wanglab/gogpt-training-data huggingface dataset:
Protein: Plasmodium RESA N-terminal domain-containing protein (Q8IAK9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MIFVKSKILYFLKWPSVAIEENFSGSFKCLFKNKRNKYVRNNLSRFILSVSLILFFFHFVLCSTIENVEILKNDYNTLTESHNIINRRSRNLGANPESISLGYELSEKDEGNKNDLINSATDVSTELENLKERLFPELELYTNDQNSRNNTPNLRKGSLGFDSFKKLELGTLNQFDKDKMINLKDETNMNEFEGFLGRNSMASNVVTSELFDEPVDDSSSTTTSTGTKLQNVPSNDNNGELLKDEPIDDYINNNSKVESEDNYYAQQNMQSQSKDNYASEQNVADQSTDNYPTQHDVPVQLRDNYASEQEYFDRGEQLNDVSADNNTSNKLKDEPVDNNTSNKLKDEPVDNNTSNKLKDEPVDDNTSNKLKDEPVDNNTINKLKDEPVDDNTSNILKDEPVDDHAGKHLKDEPVDDHAGKHMKDEPVDIDRTNIKKGLNEQHVNPWTTTLADLKNINNSMKIEKNNKSNEQVKNTSVSKSCDIIKPSKFNKKNLFEQRLQSVEGKNFFEGRSQNLEGRSNFDERSQIVEQRRNFDDRDQNIMDRKNFDERNQQVNDRRNFDERNQQVNDRRNFDDRDQNVMDRRNFDERNQQVNDRRNFDERNQQVNDRRNFDDRDQNVMDRRNFDERNQQVNDRRNFDERNQQVNDRRNFDDRDQNVMDRRNFDERNQQVNDRRNFDERNQQVNDRRNFDERNQHVNDRRNFDERNQNVNDRRNFDERNQNVNDRRNFDERNQQVNDRRNFDERYQNVNERRNFDERNQQVNDRRNFDERNQHVNERYQNVNDRRNFDERNQQVNDRRNFDERNQHVNERRNFDERNQHVNERYQNVNDRRNFDERNQHVNERRNFDQRAPNVEERRYMDPRNPNIPYVRFPHHQWGQGMMYGRPYYPWVPFMGDGRGYNFYNPHQHMVYGRPYYWVPPPPALEYTKGFNPMEQRREEDRGHMGGRGSRYPEEERYNYNNKRSNSIPEGRNYEENAYERGGGNNKWDFRNMYDRLRDEDENDYDQPPSTSSSNRGRGNERYSQSRDRREERNNYNSDYYTRGNERTYNNSNVTSSSNRELIPYKKEILPFGVSNSELEDKLTEEELNERIRRLDYTVSVKDMFILWNHILAHERKKYTKMQEYLMYYSQYLEKTYLVPTAFRKKYWWRVHYMLTEEVVKRERTDNLDFHQFLRKGSCEKREFLYFINSKRKGWADLTETMKNIWMERLTYKMRKYSGA
Protein: tRNA(Ile)-lysidine/2-thiocytidine synthase N-terminal domain-containing protein (Q725M8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Peptidase, M23/M37 family
- PAP2 family protein
Sequence:
MAREKYTYAQQVCIKSAGKTMQHTGMLYPGARIGVAVSGGMDSWVLLQVLRIRQRIVPFPFEIMALHVNPGFDPENHAPLLPWLERNGVAAHIEVTDHGPRAHSPENRRNSACFYCAWLRRKRLFELCAQYRLSHLAFGHNADDLVGTFLMNLYQNGRVDGMSMKEAFFGGRLQVIRPLLMVEKSDIARAVRQWGLPVWSNPCPSAGATRRSEVMDDFQRLCRENKGMKRNVFNGLCRWQMDLTPKAD
Protein: MICOS complex subunit MIC19 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 3) (Q9NX63)
Organism: Homo sapiens (Human)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9CRB9}; Lipid-anchor {ECO:0000305}; Intermembrane side {ECO:0000250|UniProtKB:Q9CRB9}. Cytoplasm {ECO:0000269|PubMed:22567091}. Nucleus {ECO:0000269|PubMed:22567091}. Mitochondrion {ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101}.
Interaction partners:
- MICOS complex subunit MIC27
- MICOS complex subunit MIC10
- MICOS complex subunit MIC25
- Sorting and assembly machinery component 50 homolog
- MICOS complex subunit MIC60
- MICOS complex subunit MIC13
- MICOS complex subunit MIC26
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial
- Metaxin-2
- DnaJ homolog subfamily C member 11
Sequence:
MGGTTSTRRVTFEADENENITVVKGIRLSENVIDRMKESSPSGSKSQRYSGAYGASVSDEELKRRVAEELALEQAKKESEDQKRLKQAKELDRERAAANEQLTRAILRERICSEEERAKAKHLARQLEEKDRVLKKQDAFYKEQLARLEERSSEFYRVTTEQYQKAAEEVEAKFKRYESHPVCADLQAKILQCYRENTHQTLKCSALATQYMHCVNHAKQSMLEKGG
Protein: Immunoglobulin heavy constant delta (Ig delta chain C region) (Ig delta chain C region NIG-65) (Ig delta chain C region WAH) (P01880)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen. IgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. The membrane-bound IgD (mIgD) induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. Soluble IgD (sIgD) concentration in serum below those of IgG, IgA, and IgM but much higher than that of IgE. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. After the antigen binds to the B-cell receptor, the secreted form sIgD is shut off. IgD is a potent inducer of TNF, IL1B, and IL1RN. IgD also induces release of IL6, IL10, and LIF from peripheral blood mononuclear cells. Monocytes seem to be the main producers of cytokines in vitro in the presence of IgD.
Subcellular location: [Isoform 1]: Secreted {ECO:0000303|PubMed:11282392}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein {ECO:0000303|PubMed:11282392}.
Interaction partners:
- Immunoglobulin lambda-like polypeptide 5
- B-cell antigen receptor complex-associated protein alpha chain
- B-cell antigen receptor complex-associated protein beta chain
- Mevalonate kinase
- Immunoglobulin heavy variable 3-11
- Immunoglobulin heavy variable 4-38-2
- Immunoglobulin J chain
- B-lymphocyte antigen CD19
- Immunoglobulin heavy variable 1-3
- Immunoglobulin lambda-like polypeptide 1
Sequence:
APTKAPDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKCVVQHTASKSKKEIFRWPESPKAQASSVPTAQPQAEGSLAKATTAPATTRNTGRGGEEKKKEKEKEEQEERETKTPECPSHTQPLGVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTCTLNHPSLPPQRLMALREPAAQAPVKLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPRSTTFWAWSVLRVPAPPSPQPATYTCVVSHEDSRTLLNASRSLEVSYLAMTPLIPQSKDENSDDYTTFDDVGSLWTTLSTFVALFILTLLYSGIVTFIKVK
Protein: Arrestin domain-containing protein 17 (Calcineurin-interacting protein 1) (O45782)
Organism: Caenorhabditis elegans
Function: Involved in several behavioral responses including chemotaxis towards lysine and adaptation to repeated osmotic stress. In addition, plays a role in resuming egg-laying and locomotion after starvation.
Interaction partners:
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
Sequence:
MVQLDRFEILFNNPEQAYFAGQEISGKVIIENKEPKKVNEILLELKGRARTYWTKHSGKSRKHCSHSEPYFLEQFNPGYTHKFTVVKDGKEKERILPAGIHQVPFSYTLPKSLPSSFEGEFGHIRYTCKAICERPWDFDIVSRKAFTVVGIEDINSDPKLNEPATCVESNHAVTFCCRSAGSVTGEIRISKCGYTPGEKIDVSFKVINLSSKTRTTALRFVQQTTYKAKTFAGHEHIKNVVRVISKIDKGEVPGGSTTEWQEESITIPSLPPKLGKCKILSVTYSVELEVEQTLTVPCPIVIGSIPQLSQLLIHSKQSVQSAGNGSLPKSSIKDSPPKWDSESCVQVTITDESGQLVEELGNEMEALLSARKRVRMPSSILSELYPTMPSPYYKESFFGASDISEEKEQAQFGEASFAPKYPFYTD
Protein: Uncharacterized protein (Q582N0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- RNA polymerase-associated protein CTR9
Sequence:
MTSVLRAPTVRLEMSYGEFIRACTRGYCFDCSWNIAPPTVPNAPILYNLLPMVEFLKSTEPLGVMGAELDAMAIGVLNSIPLSYHLLRPQVVEEARQLSMESERRVENAKQRAIAEGLSDQTTWSPGSVNENLDPKDAELLDTDIDVSMMLERDKPSLTHLQRPLYTDMGLVSPEQRHLERISRIVPDELRSIVSLPLSLMSQTQPGGPPQHGGYLLSSASLAGAARGSGETSENTAVQWKDGVIASFKAARSLDVSHEKMLKAIARTKLGLGGENCRTLAFVQRLWKLLFEGTNERQQCGMWSCLCHFSANYGSHDESEEVLEHAVEALELPDRGLWCSVTREYVKLLREYTASLPGGVEERRAALQISESELNPPKGGAFGADISVDNRLRRERGELGPNRQPVPIYPVEVVPLYPAGFQEYAEVYGTSGNEAANEVKLGEVETALHHVVLPGAVVGPESRSGGPHVLVANTNLLVADKQSDLQAADGVTLTYHASRENTFERLVLDANNTSSYLFQLCSVPETSGDVPTGLASAAGHYAVYRRLALRDLYVKAPDAKDPPLERYVVVFGEKENPRTESRKRSREDLGAGEGSAFYGTEGGGKYVE
Protein: Uncharacterized protein C4C5.01 (O14165)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Riboflavin kinase
Sequence:
MAAKHVKYMACLFDMDGLLVDSETIYTKTTNLILDRYGKDPLPISVKAQMMGRPGSAAAKVVIDWSNIPMTPQQFVDEQQVIRAKFWSSLKPMPGAESLINNLSNHGIDIGLATSSNTANYNMKTAHLKHIFEKFGKNVITGDNPSIAPGRGKPFPDIWLKVLNLINESRKQRGLKALTPSQCIAFEDSIPGVKSAKAAGMHVIWVPDAAIKNLVGDQLNEIVDSQCETLPSLSEFDINKYLNINSKQA
Protein: Insulin-degrading enzyme (EC 3.4.24.56) (Abeta-degrading protease) (Insulin protease) (Insulinase) (Insulysin) (P14735)
Organism: Homo sapiens (Human)
Function: Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling. Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin. Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP (By similarity). Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia (Probable). Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP. Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients. Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20364150, ECO:0000269|PubMed:9830016}. Cell membrane {ECO:0000250|UniProtKB:P35559}. Secreted {ECO:0000269|PubMed:9830016}. Note=Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform.
Interaction partners:
- Insulin
- Amyloid-beta precursor protein
- Islet amyloid polypeptide
- Pro-glucagon
- Polyubiquitin-C
- C-C motif chemokine 3
- Ubiquitin-ribosomal protein eS31 fusion protein
- Insulin-like growth factor 2
- Polyubiquitin-B
- Membrane metallo-endopeptidase-like 1
Sequence:
MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL
Protein: NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 6) (NADH-plastoquinone oxidoreductase subunit 6) (Q95695)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
Sequence:
MDLPGPIHDFLLVFLGSGLLVGGLGVVLLPNPIFSAFSLGFVLVCISLLYILSNSHFVAAAQLLIYVGAINVLIIFAVMFMNDSEYSTDFNLWTIGNGITSLVCTTILFLLMSTILDTSWYGVIWTTKLNQILEQDLISNSQQIGIHLSTDFFLPFELISIILLVALIGAISVARQ
Protein: D(-)-tartrate dehydratase (EC 4.2.1.81) (Q89FH0)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Function: Catalyzes the dehydration of D-tartrate to oxaloacetate.
Interaction partners:
- Galactarate dehydratase
- Vanillate O-demethylase oxidoreductase
Sequence:
MSVRIVDVREITKPISSPIRNAYIDFTKMTTSLVAVVTDVVREGKRVVGYGFNSNGRYGQGGLIRERFASRILEADPKKLLNEAGDNLDPDKVWAAMMINEKPGGHGERSVAVGTIDMAVWDAVAKIAGKPLFRLLAERHGVKANPRVFVYAAGGYYYPGKGLSMLRGEMRGYLDRGYNVVKMKIGGAPIEEDRMRIEAVLEEIGKDAQLAVDANGRFNLETGIAYAKMLRDYPLFWYEEVGDPLDYALQAALAEFYPGPMATGENLFSHQDARNLLRYGGMRPDRDWLQFDCALSYGLCEYQRTLEVLKTHGWSPSRCIPHGGHQMSLNIAAGLGLGGNESYPDLFQPYGGFPDGVRVENGHITMPDLPGIGFEGKSDLYKEMKALAE
Protein: Small nuclear ribonucleoprotein Sm D2 (Sm-D2) (snRNP core protein D2) (P62316)
Organism: Homo sapiens (Human)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000305}.
Interaction partners:
- U4/U6 small nuclear ribonucleoprotein Prp4
- U4/U6 small nuclear ribonucleoprotein Prp31
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein F
- U6 snRNA-associated Sm-like protein LSm3
- Small nuclear ribonucleoprotein-associated protein N
- Protein BUD31 homolog
- U1 small nuclear ribonucleoprotein C
- U1 small nuclear ribonucleoprotein 70 kDa
Sequence:
MSLLNKPKSEMTPEELQKREEEEFNTGPLSVLTQSVKNNTQVLINCRNNKKLLGRVKAFDRHCNMVLENVKEMWTEVPKSGKGKKKSKPVNKDRYISKMFLRGDSVIVVLRNPLIAGK
Protein: Dedicator of cytokinesis 1 (A0A096LNH6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTRWVPTKREEKYGVAFYNYDARGADELSLQIGDTVHILETYEGWYRGYTLRKKSKKGIFPASYIHLKEAIVEGKGQHETVIPGDLPLIQEVTTTLREWSTIWRQLYVQDNREMFRSVRHMIYDLIEWRSQILSGTLPQDELKELKKKVTAKIDYGNRILDLDLVVRDEDGNILDPELTSTISLFRAHEIASKQVEERLQEEKSQKQNIDINRQAKFAATPSLALFVNLKNVVCKIGEDAEVLMSLYDPVESKFISENYLVRWSSSGLPKDIDRLHNLRAVFTDLGSKDLKREKISFVCQIVRVGRMELRDNNTRKLTSGLRRPFGVAVMDVTDIINGKVDDEDKQHFIPFQPLALDDAIRHKPLNMSSRFSPRVAGENDFLQTVINKVIAAKEVNHKGQGLWVTLKLLPGDIHQIRKEFPHLVDRTTAVARKTGFPEIIMPGDVRNDIYVTLVQGDFDKGSKTTAKNVEVTVSVYDEDGKRLEHVIFPGAGDEAISEYKSVIYYQVKQPRWFETVKVAIPIEDVNRSHLRFTFRHRSSQDSKDKSEKIFALAFVKLMRYDGTTLRDGEHDLIVYKAEAKKLEDAATYLSLPSTKAELEEKGHSATGKSMQSLGSCTISKDSFQISTLVCSTKLTQNVDLLGLLKWRSNTSLLQQNLRQLMKVDGGEVVKFLQDTLDALFNIMMENSESETFDTLVFDALVFIIGLIADRKFQHFNPVLETYIKKHFSATLAYTKLTKVLKNYVDGAEKPGVNEQLYKAMKALESIFKFIVRSRILFNQLYENKGEADFVESLLQLFRSINDMMSSMSDQTVRVKGAALKYLPTIVNDVKLVFDPKELSKMFTEFILNVPMGLLTIQKLYCLIEIVHSDLFTQHDCREILLPMMTDQLKYHLERQEDLEACCQLLSHILEVLYRKDVGPTQRHVQIIMEKLLRTVNRTVISMGRDSELIGNFVACMTAILRQMEDYHYAHLIKTFGKMRTDVVDFLMETFIMFKNLIGKNVYPFDWVIMNMVQNKVFLRAINQYADMLNKKFLDQANFELQLWNNYFHLAVAFLTQESLQLENFSSAKRAKILNKYGDMRRQIGFEIRDMWYNLGQHKIKFIPEMVGPILEMTLIPETELRKATIPIFFDMMQCEFHSTRSFQMFENEIITKLDHEVEGGRGDEQYKVLFDKILLEHCRKHKYLAKTGETFVKLVVRLMERLLDYRTIMHDENKENRMSCTVNVLNFYKEIEREEMYIRYLYKLCDLHKECDNYTEAAYTLLLHAKLLKWSEDVCVAHLTQRDGYQATTQGQLKEQLYQEIIHYFDKGKMWEEAIALGKELAEQYENEMFDYEQLSELLKKQAQFYENIVKVIRPKPDYFAVGYYGQGFPTFLRGKVFIYRGKEYERREDFEARLLTQFPNAEKMKTTSPPGDDIKNSPGQYIQCFTVKPKLDLPPKFHRPVSEQIVSFYRVNEVQRFEYSRPIRKGEKNPDNEFANMWIERTIYTTAYKLPGILRWFEVKSVFMVEISPLENAIETMQLTNDKINSMVQQHLDDPSLPINPLSMLLNGIVDPAVMGGFANYEKAFFTDRYLQEHPEAHEKIEKLKDLIAWQIPFLAEGIRIHGDKVTEALRPFHERMEACFKQLKEKVEKEYGVRIMPSSLDDRRGSRPRSMVRSFTMPSSSRPLSVASVSSLSSDSTPSRPGSDGFALEPLLPKKMHSRSQDKLDKDDLEKEKKDKKKEKRNSKHQEIFEKEFKPTDISLQQSEAVILSETISPLRPQRPKSQVMNVIGSERRFSVSPSSPSSQQTPPPVTPRAKLSFSMQSSLELNGMTGADVADVPPPLPLKGSVADYGNLMENQDLLGSPTPPPPPPHQRHLPPPLPSKTPPPPPPKTTRKQASVDSGIVQ
Protein: LP13728p (Leucine-rich repeat-containing G protein-coupled receptor 1, isoform A) (Leucine-rich repeat-containing G protein-coupled receptor 1, isoform B) (Q9VEG4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Beta glycoprotein hormone related polypeptide
- Glycoprotein hormone alpha 2
Sequence:
MEKHPSLSQRMGTTYRPRKGLKCLSFEFQCRLLLHHLLLTSLSGRHFVYATSAVGGALSANNCHDIHHGFDVYPNLTAVSLAQSTDTPLTATMPRSAWKCCCWNASNQAEEVECRCEGDGLNRVPQTLTLPIQRLTIASAGLPRLRHTGLKVYGSTLLDVAFTDCLQLELIQDGAFANLTLLRTIYITNAPKLTFLSKDVFLGISDTVDIIRIINSGLTRVPDLGHLPPHNILQMIDLDNNQITRIDSKSIKVKTAQLILTNNEISYVDDSAFFGSKIAKLSLKENKKLQMMHPNAFDGIIDITELDLSSTSLVGLPSAGLQNIEALYIQNTHTLKTIPSIYNFRNLQRAYLTHSFHCCAFQFPSRHDPQRHAQRMLEIEKWRKQCKSDSGTRKERSTLDNPFNMPEDFGSFGGTDDSATDITPITFASFDYMADDTMNKGTFHEKIILNPGDDSSAELCGNFTFRKPNIECYPMPNDLNPCEDVMGYQWLRISVWIVVALAVVGNVAVLTVILSIRPESTPVPRFLMCHLAFADLCLGLYLLLVACIDAHSMGEYFNFAYDWQYGLGCKVAGFLTVFASHLSVFTLTVITIERWLAITQAMYLNHRIKLRPAALIMLGGWIYSMLMSSLPLFGISNYSSTSICLPMENRDVYDTIYLIAILGSNGVAFSIIAVCYAQIYLSLGRETRQAHQNSPGELSVAKKMALLVFTNFACWSPIAFFGLTALAGYPLINVTKSKILLVFFYPLNSCADPYLYAILTSQYRQDLFTLLSKLGLCQQSALKYKDSLSGQATTRFTIHGSIQRHSSLTCKMQTVMGAETQKMLKNSEDYV
Protein: Opaque 2 (Q39532)
Organism: Coix lacryma-jobi (Job's tears)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEHVISMEEILGPFWDLPPSPPPLPLPEQQPLVTDTGSVVIDGVVTQGGGDGEGGDMMGQNTTEWTFERLLEEEILINKTTLVTNSSCSTLNIDPVVEVDQGTMASGAVSAVGDPMEYNAILKRKLEVDLVAFKMWRASSVVNSERSQDSNNHNGGSKNVVQNKLNGEDPINNHAQNVDLRVRLATSSSSRDPSPSDEDMDGEVEILGFKMPTEERVRKRKESNRESARRSRYRKAAHLKELEDQVEQLKAENSCLLRRLAALNQKYNEANVDNRVLRADMETLRAKVKMGEDSLKRVMEMSSLPPSMPIPALPSSSDASVPIQDDIINYFSTTPAADEDAPVDNNSFIIMPMADPLQLVQAEDQPTMGAMELIQKTMGAMPTSPGSALQESQLLGLGPDETINMDMY
Protein: Centrin-4 (Q8I714)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Thioredoxin-like protein
- NADH-cytochrome b5 reductase, putative
Sequence:
MNTMLIKDNINISINEDVEKELYECFSLFDTNKCGYIDIREFYFALKSLGLNFKKEQVKNIFLDIKKDIDEKLNFDEFFDIATKYLHTRYNDDEMDQMFSLFDPNDTGKITLQALRKVCTDIGENISDTELNNMIHFADKNNDKVIDKNEFKKVLLCSWKNDPLSDVDSDS
Protein: Sestrin-3 (EC 1.11.1.-) (Q9CYP7)
Organism: Mus musculus (Mouse)
Function: May function as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway. May also regulate the insulin-receptor signaling pathway through activation of TORC2. This metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By similarity). May prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25377878}.
Interaction partners:
- Sestrin-1
- GATOR2 complex protein WDR24
- Sestrin-2
- GATOR1 complex protein DEPDC5
- GATOR2 complex protein MIOS
- GATOR2 complex protein WDR59
- GATOR1 complex protein NPRL3
- GATOR1 complex protein NPRL2
- Nucleoporin SEH1
- Ras-related GTP-binding protein A
Sequence:
MNRGGSSASASANYLLCTNCRKVLRKDKRIRVSQPLTRGPSAFIPEKEVVQANTADERTNFLVEEYSTSGRLDNITQVMSLHTQYLESFLRSQFYMLRMDGPLPLPDRHYIAIMAAARHQCSYLINMHVDEFLKTGGIAEWLNGLEYVPQRLRNLNEINKLLAHRPWLITKEHIQKLVKTGENNWSLPELVHAVVLLAHYHALASFVFGSGINPERDPGIANGFRLISVSSFCVCDLANDNSIENTSLAGSNFGIVDSLGELEALMERMKRLQEDREDDETTREEMTTRFEKEKKESLFVVPGETLHAFPHSDFEDDVIVTADVSRYIEDPSFGYEDFARRGEEHLPTFRAQDYTWENHGFSLVNRLYSDIGHLLDEKFRMVYNLTYNTMATHEDVDTTTLRRALFNYVHCMFGIRYDDYDYGEVNQLLERSLKVYIKTVTCYPERTTKRMYDSYWRQFTHSEKVHVNLLLMEARMQAELLYALRAITRHLT
Protein: Type I iodothyronine deiodinase (EC 1.21.99.3) (EC 1.21.99.4) (5DI) (DIOI) (Type 1 DI) (Type-I 5'-deiodinase) (P49895)
Organism: Homo sapiens (Human)
Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine). Plays a role in providing a source of plasma T3 by deiodination of T4 in peripheral tissues such as liver and kidney.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P24389}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:P24389}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P24389}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:P24389}. Basolateral cell membrane {ECO:0000250|UniProtKB:P24389}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:P24389}.
Interaction partners:
- Type II iodothyronine deiodinase
- Selenide, water dikinase 2
- Selenide, water dikinase 1
- Glutathione peroxidase 6
- Epididymal secretory glutathione peroxidase
- Glutathione peroxidase 3
- Glutathione peroxidase 2
- Glutathione peroxidase 7
- Probable glutathione peroxidase 8
- G-protein coupled bile acid receptor 1
Sequence:
MGLPQPGLWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMGEKTGMTRNPHFSHDNWIPTFFSTQYFWFVLKVRWQRLEDTTELGGLAPNCPVVRLSGQRCNIWEFMQGNRPLVLNFGSCTUPSFMFKFDQFKRLIEDFSSIADFLVIYIEEAHASDGWAFKNNMDIRNHQNLQDRLQAAHLLLARSPQCPVVVDTMQNQSSQLYAALPERLYIIQEGRILYKGKSGPWNYNPEEVRAVLEKLHS
Protein: Exocrine gland-secreted peptide 22 (A8R0V4)
Organism: Mus musculus (Mouse)
Function: Pheromone produced by juveniles which activates a small number of vomeronasal organ sensory neurons and exhibits a powerful inhibitory effect on adult male mating behavior.
Subcellular location: Secreted {ECO:0000269|PubMed:24089208}. Note=Secreted from the lacrimal gland into tears. {ECO:0000269|PubMed:24089208}.
Interaction partners:
- Vomeronasal type-2 receptor 116
- Vomeronasal 2, receptor 115
Sequence:
MNSVPVMLFSISILLAAMLTEGRGLTQTQKESIFSAEHKSDLKSYLEMLVCRRLRDVPESVIHISKVSKEILPDDLLSTYLLELLVCFDKDKLVQSKGIVFNTIKRLLTNT
Protein: GATA-type domain-containing protein (H9G2S6)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHYRDANYSISRNKVNLHHEEFMLDGVVGGEDHDMQNTNEVRAELDSLLRLDPDTNSIIDALHISQPIEENMDYEGKPVEFTLGTSSGGASLAPTSSTTAASIAPFSYNTSATNYYNTTPSSYPMFLNYQYAGGTTVTTDMDAFSGMDMSMNNGVFGTQNNPSYFYPTTQLNTYGYDTLAAATTASGITVNNNQLNVNIVQGNGTIVPQPITQNIISTVSNVQSSVPINNSQPLTPTGLAGCSTSSGSSSASSSSANSTSTPKNTISKANRSSGGANNSQFSTEDRECVNCGVHNTPLWRRDGSGNYLCNACGLYFKMNHHARPLVKPKKRQQNAQKRTGIECVNCRTNTTTLWRRNGEGHPVCNACGLYFKLHKVERPITMKKDGIQTRNRKLSAKGSRRMKKENGGTPTSMGMPTTSSSISSGIELDQSGVWGMKNTQPMLMTPTAYAFPASNFYFNSIEDQLEYKTCPPMMVDFGGQMKNLNLN
Protein: SD19533p (Sorting nexin 16) (Q7JR96)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Protein nervous wreck
- LD15323p
- Sorting nexin
Sequence:
MSLRALRKRETGTGYGNNNNHLAAPARTSQATLFKKASTAITSPKKSLLKTGNSVCGLDKRSQFREQKLLGRKCHSSPDLRQIGKYQNNSLLRSKSEGDVSLILASNSGAPLTVANAKSEVCLQRISSHSYEQSPRTPINKSEMLGGARSHRDLTQSSYGNQAGGHSVDLESRSRTPRRMSECSLGYSQSSSRHTGSNSMFASQMTLSSGSVVPPVDPNAVLRVPIIGYEVMEERARFTAYKLRVENPETNDYWLVMRRYTDFVRLNSKLKQAFPNLTLMLPRKKLFGDNFNAVFLDNRVQGLQIFVNSVMAKEELRKCKLVREFFCLDEPPSYSESMEECRAIFEAQEETIEHLKLQIRNKNDLILSLQQKLREEMNEKEQLREAMKNMELNCSHCSSASDSLGIK
Protein: T. brucei spp.-specific protein (Q584I4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFPNAHYPVARTPHIREGYSGGYQRANKHTRNWNTSYTRHPRRTYDRDPPPYTATDVPSVTGSYGLNENFIVVAAPPNDVNCESVITNTHGNAAKQNGSSRATVETGVDTNACTGSISEKSEGTRAVTSRAEIDKGVDTSEKEKYKDLQKLLRRIIDLEFSERCTQRSITVVTTICDTLCVNPVAVVKVMEVMDQCFNESVQNQQPQLLMHYWYIVDAVLKQFNDKPPLLKAALVAIPHFVQKYLPWRGSNLASQSWSNLQSYKSAYEDMLDTWKVFLEKQTHQEIMNLWREGVKDQPTDDTKSEVGGSGLARDAAINTG