wanglab/gogpt-training-data huggingface dataset:
Protein: Inner membrane ABC transporter permease protein YejB (P0AFU0)
Organism: Escherichia coli (strain K12)
Function: Probably part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized ABC transporter ATP-binding protein YejF
- Uncharacterized protein YejA
- Inner membrane ABC transporter permease protein YejE
- Glutathione import ATP-binding protein GsiA
- Probable cyclic di-GMP phosphodiesterase PdeN
- Oligopeptide transport system permease protein OppC
- Nickel import ATP-binding protein NikD
- Glutathione transport system permease protein GsiD
- Probable D,D-dipeptide transport ATP-binding protein DdpD
- Dipeptide transport system permease protein DppC
Sequence:
MGAYLIRRLLLVIPTLWAIITINFFIVQIAPGGPVDQAIAAIEFGNAGVLPGAGGEGVRASHAQTGVGNISDSNYRGGRGLDPEVIAEITHRYGFDKPIHERYFKMLWDYIRFDFGDSLFRSASVLTLIKDSLPVSITLGLWSTLIIYLVSIPLGIRKAVYNGSRFDVWSSAFIIIGYAIPAFLFAILLIVFFAGGSYFDLFPLRGLVSANFDSLPWYQKITDYLWHITLPVLATVIGGFAALTMLTKNSFLDEVRKQYVVTARAKGVSEKNILWKHVFRNAMLLVIAGFPATFISMFFTGSLLIEVMFSLNGLGLLGYEATVSRDYPVMFGTLYIFTLIGLLLNIVSDISYTLVDPRIDFEGR
Protein: LETM1-like protein (F4K2D7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized mitochondrial protein AtMg00860
- Gamma-soluble NSF attachment protein
- TLC domain-containing protein At5g14285
- Receptor-like protein 35
- Chaperone protein dnaJ 16
Sequence:
MAVKFHRPGLVPSSCSNPWMSVGTLISCRRVLQLDYISNCCGNSRTQLFVTYDDKNYFLQRKLFGNKKMSSRRTTQPFLLASAEDGVAVNGSRASDDVQEMRAKLSGSLQDEYSCGELIQSLHDAARTFELALKEKISSSRLPWFSAAWLGVDRNAWVKTFSYQASVYCLLQAANEVSSRGNNRDDDLNVFVQRSLSRQAAPLDSMMRDKLSSSHPEANEWFWSGQVPSAVTSFVNCFEGDQRFVSATSVYVKSNSTAASNEIEVSLLMLVLNCIAAVTKLGPTKLSCPPFFSVIPDTTGRLMDKFVGFVPLPQTYHSMKTLGLRREFLLHFGPRAAACRVKSDCDTDEVVFWVDLIQNQLLRAIDREKIWSRLITSESIEVLDRDLAIFGFFIALGKSTQSFLAANGFSSLENPVEDLVRHFIGGSLLQYPQLSAISSYQLYVEVVCEELDWIPFYPARKDSQPAEQSHGHKSRPQGPPNYDALPQILNVCSYWLQSFIKYSKWPENPSNVKAAKFLSKGARKNWEYQGKLMKSDVFCRKKLRVSIFRTPYISIPMHFAFFLAVTEASFIDMTSSSTDGESSSFDKALESVDGALVRLESLLQQLHASSSSSGKEQIKAACSDLEKIRKLKKEAEFLEASFRAKAASLQEGGGDSDSQEYSEEQSQYLRGKDPKNSINSVDQGTRDSGFWGFFVRTPKGKPGPESLTDKYFEKSRENVDNVDSNPNEIYRFELLRNELIELEKRVQGSTDESGRTSEDLPKSSSSTKGVQLVQSSKKENVIEKTLDQLKDATTDVWQGTQLLAFDSAAAMELLRRSVVGDELTEKEKKALRRTMTDLASVVPIGVLMLLPVTAVGHAAMLAAIQRYVPGLIPSTYGAERLNLLRQLEKVKQMQTNETEPEEGIDEPES
Protein: RING finger protein 207 (E9QHE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in cardiac repolarization possibly by stabilizing membrane expression of the potassium channel kcnh6a/zerg, or by assisting its synthesis, folding or export from the endoplasmic reticulum, in a heat shock protein-dependent manner.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6ZRF8}. Note=Probably located in the endoplasmic reticulum and/or possibly the cis-Golgi apparatus. {ECO:0000250|UniProtKB:Q6ZRF8}.
Interaction partners:
- Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog
- RING-type E3 ubiquitin transferase
- GINS complex subunit 3.
- G protein-coupled receptor 153.
- Solute carrier family 35 member F1
- Thioredoxin domain-containing 11
- NDRG family member 4
- Polynucleotide 5'-hydroxyl-kinase NOL9
Sequence:
MSGEIFYSVDNLYDLDSANCHPLVCHLCQEQYEHPCLLDCYHTFCASCLRGRVADSRLTCPVCGHQSVVKGINALPPEDRLLKFLVDSSADSEETVQCANCDLECKKQDVDAMYYCNTCCQPLCRDCRETTHKAKMFSRHEIVSLAKRTKEAHKKCALHEEFYIMFSTEKKSMLCINCFRDMQVESRAHCIDIETAYIQGCEKLDQAVLAVKELQMSAREAIILLKAMIGEVRANVDEEESAICTLFSNMQEKLAERKKILLKAARSQHEEKERTFKEQLSHLAALLPTLQVHLVTCSAFLSSANKFEFLDMGYQLMERLKKIVKLPHRLRPTQSSKINTEYRSEFARCLEPLLLLGQRRSMSTTGSVALALGNASGLMQSSLSVQCHSPAMSDMSLCSSVVRRPTSHRYISTKVLLAKGGETPFMEHCCNYENSYRTLQTEIQKLKDQVQEIHRDLTKHHSLTKPDSMSEILEKSVQVDSQISSEYASVELMRAMFEEIWEETLQRVANEQEIYEAQLHDLLQLKQENSYLTTISRQIGPYIRSIAKVKERLEPRLKEPKELKDDRTEIMLKLYEDSTSTADTQPSNELSCNTEDNWTLNSLSEETNPKNKDYYRTNKQKNTTDSTNRKEIPM
Protein: Leucine-rich repeat protein (LRRP), putative (Q57V18)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLQAAEQRNSLRLANAVALVADASDQPITEYVAENGGAAPRTSSTLTLAERAIRNMEIRALCEDKNYQRVKLTSCRGSVDLKLFTCMTSLRDIHVEMDGDICNIPSLQDLPDIRRIYLSSKTMNDSDVRPLCNIETLEEINICNSPNVVNLGNVGRLPRVHTLMVNRTGVIDEFLCGLTLSNTLRRIDLSECLRLTDVEPLASIETLEEIDVSGCFPCVCGIGALGALPRLKILNASLTGITDECLARLSASQSLKKLLLSKCERLTNVSRLDTVTTLQELDLAECKNVVSGIGSLGTLPVLQCLDLSGTGVADDDLCALSCSATISKLIMKRCVLLTNVSPLEKLRTLQHVNIGECINVIEGLNSFSELPSLRTLYMHYTPVTNECLSVISTSQSIVSLNIAACTRITDISCLANLKTLEDVNINMCESVEKGLGDISGLSNLRMLSARSTVLDDECVKIMSSSSNLERSSLEGCAKITDVTPLAAVKSLEYVNLDNCPVVKGIAELGKLPLLRVISLRETNICEEDIKNLKKFNRRLYIER
Protein: Cell cycle regulator of non-homologous end joining (Cell cycle regulator of NHEJ) (Modulator of retrovirus infection homolog) (Q9BWK5)
Organism: Homo sapiens (Human)
Function: Cell-cycle-specific regulator of classical non-homologous end joining (NHEJ) of DNA double-strand break (DSB) repair, which can act both as an activator or inhibitor of NHEJ, depending on the cell cycle phase. Acts as a regulator of DNA repair pathway choice by specifically inhibiting classical NHEJ during the S and G2 phases, thereby promoting error-free repair by homologous recombination during cell cycle phases when sister chromatids are present. Preferentially protects single-stranded overhangs at break sites by inhibiting classical NHEJ, thereby creating a local environment that favors homologous recombination. Acts via interaction with XRCC5/Ku80 and XRCC6/Ku70. In contrast, acts as an activator of NHEJ during G1 phase of the cell cycle: promotes classical NHEJ in G1 phase cells via multivalent interactions that increase the affinity of DNA damage response proteins for DSB-associated chromatin. Also involved in immunoglobulin V(D)J recombination (By similarity). May also act as an indirect regulator of proteasome (By similarity).
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:24610814}. Nucleus {ECO:0000269|PubMed:24610814}. Chromosome {ECO:0000269|PubMed:27063109}. Note=Nuclear localization may depend upon interaction with XRCC5/Ku80 and XRCC6/Ku70 heterodimer (PubMed:24610814). Localizes to DNA damage sites (PubMed:27063109). {ECO:0000269|PubMed:24610814, ECO:0000269|PubMed:27063109}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:24610814}. Note=Some nuclear localization may be due to passive diffusion. {ECO:0000269|PubMed:24610814}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:24610814}. Nucleus {ECO:0000269|PubMed:24610814}. Note=Nuclear localization may depend upon interaction with XRCC5/Ku80 and XRCC6/Ku70 heterodimer and increases upon etoposide treatment. {ECO:0000269|PubMed:24610814}.
Interaction partners:
- X-ray repair cross-complementing protein 6
- Methylthioribose-1-phosphate isomerase
- X-ray repair cross-complementing protein 5
- DNA excision repair protein ERCC-6-like 2
- Anti-Muellerian hormone type-2 receptor
- Catenin delta-2
Sequence:
METLQSETKTRVLPSWLTAQVATKNVAPMKAPKRMRMAAVPVAAARLPATRTVYCMNEAEIVDVALGILIESRKQEKACEQPALAGADNPEHSPPCSVSPHTSSGSSSEEEDSGKQALAPGLSPSQRPGGSSSACSRSPEEEEEEDVLKYVREIFFS
Protein: CREB-regulated transcription coactivator 1 (Mucoepidermoid carcinoma translocated protein 1 homolog) (Transducer of regulated cAMP response element-binding protein 1) (TORC-1) (Transducer of CREB protein 1) (Q68ED7)
Organism: Mus musculus (Mouse)
Function: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated. Acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells (By similarity). In the hippocampus, involved in late-phase long-term potentiation (L-LTP) maintenance at the Schaffer collateral-CA1 synapses. May be required for dendritic growth of developing cortical neurons. In concert with SIK1, regulates the light-induced entrainment of the circadian clock. In response to light stimulus, coactivates the CREB-mediated transcription of PER1 which plays an important role in the photic entrainment of the circadian clock.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17360587, ECO:0000269|PubMed:23993098}. Nucleus {ECO:0000269|PubMed:17360587, ECO:0000269|PubMed:23699513, ECO:0000269|PubMed:23993098}. Note=Cytoplasmic when phosphorylated by SIK or AMPK and when sequestered by 14-3-3 proteins (By similarity). Translocated to the nucleus on Ser-151 dephosphorylation, instigated by a number of factors including calcium ion and cAMP levels (By similarity). Light stimulation triggers a nuclear accumulation in the suprachiasmatic nucleus (SCN) of the brain (PubMed:23699513). {ECO:0000250|UniProtKB:Q6UUV9, ECO:0000269|PubMed:23699513}.
Interaction partners:
- CREB-regulated transcription coactivator 3
- CREB-regulated transcription coactivator 2
- Cyclic AMP-responsive element-binding protein 1
Sequence:
MATSNNPRKFSEKIALHNQKQAEETAAFEEVMKDLSLTRAARLQLQKSQYLQLGPSRGQYYGGSLPNVNQIGSSSVDLAFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLSVDKHGRQADSCPYGTVYLSPPADTSWRRTNSDSALHQSTMTPSQAESFTGGSQDAHQKRVLLLTVPGMEDTGAETDKTLSKQSWDSKKAGSRPKSCEVPGINIFPSADQENTTALIPATHNTGGSLPDLTNIHFPSPLPTPLDPEEPPFPALTSSSSTGSLAHLGVGGAGQGMNTPSSSPQHRPAVVSPLSLSTEARRQQAQQVSPTLSPLSPITQAVAMDALSLEQQLPYAFFTQTGSQQPPPQPQPPPPPPPVSQQQPPPPQVSVGLPQGGPLLPSASLTRGPQLPPLSVTVPSTLPQSPTENPGQSPMGIDATSAPALQYRTSAGSPATQSPTSPVSNQGFSPGSSPQHTSTLGSVFGDAYYEQQMTARQANALSRQLEQFNMMENAISSSSLYNPGSTLNYSQAAMMGLSGSHGGLQDPQQLGYTGHGGIPNIILTVTGESPPSLSKELSSTLAGVSDVSFDSDHQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL
Protein: Probable serine/threonine-protein kinase PBL1 (EC 2.7.11.1) (BIK1-like protein kinase) (PBS1-like protein 1) (Protein CHANGED CALCIUM ELEVATION 5) (Q8H186)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling, including calcium signaling and root growth inhibition, and defense responses downstream of FLS2. Acts additively with BIK1 in PTI defenses. Seems not required for flg22-induced MAPK activation (Probable). Required for Pep1-induced defenses. Pep1 is an endogenous elicitor that potentiates PAMP-inducible plant responses. Required during SCOOP small peptides (e.g. SCOOP10 and SCOOP12) perception and signaling; receptor-like cytosolic kinases (RLCK) activated by BAK1/SERK3 and SERK4 coreceptors when associated with MIK2 upon the perception of SCOOP peptides.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25522736}; Lipid-anchor {ECO:0000269|PubMed:25522736}. Note=Myristoylation and proper targeting to plasma membrane is essential for signaling function in response to pathogen-associated molecular pattern (PAMP) such as flg22. {ECO:0000269|PubMed:25522736}.
Interaction partners:
- Respiratory burst oxidase homolog protein D
- RPM1-interacting protein 4
- Precursor of elicitor peptide 1
- Elongation factor Tu, chloroplastic
- Leucine-rich repeat receptor-like protein kinase PEPR1
- Elongation factor Tu
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
Sequence:
MGSCLSSRVLNKSSSGLDDLHLSSCKSSSSATAHKTEGEILSSTTVKSFSFNELKLATRNFRSDSVVGEGGFGCVFRGWLDETTLTPTKSSSGLVIAVKRLNPDGFQGHREWLTEINYLGQLSHPNLVKLIGYCLEDEQRLLVYEFMHKGSLENHLFANGNKDFKPLSWILRIKVALDAAKGLAFLHSDPVKVIYRDIKASNILLDSDFNAKLSDFGLARDGPMGEQSYVSTRVMGTFGYAAPEYVSTGHLNARSDVYSFGVVLLELLCGRQALDHNRPAKEQNLVDWARPYLTSRRKVLLIVDTRLNSQYKPEGAVRLASIAVQCLSFEPKSRPTMDQVVRALVQLQDSVVKPANVDPLKVKDTKKLVGLKTEDKYQRNGLNKKTVGL
Protein: Late genes activator p4 (Gene product 4) (gp4) (Protein p4) (P03682)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Mediates, together with protein p6, the early to late transcriptional switch by stabilizing the binding of host RNA polymerase (RNAP) to the late A3 promoter. Activates transcription from the late A3 promoter and represses the main early promoters A2b and A2c by modifying the topology of the sequences encompassing early promoters A2c and A2b and late promoter A3 in a hairpin. Proteins p6 and p4 bind cooperatively to an approximately 200 bp DNA region located between the late A3 and the early A2c promoters. Binding of p4 molecules induces the reorganization of the binding of protein p6, giving rise to the nucleoprotein complex responsible for the switch from early to late transcription.
Interaction partners:
Sequence:
MPKTQRGIYHNLKESEYVASNTDVTFFFSSELYLNKFLDGYQEYRKKFNKKIERVAVTPWNMDMLADITFYSEVEKRGFHAWLKGDNATWREVHVYALRIMTKPNTLDWSRIQKPRLRERRKSMV
Protein: carboxylesterase (EC 3.1.1.1) (A0A0B4LHM3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RT09038p
- Cytosolic beta-glucosidase
Sequence:
MPCPRNWQRGAAIAALSLAIGLIVMAICVQRPNESGHRIIVTEQRKSSAEEAQEGYDPHGGDLQDLRDKARAFYLIATTTTTSTTMSPENATKSENASGSLDMRQMAHMGSSTTETTAWKTLTSHPNSLVQLLPSRAMRVVQEVVRSLRKEREIVATTSLGKVRGRYQKYRSGERGGYYSFKGMRYGAPPTGARRFRAAEPEKPWSGIRDASREGQSCPHKNMILDTFKGDEDCLFVNVFTTQMPKDDESAEQPKLPVMVWLHGGGFSFGSGNSFLYGPDYLVAEDIVLVTLNYRLGPLGFLTAGPDAPGNQGLKDQVLALKWVRDNIAAFGGDPNQVTIFGESAGASSVQLLLLSSQAKGLFHRAISQSGSALNPWSMSASSSQRAARLAANLGYVGANKTEDILDFLRRVPAMKLVEAAPTTITAEDQRNNIGLPFVPVVEGYWNQDSQEEQFYEEPFLTQHPSDMYHSQNFNSDVAYMTGYNTHEAMLFIRRLRKNPQLLSIIENDFGRLVPQDLNVTESHDRVTREIRSFYLGSKHVGIESVDEMIALLTDLMFLQGIRRTARNHAKFGNAPVYMYRFSFDGSLGLYKRMLGIPRPGVCHGDELGYLFKFGFFNLSLDPKSMEVQVKNRMVRMWTNFAKYGSPTPDSEDPMLTTKWAPIDPTNVMNSLNYMDISANLAMKTNPEPERQRFWDEMYQHYNGAAM
Protein: Glycerophosphodiester phosphodiesterase GDPDL4 (EC 3.1.4.46) (Glycerophosphodiester phosphodiesterase-like 4) (ATGDPDL4) (Glycerophosphodiesterase-like 1) (Protein SHV3-LIKE 1) (Q9FJ62)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in primary cell wall organization. Required for the accumulation of crystalline cellulose.
Subcellular location: Cell membrane; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Fasciclin-like arabinogalactan protein 8
- Early nodulin-like protein 11
- Uclacyanin 1
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- At4g22010
Sequence:
MINMRDNPTMHVLQASKFLFLALILIQLLSTQLFAQRSKSPWQTLTGDAPLVIARGGFSGLLPDSSLDAYSFVSQTSVPGAVLWCDVQLTKDAIGLCFPDVKMMNASNIQDVYPKRKTSYLLNGVPTQDWFTIDFNFKDLTKVILKQGILSRSAAFDGNSYGISTVKDISTQLKPEGFWLNVQHDAFYAQHNLSMSSFLLSISKTVIIDYLSSPEVNFFRNIGRRFGRNGPKFVFRFLEKDDVEVSTNQTYGSLAGNLTFLKTFASGVLVPKSYIWPIESQYLLPRTSFVQDAHKAGLEVYASGFGNDFDLAYNYSFDPLAEYLSFMDNGDFSVDGLLSDFPLTASSAVDCFSHLGSNASSQVDFLVISKNGASGDYPGCTDLAYTKAIKDGADVIDCSLQMSSDGIPFCLSSINLGESTNVVQSPFRNRSTTVPEIGSLPGIYSFSLAWSEIQTLRPAIENPYSREFTMFRNPRERSSGKFVSLSDFLNLAKNSSSLTGVLISVENATYLREKQGLDAVKAVLDTLTEAGYSNKTTTTRVMIQSTNSSVLIDFKKQSRYETVYKVEETIRDILDTAIEDIKKFADAVVISKKSVFPTSESFTTGQTKLVERLQKFQLPVYVEVFRNEFVSQPWDFFADATVEINSHVTGAGINGTITEFPLTAARYKRNSCLTRKDVPPYMIPVQPAGLLTIVSPASLPPAEAPSPVFTDADVTEPPLPPVSARAPTTTPGPQSTGEKSPNGQTRVALSLLLSAFATVFASLLLL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0G2K2H4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- TNF receptor-associated factor
- X-box-binding protein 1
- mitogen-activated protein kinase kinase kinase
- Presenilin-1
- Presenilin-2
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Small ribosomal subunit protein RACK1
- Disabled homolog 2-interacting protein
- Bax inhibitor 1
Sequence:
MPARWLLLLLALLLLPPGPGSFGRASTVTLPEALLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGGKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYIWQREGLRKVVHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDLKFDPGLKGKSKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKRSFEEVINLVGQTSENTPTTVSQDVEEKLPRAPAKPEAPVDSMLKDMATIILSTFLLVGWVAFIITYPLSMHQQRQLQHQQFQKELEKIQLLQQQQLPFHPHGDLTQDPDFLDSSGLFSESSGTSSPSPSPRASNHSLNSSSSASKAGTSPSLEPDDEDEETRMVIVGKISFCPKDVLGHGAEGTIVYKGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLHQTTSGLAHLHSLNIVHRDLKPHNILLSMPNAHGRIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGNHPFGKSLQRQANILLGACSLDCFHSDKHEDVIARELIEKMIAMDPQQRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVRQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKRHHYRELPLEVQETLGSIPDDFVRYFTSRFPHLLSHTYRAMELCRHERLFQTYYWHEPTEAQPPGIPDAL
Protein: DOMINA protein (Jumeau) (LD24749p) (Winged-helix nude transcription factor) (Q9XTP7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MFELEDYSSGIHEGFFSKYADAAGPSLDFYVSDSMQEMLNVDIRAEIANVVGSSSSDLTSSLDQTLEAISAINNNQSNGNSSQSASYNANANFLTSSGLHASPTAKWMGSSANFWSNSDYYADLGACVNPISVMPLINSTSAGMFSPKKNKTASSTQGRSGAVPSSPSAERDQHKSHLTFSPAQMKVSAGSMRRDQVMAHIPKQISVVTGTGTTAPATMATNSVLQRRNSSAVDAVRKDLVTELRKAQSSPVPNSLEELGKGKGSTLLNASVGATNTIKLAPGIGGLTFANSAAYQKLKQTSLVKSPGGISPGAGSNMGLKREDSNKRGLQASTTPKSIASAANSPHHQMQSNYSLGSPSSLSSSSASSPLGNVSNLVNIANNNTSGAGSGLVKPLQQKVKLPPVGSPFPKPAYSYSCLIALALKNSRAGSLPVSEIYSFLCQHFPYFENAPSGWKNSVRHNLSLNKCFEKIERPATNGNQRKGCRWAMNPDRINKMDEEVQKWSRKDPAAIRGAMVYPQHLESLERGEMKHGSADSDVELDSQSEIEESSDLEEHEFEDTMVDAMLVEEEDEEEDGDDDEQIINDFDAEDERHANGNQANNLPINHPLLGQKSNDFDIEVGDLYDAIDIEDDKESVRRIISNDQHIIELNPADLNATDGYNQQPALKRARVDINYAIGPAGELEQQYGQKVKVQQVIQPQQHPPTYNRRKMPLVNRVI
Protein: Non-selective voltage-gated ion channel 1 (Outer mitochondrial membrane protein porin 1) (Voltage-dependent anion-selective channel protein 1) (VDAC-1) (P04840)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. Is the major permeability factor of the mitochondrial outer membrane.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:7499333, ECO:0000305|PubMed:38065946}.
Interaction partners:
- Mitochondrial import receptor subunit TOM40
- Sorting assembly machinery 50 kDa subunit
- Mitochondrial import receptor subunit TOM20
- Mitochondrial import receptor subunit TOM22
- Mitochondrial outer membrane protein OM45
- Cytochrome c isoform 2
- Sorting assembly machinery 35 kDa subunit
- Mitochondrial import receptor subunit TOM70
- Cytochrome c isoform 1
- ADP,ATP carrier protein 2
Sequence:
MSPPVYSDISRNINDLLNKDFYHATPAAFDVQTTTANGIKFSLKAKQPVKDGPLSTNVEAKLNDKQTGLGLTQGWSNTNNLQTKLEFANLTPGLKNELITSLTPGVAKSAVLNTTFTQPFFTARGAFDLCLKSPTFVGDLTMAHEGIVGGAEFGYDISAGSISRYAMALSYFAKDYSLGATLNNEQITTVDFFQNVNAFLQVGAKATMNCKLPNSNVNIEFATRYLPDASSQVKAKVSDSGIVTLAYKQLLRPGVTLGVGSSFDALKLSEPVHKLGWSLSFDA
Protein: Inositol phosphorylceramide synthase regulatory subunit kei1 (ICP synthase regulatory subunit kei1) (O13994)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory component of the inositol phosphorylceramide (ICP) synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis. Helps the medial Golgi localization of IPC synthase in a COPI vesicle-dependent manner (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Inositol phosphorylceramide synthase catalytic subunit aur1
- Large ribosomal subunit protein mL60
Sequence:
MALFRRPNWSALFEKIFIQKSFLGFCSLRVGCEIIIWFAIINKVSGLYGIVSLFQNSDASPWQVLMYVSSVLMLILFSWLAIHIPKSSVPHALILFYVYLIDFLLNVLFTVLFALSWFSKLVQSDSSSTEESADSDPSPSLLYLFFQAESIPSLLLLIFFASLKFYFVLITLSYSNKLIVDSGIRPQNLPPNFSGRVTRLLMKPYIMAANRSYLRNHTKRFTDSIELEQRLMDEVV
Protein: Ras suppressor protein 1 (Q09497)
Organism: Caenorhabditis elegans
Interaction partners:
- LIM domain-containing protein unc-97
- Integrin-linked protein kinase homolog pat-4
- Paralyzed arrest at two-fold protein 6
- LIM domain-containing protein pin-2
- U2A'/phosphoprotein 32 family A C-terminal domain-containing protein
Sequence:
MPKDKKKDEVTEVEHVDRNISSFSQISHLIDAEIITRLTLSHNKLTSVPPNIADLVSLQSLNLWNNQIEDLPPSISSLPKLRILNVGMNKLSILPRGFGSFPELEILDLTYNNLSERSLPGNFFFMQTLRALYLGDNDFEMLPGDVENLTNLQILVLRENDLLTLPKELGKLTRLRELHIQGNRLAMIPPELGNLELVGSKQVLRLEHNPFIPRIEEQFEANGAAGVWAHIRTDDYRYFFGRQEPSSTPVPPKRNKEKKVSRKGIQQA
Protein: Protein-glutamine gamma-glutamyltransferase K (EC 2.3.2.13) (Epidermal TGase) (Transglutaminase K) (TG(K)) (TGK) (TGase K) (Transglutaminase-1) (TGase-1) (P22735)
Organism: Homo sapiens (Human)
Function: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum. Involved in cell proliferation.
Subcellular location: Membrane {ECO:0000269|PubMed:17762858}; Lipid-anchor {ECO:0000305|PubMed:17762858}.
Interaction partners:
- Involucrin
- Magnesium transporter NIPA4
- Glucosylceramide transporter ABCA12
- Cornifin-B
- Loricrin
- Ultra-long-chain fatty acid omega-hydroxylase
- Filaggrin
- Arachidonate 12-lipoxygenase, 12R-type
- Hydroperoxide isomerase ALOXE3
- Cystatin-A
Sequence:
MMDGPRSDVGRWGGNPLQPPTTPSPEPEPEPDGRSRRGGGRSFWARCCGCCSCRNAADDDWGPEPSDSRGRGSSSGTRRPGSRGSDSRRPVSRGSGVNAAGDGTIREGMLVVNGVDLLSSRSDQNRREHHTDEYEYDELIVRRGQPFHMLLLLSRTYESSDRITLELLIGNNPEVGKGTHVIIPVGKGGSGGWKAQVVKASGQNLNLRVHTSPNAIIGKFQFTVRTQSDAGEFQLPFDPRNEIYILFNPWCPEDIVYVDHEDWRQEYVLNESGRIYYGTEAQIGERTWNYGQFDHGVLDACLYILDRRGMPYGGRGDPVNVSRVISAMVNSLDDNGVLIGNWSGDYSRGTNPSAWVGSVEILLSYLRTGYSVPYGQCWVFAGVTTTVLRCLGLATRTVTNFNSAHDTDTSLTMDIYFDENMKPLEHLNHDSVWNFHVWNDCWMKRPDLPSGFDGWQVVDATPQETSSGIFCCGPCSVESIKNGLVYMKYDTPFIFAEVNSDKVYWQRQDDGSFKIVYVEEKAIGTLIVTKAISSNMREDITYLYKHPEGSDAERKAVETAAAHGSKPNVYANRGSAEDVAMQVEAQDAVMGQDLMVSVMLINHSSSRRTVKLHLYLSVTFYTGVSGTIFKETKKEVELAPGASDRVTMPVAYKEYRPHLVDQGAMLLNVSGHVKESGQVLAKQHTFRLRTPDLSLTLLGAAVVGQECEVQIVFKNPLPVTLTNVVFRLEGSGLQRPKILNVGDIGGNETVTLRQSFVPVRPGPRQLIASLDSPQLSQVHGVIQVDVAPAPGDGGFFSDAGGDSHLGETIPMASRGGA
Protein: F-box only protein 7 (Q9Y3I1)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16096642, ECO:0000269|PubMed:18495667}. Nucleus {ECO:0000269|PubMed:16096642, ECO:0000269|PubMed:18495667, ECO:0000269|PubMed:33010352}. Mitochondrion {ECO:0000269|PubMed:23933751}. Cytoplasm, cytosol {ECO:0000269|PubMed:23933751}. Note=Predominantly cytoplasmic (PubMed:16096642). A minor proportion is detected in the nucleus (PubMed:16096642). Relocates from the cytosol to depolarized mitochondria (PubMed:23933751). {ECO:0000269|PubMed:16096642, ECO:0000269|PubMed:23933751}.
Interaction partners:
- S-phase kinase-associated protein 1
- Serine/threonine-protein kinase PINK1, mitochondrial
- Cullin-1
- Proteasome inhibitor PI31 subunit
- E3 ubiquitin-protein ligase RBX1
- E3 ubiquitin-protein ligase parkin
- 85/88 kDa calcium-independent phospholipase A2
- GRB10-interacting GYF protein 2
- Polyamine-transporting ATPase 13A2
- Parkinson disease protein 7
Sequence:
MRLRVRLLKRTWPLEVPETEPTLGHLRSHLRQSLLCTWGYSSNTRFTITLNYKDPLTGDEETLASYGIVSGDLICLILQDDIPAPNIPSSTDSEHSSLQNNEQPSLATSSNQTSMQDEQPSDSFQGQAAQSGVWNDDSMLGPSQNFEAESIQDNAHMAEGTGFYPSEPMLCSESVEGQVPHSLETLYQSADCSDANDALIVLIHLLMLESGYIPQGTEAKALSMPEKWKLSGVYKLQYMHPLCEGSSATLTCVPLGNLIVVNATLKINNEIRSVKRLQLLPESFICKEKLGENVANIYKDLQKLSRLFKDQLVYPLLAFTRQALNLPDVFGLVVLPLELKLRIFRLLDVRSVLSLSAVCRDLFTASNDPLLWRFLYLRDFRDNTVRVQDTDWKELYRKRHIQRKESPKGRFVMLLPSSTHTIPFYPNPLHPRPFPSSRLPPGIIGGEYDQRPTLPYVGDPISSLIPGPGETPSQFPPLRPRFDPVGPLPGPNPILPGRGGPNDRFPFRPSRGRPTDGRLSFM