wanglab/gogpt-training-data huggingface dataset:
Protein: Inositol-3-phosphate synthase 1 (IPS 1) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (MI-1-P synthase) (MIP synthase) (MIPS) (Q8A7J8)
Organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3-phosphate in a NAD-dependent manner.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inositol-1-monophosphatase
- Phosphatidylinositol phosphate synthase
- Phosphoinositol dihydroceramide synthase
- Hexokinase type III
- Phosphoglucomutase phosphomannomutase
- ROK family transcriptional repressor, with glucokinase domain
- ROK family transcriptional repressor
- ROK family transcriptional repressor, with glucokinase domain
- GtrA/DPMS transmembrane domain-containing protein
- Putative phosphatidylinositol-3-phosphatase
Sequence:
MKQEIKPATGRLGVLVVGVGGAVATTMIVGTLASRKGLAKPIGSITQLATMRMENNEEKLIKDVVPLTDLNDIVFGGWDIFPDNAYEAAMYAEVLKEKDLNGVKDELEAIKPMPAAFDHNWAKRLNGTHIKKAATRWEMVEQLRQDIRDFKAANNCERVVVLWAASTEIYIPLSDEHMSLAALEKAMKDNNTEVISPSMCYAYAAIAEDAPFVMGAPNLCVDTPAMWEFSKQKNVPISGKDFKSGQTLMKTVLAPMFKTRMLGVNGWFSTNILGNRDGEVLDDPDNFKTKEVSKLSVIDTIFEPEKYPDLYGDVYHKVRINYYPPRKDNKEAWDNIDIFGWMGYPMEIKVNFLCRDSILAAPIALDLVLFSDLAMRAGMCGIQTWLSFFCKSPMHDFEHQPEHDLFTQWRMVKQTLRNMIGEKEPDYLA
Protein: Uncharacterized protein (Q583P8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MQQRSISPGRGRVVPRGQLTRSARGSTISCSSPQRPQAVVNELHRRDGTNPTTDRGRQIAEEVDELMNEVYGGTAHQPPPESLQRHAEGGNLLARYKTSILASALPTSWQRGPSDPAGLCFDASDRNLLCMDVYEKRGLCVVGSADHGLKVFDLATGAEKRNLYTKKYGHTEWVTCCKFLPDSGKILSGGMDSKLCLWEASGPARCTDLTGHTGSISQVEVCGNNGFALSSSYDRTLRLWDCGAGGRCIATFAGHKAPVMMFSWCGTQLLSGDRQGTAKMWDVESGECLATMATKRGQIGSLWHTLHTSVGLLSAIGDQGGVLTVMDFPRTGSRPIFQGELHPGGVISSIRSVDETPYLITAGADKVILTLDPRAGFAVVHNFTDHRDFIYSMETFGPLVLSGGGNGWLLVHNVLDGKCCYGLGANGAAVREIRTTSEYLVAAGDDGKAMVYRFN
Protein: Tight junction protein 2 (Tight junction protein ZO-2) (Zona occludens protein 2) (Zonula occludens protein 2) (Q9UDY2)
Organism: Homo sapiens (Human)
Function: Plays a role in tight junctions and adherens junctions (By similarity). Acts as a positive regulator of RANKL-induced osteoclast differentiation, potentially via mediating downstream transcriptional activity (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9Z0U1}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9Z0U1}. Nucleus {ECO:0000250}. Note=Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures. Localizes to tight junctions during initial stages of their formation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q95168}.
Interaction partners:
- Occludin
- Afadin
- Cingulin
- Tight junction protein 1
- Claudin-1
- MARVEL domain-containing protein 2
- Junctional adhesion molecule A
- Claudin-7
- Transcriptional coactivator YAP1
- Claudin-5
Sequence:
MPVRGDRGFPPRRELSGWLRAPGMEELIWEQYTVTLQKDSKRGFGIAVSGGRDNPHFENGETSIVISDVLPGGPADGLLQENDRVVMVNGTPMEDVLHSFAVQQLRKSGKVAAIVVKRPRKVQVAALQASPPLDQDDRAFEVMDEFDGRSFRSGYSERSRLNSHGGRSRSWEDSPERGRPHERARSRERDLSRDRSRGRSLERGLDQDHARTRDRSRGRSLERGLDHDFGPSRDRDRDRSRGRSIDQDYERAYHRAYDPDYERAYSPEYRRGARHDARSRGPRSRSREHPHSRSPSPEPRGRPGPIGVLLMKSRANEEYGLRLGSQIFVKEMTRTGLATKDGNLHEGDIILKINGTVTENMSLTDARKLIEKSRGKLQLVVLRDSQQTLINIPSLNDSDSEIEDISEIESNRSFSPEERRHQYSDYDYHSSSEKLKERPSSREDTPSRLSRMGATPTPFKSTGDIAGTVVPETNKEPRYQEDPPAPQPKAAPRTFLRPSPEDEAIYGPNTKMVRFKKGDSVGLRLAGGNDVGIFVAGIQEGTSAEQEGLQEGDQILKVNTQDFRGLVREDAVLYLLEIPKGEMVTILAQSRADVYRDILACGRGDSFFIRSHFECEKETPQSLAFTRGEVFRVVDTLYDGKLGNWLAVRIGNELEKGLIPNKSRAEQMASVQNAQRDNAGDRADFWRMRGQRSGVKKNLRKSREDLTAVVSVSTKFPAYERVLLREAGFKRPVVLFGPIADIAMEKLANELPDWFQTAKTEPKDAGSEKSTGVVRLNTVRQIIEQDKHALLDVTPKAVDLLNYTQWFPIVIFFNPDSRQGVKTMRQRLNPTSNKSSRKLFDQANKLKKTCAHLFTATINLNSANDSWFGSLKDTIQHQQGEAVWVSEGKMEGMDDDPEDRMSYLTAMGADYLSCDSRLISDFEDTDGEGGAYTDNELDEPAEEPLVSSITRSSEPVQHEESIRKPSPEPRAQMRRAASSDQLRDNSPPPAFKPEPPKAKTQNKEESYDFSKSYEYKSNPSAVAGNETPGASTKGYPPPVAAKPTFGRSILKPSTPIPPQEGEEVGESSEEQDNAPKSVLGKVKIFEKMDHKARLQRMQELQEAQNARIEIAQKHPDIYAVPIKTHKPDPGTPQHTSSRPPEPQKAPSRPYQDTRGSYGSDAEEEEYRQQLSEHSKRGYYGQSARYRDTEL
Protein: SET domain-containing protein (Q382I1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRAVAGGTQSFFVAARALFFHFFFSFPVFAELLGGEPFYQHSEGTAGSPASLSRRVKMRCCRTMHGLGEWSNGLSILSDALTQVIESRGTGKDNVLRAPLRCVVASRSICRGEQLCVVPESHILHGEIADSVLQHATAGGNFTSYAELRRRLATVSGMPHLLSTRDSLLITLALYTLRHGGVNHPLTKWVSSLPPRVPPMGLLLQLQEKRASAFTPLQRRLRAGTRTALISSPLEHADTDVATVELMLQAAESCGIDAVSKPQVEVVATEPLIAAFCRGKRHPLTQRQHEANLAKSRGSLSAAQQQLVQLETSVYSDILTPLQRCMFADNLLPTPPTSTTNQPGDDDAGGDPKTIEQLRWSHFMMRSRAVNLHFIPHRQQQRAQPPKVAVVPFLDMLNHSVRSHNVTYRYRSGIGVVVVASRLIKKGEELTLNYGDFRQRGCLFHEPSCCAGADVIDGSAAMRLIESRQMHEWDNAADSSLDVDHPEDAPFGQGPERQQQRDGKSNLGDQSDYGEEARMEATWLWRFGFPRTEDEKAYVASHLWSKGLRRRVAQLTDVRRRGRPGEFVIGVPEGLQHLREQRERLERERFGGVKVFPPQNA
Protein: Integration host factor subunit alpha (IHF-alpha) (A5F1W7)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Function: This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Interaction partners:
Sequence:
MALTKAELAEALFEQLGMSKRDAKDTVEVFFEEIRKALESGEQVKLSGFGNFDLRDKNERPGRNPKTGEDIPITARRVVTFRPGQKLKARVENIKVEK
Protein: Chloride intracellular channel protein 4 (Glutaredoxin-like oxidoreductase CLIC4) (EC 1.8.-.-) (Intracellular chloride ion channel protein p64H1) (Q9Z0W7)
Organism: Rattus norvegicus (Rat)
Function: Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. May play a role in angiogenesis (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y696}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9Y696}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9Y696}. Nucleus {ECO:0000250|UniProtKB:Q9Y696}. Cell membrane {ECO:0000250|UniProtKB:Q9Y696}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9Y696}. Mitochondrion {ECO:0000269|PubMed:26777142}. Cell junction {ECO:0000250|UniProtKB:Q9Y696}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9295337}; Single-pass membrane protein {ECO:0000305|PubMed:17453412}. Note=Colocalized with AKAP9 at the centrosome and midbody. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain. Present in an intracellular vesicular compartment that likely represent trans-Golgi network vesicles. Might not be present in the nucleus of cardiac cells. {ECO:0000250|UniProtKB:Q9Y696, ECO:0000269|PubMed:26777142}.
Interaction partners:
Sequence:
MALSMPLNGLKEEDKEPLIELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFSVTTVDLKRKPAHLQNLAPGTHPPFITFNSEVKTDVNKIEEFLEEVLCPPKYLKLSPKHPESNTAGMDIFAKFSAYIKNSRPEANEALERGLLKTLQKLDEYLNSPLPGEIDENSMEDIKSSTRRFLDGDEMTLADCNLLPKLHIVKVVAKKYRNFDIPKGMTGIWRYLTNAYSRDEFTNTCPSDKEVEIAYSDVAKRLTK
Protein: Dek, isoform C (A1ZAK3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVCKKDANKAAETAAKENAADKVSDVENASVTAGVAKAVGAQPERGSKDAAESPAAVDASASAATDDVADKKAKGDSTAVSNTESDAAAADKKEKSPSPVIKKSNNKDAKKEDNSEKDEENSEDGDEPEDEADEKASDEESEKKKPKLDAEDKIKDATDESKPKSGADKPKKPEPKAKNGKVAKEEDDDEEDEDDEDAEDDDGDENDGLDKNNEVAEDDENVVALAEIDRINENINKTRVDGLQTLHAICFGAQGKNNVVKKNLRSFAGFEFAKDSAEYNKKLEAIKKVDNKGLRSICEILTLDRKGSKNETVLRVLKFLMEPDESLCLEQGDEEEEEDAEDEDLDEDEEDPPSEEDKKRKSGKSSGGAGRGSARNSTGRPRRATAGKKMSAYVDFSSSDDSEQKVAVPKRRRNDDSESGSDYNPSANSDSDGGRGGGAGAAGRKVPSRGGRGRPARKSRRRNSDSEEEEESEVSDADSDVPKRKRGSVGKRGRPAAPASAGRRGRGRGAASRKRKDSDSEDEEVSEDEEEEDVSDFASDQSEEERPKKSKKPITPAKNSKANNKSKPAGKADSRSKKSKKESSEEDDDVDDKDESDEDEPLTKKGKQAFPTDEQIRGYVKEILDKANLEEITMKTVCKQVYAKYPDFDLTDKKDFIKATVKALIAT
Protein: Beta-arrestin arr-1 (P51485)
Organism: Caenorhabditis elegans
Function: Adapter protein required for olfactory adaptation and recovery to volatile odorants, probably by desensitization of G-protein coupled receptors (GPCR). May play a role in clathrin-mediated GPCR endocytosis. Acts as positive regulator of insulin-like daf-2 signaling pathway probably by forming a complex with mpz-1 and phosphatase daf-18 likely resulting in daf-18 inhibition. Involved in egg-laying.
Subcellular location: Perikaryon {ECO:0000269|PubMed:15878875}. Cell projection, dendrite {ECO:0000269|PubMed:15878875}. Note=Localizes to the amphid processes of chemosensory neurons. {ECO:0000269|PubMed:15878875}.
Interaction partners:
- Probable clathrin heavy chain 1
- mitogen-activated protein kinase kinase
- mitogen-activated protein kinase kinase
- MAP kinase kinase mkk-4
- G-protein coupled receptors family 1 profile domain-containing protein
- AP complex subunit beta
- Dynamin
- G protein-coupled receptor kinase 2
- ENTH domain-containing protein
- Muscarinic acetylcholine receptor gar-3
Sequence:
MVDEDKKSGTRVFKKTSPNGKITTYLGKRDFIDRGDYVDLIDGMVLIDEEYIKDNRKVTAHLLAAFRYGREDLDVLGLTFRKDLISETFQVYPQTDKSISRPLSRLQERLKRKLGANAFPFWFEVAPKSASSVTLQPAPGDTGKPCGVDYELKTFVAVTDGSSGEKPKKSALSNTVRLAIRKLTYAPFESRPQPMVDVSKYFMMSSGLLHMEVSLDKEMYYHGESISVNVHIQNNSNKTVKKLKIYIIQVADICLFTTASYSCEVARIESNEGFPVGPGGTLSKVFAVCPLLSNNKDKRGLALDGQLKHEDTNLASSTILDSKTSKESLGIVVQYRVKVRAVLGPLNGELFAELPFTLTHSKPPESPERTDRGLPSIEATNGSEPVDIDLIQLHEELEPRYDDDLIFEDFARMRLHGNDSEDQPSPSANLPPSLL
Protein: Spindle assembly abnormal protein 6 homolog (Q9VAC8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication. In ciliated neurons, required for centriole assembly but not necessary for cilium basal body and cilia function. Required for sperm cilium basal body elongation together with Cep135 and Ana2.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17463247, ECO:0000269|PubMed:30013109}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:29892014}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:30013109}. Note=Component of the centrosome. {ECO:0000269|PubMed:17463247}.
Interaction partners:
- Anastral spindle 2, isoform A
- Spindle assembly abnormal 4
- Centrosomal protein 135kDa, isoform B
- Serine/threonine-protein kinase PLK4
- BcDNA.LD24702
- Anastral spindle 1, isoform A
- Asterless
- Centriolar coiled coil protein 110kDa, isoform B
- Pericentrin-like protein, isoform F
- Centrosomin
Sequence:
MWPPGSEDSYSAKMDYGKSVVNILPSVEMLVNFNGEMTRSSKRSCLLYAERVDFKELLQLRLTEKSDQRRMYITTVDSASFQDLKQDQSLNVSFSGFIDNVVRMLKDCQSGKLELHLTTRDQNLSSGREVHDYYLQFVEIRSFKNLVHLSLPCRSAPLNTVLFYINSMLEASHKKQYILEQSMQQMQAEINAQRAHAERLTTENTNIREALAENTRILEEKHAAEVHQYQEKLSKINEQRSNELERNRRAISGFQAQLDKASLEKAELKSAQEQAEKRCQTLSEELSCCKARVCTLKEQNDKLHGDVANIRKHERKLEYKIEDLKQHTVELQEHIQKGNKEKANIAAELEAEKKILHTKRQALEMASEEISKANQIIVKQSQELLNLKKTIAWRTEVALQQEKAVQAKESLLSLRENELREARITIEKLREEIPQQLQSMRNFAQGLEQKYSKQILILKERLAIPTGKENRR
Protein: High affinity choline transporter 1 (rCHT1) (Hemicholinium-3-sensitive choline transporter) (CHT) (Solute carrier family 5 member 7) (Q9JMD7)
Organism: Rattus norvegicus (Rat)
Function: Transmembrane transporter that imports choline from the extracellular space to the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion- and chloride ion-dependent.
Subcellular location: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9GZV3}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BGY9}. Early endosome membrane {ECO:0000250|UniProtKB:Q9GZV3}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12969261}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to synaptic vesicles. {ECO:0000269|PubMed:12969261}.
Interaction partners:
- Choline transporter-like protein 1
- Choline transporter-like protein 2
- Choline transporter-like protein 3
- Choline transporter-like protein
- Choline transporter-like protein 4
- Solute carrier family 22 member 2
- Solute carrier family 22 member 1
- Solute carrier family 22 member 3
- Vesicular acetylcholine transporter
- Choline O-acetyltransferase
Sequence:
MPFHVEGLVAIILFYLLIFLVGIWAAWKTKNSGNAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYGPGCGLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVDVNISVIVSALIAILYTLVGGLYSVAYTDVVQLFCIFIGLWISVPFALSHPAVTDIGFTAVHAKYQSPWLGTIESVEVYTWLDNFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMALPAICIGAIGASTDWNQTAYGFPDPKTKEEADMILPIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTKTVYGLWYLSSDLVYIIIFPQLLCVLFIKGTNTYGAVAGYIFGLFLRITGGEPYLYLQPLIFYPGYYPDKNGIYNQRFPFKTLSMVTSFFTNICVSYLAKYLFESGTLPPKLDIFDAVVSRHSEENMDKTILVRNENIKLNELAPVKPRQSLTLSSTFTNKEALLDVDSSPEGSGTEDNLQ
Protein: Multidrug resistance protein 1 (PfMDR1) (EC 7.6.2.2) (P-glycoprotein homolog) (PGH1) (Q7K6A5)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:1674943, ECO:0000269|PubMed:8097560}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Multidrug resistance-associated protein 1
- Multidrug resistance-associated protein 2
- Chloroquine resistance transporter
Sequence:
MGKEQKEKKDGNLSIKEEVEKELNKKSTAELFRKIKNEKISFFLPFKCLPAQHRKLLFISFVCAVLSGGTLPFFISVFGVILKNMNLGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVICNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHIGLINGLILVSYAFGFWYGTRIIINSATNQYPNNDFNGASVISILLGVLISMFMLTIILPNITEYMKALEATNSLYEIINRKPLVENNDDGETLPNIKKIEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEAMENYYEENTNDTYENKNFSLISNSMTSNELLEMKKEYQTIKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRERSDNNNNNNNDDNNNNNNNNNNKINNEGSYIIEQGTHDSLMKNKNGIYHLMINNQKISSNKSSNNGNDNGSDNKSSAYKDSDTGNDADNMNSLSIHENENISNNRNCKNTAENEKEEKVPFFKRMFRRKKKAPNNLRIIYKEIFSYKKDVTIIFFSILVAGGLYPVFALLYARYVSTLFDFANLEYNSNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCPIVAAVLTFIYFINMRVFAVRARLTKSKEIEKKENMSSGVFAFSSDDEMFKDPSFLIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGKLMSLKGDSENAKLSFEKYYPLMIRKSNIDVRDDGGIRINKNLIKGKVDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMTNFQDYQNNNNNSLVLKNVNEFSNQSGSAEDYTVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRNGTFVQSHGTHDELLSAQDGIYKKYVKLAK
Protein: Medium/long-chain-fatty-acid--CoA ligase FadD17 (FACL) (EC 6.2.1.2) (EC 6.2.1.3) (Acyl-CoA synthetase) (FACL17) (Steroid-24-oyl-CoA synthetase) (O53551)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. Also involved in steroid side-chain degradation. Activates cholesterol metabolites with a C5 side chain, including cholate and chenodeoxycholate.
Interaction partners:
- Acyl-CoA dehydrogenase FadE26
- Acyl-CoA dehydrogenase FadE27
- Probable fatty-acid-CoA ligase FadD18
- Probable lipid carrier protein or keto acyl-CoA thiolase Ltp3
- Possible lipid transfer protein or keto acyl-CoA thiolase Ltp4
- Hydroxyacyl-CoA dehydrogenase ChsB1
- Enoyl-CoA hydratase EchA19
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- p-hydroxybenzoic acid--AMP ligase FadD22
- Probable 2-succinylbenzoate--CoA ligase
Sequence:
MTPTHPTVTELLLPLSEIDDRGVYFEDSFTSWRDHIRHGAAIAAALRERLDPARPPHVGVLLQNTPFFSATLVAGALSGIVPVGLNPVRRGAALAGDIAKADCQLVLTGSGSAEVPADVEHINVDSPEWTDEVAAHRDTEVRFRSADLADLFMLIFTSGTSGDPKAVKCSHRKVAIAGVTITQRFSLGRDDVCYVSMPLFHSNAVLVGWAVAAACQGSMALRRKFSASQFLADVRRYGATYANYVGKPLSYVLATPELPDDADNPLRAVYGNEGVPGDIDRFGRRFGCVVMDGFGSTEGGVAITRTLDTPAGALGPLPGGIQIVDPDTGEPCPTGVVGELVNTAGPGGFEGYYNDEAAEAERMAGGVYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLMRYPDATEVAVYPVPDPVVGDQVMAALVLAPGTKFDADKFRAFLTEQPDLGHKQWPSYVRVSAGLPRTMTFKVIKRQLSAEGVACADPVWPIRR
Protein: Putative RNA-binding protein (RNA-binding (RRM/RBD/RNP motifs) family protein) (Q949Z3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MESDLGKLFIGGISWDTDEERLRDYFSNYGDVVEAVIMRDRATGRARGFGFIVFADPCVSERVIMDKHIIDGRTVEAKKAVPRDDQQVLKRHASPIHLMSPVHGGGGRTKKIFVGGLPSSITEEEFKNYFDQFGTIADVVVMYDHNTQRPRGFGFITFDSDDAVDRVLHKTFHELNGKLVEVKRAVPKEISPVSNIRSPLASGVNYGGGSNRMPANSYFNNFAPGPGFYNSLGPVGRRFSPVIGSGRNAVSAFGLGLNHDLSLNLNPSCDGTSSTFGYNRIPSNPYFNGASPNRYTSPIGHNRTESPYNSNNRDLWGNRTDTAGPGWNLNVSNGNNRGNWGLPSSSAVSNDNNGFGRNYGTSSGLSSSPFNGFEGSIGELYRGGSVYSDSTWQQQQLPSQSSHELDNLSRAYGYDIDNVGSDPSANDPETYNGSYNVGNRQTNRGNKKIHLNKTCNLDTF
Protein: C2H2-type domain-containing protein (Q5ZMN5)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASGDTVYIATDGSEMPAEIVELHEIEVETIPVETIETTVVGGEEDEEEEDEDECCEDCGPHHPPHHYHHHQPMIALQPLVSDGDPSGAGGGAAGGGGGQLHLHHHHQEVILVQTREEVVGGDDSDGLRADDGFEDQILIPVPAPAGEDEYIEQTLVTVAAAGSKSGGGGSSSAGGGGRVKKGGSGKKSSKKSYLSGGGGGGAEGGGGRKWEQKQVQIKTLEGEFSVTMWASDDKKDIDHETVVEEQIIGENSPPDYSEYMTGKKLPPGGIPGIDLSDPKQLAEFARMKPRKIKEDDAPRTIACPHKGCTKMFRDNSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPYVCPFDGCNKKFAQSTNLKSHILTHAKAKNNQ
Protein: Germ cell-specific gene 1-like protein (GSG1-like protein) (D3ZK93)
Organism: Rattus norvegicus (Rat)
Function: As a component of the inner core of AMPAR complexes, modifies AMPA receptor (AMPAR) gating.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22632720}; Multi-pass membrane protein {ECO:0000269|PubMed:22632720}. Synapse {ECO:0000250}.
Interaction partners:
Sequence:
MKTSRRGRALLAVALNLLALLFATTAFLTTYWCQGTQRVPKPGCGQGGGANCPNSGANATANSTAAPVAASPAGAPYSWEAGDERFQLRRFHTGIWYSCEEELGGPGEKCRSFIDLAPASEKGVLWLSVVSEVLYILLLVVGFSLMCLELLHSSSVIDGLKLNAFAAVFTVLSGLLGMVAHMMYTQVFQVTVSLGPEDWRPHSWDYGWSFCLAWGSFTCCMAASVTTLNSYTKTVIEFRHKRKVFEQGYREEPTFIDPEAIKYFRERIEKGDVSEEEDFRLACRHERYPTRHQPHMGDSWPRSSAHEAAELNRQCWVLGHWV
Protein: KRAB domain-containing protein 5 (Q7Z2F6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGLLTFRDVAIEFSREEWEHLDSDQKLLYGDVMLENYGNLVSLGLAVSKPDLITFLEQRKEPWNVKSAETVAIQPDIFSHDTQGLLRKKLIEASFQKVILDGYGSCGPQNLNLRKEWESEGKIILW
Protein: EEF1A lysine methyltransferase 3 (EC 2.1.1.-) (Hepatocellular carcinoma-associated antigen 557a) (Methyltransferase-like protein 21B) (Protein-lysine methyltransferase METTL21B) (eEF1A-KMT3) (Q96AZ1)
Organism: Homo sapiens (Human)
Function: Protein-lysine methyltransferase that selectively mono-, di- and trimethylates 'Lys-165' of the translation elongation factors EEF1A1 and EEF1A2 in an aminoacyl-tRNA and GTP-dependent manner. EEF1A1 methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:28108655}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:28108655}.
Interaction partners:
- Elongation factor Ts, mitochondrial
Sequence:
MADPGPDPESESESVFPREVGLFADSYSEKSQFCFCGHVLTITQNFGSRLGVAARVWDAALSLCNYFESQNVDFRGKKVIELGAGTGIVGILAALQGGDVTITDLPLALEQIQGNVQANVPAGGQAQVRALSWGIDHHVFPANYDLVLGADIVYLEPTFPLLLGTLQHLCRPHGTIYLASKMRKEHGTESFFQHLLPQHFQLELAQRDEDENVNIYRARHREPRPA
Protein: Cytochrome P450 2C9 (EC 1.14.14.1) ((R)-limonene 6-monooxygenase) (EC 1.14.14.53) ((S)-limonene 6-monooxygenase) (EC 1.14.14.51) ((S)-limonene 7-monooxygenase) (EC 1.14.14.52) (CYPIIC9) (Cholesterol 25-hydroxylase) (Cytochrome P-450MP) (Cytochrome P450 MP-4) (Cytochrome P450 MP-8) (Cytochrome P450 PB-1) (S-mephenytoin 4-hydroxylase) (P11712)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. Exhibits low catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2. Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol. Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:21576599}; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 2C19
- Vitamin K epoxide reductase complex subunit 1
- Cytochrome P450 3A4)
- Cytochrome P450 4F2
- Cytochrome P450 3A7
- Bifunctional epoxide hydrolase 2
- Aldehyde oxidase
- Cytochrome P450 1A1
- UDP-glucuronosyltransferase 1A6
- Epoxide hydrolase 1
Sequence:
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYIDLLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVPPFYQLCFIPV