wanglab/gogpt-training-data huggingface dataset:
Protein: Cytosolic Fe-S cluster assembly factor NUBP2 (Nucleotide-binding protein 2) (NBP 2) (Q9Y5Y2)
Organism: Homo sapiens (Human)
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03039}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03039}. Cytoplasm {ECO:0000269|PubMed:29848660}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9R061}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9R061}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q9R061}. Note=Enriched at the centrosomes during mitosis. Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis (By similarity). Localized at centrioles and in the nucleus at interphase (By similarity). Colocalizes with nubp-1 at prometaphase (By similarity). {ECO:0000250|UniProtKB:Q9R061, ECO:0000255|HAMAP-Rule:MF_03039}.
Interaction partners:
- Cytosolic Fe-S cluster assembly factor NUBP1
- Cytosolic iron-sulfur assembly component 3
- Probable cytosolic iron-sulfur protein assembly protein CIAO1
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- NSFL1 cofactor p47
- Anamorsin
- FAD-dependent oxidoreductase domain-containing protein 1
- NADPH-dependent diflavin oxidoreductase 1
- Cytoplasmic aconitate hydratase
- Transforming protein RhoA
Sequence:
MEAAAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDREQSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPYQPLGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDATPACLP
Protein: protein-lysine 6-oxidase (EC 1.4.3.13) (Q2PS19)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MLHVLLMSLWVLGSVTGQSQSQPDDTNPWRQMIQWENNGRVYSLLNSGAEYVPARNQERDRNHRVLLADAPNRRSQGGNVRRQAPSRGSSETVRGQARHPFGFGQVPENWRQQQGAVGRSETSRFQSQTGSRYRPSSGASSSASSSYPQYPIPQQPPFGAPYDQVSDRSYEPPFLGTGYSAGTGGGLGGGGYGGYSTGSFGGGNPANDDRYRFYPPYGQQYQAVPAQPAQPPFSDGLDHRYTHSLFNEDNPAVPNGASSNTGSSFQPAVQSPQYEQFPPYGRPQPQPPFLQPAPRNPLVSNTAENPNINVGSVYRPQQRGLPDLVPDPNYVQASTYVQRAHMYSLRCAAEEKCLASSAYNAETTDYSVRVLLRFPQRVKNQGTADFMPNRPRHTWEWHSCHQHYHSMDEFSHYDLLEVSSGRKVAEGHKASFCLEDTTCDFGHLKRYACTAHTQGLSPGCFDTYNADIDCQWIDITDVQPGNYILKLQVNPKYLVLESDFTNNIVGCNIHYTGRYAKTTNCKISQS
Protein: Naphthalene 1,2-dioxygenase system, large oxygenase component (EC 1.14.12.12) (ISP NAP) (Naphthalene 1,2-dioxygenase ISP alpha) (Naphthalene 1,2-dioxygenase subunit alpha) (ND subunit alpha) (NDO subunit alpha) (P0A111)
Organism: Pseudomonas sp. (strain C18)
Function: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme.
Interaction partners:
Sequence:
MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTFGPAGFWESDDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAYQAHVSSSNWAEFEHASSTWHTELTKTTDR
Protein: 23.5 kDa heat shock protein, mitochondrial (AtHsp23.5) (Q9FGM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- 17.6 kDa class II heat shock protein
- 17.7 kDa class II heat shock protein
- Heat shock protein 90-1
- Heat shock 70 kDa protein 8
- 22.0 kDa heat shock protein
- Heat shock 70 kDa protein 4
- 17.4 kDa class III heat shock protein
- Chaperone protein ClpB1
- 15.4 kDa class V heat shock protein
- HSP20-like chaperones superfamily protein
Sequence:
MASSSALALRRLLSSSTVAVPRALRAVRPVAASSRLFNTNAARNYEDGVDRNHHSNRHVSRHGGDFFSHILDPFTPTRSLSQMLNFMDQVSEIPLVSATRGMGASGVRRGWNVKEKDDALHLRIDMPGLSREDVKLALEQNTLVIRGEGETEEGEDVSGDGRRFTSRIELPEKVYKTDEIKAEMKNGVLKVVIPKIKEDERNNIRHINVD
Protein: 2mit, isoform B (A0A0B4KFU1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RING-type E3 ubiquitin transferase
Sequence:
MVKIVNQHCDLGLALLLAWTWLTRLVVAAHLVDIPTSSRLAAEREEQQLSRQDVGRLSYQSIHRMLRDENEPDSFRGELRYQQKRHKRELELNAPANKLNLTHRDLRTFNSTGGQWKGDFQVITAMDLSSNQLESLSLDNFNQLRQLDLGNNSLEVIPLSLADTNMSLPFVTLDLSCNKFSQISTSFFAQRLPQLKNLNLAHNELLNISRESFYNLLELQTLVLSHNNISDIDYETFLALPNLQYLDLSHNRLSGSAIRALQGIPDLVSLSIAYNPDVGVAMQEFVASWSLKELDASGTGLCQVPAALAQSVRTLKLSDNWLKAINCGDMDSYPLLQYLDLSHSRIAQVEDDALGRLELLESLFLDRNLLMRVPSSLPPSLEHLFLQHNQIMELPPQAFVGLVNLQTLDLSNNRLIFLPPLSLPKLLTLNLESSGVESVSQSIVHTLPQLRDLLLEDNPIKCSDLLGIAEWASPCRSVDAGQSNGASVSGRVDLKTEYLQFHNFYENFSSRECGIRKPENDTKPPSCSLTRASATLTTTPRSMSKVEKSQEAQATATSVEVAAATAATSEKTGIQATSAAQSTAAATTAEREAIATATSSDTTATPTLAAAAAIQSAGNIPAQLTTKTLRPTETTSLAQLQRRQQMPGMPAKTTETPAKNLPSLAQTKATTALPILATRDAATATTEINSDKPTNISGATKTVATSAAEIATPPAIEVPQTILAGKKSDKMPADKAHETLLKYPTRDTSGQVATTPHKHATLQLHVKDRHLIGTPLLMHKGDVLLVDAEQLLLPGTATVADADSEVLDPSQQHQSAEQEKHQSATDKRQADAINGDTKSPAKGHKKKPSLSIKKMTYSTKHAAKTVEDMAATSKTPQHQHSSVNTPKEAAPEELSTFAQLKAYVELKSESKPEHLMDQREENHHNLTGNHPGVMLLVACVLFIVLLAGLAHVYRCELPWQRSNRSGQLRPHHQRHLNETDDAHSFLHYQGSVNSNGGDPARLQKWHHSTRREAPYSSPLHNLQARELQQQRCQQFYSSSLADKSSSTSSSSSGSSRSSLHSPSRDDSYYIEMAPSSPPAANLPSLPMELLGSRSNALGCRTDRVAATDLGGTTEAVPSSAAAIKSVSSRLMTPSSRRLNIWXQTVFGQRQYAPFQ
Protein: Gametocyte erythrocyte cytosolic protein (Q8I4Q6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Early gametocyte enriched phosphoprotein EGXP
Sequence:
MLLKTSLKNICFLLCVVAFVYNNVGRKRVLSFNINNVYSRILSDLEERESESYNNNSNLKYNDSEFKYSFGYYNDDTSGMSTFNGKDIISYLEEKNDNVLDDYNEDDNSPDMDTDDPVESYYDLLNVDKYGDLSELKNNFYNLSLKYYPKMKNGKLLELNKKFEELSEAYQILSYKIRKEIYDNEGISGIEKMNIIHPLLYFNGIFIFDMMYQYIGTTEIGYIIKIFLENNISSENIPSFREEMNENIMEYQIKREEELTELLKKRLDLHMDNDEQWKNVMENEINLLSNKSFSNFILESIGWTYQNVANIYLEEIENVGKIYRGIYMFQANERINKNEEMFDNSRNHIHSLINSFYPYNEQINPFLKRAQYNRTNVECITSNRENKMNSEYDALYNENVNNISDKVKYNLLNDLLISILYINVYDIEETVRNIAEVVLRDNDVNVNTRSKRAHRMRLLGSMILQKINV
Protein: Sulfotransferase 1E1 (ST1E1) (EC 2.8.2.4) (Estrogen sulfotransferase, isoform 1) (EST-1) (Estrogen sulfotransferase, isoform 6) (EST-6) (Estrone sulfotransferase) (Sulfotransferase, estrogen-preferring) (P52844)
Organism: Rattus norvegicus (Rat)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. Is a key enzyme in estrogen homeostasis, the sulfation of estrogens leads to their inactivation. Also sulfates dehydroepiandrosterone (DHEA), pregnenolone, (24S)-hydroxycholesterol and xenobiotic compounds like ethinylestradiol, equalenin, diethyl stilbesterol and 1-naphthol at significantly lower efficiency. Does not sulfonate cortisol, testosterone and dopamine. May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49887}.
Interaction partners:
Sequence:
METSMPEYYEVFGDFHGVLMDKLFTKYWEDVETFSARPDDLLVVTYPKSGSTWIGEIVDMIYKEGDVEKCKEDAIFNRIPYLECRNEDLINGIKQLKEKESPRIVKTHLPAKLLPASFWEKNCKIIYLCRNAKDVVVSYYYFFLIIKSYPNPKSFSEFVEKFMEGQVPYGSWYDHVKSWWEKSKNSRVLFMFYEDMKEDIRREVVKLIEFLERDPLAELVDKIIQHTSFQEMKNNPCTNYSMLPETMIDLKVSPFMRKGIVGDWRNHFPEALRERFEEHYQRHMKDCPVKFRAEL
Protein: Putative pectate lyase 11 (EC 4.2.2.2) (Q9LTZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 2-oxoglutarate
- Uncharacterized membrane protein At3g27390
- At1g64385
- Pectin acetylesterase 12
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- microtubule-severing ATPase
- L-type lectin-domain containing receptor kinase IX.2
- Endoglucanase 6
- Pectin lyase-like superfamily protein
- Dof zinc finger protein DOF5.7
Sequence:
MVSYSNNHFAYAFLLLLTIGNTLAFSSSLPDHVQDPNLVVDDVNRSVFNASRRSLAYLSCRTGNPIDDCWRCDPNWETNRQRLADCAIGFGKNAIGGRKGRIYVVTDPANDDPVNPRPGTLRYAVTQEEPLWIIFKRDMVIRLKKELIITSFKTIDGRGSSVHITDGPCLKIHYATNIIIHGINIHDCKPGSGGMIKDGPHHTGWWMQSDGDAVAIFGGKHVWIDHCSLSNCDDGLIDAIHGSTAITISNNHMTHHDKVMLLGHSDSYTQDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSASPTIYSQGNRFLAPNTRFNKEVTKHEDAPESKWRDWNWRSEGDMLLNGAYFRESGAEAPSTYARASSLSARPSSLVGSITTTAGTLSCRRGRRC
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (Q7KUU5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIFTIAERSFKILELPTTPTLLLRRQSHNYGYDYISPTHIELSREATRLVIRRLQRTVLRLIRDPDFIMSAEANPEMDKEHHESPFAANRKAGASGAGKQDSNCRTCNDFKSWSKQQRLISNVQSAKVKHMAAAEKLTVNAAEDPLPRDDCPLDKVRLGISTWGLLHTMAAFYSDNPTDTEKRDMKTFFEVLSRLYPCEFCAKDFRTDLDVNPINVNSQKELALWLCKFHNRVNDKLGKPLFDCTKVNERWRDGWLDGSCD
Protein: Transcriptional coregulator SSA1 (J9VZ70)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Transcriptional coregulator that functions together with transcription factor HSF1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5KKP4}.
Interaction partners:
Sequence:
MVKAVGIDLGTTYSCVAVWQNDRVEIIANDQGNRTTPSYVAFNDSERLIGDAAKNQVAMNPYNTVFDAKRLIGRKFEDAEVQADMKHWPFKVIDRSGKPAIQVEYRGEEKIFTPEEISSMVLIKMKETAEAYLGGTVSKAVVTVPAYFNDSQRQATKDAGAIAGLDVLRIINEPTAAAIAYGLDKKSEGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFKRKNKKDLSSNARALRRLRTACERAKRTLSSAAQTSIEIDSLFDGIDFYTSITRARFEELCQDLFRSTMDPVEKVLRDSKIDKSSVNEIVLVGGSTRIPKIQKLVSDMFSGREPNRSINPDEAVAYGAAVQAAILTGDTSEATQDLLLLDVAPLSMGIETAGGIMTPLIKRNTTVPTKKSEVFSTYSDNQPGVLIQVFEGERAKTKDCNLLGKFDLSGIPPAPRGVPQIEVSFDVDANGILNVNAADKSTGKSNKITITNDKGRLSKEEIERMLAEAEKFKAEDEAAAATVQAKNGLESYAYSLKTTLSDNQDKFDSADHETLSKKVDEVISSLDTMQSASKEEFEGLQKELEAVANPIMTKFYGAQGGAPGGAPGGFPGAGGAGGAPAHEEGPSVEEVD
Protein: Immunoglobulin lambda variable 1-47 (Ig lambda chain V-I region HA) (Ig lambda chain V-I region WAH) (P01700)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. 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.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAGFPLLLTLLTHCAGSWAQSVLTQPPSASGTPGQRVTISCSGSSSNIGSNYVYWYQQLPGTAPKLLIYSNNQRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCAAWDDSLSG
Protein: Vacuolar protein sorting-associated protein 4 (DOA4-independent degradation protein 6) (Protein END13) (Vacuolar protein-targeting protein 10) (P52917)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex.
Subcellular location: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 20
- DOA4-independent degradation protein 4
- Vacuolar protein sorting-associated protein VTA1
- Vacuolar-sorting protein SNF7
- Vacuolar protein-sorting-associated protein 46
- Vacuolar protein-sorting-associated protein 24
- Vacuolar-sorting protein BRO1
- Vacuolar protein sorting-associated protein IST1
- Vacuolar protein-sorting-associated protein 60
- VPS4-associated protein 1
Sequence:
MSTGDFLTKGIELVQKAIDLDTATQYEEAYTAYYNGLDYLMLALKYEKNPKSKDLIRAKFTEYLNRAEQLKKHLESEEANAAKKSPSAGSGSNGGNKKISQEEGEDNGGEDNKKLRGALSSAILSEKPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFKGNRKPTSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDALTGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSAIRRRFERRIYIPLPDLAARTTMFEINVGDTPCVLTKEDYRTLGAMTEGYSGSDIAVVVKDALMQPIRKIQSATHFKDVSTEDDETRKLTPCSPGDDGAIEMSWTDIEADELKEPDLTIKDFLKAIKSTRPTVNEDDLLKQEQFTRDFGQEGN
Protein: Fumagillin beta-trans-bergamotene synthase af520 (EC 4.2.3.211) ((+)-exo-beta-bergamotene synthase) (Fumagillin biosynthesis terpene cyclase) (Fma-TC) (M4VQY9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Beta-trans-bergamotene synthase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The initial oxidation of beta-trans-bergamotene by the multifunctional cytochrome P450 monooxygenase af510 involves C-H hydroxylation at the bridgehead C5 position to yield 5R-hydroxyl-beta-trans-bergamotene. Subsequently, a four electron oxidation initiated at C-9 coupled to cleavage of the cyclobutane C5-C8 bond of the bicyclo[3.1.1] core yields the epoxyketone intermediate 5-keto-cordycol. An additional epoxidation reaction also catalyzed by af510 then furnishes the characteristic bisepoxide ketone 5-keto-demethoxyfumagillol. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDRVLSLGKLPISFLKTLYLFSKSDIPAATLPSMAVALVLAAPCSFHLIIKGFLWNQLHLLTFQVKNQIDGIDEDSIAKPHRPLPSGRITPGQATLLYRVLFFLMWVAAVYTNTISCTLVYSIAIVVYNEGGLAAIPVVKNLIGAIGLGCYCWGTTIIFDGGKELHGLKAVAVLMIVGIFATTGHAQDFRDRTADATRGRKTIPLLLSQPVARWSLATITAAWTIGLIALWKPPAIVTLAYVAASLRCLDGFLSSYDEKDDYVSYCWYGFWLLGSNILPIFPRLRGELP
Protein: Vomeronasal 2, receptor 120 (A0A3Q4EG79)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLIFVSVLLFLNFPVASCEPINPGCSLGMADAIFQDGDVLVDCHFVLLTVSIALQKIFHFLRFHLSFPMFIYRIHPNKYQYVIALNFAIEEINKNIHLLPNISLGYDMYSIVQYQATILEHSIRFLTGLKEAIPNYTCRKESKLIAVVTGTSWEFPSRISTILGLYKYPQNPLGLFEIYGIVFFTSLHIFFSHQLTFGPFDPMLSDHVKFPFIYQMAPEDTSLALGMVSLMVHFSWTWVGLIITENEKGIKFLSDLKREMKKNSVCAAFVQMLSLKYRYNWNDLLSTDPAIMGEMVKVFIVFADIDSTLVVIFKASGQVDPWRVWVTTSQWDIASSVRHFILDSFHGTLIFSQHHPEISAFKDFIQTVNPSKYPDDIFLSHIWKMYLNCPFSRVYCKTLKTCSSNGSLALLPWHRFDMDMSEESYHIYNAVYAVAHSLHEMLQEHADVQPVKSRKRLVFSPCRLHPFLKNIQFNNPSGDKVDLSHTGKLETKYDIFNFWNFPQGLGLKVKVGTFSSFLPRNKQFSLSDGMIEWGTKDKQTPLSVCSTSCAPGLMKSPQEGKASCCFDCHPCLENEISNETDSIQCIKCPDDQYANTEQTHCIPKAVTFLAYEDPLGMALACMALCFSALTALVLGVFVKHHETPIVKANNRTLSYILLISLILCFLCSLPFIGLPNMATCILQQMSFGVVFTIAVSTVLAKTVTVVLAFRSTVPGRRMRWILVSPNLIIPICTLIQMVLCAIWLGASAPFVDINAHNERGHITIMCNKGSATAFYCVLGYLGFLAMGTLTVAFWARNLPDIFNEAKFLTFSMLVFCSVWVTFLPVYHSTKGKVMVAVEVFSILASSAGLLGCIFVPKCYIILIRPKNGSFKGLRGTRVCK
Protein: Erythrocyte membrane protein band 4.1-like 3 (A0A8I5ZZJ7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTTESGSDSESKPDQEAEPQEAAGPQEQAGAQAAPEPAGGNVEEQPGLEQFPEAAAHSTPVKREVSDKDRDFAAAAAKQLEYQQFEDDKLSQKSSSSKLSRSPLKIVKRPKSMQCKVTLLDGSEYGCDVDKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQIRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGNDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLLPEAPPKKFLTLGSKFRYSGRTQAQTRRASALIDRPAPYFERSSSKRYTMSRSLDGASVNENHEIYMKDSMSAAEVGTGQYATTKVISQTNLITTVTPEKKAEEEHVEEEDRRKKAEEATPVAALRHEGKTDSERTDTAADGETSATEELDKTQDELVKHQTNISELKRTFLETSTETALTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEEKLETKTETIETEVEPTPHPQPLSTEKVLQETVLVEERHVMNVHASGDASHTARDDVDATESAPADRHSGNGKEGSSVTEAAKEQRGEEADKSAPEQEQPATVSQEEDQVSAIHSSEGLEQKSHFESSTVKVESISVGSVSPGGVKLETSTKEVPVVHTETKTITYESSQVDPGADLEPGVLMSAQTITSETTSTTTTTHITKTVKGGISETRIEKRIVITGDADIDHDQE
Protein: Transmembrane 9 superfamily member 8 (Endomembrane protein 1) (Transmembrane nine protein 8) (AtTMN8) (F4KIB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:P32802}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q940G0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein trichome birefringence-like 13
- REF/SRPP-like protein At1g67360
- Carbohydrate-binding X8 domain-containing protein
- Alpha/beta-Hydrolases superfamily protein
- REF/SRPP-like protein At3g05500
- Seipin-2
- Voltage-dependent L-type calcium channel subunit
- Seipin-1
- COBRA-like protein 7
- Arabinosyltransferase RRA3
Sequence:
MAMEFLRSSRRILESSGCAIALIFLLFIHGAHSFYLPGVAPQDFEKGDELKVKVNKLTSIKTQLPYSYYSLPFCRPSKIVDSTENLGEVLRGDRIENAPYSFKMREAQMCNILGRVTLDAKTAKAFKEKIDDEYRVNMILDNLPLVVPIERVDQGSPSVVYQLGYHVGLKGQYEGSKEQKFFMHNHLAFTVRYHRDIQTDAARIVGFEVKPYSVKHEYEGEWSEKTRLTTCDPHTKRLVVSSATPQEVEQKKEIIFTYDVDFQESEVKWASRWDTYLLMSDNQIHWFSIVNSLMIVLFLSGMVAMIMLRTLYRDISRYNELETQEEAQEETGWKLVHGDVFRLPTNSDLLCVYVGTGVQCLGMVFVTMIFAMLGFLSPSNRGGLMTAMLLLWVFMGLFAGYASSRLYKMFKGTEWKRIAFRTAFLFPAVVSAIFFVLNALIWGQKSSGAVPFGTMFALIFLWFGISVPLVFVGGYIGFKKPAADDPVKTNKIPRQIPEQAWYMNPVFSILIGGILPFGAVFIELFFILTSIWLNQFYYIFGFLFLVFVILIVTCAEITVVLCYFQLCSEDYLWWWRSYLTSGSSALYLFLYATFYFFTKLQITKLVSAMLYFGYMLIASYAFFVLTGTIGFYACLWFTRLIYSSVKID
Protein: L-asparaginase 2-4 (EC 3.5.1.1) (L-asparaginase II) (L-asparagine amidohydrolase II) (ASP II) (P0CX79)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Secreted. Periplasm.
Interaction partners:
Sequence:
MRSLNTLLLSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTDPSEIPEVIILYSYQGLNPELIVKAVKDLGAKGIVLAGSGAGSWTATGSIVNEQLYEEYGIPIVHSRRTADGTVPPDDAPEYAIGSGYLNPQKSRILLQLCLYSGYGMDQIRSVFSGVYGG
Protein: Uncharacterized protein C8F11.08c (Q9UT29)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiotic chromosome segregation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Enhancer of rudimentary homolog 1
Sequence:
MGFATILYSIWVVLSSFVILSAYQLEVRKFLVKLLSKIVIGASESNVASFFAFVSEKSLEAASVKFVATIIAERMGAQFSSFYDKIFFVDMLGLGSLFALAAVNVLAARKLESELPASLEPSIGNRDQQKNSSLAKCFSRLFINDLHGTTVKRYPYISYLPNWLLAKNNAERLVYKSHLLLNAYSPPKSASASSVIVWVCGAKKSESIIIPYLSSLGFFVVVPNYAQPPKFPLSDAVEFVSLCVDWIVENAIYYDADPERIFFLGEDTGASVALESLKHIRPNSVKGIFALCPRSIQNLVWTNQSTIPMMTLHAGDVNPVSDSNDRESSEKASLIKNFVVPGAVPYYYEFTSPRTISTATFIARWFFLVEDNKKTI
Protein: At1g77770 (Forkhead box protein, putative (DUF1644)) (Q84K51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGKIKKVNQRGHIATPYPSPCCKKEWAGSTCPVCLESPHNAVLLLCSSYHKGCRPYMCATSSRFANCLDQYRKSYGNENSGQPELLCPLCRGQVKGWTVVKDARMHFNSKRRTCMQDNCSFLGNFRKLKKHMKEKHPHACPRAIDPALETKWKRLERERDRRDVISTIMSSTPGAVVLGDYVIEPHNRGVYDEEDEEEDYSSDDSLSNGILDLESSWQGQSHHIRFLDMESSDFASSSSSPASPSRSLHRLLFPRNQRGGNRGAV
Protein: Core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein (Glycosyltransferase) (Q9C581)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Probable xyloglucan galactosyltransferase GT14
Sequence:
MFSNQFVLFFSLLLCLPFVFFFVAPHVFPSPPGESLIPISDEIDDRSLFIAAAGSTSLSHLSSGNPNPKLKIAFLFLTNSDLHFAPIWDRFFSGHSKSLYNVYVHADPFVNVTRPGNGSVFENAFIANAKRTARASPTLISATRRLLATAFLDDPANTYFAVLSQYCIPLHSFNYVYSSLFESSIFDKSDPDPNPNPRGIRILYRSFMELISDEPRLWKRYTARGRYAMMPEVPFEKFRVGSQFFVMTRRHALLTIKDRILWRKFKLPCYRSDECYPEEHYFPTLLNMKDPDGCTGYTLTRVNWTGTVKGHPYTYKPKEVVPELIQRLRRSNHSSSYFFARKFTPDCLKPLLAIADSVIFRD
Protein: Putative uncharacterized protein YPL276W (P0CF36)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MSKGKVLLVLYEGGKHAEEQEKLLGCIENELGIRNFIEEQGYELVTTIDKDPEPTSTVDRELKDAEIVITTPFFPAYISRNRIAEAPNLKLCVTAGVGSDHVDLEAANERKITVTEVTGSNVVSVAEHVMATILVLIRNYNGGHQ
Protein: Pupal cuticle protein Edg-78E (P27779)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cuticle of the pupa of fruit fly.
Interaction partners:
- Cuticle protein LCP65Ad
- Pupal cuticle protein Edg-84A
- RE71854p
- Cuticular protein 72Eb
Sequence:
MYKYLFCLALIGCACADNINKDAQIRSFQNDATDAEGNYQYAYETSNGIQIQEAGNANGARGAVAYVSPEGEHISLTYTADEEGYHPVGDHLPTPPPVPAYVLRALEYIRTHPPAPAQKEQQ
Protein: Steroid receptor RNA activator 1 (Steroid receptor RNA activator protein) (SRAP) (Q9HD15)
Organism: Homo sapiens (Human)
Function: Functional RNA which acts as a transcriptional coactivator that selectively enhances steroid receptor-mediated transactivation ligand-independently through a mechanism involving the modulating N-terminal domain (AF-1) of steroid receptors. Also mediates transcriptional coactivation of steroid receptors ligand-dependently through the steroid-binding domain (AF-2). Enhances cellular proliferation and differentiation and promotes apoptosis in vivo. May play a role in tumorigenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:12565891}. Cytoplasm {ECO:0000269|PubMed:12565891}.
Interaction partners:
- Abl interactor 1
- Actin-binding protein WASF2
- Abl interactor 2
- Nck-associated protein 1
- Protein BRICK1
- Nck-associated protein 1-like
- Retinoic acid receptor gamma
- Probable ATP-dependent RNA helicase DDX5
- Probable ATP-dependent RNA helicase DDX17
- Deleted in malignant brain tumors 1 protein
Sequence:
MAELYVKPGNKERGWNDPPQFSYGLQTQAGGPRRSLLTKRVAAPQDGSPRVPASETSPGPPPMGPPPPSSKAPRSPPVGSGPASGVEPTSFPVESEAVMEDVLRPLEQALEDCRGHTRKQVCDDISRRLALLQEQWAGGKLSIPVKKRMALLVQELSSHRWDAADDIHRSLMVDHVTEVSQWMVGVKRLIAEKRSLFSEEAANEEKSAATAEKNHTIPGFQQAS