wanglab/gogpt-training-data huggingface dataset:
Protein: Excinuclease ABC subunit A (Q2YNH3)
Organism: Brucella abortus (strain 2308)
Interaction partners:
Sequence:
MKSTKIILSAIFAFGFTAAAQADAVPKRTKDFTANYQTLVKDQQASPQVADCIASGYDYVKKSKKYDRLGFTKADIAAAATSDKSAKFSAKDAKKVSAIISVPGEARIKSVGYKWDSITLRCGITRGKLQAIEIVRK
Protein: Sigma non-opioid intracellular receptor 1 (Sigma 1-type opioid receptor) (Sigma1-receptor) (Sigma1R) (Q9R0C9)
Organism: Rattus norvegicus (Rat)
Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity).
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15466698}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:15466698}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:15466698). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:15466698}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Lanosterol 14-alpha demethylase
- Squalene monooxygenase
- Ergosterol biosynthesis 28 homolog
- Sigma intracellular receptor 2
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Lathosterol oxidase
- Methylsterol monooxygenase 1
- Fatty acid hydroxylase domain containing 2
- 7-dehydrocholesterol reductase
Sequence:
MPWAVGRRWAWITLFLTIVAVLIQAVWLWLGTQSFVFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWREGTTKSEVYYPGETVVHGPGEATAVEWGPNTWMVEYGRGVIPSTLAFALSDTIFSTQDFLTLFYTLRAYARGLRLELTTYLFGQDP
Protein: Sal-like protein 4 (Zinc finger protein 797) (Zinc finger protein SALL4) (Q9UJQ4)
Organism: Homo sapiens (Human)
Function: Transcription factor with a key role in the maintenance and self-renewal of embryonic and hematopoietic stem cells.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Homeobox protein NANOG
- POU domain, class 5, transcription factor 1
- Transcription factor SOX-2
- Histone-binding protein RBBP4
- Sal-like protein 1
- Steroid hormone receptor ERR2
- PR domain zinc finger protein 14
- Protein lin-28 homolog A
- Nuclear receptor subfamily 0 group B member 1
- Protein cereblon
Sequence:
MSRRKQAKPQHINSEEDQGEQQPQQQTPEFADAAPAAPAAGELGAPVNHPGNDEVASEDEATVKRLRREETHVCEKCCAEFFSISEFLEHKKNCTKNPPVLIMNDSEGPVPSEDFSGAVLSHQPTSPGSKDCHRENGGSSEDMKEKPDAESVVYLKTETALPPTPQDISYLAKGKVANTNVTLQALRGTKVAVNQRSADALPAPVPGANSIPWVLEQILCLQQQQLQQIQLTEQIRIQVNMWASHALHSSGAGADTLKTLGSHMSQQVSAAVALLSQKAGSQGLSLDALKQAKLPHANIPSATSSLSPGLAPFTLKPDGTRVLPNVMSRLPSALLPQAPGSVLFQSPFSTVALDTSKKGKGKPPNISAVDVKPKDEAALYKHKCKYCSKVFGTDSSLQIHLRSHTGERPFVCSVCGHRFTTKGNLKVHFHRHPQVKANPQLFAEFQDKVAAGNGIPYALSVPDPIDEPSLSLDSKPVLVTTSVGLPQNLSSGTNPKDLTGGSLPGDLQPGPSPESEGGPTLPGVGPNYNSPRAGGFQGSGTPEPGSETLKLQQLVENIDKATTDPNECLICHRVLSCQSSLKMHYRTHTGERPFQCKICGRAFSTKGNLKTHLGVHRTNTSIKTQHSCPICQKKFTNAVMLQQHIRMHMGGQIPNTPLPENPCDFTGSEPMTVGENGSTGAICHDDVIESIDVEEVSSQEAPSSSSKVPTPLPSIHSASPTLGFAMMASLDAPGKVGPAPFNLQRQGSRENGSVESDGLTNDSSSLMGDQEYQSRSPDILETTSFQALSPANSQAESIKSKSPDAGSKAESSENSRTEMEGRSSLPSTFIRAPPTYVKVEVPGTFVGPSTLSPGMTPLLAAQPRRQAKQHGCTRCGKNFSSASALQIHERTHTGEKPFVCNICGRAFTTKGNLKVHYMTHGANNNSARRGRKLAIENTMALLGTDGKRVSEIFPKEILAPSVNVDPVVWNQYTSMLNGGLAVKTNEISVIQSGGVPTLPVSLGATSVVNNATVSKMDGSQSGISADVEKPSATDGVPKHQFPHFLEENKIAVS
Protein: Oxidoreductase stcQ (EC 1.-.-.-) (Sterigmatocystin biosynthesis cluster protein Q) (Q00713)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
- Glutathione S-transferase stcT
- Norsolorinic acid ketoreductase stcE
- FAD-binding monooxygenase stcW
- Norsolorinic acid synthase stcA
- Versicolorin B desaturase stcL
Sequence:
MPSYAVLGATGNTGRAIVQVLLDRADTDTRIHICAYCRSKEKLFRVCPAAETSKSLSVFQGRLDDDSLIDECLRGTDAVFLVVAIVDNMPGCTVAMQTAEAVVASLQRLRATDPAIRLPRLVILSSASLEPTFCNDVPAPVHWVLKTAVSHLYRDLAAAEAYLRAQSDWLSATFVKPGGLVHDQARGHKVCLDRAQTPLSFLDLAAGMVEVADADDGRYHMRSVSVVPASRVAIFPWDGVYYTFTGLLFHFCPWTYRFLGEYKLQSRKERDKQA
Protein: PH domain and leucine rich repeat protein phosphatase 2 (H3BMS5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGEVEPGPAGPLEPPEPPEAPASRRPGGIRVLKRNMKRNGSRNCLNRRSRFGSRERDWLREDVKRGCVYLYGADTTTATTTTTTSSSSSSSSSSSDLHLVLCTVETPASEICAGEGRESLYLQLHGDLVRRLEPTERPLQIVYDYLSRLGFDDPVRIQEEATNPDLGCMIRFYGEKPCHMDRLDRILLSGIYNVRKGKTQLHKWAERLVVLCGTCLIVSSVKDCQTGKMHILPLVGGKIEEVKRRQYSLAFSSAGAQAQTYHVSFETLAEYQRWQRQASKVVSQRISTVDLSCYSLEEVPEHLFYSQDITYLNLRHNFMQLERPGGLDTLYKFSQLKGLNLSHNKLGLFPILLCEISTLTELNLSCNGFHDLPSQIGNLLNLQTLCLDGNFLTTLPEELGNLQQLSSLGISFNNFSQIPEVYEKLTMLDRVVMAGNCLEVLNLGVLNRMNHIKHVDLRMNHLKTMVIENLEGNKHITHVDLRDNRLTDLDLSSLCSLEQLHCGRNQLRELTLSGFSLRTLYASSNRLTAVNVYPVPSLLTFLDLSRNLLECVPDWACEAKKIEVLDVSYNLLTEVPVRILSSLSLRKLMLGHNHVQNLPTLVEHIPLEVLDLQHNALTRLPDTLFSKALNLRYLNASANSLESLPSACTGEESLSMLQLLYLTNNLLTDQCIPVLVGHLHLRILHLANNQLQTFPASKLNKLEQLEELNLSGNKLKTIPTTIANCKRLHTLVAHSNNISIFPEILQLPQIQFVDLSCNDLTEILIPEALPATLQDLDLTGNTNLVLEHKTLDIFSHITTLKIDQKPLPTTDSTVTSTFWSHGLAEMAGQRNKLCVSALAMDSFAEGVGAVYGMFDGDRNEELPRLLQCTMADVLLEEVQQSTNDTVFMANTFLVSHRKLGMAGQKLGSSALLCYIRPDTADPASSFSLTVANVGTCQAVLCRGGKPVPLSKVFSLEQDPEEAQRVKDQKAIITEDNKVNGVTCCTRMLGCTYLYPWILPKPHISSTPLTIQDELLILGNKALWEHLSYTEAVNAVRHVQDPLAAAKKLCTLAQSYGCQDNVGAMVVYLNIGEEGCTCEMNGLTLPGPVGFASTTTIKDAPKPATPSSSSGIASEFSSEMSTSEVSSEVGSTASDEHNAGGLDTALLPRPERRCSLHPTPTSGLFQRQPSSATFSSNQSDNGLDSDDDQPVEGVITNGSKVEVEVDIHCCRGRDLENSPPLIESSPTLCSEEHARGSCFGIRRQNSVNSGMLLPMSKDRMELQKSPSTSCLYGKKLSNGSIVPLEDSLNLIEVATEVPKRKTGYFAAPTQMEPEDQFVVPHDLEEEVKEQMKQHQDSRLEPEPHEEDRTEPPEEFDTAL
Protein: Fibroblast growth factor 1 (Acidic fibroblast growth factor) (Heparin-binding growth factor 1) (B5MCF4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU364136}. Cytoplasm {ECO:0000256|RuleBase:RU364136}. Cytoplasm, cell cortex {ECO:0000256|RuleBase:RU364136}. Cytoplasm, cytosol {ECO:0000256|RuleBase:RU364136}. Nucleus {ECO:0000256|RuleBase:RU364136}.
Interaction partners:
Sequence:
MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHTAAQCGKRGGGVYKEYRDWPVLGHGHRRAFIRLTDTK
Protein: Serine/threonine-protein kinase receptor (EC 2.7.11.30) (Q9YGU4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.
Interaction partners:
Sequence:
MFASLLTLALLLATFAADPSHGEVETRECLYYNVNWEVEKTNRSGVERCEGEKDKRSHCYASWRNNSGSIQLVKKGCWLDDFNCYDRQECVATEENPQVFFCCCEGNFCNERFTHLPDISGPVISPPPVSPSLLNVLVYSLLPLSMLSMAVLLAFWMYRHRKPPYGHVDVNEDPGPSPPSPLVGLKPLQLLEVKARGRFGCVWKAQMINEYVAVKIFPIQDKLSWQNEREMFSTPGMKHDNLLRFIAAEKRGSNLEMEFWLITEFHERGSLTDYLKGNAVSWADLCVIAESMACGLAYLHEDVPRSKGEGPKPAIAHRDFKSKNVMLKMDLTAVIGDFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDSFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEDLQDAVVHKKLRPAFKDCWLKHSGLCQMCETMEECWDHDAEARLSAGCVQERISQIRRVSSSTSDCLFSMVTSLTNVDLPPKESSI
Protein: Splicing factor 1 (A0A8I5ZQ56)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367126}.
Interaction partners:
Sequence:
MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHTLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPASNPPPPSRPPWMNSGPSENRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMVPGKYACGLWGLSPASRKRYDAAAAYGHDAAASATSQWAAPASSLWSSSSMAAAAAAASTTPSAQQQYGFQHPLAMAAKIPPRSSDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA
Protein: Slfn4 protein (Q80UG3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPGKVICSPEALCMKPFSQHEGYEQLVRTELGSLRKGTLVVSKSWALDLGLQEKQEVIWDVLHISQGSLLTLHVFVQGDENLEGNSSLLGKLGAELKGYYKQIALTLKQTLVNLCGYTAKIGIIVKITYLGHKTMCLYDSSAKICYPQIYYLTTKAVKDLEKALAEILGSYESFYSLPRRNWDSFMSAFLNVGSYIVYFSRNVLTHIRI
Protein: Protein C4 (P17370)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Plays a role in the inhibition of host NF-kappa-B activation. Mechanistically, blocks the subunit p65/RELA translocation into the host nucleus.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:22791606}. Host nucleus {ECO:0000269|PubMed:22791606}.
Interaction partners:
Sequence:
MDTIKIFNHGEFDTIRNELVNLLKVVKWNTINSNVTVSSTDTIDISDCIREILYKQFKNVRNIEVSSDISFIKYNRFNDTTLTDDNVGYYLVIYLNRTKSVKTLIYPTPETVITSSEDIMFSKSLNFRFENVKRDYKLVMCSISLTYKPSICRIQYDNNKYLDISDSQECNNLCYCVITMDPHHLIDLETICVLVDKSGKCLLVNEFYIRFRKNHIYNSFADLCMDHIFELPNTKELFTLRNDDGRNIAWDNDKLESGNNTWIPKTDDEYKFLSKLMNIAKFNNTKFDYYVLVGDTDPCTVFTFKVTKYYINLNYE
Protein: Solute carrier family 22 member 12 (Organic anion transporter 4-like protein) (Renal-specific transporter) (RST) (Urate anion exchanger 1) (URAT1) (Urate:anion antiporter SLC22A12) (Q96S37)
Organism: Homo sapiens (Human)
Function: Electroneutral antiporter that translocates urate across the apical membrane of proximal tubular cells in exchange for monovalent organic or inorganic anions. Involved in renal reabsorption of urate and helps maintaining blood levels of uric acid. Mediates urate uptake by an exchange with organic anions such as (S)-lactate and nicotinate, and inorganic anion Cl(-). Other inorganic anions such as Br(-), I(-) and NO3(-) may also act as counteranions that exchange for urate. Also mediates orotate tubular uptake coupled with nicotinate efflux and to a lesser extent with lactate efflux, therefore displaying a potential role in orotate renal reabsorption. Orotate transport is Cl(-)-dependent.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12024214, ECO:0000269|PubMed:22194875, ECO:0000269|PubMed:35144162, ECO:0000269|PubMed:35462902}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 2, facilitated glucose transporter member 9
- Sodium-coupled monocarboxylate transporter 1
- Sodium-coupled monocarboxylate transporter 2
- Sodium-dependent phosphate transport protein 1
- Na
- Broad substrate specificity ATP-binding cassette transporter ABCG2
- Sodium-dependent phosphate transport protein 4
- ATP-binding cassette sub-family C member 4
- CCAAT/enhancer-binding protein delta
- Monocarboxylate transporter 9
Sequence:
MAFSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAQASILGSLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGWVYDRSIFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAACGPASDRFGRRLVLTWSYLQMAVMGTAAAFAPAFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTAARARPLVMTLNSLGFSFGHGLTAAVAYGVRDWTLLQLVVSVPFFLCFLYSWWLAESARWLLTTGRLDWGLQELWRVAAINGKGAVQDTLTPEVLLSAMREELSMGQPPASLGTLLRMPGLRFRTCISTLCWFAFGFTFFGLALDLQALGSNIFLLQMFIGVVDIPAKMGALLLLSHLGRRPTLAASLLLAGLCILANTLVPHEMGALRSALAVLGLGGVGAAFTCITIYSSELFPTVLRMTAVGLGQMAARGGAILGPLVRLLGVHGPWLPLLVYGTVPVLSGLAALLLPETQSLPLPDTIQDVQNQAVKKATHGTLGNSVLKSTQF
Protein: Tropomodulin-1 (Erythrocyte tropomodulin) (E-Tmod) (P28289)
Organism: Homo sapiens (Human)
Function: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25250574}. Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments (PubMed:25250574, PubMed:38168645). {ECO:0000269|PubMed:25250574, ECO:0000269|PubMed:38168645}.
Interaction partners:
- Alpha-adducin
- Nebulin
- Beta-adducin
- Gamma-adducin
- Dematin
- Actin, alpha skeletal muscle
- Protein 4.1
- Capping protein, Arp2/3 and myosin-I linker protein 2
- F-actin-capping protein subunit alpha-2
- Tropomyosin beta chain
Sequence:
MSYRRELEKYRDLDEDEILGALTEEELRTLENELDELDPDNALLPAGLRQKDQTTKAPTGPFKREELLDHLEKQAKEFKDREDLVPYTGEKRGKVWVPKQKPLDPVLESVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYQALSSSSIMNKEGLNSVIKPTQYKPVPDEEPNSTDVEETLERIKNNDPKLEEVNLNNIRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAYALAEMLKENKVLKTLNVESNFISGAGILRLVEALPYNTSLVEMKIDNQSQPLGNKVEMEIVSMLEKNATLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLADLTGPIIPKCRSGV
Protein: Rab family GTPase (Q59X89)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Phosphatidylinositol 3-kinase VPS34
- Pep7p
- Rab family GTPase
- Rab GDP dissociation inhibitor
- CORVET complex membrane-binding subunit
- CNH domain-containing protein
- E3 ubiquitin-protein ligase PEP5
- Probable vacuolar protein sorting-associated protein 16 homolog
- CORVET complex subunit
- Tethering complex ATP-binding subunit
Sequence:
MSQHPAPATAVKLVLLGEAAVGKSSLVLRFVSNDFQENKEPTIGAAFLTQKCTIGERTIKYEIWDTAGQERFASLAPMYYRNAQAAIVVYDITKPASFIKARHWVKELHEQANRDITIALVGNKLDLVEDDSAEDGETLRKVSVEEGQSLADEEGLLFFETSAKTGNNVNEVFVGIGSKIPSVTVTGGEAQEGSNGRRIDLTANTDNANAPRSTCC
Protein: Sodium-dependent multivitamin transporter (Na(+)-dependent multivitamin transporter) (hSMVT) (Solute carrier family 5 member 6) (Q9Y289)
Organism: Homo sapiens (Human)
Function: Sodium-dependent multivitamin transporter that transports pantothenate, biotin and lipoate. Required for biotin and pantothenate uptake in the instestine (By similarity). Plays a role in the maintenance of intestinal mucosa integrity, by providing the gut mucosa with biotin (By similarity). May play a role in the transport of biotin and pantothenate into the brain across the blood-brain barrier. May also be involved in the sodium-dependent transport of iodide ions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25809983, ECO:0000269|PubMed:27904971, ECO:0000269|PubMed:35013551}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:19211916}; Multi-pass membrane protein {ECO:0000255}. Note=Preferentially localized at the luminal membrane of brain capillary endothelium (PubMed:25809983). Localized to the brush border/apical membrane of intestine and renal polarized cells (PubMed:19211916). {ECO:0000269|PubMed:19211916, ECO:0000269|PubMed:25809983}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28052864}; Multi-pass membrane protein {ECO:0000255}. Note=(Microbial infection) Exposure to E.coli lipopolysaccharides leads to reduced cell membrane localization. {ECO:0000269|PubMed:28052864}.
Interaction partners:
- PDZ domain-containing protein 11
Sequence:
MSVGVSTSAPLSPTSGTSVGMSTFSIMDYVVFVLLLVLSLAIGLYHACRGWGRHTVGELLMADRKMGCLPVALSLLATFQSAVAILGVPSEIYRFGTQYWFLGCCYFLGLLIPAHIFIPVFYRLHLTSAYEYLELRFNKTVRVCGTVTFIFQMVIYMGVVLYAPSLALNAVTGFDLWLSVLALGIVCTVYTALGGLKAVIWTDVFQTLVMFLGQLAVIIVGSAKVGGLGRVWAVASQHGRISGFELDPDPFVRHTFWTLAFGGVFMMLSLYGVNQAQVQRYLSSRTEKAAVLSCYAVFPFQQVSLCVGCLIGLVMFAYYQEYPMSIQQAQAAPDQFVLYFVMDLLKGLPGLPGLFIACLFSGSLSTISSAFNSLATVTMEDLIRPWFPEFSEARAIMLSRGLAFGYGLLCLGMAYISSQMGPVLQAAISIFGMVGGPLLGLFCLGMFFPCANPPGAVVGLLAGLVMAFWIGIGSIVTSMGSSMPPSPSNGSSFSLPTNLTVATVTTLMPLTTFSKPTGLQRFYSLSYLWYSAHNSTTVIVVGLIVSLLTGRMRGRSLNPATIYPVLPKLLSLLPLSCQKRLHCRSYGQDHLDTGLFPEKPRNGVLGDSRDKEAMALDGTAYQGSSSTCILQETSL
Protein: (thale cress) hypothetical protein (A0A384KYS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDGRGGCCIARYAIGSGPYDLSKADRIMLRFRPIAPKPASPGGVNPVSSGDSGGGSSDVSFRSASRRKRKCHQLKENGGNAKRCTRRKTSDKPVVHGSANAVTLSLLPEKPIDLKAAVEKQKRQGPLWLSFKDGGGMLTPAYQTPEIVQRTVVISSCMTVERVTDAWIDGYGLGRSDEERKMNLVRDTCPGFISDGSGRVTWTNDAYRKMARDIIPVEEGAPEITSGDSFHVIVRLVMRERPMLTSPGFTCRMKLQYTCQNRERGSVTVPCDVWRMDVGGGFAWRLDVKAALCL
Protein: Uncharacterized protein (P95147)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS14A
- Small ribosomal subunit protein uS14B
- Large ribosomal subunit protein uL4
Sequence:
MQILVTDATGAVGRSVTRQLIAAGHTVSGIAQHPHDALDPRVDYVCASLRNPVLQELAGEADAVIHLAPVDTSAPGGVGITGLAHVANAAARAGARLLFVSQAAGRPELYRQAETLVSTGWAPSLVIRIAPPVGRQLDWMVCRTVATLLRSKVSARPIRVLHLDDLVRFLVLALNTDRNGVVDLATPDTTNVVTAWRLLRSVDPHLRTRRVRSWEQLIPEVDIAAVQEDWNFEFGWQATEAIVDTGRGLVGRRLHPAGATNGSGQLALPVEAPPRSVPSHGEPLGSAAPEGLEGEFDDRIDERFPVFSSASLAEALPGPLTPMTLDVQLSGLRAAGRAMGRVLALGGVVADEWERRAIAVFGHRPYIGVSANIVAAAQLPGWDAQAVARRALGEQPQVTELLPFGRPQLAGGPLGSVAKVVVTARSLALLRHLRSDTHHYVAAADAEHLAAGQLASLPDAGLEVRIRLLRDRIHQGWILTVLWVIDTGVTAATLEHTRAGSAVSGGGMIMESGRIGAEIAPLAAVLRADPPLCALANDGNLASIRALSAPAAAAVDAVIARIGHRGLGEAELANLTFADDPALLLKTAAEIAARPAGPAHPATLIQRLAAGTRSARELAHDTTIRFTHELRMTLRELGSRRVAADVIDVVDDVFYLTCDELITTPADARLRIKRRRAERERLQAQRPPDVIDHAWVPVE
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (Q01604)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm.
Interaction partners:
- Triosephosphate isomerase
- Enolase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Phosphoglycerate mutase
- Phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Pyruvate kinase
- Phosphoglycerate mutase
Sequence:
MAFNKLSIENLDLAGKRVLMRVDFNVPIKEGKITSNQRIVAALDSIKLALSKKAKSVVLMSHLGRPDGNKNIKYTLAPVAAELKTLLGQDVIFLSDCVGSEVEAACKDPAPGSVILLENVRFYVEEEGKGLDASGGKVKADPAKVKEFRASLAKLGDVYVNDAFGTAHRAHSSMMGDGFEQRAAGLLLNKELKYFSQALDKPPNPFLAILGGAKVADKIQLIENLLDKVNEMIIGGGMAFTFLKVLNNMKIGGSLFDEEGSKIVEKLVEKAKKNNVQLHLPVDFVCGDKFAENAAVSEATVEAGIPDGHMGLDVGPKTRELFAAPIARAKLIVWNGPPGVFEFPNFANGTKSIMDGVVAATKNGTVSIIGGGDTASCCAKWNTEALVSHVSTGGGASLELLEGKTLPGVAALTSA
Protein: IP15312p (Uncharacterized protein, isoform J) (Q1RKY9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDSTLNIENVNDPTSIASDLSAENTKADLVSLNEPNVNDQTSSASDLTAENTKADHDSLNKPKDFNNQILNIISDIDINIKAQEKITQLKEQELKLIQKQNDLANEIHKQQILAKQLSAQNQLKQNECQSGELDLHSQYQNERGGPTSTLYQEKNIASKESANVSKTVDLRKIFTPATDAAEILPKNRKLYASSAFYSPTLHPTVEDQVELARRISHSLSDISNQTSKGQSMYVNRKKRSDKWVHEGGSQGNDAINPFKENSETKSTMEVAKLEKIPLKLIMNPNGKVRDYNSLKDLINVEAGLLSPDNCAELITALQLHQGRGAELFAKRRRKADNWVVDESHSGTQYHPSGIPDFQQYQQRPVLSPNILPAYSDAGKHRVQLNIHQNQLIEKYSKPGLQVVQSPWKAALQTGSASSAFLEDTKSFSPPALTPIPSSQAGSKDWTDANEPMPHGSSRRNTNAVASSPRSVIVPSNPQRDLAYTPCVAQGWGGRSVELPKGLYVPKEISLSSYAAPSQQCEIHSKHFERPYEDTFPRTFPRNNYSANNNFPGNDGIGEFPLSKPTGLTTGTLHQQPYSPTSYKKTVPGLEKVENFARYEQPDRKRLTSGSPQYLNALQNSQVRNASPIPFGTSLNEQTSWPPRSVLLQGGSPSPLPNHVQTFNKCAKGWGSIPVKQQSYSSQYNLPGNLPYSDF
Protein: Phospholipase ABHD3 (EC 3.1.1.32) (EC 3.1.1.4) (Abhydrolase domain-containing protein 3) (Q8WU67)
Organism: Homo sapiens (Human)
Function: Phospholipase that may play a role in phospholipids remodeling. May selectively cleave myristate (C14)-containing phosphatidylcholines through its predominant phospholipase 1 activity, cleaving preferentially acyl groups in sn1 position. In parallel, may have a minor phospholipase 2 activity acting on acyl groups in position sn2. In addition to (C14)-containing phosphatidylcholines, may also act on other medium-chain-containing and oxidatively truncated phospholipids.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MQRLAMDLRMLSRELSLYLEHQVRVGFFGSGVGLSLILGFSVAYAFYYLSSIAKKPQLVTGGESFSRFLQDHCPVVTETYYPTVWCWEGRGQTLLRPFITSKPPVQYRNELIKTADGGQISLDWFDNDNSTCYMDASTRPTILLLPGLTGTSKESYILHMIHLSEELGYRCVVFNNRGVAGENLLTPRTYCCANTEDLETVIHHVHSLYPSAPFLAAGVSMGGMLLLNYLGKIGSKTPLMAAATFSVGWNTFACSESLEKPLNWLLFNYYLTTCLQSSVNKHRHMFVKQVDMDHVMKAKSIREFDKRFTSVMFGYQTIDDYYTDASPSPRLKSVGIPVLCLNSVDDVFSPSHAIPIETAKQNPNVALVLTSYGGHIGFLEGIWPRQSTYMDRVFKQFVQAMVEHGHELS