wanglab/gogpt-training-data huggingface dataset:
Protein: 2-methyl-aconitate isomerase (EC 5.3.3.-) (Cis-trans isomerase) (Q8EJW4)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle II (propionate degradation route). PrpF catalyzes the cis-trans isomerization of 2-methyl-aconitate through a base-catalyzed proton abstraction coupled with a rotation about C2-C3 bond of 2-methyl-aconitate.
Interaction partners:
- 2-methylcitrate dehydratase
- 2-methylisocitrate lyase
- Aconitate hydratase B
- 2-methylcitrate synthase
- Propionyl-CoA synthetase PrpE
- Methycitrate-responsive transcriptional regulator of methylisocitrate utilization PrpR
- Diaminopimelate epimerase
- GMP synthase
Sequence:
MSNKLFPPQIKVAATYMRGGTSKGVFFRLQDLPEAAQVPGPARDALLLRVIGSPDPYAKQIDGMGGATSSTSKTVILSHSSKANHDVDYLFGQVSIDKPFVDWSGNCGNLTAAVGAFAISNGLIDAARIPRNGVCTVRIWQANIGKTIIAHVPITDGAVQETGDFELDGVTFPAAEVQIEFMNPAADDDGEGGCMFPTGNLVDVLEVPGIGRFNATMINAGIPTIFINAEDLGYTGTELQDDINSDNAALAKFETIRAHGALRMGLIKHIDEAASRQHTPKIAFVAPPKSYASSSGKTVAAEDVDLLVRALSMGKLHHAMMGTAAVAIGTAAAIPGTLVNLAAGGGEKEAVRFGHPSGTLRVGAQAVQENGEWTVIKAIMSRSARVLMEGFVRVPKP
Protein: Uncharacterized protein (Q389Q1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRNSLRLRLSSTSSSLLRSTFWLRQCGSGGCGFSGGPGGYPTDADALAKILTQAKKGSFNGSSSSPSDFFDGRFVGGSPTMDPAMLQDMHQKLNQSLTPEVRESMKAMMESIQRGDGMPQMGMMAFGVGENEKGKKVARGAKLMFDPSTGKLSKDFVEKQLEDDDPVLPKETVGDYNTEGAIEVEFEEDARKEASVRENIPEAEVIVEEVPREK
Protein: NADH-cytochrome b5 reductase (EC 1.6.2.2) (B5XEF8)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00037811}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037811}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037811}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00037821}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037821}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037821}.
Interaction partners:
Sequence:
MLSYIIGLIRSSIGNIINLILSLFLSKKKRAITLEDPNIKYALKLIDKEIISHDTRKFRFALREKDCVLGLPIGQHIYLSAKPDGVLVVRPYTPVSSDDDVGFVDLVVKIYYKNVNPKFPEGGKMSQYLESIRIGDTIDFRGPSGLLVYQGNGAFAIKAEKKAEPVIKTAKQVGMIAGGTGITPMLQLITAIMKDPQDQTVCHLLFANQTEKDILLRPELEEIAANHPTRFKLWFTLDWEYSQGFISEEMVRDHLPPPGDDTLILLCGPPPMIQFACNPNLDKVGHASSRRFTF
Protein: Protein EXPORTIN 1B (F4IZR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor for the leucine-rich nuclear export signal (NES). Binds cooperatively to the NES on its target protein and to the small GTPase Ran in its active GTP-bound form (By similarity). Required for the maternal-to-embryonic transition and during gametophyte development.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9TVM2}. Nucleus membrane {ECO:0000250|UniProtKB:Q9TVM2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9TVM2}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9TVM2}.
Interaction partners:
- GTP-binding nuclear protein Ran-3
- GTP-binding nuclear protein Ran-1
- GTP-binding nuclear protein Ran-2
- GTP-binding nuclear protein Ran-4
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP214
- Snurportin-1
- Protein EXPORTIN 1A
- Zinc finger CCCH domain-containing protein 16
- At4g27240
Sequence:
MAAEKLRDLSQPIDVVLLDATVEAFYSTGSKEERASADNILRDLKANPDTWLQVVHILQNTSSTHTKFFALQVLEGVIKYRWNALPVEQRDGMKNYISDVIVQLSRDEASFRTERLYVNKLNIILVQIVKQEWPAKWKSFIPDLVIAAKTSETICENCMAILKLLSEEVFDFSKGEMTQQKIKELKQSLNSEFQLIHELCLYVLSASQRQELIRATLSALHAYLSWIPLGYIFESPLLEILLKFFPVPAYRNLTLQCLSEVASLNFGDFYDMQYVKMYSIFMNQLQAILPLNLNIPEAYSTGSSEEQAFIQNLALFFTSFFKLHIKILESAPENISLLLAGLGYLISISYVDDTEVFKVCLDYWNSLVLELFGTRHHACHPALTPSLFGLQMAFLPSTVDGVKSEVTERQKLYSDPMSKLRGLMISRTAKPEEVLIVEDENGNIVRETMKDNDVLVQYKIMRETLIYLSHLDHEDTEKQMLSKLSKQLSGEEWAWNNLNTLCWAIGSISGSMVVEQENRFLVMVIRDLLSLCEVVKGKDNKAVIASNIMYVVGQYSRFLRAHWKFLKTVVHKLFEFMHETHPGVQDMACDTFLKIVQKCKRKFVIVQVGESEPFVSELLSGLATIVGDLQPHQIHTFYESVGSMIQAESDPQKRGEYLQRLMALPNQKWAEIIGQARQSADILKEPDVIRTVLNILQTNTRVATSLGTFFLSQISLIFLDMLNVYRMYSELVSSSIANGGPYASRTSLVKLLRSVKREILKLIETFLDKAENQPHIGKQFVPPMMDQVLGDYARNVPDARESEVLSLFATIINKYKVVMRDEVPLIFEAVFQCTLEMITKNFEDYPEHRLKFFSLLRAIATFCFRALIQLSSEQLKLVMDSVIWAFRHTERNIAETGLNLLLEMLKNFQKSDFCNKFYQTYFLQIEQEVFAVLTDTFHKPGFKLHVLVLQHLFSLVESGSLAEPLWDAATVPHPYSNNVAFVLEYTTKLLSSSFPNMTTTEVTQFVNGLYESRNDVGRFKDNIRDFLIQSKEFSAQDNKDLYAEEAAAQMERERQRMLSIPGLIAPSEIQDDMADS
Protein: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase (EC 4.3.1.32) (FO synthase subunit 1) (Q57888)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.
Interaction partners:
- 5-amino-6-
- 2-phospho-L-lactate transferase
- 2-phospho-L-lactate guanylyltransferase
- Coenzyme F420:L-glutamate ligase
- Phosphomethylpyrimidine synthase
- Tetrahydromethanopterin S-methyltransferase subunit B
- Tetrahydromethanopterin S-methyltransferase subunit C
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- DNA/RNA-binding protein Alba
- 2-
Sequence:
MISREEAINFLNSTSSKDILDKLAQINNTFKREYITYSKNVFIPLSKWCRNKCGYCIFREDKPSLMKPNEVKEILLKGDRLGCREALFTFGEHVDENKEIKEQLKSMGYDNILEYLYDLEEWTLNNTSLLPHTNCGILNYDELKMLKDVNASMGLMLENASERLMNTIAHKHSPGKHPKLRIEMIENAGKLKIPFTTGLLIGIGETNEEIVDSLFKIKEIHEKYGHIQEVIIQNFRAKKGIPMENFKEPSPIKMLKVIILAKLILDDISIQIPPNLNRETGQLFLLAGVDDWGGVSPLTRDYVNPEAEWPEIKELREWTEELGLKLKMRLPVYDKYISEEWLSEKVYNKIIEMGWLKE
Protein: WASP like actin nucleation promoting factor a (Zgc:158395 protein) (A2RUY4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGHPPPRRVANVGSLLLTPQENDCLFNYLGRKCITLCSAVVQVYGADRGSSWAKRCCGVACLVKDNPQRSYFIRVFDIKDGKTKFEQELYNNFAINSSRAYFITFAGDSCQMGLNFASEEEAKRFRSALNELLNRRQRKTEKRRDPPNGPTLPMATVDIKNPEINNMRFHNNSHVNNMVHSGLNKKEKKVKGKRKKLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDKETSKVIYDFIEKKGGVEAVKNELRRQAPPPPPSRGGPPPPPPPHTSGPPPPPPPVRGRGAPPPPPPSRAPTSAPPPPPPSRPSMGAPPPPPPSRGHPPPPPPAPASMPPPPPPPPMSGGAAPPPPPPPPPPPGPPPPSEMDGGHGESTPPPAGGKSALLEQIREGTQLKKVEQNNRPVSSTGRDALLDQIRQGIQLKTVSDNDSGPPTPAQSAGIVGALMEVMQKRSKAIHSSDEDEDDDEDEDFEDDDEWDD
Protein: Zinc-regulated GTPase metalloprotein activator 1 (EC 3.6.5.-) (Cobalamin synthase W domain-containing protein 1) (COBW domain-containing protein 1) (B0R0B1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1 to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8VEH6}.
Interaction partners:
- Methionine aminopeptidase 1
- Large ribosomal subunit protein bL33m
- Novel protein similar to vertebrate mitochondrial ribosomal protein S14
- Solute carrier family 30 member 10
- Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
- Small ribosomal subunit protein uS14
- Zgc:162634.
- FAM3 metabolism-regulating-signaling molecule A
- Uricase
- Proton-coupled zinc antiporter SLC30A5
Sequence:
MEDEDECPELVPIKEKPSGPTAQIPVTIITGYLGAGKTTLLNYILTEQHNKRIAVILNEFGEGSALEKSLAVSQAGELYEEWLELRNGCLCCSVKDNGLKAIENLMEKKGKFDYILLETTGLADPGAVASMFWVDAELGSDVYLDGIVTVIDAKYGLQHLTEEKPEGLINEAARQIALADLTIINKTDLVHETELLKLRDTVRSINALVKILETQKSRVDLSEVLDLHSFDTKDGERLTKKLQLVKTSQPHLDKSMLTITFEVPGSVSEDLLNIFIQELLWEKTFKNKAGLPMTVIRLKGILSLQQKQKKVMLQGVHELYELEETPEFWADQEPRLNRLVFIGRNLDGEILKKEFISAVSNKDSVE
Protein: Uncharacterized protein ANR2 (AVL9-related family protein 2) (P36090)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in lipid metabolism.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:24868093}.
Interaction partners:
- Endonuclease NBR9
- Serine/threonine-protein kinase ENV7
- Protein SNA4
- Palmitoyltransferase AKR1
Sequence:
MNSGGEEPTIKPNVFNITQLLNSNGEKPGIACIFLSKFDMKKGNIIIWSKSINGAAIDLSNIEFKSLPAGIHEQTDDVVNFVVPKELDVCQTAKTTTYDYGIAYFKQNSFDIIENDNRIDRSKVQMFSLGVIIDVQNASSDSKKHFYKEIYHAYAANRYSSYLESLLGQWIRQRDLDKFDIFEKFFDENNQGHMAENSVEVFEHSPKERRHLVEYLPYWTRKLGPLIFPLWKASLLQSRILILVPQGESFELCNSLAYCVFLISMLPKNLIGNHVSDEYIKPIFTVSTSDIPFLESFKKGNGYVATTSEEILLYKPEIYDIVVKLTSSSTIEESPEKEVEILTASGEQNKATPLDLEVYEKLILGELQEDASTNATCRHHEVTEPISWLQFLIDGFFLLTTAGYLVAPYHLANNFKIPRHVSGPEPNNSEIQIAENLVRYFHRRTSNLYNDLKDVIQKSENIDSEQPITIAASFLTKLNLDCFSKQDHQFVKDIALKWFQRSIDISNLPECLGNLC
Protein: Guanine nucleotide-binding protein-like 3 N-terminal domain-containing protein (Q388B9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pescadillo homolog
- Ribosome biogenesis protein BOP1 homolog
- NLE domain-containing protein
- rRNA processing protein, putative
- Nucleolar GTP-binding protein 1
- RNA-binding protein, putative
- Nucleolar complex protein 2
- Nucleolar protein, putative
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein NSA2 homolog
Sequence:
MPKVKSGASKRVTSRQRHKVERKKREHKRDLRKAAKAMKKSGLGPKRTKRTRELARLALKVSNAHPDKESILRRVLQVREEARVERGRQKGKNKEDSDHEAAKNVGKSTKVKEGKKCFTFIPVSESNNFSYQFNRTLMELVFPTSETSTEVPSVAYVVTLDARCAVQCLPWGLLDAIVREGNAYRNAGGKRKILVLFALTKCDLVSVHALISQISLLAHVLSEQYIGVSDGDDDLNIGDSIYFTFCLVSNRFEKTVHHLSTLLKRFRASNGCSKYNNKSNLNGKICCFVIGLPNTGRRTLCRMLFQHDDSNTSIVPVSAAQLQVVNGPTNESCEGHVKFAFPNAKEVTVLQFPEDATLKRELFNLCGSEVIFKPQTFIESLADPEVVGHVLYEAVMNKDDLAQGFCQPNECNSDTTSERKEFYAARRFFTRLGQTVRREKGFYVSPSLVSNAGTMSRMCSSSLTASTTFTSCQQSTQNAPPDASYSNATPNRLVRISSVVSRRNGKRGCTTPMKRADYRNVLKLGARTFIREIHHGRNVPWAVMRSPLKDCLTLSDVERASTIFNLSLCLGKAVGSAEDAKSPSEHLTALLDHVASQMKQYLVLLPNSVVEFSPSSIVAPIHKLGFTRENEGGSNGCGDEDEEIEDYCEGEEECEDDDEQDEGDDEENEDESEEGEDDRSC
Protein: Cysteine and glycine-rich protein 3 (Cysteine-rich protein 3) (CRP3) (LIM domain protein, cardiac) (Muscle LIM protein) (P50462)
Organism: Mus musculus (Mouse)
Function: Positive regulator of myogenesis. Acts as cofactor for myogenic bHLH transcription factors such as MYOD1, and probably MYOG and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3 isoform E47 complex and may promote formation of a functional MYOD1:TCF3 isoform E47:MEF2A complex involved in myogenesis (By similarity). Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation. The role in regulation of cytoskeleton dynamics by association with CFL2 is reported conflictingly. Proposed to contribute to the maintenance of muscle cell integrity through an actin-based mechanism. Can directly bind to actin filaments, cross-link actin filaments into bundles without polarity selectivity and protect them from dilution- and cofilin-mediated depolymerization; the function seems to involve its self-association (By similarity). In vitro can inhibit PKC/PRKCA activity. Proposed to be involved in cardiac stress signaling by down-regulating excessive PKC/PRKCA signaling.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P50463}. Cytoplasm {ECO:0000269|PubMed:18258855}. Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18258855}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:P50461}. Note=Nucleocytoplasmic shuttling protein (By similarity). Mainly cytoplasmic. In the Z line, found associated with GLRX3 (via C-terminus). {ECO:0000250|UniProtKB:P50463, ECO:0000269|PubMed:18258855}.
Interaction partners:
- Telethonin
- Titin
- Myozenin-2
- Myosin light chain 3
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Alpha-actinin-2
- Myosin-binding protein C, cardiac-type
- Myopalladin
- Troponin T, cardiac muscle
- Troponin I, cardiac muscle
Sequence:
MPNWGGGAKCGACEKTVYHAEEIQCNGRSFHKTCFHCMACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGFGQGAGCLSTDTGEHLGLQFQQSPKPARAATTSNPSKFSAKFGESEKCPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTNVTDKDGELYCKVCYAKNFGPTGIGFGGLTQQVEKKE
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 3 (BLOC-1 subunit 3) (Reduced pigmentation protein) (Q5U5M8)
Organism: Mus musculus (Mouse)
Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15265785}.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- SNARE-associated protein Snapin
- Dysbindin
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- BLOC-2 complex member HPS3
- BLOC-2 complex member HPS6
- BLOC-2 complex member HPS5
Sequence:
MESSQGRRRRPGTVVPGEAAETDSELSASSSEEELYLGPSGPTRGRPTGLRVAGEAAETDSEPEPEPTVVPVDLPPLVVQRDPAETWGTEETPAMAPARSLLQLRLAESQTRLDHDVAAAVSGVYRRAGRDVAALAGRLAAAQATGLAAAHSVRLARGDLCALAERLDIVAGCRLLPDIRGVPGMEPEQDPGPRA
Protein: ATP synthase, epsilon chain, putative (EC 3.6.3.-) (Q586H1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- ATP synthase F1 subunit gamma protein, putative
- ATP synthase alpha chain
- ATPase subunit 9, putative
- ATP synthase subunit beta
- Uncharacterized protein
- ATPase subunit 9, putative
- ATPase subunit 9, putative
- ATP synthase delta chain
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MFRTFGRRLVSCTLPLLQSAPHDLPEGFEFMEHKVVNKDIHAPHENLETLRLTLTRQDEFLLREEPVKCVTVTGTNGEYGIYPGHAYKIVQLNPSPLTVEYTDGTTKKYFVSGGFAHINNEGSCDVNTVECTLLDDLDLAIAEKELAAQQAALGSAKDDKAKSVVEIRISVIEAVIAALKHH
Protein: Carbonic anhydrase (EC 4.2.1.1) (Q9V396)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH06388p
- GH03305p
- Cytosol aminopeptidase
- Carbonic anhydrase
Sequence:
MSHHWGYTEENGPAHWAKEYPQASGHRQSPVDITPSSAKKGSELNVAPLKWKYVPEHTKSLVNPGYCWRVDVNGADSELTGGPLGDQIFKLEQFHCHWGCTDSKGSEHTVDGVSYSGELHLVHWNTTKYKSFGEAAAAPDGLAVLGVFLKAGNHHAELDKVTSLLQFVLHKGDRVTLPQGCDPGQLLPDVHTYWTYEGSLTTPPCSESVIWIVFKTPIEVSDDQLNAMRNLNAYDVKEECPCNEFNGKVINNFRPPLPLGKRELREIGGH
Protein: Replication factor C subunit 1 (Activator 1 140 kDa subunit) (Activator 1 subunit 1) (Germline transcription factor 1) (Replication factor C large subunit) (P35600)
Organism: Drosophila melanogaster (Fruit fly)
Function: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit binds to the primer-template junction (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Replication factor C subunit 2
- Replication factor C subunit 3
- Replication factor C subunit 2
- Activator 1 subunit 5
- Proliferating cell nuclear antigen
- Proliferating cell nuclear antigen 2
- Rad17
- DNA polymerase alpha subunit B
- Replication protein A 70 kDa DNA-binding subunit
- Flap endonuclease 1
Sequence:
MQRGIDSFFKRLPAKAKSAEAENGETPSKAPKRRKAVIISSDEDEVVSPPETKKRKASKTASSEDDVVAATPEPIAKKARNGQKPALSKLKRHVDPTELFGGETKRVIVPKPKTKAVLEFENEDIDRSLMEVDLDESIKEAAPEKKVHSITRSSPSPKRAKNSSPEPPKPKSTKSKATTPRVKKEKPAADLESSVLTDEERHERKRASAVLYQKYKNRSSCLNPGSKEIPKGSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGPKKLAVAEELNIPILSEDGLFDLIREKSGIAKQVKEEKKSPKKEHSSEEKGKKEVKTSRRSSDKKEKEATKLKYGEKHDIAKHKVKEEHTSPKETKDKLNDVPAVTLKVKKEPSSQKEHPPSPRTADLKTLDVVGMAWVDKHKPTSIKEIVGQAGAASNVTKLMNWLSKWYVNHDGNKKPQRPNPWAKNDDGSFYKAALLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKRLLKDEVSTLLSNKSLSGYFTGQGQAVSRKHVLIMDEVDGMAGNEDRGGMQELIALIKDSSIPIICMCNDRNHPKIRSLVNYCYDLRFQRPRLEQIKGKIMSICFKEKVKISPAKVEEIIAATNNDIRQSINHIALLSAKEDASQKSGQQVATKDLKLGPWEVVRKVFTADEHKHMSFADKSDLFFHDYSLAPLFVQQNYLQVLPQGNKKDVLAKVAATADALSLGDLVEKRIRANSAWSLLPTQAFFSSVLPGEHMCGHFTGQINFPGWLGKNSKSGKRARLAQELHDHTRVCTSGSRLSVRLDYAPFLLDNIVRPLAKDGQEGVPAALDVMKDYHLLREDLDSLVELTSWPGKKSPLDAVDGRVKAALTRSYNKEVMAYSYSAQAGIKKKKSEAAGADDDYLDEGPGEEDGAGGHLSSEEDEDKDNLELDSLIKAKKRTTTSKASGGSKKATSSTASKSKAKAKK
Protein: Transmembrane protease serine 11D (EC 3.4.21.-) (Adrenal secretory serine protease) (AsP) (Airway trypsin-like protease) (AT) [Cleaved into: Transmembrane protease serine 11D non-catalytic chain; Transmembrane protease serine 11D catalytic chain] (Q8VHJ4)
Organism: Rattus norvegicus (Rat)
Function: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides (By similarity). Isoform 2 may play a key role in regulating adrenal proliferation by specifically cleaving N-POMC.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Transmembrane protease serine 11D catalytic chain]: Secreted {ECO:0000250}. Note=Activated by cleavage and secreted. {ECO:0000250}.
Interaction partners:
Sequence:
MYRPRSMVSPSRFFNPFMVALIVIITVGLLAMTAGLLIHFLAFDKRAYFYHSNFHILNVDYTEALNSPATHEYRTLSERIESMITDAFRESNLRSEFIRTHVVKLRKEGSGVVADVVMKFRSSKRNNKKAIKTRIQSVLQRLSSSGNLEIAPSNGITSLTDQDTENVLTQECGARPDLITLSEERIIGGTQAETGDWPWQVSLQLNNVHHCGGTLISNLWVLTAAHCFRSYSNPQQWTATFGVSTISPRLRVRVRAILAHAEYNSITRDNDIAVVQLDRPVTFTRNIHRVCLPAATQNIMPDSVAYVTGWGSLTYGGNTVTNLQQGEVRIVSSEVCNEPAGYGGSVLPGMLCAGVRSGAVDACQGDSGGPLVQEDTRRLWFVVGIVSWGYQCGLPNKPGVYTRVTAYRNWIRQQTGI
Protein: Dybowskin-2CDYa (B5A9T1)
Organism: Rana dybowskii (Dybovsky's frog) (Korean brown frog)
Function: Antimicrobial peptide. Has activity against the Gram-positive bacterium S.aureus (MIC=6 uM) and the Gram-negative bacterium E.coli (MIC=3 uM). Lacks hemolytic activity against human erythrocytes.
Subcellular location: Secreted {ECO:0000250|UniProtKB:B5A9S9}.
Interaction partners:
Sequence:
MFTLKKSLLLLFFIGVIKLSLCEEERNADDDERRDDPDEMDVEVENRSAVGRHGRRFGLRKHRKH
Protein: Branched-chain-amino-acid aminotransferase, cytosolic (BCAT(c)) (EC 2.6.1.42) (P24288)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P54690}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Cystathionine gamma-lyase
- L-amino-acid oxidase
- Amine oxidase
- Glutamate--cysteine ligase regulatory subunit
- Glutamate--cysteine ligase catalytic subunit
- Amine oxidase
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Serine dehydratase-like
Sequence:
MKDCSNGCSAPFAGERGSEEVAETFRAKDLIITPATVLKEKPDPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRQSILELAQQWGEFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPKLASRILGKLTDIQYGRVESDWTIELP
Protein: Glutamine synthetase inactivating factor IF7 (A0A068MVV3)
Organism: Synechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714))
Interaction partners:
- Glutamine synthetase inactivating factor IF17
- Small heat shock protein
- Phycobilisome degradation protein NblA
- Transcriptional regulator, Crp/Fnr family
- Acid phosphatase
- DUF4168 domain-containing protein
Sequence:
MSTQQQARALMMRHHQFIKNRQQSLLSRAAAEIGVQAEKDFWTTVQGKPQSSFRETYDRSSASLS
Protein: DNA topoisomerase 1 (EC 5.6.2.1) (DNA topoisomerase I) (P30189)
Organism: Drosophila melanogaster (Fruit fly)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex (By similarity). Introduces a single-strand break via transesterification at a target site in duplex DNA (By similarity). The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand (By similarity). The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils (By similarity). Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10885744}. Cytoplasm {ECO:0000269|PubMed:10885744}. Note=During early cell divisions of developing embryos, it is detected in the nucleus at interphase then diffusely dispersed in the cytoplasm at metaphase. {ECO:0000269|PubMed:10885744}.
Interaction partners:
- DNA topoisomerase 2
- Tyrosyl-DNA phosphodiesterase 1
- DNA topoisomerase 3-alpha
- DNA topoisomerase 3-beta
- Crossover junction endonuclease MUS81
- DNA polymerase epsilon catalytic subunit 1
- Ribonuclease H2 subunit A
- RecQ-like DNA helicase Blm
- ATP-dependent DNA helicase Q4
- Suppressor of variegation 2-10, isoform I
Sequence:
MSGDVAAENSIHIQNGGSCEVVQSNGVTTNGHGHHHHHHSSSSSSSKHKSSSKDKHRDREREHKSSNSSSSSKEHKSSSRDKDRHKSSSSSSKHRDKDKERDGSSNSHRSGSSSSHKDKDGSSSSKHKSSSGHHKRSSKDKERRDKDKDRGSSSSSRHKSSSSSRDKERSSSSHKSSSSSSSSKSKHSSSRHSSSSSSKDHPSYDGVFVKPEPVSQQLMHSGSVDAFQMQQLGSYEAAAAGTNFNGNGNVAGANYKNGYEESIVDIKKEEESFNNLSQASSCDYSMSQFRADEPPFVVKHEQSYAEEDSTMNYNDHDDDADEMNDDEEDVPLAMRKRKQEATDRPDGGMDNDDDDDIPLLARKKVKKEKIKKESKEKSKKRVKEEPSDDYGNVKPKKKKMKKEPEPAVSPGKRQKAKAKVEEEEVWRWWEEEKRADGVKWSTLEHKGPVFAPRYERVPRNVRFYYDGKPLELSEETEEAATFYAKMLNHDYCTKEVFNNNFFKDFRKSMTPREREIIKDFRKCNFQEMFNYFQAESEKRKAASKEEKLIKKNENEALMKEFGFCMIDGHKEKIGNFRLEPPGLFRGRGEHPKMGMIKRRIQASDVSINCGKDSKVPSPPPGSRWKEVRHDNTVTWLASWIENVQGQVKYIMLNPSSKLKGEKDHIKYETARRLDKVIDKIRATYRDEWKSKEMRVRQRAVALYFIDKLALRAGNEKDEDQADTVGCCSLRVEHVQLHKELNGKENVVVFDFPGKDSIRYYNEVEVEKRVFKNLELFMEHKKEGDDLFDRLNTQVLNEHLKELMEGLTAKVFRTYNASKTLQSQLDLLTDPSATVPEKLLAYNRANRAVAILCNHQRSVPKSHEKSMENLKEKIKAKREAIEKCESEYHSRDEKKGKQLERLRDQLKKLELQETDRDENKTIALGTSKLNYLDPRISVAWCKKHDVPIEKIFNKTQRTKFLWAVHMADENYRF
Protein: Homeobox protein slou (Homeobox protein NK-1) (Protein slouch) (S59/2) (P22807)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in specifying the identity of particular somatic muscles and neurons of the CNS.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Paired box pox-meso protein
- Homeobox protein caupolican
Sequence:
MVMLQSPAQKASDSASAQNTAVGGLMSPNSNPDSPKSNTSPDVASADSVVSGTGGGSTPPAAKIPKFIISANGAAVAGKQEQELRYSLERLKQMSSESGSLLSRLSPLQEDSQDKEKPNHNNNNSLTNHNANSNTRRSQSPPASVGSVSFSSPAQQRKLLELNAVRHLARPEPLQHPHAALLQQHPHLLQNPQFLAAAQQHMHHHQHQHHQHPAHPHSHQHPHPHPHPHPHPHPSAVFHLRAPSSSSTAPPSPATSPLSPPTSPAMHSDQQMSPPIAPPQNPPHSSQPPQQQQVAAPSDMDLERIKLVAAVAARTTQASSTSALASASNSVSNASISISNSSSGSPSGRDLSDYGFRIQLGGLAAAAAAAAATSRQIAAATYARSDTSEELNVDGNDEDSNDGSHSTPSVCPVDLTRSVNSSAAANPSSASTSASSDRDAATKRLAFSVENILDPNKFTGNKLPSGPFGHPRQWSYERDEEMQERLDDDQSEDMSAQDLNDMDQDDMCDDGSDIDDPSSETDSKKGGSRNGDGKSGGGGGGGSKPRRARTAFTYEQLVSLENKFKTTRYLSVCERLNLALSLSLTETQVKIWFQNRRTKWKKQNPGMDVNSPTIPPPGGGSFGPGAYASGLLYSHAVPYPPYGPYFHPLGAHHLSHSHS