wanglab/gogpt-training-data huggingface dataset:
Protein: Pro-epidermal growth factor (Q6VQA2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MNLDGGDRRRIVSRAGRSILLDFHLSEWTMFWADTQTGQISRAGLDGTRRQKLLSSVKGITGLVVDWIENSVLWSNADEGTIQRMDTDGKNDRVVLRNLSQPRGVVVDPNERYIFWLSDGATSSIQRSDMTGKMMSTVLKVADRLKVLAVDHRDRRLFWVQQGQRGHTAMGSCNYDGNIINVFNQQFRPQSLRMTIFLDYVYLSDSKSKTITRLNKYAGGRQENVSSQRMPHSPADVKVVHPINQPVVETPFTPGCSRHTGECVKVCSSHTDTGLCGCKDGFTLSKHGNICEDVNECSLWNHGCSLGCENVPGSYFCTCPEGYLLLPDLKTCQENKPCVGKAVDCDHACVHTAQGDMCVCPEGSLLNPDGQSCTGCLSADRGGCSQMCVTLYPGRWVCECHPGYQIQPDGKHCAATGPPADLLFANIVDLRKINTDGKLSIKLLEKPGGNITAVDYDPVTNKVYFADKGLKHIERASLDEGFRELLVSTGLNSPEALAVDWIQRKLYWTDSGLSSISRSSLNGLDREIFINENIQKPRGIALHPQAQKIYWTDMGDRPAVERSGLDKDLREAVVSTGLVSPSGLAVDHGSQRLYWCDMSTSVIESANLDGSHRRVISQNQVDRPFDIAVFENVLWVSDLENHLIFRLDMRSDQNPERLLVDSIQPAALVVVHPLAKPGADVCLDGNGGCAQVCASRLGLPHCSCHTNQVLSADGKGCRMINGSFSESSEGGSNDGLRNKTLNDESTPLAMLYTEKMVSDQDDCFSLSCVVNAQCFLQEGRAVCQCVRGFTGDGELCVDVDECKAGLADCSVSEAECVNTAGGYFCQCKNGFSGDGHHCVDIDECRLDLHDCDVNAECLNAVGEYQCRCRSGFTGTGFSCQAEFNGTSLWPSTASPPDVTSTLQHKNGVQSCPSTHDSYCLYDGVCFYFPEMESYACNCVLGYMGERCQFSDLEWWELQQAEEGKRRNMVIAVCIVLLITILSIAACITFCYRPKRHFGGCSLQDSVGEMSASEDSFTETTTATPEVYVVLDTSTCTADKVLHVQSTTSTICSSCPTQTGDRFSSEEAGKLQRDGCSLAVAICSVSCDIPKILLTEKTTDNLISLEDAQSPTSSQ
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase beta chain) (SCS-beta) (P53312)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03219, ECO:0000269|PubMed:14576278}.
Interaction partners:
- 2-oxoglutarate dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b subunit
- Mitochondrial inner membrane protein SHH3
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Citrate synthase, mitochondrial
Sequence:
MYSRKSLSLISKCGQLSRLNAQAALQARRHLSIHEYRSAQLLREYGIGTPEGFPAFTPEEAFEAAKKLNTNKLVIKAQALTGGRGKGHFDTGYKSGVHMIESPQQAEDVAKEMLNHNLITKQTGIAGKPVSAVYIVKRVDTKHEAYLSILMDRQTKKPMIIASSQGGMNIEEVAERTPDAIKKFSIETSKGLSPQMAKDVAKSLGFSPDAQDEAAKAVSNLYKIFMERDATQVEINPLSEIEHDPTHKIMCTDAKFGFDDNASFRQEKIYSWRDLSQEDPDEVKAKKYDLNFVKLKGNIGCLVNGAGLAMATMDVIKLNGGDPANFLDCGGGATPETIKQGFELILSNKNVDAIFVNIFGGIVRCDYVALGLVEAARELEVRVPIVARLQGTKVEEGRDIINKSGVKIYSFDELDPAAKKVVELTQN
Protein: Large ribosomal subunit protein eL13 (60S ribosomal protein L13) (O74175)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein eL18A
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL39
Sequence:
MAIHVKGQLPNAHFHKDWQRYVKTWFNQPGRKLRRRQARQTKAAKIAPRPVEAIRPAVKPPTIRYNMKVRAGRGFTLEELKAAGVSRRVASTIGIPVDHRRRNRSEESLQRNVERIKVYLAHLIVFPRKAGQPKKGDATDVSGAEQTDVAAVLPITQEAVEEAKPITEEAKNFNAFSTLSNERAYARYAGARAAFQKKRAEEAEAKKK
Protein: Uncharacterized protein (Q38B17)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMTEHIYIYRFAFNRNIVPVVVMIFQDTSSSSVDSSEEAGTAYQRAPHGISNAARVNANGDVESDAFSGDFSSTPDNDPKMSASLTPPSHRPKTTTAMPSTKNPVSTGLPPTDGTFVLVNVKPATNGERVPAATPPGASRIEDTHVAAVSLTSSRCSDKISPRRVHQTSMTSYEALGLGYSTSGLADAPPLKNADGINQRAAYTSTAAGLDKDKMAEVTLRTLTPSRRSVSVGKNIHTAFSYAKTQGTLPEEKNSDQWYSGHPVPRSSPPMGNSIPRSANNSTRPSILNPHGSGYDGGTGAATCNSVESWRERIMWSTRPRRNSPRHTSSYNSSRAPSRLATPRAASVPVSSVGAHAHRGHHEDLARFVGAYNTPSRRFPNDIPYANRSNTDFIAWGSGVEMSHSPRYPSTPRRFKESRSYRVKHKLLDPPEPTATGLTTKDDIVDPLAELEKYQKRLERAVAIMALEREHRMLRHRR
Protein: Mec-8 protein (RRM domain-containing protein) (G5ECJ4)
Organism: Caenorhabditis elegans
Interaction partners:
- RNA-binding protein sym-2
- Basement membrane proteoglycan
- RRM domain-containing protein
- Smu-2 suppressor of mec-8 and unc-52 protein
- Smu-1 suppressor of mec-8 and unc-52 protein
- Sex determination protein fox-1
- RNA-binding protein asd-2
- Mechanosensory protein 2
- WD repeat-containing protein 44
- RRM domain-containing protein
Sequence:
MDGPKPNLASAASMESLNSVSSEATNPSQVRTLFVSGLPMDAKPRELYLLFRGCRGYEGALLKMTSKNGKPTSPVGFVTFLSQQDAQDARKMLQGVRFDPECAQVLRLELAKSNTKVARPKQSPPPPQHAALSAAAAGVPQFLAPMQHDLLLDPQSAALFNEQQLLALSLPHLHAAQALQAAYMPASALQQYSQNQLFAAAQMHPAAAAAASLQHSQQASQASTSACSTLFVANLSAEVNEDTLRGVFKAFSGFTRLRLHNKNGSCVAFVEYSDLQKATQAMISLQGFQITANDRGGLRIEYARNKMADVNG
Protein: 3-ketoacyl-CoA synthase 2 (KCS-2) (EC 2.3.1.199) (Docosanoic acid synthase) (Very long-chain fatty acid condensing enzyme 2) (VLCFA condensing enzyme 2) (Q5XEP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the synthesis of VLCFAs from 22 to 26 carbons in length (e.g. C22, C24, C26). Involved in the elongation of C20 fatty acid suberin precursors. Functionally redundant with KCS20 in the two-carbon elongation of C22 fatty acids that is required for cuticular wax and root suberin biosynthesis.
Subcellular location: Membrane {ECO:0000269|PubMed:15277688}; Multi-pass membrane protein {ECO:0000269|PubMed:15277688}.
Interaction partners:
- Protein ECERIFERUM 2
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Very-long-chain
- Very-long-chain enoyl-CoA reductase
- 3-ketoacyl-CoA synthase 6
- 3-ketoacyl-CoA synthase 9
- Very-long-chain 3-oxoacyl-CoA reductase-like protein At1g24470
- Fatty acyl-CoA reductase 3
- Cytochrome P450 86B1
- Omega-hydroxypalmitate O-feruloyl transferase
Sequence:
MNENHIQSDHMNNTIHVTNKKLPNFLLSVRLKYVKLGYHYLISNAVYILILPVGLLAATSSSFSLTDLTLLYNHLLKFHFLSSTLFAALLIFLTTLYFTTRPRRIFLLDFACYKPDSSLICTRETFMDRSQRVGIFTEDNLAFQQKILERSGLGQKTYFPEALLRVPPNPCMSEARKEAETVMFGAIDAVLEKTGVNPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNVLSYNLGGMGCSAGLISIDLAKQLLQVQPNSYALVVSTENITLNWYLGNDRSMLLSNCIFRMGGAAVLLSNRSSDRCRSKYQLIHTVRTHKGSDDNAFNCVYQREDNDDNKQIGVSLSKNLMAIAGEALKTNITTLGPLVLPMSEQLLFFATLVARKVFNVKKIKPYIPDFKLAFEHFCIHAGGRAVLDEIEKNLDLSEWHMEPSRMTLNRFGNTSSSSLWYELAYSEAKGRIKRGDRTWQIAFGSGFKCNSAVWRALRTIDPSKEKKKKTNPWIDEIHEFPVPVPRTSPVTSSSESR
Protein: Oxygenase-beta NBDO (Q8RTL3)
Organism: Comamonas sp. JS765
Interaction partners:
Sequence:
MMINTQEDKLVSAHDAEEFHRFFVGHDSDLQQEVTTLLTREAHLLDIQAYKAWLEHFVAPEIKYQVISRELRSTSERRYQLNDAVNLYNENYQQLKVRVEHQMDPQNWANNPKIRFTRFVTNVTAAKDKSAPEILHVRSNLILHRARRENQVDVFYATREDKWKRIEGGGIKLVERFVDYPERIPQTHNLLVFL
Protein: Alpha-taxilin (Q6PAM1)
Organism: Mus musculus (Mouse)
Function: May be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells.
Interaction partners:
- Syntaxin-3
- Syntaxin-4
- Syntaxin-1A
- Tumor susceptibility gene 101 protein
Sequence:
MKNQDKKNGPAKHSNSKGSPGQREAGPEGAHGRPRQTAPGAEAEGSTSQAPGKTEGARAKAAQPGALCDVSEELSRQLEDILSTYCVDNNQGGPAEEGAQGEPTEPEDTEKSRTYAARNGEPEPGIPVVNGEKETSKGEPGTEEIRASDEVGDRDHRRPQEKKKAKGLGKEITLLMQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKEFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLTAGGITDIGSERRPEATTASKEQGVESPGAQPASSPRATDAPCCSGAPSTGTAGQTGPGEPTPATA
Protein: Vacuolar protein sorting-associated protein 53 A (AtVPS53) (Protein HEAT-INTOLERANT 1) (Q0WQF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (By similarity). Required for vesicle trafficking involved in plasma membrane protein composition. Probably involved in pollen tube elongation and other polar growth. Confers basal tolerance to long-term heat stress and osmotic stress, by acclimation of the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21398432}. Golgi apparatus membrane {ECO:0000269|PubMed:21398432}; Peripheral membrane protein {ECO:0000269|PubMed:21398432}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21398432}; Peripheral membrane protein {ECO:0000269|PubMed:21398432}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localized in the GARP complex in the Golgi and post-Golgi compartments.
Interaction partners:
- Vacuolar protein sorting-associated protein 52 A
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 54, chloroplastic
- At2g27890
- Conserved oligomeric Golgi complex subunit 4
- Vacuolar protein sorting-associated protein 52 B
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 2
Sequence:
MDKSSALEYINQMFPTEASLTGVEPLMQKIQGEIRRVDASILSAVRQQSNSGTKAKEDLADATRAVEELSHKIQEIKSKAEQSEAMVQEICRDIKKLDFAKKNITTTITALHRLTMLVSAVEQLQVMASKRQYKEAAAQLEAVNQLCNHFEAYRDVPKITELREKLNNIKQILKSHVFSDFSSLGTGKETEETNLLQKLSDSCLVVDALEPSVREELVNNFCSRELTSYEQIFEGAELAKLDKTERRYAWIKRRIRTNEEIWKIFPASWHVPYRLCIQFCKQTRKQVESILVNMKEKPVVAILLLALQSTVEFEKELEKKFGGGVPTKDIEDDIEEIGTWEDNSQNISKIRKKYEKKFAASQETEENGFQQEKTGNKDLSVTGAGFNFRGMISSCFEPHLTPYIELEEKTLMDDLEKIVQEESWDVEDGSQNNVLSSSTQLFSNIKKSLKRCNTLSKNQTLFNLFKVFQRVLKAYATKLFFKLPKGGTGIVAAATGMDGQIKVSERDERVICYIVNSAEYCHKTSGELAENVSEIIDPHYADGVDMSEVQDEFSAVITKALVTLVLGLETKFDTEMAVMTRVPWSTLESVGDQSGYVNGINTVLSGSIPVLGKLLTPVYFQFFLDKLASSLGPRFYANIFRCKQLSETGAQQMLLDTQAVKSILLEIPSLARQTSTAASYSKFVSREMSRAEALLKVILSPIDSVADTYRALFPEGTPMEFQRILELKGLKKADQQSILDDFNKHGPGFTQQSVAAAMPQPMPTPPAPPLAITNPATAAGFIANSEDVLTRAAALGRGAASTGFKKFIALTEAAKDRKDGPLRRLFNA
Protein: Stretchin-MLCK (Q9NBB2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
PTAKWFFGDQPIAFGPRSKMSMQDGIAWLNLVGVTEEDAGEYTLRVRGSENEIVSTCNLFVYSTGKPEVIPPTFVVGIKDTYSLNENELVLDCRVRGQPRPEIQWIKGTEPIEASEKFKPSDQADGYAKLVIVNPTEKDSGIYWCVARNEGAENKISHQVDFKGRQHYSLEKTHGFFHRDPNKPHFLLPLGNQTVCNGGTVAISAEFMETSTPIEVKWLRDRRVVDGPNVKALADRGVYTLTIMNAGPEVEGTYTCRASNAFGRIESNVNVDVAVGAEKDERPPLFLSRPDTEMKIAVGDPFSLSFRIAGDPKPKLTFMKGTKDITQSDRVSKEVSDDYTRFSVQQAQISDFGTYXXVXRNXFXXDRIFVTXXXXIPXKEGGXXXXIXYNLFCKFRTPPSSSKHQIQITIISYLAHLSFLS
Protein: Epsilon-sarcoglycan (Epsilon-SG) (O70258)
Organism: Mus musculus (Mouse)
Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Subcellular location: Cell membrane, sarcolemma {ECO:0000269|PubMed:17200151}; Single-pass membrane protein {ECO:0000269|PubMed:17200151}. Golgi apparatus {ECO:0000269|PubMed:17200151}. Cell projection, dendrite {ECO:0000269|PubMed:17200151}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Delta-sarcoglycan
- Zeta-sarcoglycan
- Gamma-sarcoglycan
- Sarcospan
- Dystroglycan 1
- Beta-sarcoglycan
- Dystrophin
- Utrophin
- Dystrobrevin alpha
- Retrotransposon-derived protein PEG10
Sequence:
MLLFWWWELGDPCAWTGKGRGTLKMSPATTGTFLLTVYTLFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEVSNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEEFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDMKEGVYVMVGADVAFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTHFHIDWCKISLVDKTKQVSTYQEVVRGEGILPDGGEYKPPSDSLKSRDYYTDFLVTLAVPSAVALVLFLILAYIMCCRREGVEKRDMQTPDIQLVHHSSIQKSTKELRDMSKNREIAWPLSTLPVFHPVTGEVIPPTHTDNYDSTNMPLMQAQQNLPHQTQIPQPQTTGKWYP
Protein: Optineurin (Q8K3K8)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation. In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15607428}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- Ras-related protein Rab-8A
- Gamma-aminobutyric acid receptor-associated protein
- Microtubule-associated protein 1 light chain 3 beta
- TRAF family member-associated NF-kappa-B activator
- Gamma-aminobutyric acid receptor-associated protein-like 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Calcium-binding and coiled-coil domain-containing protein 2
- Ras-related protein Rab-11A
- Inhibitor of nuclear factor kappa-B kinase subunit beta
Sequence:
MSHQPLSCLTEKGDSPCETPGNGPSNMVHPSLDTFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLKEELGKFKEKSEKPLEDLTGGYRYPRALEEEVEKLKTQVEQEVEHLKIQVMRLRAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGETEGAMKEMKNCPTPTRTDPISLSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQCRHGARTSDSDQQTYLFQRGAEDRSWQHGQQPRSIPIHSCPKCGEVLPDIDTLQIHVMDCII
Protein: Oligosaccharyltransferase (G1FG65)
Organism: Neisseria meningitidis
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPAETTVSGAHPAAKLPIYILPCFLWIGIVPFTFALKLKPSPDFYHDAAAAAGLIVLLFLTAGKKLFDVKIPAISFLLFAMAAFWYLQARLMNLIYPGMNDIVSWIFILLAVSAWACRSLVAHFGQERIVTLFAWSLLIGSLLQSCIVVIQFAGWEDTPLFQNIIVYSGQGVIGHIGQRNNLGHYLMWGILAAAYLNGQRKIPAALGVICLIMQTAVLGLVNSRTILTYIAAIALILPFWYFRSDKSNRRTMLGIAAAVFLTALFQFSMNTILETFTGIRYETAVERVANGGFTDLPRQIEWNKALAAFQSAPIFGHGWNSFAQQTFLINAEQHNIYDNLLSNLFTHSHNIVLQLLAEMGISGTLLVAATLLTGIAGLLKRPLTPASLFLICTLAVSMCHSMLEYPLWYVYFLIPFGLMLFLSPAEASDGIAFKKAANLGILTASAAIFAGLLHLDWTYTRLVNAFSPATDDSAKTLNRKINELRYISANSPMLSFYADFSLVNFALPEYPETQTWAEEATLKSLKYRPHSATYRIALYLMRQGKVAEAKQWMRATQSYYPYLMPRYADEIRKLPVWAPLLPELLKDCKAFAAAPGHPEAKPCK
Protein: proton-translocating NAD(P)(+) transhydrogenase (EC 7.1.1.1) (P96832)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- NAD
- proton-translocating NAD
- Probable soluble pyridine nucleotide transhydrogenase
- NAD kinase
- NAD-dependent protein deacylase
- Glutamine-dependent NAD
- Probable nicotinate-nucleotide adenylyltransferase
- Possible transcriptional regulatory protein NadR
- NAD-capped RNA hydrolase NudC
Sequence:
MTDPQTQSTRVGVVAESGPDERRVALVPKAVASLVNRGVAVVVEAGAGERALLPDELYTAVGASIGDAWAADVVVKVAPPTAAEVGRLRGGQTLIGFLAPRNADNSIGALTQAGVQAFALEAIPRISRAQVMDALSSQANVSGYKAVLLAASESTRFFPMLTTAAGTVKPATVLVLGVGVAGLQALATAKRLGARTTGYDVRPEVADQVRSVGAQWLDLGISASGEGGYARELTDDERAQQQKALEEAISGFDVVITTALVPGRPAPTLVTAAAVEAMKPGSVVVDLAGETGGNCELTEPGRTVVKHDVTIAAPLNLPATMPEHASELYSKNITALLDLLIKDGRLAPDFDDEVIAQSCVTRGKDS
Protein: Outer spore wall protein 6 (Increased recombination centers protein 18) (P47056)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in spore wall assembly.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Outer spore wall protein LDS2
- Outer spore wall protein 7
- Outer spore wall assembly protein SHE10
- Ectonucleotide pyrophosphatase/phosphodiesterase 2
- Outer spore wall protein 2
- Outer spore wall protein RRT8
- Ectonucleotide pyrophosphatase/phosphodiesterase 1
- Subtilase-type proteinase RRT12
Sequence:
MKVQMIERIFLIQLCLLTVVLASSRAVVEFESTGTKLVNSLRVLAAYSQSSVCVDEKISGIERQIEEVKDMYGNHSFILKGLNGILNNKVNMLTREIQMETVGNNTFETETGKLTKGLNRAVNISPFKYIKKFKTVSTKKFESLLNKYDLVAKKGGELTEEQKKKKEVLSRISRVVAATTIEAGLAQGVVDLCITVTTSLCLVSASIGGVGFLIWLTIIYQALT
Protein: 26S proteasome regulatory subunit 7 (Proteasome 26S subunit ATPase 2) (Q7KMQ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome regulatory subunit 8
- Proteasome subunit alpha type-2
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 8
- Proteasome subunit alpha type-5
Sequence:
MPDYLGDDQRKVKHDEKEDKEIKSLDEGDIELLKTYGQSQYHKSIKSIEEDIQKAVKQVNELTGIKESDTGLAPPALWDLAADKQILQNEQPLQVARCTKIINADSDDPKYIINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEDKPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAVKKVIKSYAKFSATPRYMTYN
Protein: Uncharacterized protein (Q57WR0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MNNANDTLDYSGNTSSTYSAAVNEEFLTPTRRTHVSVSTSHVSSSEADFVTGSMVDDEEYYNEYTSGYESRVYTHASFTYDEFSSGSPNSDDLSSTFMSYYIDSVIGQKTRYFFSVLRKPIVFFSLILPGSNFVGSLGRLVYAVTVSASRRTAVNYSMGVETLCVLPKGYGHMPEHLQRARLALPSFVEYFAKMLLRLSGVPSLADLQKRKWLETVRILKSATGEIISQSAHRSSGPMIPLAVFLPVFSLSVITIARGVISRQQTYNEYEEDEDVAYEAAHSGSYKGVAASRGLDALQLSGLDDSFPNLGSEKSNEVNYSGVETPKGSPPAPELFPSPKPQGERHAPSETQTNPQTVPTSRDLSPDSSAVGDEFKLIMSPTSEDPGRAPSAASREAVRHPKQYDLRGDVVIALTGEPSPQEVDVLLMAAAKYKCRRVILPSLVADTALASVHPLVDVVKVSDVMEHVMSVEESEGRTTVGVFLRPVTDETEELRLFTHPTSVVYIFVPAAFLEANVIAHLVDRSVYYSASLDEPFPINVCLYDRLTKERREGA
Protein: Period3 circadian clock protein (Q9I8L4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPGGDGFPDGEQENSSPGPDIHTGQTDQTSSGQDPGTSGNISASGEEEEAEERIGRRSSGCEESGGEQTHEDVDMNSTHTSSSGNDSIHHRHHHHHRHHHHHHHHSSSNCSPGSTTGSGSTKSSKSATGSSSSSFHSTHHTECGEQTETGREHTHREMMHTVQEMKKRLPSEKRSRSKASTVEALHYALNCVKQVQANSEYYNLLMSSGLDERRDATVCTLEELEGFTSEHTLKNTDSFVVVFSLASGKVVYASEQASSVLHCKRKFLESAKFVEMLYHQDVNVFYSHTAQPRLPSWNLGTDSAAVLFECAQVKSFFCRIRGGKDRDGDMRYSPFRITPYLLKVQGSSGEEEPCCLALAERIISGYEAPRIPMDKRIFSTTHSPGCVFLEVDDRAVPLLGYLPQDLIGTSVLTCLHPDDRLLMLAMHRKIVKYAGQPPFEHSPIRFRCQNGDYVTLDSSWSSFINPWSRKVAFIIGRHKVRTGPLNEDVFAARSKADQPVMCEDVKELQAMIHKLFLQPVHNNGSSGYGSLGSNGSHEHYISVASSSDSNGNLWEDSHRETMTLQQFCADVNKVKNWGQQAYLESRKKLTALGPATAVAGAGVHASSSHDLGIRDHLKQSLQKARKQPHIPSYQQINCVDSIIRYLESCATSALKRKCESLSITTSSSSSTSEEDKPTAAAHENTDEAALDAARALDSQVSAGSATTAAVVGAPLTDITISTEAMSVVSVTSQCSYSSTIVHVPQPESEVTALEDAPMGSEPADSAPAPASPAHDSGSASTSQEELLVLGLTKEVLSAHTQKEEQQFVDRFRHRIVQSPYSSYLQQDNSSNAHSHHRGDVVRQPNKHKRPKPEDSSDSYECSQPGNYWSLPGPTAAPHSSWPSSESSQPPPSNIGFVPPMAVPMQTPPYFNIIGADQQPVMLQPDPGVQNLQPMTPMMVVLLPSFPMYPPNNGMYFPMAAPGVVPYNIGGFVPPGTPMPAEAPLQGHNLESAGVGVPAEPDSIPEPWFGEDLDAAQPTALFSSSRSSSPIQLNLLQEELTKPSEAQTSTNADSLHEHHTKTDDARSECGHQDAHSSSSEMLDQLLQEDARSGTGSNASGSGSGESGGSLGSGSGLGSNGTSTSHTGSSNSSKYFASNDSSDTSRKARKSAEAQERERSGFKKHVDDPLWSMIKQTPEPVMLTYQISSRDQAQVLQEDREKLILMQPMQPWFTSDQKKELAEVHPWIQQNTVPQEINTQGCVSCNTIEPNEKLNLQTDSPNPPDISCPQDCPPQENRPDTDT
Protein: E3 ubiquitin-protein ligase TM129 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TM129) (A0AVI4)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase involved in ER-associated protein degradation, preferentially associates with the E2 enzyme UBE2J2. Exploited by viral US11 proteins to mediate HLA class I proteins degradation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24807418}; Multi-pass membrane protein {ECO:0000269|PubMed:24807418}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 J2
- Derlin-1
- Transitional endoplasmic reticulum ATPase
- Selenoprotein S
- Peroxisomal ATPase PEX6
- Serine/threonine-protein kinase H1
- E3 ubiquitin-protein ligase RNF139
Sequence:
MDSPEVTFTLAYLVFAVCFVFTPNEFHAAGLTVQNLLSGWLGSEDAAFVPFHLRRTAATLLCHSLLPLGYYVGMCLAASEKRLHALSQAPEAWRLFLLLAVTLPSIACILIYYWSRDRWACHPLARTLALYALPQSGWQAVASSVNTEFRRIDKFATGAPGARVIVTDTWVMKVTTYRVHVAQQQDVHLTVTESRQHELSPDSNLPVQLLTIRVASTNPAVQAFDIWLNSTEYGELCEKLRAPIRRAAHVVIHQSLGDLFLETFASLVEVNPAYSVPSSQELEACIGCMQTRASVKLVKTCQEAATGECQQCYCRPMWCLTCMGKWFASRQDPLRPDTWLASRVPCPTCRARFCILDVCTVR
Protein: Acetolactate synthase catalytic subunit, mitochondrial (EC 2.2.1.6) (Acetohydroxy-acid synthase catalytic subunit) (AHAS) (ALS) (P07342)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of mitochondrial acetolactate synthase, which catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:10213630}.
Interaction partners:
- Acetolactate synthase small subunit, mitochondrial
- Ketol-acid reductoisomerase, mitochondrial
- Dihydroxy-acid dehydratase, mitochondrial
- 2-isopropylmalate synthase
- Threonine dehydratase, mitochondrial
- 3-isopropylmalate dehydrogenase
- Branched-chain-amino-acid aminotransferase, cytosolic
- 3-isopropylmalate dehydratase
- 2-isopropylmalate synthase 2, mitochondrial
- Catabolic L-serine/threonine dehydratase
Sequence:
MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH