wanglab/gogpt-training-data huggingface dataset:
Protein: Dual oxidase 1 (DUOX1) (EC 1.11.1.-) (EC 1.6.3.1) (Blistered cuticle protein 3) (NADPH thyroid oxidase 1) (O61213)
Organism: Caenorhabditis elegans
Function: Plays a role in cuticle biogenesis. In complex with doxa-1 and tsp-15, produces reactive oxygen species (ROS), which are probably used by mlt-7 for tyrosine cross-linking, thus stabilizing cuticular extracellular matrix. May regulate the production of ROS by playing a role in modulating proline catabolism. Required in combination with mlt-7 for correct formation of cross-links in cuticle collagens. Association with the GTPase rho-1 promotes ROS production and this interaction may be modulated by memo-1, in order to control the oxidative stress response and longevity.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Dual oxidase maturation factor 1
- Tetraspanin-15
- NAD
- Protein memo-1 homolog
- Tetraspanin
- Tetraspanin
- Tetraspanin
- Tetraspanin
- Tetraspanin
- Tetraspanin
Sequence:
MRSKHVLYIAILFSSIFGGKGIQQNEEFQRYDGWYNNLANSEWGSAGSRLHRDARSYYSDGVYSVNNSLPSARELSDILFKGESGIPNTRGCTTLLAFFSQVVAYEIMQSNGVSCPLETLKIQVPLCDNVFDKECEGKTEIPFTRAKYDKATGNGLNSPREQINERTSWIDGSFIYGTTQPWVSSLRSFKQGRLAEGVPGYPPLNNPHIPLNNPAPPQVHRLMSPDRLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIHREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDVRLSNYTKYMPHVPPGISHAFGAAAFRFPHSIVPPAMLLRKRGNKCEFRTEVGGYPALRLCQNWWNAQDIVKEYSVDEIILGMASQIAERDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGLAPKTWETMNEDFYKKHTAKVEKLKELYGGNILYLDAYVGGMLEGGENGPGELFKEIIKDQFTRIRDGDRFWFENKLNGLFTDEEVQMIHSITLRDIIKATTDIDETMLQKDVFFFKEGDPCPQPFQVNTTGLEPCVPFMQSTYWTDNDTTYVFTLIGLACVPLICYGIGRYLVNRRIAIGHNSACDSLTTDFANDDCGAKGDIYGVNALEWLQEEYIRQVRIEIENTTLAVKKPRGGILRKIRFETGQKIELFHSMPNPSAMHGPFVLLSQKNNHHLVIRLSSDRDLSKFLDQIRQAASGINAEVIIKDEENSILLSQAITKERRQDRLDLFFREAYAKAFNDSELQDSETSFDSSNDDILNETISREELASAMGMKANNEFVKRMFAMTAKHNEDSLSFNEFLTVLREFVNAPQKQKLQTLFKMCDLEGKNKVLRKDLAELVKSLNQTAGVHITESVQLRLFNEVLHYAGVSNDAKYLTYDDFNALFSDIPDKQPVGLPFNRKNYQPSIGETSSLNSFAVVDRSINSSAPLTLIHKVSAFLETYRQHVFIVFCFVAINLVLFFERFWHYRYMAENRDLRRVMGAGIAITRGAAGALSFCMALILLTVCRNIITLLRETVIAQYIPFDSAIAFHKIVALFAAFWATLHTVGHCVNFYHVGTQSQEGLACLFQEAFFGSNFLPSISYWFFSTITGLTGIALVAVMCIIYVFALPCFIKRAYHAFRLTHLLNIAFYALTLLHGLPKLLDSPKFGYYVVGPIVLFVIDRIIGLMQYYKKLEIVNAEILPSDIIYIEYRRPREFKYKSGQWVTVSSPSISCTFNESHAFSIASSPQDENMKLYIKAVGPWTWKLRSELIRSLNTGSPFPLIHMKGPYGDGNQEWMDYEVAIMVGAGIGVTPYASTLVDLVQRTSSDSFHRVRCRKVYFLWVCSTHKNYEWFVDVLKNVEDQARSGILETHIFVTQTFHKFDLRTTMLYICEKHFRATNSGISMFTGLHAKNHFGRPNFKAFFQFIQSEHKEQSKIGVFSCGPVNLNESIAEGCADANRQRDAPSFAHRFETF
Protein: Protein tweety-2 (Dttyh2) (Q9W5A5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable chloride channel.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Uncharacterized protein
- RE15974p
- Protein tweety
- FI24431p1
Sequence:
MEQPSILVKILHSIPHVNYTFRRVNDTFNPDSDVYLEPTNNKLQCQQKGIELQSLVILASIPAGLLIGSLLGLLLYLLTRCCDRRQRKPSAQRCQSCSLVIITLMTCAAIGLGLYGNDDFHNGLLQAFGSGKSVEGLVLTLKRQTESIKHDLETRMAGHKVEQLVEKPHYNQTVVMLLIETSRLVTENTSRAVASLDSMVHYFMKAKGSENDTSLMGLLQLGEFYESIRWPATLAFLTVLLLLCTVLVIGVARRSRCTLIFFSVSGLFCIIICWLLAGVYLASSVAAGDFCMRPHDYMCRQVGMRSPYVDFLNCGTPRNRFILRLNESRDLVDRARESVEHMQRMSQETYPHIDIQRTLNAMDNDLEITLRNLTTLSATLDRRTIDMHYEEALRGLCGGGLLGLSLMMVAGLLTSFLLTILVYADSHAWIYLTKRPTLDADKSETAPLFPASNAPSASISPTAPLSTGTINRTLLHHQQASSGGGSGTLPGSGGGAGAGGGVGANGHNGVGPYRNGSAGLRQGLASPSSQSSHTSSTATYNNGTTSYHNSHQQHNNHLYSNHYSHSNNHYNNTQHRTNPAAGAVAAAVGVVSSGQRSPSPPPVYDLVHGTRSGHHTLGRLPSHHQQSATYLPGPNNGKYATLSKQCKTLESNDFY
Protein: Aberrant microtubules protein 1 (P47146)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for normal microtubule organization.
Interaction partners:
- Putative lipase LIH1
Sequence:
MSWRYSILTVDGSFKIFIPWEIFLTWNFLSAAWLNSTESNTYIHYSTCWGTSDYTLNISVIEATTEKLVDTRLLTTLENATAWINSNSIDEDEDDMPHATNVADRLDGLSLSKRVYSICHYEF
Protein: Kynurenine 3-monooxygenase (EC 1.14.13.9) (Kynurenine 3-hydroxylase) (Q86PM2)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Function: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03018}. Membrane {ECO:0000255|HAMAP-Rule:MF_03018}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018}.
Interaction partners:
- Kynurenine formamidase
- Kynurenine aminotransferase
- Tryptophan 2,3-dioxygenase
- cholesterol 7-desaturase
- 15-cis-phytoene synthase
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MTAQYKQTNTNGLTARNLNVAVVGGGLVGSLFALHLGKKGHTVDLYEYREDIRTAELVIGRSINLALSARGRKALAEVGLEDALLQHGIPMKGRMLHDLKGNRKIVPYDANTNQCIYSVGRKHLNEVLLDAAEKYPNIHLYFNKKLQSANLDEGEMSFIDPTTKESTHTKADLIVGCDGAYSAVRKEIVKRPGYDYSQTYIEHGYLELCIPPTKDGDFAMPHNYLHIWPRGKFMMIALPNQDRTWTVTLFMPFTNFNSIKCDGDLLKFFRTYFPDAIDLIGRERLVKDFFKTRPQSLVMIKCKPYNVGGKAVIIGDAAHAMVPFYGQGMNAGFEDCTVLTELFNQHGSDVDRILAEFSDTRWEDAHSICDLAMYNYVEMRDLVTKRSYLFRKKLDELLYWMLPNTWVPLYNSVSFSHMRYSKCIANRKWQDKILTRVLYCCSITAVAAAGYFGYKYGNMDLVQHYSSSVLQLLKLK
Protein: Acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.12) (G8BAA7)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU361137}.
Interaction partners:
- Dihydrolipoyl dehydrogenase
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate dehydrogenase E1 component subunit beta
- 2-oxoglutarate dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Citrate synthase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Endonuclease/exonuclease/phosphatase domain-containing protein
- Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
- dihydrolipoyllysine-residue succinyltransferase
Sequence:
MSSALFAVSRSAMALRTAAVATKPVSIKTSSFLTLARLYSSGKFPPHTVIHMPALSPTMTSGGILEWTKKVGDELAPGEPIAEIETDKASMDFEFQEEGYLAKILKEAGSKDVPVGEPIAVYVEDASEVSAFDSFTAADAGEAPKQPAPEKEEESKPKEQESKSEEPKKTESKPSTSSSSAKSSSAKPSGRIFASPLAKTIALEKGISLKSVKGTGPHGRIVAKDLEGLEPAQAASAASSTAATATPAGATYEDIPLTNMRKTIATRLLQSTQQSPTYIIQSQISVSKLLKLRASLNASAEDRYRLSVNDLLIKAIAVASVRVPQINSAWLGDQGVIRQYKNVDVSVAVATPTGLITPIIKDAQNKRLSAISNEIKDLGKRAKIGKLNPEEYQGGTICISNLGMNHAVTAFTSIINPPQSAIVAIGTTEKKAVPSDVNEQGFVFDDVLTITGTFDHRVVDGALGGEWIKELKRIVENPLEMLV
Protein: mRNA export factor ICP27 homolog (Transcriptional regulator IE63 homolog) (Q05906)
Organism: Equine herpesvirus 1 (strain Kentucky A) (EHV-1) (Equine abortion virus)
Function: Multifunctional regulator of the expression of viral genes that mediates nuclear export of viral intronless mRNAs. This immediate early (EI) protein promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP (By similarity).
Subcellular location: Host cytoplasm {ECO:0000250}. Host nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}.
Interaction partners:
Sequence:
MALSSVSSCEPMEDEMSIMGSDTEDNFTGGDTCAEATRGLVNKSAFVPTQTVGTVSALRNVVGNPPKSVVVSFSASPQRAQPSNPKSERPAFGHGRRNRRRPFRRNNWKQQQRGWEKPEPENVPARQSAGSWPKRSSLPVHMRLGQRGGDSSSADSGHGGAGPSDRWRFKTRTQSVARVHRNRRRGNANHGSNTPGRSAGDRLNAAAARSIADVCRRVTSSRIGEMFHGARETLTTPVKNGGFRAENSSPWAPVLGFGSDQFNPEARRITWDTLVEHGVNLYKLFEVRSHAAEAARSLRDAVMRGENLLEALASADETLSWCKMIVTKNLPMRTRDPIISSSVALLDNLRLKLEPFMRCYLSSSGSPTLAELCDHQRLSDVACVPTFMFVMLARIARAVGSGAETVSRDALGPDGRVLADYVPGACLAGTLEAIDAHKRRCKADTCSLVSAYTLVPVYLHGKYFYCNQIF
Protein: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (EC 3.2.2.-) (EC 3.2.2.6) (2'-phospho-ADP-ribosyl cyclase) (2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase) (EC 2.4.99.20) (2'-phospho-cyclic-ADP-ribose transferase) (ADP-ribosyl cyclase 1) (ADPRC 1) (Cyclic ADP-ribose hydrolase 1) (cADPR hydrolase 1) (CD antigen CD38) (Q9MZ03)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Synthesizes the second messengers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10477767}; Single-pass type II membrane protein. Microsome membrane {ECO:0000269|PubMed:10891341}; Single-pass type II membrane protein. Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Interaction partners:
- Nicotinamide phosphoribosyltransferase
- Nicotinamide-nucleotide adenylyltransferase
- protein acetyllysine N-acetyltransferase
- Uncharacterized protein
- NAD-dependent protein deacetylase
- Protein kinase C beta type
- Ryanodine receptor 3
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Purine nucleoside phosphorylase
- NAD-dependent protein deacylase sirtuin-5, mitochondrial
Sequence:
MPDYEFSPASGDRPRSWISKQVLIVLGVCLPVILALAIWVGVLTWRQSSMGATDHVSAIVLGRCLTYTRNMHPELRNQDCKKILNTFTSAFVSKDPCNITKEDYQPLIDLVTQTVPCNKTLFWSRSKELAHQYSGIQKEMFTLEDTLLGYIADNLVWCGDPRTSEVKEEFCPYRNENCSSTATSVFWTVVSQKFAESACGTVYVMLNGSRTTAFSKASTFGSVEVFNLHPDRVHTLHAWVMHDIGGVERDSCLGSSIKELKSIVNQRNISFFCQDDYRPARFVQCVRHPEHPSCSVLM
Protein: Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3) (A0A494C012)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364110}. Nucleus {ECO:0000256|RuleBase:RU364110}.
Interaction partners:
Sequence:
MPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
Protein: 5-aminolevulinate synthase (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase) (Q8T4G6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQCPFLNRFTASFIRNYAETLCQSYGSHCPVVGKTLVSGEKKLLLVAASVTRSHSTGANAHANAGGPATANATAPVSAPASADPGKASAKETFPYERFFNEQIMKKKRDHSYRVFKKVNRLAGDGLFPHALEYSERTEKPITVWCSNDYLGMSAHPGVKRAVQDALNRHGSGAGGTRNISGNSLHHERLESKLAELHQKEAALLFTSCFVANDSTLFTLAKLLPGCEIFSDAGNHASMIMGIRNSGVPKHIFRHNDVDHLHQLLKQTDKSVPKIVAFETVHSMTGAICPLEELLDVAHEHGAITFIDEVHAVGLYGDHGAGVGERDGVLHKMDIISGTLGKAFGNIGGYIAGTHNLVDMIRSYAAGFIFTTSLPPTVLCGALEAVNILASEEGRQLRHLHQRNVSYLKSLLKREGFPVEETPSHIIPIKIGDPLKSSQISNVLIEQFGHYLQSINYPTVARGQEKLRLAPTPFHTFEMMNALVTDLKKVWEMVDLSTNVPLSPNACMFCNSESCWHQDTSPDLECGIPNCPRLEISLAA
Protein: Odorant receptor 98a (Q9VAZ3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 67a
- Odorant receptor 56a
- Putative odorant receptor 92a
- Odorant receptor 47a
- Putative odorant receptor 69a, isoform A
- Odorant receptor 49b
- Odorant receptor 67d
- Odorant receptor 85b
- Odorant receptor 67b
- Odorant receptor 88a
Sequence:
MLFNYLRKPNPTNLLTSPDSFRYFEYGMFCMGWHTPATHKIIYYITSCLIFAWCAVYLPIGIIISFKTDINTFTPNELLTVMQLFFNSVGMPFKVLFFNLYISGFYKAKKLLSEMDKRCTTLKERVEVHQGVVRCNKAYLIYQFIYTAYTISTFLSAALSGKLPWRIYNPFVDFRESRSSFWKAALNETALMLFAVTQTLMSDIYPLLYGLILRVHLKLLRLRVESLCTDSGKSDAENEQDLIKCIKDHNLIIDYAAAIRPAVTRTIFVQFLLIGICLGLSMINLLFFADIWTGLATVAYINGLMVQTFPFCFVCDLLKKDCELLVSAIFHSNWINSSRSYKSSLRYFLKNAQKSIAFTAGSIFPISTGSNIKVAKLAFSVVTFVNQLNIADRLTKN
Protein: Protein LSM12 (Sm-like protein 12) (P38828)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- PAB1-binding protein 1
- Protein NAM8
- U1 small nuclear ribonucleoprotein A
- Protein PBP4
- ATP-dependent RNA helicase DHH1
- Polyadenylate-binding protein, cytoplasmic and nuclear
- LSM1-LSM7 complex subunit LSM1
- mRNA-binding protein PUF3
- Post-transcriptional regulator MKT1
- LSM complex subunit LSM3
Sequence:
MSVSLEQTLGFRIKVTNVLDVVTEGRLYSFNSSNNTLTIQTTKKNQSPQNFKVIKCTFIKHLEVIGDKPSFNSFKKQQIKPSYVNVERVEKLLKESVIASKKKELLRGKGVSAEGQFIFDQIFKTIGDTKWVAKDIIILDDVKVQPPYKVEDIKVLHEGSNQSITLIQRIVERSWEQLEQDDGRKGG
Protein: Guanine nucleotide-binding protein G(f) subunit alpha (G protein alpha f subunit) (Q05337)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma-e
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- G protein beta subunit 5
- Adenylate cyclase type 9
- Guanine nucleotide-binding protein subunit gamma
- Uncharacterized protein, isoform B
- Actin-related protein 2/3 complex subunit 2
- Guanine nucleotide-binding protein subunit gamma-1
- 5-hydroxytryptamine
Sequence:
MKLRLLRCLRQQPAKPAAVMTHKEDQYPVSLDHHVLKDMAKGVRDTTVKILLLGTAESGKTTIIKQMRILHINGFTDDERREKIPEIYQNIHESILQLVGQMGVLGIDFGSCTSERSADYILSLPGSAPEYMNEEYCDHVTTLWNDVGIRACYDRSNEFPLLDSAKYFLDNFVRISDAEYIPSTEDILHSRKITTGISQITFRVPIPKSMGGGEQQFQMYDVGGQRDQRNKWIQVFEGIQAVLFLISCSEFDQNLREDPSQNRLQEALKLFRAVWQNRFLASAGLIVFLNKYDIMERKIRAGKHIVDYFPEYEDFCKRPQQDNCFGESDWTKMFIKQKLVDITQEPFKRHSRNQVDLGTSERECYYHFTVATDTRCIRDVFCDVQKMILSENVSSMGLF
Protein: Probable RNA methyltransferase C2A9.10 (EC 2.1.1.-) (Q9Y7L2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable RNA methyltransferase.
Interaction partners:
- Uncharacterized protein C18B5.09c
- Ribonucleases P/MRP protein subunit pop1
- La-related protein 7 homolog
- Telomerase reverse transcriptase
- Trimethylguanosine synthase
- H/ACA ribonucleoprotein complex subunit gar1
- Ribonucleases P/MRP protein subunit POP7
- U4/U6 snRNA-associated-splicing factor prp24
Sequence:
MSNFQHGNYHSYYSMRGGTSIIDPRLKCLPDSLFYEASVLDIGCNNGTVSAQIASIFGASFVLGLDIDHVLIQKARKHLEFVSSRIGPVRNPGSIVEDQFNYYPISSIKKFSRIPVQLQPPLNKQNFPHNIEFETADFLRWESKRKFKIILALSVSKWVHLNNHDEGIIKFFGKISSLLETNGVLILEPQGWDSYLKAAKKISVFNQTPENLKIQPDAFEHLLNQAGLVLEYSIEPQVNNSEYKNFAKRTMYIYKKKGIGIIKLLTST
Protein: Transporter (Q63380)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLLARMKPQVQPELGGADQLPEQPLRPCKTADLLVVKERNGVQCLLASQDGDAQPRETWGKEIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQFNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFASFTLNLPWTNCGHAWNSPNCTDPKLLNASVLGDHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVIVVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVKIEDVATEGAGLVFVLYPEAISTLSGSTFWAVLFFLMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTCAVTLGTFLLAMFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYVYPPWANWVGWGIALSSMILVPAYVIYKFFSIRGSLWERVAYGITPENEHHLVAQRDVRQFQLRHWLAI
Protein: Ubiquitin-like modifier-activating enzyme 6 (Ubiquitin-activating enzyme 6) (EC 6.2.1.45) (Monocyte protein 4) (MOP-4) (Ubiquitin-activating enzyme E1-like protein 2) (E1-L2) (A0AVT1)
Organism: Homo sapiens (Human)
Function: Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Required for UBD/FAT10 conjugation. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility.
Interaction partners:
- Ubiquitin D
- Ubiquitin-conjugating enzyme E2 Z
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-conjugating enzyme E2 R2
- Ubiquitin-conjugating enzyme E2 D2
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-conjugating enzyme E2 N
Sequence:
MEGSEPVAAHQGEEASCSSWGTGSTNKNLPIMSTASVEIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNRAEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPIKFISADVHGIWSRLFCDFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLNGSIQQITVISPFSFSIGDTTELEPYLHGGIAVQVKTPKTVFFESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLKLATSISETLEEKPDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLYLEAADIVESLGKPECEEFLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTSKEKGMITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYNSHRDPPEEEIPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQSGHSLEGCFQVIKLLSRRPRNWSQCVELARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPFAEEDLSADALLNILSEVKIQEFKPSNKVVQTDETARKPDHVPISSEDERNAIFQLEKAILSNEATKSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVTGGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGKEDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMPGHAKRLKLTMHKLVKPTTEKKYVDLTVSFAPDIDGDEDLPGPPVRYYFSHDTD
Protein: Tubulin alpha-3E chain (EC 3.6.5.-) (Alpha-tubulin 3E) [Cleaved into: Detyrosinated tubulin alpha-3E chain] (Q6PEY2)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Tubulin beta-2A chain
- Tubulin beta chain
- Tubulin beta-4A chain
- Tubulin beta-2B chain
- Tubulin beta-8 chain
- Tubulin beta-6 chain
- Tubulin beta-1 chain
- Tubulin beta-3 chain
- Tubulin beta-4B chain
- Cell division control protein 42 homolog
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSVEAEAEEGEAY
Protein: Uncharacterized protein (Q382W5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRSPCADYFTSLMATAGFVRCRGLSSSGQTNTTQTVHVLHSLYRRLRKEGEERKMLEDALSVNQLETNIRIGLRLLHCHTQLVDLNRQLKELPFWRLVRRMSLAVARRYYAWRIFSIRLRLRSTTAISNALVYTLFLVVCFMLYEIYCVCRIGVTRAEDRYKSLAVPIVQTFEALEEAARRRKDILLKEMEGDIVRQRN
Protein: Transcription regulator protein BACH1 (BTB and CNC homolog 1) (HA2303) (O14867)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator that acts as repressor or activator, depending on the context. Binds to NF-E2 DNA binding sites. Plays important roles in coordinating transcription activation and repression by MAFK (By similarity). Together with MAF, represses the transcription of genes under the control of the NFE2L2 oxidative stress pathway.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:24035498}.
Interaction partners:
- Transcription factor MafK
- F-box/LRR-repeat protein 17
- Transcription factor MafF
- Transcription factor MafG
- Hyaluronan mediated motility receptor
- Heme oxygenase 1
- Transcription factor Maf
- Exportin-1
- Transcription factor MafB
- F-box only protein 22
Sequence:
MSLSENSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFLKFKFLDSTADQQECPRKKCFSSHCQKTDLKLSLLDQRDLETDEVEEFLENKNVQTPQCKLRRYQGNAKASPPLQDSASQTYESMCLEKDAALALPSLCPKYRKFQKAFGTDRVRTGESSVKDIHASVQPNERSENECLGGVPECRDLQVMLKCDESKLAMEPEETKKDPASQCPTEKSEVTPFPHNSSIDPHGLYSLSLLHTYDQYGDLNFAGMQNTTVLTEKPLSGTDVQEKTFGESQDLPLKSDLGTREDSSVASSDRSSVEREVAEHLAKGFWSDICSTDTPCQMQLSPAVAKDGSEQISQKRSECPWLGIRISESPEPGQRTFTTLSSVNCPFISTLSTEGCSSNLEIGNDDYVSEPQQEPCPYACVISLGDDSETDTEGDSESCSAREQECEVKLPFNAQRIISLSRNDFQSLLKMHKLTPEQLDCIHDIRRRSKNRIAAQRCRKRKLDCIQNLESEIEKLQSEKESLLKERDHILSTLGETKQNLTGLCQKVCKEAALSQEQIQILAKYSAADCPLSFLISEKDKSTPDGELALPSIFSLSDRPPAVLPPCARGNSEPGYARGQESQQMSTATSEQAGPAEQCRQSGGISDFCQQMTDKCTTDE
Protein: Mitochondrial inner membrane protease subunit 2 (EC 3.4.21.-) (IMP2-like protein) (Q8BPT6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- KICSTOR complex protein ITFG2
- Mitochondrial inner membrane protease subunit 1
- Mitochondrial intermediate peptidase
Sequence:
MAQSQSWARRCFKAFCKGFFVAVPVAVTFLDRVACVARVEGSSMQPSLNPGGSQSSDVVLLNHWKVRNFEVQRGDIVSLVSPKNPEQKIIKRVIALEGDIVRTIGHKNRLVKVPRGHMWVEGDHHGHSFDSNSFGPVSLGLLHAHATHILWPPERWQRLESVLPPERCPLQTGEK
Protein: Tripartite motif containing 73 (C9JQH3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKEELAALFSELKQEQKKVDELIAKLVKNRTRIVNESDVFSWVIRREFQELRHPVDEEKARCLEGIGGHTRGLVASLDMQLEQAQGTRERLAQAECVLEQFGNEDHHEFIWKFHSMASR
Protein: Homeobox protein Hox-C4 (Homeobox protein Hox-3.5) (Q08624)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-C5
- Homeobox protein Hox-B6
- Homeobox protein Hox-C6
- Homeobox protein Hox-B5
- Pre-B-cell leukemia transcription factor 1
- Homeobox protein Hox-C8
- Homeobox protein Hox-C9
- Homeobox protein Hox-D4
- Homeobox protein Hox-A6
- Homeobox protein Hox-B7
Sequence:
MIMSSYLMDSNYIDPKFPPCEEYSQNSYIPEHSPEYYGRTRESGFQHHHQELYPPPPPRPSYPERQYSCTSLQGPGNSRAHGPAQAGHHHPEKSQPLCEPAPLSGTSASPSPAPPACSQPAPDHPSSAASKQPIVYPWMKKIHVSTVNPNYNGGEPKRSRTAYTRQQVLELEKEFHYNRYLTRRRRIEIAHSLCLSERQIKIWFQNRRMKWKKDHRLPNTKVRSAPPAGAAPSTLSAATPGTSEDHSQSATPPEQQRAEDITRL
Protein: Prostate tumor-overexpressed gene 1 protein (A0A0C4DGR2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU369088}. Nucleus {ECO:0000256|RuleBase:RU369088}. Cell membrane {ECO:0000256|RuleBase:RU369088}. Cytoplasm, perinuclear region {ECO:0000256|RuleBase:RU369088}. Note=Translocates from the cytoplasm to the nucleus at the onset of S-phase. Also localizes to lipid rafts. {ECO:0000256|RuleBase:RU369088}.
Interaction partners:
Sequence:
MRSPAVPTPARGQLGVAFVLLPPHSEGARVFGALGPIGPSSPGLTLGGLAVSEHRLSNKLLAWSGVLEWQEKRRPYSDSTAKLKRTLPCQAYVNQGENLETDQWPQKLIMQLIPQQLLTTLGPLFRNSQLAQFHFTNRDCDSLKGLCRIMGNGFAGCMLFPHISPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVSAIRQVITTRKQAVGPGGVNSGPVQIVNNKFLAWSGVMEWQEPRPEPNSRSKRWLPSHVYVNQGEILRTEQWPRKLYMQLIPQQLLTTLVPLFRNSRLVQFHFTKDLETLKSLCRIMDNGFRRKSSLASSPMTRATLSTASGVSLPTSSRSCSGTWSRSNSNEGWGGSGYPGLGPSRSHR