wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisomal adenine nucleotide carrier 2 (Q8VZS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Peroxisomal adenine nucleotide transporter catalyzing the counterexchange of ATP with AMP. ATP is needed by reactions that generate acyl-CoA for peroxisomal fatty acid beta-oxidation during postgerminative growth. Required for the beta-oxidation reactions involved in auxin biosynthesis and for the conversion of seed-reserved triacylglycerols into sucrose that is necessary for growth before the onset of photosynthesis.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:19073762, ECO:0000269|PubMed:19073763}; Multi-pass membrane protein {ECO:0000269|PubMed:19073762, ECO:0000269|PubMed:19073763}.
Interaction partners:
- ABC transporter D family member 1
- Peroxisome biogenesis protein 19-1
- Peroxisome biogenesis protein 19-2
- Peroxisome biogenesis protein 16
- Peroxisome biogenesis protein 12
- Dihydropyrimidinase
- Allantoinase
- Mitochondrial adenine nucleotide transporter ADNT1
Sequence:
MGVDLDLESISEATSGAIGSLLSTTILYPLDTCKSKFQAEIRVRGQQKYRYLSDVFWEAISSGNVLSLYQGLGTKNLQSFISSFIYFYSYSYFKRLHSQRIGSKSIGTKANLLIAAAAGACTSVLTQPLDTASSRMQTSEFGKSKGLWKTLTDGSWGNAFDGLGISLLLTSNPAIQYTVFDQLKQNLLEKGKAKSNKDSSPVVLSAFMAFVLGAVSKSAATVITYPAIRCKVMIQAADDSKENEAKKPRKRIRKTIPGVVYAIWKKEGILGFFKGLQAQILKTVLSSALLLMIKEKITATTWILILAIRTLFVTKARLKSP
Protein: DNA-directed RNA polymerase II subunit RPB1 (EC 2.7.7.6) (3'-5' exoribonuclease) (EC 3.1.13.-) (RNA-directed RNA polymerase II subunit RPB1) (EC 2.7.7.48) (G3MZY8)
Organism: Bos taurus (Bovine)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P24928}. Cytoplasm {ECO:0000250|UniProtKB:P24928}. Chromosome {ECO:0000250|UniProtKB:P24928}. Note=Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear. Co-localizes with kinase SRPK2 and helicase DDX23 at chromatin loci where unscheduled R-loops form. {ECO:0000250|UniProtKB:P24928}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB4
- Transcription elongation factor SPT5
- Transcription initiation factor IIB
Sequence:
MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDDEN
Protein: Isoepoxydon dehydrogenase patN (IDH) (EC 1.1.1.-) (Patulin biosynthesis cluster protein N) (A0A075TRB3)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: Isoepoxydon dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatN catalyzes the conversion of isoepoxydon into phyllostine. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
Interaction partners:
Sequence:
MVLTTGLKGAHVLITGGTRGMGEAMVHKFLQEEANVSYCARTVTNTEYDDFYSTLAEGNTARAVGTAFDVASKDSLVKWVESSAERLGRIDVIIANASPMHMEGETEHWESSFAIDVMGFVELVKAATPYLEKSPQASIIVQSSFMGREFYRSPPAAYGPCKAAQLQHVQELSHFLGPKGIRVNAISPGPVLCKGGPWELYSKINPEWVEEQRLKIPLKRLGGPTEVANVAVFLASPLASFVSGTNMLVDGGIHVGTQF
Protein: Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (PDZ domain-containing protein NHERF-2) (Sodium-hydrogen exchanger regulatory factor 2) (Solute carrier family 9 isoform A3 regulatory factor 2) (Q8SQG9)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus (By similarity).
Subcellular location: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Apical cell membrane {ECO:0000250}. Note=Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes. Nuclear, in a punctate pattern (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MAAPEPLRPRLCRLVRGEQGYGFHLHGEKGRRGQFIRRVEPGSPAEAAALRAGDRLVEVNGVNVEGETHHQVVQRIKAVEGETRLLVVDKETDEELRRRQLTCTEDMAQRGLPPAHDPWEPKPDWARAGSLSSDAGQKDVNGPPRELRPRLCHLRKGPQGYGFNLHSDKSRPGQYIRSVDPGSPAAHSGLCAQDRLIEVNGQNVEGLRHAEVVARIKAKEDEARLLLVDPETDEYFKRLRVTPTEEHVEGPLPSPITNGTSPAQDASAWKRDPFQESGLHLSPTAAEAKEKARATRVNKRAPQMDWNRKREIFSNF
Protein: Uncharacterized protein C19G7.17 (O42965)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Protein transport protein sec61 subunit beta
- Probable protein transport protein Sec61 subunit gamma
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL29
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
- Uncharacterized protein C553.06
- Protein transport protein sec61 subunit alpha
Sequence:
MGGARFINFIKPLSSLLPEVEGPKTHLELVEKLGWMAGCVVVYQILSIIPVYGAEKTDTLDPINNFRVLDGSSASGLMITGLAPIYLSSFLLQILASKKKIAVNFNLIIDRVLFQNAQKVVSALLYLILAVTYVSSGYYGSFSDLGIFRFIMLILQIFLPGIVCIYLCEIIEKGHGLGSGPVLLLGSHILGNIMWDVLSLHRYPVNESGDSQYQGALVGFAFNLFSFKNKFSSLRSILFRSEGLSFVQFLVCIAVFATFMYTLNIRIDVPIRSSRVRGVRQNFPLKLLYTSVIPLIYFYSILSHLLVFAYALYSLCPNSLITRLLVQYSPIDTFAEHKLQLVGGLVYFLYPPLGLSEALLHPVHTVIYTITLICITIYFSLLWMNATAGGPRDVLLFFKENQLVIAGYREATMLKELEKIIPIAAKLSAFFVSILSVIAGIFASTFGVGVLIASALVYASFEMIVGANTSLGNGN
Protein: Guided entry of tail-anchored proteins factor CAMLG (Calcium signal-modulating cyclophilin ligand) (P49070)
Organism: Mus musculus (Mouse)
Function: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum (By similarity). Together with GET1/WRB, acts as a membrane receptor for soluble GET3/TRC40, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol (By similarity). Required for the stability of GET1 (By similarity). Stimulates calcium signaling in T cells through its involvement in elevation of intracellular calcium (By similarity). Essential for the survival of peripheral follicular B cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49069}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 13B
- Guided entry of tail-anchored proteins factor 1
- ATPase GET3
- Tumor necrosis factor receptor superfamily member 13C
- Peptidyl-prolyl cis-trans isomerase B
- Tumor necrosis factor ligand superfamily member 13B
Sequence:
MEPVPAATDGGERPATPSGLSASQRRAELRRRKLLMNSEQRINRIMGFHRPGSGSEEENQTKSKPQDSDKLNSLSIPSVSKRVVLGDSVDGGGADQLGGVAEVRGTQLGDKLDSFIKAPECSSKDGAELRQRTRGDLTADPAQRASHHGLEQYLSRFEEAMKLRKQLISEKPSQEDGSTAEEFDSFRIFRLVGCALLALGVRAFVCKYLSIFAPFLTLQLAYMGLYKYFPKGEKKVKTTVLTAALLLSGIPAEVINRSMDTYSKMGEVFTDLCVYFFTFIFCHELLDYWGPEVP
Protein: Probable pectate lyase 3 (EC 4.2.2.2) (Pectate lyase A2) (Q9M9S2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g55560
- Probable pectinesterase/pectinesterase inhibitor 21
- Putative pectinesterase/pectinesterase inhibitor 28
- RING-type E3 ubiquitin transferase
- Probable pectinesterase 67
- Probable pectinesterase/pectinesterase inhibitor 13
- Probable pectinesterase/pectinesterase inhibitor 58
- Pectinesterase 31
- Exopolygalacturonase clone GBGE184
- Probable pectinesterase 49
Sequence:
MAAAFLNLGGYVFVFFSSFLAIVAPQVRGNVAVFDSYWTQRQSDALKQTIGSYDPHPLNVTNHFNYHVNIAVDASESRNDTRRELTQVRSGRKTHKSSGKCLAYNPIDNCWRCDRNWANNRKKLADCVLGFGRRTTGGKDGPIYVVKDASDNDLINPKPGTLRHAVTRDGPLWIIFARSMIIKLQQELMITSDKTIDGRGARVYIMEGAGLTLQFVNNVIIHNIYVKHIVPGNGGLIRDSEAHIGLRTKSDGDGISLFGATNIWIDHVSMTRCADGMIDAIDGSTAVTISNSHFTDHQEVMLFGARDEHVIDKKMQITVAFNHFGKRLEQRMPRCRYGTIHVVNNDYTHWEMYAIGGNMNPTIISQGNRFIAPPNEEAKQITKREYTPYGEWKSWNWQSEGDYFLNGAYFVQSGKANAWSSKPKTPLPNKFTIRPKPGTMVRKLTMDAGVLGCKLGEAC
Protein: Phosphatidic acid phosphatase alpha, putative (EC 3.1.3.4) (Q388M9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Phosphatidic acid phosphatase protein, putative
- 3-dehydrosphinganine reductase
- Phosphatidic acid phosphatase, putative
- Phosphatidate cytidylyltransferase
- Ethanolaminephosphotransferase, putative
- Acyltransferase
- Lipase-like protein, putative
- Phosphatidylinositol:ceramide inositolphosphotransferase
- Lipin, putative
- Phosphatidylcholine:ceramide cholinephosphotransferase 3
Sequence:
MPRPCILPQLRRLRDNRHHSGDVVAGSVIGMLSGLLAVAIFFRLGKGKAFLVPRRLDFVRRHGGQVVSDITK
Protein: Fibroblast growth factor 17 (FGF-17) (O60258)
Organism: Homo sapiens (Human)
Function: Plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. Required for normal brain development.
Subcellular location: Secreted.
Interaction partners:
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Fibroblast growth factor receptor 3
- Fibroblast growth factor 2
- Fibroblast growth factor 1
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Fibroblast growth factor-binding protein 1
Sequence:
MGAARLLPNLTLCLQLLILCCQTQGENHPSPNFNQYVRDQGAMTDQLSRRQIREYQLYSRTSGKHVQVTGRRISATAEDGNKFAKLIVETDTFGSRVRIKGAESEKYICMNKRGKLIGKPSGKSKDCVFTEIVLENNYTAFQNARHEGWFMAFTRQGRPRQASRSRQNQREAHFIKRLYQGQLPFPNHAEKQKQFEFVGSAPTRRTKRTRRPQPLT
Protein: Augmin complex subunit dgt5 (Dim gamma-tubulin 5) (Q7K4B4)
Organism: Drosophila melanogaster (Fruit fly)
Function: As part of the augmin complex, plays a role in centrosome-independent generation of spindle microtubules. The complex is required for mitotic spindle assembly through its involvement in localizing gamma-tubulin to spindle microtubules.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17412918, ECO:0000269|PubMed:18443220}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18443220, ECO:0000269|PubMed:24829288}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24829288}. Chromosome, centromere {ECO:0000269|PubMed:24829288}. Note=In mitotic cells, detected on kinetochore microtubules but greatly reduced at the spindle equator where only non-kinetochore microtubules are present (PubMed:18443220). During male meiosis, localizes to kinetochores in a microtubule-independent manner but does not concentrate on spindle microtubules (PubMed:24829288). {ECO:0000269|PubMed:18443220, ECO:0000269|PubMed:24829288}.
Interaction partners:
- Augmin complex subunit dgt2
- Augmin complex subunit msd1
- Augmin complex subunit dgt6
- Augmin complex subunit msd5
- Augmin complex subunit dgt3
- Augmin complex subunit dgt4
- Augmin complex subunit wac
- Grip71
- Kinesin-like protein Klp61F
Sequence:
MAYQEKITEFKNWATNLGCPPTALPTDDALRRIFKSGSSLLLNQLQSRIQPVDYVREVRENLLIAQVARYKDKMVPLASRSFQPPELQRYQKIQELKKHKEKANQQLTEARKEYQKLSAGIKTKNIQTISAENRKQLLESKCNILDLKLESLNKNYDQELKNKIQILGTTPVKLSARNASEAQATRAVEQALKQLETFYGMCDDGNAVNNLAEAKQRLWDQMRSTFADIPNSLLLNVVMKIKEEQLQHIMKLNESRGECTNDKPPLNNYEVKLLKTKADMLGLAAKYFAAQKELELKEERFCQDYSVFVDKLQSKVYRFNGISLGDEENADELISDYLVQYNMRNFNRSQNEFLREQIEQLRLELDAGAKQLENHDLKLGSVKQVYGDINSSINRIQQDMVQLSQIKEKILFSRNMMKNLLDDMQAATQKQNAKSQLMSTKLKVSNMSMLGAESFCLANDSVFSSTKVEFDGNCSAINSTMRRSFDNKTLVPGGAASTTLMAASGATLPSHLLEFNTFLEIPLEKFSCTPRACSFLLSANPLIVEAQELASTVQLAPGYLLTPFGALQEVRKRILWASAIAAHTSELKLNLQPLIVDPHDLRLKASRQHEEIDQLLDNLMAIGVKTQLQLEKAERIYQFLLENPLRRYVPPSKRYNNGSFADYESEFNLYYRMTTNGSSMRAPPN
Protein: Uncharacterized protein (P91246)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein C27D6.3
- RanBD1 domain-containing protein
- Uncharacterized protein
- BAR domain-containing protein
- DNA-binding protein
- Regulator of microtubule dynamics protein 1
- non-specific serine/threonine protein kinase
Sequence:
MADDNVSFTDAGDPTQGAKPQGGSSAMLDLLGALDKKEEKKKKDKKGKKGKKSKGKSKTKKVRKADKFESQNFLFRIEGTIFCAGIVVGLVVLLVFIAVAIFFSVKAGGNMVHYIHPWWGGLEESSAN
Protein: Decapping and exoribonuclease protein 1 (EC 3.6.1.-) (5'-3' exoribonuclease DXO1) (EC 3.1.13.-) (NAD-capped RNA hydrolase DXO1) (DeNADding enzyme DXO1) (EC 3.6.1.-) (Q06349)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs. Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1). Also has 5'-3' exonuclease activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 5'-3' exoribonuclease 2
- Exosome complex component RRP42
- 5'-3' exoribonuclease 1
- mRNA cap guanine-N
- Decapping nuclease RAI1
- m7GpppN-mRNA hydrolase
Sequence:
MSTEQDAVLGLAKDLEGINLLTVPNLERGHQSKLCKEKTTSDSSSSRKPSQQRDNYRKRRPKLICIPYTSFLHTGMHNFLTKPPRDIFHESKEVALFTNGRAYTILRKDLIPNLKESIAELYESSLLEAKKRKVPYLGHDLFANIDEFVPMTISELDSVSPCFSYIENWILDNPGKDFKIGKKFTVVTTRHHIVDLTMHLFNRRNRQTSLIVTYMGAGLLSFCRNVKKDSQMSKEGIYSNDPNMKKICYSGFEFENWVTENSKVADLTGSKCPIFSLVESKLSEEIGLLIRCEMDAFNPVSETNTELKCFAPLSMHNSNHRRKLLKTWVQTGLLPNSDIMIGLRDSHSGQLLDIQWYSRDLLCKKFNHPGLPTNKKELNYNAQIAVEWCHYCIEAICKLVEANISDYSSTKPESFEIGIDTNNAIVITKLKTTPRNVELFGM
Protein: Protein Abitram (Q581S9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNPVGVACAAAPKPSTFDYFTERYYHQYVVKNCKGVEGNNCRLLVHSNGICVLCLDETHRVVRAAKSSAGAVETNVASVVFGSGRGNSQLSSGSIHVVGKRKKQAAVCQVDTKICIITMSDGTVYHIPACVDGFVLELNSALQQHPNLLLDAPTAEGYIALISPNYSKVKFSEFTKLSAPTGGDVVEEEEEPEGLHK
Protein: E3 ubiquitin-protein ligase RMA3 (EC 2.3.2.27) (Protein RING membrane-anchor 3) (RING-type E3 ubiquitin transferase RMA3) (Q8GUK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19224217}; Single-pass type IV membrane protein {ECO:0000269|PubMed:19224217}.
Interaction partners:
- At2g35585
- At1g31940/F5M6.6
- Ubiquitin-like superfamily protein
- Chaperone DnaJ-domain superfamily protein
- Glucose-methanol-choline
- AT3g56060/F18O21_20
- At5g09540
- Ubiquitin-conjugating enzyme E2 28
- At5g64360
- Glucose-methanol-choline
Sequence:
MEGNFFIRSDAQRAHDNGFIAKQKPNLTTAPTAGQANESGCFDCNICLDTAHDPVVTLCGHLFCWPCIYKWLHVQLSSVSVDQHQNNCPVCKSNITITSLVPLYGRGMSSPSSTFGSKKQDALSTDIPRRPAPSALRNPITSASSLNPSLQHQTLSPSFHNHQYSPRGFTTTESTDLANAVMMSFLYPVIGMFGDLVYTRIFGTFTNTIAQPYQSQRMMQREKSLNRVSIFFLCCIILCLLLF
Protein: Small ribosomal subunit protein uS3 (30S ribosomal protein S3) (P0A7V3)
Organism: Escherichia coli (strain K12)
Function: Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (By similarity).
Interaction partners:
- Small ribosomal subunit protein uS13
- Elongation factor Tu 1
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL14
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL30
- GTP pyrophosphokinase
- Small ribosomal subunit protein uS7
Sequence:
MGQKVHPNGIRLGIVKPWNSTWFANTKEFADNLDSDFKVRQYLTKELAKASVSRIVIERPAKSIRVTIHTARPGIVIGKKGEDVEKLRKVVADIAGVPAQINIAEVRKPELDAKLVADSITSQLERRVMFRRAMKRAVQNAMRLGAKGIKVEVSGRLGGAEIARTEWYREGRVPLHTLRADIDYNTSEAHTTYGVIGVKVWIFKGEILGGMAAVEQPEKPAAQPKKQQRKGRK
Protein: Nuclear pore complex protein An-Nup170 (Eurofung) (C8V1X8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear pore complex protein AN-Nup192
- Nucleoporin NSP1
- Nuclear pore complex protein An-Nic96
- Peptidase S59 domain-containing protein
- Nuclear pore complex protein An-Nup57
- WD40 protein related to S. cerevisiae SEH1
- Nuclear pore complex protein
- Nuclear pore complex protein An-Nup133
- Nuclear pore complex protein An-Nup159
- Protein transport protein sec13
Sequence:
MSYPSLPPVTPQRPLPGAFFQTPAPGNALNPPQSNSAQQTAQPPSDAGQPVLPRLPPSIKPAPQNLNTEERAARTINDTLTQEARYPDLDSYLSQGFSSDYDIPVSSTWAPFQKVRMYNIPDQIFDQYNLAQVSTSMGLLAELNHAWVAIDNALYLWDYTHTNPQLVGFEDQPNSINAVKLAKPRPGVFLPSITHLLVISTTAEVLLLGMKCEPTPGGSYQVTLYQTGMSTSVRGLDIHIIASSDATGRIFFAGSSDNDVYELTYQQEEKWFQGRCSKINHTSSRISQLAPSLSFTQRPSEQVVQMVMDDSRRLLYTLSSASTIRVFHLRADGSVALAITKPALDIYANIGHIIASNQALNSKVRIVSISPIPAAEASRYHLMATTATGYRIYLSATGSYSWSPAPNGANAPTSMQAHYVKTPPFDSSAPAYQGQSRFQPSLAATRVPIHTLDPTSSSVRYPPGYFFCFTCQDSTQKSDTLFISAPDSGRVARSQENVIPGKAAETGIWLSLGSRMEDIGLSSPTTPASATPSGFGNELAVQFENPSAEIAILTNTGIHVFRRRRLVDIFAALVRNGGSGGEEGLEGEIKNFIRTYGRSETLATALAVACGQGVEVSTDSRLSKINDPDVLEFARKVFIDYGGRPTLNENAVADNSTPAIDTVVPSPRHAGIALYISRLLRSVWKKEVAVVGGGPGGAQTISPSFPRAKLLAIQHDLSALQEFFKTNKSFIEGLSGPEALARVSTKQEELELQAEHRALHSLVQLVSHTIEGISFVTVLFDEKVEEIVALLPEESKQRFLKLTYEELFSTTKGHDIAKELVKGIVNRNIAKGANVETVADALRRRCGSFCSSEDVVIFKAQELLKRATEAGFNSELGRNLLNESLHLFQQVSENLPMDYLVPAVESYISNQFFAGAIQLALNVAGRSDKANLGLGWMMDGQPSSCYDLIFKVVLAVDNLAAQDPGVVDGQLTTIAKRKNEAYGIIAVSEDQVFLTSLYDWYLEQGWSDRLLRSESPYVVEYLKRKSTDDISHADLLWRYYTQSERFFEAAQVQLELAQSSFVLPLSRRIEYLGQARANASTFTQDVGRQARQRLLQQVSNLIDVANVQDDLLQRLKDDTRLDPDAKARAVEEVDGPIMEVSTMFNQYADVASYYDICLQIFYIADYRNPADVRATWQHLLQTLHDEAVARGSAGPQPYEAVIDKLRSLGARLRMSDAVFPIPILLPMLERYALEHQRNVGPPTWVIDTFFDLGVPHETIYSVLESMYYIDEAPFHGSNRKIIARDLLYTIEHWFHDTVRLGGVVFGSDLIAERIEEMLTLLQQSGISAEQMAVAHELRARINNILR
Protein: Beta-1,4-mannosyltransferase bre-3 (EC 2.4.1.-) (Bacillus thuringiensis toxin-resistant protein 3) (Bt toxin-resistant protein 3) (Q03562)
Organism: Caenorhabditis elegans
Function: Glycosyltransferase with a proposed role in glycosphingolipid biosynthesis. Involved in susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-2, bre-4 and bre-5. Involved in resistance to the nematotoxic C.cinerea galectin Cgl2. Has a role in determining brood size.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12944392}. Note=In punctate structures throughout the cell.
Interaction partners:
- Beta-1,4-N-acetylgalactosaminyltransferase bre-4
- Beta-1,3-galactosyltransferase bre-2
- Beta-1,3-galactosyltransferase bre-5
- Ceramide glucosyltransferase 1
- Alanine--glyoxylate aminotransferase
- Galactoside 2-alpha-L-fucosyltransferase
- Ceramide glucosyltransferase 2
Sequence:
MNCEVKHALHCAVLVAWIVCFAYFCGVFTEPVEGSVPESPVASYGLIWTVCLYLLRFTALLVLPQCLCNLGGLMMFNAFREKVQLKAAPLLSPFVCFRVVTKGNFPLLVKENIDTNMKTCFEAGMENFIFEVVTDKAINLPPNPRVREVVVPTVYKTKSGAKFKARALQYCLEDDVNILQPTDWIVHLDEETLLTTNAICGILNFCEDGKHQFGQGVITYANGDIVNWLTTLSDSFRVADDMGKLRFQFKLFHKPLFGWKGSYVVTQVEAERDVSYDHGMEGSIAEDCFFSMVAMKHGYSFDFIEGEMHEKSPFTMWDFLQQRKRWLQGILLTVHSSKIAVVHKALLALSLYAWATMPLTSLQVFLCPLFPLPRCLPFDFLLSFVGALNLYMYIFGVVKSFSHKYRNSLLRLAMYLAGALMTIPFNILIENAAVLVGMFGRKDQFYIVNKDIQTV
Protein: Neuronal acetylcholine receptor subunit alpha-4 (P09483)
Organism: Rattus norvegicus (Rat)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodium ions.
Subcellular location: Presynaptic cell membrane {ECO:0000269|PubMed:22593584}; Multi-pass membrane protein {ECO:0000269|PubMed:22593584}. Cell membrane {ECO:0000250|UniProtKB:O70174}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit alpha-5
- Neuronal acetylcholine receptor subunit beta-4
- Acetylcholine receptor subunit alpha
- Acetylcholine receptor subunit epsilon
- Acetylcholine receptor subunit beta
- Neuronal acetylcholine receptor subunit alpha-3
- Acetylcholine receptor subunit delta
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-9
Sequence:
MANSGTGAPPPLLLLPLLLLLGTGLLPASSHIETRAHAEERLLKRLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPGDYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFYDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVSMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKVTLCISVLLSLTVFLLLITEIIPSPTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPAWVRRVFLDIVPRLLFMKRPSVVKDNCRRLIESMHKMANAPRFWPEPVGEPGILSDICNQGLSPAPTFCNPTDTAVETQPTCRSPPLEVPDLKTSEVEKASPCPSPGSCPPPKSSSGAPMLIKARSLSVQHVPSSQEAAEDGIRCRSRSIQYCVSQDGAASLADSKPTSSPTSLKARPSQLPVSDQASPCKCTCKEPSPVSPVTVLKAGGTKAPPQHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAAC