wanglab/gogpt-training-data huggingface dataset:
Protein: Trigger factor (TF) (EC 5.2.1.8) (PPIase) (P0A850)
Organism: Escherichia coli (strain K12)
Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates. Binds to nascent polypeptide chains via ribosomal protein L23. Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8633085}. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. {ECO:0000269|PubMed:8633085}.
Interaction partners:
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS10
- Peptide deformylase
- Elongation factor Ts
- Large ribosomal subunit protein uL22
Sequence:
MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNIVAQRYGASVRQDVLGDLMSRNFIDAIIKEKINPAGAPTYVPGEYKLGEDFTYSVEFEVYPEVELQGLEAIEVEKPIVEVTDADVDGMLDTLRKQQATWKEKDGAVEAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELPELTAEFIKRFGVEDGSVEGLRAEVRKNMERELKSAIRNRVKSQAIEGLVKANDIDVPAALIDSEIDVLRRQAAQRFGGNEKQALELPRELFEEQAKRRVVVGLLLGEVIRTNELKADEERVKGLIEEMASAYEDPKEVIEFYSKNKELMDNMRNVALEEQAVEAVLAKAKVTEKETTFNELMNQQA
Protein: von Willebrand factor A domain-containing protein 1 (A0A8I6ADR1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MRKHRHLPLVAVFSLLLSGITMTHAQQQSVMEVNKRDIVFLVDGSSSLGQANFNAIRDFISRVIQRLEIGQDLVQVSVAQYADTVKPEFYLNTYSTKKDAITTVRKMKALEGSALYTGSALDFVRNNLFTSSAGHRAAEGVPKLLVLITGGKSLDDVSQAAQELQKGSIMALVIGSRAADEDELKEIAFDSSLVFIPAEFRPAPLQSMLPSLMAPLRTLTGTTEEVKRDILFLFDGSVNVMGQFPAVRDFLYRIIEELDVKPDGTRVAIAQFSDDVRVESRFNEHQTKAEILNLVKKMKLKTGKGLNLGLALDHALRTIFVRSAGSRIEDNVQQFLVLLVAGRSTDAVAGPASSLKQRGVIPFIFQAKNANPSELEQIVPSPAFILAAESLPKIGDLQSEIVGLLKAKQTSDTVSGEKDVVFLIDGSEGVRSGFPLLKEFVQRVVESLDVGPNQVRVALVQYSDRTRPEFYLNSHMDQQGVISAIRRLTLLGGPTPNTGAALDFVLRNILTSSTGSRIEEGVPQLLIVLTAERSGDDVRGPSVVLKQGGAVPIGIGIGNADISEMQTISFIPDFAVAIPTFRELGTIQQVISERVIQLNREQLSSLTPVLMPSPSAGPGNKKDVVFLIDGSQNAGAEFQHIRTLIERLVEYLDIGFDTTRVAVIQFSEDTKMEFPLNAHFSKDEVQNAVRRLRPKGGRQVYIGNALEYVLKNIFQRPLGSRIEEGVPQFLVLISSGKSADEVDDSAVELKQFGVAPLTVARHTDQEELVKISLSPEYVFSVSTFRELPRLEQRLLTPITTLTSQQIQQILASTRYPPSVAESDAADIVFLIDSSDAMKPDGIAHIRDFVSRIVRRLNIGPNKVRIGVVQFSNDVFPEFYLKTHKSQNSVLEAIRRLRFKGGSPLNTGRALEFVARNLFVKSAGSRIEDGVPQHLVLFLGGKSQDDVSRHAQVISSSGIMSLGIGDRNIDRTDLQTITNDPRLVFTVREFRELPNIEERVMLSFGPSGPTPQPPEVEFPSSRPEKKKADIVFLLDGSINFRRDSFQEVLRFASEIVDTVYEDGDSIRVGLVQYNSDPTDEFFLRDFSTKRQIIDAINKVIYKGGRHANTRVGIEHLLKNHFVSEAGSRLDERVPQIAFVITGGKSVEDAQDVSLALTQKGVKVFAVGVRNIDSEEVGKIASNSATAFRVGSVQELSELSETVLETLHDAMHETLCPGVTDVSKACNLEVILGFDGSRDQNVFVSQKGLESKVDTILNRISQIQRISCSSNQLPTVRVSVVANTPSGPVEAFDFAEYQPDLFEKFRTMRSQHPYVLTADTLKLYQNKFRQSSPDTVKVVIHFTDGADGDMADLYRASEELRQAGVQALILVGLERVANLERLMQVEFGRGFMYDRPLRLNLLDLDYELAEQLDNIAEKACCGVPCKCSGERGDRGPIGSIGPKGISGEDGYRGYPGDEGGPGERGPPGVNGTQGFQGCPGQRGVKGSRGFPGEKGELGEIGLDGLDGEEGDKGLPGSSGEKGSPGRRGDKGPKGDKGERGDVGIRGDPGDSGRDSQQRGPKGETGDIGPMGLPGRDGIPGSPGDPGKDGGFGRRGPAGAKGNRGGPGQPGFEGEQGTRGSQGPPGPIGPPGLIGEQGIPGPRGGGGTAGAPGERGRTGPLGRKGEPGEPGPKGGTGNRGPRGETGDDGRDGVGSEGRRGKKGERGFPGYPGPKGTPGEPGADGPPGPKGIRGRRGNSGPPGVVGQKGDPGYPGPSGHRGNRGDSVDQCALIQSIRDKCPCCYGPLECPVFPTELAFALDTSEGVTQDTFSRMREVLLSIVGDLTIAESNCPRGARVAVVTYNNEVTTEIRFADSKKKSALLDSIQNLQVALTSKQPSLETAMSFVARNTFKRVRNGFLMRKVAIFFSNQPTKPSLQLREAVLKLSDAGITPLFLTSQEDRELINALQINNTAVGHALVLPARRDLRDFLKNVLTCHVCLDICNIDPSCGFGNWRPSFRDRRAAGSDVDIDLAFILDSSEATTLFQFNEMKKYISYMVRQLDLSPDPKASQHFARVAVVQQATYESVDNTSVPPVKVEFSLTDYGAKEKLLDFLSRRMTQLQGTMDLGNAIEYTIENIFESAPNPRDLKIVVLMLTGEIPREQLEEAQRAILQAKCKGYFFVVLGIGRKVNVKEVYSFASEPNDVFFKFMDKSTELNEEPLMRFGRLLPSFVGSGNAFYLPPDLRKQCDWFQGDQPVKNGVKFGHRQINTPHTVNSSLTSKVVTTMKPVTTTKPTSIVNLPPAKPAPVRPAPAQPVLAKPDPAKPVSAKSVPPQPVHAQPDPAQPVHVQSASAQTASAKPAPAKPAPPQTAAAKPAPPQTAAAKPAPPQTAAAKPAPPQTAAAKPVPVKPAPAQPVHVQSASAQTASAKPVPAKPAPPQTAAAKPVPVKPAVPAQPAPAQPVHAQPAPAQPVLTKPAAMKPASANKPVAAKPVATNTATVRPASAVKPAAASKPAATRPLPAAVRPVATKPEAPRPQAKPAATKPATTKPMARVSREVQVSEVTENSARLHWERPEPSSSYFYDLTVTSAHDQSLVLRQNLTVTDRVIGGLLAGQLYHVVVVSYLQSQVRAIYQGSFNTKKTQPPVLQAAHRASSSTINLMVNTEPLFLTKTDICKLPKDAGTCEDFKLLWHYDLESKSCKRFWYGGCGGNENRFHSQEECEKMCSPELSV
Protein: Methionine--tRNA ligase, cytoplasmic (EC 6.1.1.10) (Methionyl-tRNA synthetase) (MetRS) (Q68FL6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Plays a role in the synthesis of ribosomal RNA in the nucleolus.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56192}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P56192}. Note=Localizes to the nucleolus in proliferative cells but disappears in quiescent cells. {ECO:0000250|UniProtKB:P56192}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Arginine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Isoleucine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Leucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
Sequence:
MRLFVSEGSPGSLPVLAAAARARGRAELLISTVGPEECVVPFLTRPKVPVLQLDSGNYLFSASAICRYFFLLCGWEQDDLTNQWLEWEATELQPVLSAALHCLVVQGKKGEDILGPLRRVLTHIDHSLSRQNCPFLAGDTESLADIVLWGALYPLLQDPAYLPEELGALQSWFQTLSTQEPCQRAAETVLKQQGVLALRLYLQKQPQPQPPPPEGRTVSNELEEEELATLSEEDIVTAVAAWEKGLESLPPLKLQQHPVLPVPGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIYRWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPFCGYEEARGDQCDRCGKLINAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKTVPGSDWTPNARFIIRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYVSITANYTDQWEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAEDNYTLVKHIIATEYLNYEDGKFSKSRGIGVFGDMAKDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFINRAGMFVSKFFGGCVPEMALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGGEMDRQRAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPPAACRILATSFICTLPAGHRIGTVSPLFQKLENDQIENLRQRFGGGQAKGSPKPAAVEAVTAAGSQHIQTLTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGKPIETPKGKKKK
Protein: Endosialin (Tumor endothelial marker 1) (CD antigen CD248) (Q9HCU0)
Organism: Homo sapiens (Human)
Function: May play a role in tumor angiogenesis.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Fibronectin
- GTP-binding protein Rhes
- Mitochondrial inner membrane protein OXA1L
- Ubiquitin-associated domain-containing protein 1
- Plexin domain-containing protein 1
Sequence:
MLLRLLLAWAAAGPTLGQDPWAAEPRAACGPSSCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASRLLWIGLQRQARQCQLQRPLRGFTWTTGDQDTAFTNWAQPASGGPCPAQRCVALEASGEHRWLEGSCTLAVDGYLCQFGFEGACPALQDEAGQAGPAVYTTPFHLVSTEFEWLPFGSVAAVQCQAGRGASLLCVKQPEGGVGWSRAGPLCLGTGCSPDNGGCEHECVEEVDGHVSCRCTEGFRLAADGRSCEDPCAQAPCEQQCEPGGPQGYSCHCRLGFRPAEDDPHRCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGISCSPAGAMGAQASQDLGDELLDDGEDEEDEDEAWKAFNGGWTEMPGILWMEPTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPALSRDHQIPVIAANYPDLPSAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAGTQTTTHLPGIPPNHAPLVTTLGAQLPPQAPDALVLRTQATQLPIIPTAQPSLTTTSRSPVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISPTHPHSKAPQIPREDGPSPKLALWLPSPAPTAAPTALGEAGLAEHSQRDDRWLLVALLVPTCVFLVVLLALGIVYCTRCGPHAPNKRITDCYRWVIHAGSKSPTEPMPPRGSLTGVQTCRTSV
Protein: Nucleoredoxin-like protein 1 (Rod-derived cone viability factor) (RdCVF) (Thioredoxin-like protein 6) (Q8VC33)
Organism: Mus musculus (Mouse)
Function: Plays an important role in retinal cone photoreceptor survival. In association with glucose transporter SLC16A1/GLUT1 and BSG, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors. May play a role in cone cell viability, slowing down cone degeneration, does not seem to play a role in degenerating rods.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:15220920}.
Interaction partners:
- Zinc finger and BTB domain-containing protein 24
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
Sequence:
MASLFSGRILIRNNSDQDEVETEAELSRRLENRLVLLFFGAGACPQCQAFAPVLKDFFVRLTDEFYVLRAAQLALVYVSQDPTEEQQDLFLRDMPEKWLFLPFHDELRRDLGRQFSVRQLPAVVVLKPGGDVLTSDATEEIQRLGPACFANWQEAAELLDRSFLQPEDLDEPARRSITEPLRRRKYRVDRDVGRERGRNGRDSGDPQGDAGTRAELW
Protein: Somatostatin receptor type 5 (SS-5-R) (SS5-R) (SS5R) (SST5) (P35346)
Organism: Homo sapiens (Human)
Function: Receptor for somatostatin 28 and to a lesser extent for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Somatostatin
- Cortistatin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Appetite-regulating hormone
- Somatostatin receptor type 1
- D
- Somatostatin receptor type 2
Sequence:
MEPLFPASTPSWNASSPGAASGGGDNRTLVGPAPSAGARAVLVPVLYLLVCAAGLGGNTLVIYVVLRFAKMKTVTNIYILNLAVADVLYMLGLPFLATQNAASFWPFGPVLCRLVMTLDGVNQFTSVFCLTVMSVDRYLAVVHPLSSARWRRPRVAKLASAAAWVLSLCMSLPLLVFADVQEGGTCNASWPEPVGLWGAVFIIYTAVLGFFAPLLVICLCYLLIVVKVRAAGVRVGCVRRRSERKVTRMVLVVVLVFAGCWLPFFTVNIVNLAVALPQEPASAGLYFFVVILSYANSCANPVLYGFLSDNFRQSFQKVLCLRKGSGAKDADATEPRPDRIRQQQEATPPAHRAAANGLMQTSKL
Protein: phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) (EC 5.4.2.2) (Q6FMJ8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Glucose-6-phosphate isomerase
- Alpha-1,4 glucan phosphorylase
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen debranching enzyme
- phosphopentomutase
- Phosphotransferase
- Phosphotransferase
- Transketolase
- Phosphotransferase
- Phosphotransferase
Sequence:
MQVETVPTKPYQDQKPGTSGLRKKTKVFMEEPNYTENFIQAIMDAIPEGAKDAVLVVGGDGRFYNDVIMQKIAAIGAANGVRKLIIGQNGLLSTPAASHVIRSYAEKCTGGIILTASHNPGGPENDLGIKYNLANGGPAPEPVTNKMWEVSKQLTHYKIIKDFPQVDFSKIGKDQQYGPLLVDIIDTTEDYVKFMKEIFDFKLIKEFIHKQREAKNWKLLFDSLNGITGPYGKAIFVDEFDLPADEVLQNWHPQPDFGGLHPDPNLTYAHTLVERVDREKIEFGAASDGDGDRNMIYGAGPAFVSPGDSVAIIAEYAKEIPYFQKQGIYGLARSFPTSGAIDRVAKAQGLNCYEVPTGWKFFCALFDAKKLSICGEESFGTGSNHIREKDGVWAICAWLNILALYNKHNPEKEASIKTIQEEFWAKYGRTFFTRYDYEGITTEKANKVVDLLDKFVNDPKSKNAPFPGDESLTVSDCGDFSYTDLDGSVSDHQGLFVKLSNGARFVLRLSGTGSAGATIRLYIEEYSDDKSTYTQSADQYLQKMIKSVTSFLNFKELIGTDEPTVRT
Protein: Transcription elongation factor spt5 (Chromatin elongation factor spt5) (O13936)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The spt4-spt5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA-directed RNA polymerase II subunit rpb1
- Transcription elongation factor spt4
- FACT complex subunit spt16
- Transcription elongation factor spt6
- Cell division control protein 73
- RNA polymerase-associated protein C651.09c
- DNA-directed RNA polymerase II subunit rpb7
- DNA-directed RNA polymerase II subunit RPB3
- Transcription elongation factor S-II
- DNA-directed RNA polymerase II subunit rpb4
Sequence:
MDTNSPKSIDKDANSTEVDAAEQDAASVKINSTRASPNGSDLLNDDSEAAKITTNEKQSSPVDSHNESPNDTTINKGEDGNENEVDNVNNNDKKEDEDNVEENEEEADANEEEEEDEEDDEEDEEDEDESGGGRRKRARHDRRNQFLDIEAEVDEDEEELEDEEDEIGREDGFIEEEVGADYVGDDRRHRELDRQRQELQSVDAERLAEEYREKYGRSQTVVGDTSNVPQRLLLPSVNDPNIWAVRCKIGKEKDIVFTIMRKAMDLQYTSSPLEIISAFQRDSLVGYIYVEARKQSHVLDALNGVLNVYTNNMILVPIKEMPDLLKVQKQVVELLPGAYVRIRRGKYAGDLAQVDNLSENGLTARVRIVPRIDYSDGLKRKNSATRPQARLFNESEAFKSNPSKFSKRGPRLFLFNNEEFEDGFLVKDIRISSLITEGVNPTLDEVSKFNPNNEDLDLSSLALSVKGGHAEFQPGDHVEVYVGEQTGVSGVVENVRGSVITMVSSDGLRLDVPSRGLRKRFRHGDYVKVIAGKYKDDTGMVVRISKDEVTFLSDTLMTELTVFSRDLGEASSAQAVNSAYELHDLVQLDVNTVACIFSVDRDTYKVIDQNGGVRTVLASQITMRHSNRRGVATDRNGAEIRIGDKVKEVGGEGKQGTILHIYRAFVFLHNRDIAENNGVFSARSRNVATIAAKGARISADLTKMNPALSNGPALPPVANLKRTIGRDKAIGATVRIRRGPMKGLLGVIKDTTDANARVELHTGNKMVTIPKENLLYTTKTGELISYTEFIERSRGIRPGSISTADGPNVPNWAQGARTPAVANGSRTPAWNTGSRTPAWNSGSKTPAWNSGSRTPAWNSGNKTPAWNAGSRTPAWNSGNKTPAWNVGNKTPAWNSGAKTPAWNAGNKTPSWNNGTKTPAWNANQTPMVANGTNTSWGQTPAYGGFSETNWDTEDNSKPYTAPTPGAWAAPTPGGWDDEEGDSPKYVPPSP
Protein: Responsive to centrifugal force and shear stress gene 1 (Q1MW40)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSNPSAPPPYEDRNPLYPGPLPPGGYGQPSVLPGGYPAYPGYPQPGYGHPAGYPQPMPPTHPMPMNYGPGHGYDGEERAVSDSFGPGEWDDRKVRHTFIRKVYSIISVQLLITVAIIAIFTFVEPVSAFVRRNVAVYYVSYAVFVVTYLILACCQGPRRRFPWNIILLTLFTFAMGFMTGTISSMYQTKAVIIAMIITAVVSISVTIFCFQTKVDFTSCTGLFCVLGIVLLVTGIVTSIVLYFQYVYWLHMLYAALGAICFTLFLAYDTQLVLGNRKHTISPEDYITGALQIYTDIIYIFTFVLQLMGDRN
Protein: Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS) (NAGS) (P0A6C5)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000305|PubMed:16890}.
Interaction partners:
- Acetylglutamate kinase
- N-acetyl-gamma-glutamyl-phosphate reductase
- Argininosuccinate synthase
- Ornithine carbamoyltransferase subunit I
- Ornithine carbamoyltransferase subunit F
- Acetylornithine/succinyldiaminopimelate aminotransferase
- Argininosuccinate lyase
- Arginine repressor
- Acetylornithine deacetylase
- NADP-specific glutamate dehydrogenase
Sequence:
MVKERKTELVEGFRHSVPYINTHRGKTFVIMLGGEAIEHENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTLELVKQAAGTLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEDAIHRQLDSGAIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSELFPNEAQARVEAQEEKGDYNSGTVRFLRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQIVMESAEQIRRATINDIGGILELIRPLEQQGILVRRSREQLEMEIDKFTIIQRDNTTIACAALYPFPEEKIGEMACVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFVLTTRSIHWFQERGFTPVDIDLLPESKKQLYNYQRKSKVLMADLG
Protein: Dihydrolipoyl dehydrogenase 2, mitochondrial (AtmLPD2) (mtLPD2) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase 2) (Glycine cleavage system L protein 2) (Pyruvate dehydrogenase complex E3 subunit 2) (E3-2) (PDC-E3 2) (Q9M5K2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipoamide dehydrogenase is a component of the glycine decarboxylase (GDC) or glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. LPD1 is probably the protein most often associated with the glycine decarboxylase complex while LPD2 is probably incorporated into alpha-ketoacid dehydrogenase complexes.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14764908, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 5 of pyruvate dehydrogenase complex, chloroplastic
- Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic
- 2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial
Sequence:
MAMASLARRKAYFLTRNISNSPTDAFRFSFSLTRGFASSGSDDNDVVIIGGGPGGYVAAIKAAQLGLKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHVFANHGVKVSSVEVDLPAMLAQKDTAVKNLTRGVEGLFKKNKVNYVKGYGKFLSPSEVSVDTIDGENVVVKGKHIIVATGSDVKSLPGITIDEKKIVSSTGALSLTEIPKKLIVIGAGYIGLEMGSVWGRLGSEVTVVEFAADIVPAMDGEIRKQFQRSLEKQKMKFMLKTKVVGVDSSGDGVKLIVEPAEGGEQTTLEADVVLVSAGRTPFTSGLDLEKIGVETDKGGRILVNERFSTNVSGVYAIGDVIPGPMLAHKAEEDGVACVEFIAGKHGHVDYDKVPGVVYTYPEVASVGKTEEQLKKEGVSYNVGKFPFMANSRAKAIDTAEGMVKILADKETDKILGVHIMSPNAGELIHEAVLAINYDASSEDIARVCHAHPTMSEAIKEAAMATYDKPIHM
Protein: Glutathione gamma-glutamylcysteinyltransferase 1 (EC 2.3.2.15) (Cadmium tolerance protein) (Phytochelatin synthase 1) (AtPCS1) (Q9S7Z3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants. Also involved in glutathione-conjugates degradation.
Interaction partners:
- ABC transporter C family member 1
- ABC transporter C family member 2
- Metallothionein-like protein 1A
- Metallothionein-like protein 1C
- ABC transporter B family member 25, mitochondrial
- Glutamate--cysteine ligase, chloroplastic
- Glutathione synthetase, chloroplastic
- Beta-glucosidase 27
- WD repeat-containing protein PCN
- ACT domain-containing protein ACR3
Sequence:
MAMASLYRRSLPSPPAIDFSSAEGKLIFNEALQKGTMEGFFRLISYFQTQSEPAYCGLASLSVVLNALSIDPGRKWKGPWRWFDESMLDCCEPLEVVKEKGISFGKVVCLAHCSGAKVEAFRTSQSTIDDFRKFVVKCTSSENCHMISTYHRGVFKQTGTGHFSPIGGYNAERDMALILDVARFKYPPHWVPLKLLWEAMDSIDQSTGKRRGFMLISRPHREPGLLYTLSCKDESWIEIAKYLKEDVPRLVSSQHVDSVEKIISVVFKSLPSNFNQFIRWVAEIRITEDSNQNLSAEEKSRLKLKQLVLKEVHETELFKHINKFLSTVGYEDSLTYAAAKACCQGAEILSGSPSKEFCCRETCVKCIKGPDDSEGTVVTGVVVRDGNEQKVDLLVPSTQTECECGPEATYPAGNDVFTALLLALPPQTWSGIKDQALMHEMKQLISMASLPTLLQEEVLHLRRQLQLLKRCQENKEEDDLAAPAY
Protein: Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic (EC 2.3.1.12) (Dihydrolipoamide S-acetyltransferase component 4 of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2 4) (PDC-E2 4) (PDCE2 4) (plE2) (Q9SQI8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:10364395}.
Interaction partners:
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-2, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial
Sequence:
MAVSSSSFLSTASLTNSKSNISFASSVSPSLRSVVFRSTTPATSHRRSMTVRSKIREIFMPALSSTMTEGKIVSWIKTEGEKLAKGESVVVVESDKADMDVETFYDGYLAAIVVGEGETAPVGAAIGLLAETEAEIEEAKSKAASKSSSSVAEAVVPSPPPVTSSPAPAIAQPAPVTAVSDGPRKTVATPYAKKLAKQHKVDIESVAGTGPFGRITASDVETAAGIAPSKSSIAPPPPPPPPVTAKATTTNLPPLLPDSSIVPFTAMQSAVSKNMIESLSVPTFRVGYPVNTDALDALYEKVKPKGVTMTALLAKAAGMALAQHPVVNASCKDGKSFSYNSSINIAVAVAINGGLITPVLQDADKLDLYLLSQKWKELVGKARSKQLQPHEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGASKPTVVADKDGFFSVKNTMLVNVTADHRIVYGADLAAFLQTFAKIIENPDSLTL
Protein: Two-component response regulator ORR2 (OsRR2) (Q6YVX7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22383541}. Nucleus {ECO:0000269|PubMed:22383541}.
Interaction partners:
Sequence:
MGAEAVRVLVVDDSPVDRRVVELLLRAHCGGGGGAAAGEAAPFHVTAVDSGKKAMELLGRRRGDRDHLTPSSPAAAAAANDQAIDIVLTDYCMPEMTGYDLLKAIKALGSPNPIPVVVMSSENEPQRISRCLTAGAEDFILKPLKMNDVQRLRKCSGATRPKSAVAGDDDRCCNTAKKAAAAAAATPEQQQQQQRSSHLAGLAMVMNASSFEVSHYFQLIFKLILLAYAVLCLSQLLHRWSNGSSLLSLWCA
Protein: Glutathione S-transferase Mu 1 (EC 2.5.1.18) (GST 3-3) (GSTM1-1) (Glutathione S-transferase Yb-1) (GST Yb1) (P04905)
Organism: Rattus norvegicus (Rat)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process. Participates in the formation of novel hepoxilin regioisomers (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase theta-1
- Glutathione S-transferase alpha-4
- Epoxide hydrolase 1
- Glutathione S-transferase omega-1
- Microsomal glutathione S-transferase 1
- Glutathione S-transferase theta-2
- Cytochrome P450 1A1
- Glutathione S-transferase omega-2
- Glutathione peroxidase 1
- Cytochrome P450 2E1
Sequence:
MPMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRADIVENQVMDNRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSSRYLSTPIFSKLAQWSNK
Protein: Heat shock protein 90kDa alpha (Cytosolic), class A member 1 (C7G496)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Interaction partners:
Sequence:
MPEAVQTQDQPMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKDLKINLIPNKHDRTLTIVDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRLDNGEPLGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPIRLFVEKERDKEVSDDEAEEKEEEKEEKEEKTEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDEEELNKTKPIWTRNPDDITNEEYGEFYRSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFMRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHVYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVAKEGLELPEDEEEKKKQEEKKAKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDAAAEEASPAVTEEMPPLEGDDDTSRMEEVD
Protein: Mu-adaptin 1, putative (Q57YC8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- AP-4 complex subunit epsilon
- AP-1 complex subunit gamma
- AP complex subunit sigma
- AP complex subunit sigma
- AP complex subunit beta
- AP complex subunit beta
- Clathrin heavy chain
- AP-3 complex subunit delta
- AP complex subunit sigma
Sequence:
MASVFYILDSKGSPLICRSYRGDVTHNPPSVFQRRVLDEEEFRITPIFEEQGYIYCYIRVNNVFFLMVSKLNILPLQQFAFMRQCVTVFESYFKHVLEETIMDNFVIVYELLDEMCDFGFPQYTEEKSLKKYITQESLISYLLPEDKLHVKELPAEASGRGGLTPWRQPGKYKYRKNEVFLDVIESVNILLSPGGETLSSEICGQIKMRVRLSGMPVLKLGLNDKATFEMLASRGRAVEMEGVKLHQCVKLSQFESHRVISFVPPDGEFELMSYRTSKKVAPMVTVECTTVSKSATQVEMALVARTTFRRTLTASFLDILVPVPSDAFKPEGRCSAGKVRHAPESNLLMWSLREVSGGKQFTCSFKFSLPSVRSSDPSVFAKAPVQVKFEVPYLTASGIQVRYLKVEEEPNYQALSWVRYVTQSGDYQIRTA