wanglab/gogpt-training-data huggingface dataset:
Protein: Steroidogenic factor 1 (SF-1) (STF-1) (hSF-1) (Adrenal 4-binding protein) (Fushi tarazu factor homolog 1) (Nuclear receptor subfamily 5 group A member 1) (Steroid hormone receptor Ad4BP) (Q13285)
Organism: Homo sapiens (Human)
Function: Transcriptional activator. Essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. Binds phosphatidylcholine (By similarity). Binds phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:11479297, ECO:0000269|PubMed:27490115}.
Interaction partners:
- Nuclear receptor subfamily 0 group B member 1
- Transcription factor SOX-9
- Sex-determining region Y protein
- Wilms tumor protein
- Steroidogenic acute regulatory protein, mitochondrial
- Transcription factor GATA-4
- Nuclear receptor coactivator 2
- Muellerian-inhibiting factor
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKTQRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKLETGPPMGVPPPPPPAPDYVLPPSLHGPEPKGLAAGPPAGPLGDFGAPALPMAVPGAHGPLAGYLYPAFPGRAIKSEYPEPYASPPQPGLPYGYPEPFSGGPNVPELILQLLQLEPDEDQVRARILGCLQEPTKSRPDQPAAFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVFDHIYRQVQHGKEGSILLVTGQEVELTTVATQAGSLLHSLVLRAQELVLQLLALQLDRQEFVCLKFIILFSLDLKFLNNHILVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAKQT
Protein: Nuclear pore complex protein Nup75 (Nucleoporin Nup85) (A1YK03)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567, ECO:0000256|RuleBase:RU365073}.
Interaction partners:
Sequence:
MSDSGVFAFELGDDLATRCGNTLTGVFVPGSRIALSAYRHVTHSSRDEPTENAGQVPVLIYMAQESTLFDEPVLRSVLAEANATFATLQQLGSRATRAEYVNISRAYRSIVRSCLEKLEQAKKSPEVQTDEARLQRLCDAIVVFYAAECLWHLFEILYIQSNQLVVPQLLDWARFHSPHAEDRATDLLLMGEEASESDDYWSIVKSLIMLGEIDVTRAVLSQNRKAGQTSFKAAEQILKSMPVYQEGYALQKFHSQWEFWHVDTERKIQSGLFATEPDLEQLIRLVAGDSEQWDAGIKESQDFYEYLPGYLLFTKPTCKPFELKIAAAKWLNRWCLLRPEREQCSMNRMVSQLMDHDLRLFIYDAQKLNDTHWFSTHLIDLIHHCGQLKSYFDQNNIDLPALRHSMIYEYGSYLMTSHNMWQLGIDYLDCCKQEGQAAIELLLPRITLRSERQATKLINLARQRGLISVEREICKVLSKRSYDNERYGNALEWAIRSKDVLLVTAVADFILKHYSKTGCMLCPDTIANVGGRMFASPRLVFLSKYFEFYEFYRTRDFLSASELLVNLLESKITPDYFWPSLLIDSMPLLESKDPKIFAKETVAILHHIETDLVPIIERDVSKYGKHHTETVFKDYRVENVDEIMNLLRLACARNLARALIIENTLPVV
Protein: RING-type E3 ubiquitin transferase (cysteine targeting) (EC 2.3.2.36) (Peroxin-2) (C8ZB10)
Organism: Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004585}.
Interaction partners:
Sequence:
MSRVAQLDSIALDKELYGQFWSEFNAAFNTSEHKEEWELALNTVVFMCATRFLPHYGSSCTYGSALSGVAFQCRKRTLYVVTVLAGYVWKKITHIIFNGPHCGNQMMWLKLYKWVNLLYHGCDVTNFLRFLAAEGPNARAFLSPLYRAFNVHSTRLIRDGSAIASEFYSNSVFAGLEYQNRQLLWNALLELFSNTLLTKRGLLTFVKNPPRSRSTTTYKTVCPRCGGFPTNPYQIACCRANYCYVCVVKALEWSMCDACGSSGRLTASPVY
Protein: Protein trichome birefringence-like 3 (Q8LED3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in secondary cell wall cellulose deposition. Required for normal stem development. May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Probable galacturonosyltransferase 12
- Cellulose synthase A catalytic subunit 8
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- COBRA-like protein 4
- Protein REDUCED WALL ACETYLATION 2
- Chitinase-like protein 2
- At5g19870)
- Beta-1,4-xylosyltransferase IRX9
- Glucuronoxylan 4-O-methyltransferase 1
- Cellulose synthase A catalytic subunit 7
Sequence:
MSFLIPNRGVGGTKIPLSIIVLVLCGFMFFILLYTERISLLSSSSSSSSSFFKLKSCPRKDVSSKPKEKIRKERSEILEVLDDRFEFDPEECNVAAGKWVYNSSIEPLYTDRSCPYIDRQFSCMKNGQPETDYLRWEWQPDDCTIPRFSPKLAMNKLRGKRLLFVGDSLQRSQWESFVCLVESIIPEGEKSMKRSQKYFVFKAKEYNATIEFYWAPYIVESNTDIPVISDPKKRIVKVDSVKDRAKFWEGADILVFNTYVWWMSGLRMKALWGSFGNGESGAEALDTQVAYRLGLKTWANWVDSTVDPNKTRVFFTTMSPTHTRSADWGKPNGTKCFNETKPIKDKKFWGTGSNKQMMKVVSSVIKHMTTHVTVINITQLSEYRIDAHTSVYTETGGKILTAEQRADPMHHADCIHWCLPGLPDTWNRILLAHL
Protein: Ubiquitin-ribosomal protein eS31y fusion protein [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31y (40S ribosomal protein S27a-2)] (P59232)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31y]: Cytoplasm {ECO:0000305}.
Interaction partners:
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Protein NBR1 homolog
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS12z
- E3 ubiquitin-protein ligase PRT1
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein eS21z
- Small ribosomal subunit protein eS6y
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGAKKRKKKTYTKPKKIKHKHKKVKLAVLQFYKVDGSGKVQRLRKECPNATCGAGTFMASHFDRHYCGKCGLTYVYQKEGAQE
Protein: Zinc finger protein 491 (Q8N8L2)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MGERLFESAEGSQCGETFTQVPEDMLNKKTLPGVKSCESGTCGEIFMGYSSFNRNIRTDTGHQPHKCQKFLEKPYKHKQRRKALSHSHCFRTHERPHTREKPFDCKECEKSFISPASIRRYMVTHSGDGPYKCKFCGKALDCLSLYLTHERTHTGEKRYECKQCGKAFSWHSSVRIHERTHTGEKPYECKECGKSFNFSSSFRRHERTHTGEKPYKCKECGKAFNCPSSFHRHERTHTGEKPYECKLYGKALSRLISFRRHMRMHTGERPHKCKICGKAFYSPSSFQRHERSHTGEKPYKCKQCGKAFTCSTSFQYHERTHTGEKPDGCKQCGKAFRSAKYIRIHGRTHTGEKPYECKQCGKAFHCVSSFHRHERTHAGEKPYECKHCGKAFTCSIYIRIHERIHTGEKPYQCKECGKAFIRSSYCRKHERTHTINI
Protein: Phosphatidylethanolamine-binding protein 1 (PEBP-1) (23 kDa morphine-binding protein) (HCNPpp) (P23K) [Cleaved into: Hippocampal cholinergic neurostimulating peptide (HCNP)] (P31044)
Organism: Rattus norvegicus (Rat)
Function: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation (By similarity).
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein.
Interaction partners:
- Polyunsaturated fatty acid lipoxygenase ALOX15
- RAF proto-oncogene serine/threonine-protein kinase
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein uL16m
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL10m
- Mitochondrial ribosomal protein L44.
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL27m
Sequence:
MAADISQWAGPLSLQEVDEPPQHALRVDYGGVTVDELGKVLTPTQVMNRPSSISWDGLDPGKLYTLVLTDPDAPSRKDPKFREWHHFLVVNMKGNDISSGTVLSEYVGSGPPKDTGLHRYVWLVYEQEQPLNCDEPILSNKSGDNRGKFKVESFRKKYHLGAPVAGTCFQAEWDDSVPKLHDQLAGK
Protein: chitin synthase (EC 2.4.1.16) (Q5A594)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Formin-binding protein
- UDP-N-acetylglucosamine diphosphorylase
- chitin deacetylase
- Chitin synthase export chaperone
- Serine/threonine-protein kinase
- Bni4p
- NEDD8-conjugating enzyme UBC12
- Chs4p
- Galactose oxidase
Sequence:
MKNPFDSGSDDEDPFLSNPQSAPSMPYAAYTSDRTSPRKTYQPLNFDSEDEDAKESEFMAFPSSTSGSPFHQQQSPRQSPNIFSRSTARAATSKSNMSIYDNTPNLQFNKSGAATPRAQFTSKESPKRQKTTEVTIDFDNDDDNNHTLEFENGSPRRSFRSSAISSERFLPPPQPIFSRETFAEANSREEEKSADQETLDEKYDYDSYQKGYEEVETLHSEGTAYSGSSYLSDDASPETTDYFGASIDGNIMHNINNGYVPNREKTITKRKVRLVGGKAGNLVLENPVPTELRKVLTRTESPFGEFTNMTYTACTSQPDTFSAEGFTLRAAKYGRETEIVICITMYNEDEVAFARTMHGVMKNIAHLCSRHKSKIWGKDSWKKVQVIIVADGRNKVQQSVLELLTATGCYQENLARPYVNNSKVNAHLFEYTTQISIDENLKFKGDEKNLAPVQVLFCLKESNQKKINSHRWLFNAFCPVLDPNVIVLLDVGTKPDNHAIYNLWKAFDRDSNVAGAAGEIKAMKGKGWINLTNPLVASQNFEYKLSNILDKPLESLFGYISVLPGALSAYRYIALKNHDDGTGPLASYFKGEDLLCSHDKDKENTKANFFEANMYLAEDRILCWELVSKRNDNWVLKFVKSATGETDVPETIAEFLSQRRRWINGAFFAALYSLYHFRKIWTTDHSYARKFWLHVEFIYQLVSLLFSFFSLSNFYLTFYFLTGSLVSYKSLGKKGGFWIFTLFNYLCIGVLTSLFIVSIGNRPHASKNIFKTLIILLTICALYALVVGFVFVINTIATFGTGGTSTYVLVSIVVSLLSTYGLYTLMSILYLDPWHMLTCSVQYFLMIPSYTCTLQIFAFCNTHDVSWGTKGDNNPKEDLSNQYIIEKNASGEFEAVIVDTNIDEDYLETLYNIRSKRSNKKVALGHSEKTPLDGDDYAKDVRTRVVLFWMIANLVFIMTMVQVYEPGDTGRNIYLAFILWAVAVLALVRAIGSLGYLIQTYARFFVESKSKWMKRGYTAPSHNPLN
Protein: Kelch-like ECH-associated protein 1 (K7ESE0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPN
Protein: Coiled-coil domain containing 174 (A0A0B4J1R8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRRKKPLDVTASSLVDLKAELFRKQEEFKQEKLLKDSGVFGKPKTTNKKPSIWSKQNVGVSNRAEKDAEQKIEEQKTLDKAREKLEEKAKLYEKMTKGDFIDEEVEDMYLVDFTQKIIDKRKEMEASGAHRDSQKAGERDDDEENLPEGEIPPPQDPSEEWVDYVDSLGRSRRCMRKDLPDLLEMDKNLQGRLFISPANEKTLLSEDMRKELQRQQWEEEEREALKRPMGPVHYEDIRENDGDVIGPLPPEPEAVPTPRPAAQSSKVEVIVQERKDTKPGVPHIREWDRGKEFSFGYWSKRQSDLRAERDPEFAPPSDYFVGQKRTGFSSSQAWSRPGPAQSDPGQCPDQSHGPSPEHTSPTPAPDNPPQAPTVTFKTLDDMISYYKQVT
Protein: Olfactory receptor (F8VPJ9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363047}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVLSNITHFSPMFYLSGFPGLEAFEHWIFIPFFLMYLVAISGNCLILIIIKTNPRLHTPMYYLLSLLALTDLGLSVSTLPTMVGIFWFNYHGIYFGACQIQMFCIHSFSFMESAVLLVMSFDRFVAICHPLRYSSIITVQRVMRAGLCVILRGPVALIPIVLLLKDFPYCGPLVLSHSFCLHQEVIHLACVDTTFNNLYGLSLVVFTVMLDLVLIALSYGFILYTVAGLASQEEQIRAFQTCTSHLCAVLVFFVPMMGLSLVHRFGKHAPPAVHLLMANIYLFVPPMLNPVIYSIKTKEIRKAIIRFLGFRKVNSESWG
Protein: COMM domain-containing protein 3 (Protein Bup) (Protein PIL) (Q9UBI1)
Organism: Homo sapiens (Human)
Function: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21778237}. Nucleus {ECO:0000269|PubMed:21778237}.
Interaction partners:
- COMM domain-containing protein 2
- Coiled-coil domain-containing protein 22
- COMM domain-containing protein 4
- COMM domain-containing protein 6
- COMM domain-containing protein 10
- COMM domain-containing protein 9
- COMM domain-containing protein 1
- COMM domain-containing protein 8
- COMM domain-containing protein 7
- COMM domain-containing protein 5
Sequence:
MELSESVQKGFQMLADPRSFDSNAFTLLLRAAFQSLLDAQADEAVLDHPDLKHIDPVVLKHCHAAAATYILEAGKHRADKSTLSTYLEDCKFDRERIELFCTEYQNNKNSLEILLGSIGRSLPHITDVSWRLEYQIKTNQLHRMYRPAYLVTLSVQNTDSPSYPEISFSCSMEQLQDLVGKLKDASKSLERATQL
Protein: Complex I assembly factor Egm, mitochondrial (Acyl-CoA dehydrogenase family member 9 homolog) (dACAD9) (EC 1.3.8.-) (Protein Enigma) (Q5U117)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16434470}.
Interaction partners:
- Complex I intermediate-associated protein 30, mitochondrial
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- Complex I assembly factor TIMMDC1, mitochondrial
- Transmembrane protein 186
- Transmembrane protein 70 homolog
- Distal membrane arm assembly component 2
- Translocon-associated protein subunit delta
- Transmembrane protein 126
- Electron transfer flavoprotein subunit alpha
Sequence:
MRPNLFSGASRLLTYSRNGKLLTRGRSTKATSSSLDSQHQDAATTEGGRAESVEESPEQQRKLPTREPLAKNFFIGVVDKELLAYPEVIPRDEMAQLENSLLPLKNYFVEPRETEETSPETLRQLGLYGLNVSTDYEGKGYGWSASLMASEPDSTDINVTLGLQTHRVVVDLLKEVGTPLQQQRYLQDLATGKLIGTEAIYEISPPEEDYFNTTAELFPEYGKWQLNGEKSFVICTPGERQLFLVLAQTQQPNVPGVLGRGTTIFLVDSQQEGVRLGEKHATFGCRKAEIRRVHFEGVKLGEDQVVGLPHDGNRYSEQLVRSSRLRGSLVGLSLAKKLLNELAQYTVNTTQCGVQLQDLELTRIHMSRAMCSVYAMESMLYLTAGLLDEFRAQDVTLESAITKYFTLRQVYAIASQNLGVVGPKSLLSGETTELGLRDAAQLCTQGESLDTLGMFIALTGLQHAGQAMNTGVRKSRNPLFNPGHIFGKFLDNNSIDNPKTKMQLSEHVHPSLEAAAQCIELSVARLQMAVELMFTKHGNAVVERQSEMQRLAEVGTLIYAMWASVARASRSYCIGLPLADHELLTATAICSEGRDRVRTLCTEIYGGHFVNNDNNLVRLSKQVAKSKGYFAVHPLTFNF
Protein: Signal peptidase complex catalytic subunit SEC11 (EC 3.4.21.89) (Signal peptidase complex catalytic subunit sec11) (Q57Z71)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648}.
Interaction partners:
- Signal peptidase complex subunit 3
- Protein artemis
- Vacuolar membrane-associated protein Iml1 N-terminal domain-containing protein
- Prolyl endopeptidase-like
- Prolyl endopeptidase-like
- WD repeat protein mio zinc-ribbon like domain-containing protein
Sequence:
MSLLHRADATALRILREQHVESLAMSAQTGPINYIKKTFKDIVDTMPDRRNTFLMLVTLCTFFVGWRTAIAVTDCESPLVVVLSGSMEPFMFRGDLLVLHNIGEPTMGDVVVFSLPNRTIPIVHRVHRIRLLEDGVTRLYLTKGDNNEMDDRTLYPRGYHWVEKKDIIGKVAVLVPRVGFITLIAEDHSWAKLVLVPLALIWCWYTGM
Protein: Probable arabinosyltransferase ARAD2 (EC 2.4.2.-) (Arabinan alpha-1,5-arabinosyltransferase) (L-Arabinosyltransferase) (Protein ARABINAN DEFICIENT 2) (Q9FLA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan. May function as inverting enzyme using UDP-beta-L-arabinopyranoside. Cell wall pectic arabinans are involved in thigmomorphogenesis response of inflorescence stems to mechanical stress.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:22270560}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Probable galacturonosyltransferase 7
- Polygalacturonate 4-alpha-galacturonosyltransferase
- Galactan beta-1,4-galactosyltransferase GALS3
- Xyloglucan glycosyltransferase 4
- Galactan beta-1,4-galactosyltransferase GALS1
- Xyloglucan 6-xylosyltransferase 2
- UDP-arabinopyranose mutase 1
- Xyloglucan 6-xylosyltransferase 1
- Probable methyltransferase PMT4
- Xyloglucan galactosyltransferase XLT2
Sequence:
MNPKIRKPNNSSSKKVTVSVLSVFLVFVFVNTFFYPSFYSDSGSIRRNLVDSRESFHFPGNFRKTKVYMYELPTNFTYGVIEQHGGEKSDDVTGLKYPGHQHMHEWYLYSDLTRPEVKRVGSPIVRVFDPAEADLFYVSAFSSLSLIVDSGRPGFGYSDEEMQESLVSWLESQEWWRRNNGRDHVIVAGDPNALKRVMDRVKNAVLLVTDFDRLRADQGSLVKDVIIPYSHRIDAYEGELGVKQRTNLLFFMGNRYRKDGGKVRDLLFKLLEKEEDVVIKRGTQSRENMRAVKQGMHTSKFCLHLAGDTSSACRLFDAIASLCVPVIVSDGIELPFEDVIDYRKFSIFLRRDAALKPGFVVKKLRKVKPGKILKYQKVMKEVRRYFDYTHLNGSVNEIWRQVTKKIPLIKLMINREKRMIKRDGSDPQCSCLCSNQTGIIHGV
Protein: Aldehyde oxidase 3, isoform A (Aldehyde oxidase 3, isoform B (EC 1.-.-.-, EC 1.2.3.1)) (FI04488p) (Q9VF51)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Uricase
- Guanine deaminase
- purine-nucleoside phosphorylase
- Aldehyde oxidase 1
Sequence:
MTTKFSINGLPYAVNLTNLPPDITLNTFIREHAQLTATKFMCQEGGCGACICVVRDGKRSWAVNSCLTLLNTCAQLEIVTAEGLGNQRTGYNPIQKRLAKMNGTQCGFCSPGFVMNMYGLMEQNEGKVTMAEVENSFGGNICRCTGYRPILDAMKSFAVDSNIAIPAECGDIEDLKPRNCPKTGQACSGSCLPSTLVYEDGVQWHWPKSLSELFDALDKVKDSEEFMLVAGNTAHGVYRRSTDIKHFIDVQGVEELHQHSSEGQQLKLGANLSLTQTMEIIRTTSKQPGFEYLDVLWNHIDLIANVPVRNSGTLAGNISIKKQNPEFPSDIFISFEALNVKVVALKNAADEKEMSLAEYLGTNDKKLVLKTFVLPAYPKDKYIYESYKIMPRAQNAHAYVNAAFLLELEADNKVKSARICFGGIRPDFIHASAIEKLLVGQNPYESSLVEQTFTKLEDLIKPDEVLPDASPAYRSKLACGLFYKFLLKHAPVAEVGEKFRSGGQILQRPLSSGLQVFQTQKKNYPVTQAVEKVEGMIQCSGEATYMNDVLTTSNTLHCAFVGATKVGSTIDSIDASEALKQPGVIAFYSAKDIPGTNTFCEPSFGFEVEEIFCSGLVRHSEQPAGVIVALTADQAHRAAKLVRISYSNPSSDFKLQPSLGDVFASPTPDSSRIVPASKSTSKKIKFSEQPDKEVRGIFQMGLQYHFTMEPQTTVAIPFEDGLKIFSATQWMDQTQSVIAHMLQVKAKDVQLQVRRLGGGYGSKITRGNQVACAASLVAYKLNRPVRFVQSLESMMDCNGKRWACRSDYKCHIKDNGKIVGLTNDFYEDAGWSPNESPIEGHSTFTAVNCYDLNGDNFKNNGNAVLTDAPSSTWCRAPGSVEGIAMIENIIEHVAFEVQKDPAEVRLANIAAGNKISELLPQFLESREYAQRKKEIESHNAKNRWTKRGLGLAVMDYPIFYFGQYPATVAIYHVDGTVVVTHGGIEMGQGMNTKVAQVAAYTLGIDLSFIKVESSDTINGANSMVTGGAVGSESLCYAVRKACETLNSRLEPVKKKDASWIETVEAAYGKSINLIASDHYKKGDMQNYHIYGLALTEVELDVLTGNSQIKRVDILEDAGESLSPWIDIGQIEGAFVMCLGYWMSEQLVYDRETGRLLTNRTWNYKPPGAKDIPIDFRIELIQKPNPSGAGFMRSKATGEPPCCLAVSVVFALRQALDSARHDAGLPREWVRLGAPTTPETLVVNAGHEAASFRLK
Protein: Activating transcription factor 3 (Q5VTZ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMLQHPGQVSASEVSASAIVPCLSPPGSLVFEDFANLTPFVKEELRFAIQNKHLCHRMSSALESVTVSDRPLGVSITKAEVAPEEDERKKRRRERNKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDERNLFIQQIK
Protein: E3 ubiquitin-protein ligase etc-1 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase) (O17736)
Organism: Caenorhabditis elegans
Function: E3 ubiquitin-protein ligase that accepts ubiquitin from E2 ubiquitin-conjugating enzymes, such as ubc-18, in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates ify-1 and cyb-1 targeting them for degradation in post-meiotic embryos.
Interaction partners:
- RING-type E3 ubiquitin transferase
- Securin-like protein
- Polyubiquitin-A
- Ubiquitin-like domain-containing protein
Sequence:
MIKSLNERDNFLNRLREMEHKREKDEKQEKAARKVQKFWRGHRVQHNQRLLFRAEFDAVSDRQRGLEETIKMAQLLVNFYETNKDEERLVMTLSELVKLKTSDKEFEKRIRETQRLLLARCCIKFLKNATENTIFFHIFRYLEDYVTCHSKLFEASSKLGLFNAEFHLLEALIGKPTGKTVERASLNPRILQLLTRIFETFVNPSRSTSVSVNVANRLLKTICVNITDLNFSNYILYYIKDHIKPTSPNFTNLFEAMKSVDILNNWKVRPEIAETASLRLQSIFVSQIVHVSNTQSEDVKQYFNSLAVFLEHHSKIMRSLNVKEDLSEFGRLRTSVNNHLKQYCEEMLISNEFRRAACIYANLPGVQVETIISLRKYFSQFLDLLAASNTFVEALYAFIARLCPNGEFDPIDAKSPKVNALELFCNCLNKRVSSVADSDFVPTDIFVDFDHTVEFLRDVSIKLIHLMFPTMARGDLYSGNLKEKMYKAETDWKDVTESVFSILGAIYQKDIRLKYFPEEFWTNHGREVLSGIGEHRRMPRRRMPNGRLQIERTMDTEFVERLAAIYEMDSDSENDDEDEDNNLPAVLRRAICVMKHIPFIVPFMDRVKLFTRLLNQDKEKHYTSTFGMGFNGPSVTVRRDQVYMDAFETFAPKMQGDKVNDLKSMVRVKMVNWAGMNESGIDGGGIFREFLSELLKTAFNVERGFFTFTESKLLYPNPTAPFLLGVDCLAHFQFIGRMIGKLIYERQLQEVRFAEFFIAQIFETDKNKDVDLQHMKSFDPIIFKHLKALQKMNNRELDELQLDFSVVTSDMGLVRNVNLKPNGSKFRVTVENVHEYVRLYVNYHLKQRIASMVDAVRKGISEIISIEWMRMFAPHELQIMIAGYEEVFTAKELRKFCELRFAAGTQDINYEEMFWDVIDKLSNDDKKALLKFVTGCSRAPVDGFKSIQPRMGVLVIPSSDDELPTSATCMNMLRIPKYSNRTKLEEKLRYAINSGAGFELA
Protein: Protein Smaug (Q23972)
Organism: Drosophila melanogaster (Fruit fly)
Function: Translation regulator that binds to the 3'-UTR of specific mRNAs such as nanos (nos) and prevents their translation. Prevents translation of unlocalized nos in the bulk cytoplasm via the recruitment of cup.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10488336, ECO:0000269|PubMed:20953170}. Note=In the cytoplasm of syncytial embryos, accumulates in discrete foci.
Interaction partners:
- Protein cup
- Protein nanos
- poly
- Heat shock protein 83
- Maternal effect protein oskar
- Trailer hitch, isoform H
Sequence:
MKYATGTDNAMTSGISGQTNNSNSASNEMQPTTSTPTAAHKEATSTATTTATYANGNPNSNANPSQSQPSNALFCEQVTTVTNLFEKWNDCERTVVMYALLKRLRYPSLKFLQYSIDSNLTQNLGTSQTNLSSVVIDINANNPVYLQNLLNAYKTFQPCDLLDAMSSSSSDKDSMPCYGSDFQITTSAQCDERKLYARKEDILHEVLNMLPLLKPGNEEAKLIYLTLIPVAVKDTMQQIVPTELVQQIFSYLLIHPAITSEDRRSLNIWLRHLEDHIQAAAAGLTNRSYFLQPSPQLVAGGSSTGSGSCSSSATSSSTASCSSVASSSLCPASGSRSSRTNDWQTIAPPSKQLQNKLAGDWRGNGGGSSSGSINPLCDNLNGITLNELASSQNSLGLSLEGSSSLVNGVVAGAGSMLGIAGGDDHDTSFSKNGTEILDFDPVTADMGEACSLASSSLCGRNGGNPVEDRSQPPPNLQQQLLQPPPYASILMGNVGDQFGEINRWSLDSKIAALKTRRSNSLTTQTISSCSSSSNSSVITVNDNCSNSTENLAQFANKPRSFSLSIEHQRGALMNSGSDTRLDEFKPNYIKFHTRNVGMSGIGLWLKSLRLHKYIELFKNMTYEEMLLITEDFLQSVGVTKGASHKLALCIDKLKERANILNRVEQELLSGQMELSTAVEELTNIVLTPMKPLESPGPPEENIGLRFLKVIDIVTNTLQQDPYAVQDDETLGVLMWILDRSIHNEAFMNHASQLKDLKFKLSKMKISMVPKMHHVKPAGVGPNNGNINKPRWNGKTRKCDTKNGSNDRINNRKNSNDMLNFSLNCLPHPLPHHSQQAPPPLPQFDYNGYGGGPSHQPQYKSSSYPSFMGNPQQQPPPPPSSKSHHHPQQMQQMLQQHNHFPALPQQTPPQSHRRSLNNLILVAGGPQQPQQLIFKPGQGVLTNNGSNDNLVLERNQQSQQQQQQRKLSGGVSSAEQQPKKTMAAVVMENLAKFDQHFTLF
Protein: Conserved protein (O06198)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MDLNALADLPLTYPEVGATATGRLPAGYNHLDVSTQIGTGRQRFEQAADAVMHWGMQRNAGLRVRASSETAVVSAVVLVGIAFLRAPCRVVYVIDEPDVRGFGYGTLPGHPVSGEERFAVRCDPMTSVVFAEVLSFSRPATWASKAAGPLGAVTQRFIAQRYLRAV
Protein: Protein spaetzle 3 (Protein spatzle 3) (Q9VLV7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Neurotrophin which may function as a ligand to the Toll-related receptor Tollo. Involved in a Tollo and JNK signaling pathway that positively regulates neuromuscular junction (NMJ) growth in presynaptic motorneurons. May function by activating Tollo to promote the phosphorylation of JNK.
Interaction partners:
- RE45222p
- Toll-like receptor Tollo
- Protein spaetzle
Sequence:
MALTNFSLPFGALGQPWGVTIAPLHPIHQLASNTNNLLYSPADHQQQTPAEAAADPEYFKNNPYAPPQSGGYQYQNTAGRRKQSNAYLPPTAPNAVRNSVYHIQQVQQTQQQQTQQQHQQQDQHENSVSFQSSSSRSSSSSTTGQSSIQLTQTHASGRGPAEGSYSRYPGQQAQPPQQQQPQQKQYFNAHGSASATFTKNSGSFSITSFGSRQQQQQPPQPQQPPPSQQQQPPPAPPPQRSRQAKPEAQPAQTYGVAPPENYPERAPGFTRVQAGQGSRTQVHAVLDYDVEEGEEDEEEDGEEEGQFYEGQENDKSNNNQMPTVTPIQGPIYLKNGTVPVVPLFSYPKLNNGSFLQIPIWWTALSVALGLDVRGDVIKGVPCIKRYHQLFCPTAGNSYPIDKIERFIDDNKALMRRMYGDFEMNMEGPGGGGGRQQGKVRKRRFIDEPDIFIPPGAFAANAGETVEAGDSYFGQLRKKRQAAAGGSRNRGGSAGGSGNGNTNANRQPGNKNGSSGTGRLDACESKIEIVTPYWASNSAGKIRAIVNTQHFEQAIHQEVCSNTQTPRCEGECGCEQKYKWHRLLAYDPDNDCKGIFMDWFLFPSCCVCRCNP
Protein: XPA, DNA damage recognition and repair factor (A0A8I6G6T5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATAEEKRTSPEPAAAEKPAELPAAVRASVERKRQRALMLRQARLAARPYPAAAATGGVTSIKAAPKVIDTKGGFILEEEEEEKHKIGDVVHEPGPVMEFDYTICEECGKEFMDSYLMNHFDLPTCDSCRDADDKHKLITKTEAKQEYLLKDCDLEKREPALRFIVKKNPRHSQWGDMKLYLKLQVVKRALEVWGSQEALEDAKEVRQENREKMKQKKFDKKVKELRRAVRSSVWKRETTAHQHEYGPEEHLEEDMYRKTCTLCGHELTYEKM