wanglab/gogpt-training-data huggingface dataset:
Protein: Lupeol synthase (KdLUS) (EC 5.4.99.41) (E2IUA9)
Organism: Kalanchoe daigremontiana (Devil's backbone) (Bryophyllum daigremontianum)
Function: Oxidosqualene cyclase that generates lupeol, a triterpenoid product. Lupeol is probably required to coat the leaf exterior as a defense compound against pathogens or herbivores.
Interaction partners:
Sequence:
MWKLKIADGGSNPYIFTTNNFVGRQIWEFDPQATDPQQLAKVEAARLDFYHNRYKLKPNSDLLWRMQFLEEKAFTQTIPQVKVEDGEEVSYEAVTAALRRGVHLYSALQASDGHWPAENAGPMFFMPPMVMCLYITGHLNAIFTEEHRSETLRYIYYHQNEDGGWGFHIEGHSTMFGTVLNYICMRLLGEGPEGGQDNAVSRGRKWILDHGGATSIPSWGKTWLSIMGLCDWSGCNPMPPEFWLLPSYLPMHPGKMWCYCRMVYMPMSYLYGKRFTARITPLILQLREEIHIQPYDQIDWKKVRHVCCKEDMYYPHPLLQDLLWDTLYLTTEPLLTRWPLNKLIRKRALQTTMKHIHYEDENSRYITIGCVEKVLCMLACWVEDPNGDYFKKHLARIPDYLWIAEDGMKMQSFGSQHWDTAFSIQALLASNMAEEIGITLAKGHDFIKKSQVKDNPSGDFKGMYRHISKGAWTFSDQDHGWQVSDCTAEGLKCCLLFSMMQPEVVGESMAPESLYNSVNVLLSLQSQNGGLPAWEPAGAPEWLELLNPTEFFENIVIEHEYVECTSSAVQALVLFKKLYPLHRRKEVERFITNGAKYLEDIQMPDGSWYGNWGVCFTYGAWFALEGLSAAGKTYNNCAAVRKGVDFLLNIQLEDGGWGESYQSCPDKKYVPLEDNRSNLVQTSWALMGLIYAGQADRDPTPLHRAAQLLINSQLEDGDFPQQEITGVFQRNCMLHYAAYRNIFPLWALAEYRRQIQLHSEATKMV
Protein: Diacylglycerol kinase (DAG kinase) (DAGK) (EC 2.7.1.107) (Q6GFF9)
Organism: Staphylococcus aureus (strain MRSA252)
Function: Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway.
Interaction partners:
Sequence:
MRKRARIIYNPTSGKEQFKRELPDALIKLEKAGYETSAYATEKIGDATLEAERAMHENYDVLIAAGGDGTLNEVVNGIAEKPNRPKLGVIPMGTVNDFGRALHIPNDIMGALDVIIEGHSTKVDIGKMNNRYFINLAAGGQLTQVSYETPSKLKSIVGPFAYYIKGFEMLPQMKAVDLRIEYDGNVFQGEALLFFLGLTNSMAGFEKLVPDAKLDDGYFTLIIVEKSNLAELGHIMTLASRGEHTKHPKVIYEKAKAINISSFTDLQLNVDGEYGGKLPANFLNLERHIDVFAPNDIVNEELINNDHVDDNLIEE
Protein: Uncharacterized protein Rv1815 (P9WLR9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- HTH-type transcriptional regulator Rv1816
- Resuscitation-promoting factor RpfC
- Coenzyme Q-binding protein COQ10 START domain-containing protein
- C-5 sterol desaturase
Sequence:
MVRLVPRAFAATVALLAAGFSPATASADPVLVFPGMEIRQDNHVCTLGYVDPALKIAFTAGHCRGGGAVTSRDYKVIGHLRAIRDNTPSGSTVATHELIADYEAIVLADDVTASNILPSGRALESRPGVVLHPGQAVCHFGVSTGETCGTVESVNNGWFTMSHGVLSEKGDSGGPVYLAPDGGPAQIVGIFNSVWGGFPAAVSWRSTSEQVHADLGVTPLA
Protein: BPI fold-containing family A member 1 (Palate lung and nasal epithelium clone protein) (P97361)
Organism: Mus musculus (Mouse)
Function: Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC) (By similarity). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid homeostasis and proper clearance of mucus (By similarity). Plays a role in the airway inflammatory response after exposure to irritants (By similarity). May attract macrophages and neutrophils (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:23499554}. Note=Apical side of airway epithelial cells. Detected in airway surface liquid, nasal mucus and sputum.
Interaction partners:
- BPI fold-containing family B member 1
- Secretoglobin family 3A member 1
- Uteroglobin
- Secretoglobin family 3A member 2
- BPI fold-containing family B member 4
- Mucin-2
- BPI fold-containing family B member 2
- BPI fold-containing family B member 6
- Lactotransferrin
Sequence:
MFLVGSLVVLCGLLAHSTAQLAGLPLPLGQGPPLPLNQGPPLPLNQGQLLPLAQGLPLAVSPALPSNPTDLLAGKFTDALSGGLLSGGLLGILENIPLLDVIKSGGGNSNGLVGGLLGKLTSSVPLLNNILDIKITDPQLLELGLVQSPDGHRLYVTIPLGLTLNVNMPVVGSLLQLAVKLNITAEVLAVKDNQGRIHLVLGDCTHSPGSLKISLLNGVTPVQSFLDNLTGILTKVLPELIQGKVCPLVNGILSGLDVTLVHNIAELLIHGLQFVIKV
Protein: SD09647p (Q5U1D9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MQATKMRTPFAIQEILGLGAYQQQATASATPSEAPPSPAATPPPTANTPANGSLSAVQQQQQQQQQQQQQQQQLQQQQQQAIDSLRESRSISPDVSRLSAAAAAAAAAAAHCQLPVFNPANFYAAAGYAAAADPGNAAAAHHHHMTTLAAAAYLRGFLPPGFSTPHEFRGHFQQHFGAQFAEQAAARGQEYASSLANASGDEQSPSKNSSSSGNGGSGGSGSGSGGGNPTSNGLGHLGSPTASNGGSGGGAGVGGSGGGSGTSGSSSSTSGNGGNGGSSGSRSSPAGPHHSAALAAHQHAAAAAAAAHHHAAAAAAAHHAHHAHAQAHAHAHAHVHAHAAHAAHAAHAHAHHAEAFLGAAGGAGGNPNSLLAAHGGDVLVGPGGTGPGGKKKNKRRHGRTIFTSSQLEELEKAFKEAHYPDVSARELLSMKTGLAEDRIQVWYQNRRAKWRKTEKCWGHSTKMAEYGLYGAMVRHSLPLPETIIKSAKEDESVAPWLLGMHKKSLEAAELLKSDESDRETPTSDDTNTSYSAGSTHNSPISSFSISRLLFDAPPPAAGSAGGKGHHHHHHHHKGHHHAHVHAQAQAHAHMLLHHQQQQQQQQQQQQHHHHLHAAENSLQQQQVAGTGSGSGSGSGSGTGAGSTGPPAHHPYNQQQHLHHLQQLQQQQQQQQQQAQQQQQHHHHQHHHSVHHMHHHNAAAGYAEAAVAAAAAAAAVAAAANARNAAAAAAVAAASASASAAVTIAESEAEEEQDDIEDMELDKDCEVEEDVEPVDNDTNTNNEHDNECDADADVEADVDADADADPEIDICDDHDEEMRLQEQLLLKVKQEQAHLGSR
Protein: valine--tRNA ligase (EC 6.1.1.9) (Valyl-tRNA synthetase) (Q587B4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GST N-terminal domain-containing protein
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- threonine--tRNA ligase
- Alanine--tRNA ligase
- Tyrosyl/methionyl-tRNA synthetase, putative
- serine--tRNA ligase
- GMP synthase
- arginine--tRNA ligase
- rRNA biogenesis protein, putative
Sequence:
MKQLAPQMAPAYIPKDVESGWYEWWEESGFFRPASDMGRPIRGRSFVIVSPPPNVTGHLHIGHALTGAVQDALIRFHRMKGDDTLYLPGTDHAGIATQVVVEKRLMKESGKSRHDVGREEFLKQVWVFKENHCGVITRQLRRIGLSLDWSRERFTMDEQCAKAVVEGFVKLHEDGLIYRATRLINWCCSLQSAISDLEVVFEDVPKNAKLTIPGYDRKVDMGVLTHVAYKFADSEDEIIIATTRPETILGDTAVAVHPDDERYKKYHGKRLKCPFRDETIPLILDPVLVDVNFGTGAVKITPAHDPNDFEAGLRHNLSQLTMMDLKGHVTTEGPFKGMHRFDCRREIVKELEKMGLLREVVPYEYRVGRCSRTGDIVEPLLMPQWFVDCTEMARKSVEAVRNNELRLYPPTHQVVWYHWLENIKPWCVSRQLWWGHRIPAYKCTGAVPSTHEDPWVVARNLEEAKAKAKEKFNLSDAEVRELVLEQDSDVLDTWFSSAMWPFSTMGWPAETGDMQRFFPGSLMETGHDILFFWVARMVMTSLHFTGKLPFSEVFLHAMVRDKNGEKMSKSKGNVIDPLFIISGVSLEALHDTVRSGNLDEKEVSRALKLQRETFPNGIPECGSDALRFGLLSYTQSGRNVNLDIDRVVAYRQLCNKLWNAVRFVLYHALGEDYKPKATLVNSQKVASLPLECRWILSRLDVAVEECTRGFSEGTYDFALATNAVYRFWLYELCDVYLELTKPTIQAGGEKKVIVQDVLLHVVEVALRLLHPMMPFLTEELWHYLPNYESFGVQSIVVAPYPEVSGWQDSQVEEQMKLLMETVHIVRSTKAFYSLTNKHKPDVWVTARAAETREIVESHKFMIESLGVVGRVSVIPPEEEAAAVPKGCGFAVVNKDLSINMMLLGFIDVQKEVAKLEKQLAGLQKQIEGVNKKISMPGYETKVPADVREANKVKLESLVEQEAQLTEGLTKMKSLL
Protein: Sphingolipid delta(4)-desaturase DES1 (EC 1.14.19.17) (Cell migration-inducing gene 15 protein) (Degenerative spermatocyte homolog 1) (Dihydroceramide desaturase-1) (Membrane lipid desaturase) (Retinol isomerase) (EC 5.2.1.-) (O15121)
Organism: Homo sapiens (Human)
Function: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). Catalyzes the equilibrium isomerization of retinols (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:30620338}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:30620338, ECO:0000269|PubMed:9188692}; Multi-pass membrane protein {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:9188692}.
Interaction partners:
- Ceramide synthase 6
- Ceramide synthase 2
- 3-ketodihydrosphingosine reductase
- Ceramide glucosyltransferase
- Ceramide synthase 5
- Ceramide synthase 4
- Ceramide synthase 3
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Sphingosine kinase 2
- Sphingosine kinase 1
Sequence:
MGSRVSREDFEWVYTDQPHADRRREILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNCKAMWNRWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRHQKGEMVLE
Protein: Signal recognition particle subunit SEC65 (P29478)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SEC65 is required for SRP integrity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP21
- Signal recognition particle subunit SRP54
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP14
- Signal recognition particle receptor subunit alpha homolog
- Signal recognition particle receptor subunit beta
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL38
Sequence:
MPRLEEIDDFNDIDDLDMELAELDPSLRTPIAPKITPKVVRSQDQENPAFLPGTNNNSNSNNNSSNEKEQLSFINPKTGKVERSEAISKKDLEEVKRFQVLYPCYFDINRSHKEGRRVPKELAVENPLAKTMADAVRELGILCIFEGEKCHPQDFGNPGRIRVLFKENGQLIGAATKFKGGKRQLMKAVGEYMKRHPTTIESLREIPYGPDFDNIEFKKIPRVKGFKMNEIVPLHSPFLMGHPMTKSVYETPKITAAEKSFKPPKNKYKVVRR
Protein: E3 ubiquitin-protein ligase DA2L (EC 2.3.2.27) (Protein DA2-like) (RING-type E3 ubiquitin transferase DA2L) (Q940G8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase involved in the regulation of organ and seed size. Probably functions to restrict cell proliferation during organ and seed development.
Interaction partners:
- Transcription initiation factor IIF, beta subunit
- At1g75700
Sequence:
MGNKLGRKRQIVDERYTKPQQGLYMSKDVDIKKLKKLILESKLAPCYPGLEETPSSHHDLEECPICFLYYPSLNRSRCCMKSICTECFLRMKSPNSAQPTQCPFCKTSNYAVEYRGGKTKEEKSFEQIEEQRVIEAKIRMRQKEVEDDEERMQKRLESYSSSSSTSAATLDTEYGSAAEDDEEIVSSQESCLPSHHPQVTRDGQFDFDLEDIMVMEAIWLSMQEPGIQRNTSPDDISEKDRNEEPSTPSSSSPSGGLACAIAVLAERQQMVGVSSSNQNVNLASQNLVPDNGNNSHYNAIEQDSNHYLQGAGISYTRSDMTDDSGGETSREVTWQ
Protein: Meiotic recombination protein DMC1/LIM15 homolog (Q14565)
Organism: Homo sapiens (Human)
Function: Participates in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks.
Subcellular location: Nucleus {ECO:0000269|PubMed:31429579}. Chromosome {ECO:0000250|UniProtKB:Q61880}.
Interaction partners:
- DNA repair protein RAD51 homolog 1
- Breast cancer type 2 susceptibility protein
- Meiotic recombination protein SPO11
- Serine-protein kinase ATM
- MutS protein homolog 4
- Breast cancer type 1 susceptibility protein
- Cyclin-dependent kinase 4
- Replication protein A 70 kDa DNA-binding subunit
- Homologous-pairing protein 2 homolog
- Fanconi anemia group M protein
Sequence:
MKEDQVVAEEPGFQDEEESLFQDIDLLQKHGINVADIKKLKSVGICTIKGIQMTTRRALCNVKGLSEAKVDKIKEAANKLIEPGFLTAFEYSEKRKMVFHITTGSQEFDKLLGGGIESMAITEAFGEFRTGKTQLSHTLCVTAQLPGAGGYPGGKIIFIDTENTFRPDRLRDIADRFNVDHDAVLDNVLYARAYTSEHQMELLDYVAAKFHEEAGIFKLLIIDSIMALFRVDFSGRGELAERQQKLAQMLSRLQKISEEYNVAVFVTNQMTADPGATMTFQADPKKPIGGHILAHASTTRISLRKGRGELRIAKIYDSPEMPENEATFAITAGGIGDAKE
Protein: Negative regulator of transcription (Ner) (Gene product 2) (gp2) (P06020)
Organism: Escherichia phage Mu (Bacteriophage Mu)
Function: Switches off the PcM promoter thereby blocking expression of the major repressor Repc (latency factor) and favoring transcription from the early promoter (Pe) and hence viral transposition and lytic development. Negatively regulates the early promoter (Pe) thereby controlling its own expression and keeping the level of early genes expression independent of the viral genome copy number.
Subcellular location: Host cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MCSNEKARDWHRADVIAGLKKRKLSLSALSRQFGYAPTTLANALERHWPKGEQIIANALETKPEVIWPSRYQAGE
Protein: Dipeptidase 1 (EC 3.4.13.19) (Beta-lactamase) (EC 3.5.2.6) (Microsomal dipeptidase) (P43477)
Organism: Ovis aries (Sheep)
Function: Hydrolyzes a wide range of dipeptides. Hydrolyzes the conversion of leukotriene D4 to leukotriene E4 (By similarity). Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation. Possesses also beta lactamase activity and hydrolytically inactivates beta-lactam antibiotics (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P16444}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P16444}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P16444}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P16444}. Note=Brush border membrane. {ECO:0000250|UniProtKB:P31429}.
Interaction partners:
- BTB domain-containing protein
- 2-oxoglutarate dehydrogenase-like, mitochondrial
Sequence:
MWTGWWLWPLVAVCTADQFRDNAVRLMQSTPVIDGHNDLPWALLKKFNNQLQDPRANLTSLNSTHTNIPKLKAGFVGAQFWSAYTPCDTQNKDSVKRTVEQIDVIQRMCQLYPETFLCVTDSAGIQQAFQEGKVASLVGVEGGHSIDSSLGVLRALYHLGMRYLTLTHSCNTPWADNWLVDTGEDKAQSQGLSSFGQSVVKEMNRLGIIIDLAHVSVATMEAALQLSKAPVIFSHSSAYSLCHHRRNVPDHVLQLVKQTGSLVMVNFYNDYVSCKAEANLSQVADHLDYIKKVAGAGAVGFGGDYDGVSRLPSGLEDVSKYPDLVAELLRRQWTEEEVRGALAENLLRVFKAVEQASDHKQAPGEEPIPLGQLEASCRTKYGYSGTPSLHLQPGSLLASLVTLLLSLCLL
Protein: ADP-ribosylation factor 6 (ARF6) (ADP ribosylation factor at 51F) (ADP-ribosylation factor 3) (P40946)
Organism: Drosophila melanogaster (Fruit fly)
Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity). Promotes cell movement and remodeling of the actin cytoskeleton during compound eye morphogenesis. Required for normal ethanol-induced tolerance and preference. Probably after Efa6-mediated activation, counteracts ethanol-induced sedation.
Subcellular location: Golgi apparatus.
Interaction partners:
- Kinesin-like protein
- PH and SEC7 domain-containing protein
- FI21420p1
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- ADP-ribosylation factor 1
- Rab11
- Exocyst complex component 5
- MIP16918p
- Arfaptin
- ADP ribosylation factor 4
Sequence:
MGKLLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARTELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLSEGLIWLTSNHKL
Protein: Dynein, axonemal, heavy chain 9 (Q5SX07)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MATVSQYAIDKSTLYAVESAVIKWSHQVQVVLKRESSQALIQGQNPTPKVELEFWKSRCEDLEHIYNQLMTIKVKGMAELLDKLQSSYLPAFKAMFRDVEAALTEAQDIHVHLLPLQQHLDILENVEFPKVKGRLRPLLHVVCLIWATCKWYRSPGRLTVLLQEICNLLIQQASNYLSPEDLLRSEVEESQKKLQVVSDTLSFFKQAFQDRREHLHTYFKEDSEVRVWDFQASLVFVRLDGFLGRVHMVEDLLKTALDLNNLEKLEFSGLRGNSLSQKVQRMHEEFEEMYKVFLDCSYDCLDPKGTEFENDVCEFNKRVEDLDRRLGTILIQAFDDAPDVEHAFKLLDITGTLIKRPLVAQDVSQKYLALIRMFSTELDAVRVIYSQHIQKEAEHGFSPVHKNMPTMAGGICWAQELRQRVKGPFGNFKNIPHLYLQSAEGKRMIQKYEDLLSLLEE
Protein: Kinesin-like protein (Q00085)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
TSRSHAIFSITVERSELGEGDVQHVRMGKLQLVDLAGSERQSKTQASGQRLKEATKINLSLSVLGNVISALVDGKSTHIPYRNSKLTRLLQDSLGGNSKTVMCATISPADSNYMETDITLRYASVLRIS
Protein: Nodulation protein E (EC 2.3.1.41) (Host-specificity of nodulation protein B) (C6KT99)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004533}.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- Beta-ketoacyl-ACP synthase III
- 3-oxoacyl-[acyl-carrier-protein] reductase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- Enoyl-acyl carrier reductase
- Acyl carrier protein
- Acyl carrier protein, mitochondrial, putative
- Inactive lipoate--protein ligase 2
- Acetyl-CoA carboxylase
- SAS6-like protein, putative
Sequence:
MRKYIIKIYYFLFFYVLQVNSKRYAFIKRGIPGISKNYFKGFKLYNSREMKNLCETSRVVCTGVGVVTGLGIGIEHFWNNIINGYTSIDKITKFDITGMSCGIGSEIKKSDFNPSDYYTNKKDVNRNDDCTHYAVAATRLALDDAKLNLEKLDKDKTGTIIGSGIGGLRFLEKEMKTMYEKGHKRITPYLIPAMIANTPSGYVSIENNIRGISLGMLSACATSGNTIGEAYRYIKYKEYDVMICGGTEASITPISFAGFNSLKALCTGYNDNPKKGCRPFDLKRSGFVMGEGSGILILESYEHAIKRNAPIYGEIISYSSECDAYHITAPEPNGKGLTNSIHKALKNANININDVKYINAHGTSTNLNDKIETKVFKNVFKDHAYKLYISSTKSMTGHCIGAAGAIESIVCLKTMQTNIIPPTINYEYKDPDCDLNYTPNKYIHAKENIDISLNTNLGFGGHNTALLFKKIVK
Protein: CCR4-NOT transcription complex subunit 3a isoform X2 (CCR4-NOT transcription complex, subunit 3a) (E9QGK5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADKRKLQGEIDRCLKKVAEGVEQFEDIWKKLHNAANANQKEKYEADLKKEIKKLQRLRDQIKTWVASNEIKDKRQLVENRKLIETQMERFKVVERETKTKAYSKEGLGLAQKVDPAQKEKEETEQWLTNTIDTLNMQVDQFESEVESLSVQTRKKKGDKEKQDRIEELKRLIERHRYHIRMLETILRMLDNDSIQVDAIHKIKDDVEYYIDSSQDPDFEENEFLYDDLDLEDIPATLMATSPQGHIEDEMFLQSSSTPTSTTSSSPIPPSPATGTTEILEDKRGRSTDSEVSQSPVKNGNPSLSSFSSSASSGSSSSSSSLVSMATVVGGCTAVSGGSSLLASFSSAVQQHPPQSQQQTQVKLSSTSIPSNNTPSPPSHPTLPASTASSLPSSSTPGPITSNSLSQASSVPGVESSRLGLGKGGVTVTSSSSVSQMPGLGLTSLSSSLNTMAGLLSGSTPAPYAQAAAGGTTGGASSGPVGSGSSSAGISIPSGVVGGANTGATSNGTGTGASIGLLGSSPGHGTLTGGILNLVQGQSALQGSTQVPVSPVGTAPGGGTGESGLGGNGSSSGVSGGVGTNVAPARPPSGLKQNGATSYSAVVADNTPDSSLSSASQSQNSHSSSSSSSTNQTLDNGPSLLSSITLPPSTPSPAFTDSTPGGGSLLNGPHSYTPNTEAIKAPEPPSSLKAMAERAALGLALDGEIPSLHLTDRDSLELFSGSSAPPGPTTAPQPAVSEVSLPPSLGACPLGPTPLTKEQLYQQAMQEAAWTHMPHPSDSERIRQYLMRNPCPTPPFHHQMPPHHSDSIEFYQRLSTETLFFIFYYLEGTKAQYLSAKALKKQSWRFHTKYMMWFQRHEEPKTITDEFEQGTYIYFDYEKWGQRKKEGFTFEYRYLEDRDLQ
Protein: TMEM14 protein homolog YJR085C (P47131)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized mitochondrial outer membrane protein YPR098C
- Putative uncharacterized protein YDL026W
- Uncharacterized protein YDR249C
Sequence:
MEHPAYTLSLLTTAGGLMGYYRKGSIPSLVSGLVFGSVYGIAGYLLHMNRDGGLEMALGASTLLLGAGVIRGMPSRFTKPVPVVLTALGGLGSYYYYNKYKEFYP
Protein: FI16633p1 (Q9VI97)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP08087p
- Uncharacterized protein
- Prolyl 4-hydroxylase alpha subunit domain-containing protein
- procollagen-proline 4-dioxygenase
- SCP domain-containing protein
- HDC01001
- Hat-trick, isoform D
- NTF2-related export protein
- Uncharacterized protein, isoform A
Sequence:
MANCNLVKVFLLVTLLGLSLMPFCQAHPKRGRKRAFGVGLLGGALAGAVIGNVVAKSQQAPAAAPAAPVAVVHHHYPPGAPAAPAPASQPDPKKMTVIETGTPDANGCYTQTIREPNPSNPKSYTETQHLICPTLQQANQPAPAIAPSIAQVPVMPQPSPVFPAVSPAAAPANVAPAPAAPVAPAAPAAPVVPVAPAAPSVVPVAPVAPVVVHPAAPILVHPAPVPVAAPAPAPIAPAVQQNPGQPQVILLSKKTVYYPKKRSSAPTLNTPQGVLAMLVIFYSIKAFTL
Protein: Wunen-2, isoform B (EC 3.1.3.-, EC 3.1.3.4) (A0A0B4LEJ6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLGFSLWGEAVKRGFFCDDSSLRHPYRDSTMPSWILYLMCGALPLTVMLVVEFFRGQDKRLHSPFPKSTMCSGYHLCHLELPTWLVECYHRMGIFIFGLGVEQLSTNIAKYSIGRLRPHFYTLCQPVMKDGTTCSDPINAARYIEEFTCAAVDITSKQLKDMRLSFPSGHASFACYSMLYLVIYLHRRMQWKQLRMLCHLLQFLLLMFAWYTALTRVSDYKHHWSDVLAGSGIGLTYAVVVTSTMW
Protein: Heat shock protein 75 kDa, mitochondrial (HSP 75) (Heat shock protein family C member 5) (TNFR-associated protein 1) (Tumor necrosis factor type 1 receptor-associated protein) (TRAP-1) (Q12931)
Organism: Homo sapiens (Human)
Function: Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23564345}. Mitochondrion inner membrane {ECO:0000269|PubMed:23564345}. Mitochondrion matrix {ECO:0000269|PubMed:23564345}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Cytochrome c
- Stress-induced-phosphoprotein 1
- Activator of 90 kDa heat shock protein ATPase homolog 1
- Prostaglandin E synthase 3
- 10 kDa heat shock protein, mitochondrial
- Serine/threonine-protein kinase PINK1, mitochondrial
- Stress-70 protein, mitochondrial
- Endoplasmic reticulum chaperone BiP
- Exostosin-1
Sequence:
MARELRALLLWGRRLRPLLRAPALAAVPGGKPILCPRRTTAQLGPRRNPAWSLQAGRLFSTQTAEDKEEPLHSIISSTESVQGSTSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVSDGQALPEMEIHLQTNAEKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLDALQNQAEASSKIIGQFGVGFYSAFMVADRVEVYSRSAAPGSLGYQWLSDGSGVFEIAEASGVRTGTKIIIHLKSDCKEFSSEARVRDVVTKYSNFVSFPLYLNGRRMNTLQAIWMMDPKDVREWQHEEFYRYVAQAHDKPRYTLHYKTDAPLNIRSIFYVPDMKPSMFDVSRELGSSVALYSRKVLIQTKATDILPKWLRFIRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRLIKFFIDQSKKDAEKYAKFFEDYGLFMREGIVTATEQEVKEDIAKLLRYESSALPSGQLTSLSEYASRMRAGTRNIYYLCAPNRHLAEHSPYYEAMKKKDTEVLFCFEQFDELTLLHLREFDKKKLISVETDIVVDHYKEEKFEDRSPAAECLSEKETEELMAWMRNVLGSRVTNVKVTLRLDTHPAMVTVLEMGAARHFLRMQQLAKTQEERAQLLQPTLEINPRHALIKKLNQLRASEPGLAQLLVDQIYENAMIAAGLVDDPRAMVGRLNELLVKALERH
Protein: Thioesterase pkgB (EC 3.1.2.-) (Pkg biosynthesis cluster protein B) (Q5AXB0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Thioesterase; part of the pkg gene cluster that mediates the biosynthesis of dihydrocitreoisocoumarin and 6,8-dihydroxy-3-(2-oxopropyl)-isocoumarin. The non-reducing polyketide synthase pkgA performs the condensation of one acetyl-CoA starter unit with 6 and 5 malonyl-CoA units, respectively. As pkgA lacks a releasing domain, the thioesterase pkgB is necessary to break the thioester bond and release dihydrocitreoisocoumarin and 6,8-dihydroxy-3-(2-oxopropyl)-isocoumarin from pkgA.
Interaction partners:
Sequence:
MSGGFYSSPFWAGYLETQRSRLPVLPEIDDGLSHCVVRFLGYNPGSMQLQGTNTYLVGTGSTRILIDTGEGAPQWAVSVTRYLEDHDISISHVLLTHWHKDHTGGVADLLAHDPSIIVYKHAPDPGQQAIANGQTFKTQGATLRAVLTPGHAVDHMCFLLEEENALFTGDNVLGHGYSVAEDLETYTASLRLMAGLKCSVGYPGHGDAILNLPQTIARYISQRVAREKKIYAILALHACSCSSRNGGSTSSIGSVSESGDSDEEDNNMKTSRPAMQGLSTAEIGGLVYGESVKNSPTFDSAVGPLLNQVLYMLLEQGKCCDHVSILVIFQKPGFFSIPVI
Protein: Ubiquitin-conjugating enzyme E2M (A0A8I5ZYZ8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MIKLFSLKQQKKEEESAGGTKGSSKKASAAQLRIQKDINELNLPKTCDISFSDPDDLLNFKLVICPDEGFYKSGKFVFSFKVGQGYPHDPPKVKCETMVYHPNIDLEGNVCLNILREDWKPVLTINSIIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRSMRGGYIGSTYFERCLK
Protein: Kynurenine 3-monooxygenase (EC 1.14.13.9) (Kynurenine 3-hydroxylase) (O15229)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract (Probable).
Subcellular location: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:9237672}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:9237672}.
Interaction partners:
- Kynureninase
- Kynurenine formamidase
- Kynurenine--oxoglutarate transaminase 1
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Kynurenine--oxoglutarate transaminase 3
- 3-hydroxyanthranilate 3,4-dioxygenase
- Tryptophan 2,3-dioxygenase
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
- Opsin-3
- Indoleamine 2,3-dioxygenase 1
Sequence:
MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSHRGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKKPRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCVLLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDDHAISDLSMYNYIEMRAHVNSSWFIFQKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQRWHWQKKVINKGLFFLGSLIAISSTYLLIHYMSPRSFLRLRRPWNWIAHFRNTTCFPAKAVDSLEQISNLISR