLDLESSLAEQAEEIEGVNVSRKNSLVVRTQLNVRVQAIIEKLLSAQGSDLRRALFSLKQVFQEDKDLVHAFVALGGLNCLVRVGNCADQNYQNYILRALGQVMLYVDGMNGVMKHEPTMQWLYSLIASNYRSVVKTALKLLLVFVEYAESNCYVLVSAIHAVDASQGTLPWSNIMRLLKDYDNADAELVIYATSLINKTLAGLNDQDSFYDESDLLEQQGMETVIQRYMSKPGTDLDLLDQLQLYEAVLKFEDGESDGQRLPQNSMRKTQRYRPGANTTERRKSRRHSTDNSPASLTKVLPTTVLRMTPTQATVDEDSSGSTNSTEFSGGLFNEKKPRDGAGVTPGLRRRRERAERHKSFLKEQQEAAANGIFAALEQREGLGQIVTAIPATIQTGDSPPQSLQHEVPPCNNISGITNISNNNVSNLSCNDTPNNSLLVMSPSKQLLTGSHSISIINNSFDKASNNNQSEFLTKKNLFRERNSTVINGIMKNIQQTDSAYKKYENEANRLNNYYSQSPKHQIHQPIQPTPEVLLSPKKTLNASGFDFTPAPLSSTPVKCDVPPEPEPLSPVKKPAAAPPPPPPPPPPPPPPPGWWHAPIYNSPQARTLTSTNPELLPHPVDPSDMESEDQQLLLQLKRDHTVKDLTQKLSNLPMSPTQDSANRALVGDMSGLISKAKEGLAKSKSKGEISRSSSVDQDVKKSEPKKSENELHWEELVRNMTRPLNLCDLDFTDLRDDDEKDVLAPRSLGAGIPPPPPPLGGAIAPPPMMPPSLAPPPMYGYGGSLTNSVNSLNGSINGELVNGNNTIKKNKKTVKLFWKEVREDMIPQVVGKTIWDELPDANVDTQKLEHLFESRAKDLMTKKQQELNKSKEIIVLDHKRSNAINIAITKLPPPRAIKTAILKMDATVVTREGIDKLLNMLPTDEERGKIQEAQLSNPELPLGSAEQFLLTLASISELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNGAPVKGFQIEYLAKVPEVKDTVHKHSLLHHLCHMVMESSSDTSDLYSEIGPITRASKADFTDLAHNLNQLEAECKACWDRLKLIAKHDCPPPLKQKLVDFLADCAERIIILQIVHRRVMNRYRKFLLWLGMPQHSVAESRPNEFCRTLSEFALEYRTTRERVQQQLEKKANHRERNKTRGKLIIDMAKFKTKDDVADDELK
Protein: PhoP/PhoQ regulator MgrB (P64512)
Organism: Escherichia coli (strain K12)
Function: Represses PhoP/PhoQ signaling, possibly by binding to the periplasmic domain of PhoQ, altering its activity and that of downstream effector PhoP. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB are required for its action on PhoQ, and thus PhoP.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:20041203}; Single-pass membrane protein {ECO:0000305|PubMed:20041203}.
Interaction partners:
- Sensor protein PhoQ
- Signal transduction protein PmrD
- Transcriptional regulatory protein PhoP
- Sensor protein BasS
- Transcriptional regulatory protein BasR
- Phosphoethanolamine transferase EptA
- Uncharacterized protein YebO
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Magnesium-transporting ATPase, P-type 1
- Two-component-system connector protein SafA
Sequence:
MKKFRWVVLVVVVLACLLLWAQVFNMMCDQDVQFFSGICAINQFIPW
Protein: Type III polyketide synthase A (PKS-A) (EC 2.3.1.-) (Hydroxyalkyl alpha-pyrone synthase PKS-A) (Protein LESS ADHESIVE POLLEN 6) (O23674)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant type III polyketide synthases (PKSs) that catalyzes the condensation of malonyl-CoA units with various CoA ester starter molecules to generate a diverse array of natural products including long-chain alkyl alpha-pyrones. Accepts up to C(20) chain-length fatty acyl CoAs as starter substrates, and carries out sequential condensations with malonyl-CoA to produce triketide and tetraketide alpha-pyrones, potential sporopollenin precursors. Favorite substrates for are midchain- and v-hydroxylated fatty acyl-CoAs (e.g. 12-hydroxyoctadecanoyl-CoA and 16-hydroxyhexadecanoyl-CoA). Required for pollen development and sporopollenin biosynthesis, the major constituent of exine in the outer pollen wall. In vitro, can use 4-coumaroyl-coenzyme A as substrate to produce bis-noryangonin and fatty acyl-coenzyme A as substrate to produce medium-chain alkyl pyrones. May play a role in both the synthesis of pollen fatty acids and phenolics found in exine.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:21193570, ECO:0000269|PubMed:23632852}.
Interaction partners:
- Putative acyl-activating enzyme 19
- Tetraketide alpha-pyrone reductase 1
- Cytochrome P450 704B1
- 4-coumarate--CoA ligase-like 1
- Cytochrome P450 703A2
- Tetraketide alpha-pyrone reductase 2
- holo-[acyl-carrier-protein] synthase
- holo-[acyl-carrier-protein] synthase
- ABC transporter G family member 26
- Short-chain dehydrogenase reductase ATA1
Sequence:
MSNSRMNGVEKLSSKSTRRVANAGKATLLALGKAFPSQVVPQENLVEGFLRDTKCDDAFIKEKLEHLCKTTTVKTRYTVLTREILAKYPELTTEGSPTIKQRLEIANEAVVEMALEASLGCIKEWGRPVEDITHIVYVSSSEIRLPGGDLYLSAKLGLRNDVNRVMLYFLGCYGGVTGLRVAKDIAENNPGSRVLLTTSETTILGFRPPNKARPYDLVGAALFGDGAAAVIIGADPRECEAPFMELHYAVQQFLPGTQNVIEGRLTEEGINFKLGRDLPQKIEENIEEFCKKLMGKAGDESMEFNDMFWAVHPGGPAILNRLETKLKLEKEKLESSRRALVDYGNVSSNTILYVMEYMRDELKKKGDAAQEWGLGLAFGPGITFEGLLIRSLTSS
Protein: Cystatin-like protein (P23779)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Superoxide dismutase
Sequence:
MNVVKSLCILGLVLVSLIATQAADEQVVGGVSQLEGNSRKEALELLDATLAQLATGDGPSYKAINVTSVTGQVVAGSLNTYEVELDNGSDKKQCTVKIWTQPWLKENGTNIKIKCSGDDGELDRTW
Protein: 5-methylthioadenosine/S-adenosylhomocysteine deaminase (MTA/SAH deaminase) (EC 3.5.4.28) (EC 3.5.4.31) (Q9X034)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine. Adenosine-5-monophosphate (AMP) and S-adenosyl-L-methionine (SAM) are not enzyme substrates.
Interaction partners:
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- Polyamine aminopropyltransferase
- Conserved hypothetical protein
- Conserved hypothetical protein
Sequence:
MIIGNCLILKDFSSEPFWGAVEIENGTIKRVLQGEVKVDLDLSGKLVMPALFNTHTHAPMTLLRGVAEDLSFEEWLFSKVLPIEDRLTEKMAYYGTILAQMEMARHGIAGFVDMYFHEEWIAKAVRDFGMRALLTRGLVDSNGDDGGRLEENLKLYNEWNGFEGRIFVGFGPHSPYLCSEEYLKRVFDTAKSLNAPVTIHLYETSKEEYDLEDILNIGLKEVKTIAAHCVHLPERYFGVLKDIPFFVSHNPASNLKLGNGIAPVQRMIEHGMKVTLGTDGAASNNSLNLFFEMRLASLLQKAQNPRNLDVNTCLKMVTYDGAQAMGFKSGKIEEGWNADLVVIDLDLPEMFPVQNIKNHLVHAFSGEVFATMVAGKWIYFDGEYPTIDSEEVKRELARIEKELYSS
Protein: ATP-binding cassette sub-family G member 5 (EC 7.6.2.-) (Sterolin-1) (Q99PE8)
Organism: Mus musculus (Mouse)
Function: ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane. Plays an essential role in the selective transport of dietary plant sterols and cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile. Required for normal sterol homeostasis. The heterodimer with ABCG8 has ATPase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:18402465, ECO:0000305|PubMed:16352607}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP-binding cassette sub-family G member 8
- Cytochrome P450 7A1
- NPC1-like intracellular cholesterol transporter 1
- Oxysterols receptor LXR-alpha
- Bile acid receptor
- Sterol regulatory element-binding protein 2
- Apolipoprotein A-I
- Oxysterols receptor LXR-beta
- Hepatic sodium/bile acid cotransporter
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MGELPFLSPEGARGPHINRGSLSSLEQGSVTGTEARHSLGVLHVSYSVSNRVGPWWNIKSCQQKWDRQILKDVSLYIESGQIMCILGSSGSGKTTLLDAISGRLRRTGTLEGEVFVNGCELRRDQFQDCFSYVLQSDVFLSSLTVRETLRYTAMLALCRSSADFYNKKVEAVMTELSLSHVADQMIGSYNFGGISSGERRRVSIAAQLLQDPKVMMLDEPTTGLDCMTANQIVLLLAELARRDRIVIVTIHQPRSELFQHFDKIAILTYGELVFCGTPEEMLGFFNNCGYPCPEHSNPFDFYMDLTSVDTQSREREIETYKRVQMLECAFKESDIYHKILENIERARYLKTLPTVPFKTKDPPGMFGKLGVLLRRVTRNLMRNKQAVIMRLVQNLIMGLFLIFYLLRVQNNTLKGAVQDRVGLLYQLVGATPYTGMLNAVNLFPMLRAVSDQESQDGLYHKWQMLLAYVLHVLPFSVIATVIFSSVCYWTLGLYPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSIVALLSISGLLIGSGFIRNIQEMPIPLKILGYFTFQKYCCEILVVNEFYGLNFTCGGSNTSMLNHPMCAITQGVQFIEKTCPGATSRFTANFLILYGFIPALVILGIVIFKVRDYLISR
Protein: Erythrocyte-binding antigen 175 (EBA-175) (P19214)
Organism: Plasmodium falciparum (isolate Camp / Malaysia)
Function: Binds to host erythrocytes; may act as bridge between erythrocytes and merozoites.
Interaction partners:
Sequence:
MKCNISIYFFASFFVLYFAKARNEYDIKENEKFLDVYKEKFNELDKKKYGNVQKTDKKIFTFIENKLDILNNSKFNKRWKSYGTPDNIDKNMSLINKHNNEEMFNNNYQSFLSTSSLIKQNKYVPINAVRVSRILSFLDSRINNGRNTSSNNEVLSNCREKRKGMKWDCKKKNDRSNYVCIPDRRIQLCIVNLSIIKTYTKETMKDHFIEASKKESQLLLKKNDNKYNSKFCNDLKNSFLDYGHLAMGNDMDFGGYSTKAENKIQEVFKGAHGEISEHKIKNFRKEWWNEFREKLWEAMLSEHKNNINNCKNIPQEELQITQWIKEWHGEFLLERDNRSKLPKSKCKNNTLYEACEKECIDPCMKYRDWIIRSKFEWHTLSKEYETQKVPKENAENYLIKISENKNDAKVSLLLNNCDAEYSKYCDCKHTTTLVKSVLNGNDNTIKEKREHIDLDDFSKFGCDKNSVDTNTKVWECKNPYILSTKDVCVPPRRQELCLGNIDRIYDKNLLMIKEHILAIAIYESRILKRKYKNKDDKEVCKIINKTFADIRDIIGGTDYWNDLSNRKLVGKINTNSKYVHRNKKNDKLFRDEWWKVIKKDVWNVISWVFKDKTVCKEDDIENIPQFFRWFSEWGDDYCQDKTKMIETLKVECKEKPCEDDNCKSKCNSYKEWISKKKEEYNKQAKQYQEYQKGNNYKMYSEFKSIKPEVYLKKYSEKCSNLNFEDEFKEELHSDYKNKCTMCPEVKDVPISIIRNNEQTSQEAVPEENTEIAHRTETPSISEGPKGNEQKERDDDSLSKISVSPENSRPETDAKDTSNLLKLKGDVDISMPKAVIGSSPNDNINVTEQGDNISGVNSKPLSDDVRPDKKELEDQNSDESEETVVNHISKSPSINNGDDSGSGSATVSESSSSNTGLSIDDDRNGDTFVRTQDTANTEDVIRKENADKDEDEKGADEERHSTSESLSSPEEKMLTDNEGGNSLNHEEVKEHTSNSDNVQQSGGIVNMNVEKELKDTLENPSSSLDEGKAHEELSEPNLSSDQDMSNTPGPLDNTSEETTERISNNEYKVNEREDERTLTKEYEDIVLKSHMNRESDDGELYDENSDLSTVNDESEDAEAKMKGNDTSEMSHNSSQHIESDQQKNDMKTVGDLGTTHVQNEISVPVTGEIDEKLRESKESKIHKAEEERLSHTDIHKINPEDRNSNTLHLKDIRNEENERHLTNQNINISQERDLQKHGFHTMNNLHGDGVSERSQINHSHHGNRQDRGGNSGNVLNMRSNNNNFNNIPSRYNLYDKKLDLDLYENRNDSTTKELIKKLAEINKCENEISVKYCDHMIHEEIPLKTCTKEKTRNLCCAVSDYCMSYFTYDSEEYYNCTKREFDDPSYTCFRKEAFSSMIFKFLITNKIYYYFYTYKTAKVTIKKINFSLIFFFFFSF
Protein: Uncharacterized protein (Q381R0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHLPPLPKNQKPRTARCGTDSVVQIDDSTLLSMFRTRRRRMETASNISKSMVKRINNLSEAVYESSMTTMLLEDLNTLVETSGANGGEKVVISDDPVMSLGAGPFSVSLESALEHETIQKLRTLTVMRAEQRKAAELNTKPHFQLKESVLETPQPPIKFSSTSLTFVLEIVSQSAFKILDATDSVMLKLSMLARKAGSPIVDEMKVISVHSQHLSRCHAAALSHLKQYEACEKCLNKATAYELGNAREQLIEQKEVLTAQEKRQKVAEDQLQALRTRLASYEAQCRLWSSFLYERQHPACTGGFPISLETESASPLTSKAASLRAPQASLHSTDPLLRTTSGLRRGSSTYQMNLHTMRPHTPLTMGSVSSSLPSSHEEINPRVDSVEMRVAQFWCNPYLLKAKQCRNWRRSGAHSVADSPPLTESIFQASISRSRLASRVESSVGPVDSAHMSRGDIHAGGSTDLSDTNTADTRLTVLLRGLLRGIVRLRRRPTNEGGSTGGGREESEEVRLEGTPTSDSNAPRGNATTEEGSTSESSPRGSLHERGVGEGSPWAELSGSEGGNTSIGECSAGPGGAVNTAGGTPERGTGTLMSEGSGEADALLASVRKLISFLEGRVSLS
Protein: Probable glutamine synthetase (Q9I6J5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Glutamate dehydrogenase
- Glutamate synthase large chain
- Glutaminase
- Assimilatory nitrite reductase large subunit
- Glutamate synthase small chain
- Probable aldehyde dehydrogenase
- Bifunctional protein PutA
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
- Glutamine--fructose-6-phosphate aminotransferase
Sequence:
MSVPQRAVQLTEPSEFLKEHPEVQFVDLLIADMNGVVRGKRIERNSLNKVFEKGINLPASLFALDITGSTVESTGLGLDIGDADRICYPIPGTLSMEPWQKRPTAQLLMTMHELEGEPFFADPREVLRQVVARFTEMELTIVAAFELEFYLIDQENVNGRPQPPRSPISGKRPQSVQVYSIDDLDEYVECLQDIIDGARAQGIPADAIVAESAPAQFEVNLNHVNDALKACDHAVLLKRLVKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISLLDKHGNNIFTSEDPEQNAALRHAIGGVLETLPASMAFLCPNVNSYRRFGSQFYVPNAPSWGLDNRTVALRVPTGSPDAVRLEHRVAGADANPYLLLAAVLAGVHHGLTNKVEPGAPIEGNSYEQMEPSLPNNLRDALRELDESEIMAKYIDPKYIDIFVACKESELEEFEHSISDLEYNWYLHTV
Protein: Hemoglobin alpha, adult chain 2 (A0A0A0MP82)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVLSADDKTNIKNCWGKIGGHGGEYGEEALQRMFAAFPTTKTYFSHIDVSPGSAQVKAHGKKIGGHGGEYGEEALQRMFAAFPTTKTYFSHIDVSPGSAQVKAHGKKVADALAKAADHVEDLPGALSTLSDLHAHKLRVDPVNFKFLSHCLLVTLACHHPGDFTPAMHASLDKFLASVSTVLTSKYR
Protein: Probable anthranilate synthase component 1 (EC 4.1.3.27) (Anthranilate synthase component I) (O94582)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
- Anthranilate phosphoribosyltransferase
- Tryptophan synthase
- Chorismate synthase
- Chorismate mutase
- Adenine phosphoribosyltransferase
- Putative aminodeoxychorismate synthase
- Aromatic amino acid aminotransferase C1773.13
- Aromatic amino acid aminotransferase C569.07
- Aromatic amino acid aminotransferase C56E4.03
Sequence:
MKIYPDLKQVQELAEKHKANKIPIYGVIPADMLTPSVAYLKLNQGKKYSFILESVTQGESVSRYSFIGSPYRILMANGKTDPLARLERELKEVKTAPVEGLPSFSGGAVGYVSYDCIKYFEPTTEMPLEDTLGLPEAMFFMTDDLVAFDHAYQTVKIISHVCIQQGRPIEEAYEAAVFKINMLKKKLESPEIPLPEQKKVHLGYEAKSNVGEDGYKAFVSNLKEHIFNGDIFQAVPSQRIARRTDLHPFNLYRHLRTVNPSPYMFYIHCDDFDIIGASPELLVKSEHGRIINHPIAGTVPRGKTKEEDEAYAKDLLASVKDRAEHVMLVDLARNDVSRVCDLDTTSVDKLMTIEKFSHVQHLVSQVSGVLRPDKTRFDAFRSIFPAGTVSGSPKVRAIQLVYGLEKEKRGIYAGAVGRWGYEDDNMDTCIAIRTMVYKDGTVYLQAGGGIVFDSDEQDEYVETLNKLRSNVTAIEETEKLYAEEENSSA
Protein: ORF169b (Q8VSD5)
Organism: Shigella flexneri
Interaction partners:
Sequence:
MINGVSLQGTAGYEAHTEEGNVNVKKLLESLNSKSLGDMDKDSELAATLQKMINPSGGDGNCSGCALHACMAMLGYGVREAPVPNEISEYMTGFFHRHLEQIDSEGIVSHPNETYSKFRERIAENILQNTSKGSVVMISIEQATHWIAGFNDGEKIMFLDVQTGKGFNLYDPVEKSPDAFVDENSSVQVIHVSDQEFDHYANSSSWKSKRLC