wanglab/gogpt-training-data huggingface dataset:
Protein: FOXP3 protein (Forkhead box P3) (B7ZLG1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MPNPRPGKPSAPSLALGPSPGASPSWRAAPKASDLLGARGPGGTFQGRDLRGGAHASSSSLNPMPPSQLQLPTLPLVMVAPSGARLGPLPHLQALLQDRPHFMHQLSTVDAHARTPVLQVHPLESPAMISLTPPTTATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPNPSAPRKDRSVDRAGKDPRPPIPSPDTLCPPSTLSAVPQSSYPLLANGVCKWPGCEKVFEEPEDFLKHCQADHLLDEKGRAQCLLQREMVQSLEQQLVLEKEKLSAMQAHLAGKMALTKASSVASSDKGSCCIVAAGSQGPVVPAWSGPREAPDSLFAVRRHLWGSHGNSTFPEFLHNMDYFKFHNMRPPFTYATLIRWAILEAPEKQRTLNEIYHWFTRMFAFFRNHPATWKNAIRHNLSLHKCFVRVESEKGAVWTVDELEFRKKRSQRPSRCSNPTPGP
Protein: Sodium-coupled neutral amino acid transporter 7 (Solute carrier family 38 member 7) (Q8BWH0)
Organism: Mus musculus (Mouse)
Function: Symporter that selectively cotransports sodium ions and amino acids, such as L-glutamine and L-asparagine from the lysosome into the cytoplasm and may participates in mTORC1 activation. The transport activity requires an acidic lysosomal lumen (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q9NVC3}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:21511949}. Note=In neurons, located in soma. {ECO:0000269|PubMed:21511949}.
Interaction partners:
Sequence:
MAQVSINSDYSEWASSTDAGERARLLQSPCVDVVPKSEGEASPGDPDSGTTSTLGAVFIVVNACLGAGLLNFPAAFSTAGGVAAGIALQMGMLVFIISGLVILAYCSQASNERTYQEVVWAVCGKLTGVLCEVAIAVYTFGTCIAFLIIIGDQQDKIIAVMSKEPDGASGSPWYTDRKFTISLTAFLFILPLSIPKEIGFQKYASFLSVVGTWYVTAIIIIKYIWPDKEMRPGDILTRPASWMAVFNAMPTICFGFQCHVSSVPVFNSMRQPEVKTWGGVVTAAMVIALAVYMGTGICGFLTFGAAVDPDVLRSYPSEDVAVAVARAFIILSVLTSYPILHFCGRAVVEGLWLRYKGMPVEEDVGRERRRRVLQTLVWFLLTLLLALFIPDIGKVISVIGGLAACFIFIFPGLCLIQAKLSEMEEVKPASWWALVSYGVLLVTLGAFIFGQTTANAIFVDLLA
Protein: Sodium/potassium-transporting ATPase subunit alpha-2 (Na(+)/K(+) ATPase alpha-2 subunit) (EC 7.2.2.13) (Na(+)/K(+) ATPase alpha(+) subunit) (Sodium pump subunit alpha-2) (Q6PIE5)
Organism: Mus musculus (Mouse)
Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity).
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-3
- Sodium/potassium-transporting ATPase subunit gamma
- Protein ATP1B4
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit alpha-3
- Phospholemman
- Mitogen-activated protein kinase 3
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGALLCFLAYGILAAMEDEPSNDNLYLGIVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGQTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILRDHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTTNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
Protein: Smooth, isoform G (Smooth, isoform W) (Smooth, isoform Y) (Q0E914)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPPGLTEDQLIGIFNIKDVPATSVRLFPLKTERSSSGLIEFSNISQAVLAIMKCNHLPIEGKGTKFPFIMKLCFSSSKSMNGAWNNAASEGMIEKENEVDTKVDIYN
Protein: Integrator complex subunit 3 (Int3) (SOSS complex subunit A) (Sensor of single-strand DNA complex subunit A) (SOSS-A) (Sensor of ssDNA subunit A) (Q68E01)
Organism: Homo sapiens (Human)
Function: Component of the Integrator (INT) complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501, ECO:0000269|PubMed:23904267, ECO:0000269|PubMed:29471365, ECO:0000269|PubMed:39032490}. Cytoplasm {ECO:0000269|PubMed:23904267}. Note=Localizes to nuclear foci following DNA damage. {ECO:0000269|PubMed:19683501}.
Interaction partners:
- Integrator complex subunit 13
- Integrator complex subunit 7
- Integrator complex subunit 11
- SOSS complex subunit B1
- Integrator complex subunit 6
- Integrator complex subunit 9
- SOSS complex subunit B2
- Integrator complex subunit 12
- Integrator complex subunit 5
- Integrator complex subunit 1
Sequence:
MELQKGKGAAAAAAASGAAGGGGGGAGAGAPGGGRLLLSTSLDAKDELEERLERCMSIVTSMTAGVSEREANDALNAYVCKGLPQHEEICLGLFTLILTEPAQAQKCYRDLALVSRDGMNIVLNKINQILMEKYLKLQDTCRTQLVWLVRELVKSGVLGADGVCMTFMKQIAGGGDVTAKNIWLAESVLDILTEQREWVLKSSILIAMAVYTYLRLIVDHHGTAQLQALRQKEVDFCISLLRERFMECLMIGRDLVRLLQNVARIPEFELLWKDIIHNPQALSPQFTGILQLLQSRTSRKFLACRLTPDMETKLLFMTSRVRFGQQKRYQDWFQRQYLSTPDSQSLRCDLIRYICGVVHPSNEVLSSDILPRWAIIGWLLTTCTSNVAASNAKLALFYDWLFFSPDKDSIMNIEPAILVMHHSMKPHPAITATLLDFMCRIIPNFYPPLEGHVRQGVFSSLNHIVEKRVLAHLAPLFDNPKLDKELRAMLREKFPEFCSSPSPPVEVKIEEPVSMEMDNHMSDKDESCYDNAEAAFSDDEEDLNSKGKKREFRFHPIKETVVEEPVDITPYLDQLDESLRDKVLQLQKGSDTEAQCEVMQEIVDQVLEEDFDSEQLSVLASCLQELFKAHFRGEVLPEEITEESLEESVGKPLYLIFRNLCQMQEDNSSFSLLLDLLSELYQKQPKIGYHLLYYLRASKAAAGKMNLYESFAQATQLGDLHTCLMMDMKACQEDDVRLLCHLTPSIYTEFPDETLRSGELLNMIVAVIDSAQLQELVCHVMMGNLVMFRKDSVLNILIQSLDWETFEQYCAWQLFLAHNIPLETIIPILQHLKYKEHPEALSCLLLQLRREKPSEEMVKMVLSRPCHPDDQFTTSILRHWCMKHDELLAEHIKSLLIKNNSLPRKRQSLRSSSSKLAQLTLEQILEHLDNLRLNLTNTKQNFFSQTPILQALQHVQASCDEAHKMKFSDLFSLAEEYEDSSTKPPKSRRKAALSSPRSRKNATQPPNAEEESGSSSASEEEDTKPKPTKRKRKGSSAVGSDSD
Protein: Myosin XI-F (B0CN60)
Organism: Nicotiana benthamiana
Interaction partners:
Sequence:
MGTPVNIIVGSQVWIEDPDDAWIDGEVTEIKGSNATVVTTNGRKTVAPISSIYPKDTEAPPAGVDDMTKLAYLHEPGVLNNLACRYALNEIYTYTGNILIAVNPFRRLPHLYDIHMMQQYKGAPFGELSPHLFAVADACYRALINEHGSQSILVSGESGAGKTETTKMLMRYLAFMGGRSGTEGRTVEQQVLESNPVLEAFGNAKTVKNNNSSRFGKFVEIQFDXHGKISGAAVRTYLLERSRVCQVSDPERNYHCFYMLCAAPPEDVKRYKLGDPRSFHYLNQTNCYEVANVDDAREYLETRNAMDVVGIGPEEQEAIFRVVAAILHLGNINFVKGKEFDSSKLKDDKSLFHLKTAAELFMCDEKALEDSLCKRVIVTPDGNITKLLDPAAATTSRDALAKTVYSRLFDWLVDKINSSIGQDPDAKSIIGVLDIYGFESFKINSFEQFCINLTNEKLQQHFNQHVFKMEQDDYTTEEINWSYVEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFAQKMYQTYKAHKRFSKPKLARTAFTINHYAGDVTYQADHFLDKNKDYVIAEFQALLMDSKCSFVANLFPPLPEESSKQSKFSSIGTRFKQQLQSLMESLSTTEPHYIRCVKPNTVLKPGIFENMNVLNQLRCGGVLEAIRISCAGYPTKRTFDEFLDRFGMLAPDVLDGCDEKSACIAICDRMGLKGYQIGKTKVFLRAGQMAELDARRTEVLAHAAKRIQRQIRTHLTRKEFIALRRATIHFQKLWRAKLARVLYEQMKREAASIRIQKHVRSHSARKSYKELQAAALVIQTGMRAMAARNEYRQRRRNKAAKIVQTQWRGFHAFSTYKQKKKASLSLQCLWRGRLARKELRKLRMAARDTGALKEAKDKLEKRVEELTWRLDFEKHLRIDLEEAKGQEISKLQKALQEMQMQLDEAHDAIIHEKEAAKIAIEQAPPVIKEVPEMDNTKVEKLTEENNKLEEEIRELKKRVEDFEQSYNEVEKECQARRREAEETQLRVSELQESIDRLQLNLSNLESENQVLRQQALVASTNEALSEEMDILKNKIKNLESENELLRTQRIAVEQIVSSDREPKGLETVDNTYTADNGHQTVEVHEEIKMEQQIPKDSSPPISLTKQRSLTDRQQENHDILIKCLAEDKQFDKGRPVAACTLYKALLQWRSFEAEKTNIFDRIVHTIRSSIEDQDNTGDLAYWLSTSSTLLFLLQTTIKAGNVPTRSPYRNRSSPTTLFGRMAQGFRSTSLSMAISSGYSGIEGSPNVRTRIEAKYPALLFKQHLTACVEKIYGMIRDNLKKEISPFLNQCIHAPRSARVRPLKGTSRSIHSNIMAKQQASIIHWQNIVNSLDSTLTILSENNVPSTITRKIFSQVFSYINVQLFNSLLLRRECCSFSNGEYLKAGLQELESWCSKATEQYVGSSWDELQHIRQAVGFLVLHQKSQKALDEITSDLCPMLSIAQIYRIGTMFWDDKYGTHGLSPEAISRMRALTLEDSASIPNNTFLLDVDSSIPFSIEEISRSFHIINLSDVEPPPLLRQRSDFQFLLQATEKEF
Protein: Excitatory amino acid transporter 4 (Sodium-dependent glutamate/aspartate transporter) (Solute carrier family 1 member 6) (P48664)
Organism: Homo sapiens (Human)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26690923, ECO:0000269|PubMed:7791878}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Spectrin beta chain, non-erythrocytic 2
- Excitatory amino acid transporter 3
- Rho guanine nucleotide exchange factor 11
- Histone acetyltransferase KAT5
- Nuclear receptor ROR-alpha
- Glutamate receptor ionotropic, delta-2
Sequence:
MSSHGNSLFLRESGQRLGRVGWLQRLQESLQQRALRTRLRLQTMTLEHVLRFLRRNAFILLTVSAVVIGVSLAFALRPYQLTYRQIKYFSFPGELLMRMLQMLVLPLIVSSLVTGMASLDNKATGRMGMRAAVYYMVTTIIAVFIGILMVTIIHPGKGSKEGLHREGRIETIPTADAFMDLIRNMFPPNLVEACFKQFKTQYSTRVVTRTMVRTENGSEPGASMPPPFSVENGTSFLENVTRALGTLQEMLSFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIAGKILEMEDMAVLGGQLGMYTLTVIVGLFLHAGIVLPLIYFLVTHRNPFPFIGGMLQALITAMGTSSSSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQEKGASRGRGGNESAM
Protein: Phosphodiesterase (EC 3.1.4.-) (G1U4Q4)
Organism: Oryctolagus cuniculus (Rabbit)
Interaction partners:
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Adenosine kinase
- Inosine triphosphate pyrophosphatase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Deoxycytidine kinase
- GMP reductase
- Hypoxanthine phosphoribosyltransferase
- Guanylate kinase
- GTP:AMP phosphotransferase AK3, mitochondrial
- Adenylosuccinate lyase
Sequence:
MHGQSLHCHCPGSASQDPLAQEPEPPGSRAGRLEDALLSLGSVIDLAGLQHAIKEALSAVLPRVETVYTYLLDEECRLVCEDPWHELPQEGKVREAVVSQKRLSCNGLGSSDLPGKPLARLVAPLAPDTQVLVLPLLDKEAGAVAAVILVHCGQLSDSEEWSLQAVEKHTLVALRRMRALQQRGLGQAPGTGAGAGAGAVQNTPVEAAEDQQGGAAYTDHDRKILHLCGELYDPDAASLQLKVLQYLQQETQAAHCCLLLVSEDNLQLSCKVIGDKVLGEEISFPLTTGRLGQVVQDKKSIQLEDLPSEDVQQLQSMLGCEVQTMLCVPVISRATDQVVALACAFNKLGGALFTEQDEQVIQHCFHYTGTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVASIDSNFANFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVGYDRTNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSHKFTIRGLPSNNSLDFLDEEYEVPGLDGTRAPVNGCCSLDTE
Protein: Polyprenyl transferase ausN (EC 2.5.1.-) (Austinoid biosynthesis clusters protein N) (Q5AR21)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Polyprenyl transferase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Terpene cyclase ausL
- FAD-binding monooxygenase ausB
- Polyprenyl synthetase
- FAD-dependent monooxygenase ausM
- Methyltransferase ausD
Sequence:
MAVISELKRHHPKTGLLRYLPTGVVPYGELVRIHRALGYYLNTSPYVVGIAYTAATAETKLPLDLLLDRLLLLTLWSLILRSAGCAWNDLVDVDIDRQISRTQSRPLPRGAISLSAATIFTACLFVLGCSLLLFLPRECLFDAGIKVFFALLYPFGKRFTDHPQLILINIAWAIPMAMHSLGMEPSSQILSMLCMCVFFSAVIVMIDLVYSRQDTEEDLKVGVKSMAVRYRNCVETMAYSLFAISSLALLFGGVLGGLRVPFVLFSVGGHIVGFWRFLRASLQAGPAGVESRAKSSCLIASVFWVLGLGIEYAEMVKEKDNPTDKKKHPH
Protein: RNA-binding protein RO60 (60 kDa SS-A/Ro ribonucleoprotein) (60 kDa Ro protein) (60 kDa ribonucleoprotein Ro) (RoRNP) (Ro 60 kDa autoantigen) (Ro60 autoantigen) (Sjoegren syndrome antigen A2) (Sjoegren syndrome type A antigen) (SS-A) (TROVE domain family member 2) (P10155)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs. Binds to endogenous Alu retroelements which are induced by type I interferon and stimulate porinflammatory cytokine secretion. Regulates the expression of Alu retroelements as well as inflammatory genes. May play roles in cilia formation and/or maintenance (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}.
Interaction partners:
- E3 ubiquitin-protein ligase TRIM21
- Lupus La protein
- U1 small nuclear ribonucleoprotein 70 kDa
- Calreticulin
- Major centromere autoantigen B
- Exosome complex component 10
Sequence:
MEESVNQMQPLNEKQIANSQDGYVWQVTDMNRLHRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTTKQEPMLFALAICSQCSDISTKQAAFKAVSEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAIADWYNEKGGMALALAVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHELYKEKALSVETEKLLKYLEAVEKVKRTRDELEVIHLIEEHRLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDAAFYKTFKTVEPTGKRFLLAVDVSASMNQRVLGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMVPCPVTTDMTLQQVLMAMSQIPAGGTDCSLPMIWAQKTNTPADVFIVFTDNETFAGGVHPAIALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTGALDVIRNFTLDMI
Protein: UPF0047 protein C4A8.02c (O14155)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MDVIQRIITLDRRSKGFYIITNDLVKKLPELKSFSSGTVNFFIQHTSAALTINENWDADTRADMNDILDKIVPESAGYRHTAEGLDDMPAHVKSSLIGPSLTVPITNGKLSLGTWQDIQLAEFRRQPHSRTIVCTIIGLRSN
Protein: Nicotinic acetylcholine receptor alpha 9 subunit (Q8K3J4)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
NLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVQGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMVMNIHFCGAEARPVPHWAKVVILKYMSRILFVYDVGESCLSPRHSQEPEQITKVYGKLPGSNLKASRNKDLSRKKELRKLLKNDLGYQGGIPQNTDSY
Protein: Profilin-3 (Profilin III) (Q9DAD6)
Organism: Mus musculus (Mouse)
Function: Binds to actin and affects the structure of the cytoskeleton. Binds to poly-L-proline, phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Slightly reduces actin polymerization. May be involved in spermatogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000269|PubMed:18692047}.
Interaction partners:
- Toll-like receptor 11
- Toll-like receptor 12
- Actin, cytoplasmic 1
- Protein diaphanous homolog 1
- Vasodilator-stimulated phosphoprotein
- Protein diaphanous homolog 2
- Actin, cytoplasmic 2
- Profilin-4
- Cofilin-1
- Cofilin-2
Sequence:
MSDWKGYISAVLRDQRIDDVAIVGHSDNRCVWASRPGGLLAAISPQEVGVLTGPDRHTFLQTGLSVAGRRCCVIRDYLLAEGDGVLDARTKGLDGRAICVGHTPRALLVLMGRRGVHGGILNKTVHDLIGGLREQCS
Protein: Actin family protein (Q8GWA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Actin-related protein 4
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
- Spc97 / Spc98 family of spindle pole body
- F-actin-capping protein subunit beta
- Actin-related protein 9
- Chromatin structure-remodeling complex protein SYD
- Actin-related protein 2/3 complex subunit 2A
- TOM1-like protein 1
- RuvB-like protein 1
Sequence:
MVGMNENDLFVGDDAEARSGILTLDYPMEHGVVSNWDDMEKIWYHTFYSELRVAPEEHPVLLTEAPLNPKADREKMTQIMFETFAVPSMYIGMQAALSLHASGRTTGTVLDSGDGVSYIVPIYEGSALPHAILRLDLAGRHLTNYLMKIMMERGYTSAEREVVRDIKEQFGYIALDYEQEMEKATKSSAIDRTYELPDGQVITIGAERFRCPEVLFQPSLIGMETSGIHEKTYNSIMKCDDDIRKDLYGNIVLSGGTTMFRGIEERMTKEINALAAANMRIKIVAPPERKYSVWIGGSILASLSTYEQMWITKAEYEENGPAIVHTKCF
Protein: Signal recognition particle receptor FtsY (SRP receptor) (EC 3.6.5.4) (P9WGD9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC) (By similarity). Most of the substrate proteins are involved in stress regulation, lipid metabolism, intermediary metabolism, and cell wall processes. Shows GTPase activity. Can also hydrolyze ATP, UTP and CTP.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00920}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00920}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00920}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00920}.
Interaction partners:
- Signal recognition particle protein
- Protein translocase subunit SecY
- Protein translocase subunit SecE
- Sec translocon accessory complex subunit YajC
- Protein translocase subunit SecA 1
- Probable ATP/GTP-binding protein
- Probable protein-export membrane protein SecG
- Protein translocase subunit SecA 2
- Membrane protein insertase YidC
- Large ribosomal subunit protein uL23
Sequence:
MWEGLWIATAVIAALVVIAALTLGLVLYRRRRISLSPRPERGVVDRSGGYTASSGITFSQTPTTQPAERIDTSGLPAVGDDATVPRDAPKRTIADVHLPEFEPEPQAPEVPEADAIAPPEGRLERLRGRLARSQNALGRGLLGLIGGGDLDEDSWQDVEDTLLVADLGPAATASVVSQLRSRLASGNVRTEADARAVLRDVLINELQPGMDRSIRALPHAGHPSVLLVVGVNGTGKTTTVGKLARVLVADGRRVVLGAADTFRAAAADQLQTWAARVGAAVVRGPEGADPASVAFDAVDKGIAAGADVVLIDTAGRLHTKVGLMDELDKVKRVVTRRASVDEVLLVLDATIGQNGLAQARVFAEVVDISGAVLTKLDGTAKGGIVFRVQQELGVPVKLVGLGEGPDDLAPFEPAAFVDALLG
Protein: Large ribosomal subunit protein mL38 (39S ribosomal protein L38, mitochondrial) (B2R894)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MPNSDIDLSNLERLEKYRSFDRYRRRAEQEAQAPHWWRTYREYFGEKTDPKEKIDIGLPPPKVSRTQQLLERKQAIQELRANVEEERAARLRTASVPLDAVRAEWERTCGPYHKQRLAEYYGLYRDLFHGATFVPRVPLHVAYAVGEDDLMPVYCGNEVTPTEAAQAPEVTYEAEEGSLWTLLLTSLDGHLLEPDAEYLHWLLTNIPGNRVAEGQVTCPYLPPFPARGSGIHRLAFLLFKQDQPIDFSEDARPSPCYQLAQRTFRTFDFYKKHQETMTPAGLSFFQCRWDDSVTYIFHQLLDMREPVFEFVRPPPYHPKQKRFPHRQPLRYLDRYRDSHEPTYGIY
Protein: Structure-specific endonuclease subunit SLX1 (EC 3.1.-.-) (GIY-YIG domain-containing protein 1) (Q8BX32)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100}.
Interaction partners:
- Structure-specific endonuclease subunit SLX4
- Structure-specific endonuclease subunit MUS81
- DNA repair endonuclease XPF
- DNA excision repair protein ERCC-1
- Structure-specific endonuclease subunit EME1
- Actin-related protein 2/3 complex subunit 4
- Fanconi anemia group M protein homolog
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- DNA topoisomerase 3-alpha
- RecQ-mediated genome instability protein 1
Sequence:
MDHAARPGRFFGVYLLYCQNPRHRGRVYVGFTVNPARRVRQHNAGRKKGGAWRTSGRGPWDMVLIIHGFPSAVAALRFEWAWQHPQASRRLTHVGPRLRSEAAFAFHLRVLAHMLRVPPWVRLPLTLRWLRPDFRHELCPAPPAHMPIAFGPPPPQPLVPKRPAVSEADSERQLDLGTKARCSLCARLLQDEEGPLCCPHPGCPLRAHIICLAEEFLQEEPGQLLPLEGHCPSCKKSLLWGNLVGQCHADTEEEEDLELEEEHWTDLLET
Protein: Probable flavin mononucleotide-dependent alkene reductase (EC 1.3.1.-) (Flavin mononucleotide-dependent nitroreductase) (EC 1.7.1.-) (NTR2) (E9AGH7)
Organism: Leishmania infantum
Function: May function as a flavin mononucleotide (FMN)-dependent alkene reductase on substrates carrying alpha,beta-unsaturated carbonyl groups (ketones, aldehydes, carboxylic acids, esters, lactones or cyclic imides). The catalysis depends on NAD(P)H, which acts as hydride donor for the reduction. Seems to be involved in metabolic pathways required for efficient replication of amastigotes within macrophages.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:27812217}.
Interaction partners:
- fumarate reductase
- Putative oxidoreductase
Sequence:
MSAASKSIDVMLKPLLVGGRPISNRFVMAPLTRCRADDNHVPTAAMVKHYSDRASMGLIITEATQIQKGYSTFAHEGGIYDKEHVDGWRKVTDAVHDKGGIIFCQIHNGGRSTVPSNVDEGVRIVAPSAVAITGHKCAGSFARNGKTQPYPVPHAMAAEEIASYVNLYAAAARNAIAAGFDGVEVHGANGYLIDQFLKTSSNQRTDEYGGSIENRCRFLFEVLDAVIQAIGRERVGLRISPLNSFNDQSDEDPQALTRYICSQLNLRTIAFLDVMRGDFFSPARGADKWAREEYEGVLFTGMSFEIEEAAKAVESGAADAVVFGTKALANPDLVARAVAGAPLNKPDPATFYTTGEAGYNDYPFM
Protein: Serine/threonine-protein phosphatase PGAM5, mitochondrial (Serine/threonine-protein phosphatase Pgam5, mitochondrial) (Q8I1V2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MYVNFFNKLNIPKCLRTNFNFKRRFSETKQNIQIKYIKENKKKYVFYTAVTSLSLSIALTYAYEKFVLYKWNRRYDYYYNPNIKFFEKKEKKEGKKDKKNTTKHIILVRHGQYERRYKDDENSKRLTKEGCKQADITGKKLKDILNNKKVSVIYHSDMIRAKETANIISKYFPDANLINDPNLNEGTPYLPDPLPRHSKFDAQKIKEDNKRINKAYETYFYKPSGDEDEYQLVICHGNVIRYFLCRALQIPLFAWLRFSSYNCGITWLVLDDEGSVVLREFGSVSHLPFESVTYF
Protein: B-box type zinc finger family protein (O81834)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- B-box zinc finger protein 23
- B-box zinc finger protein 21
- B-box zinc finger protein 25
- B-box zinc finger protein 19
- B-box zinc finger protein 24
- B-box zinc finger protein 22
- B-box zinc finger protein 20
- Uncharacterized protein
- Calponin-like domain protein
- B-box zinc finger family protein
Sequence:
MGKKCDLCNGVARMYCESDQASLCWDCDGKVHGANFLVAKHTRCLLCSACQSLTPWKATGLRLGPTFSVCESCVALKNAGGGRGNRVLSENRGQEEVNSFESEEDRIREDHGDGDDAESYDDDEEEDEDEEYSDDEDEDDDEDGDDEEAENQVVPWSAAAQVPPVMSSSSSDGGSGGSVTKRTRARENSDLLCSDDEIGSSSAQGSNYSRPLKRSAFKSTVVV