wanglab/gogpt-training-data huggingface dataset:
Protein: Transcriptional protein SWT1 (Synthetically lethal with TREX protein 1) (Q12104)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transcription. Probably functions as a transcriptional activator.
Subcellular location: Nucleus {ECO:0000269|PubMed:17030511}. Note=Mainly nuclear, but might shuttle between the nucleus and the cytoplasm.
Interaction partners:
- Nucleoporin NUP60
- EST/SMG-like protein 2
- ATP-dependent RNA helicase SUB2
- Nonsense-mediated decay protein 4
- Exosome complex exonuclease DIS3
Sequence:
MTDEKRAFPKGNNHIRSETFNGSVSHKISESIKDIASLRPHGKYTVQDIDNIIASTSSHENRGQSGDSNGCINHDEEGDIPMCDLNDESDVEMISEYLSSQREMEAQSVANYMPKINDDLPLLNPPTLKTAFVVDTNFIISHLNTLEKLRSLSSTYHHLIIVPTTVIQELDGLKKSPDIARDNDDTTNQEHDRTIGTLARWGNDWIYKNLANLDSGLIGQKLKQSLNPGSLKDDSILDCCLYFKEILNCFVILLSNDKNLCTKALTEDILTVSFRKNMDAKIIAMRAYEENQLRFANLRDSTVNNFDQNVTSYAHIPGIETPPLQFDKVSQNVFEQVKETIFFAIDHTLRKEYGEDIGFIDYNPDKLTTIENASNYIYLFWVSVFSELFTCSKIKKNEWKSLPTVLKSKPTNLNDLRTFEQFWETVLHFLFSKFTNEEKQSLEKQIHEWKTSINAIST
Protein: Leucine-rich repeats and immunoglobulin-like domains protein 1 (LIG-1) (P70193)
Organism: Mus musculus (Mouse)
Function: Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12067728}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Epidermal growth factor receptor
- Hepatocyte growth factor receptor
- Proto-oncogene tyrosine-protein kinase receptor Ret
- E3 ubiquitin-protein ligase CBL
- Pro-epidermal growth factor
- Homeodomain-only protein
- Polycomb complex protein BMI-1
- Olfactomedin-4
- Keratin, type II cytoskeletal 79
Sequence:
MARPGPGVLGAPRLAPRLLLWLLLLLLQWPESAGAQAGPRAPCAAACTCAGDSLDCSGRGLATLPRDLPSWTRSLNLSYNRLSEIDSAAFEDLTNLQEVYLNSNELTAIPSLGAASIGVVSLFLQHNKILSVDGSQLKSYLSLEVLDLSSNNITEIRSSCFPNGLRIRELNLASNRISILESGAFDGLSRSLLTLRLSKNRITQLPVKAFKLPRLTQLDLNRNRIRLIEGLTFQGLDSLEVLRLQRNNISRLTDGAFWGLSKMHVLHLEYNSLVEVNSGSLYGLTALHQLHLSNNSISRIQRDGWSFCQKLHELILSFNNLTRLDEESLAELSSLSILRLSHNAISHIAEGAFKGLKSLRVLDLDHNEISGTIEDTSGAFTGLDNLSKLTLFGNKIKSVAKRAFSGLESLEHLNLGENAIRSVQFDAFAKMKNLKELYISSESFLCDCQLKWLPPWLMGRMLQAFVTATCAHPESLKGQSIFSVLPDSFVCDDFPKPQIITQPETTMAVVGKDIRFTCSAASSSSSPMTFAWKKDNEVLANADMENFAHVRAQDGEVMEYTTILHLRHVTFGHEGRYQCIITNHFGSTYSHKARLTVNVLPSFTKIPHDIAIRTGTTARLECAATGHPNPQIAWQKDGGTDFPAARERRMHVMPDDDVFFITDVKIDDMGVYSCTAQNSAGSVSANATLTVLETPSLAVPLEDRVVTVGETVAFQCKATGSPTPRITWLKGGRPLSLTERHHFTPGNQLLVVQNVMIDDAGRYTCEMSNPLGTERAHSQLSILPTPGCRKDGTTVGIFTIAVVCSIVLTSLVWVCIIYQTRKKSEEYSVTNTDETIVPPDVPSYLSSQGTLSDRQETVVRTEGGHQANGHIESNGVCLRDPSLFPEVDIHSTTCRQPKLCVGYTREPWKVTEKADRTAAPHTTAHSGSAVCSDCSTDTAYHPQPVPRDSGQPGTASSQELRQHDREYSPHHPYSGTADGSHTLSGGSLYPSNHDRILPSLKNKAASADGNGDSSWTLAKLHEADCIDLKPSPTLASGSPELMEDAISTEAQHLLVSNGHLPKACDSSPESVPLKGQITGKRRGPLLLAPRS
Protein: G-rich sequence factor 1 (GRSF-1) (Q8C5Q4)
Organism: Mus musculus (Mouse)
Function: Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the long non-coding RNAs for MT-CYB and MT-ND5, each of which contains multiple consensus binding sequences. Involved in the degradosome-mediated decay of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules. Acts by unwinding G-quadruplex RNA structures in MT-ncRNA, thus facilitating their degradation by the degradosome. G-quadruplexes (G4) are non-canonical 4 stranded structures formed by transcripts from the light strand of mtDNA.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q12849}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids. {ECO:0000250|UniProtKB:Q12849}.
Interaction partners:
- Probable ATP-dependent RNA helicase DDX28
- FAST kinase domain-containing protein 2
- NADH-ubiquinone oxidoreductase chain 6
- ATP-dependent RNA helicase DHX30
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
- SRA stem-loop-interacting RNA-binding protein
Sequence:
MAGTRWVLGALLRGCGCNCSSCRRTGAACLPFYSAAGTFPSGVSGRRRLLLLLGAAAAAASQTRGLQLGPAAAGRLAGPIPARPSAAAAAAASYSALRAPLFPRSLAAAAGPARGYSQESKTTYLEDLPPLPEYELSPSKLGDEVDDVYLIRAQGLPWSCTVEDVLNFFSDCRIRNSENGIHFLLNRDGKRRGDALIEMESEQDVQKALEKHRMYMGQRYVEVYEINNEDVDALMKSLQVKPSPVLSDGVVRLRGLPYSCNEKDIVDFFAGLNIVDITFVMDYRGRRKTGEAYVQFEEPEMANQALLKHREEIGNRYIEIFPSRRNEVRTHVGSHKGKKMTSSPPTKYITEPEVVFEEHEVNEDIRPMTAFESDKEIELPKEMSEKLPEAVDFGTLPSLHFVHMRGLPFQANAQDIINFFAPLKPVRITMEYSSSGKATGEADVHFDTHEDAVAAMLKDRSHVQHRYIELFLNSCPKGK
Protein: TRP homologous cation channel protein (TRP-3 channel protein) (Transient receptor ion channel domain-containing protein) (G5EF09)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein
- Dendritic cell-specific transmembrane protein-like domain-containing protein
- Sperm transmembrane protein 9
- Transient-receptor-potential-like protein
- Ig-like domain-containing protein
- CX domain-containing protein
- CYtochrome P450 family
- CYtochrome P450 family
- Spermatocyte protein spe-11
- Spermiogenesis protein SPE-29
Sequence:
MVGKEKKESTRLKLSAIKEYLGKYRGVDADNNEGYDGHQKWHENDQVVLQAMAYFYKAVKSKLYSEVRSFLGILLPHGPDDGRLSSLQSLLMDTSSEESLKEALLLSIAVGSRPLVEFVLVLFVDAPYLERSGSANSPHFPPHMTPLMLACILNNFSIVQCLITRGHCIQIPHFITCECKTCKRETVTTHSSTRLVDVMRALSSEAYLWLATDDVFAATCAVARDLQQLASDDQLEYVETYRDLEMNVQRFLCRISDQAWRVDEFNMMVANRNYCPERMTEISSPRLQMAMDSQMRQFTCSTNSQTTIKSVFRSDWYNYGIKPKRDAWRFLRACILMPFLVMLHAFMPTKGTTMCVPLARFIAHITMYLVFLIAAILRPTIGFYFAWTDSIEVTVQALEIFMYAYVMGLALEKGILFYRVGRDGFFAFWWRWFDAALIFIFLFSLIFFTGKWGKREAFDPSSVDRMHWPSFEFSLLHEICLAIACVLSILKCFYYAQMMKSIGGSVISVGKCVGKTYTYILIMVAIIVSFSVGLNIIVDPYLNRSTMKIGDQDYTKTTDSYETIGTSSKNLFWSIFGYLGPSTFTTVVGNTGPNMDPVKHTLNSSTFEILAAVYHGILIITVLNLMTSILVKGADEVLDNEEMEFKFTRAAIYSEFLSWEMAAPPPLNLILVVAHFVHRNLLKRYYASPAWGEKPANDDVEDQAADEQYMQLLMVVFARFVASKECKYKSIWRSEFHREEKQPPRVTFLTTGAHSFLMDNTFEGFKMRSSRTMEAEGYKEYTTVQYYVPKSKTPGPAAAADAGTKVAPKDDKPQNNPVLARTGIDSPVPSSKQVMSSELSASIPRARDVTFLGV
Protein: Tubulin polyglutamylase ttll6 (EC 6.3.2.-) (Protein polyglutamylase TTLL6) (Tubulin tyrosine ligase-like family member 6) (A8CVX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins (By similarity). Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction (By similarity). Preferentially modifies the alpha-tubulin tail over a beta-tail (By similarity). Mediates microtubule polyglutamylation in cilia axoneme, which is important for ciliary structural formation and motility. Polyglutamylates olfactory cilia, necessary for the regulation of ciliary sructure and beating.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A4Q9E8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A4Q9E8}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:22246503}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22246503}. Note=CEP41 is required for its transport between the basal body and the cilium axoneme. {ECO:0000269|PubMed:22246503}.
Interaction partners:
- Centrosomal protein of 41 kDa
- ATP/GTP-binding protein-like 4.
- Intraflagellar transport protein 70A
- Tubulin tyrosine ligase-like family, member 12.
- Cytosolic carboxypeptidase-like protein 5
Sequence:
MGTPAERSVSEVCRCEPDPGLEGEGWGSDTHAEPSNTPIPLPVANKKKKRKKKLWINLTNCKYESVRRAARRYGIREAAEGEDWTLYWTDCSVSLDRVMDMKRYQKINHFPGMNEICRKDLLARNMNRMLKLFPKEYNIFPRTWCLPADYSDFQAYTRAKKHKTFICKPDSGCQGRGIYLTKSSKDIRPGEHMICQVYMSKPFIIDGFKFDLRIYVLVTSCDPFRVFMYDEGLVRFCTTHYTEPTVSNLEDVCMHLTNYAINKHSENFVRDEDTGSKRKLSSFKKHMEDMSYDTEKLWTDIEDAIIKTLISAHPILKHNYQTCFPNHASGSACFEILGFDVLLDRRLKPWLLEVNHSPSFTTDSRLDREVKDSLLYDTLVLINLGACDRRKITEEEKRRVKERLQQNRSREARNEEPRQSQAASMELMQKYEAKHMGGFRRIFPRDGGEKYEKYFQHSSSLFQETAASKAREECARQQLQELRLKQEQKERDKKGSRKQDLQGESAGEKVKPRKSQPPHKTSNSLPAMLELSSVREETPVSLERIEKEEAERVRELQQRETLLLNMGVVNQVRQLLQSANRLTQCINHSHEQASFPPHCRHDHKLDTLAEISWRQKNIYSTMQHQILARNRPSLPNVHSQTLQNRKPWPSLEHGLLQPVQTQAAALKHYGLEEMVASNAEEQANLIKATSAQQIPLTINGSFIWRQGSLSSSLAESRARATMLAMPPLGPGRLHRPTIFHDPNSLSIISTPAPLVPRPHLSHDLRKAPRRVLPHEHSL
Protein: Eosinophil peroxidase isoform 2 precursor (EC 1.11.1.7) (Myeloid-specific peroxidase) (F1Q944)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNLPTFLFVVGCCCALSMGAEEESPGRPFILDSIEEAKKIVDAAYKYSRDESLARVRKDVIKPSDKLRLLKQPARKTREAVRAADYMAQTLRLISEKAHHVHKRSINATNLLTQDELQTITRMTGCEAQTRPPSCRTTPLINKYRTASGVCNNRKNPLLGASNTPFARWLPAQYEDAVSQPKGWDPNKLYNGAALPMVRLVSNRILATADADIESDHDFTFMLTIFGQWVDHDLTFTPFSPSIRSFSNGIDCENSCERSEPCFPISAPPGDQRLRPNTCLPVFRSAPTCGSGHTAYMFGEVPNVREQINTLTAYLDAGQVYGSEDGLAKELRDLTNDGGLLRVNNRFKDNGRELLPFTSVNTNLCATRQKILNDSTLTEVPCFIAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGPDAYNRHLGPYPGYNENVDPTIANVFATAAFRFAHLTIQPFIFRLDENYKNHPQFPSVPLYEAFFSPWRVIFEGGIDPVLRGLIGRPAKLNTQDHMLVNALRERLFAFTSHIALDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAVVMNNTELARKLIELYGTPENIDVWLGGVAEPFAPGGRVGSLFACLISRQFQKIRDGDRLWFESNGVFTTKQKTALASVSLARIICDNTGILKVPRDPFRFRSPANFVNCGNIPAFDLEPWKETGDGGINISDIGNEIEIPSQDLPDPGDLQENVVHRV
Protein: Histidine--tRNA ligase, mitochondrial (EC 6.1.1.21) (Histidine--tRNA ligase-like) (Histidyl-tRNA synthetase) (HisRS) (P49590)
Organism: Homo sapiens (Human)
Function: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21464306}.
Interaction partners:
- Glycine--tRNA ligase
- Histidine--tRNA ligase, cytoplasmic
- Heme oxygenase 2
- Tyrosine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, mitochondrial
- Lysine--tRNA ligase
- Threonine--tRNA ligase, mitochondrial
- Threonine--tRNA ligase 2, cytoplasmic
- Tyrosine--tRNA ligase, mitochondrial
Sequence:
MPLLGLLPRRAWASLLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAHQEKPNFIIKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTIVQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPRLSQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQAGEEPLNVGSVAAGGRYDGLVGMFDPKGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSES
Protein: ISG15-like protein (Q29W12)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MELTITLLNGNSLPLTVQPHTTVGSLKSLIEEHFKVATTKQRLLGVNGSNISLSDDSKTLSDYGLHSGSKVMVLITEPAPIQVFLKNEKGQTHTYDVVPGETVTQFKAKVQNKEGVPANQQRLIHEGRQLEDCQTLEYYNIRNQSTIHLALRLRGG
Protein: J domain-containing protein (Q385T3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRPRSVLLCSSLQRVAGAIELSKDYQSIEARSCESAEAEEKRKEYERFPLRYQLLECKPGVPLALMKLKYLLACRRTHPDAGGDAEDFLRVCLAYQDVMKDYGVETIENKIVNLGNFQVDRHEARNYLEGRAQIKGFIPVSTLEDYISKLEEVKARIGDDLAERLATNDDEALLLLEDIEEIMEANGLRTVRLEVLESGDVRVLEKPTLTDGTERPLLIGDLDNLNRGTLEVDRPFGPPSGVSEDGGVHFVRENESHDEQGLDAAEGQRALRTAEITAEDIEVLTAKHTVQDRTDVAGLASRTATEVMNNTEEVYKIRLESSVLYVFVISVFVLLYVYVEGLMRAKVQEKKRPQVMSHVTTDTMLPWWGNDAEYESQVKRIFVEEWRRARASSRRVQTFQDGVSRESLDENTKKELDLGIFTVTAERLREMRERAEKHTGLR
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 4) (1-AGP acyltransferase 4) (1-AGPAT 4) (Lysophosphatidic acid acyltransferase delta) (LPAAT-delta) (Q8K4X7)
Organism: Mus musculus (Mouse)
Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Exhibits high acyl-CoA specificity for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA (22:6-CoA, DHA-CoA).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24333445}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase MBOAT7
- Lysocardiolipin acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- Glycerol-3-phosphate acyltransferase 3
- Acylglycerol kinase, mitochondrial
Sequence:
MDLIGLLKSQFLCHLVFCYVFIASGLIVNAIQLCTLVIWPINKQLFRKINARLCYCVSSQLVMLLEWWSGTECTIYTDPKACPHYGKENAIVVLNHKFEIDFLCGWSLAERLGILGNSKVLAKKELAYVPIIGWMWYFVEMIFCTRKWEQDRQTVAKSLLHLRDYPEKYLFLIHCEGTRFTEKKHQISMQVAQAKGLPSLKHHLLPRTKGFAITVKCLRDVVPAVYDCTLNFRNNENPTLLGVLNGKKYHADCYVRRIPMEDIPEDEDKCSAWLHKLYQEKDAFQEEYYRTGVFPETPWVPPRRPWSLVNWLFWASLLLYPFFQFLVSMVSSGSSVTLASLVLIFCMASMGVRWMIGVTEIDKGSAYGNIDNKRKQTD
Protein: Protein CADMIUM TOLERANCE 2 (Cd tolerant 2) (OsCDT2) (Q5VSB6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Confers resistance to heavy metal ions (e.g. cadmium (CdCl(2)) and copper (CuCl(2))) by chelating them at the plasma membrane of root cells, thus stopping their entry and reducing their accumulation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5VSB5}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000250|UniProtKB:Q5VSB5}.
Interaction partners:
Sequence:
MYNPPAQQDMSYYDHCTKRHEEKGCLYACIFTALCCFCCYETCECCLDCLCCCCN
Protein: Zinc finger nuclease 2 (F4IUS5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSETQQQVQNSTGSIRSPDKIEDTFRRMKVNEDNMEQSSPYPDRPGERDCQFFLRTGQCGYGNSCRYNHPLTNLPQGIIYYRDQLPERVGQPDCEYFLKTGACKYGPTCKYHHPKDRNGAGPVLFNVLGLPMRQGEKPCPYYMQTGLCRFGVACKFHHPHPHSQPSNGHSAYAMSSFPSVGFPYASGMTMVSLPPATYGAIPRPQVPQSQAYMPYMVAPSQGLLPPQGWATYMTASNPIYNMKTQLDSSSSASVAVTVTSHHHSFSERAECRFFMNTGTCKYGDDCKYSHPKERLLQSPPTLLNPIVLPARPGQPACGNFKAYGFCKFGANCKFDHSMLLNPYNNTGLAMSSLPTPYPYAPPVSTNLRISSPPSPSDMTTLSNGKPAAAEAQSLETEKQDDSPTEPEKSEVEDSLPPNGSDSTSLPNDKPDAETEKQDDDSAELDSSKVQDSSDKST
Protein: Serum amyloid A-3 protein (P04918)
Organism: Mus musculus (Mouse)
Function: Major acute phase reactant. Apolipoprotein of the HDL complex. In vitro exhibits antimicrobial activity against Escherichia coli, Streptococcus uberis and Pseudomonas aeruginosa (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8SQ28}.
Interaction partners:
- Serum amyloid A-1 protein
- Alpha-1-acid glycoprotein 2
- Haptoglobin
- Serum amyloid A-4 protein
- Serum amyloid A-2 protein
- Neutrophil gelatinase-associated lipocalin
Sequence:
MKPSIAIILCILILGVDSQRWVQFMKEAGQGSRDMWRAYSDMKKANWKNSDKYFHARGNYDAARRGPGGAWAAKVISDAREAVQKFTGHGAEDSRADQFANEWGRSGKDPNHFRPAGLPKRY
Protein: Geranylgeranyl diphosphate synthetase (Q5SMD0)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Interaction partners:
Sequence:
MVPAPEAIRQALQERLLARLDHPDPLYRDLLQDYPRRGGKMLRGLLTVYSALAHGAPLEAGLEAATALELFQNWVLVHDDIEDGSEERRGRPALHRLHPMPLALNAGDAMHAEMWGLLAEGLARGLFPPEVLLEFHEVVRRTAYGQHLDLLWTLGGTFDLRPEDYFRMVAHKAAYYTAVAPLRLGALLAGKTPPAAYEEGGLRLGTAFQIVDDVLNLEGGEAYGKERAGDLYEGKRTLILLRFLEEAPPEERARALALLALPREAKPEAEVGWLLERLLASRALAWAKAEAKRLQAEGLALLEAAFQDLPGKEALDHLRGLLAALVERRA
Protein: Uncharacterized protein Rv0959 (P9WKN1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible magnesium chelatase
- Bifunctional purine biosynthesis protein PurH
- Phosphoribosylglycinamide formyltransferase
Sequence:
MAKSDGDDPLRPASPRLRSSRRHSLRYSAYTGGPDPLAPPVDLRDALEQIGQDVMAGASPRRALSELLRRGTRNLTGADRLAAEVNRRRRELLRRNNLDGTLQEIKKLLDEAVLAERKELARALDDDARFAELQLDALPASPAKAVQELAEYRWRSGQAREKYEQIKDLLGRELLDQRFAGMKQALAGATDDDRRRVTEMLDDLNDLLDKHARGEDTQRDFDEFMTKHGEFFPENPRNVEELLDSLAKRAAAAQRFRNSLSQEQRDELDALAQQAFGSPALMRALDRLDAHLQAARPGEDWTGSQQFSGDNPFGMGEGTQALADIAELEQLAEQLSQSYPGASMDDVDLDALARQLGDQAAVDARTLAELERALVNQGFLDRGSDGQWRLSPKAMRRLGETALRDVAQQLSGRHGERDHRRAGAAGELTGATRPWQFGDTEPWHVARTLTNAVLRQAAAVHDRIRITVEDVEVAETETRTQAAVALLVDTSFSMVMENRWLPMKRTALALHHLVCTRFRSDALQIIAFGRYARTVTAAELTGLAGVYEQGTNLHHALALAGRHLRRHAGAQPVVLVVTDGEPTAHLEDFDGDGTSVFFDYPPHPRTIAHTVRGFDDMARLGAQVTIFRLGSDPGLARFIDQVARRVQGRVVVPDLDGLGAAVVGDYLRFRRR
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (Q8IMY4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glucosylceramidase
- Aquarius
- Uncharacterized protein
- SCP domain-containing protein
- Uncharacterized protein, isoform A
- Prolyl 4-hydroxylase alpha subunit domain-containing protein
- Ero1-like protein
- IP08087p
- trypsin
- glutaminyl-peptide cyclotransferase
Sequence:
MNPNDTLSAFSLLLCVLILSAGRGELLFNADDNVVQLDFASFESGLSEPTSGKLVQFFNGFCEESQNFIPAFKNLSRKLYKWHRLLKVHVLDCGKDENDMICSIYSIRKTPTLRYFPPSYKLAPDNLGTEITHRNPKEIQSKLALNLQKLDYFKMFKRQDNVAHIFQTHKDIEYVAFVFQMCLDHFLPHLETGNSMEEKYASQGDCNEDNPIVSLIGRNTLLELLPYRKVVVRIFDNHDVYNKFGISPVPNLVVLVNKAGKLLFLTPEMDSSKAYVAAIKQFLIFVDLKPQKPLPKTPPANISEALRYEIFEQHKHHPSRIYRADLERAIDQILNVKFPGTTHFAGAKIVVLRNFVKLIYNSSPLKPEAREKLANLYYSLHVKKQLSGVGFKNLLLKSVKDYVFDGKQYVGCIASRPSLRGFNCSLWVLFHYLSVESKKLKPKSVLLVFLGYVRFFMNCKECDMKISEFKKLRPIANVTNDDEQILWLWEAHNYVNKQLAGDSTEDPKFPKIQFPSERDCPKCRNNATEWRTEEVLHYLKGIYTLKNLSWFGMSSGKHAIE
Protein: Erythrocyte membrane protein band 4.1 like 3 (A0A0A0MSA4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTESGSDSESKPDQEAEPQEAAGAQGRAGAPVPEPPKEEQQQALEQFAAAAAHSTPVRREVTDKEQEFAARAAKQLEYQQLEDDKLSQKSSSSKLSRSPLKIVKKPKSMQCKVILLDGSEYTCDVEKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLLPEAPPKKFLTLGSKFRYSGRTQAQTRRASALIDRPAPYFERSSSKRYTMSRSLDGASVNENHEIYMKDSMSAAEVGTGQYATTKGISQTNLITTVTPEKKAEEERDEEEDKRRKGEEVTPISAIRHEGKTDSERTDTAADGETTATESDQEEDAELKAQELEKTQDDLMKHQTNISELKRTFLETSTDTAVTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEETKEETEISEKVIFLQQGSAPFLESQGTEDWVIVDRIPTEVVDGDLKKIVTYKVVTVSSKTGDLPADMLKSGTIKMQSFEELAREMQLKEDSKQKIYTLGKSYDTVSGRIVTMTGKAKEGEKVEQPSTTEALQKMEKEIPESMKIIPGLAEYEVLETLADEKSKRGPEVQTTQRKLSESLAPIKEAESRRQSPEEDDLKKAPQLEKDVAVLPGLEGRRFSKTEQVPESEVLKVGLFGPRRKSLSEWRYSQEPAFTVATAHYVTESSASRVVTKQSSGEKLMDGSEIFSLLESARKPTEFIGGVTSTSQSWVQKMETKTESSGIETEPTVHHLPLSTEKVVQETVLVEERRVVHASGDASYSAGDSGDAAAQPAFTGIKGKEGSALTEGAKEEGGEEVAKAVLEQEETAAASRERQEEQSAAIHISETLEQKPHFESSTVKTETISFGSVSPGGVKLEISTKEVPVVHTETKTITYESSQVDPGTDLEPGVLMSAQTITSETTSTTTTTHITKTVKGGISETRIEKRIVITGDADIDHDQALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED
Protein: ATP-dependent protease La (LON) domain protein (F1B16.1 protein) (Protease, putative) (Putative protease) (Q9FWT4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein cereblon
- 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic
Sequence:
MALPHVVSSPSSTSLSPSFKSKPPFHSLRSLSPTVDNRRRCKLNSSFRCSSSSFSEKHHNAKSPKSDDIVELPLFPLPLVLFPGAILPLQIFEFRYRIMMHTLLQSDLRFGVVYSDSVSGSAAEVGCVGEVVKHERLVDDRFFLVCKGQERFRVTNVVRTKPYLVGEVTWLEDRPSGEENLDSLANEVEVLMKEVIRLSNRLNGKAEKEVQDLRRNQFPTPFSFFVGSTFEGAPREQQALLELEDTAARLKRERETLRNTLNYLTAASAVKDVFPSSS
Protein: Catenin alpha-1 (E5RIB1)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDVGHRDQMAAARGILQ
Protein: Lactoylglutathione lyase GLX1 (EC 4.4.1.5) (Glyoxalase I) (AtGLX1) (GlyI) (O65398)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Interaction partners:
- Hydroxyacylglutathione hydrolase 2, mitochondrial
- Probable hydroxyacylglutathione hydrolase 2, chloroplastic
- Hydroxyacylglutathione hydrolase cytoplasmic
- Hydroxyacylglutathione hydrolase 1, mitochondrial
- Protein DJ-1 homolog D
- DJ-1 protein homolog F
- DJ-1 protein homolog E
- Persulfide dioxygenase ETHE1 homolog, mitochondrial
- Lactoylglutathione lyase
- Probable lactoylglutathione lyase, chloroplastic
Sequence:
MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSSYDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKSGEVIKIVNQELGGKITREAGPLPGLGTKIVSFLDPDGWKTVLVDNKDFLKELE
Protein: Salivary glue protein Sgs-3 (P02840)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted.
Interaction partners:
- Salivary glue protein Sgs-4
- Salivary glue protein Sgs-5
- Salivary glue protein Sgs-7
- Ecdysone-induced gene 71Ee
- Salivary gland secretion 1
- Sgs5bis
- Salivary glue protein Sgs-8
- Uncharacterized protein, isoform A
Sequence:
MKLTIATALASILLIGSANVANCCDCGCPTTTTTCAPRTTQPPCTTTTTTTTTTCAPPTQQSTTQPPCTTSKPTTPKQTTTQLPCTTPTTTKATTTKPTTTKATTTKATTTKPTTTKQTTTQLPCTTPTTTKQTTTQLPCTTPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTTKPTTPKPCGCKSCGPGGEPCNGCAKRDALCQDLNGVLRNLERKIRQCVCGEPQWLL
Protein: Zinc finger protein 18 (Heart development-specific gene 1 protein) (Zinc finger protein 535) (Zinc finger protein KOX11) (Zinc finger protein with KRAB and SCAN domains 6) (P17022)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger protein 174
- Zinc finger protein 24
- Zinc finger protein 446
- Ubiquitin-protein ligase E3B
- SCAN domain-containing protein 1
Sequence:
MPVDLGQALGLLPSLAKAEDSQFSESDAALQEELSSPETARQLFRQFRYQVMSGPHETLKQLRKLCFQWLQPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLVESLKGDPQRLWQWISIQVLGQDILSEKMESPSCQVGEVEPHLEVVPQELGLENSSSGPGELLSHIVKEESDTEAELALAASQPARLEERLIRDQDLGASLLPAAPQEQWRQLDSTQKEQYWDLMLETYGKMVSGAGISHPKSDLTNSIEFGEELAGIYLHVNEKIPRPTCIGDRQENDKENLNLENHRDQELLHASCQASGEVPSQASLRGFFTEDEPGCFGEGENLPEALQNIQDEGTGEQLSPQERISEKQLGQHLPNPHSGEMSTMWLEEKRETSQKGQPRAPMAQKLPTCRECGKTFYRNSQLIFHQRTHTGETYFQCTICKKAFLRSSDFVKHQRTHTGEKPCKCDYCGKGFSDFSGLRHHEKIHTGEKPYKCPICEKSFIQRSNFNRHQRVHTGEKPYKCSHCGKSFSWSSSLDKHQRSHLGKKPFQ