wanglab/gogpt-training-data huggingface dataset:
Protein: Endonuclease G, mitochondrial (Endo G) (EC 3.1.30.-) (P38447)
Organism: Bos taurus (Bovine)
Function: Endonuclease that preferentially catalyzes the cleavage of double-stranded 5-hydroxymethylcytosine (5hmC)-modified DNA (By similarity). The 5hmC-modified nucleotide does not increase the binding affinity, but instead increases the efficiency of cutting and specifies the site of cleavage for the modified DNAs (By similarity). Shows significantly higher affinity for four- stranded Holliday junction over duplex and single-stranded DNAs (By similarity). Promotes conservative recombination when the DNA is 5hmC-modified (By similarity). Promotes autophagy through the suppression of mTOR by its phosphorylation-mediated interaction with YWHAG and its endonuclease activity-mediated DNA damage response (By similarity). GSK3-beta mediated phosphorylation of ENDOG enhances its interaction with YWHAG, leading to the release of TSC2 and PIK3C3 from YWHAG resulting in mTOR pathway suppression and autophagy initiation (By similarity). Promotes cleavage of mtDNA in response to oxidative and nitrosative stress, in turn inducing compensatory mtDNA replication (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q14249}.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Cytochrome c
- Cytochrome c 2
- Zinc phosphodiesterase ELAC protein 2
- Apoptosis-inducing factor 1, mitochondrial
- Flap endonuclease 1
- Adenosine 5'-monophosphoramidase HINT2
- Caspase-9
- Serine protease HTRA2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
Sequence:
MQLLRAGLTLALGAGLGAAAESWWRQRADARATPGLLSRLPVLPVAAAAGLPAVPGAPAGGGPGELAKYGLPGVAQLKSRASYVLCYDPRTRGALWVVEQLRPEGLRGDGNRSSCDFHEDDSVHAYHRATNADYRGSGFDRGHLAAAANHRWSQKAMDDTFYLSNVAPQVPHLNQNAWNNLEKYSRSLTRTYQNVYVCTGPLFLPRTEADGKSYVKYQVIGKNHVAVPTHFFKVLILEAAGGQIELRSYVMPNAPVDEAIPLEHFLVPIESIERASGLLFVPNILARAGSLKAITAGSK
Protein: EGF-like domain-containing protein (Q54KR8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- U1 small nuclear ribonucleoprotein C
Sequence:
MKLLLLLFLIINSIILSKCGYSQTNEKIIVTGEFDKTIDKYTISFSNIGDITQLCSINTTILTCFPPAKSINGGFLVYDKEEGTNVIDITTVVLSPYISSMDPKVIPTSSIEITIRGFYFNANSNPETNKTSTHLLVTIGGSNVDINSTASDSVKFYPPSFFQTPLTISLTNVDSGKKSNSIKFKYELPNIESLSVVDIKDNNNKTTQQYLNISGTNFGSKQSMKLVFVEIHDFNNDSLIITKLTDILSINDTNLLIKINSDSSSGNIYVNANSQQSNTLPLYLTPIITNVDFPNYNGDTINITGSYLSDIYLSPSTKLNCSTILIKDSNTDDDDNGDDTLSSTSDSSSSSTKATTSSSSNNNIYYKKCKFPQRNLNDSISFSIFSRSVGNNVNHDSNEFKSHYQKPIIDAVVPNGFYVNNKLNFTFYGTNWANYTNTTITIADKPCKVLEITSSTIVCYYEAGVEILQNPISYVITVDGQRNNIAPDSDTSTISFYSLCPGQSFSNGTTSPTSSTNTTTQGCSNSGTCNPVTGLCQCLPTKTGKICDQDKYSSNSTSKLLSTSSLFLLLLIFITLFY
Protein: Glutathione reductase (EC 1.6.4.2) (O64409)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
NSARGNILNNAGVTLIEGRGKIVDPHTVSVNGKLYTAKHILVSVGGRPSMPDIPGIEHVIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGITFHTEQSPQAITKSNDGLLSLKTNKENFGGFSHVMFATGRRPNSKNLGLEAVGVEMDKNGAIVVDEYSRTSVDSIWAVGDVTNRVNLTPVALMEGGAFAKTVFGNEPTKPDYRAIPSAVFSQPPIGQVGLTEEQAIEEYGDVDVFVANFRPLKATLSGLPDRVLMKILVCATSNKVVGVHMCGDDAPEIIQGIAIAVKAGLTKQDFDATIGIHPTSAEEFVTMRSPTRKIRKSSTDQVESKDEVVSKQ
Protein: NOTCH-1 (Q9W737)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Endomembrane system {ECO:0000256|ARBA:ARBA00046288}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00046288}.
Interaction partners:
Sequence:
LNGGTCISMHKSSKCVCAAAFTGPECQYPASSPCISNPCYNGGTCEFLSDASPYYHCNCPANFNGLNCHILDFDFQGGFGQDIIPPKIEEKCEIAVCASYAGNKICDGKCNNHACGWDGGDCSLNFNDPWKNCSQSLQCWKYFNDGKCDSQCNNAGCLYDGFDCQKYEGQCNPLYDQYCKDHFSDGHCDQGCNNFECEWDGLDCANNMPEKLADGTLVVVVLITPENLKNNSFNFLRELSRVLHTNVVFKKNAKGEYMIFPYYGNEEELKKHYIKRSTEDWADMSSAVINKVKSSLYSRAGRRQKRELDQMDIRGSIVYLEIDNRQCIQSSSQCFQSATDVAAFLGALASLGNLNIPYKIEAVKSETAEPARNSQLYPMYVVVAALVLLAFIGVGVLVSRKRRREHGQLWFPEGFKVTESSKKKRREPLGEDSVGLKPLKNASDGTLMDDNQNEWGDEETLDTKKFRFEEQAMLPDTDDQTDHRQWTQQHLDAADLRISSMAPTPPQGEIDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEDDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINCHADVNAVDDLGKSALHWAAAVNNVEAAVVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPPLHSGPLGAPTLSPPLCSPSSYIGNLKPAVQGKKARKPSTKGLSCNGKDSKDLKARRKKSQDGKGCLLDNSSVLSPVDSLESPHGYLSDVASPPLMTSPFQQSPSMPLNHLPGMPDAHMSINHLNMAGKQEMALGGSGRMAFEAVPPRLSHLPVSSPSTAMSNAPMNFSVGGAAGLSGQCDWLSRLQSGMVQNQYGAMRGGMQPGTHQQAQNLQHGMMSSLHNGLPSTSLSQMMSYQAMPSTRLASQPHLLQNQQMQQMQQPGMQPQPGMQPQPGMQQPQQQPQQQPQPQQHHNPGSNASGHMGQNFLGTELSQPDMQPVSSSAMAVHTILPQDSQLLPTSLPSSLAQPMTTTQFLTPPSQHSYSSPLDNTPSHQLQVPDHPFLTPSPESPDQWSSSSPHSNVSDWSEGISSPPTSMQSQMGHIPEAFK
Protein: MAP kinase kinase kinase mkh1 (EC 2.7.11.25) (Q10407)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May regulate cell morphology, cell wall integrity, salt resistance, cell cycle reentry from stationary-phase arrest, and filamentous growth in response to stress. Activates the MAP kinase kinase skh1/pek1 by phosphorylation.
Interaction partners:
- MAP kinase kinase skh1/pek1
- Protein kinase C-like 1
- Shk1 kinase-binding protein 5
- Mitogen-activated protein kinase spm1
- GTP-binding protein rho2
- Protein kinase C-like 2
- Protein kinase wis1
- Protein kinase byr1
- GTP-binding protein rho1
- Rho1 guanine nucleotide exchange factor 2
Sequence:
MAADIGSQSSGSLEERFEQSLHLQNVDKQDWSLNSVLQFLKLYKFNKEWEDVFIKSRIEMDLFINLADQSKAEEFAFKNKLSKESAIQLSSCIRKTLLAPSSTRVPSKNSSYETLTYSAKDSSDDVFTETNSGFRSSNQNSSLKSFQSVPDSNVNVFGGFGGSVVDNNELLSTGKNSHQTTSLNLEGSPINLHAYKGTVTSIINDDSRNINKKTLSKQPVSEHKEKQTSFLRRFRVPGFSRDKDKTKDCPSSNSNPFHLASSNVKTLDASLDQGEWVPRIHRLESQIGLISKKKSFVLATMDDMKFTVVDITNVQNATQLRKLIAKSMYLDISIDQFDLFLTEVGGAQYIEILDDRKLDIARLYSDEFGTIKFFVKPSQNEESGMDSDTYLSFGTKSSSTYKADDDSIYHRKEDFKKQPSYPVLTSDFEITDAGPNLSLSGHQPDNKYYKGFSSAPNLAVVPELPSRRFRGFEKIRGAKGEMATKILDATEAQSEKNKFTVCRPHKKVTLKMPLNSGSSAPQSPSSNTSASVLTRNFVAHRDPPPPPTETSSLRRKNTLTRRPSIRHARSSPYIDTGHNEASKFSHTSFDPKASSKSSNSLKESVEALSEIPFEDAPALDESDLSGDPFWAIQPKQSSSQVPKENHHNIQSKLSINTEAATDLKANELSSPKTPEYCRGDDRSISLSPLSYRLRKSKHIRESPPSSKVINSGNWEVRPSADDLYEDVDRFFPRYDLDKVLVVDQSRMVSSPSKVSIRPKMKSVRLLAREASEARKEIRHNARRNKSGNLLRRSSTKLWGSRIVELKPDTTITSGSVVSQNATFKWMKGELIGNGTYGKVFLAMNINTGELIAVKQVEIPQTINGRHDQLRKDIVDSINAEISMIADLDHLNIVQYLGFEKTETDISIFLEYVSGGSIGRCLRNYGPFEEQLVRFVSRQVLYGLSYLHSKGIIHRDLKADNLLIDFDGVCKISDFGISKHSDNVYDNDANLSMQGSIFWMAPEVIHNDHQGYSAKVDVWSLGCVVLEMLAGRRPWSTDEAIQAMFKLGTEKKAPPIPSELVSQVSPEAIQFLNACFTVNADVRPTAEELLNHPFMKCDEEFNFKDTNLYDMLCKRKS
Protein: TM6SF1 protein (Transmembrane 6 superfamily member 1) (Q8N5N8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSASAATGVFVLSLSAIPVTYVFNHLAAQHDSWTIVGVAALILFLVALLARVLVKRKPPRDPLFYVYAVFGFTSVVNLIIGLEQDGIIDGFMTHYLREGEPYLNTAYGHMICYWDGSAHYLMYLVMVAAIAWECWHICSILFLTL
Protein: L-rhamnose mutarotase (EC 5.1.3.32) (Rhamnose 1-epimerase) (Type-3 mutarotase) (P32156)
Organism: Escherichia coli (strain K12)
Function: Involved in the anomeric conversion of L-rhamnose.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- L-rhamnose isomerase
- Rhamnulose-1-phosphate aldolase
- L-Rhamnulokinase
- Uncharacterized protein YbfB
- L-rhamnose-proton symporter
- L-rhamnonate dehydratase
Sequence:
MIRKAFVMQVNPDAHEEYQRRHNPIWPELEAVLKSHGAHNYAIYLDKARNLLFAMVEIESEERWNAVASTDVCQRWWKYMTDVMPANPDNSPVSSELQEVFYLP
Protein: DnaJ homolog subfamily A member 2 (RDJ2) (O35824)
Organism: Rattus norvegicus (Rat)
Function: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1A
- Heat shock cognate 71 kDa protein
- Heat shock-related 70 kDa protein 2
- Heat shock 70 kDa protein 1-like
- Stress-induced-phosphoprotein 1
- DnaJ heat shock protein family
- Heat shock protein HSP 90-beta
- DnaJ homolog subfamily A member 1
- Endoplasmic reticulum chaperone BiP
Sequence:
MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLFVQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDARQIVVKYPPGKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPEVPNVIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ
Protein: Zinc finger and BTB domain containing 32 (A0A0C4DGF1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLPPIRLPSPYGSDRLVQLAARLRPALCDTLITVGSQEFPAHSLVLAGVSQQLGRRGQWALGEGISPSTFAQLLNFVYGESVELQPGELRPLQEAARALGVQSLEEACWRARGDRAKKPDPGLKKHQEEPEKPSRNPERELGDPGEKQKPEQVSRTGGREQEMLHKHSPPRGRPEMAGATQEAQQEQTRSKEKRLQAPVGQRGADGKHGVLTWLRENPGGSEESLRKLPGPLPPAGSLQTSVTPRPSWAEAPWLVGGQPALWSILLMPPRYGIPFYHSTPTTGAWQEVWREQRRTCNLCGS
Protein: Protein MPA43 (P53583)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- DNA-directed RNA polymerase I subunit RPA49
- Putative uncharacterized protein YLR379W
- 26S proteasome regulatory subunit RPN10
- 26S proteasome regulatory subunit RPN7
- 26S proteasome regulatory subunit RPN1
- 26S proteasome regulatory subunit RPN2
- 26S proteasome regulatory subunit RPN6
- 26S proteasome regulatory subunit RPN12
- 26S proteasome regulatory subunit RPN3
Sequence:
MNSSLQVGIGIDVGSSSARIGVYNYYNDALLEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCLQKLNIREYEVKSCGVSATCSLAIFERDRTSNMLIPYPNEDNVIFWMDSSAVNECQWLNMQCPQQLLDYLGGKFVPEMGVPKLKYFLDEYSHLRDKHFHIFDLHQYIAYELSRLYEWNIEGLLGRENLNGIGNDGEVSGWSSSFYKNIINLPSNVSIGTTSLVANKHISTTVVRSCIDSYASWFAVASPHLETSLFMIAGTSSCYMYGTTISDTRIPGVWGPFDTILDNRGDFSVYAAGQSCTGKLIEHLFESHPCARKILKDGADIYQVLEQTIRDIEKNNGLSIHILTKDMFFYGDYEGNRTPFADPRIKGSFIGESTDTSMLNLTYKYICILEFLSFQTKLIIDTFQNENSNIHIKELRISGSQAKNERLLSLISLVNNGVAIIKPKENVDMMGIKGAYVLAKSAKEKKQLADVITERDISNDSEKFESLAEYRLGNDSILLRKLLCVKYHIHLDMAKQQKRYHKLVDEVFQHL
Protein: Pyrroline-5-carboxylate reductase (EC 1.5.1.2) (A0A0A0MQS1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGERSGVRGNKMAAAEPSPRRVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRNLCHFQALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEVAPVVTTEHILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETKLLQHLLEACGRCEEVPEAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLHALEQGGLRAATMSAVEAATCRAKELSRK
Protein: Nuclear receptor coactivator 1 (NCoA-1) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 74) (bHLHe74) (Protein Hin-2) (RIP160) (Renal carcinoma antigen NY-REN-52) (Steroid receptor coactivator 1) (SRC-1) (Q15788)
Organism: Homo sapiens (Human)
Function: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma
- CREB-binding protein
- Retinoic acid receptor RXR-alpha
- Histone acetyltransferase p300
- Estrogen receptor
- Estrogen receptor beta
- Nuclear receptor subfamily 1 group I member 2
- Peroxisome proliferator-activated receptor alpha
- Signal transducer and activator of transcription 6
- Nuclear receptor coactivator 2
Sequence:
MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSLSVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEALDGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNGVPWPQEATRRNSHTFNCRMLIHPPDEPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQSCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDTNSGMSIPRVNPSVNPSISPAHGVARSSTLPPSNSNMVSTRINRQQSSDLHSSSHSNSSNSQGSFGCSPGSQIVANVALNQGQASSQSSNPSLNLNNSPMEGTGISLAQFMSPRRQVTSGLATRPRMPNNSFPPNISTLSSPVGMTSSACNNNNRSYSNIPVTSLQGMNEGPNNSVGFSASSPVLRQMSSQNSPSRLNIQPAKAESKDNKEIASILNEMIQSDNSSSDGKPLDSGLLHNNDRLSDGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSCTGTSNSASANSSGGSCPSSHSSLTERHKILHRLLQEGSPSDITTLSVEPDKKDSASTSVSVTGQVQGNSSIKLELDASKKKESKDHQLLRYLLDKDEKDLRSTPNLSLDDVKVKVEKKEQMDPCNTNPTPMTKPTPEEIKLEAQSQFTADLDQFDQLLPTLEKAAQLPGLCETDRMDGAVTSVTIKSEILPASLQSATARPTSRLNRLPELELEAIDNQFGQPGTGDQIPWTNNTVTAINQSKSEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKLVQGGGLDVLSERFPPQQATPPLIMEERPNLYSQPYSSPSPTANLPSPFQGMVRQKPSLGTMPVQVTPPRGAFSPGMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLIHQNRQAILNQFAATAPVGINMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQLIQQQRAMLMRQQSFGNNLPPSSGLPVQMGNPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLANRNSMVSRGMTGNIGGQFGTGINPQMQQNVFQYPGAGMVPQGEANFAPSLSPGSSMVPMPIPPPQSSLLQQTPPASGYQSPDMKAWQQGAIGNNNVFSQAVQNQPTPAQPGVYNNMSITVSMAGGNTNVQNMNPMMAQMQMSSLQMPGMNTVCPEQINDPALRHTGLYCNQLSSTDLLKTEADGTQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE
Protein: Probable elongation factor 1-gamma 2 (EF-1-gamma 2) (eEF-1B gamma 2) (Q9FVT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably plays a role in anchoring the complex to other cellular components.
Interaction partners:
- Small ribosomal subunit protein uS2z
- Elongation factor 1-delta 1
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein uS2y
- Large ribosomal subunit protein uL10y
- Large ribosomal subunit protein uL18y
- Elongation factor 1-delta, putative
- Small ribosomal subunit protein eS1y
- Large ribosomal subunit protein uL10x
- Elongation factor 1-beta 2
Sequence:
MALVMHTYKGNKGANKALIAAEYAGVKIEESADFQMGVTNKSPEFLKMNPIGKVPVLETPEGPIFESNAIARYVSRKNGDNSLNGSSLIEYAHIEQWIDFSSLEIDANMLKWFAPRMGYAPFSAPAEEAAISALKRGLEALNTHLASNTFLVGHSVTLADIVTICNLNLGFATVMTKKFTSAFPHVERYFWTMVNQPEFKKVLGDAKQTEAVPPVPTKKAPQPAKPKEEPKKAAPVAEAPKPAEEEEAPKPKAKNPLDLLPPSPMVLDDWKRLYSNTKSNFREVAIKGFWDMYDPEGYSLWFCDYKYNDENMVSFVTLNKVGGFLQRMDLARKYSFGKMLICGSEGPFKVKGLWLFRGPEIPKFIMDEVYDMELYEWTKVDISDEAQKERVSQMIEDAEPFEGEALLDAKCFK
Protein: Voltage-dependent chloride channel 1, chloroplastic (AtVCCN1) (BESTROPHIN-like protein 1) (AtBest1) (Q9M2D2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Voltage-dependent chloride (Cl) channel critical for proton motive force (PMF) partitioning across the thylakoid membrane by anion influx into the lumen during illumination, thus being required for photoprotection under fluctuating light conditions. Influences thylakoid ultrastructure, including lumen size and organization. During photosynthetic response on transition from dark to low light, involved in a sequential mechanism of adaptation; VCCN1 and CLCe first trigger the activation of photoprotection, which is later down-regulated by KEA3 to a low steady state, while adjusting electron transport. On transition from low to high light, accelerates the activation of photoprotection by building up a pH gradient across the thylakoid membrane.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:26947269, ECO:0000269|PubMed:27216227}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chloride channel protein CLC-e
- K
Sequence:
MYQSMNLSVSSNFTHRSLLESRFPIFSTGFRKSVNLKPPRVSSGPESNDSGHETLTDKLIHLLRAVPDWADEIKERGMQQKRSLYTHEKWVEHRSSLRHVRHLLSSFSSRVILSLIPPVFFFTSVAVVIASYNSAVALDWLPGIFPILRSSSLPYQLTAPALALLLVFRTEASYSRYEEGRKAWVGIIAGTNDLARQVICSVDSSGDELIIKDLLLRYIAAFPVALKCHVIYGSDIARDLRNLIEADDLSLILQAKHRPRCVIEFISQSIQLLKLDDAKRDLLESKMLHLHEGIGVCEQLMGIPIPLSYTRLTSRFLVFWHLTLPIILWDECHWIVVPATFISAASLFCIEEVGVLIEEPFPMLALDELCDLVHSNIQEAVKSEKVIRNRIIAKIKLHEFKHSSNGRHRS
Protein: Protein DETOXIFICATION 40 (AtDTX40) (Multidrug and toxic compound extrusion protein 40) (MATE protein 40) (Q9LVD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17151019, ECO:0000269|PubMed:23903016}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:23903016}.
Interaction partners:
- Phototropic-responsive NPH3 family protein NPY4
- Heavy metal-associated isoprenylated plant protein 35
- VAN3-binding protein
- Metal tolerance protein 9
- Protein DETOXIFICATION 42
- Serine/threonine-protein kinase D6PKL1
- Protein PIN-LIKES 7
- Metal tolerance protein B
- Cation/H
Sequence:
MDSSPNDGVHQPLLHPQPSPSPPESTNGELETVLSDVETPLFLRLRKATIIESKLLFNLAAPAVIVYMINYLMSMSTQIFSGHLGNLELAAASLGNTGIQVFAYGLMLGMGSAVETLCGQAYGGRKYEMLGVYLQRSTVLLTLTGLLLTLIYVFSEPILLFLGESPAIASAASLFVYGLIPQIFAYAANFPIQKFLQSQSIVAPSAYISTATLFVHLLLSWLAVYKLGMGLLGASLVLSLSWWIIVVAQFVYIVTSERCRETWRGFSVQAFSGLWSFFKLSAASAVMLCLETWYFQILVLLAGLLENPELALDSLSICMTISGWVFMISVGFNAAISVRVSNELGAGNPKSAAFSVIIVNIYSLITCVILAIVILACRDVLSYAFTEGKEVSDAVSDLCPLLAVTLVLNGIQPVLSGVAVGCGWQTFVAKVNVGCYYIIGIPLGALFGFYFNFGAKGIWTGMIGGTVIQTFILAWVTFRTDWTKEVEEASKRLDKWSNKKQEVVPE
Protein: CCAAT/enhancer binding protein (C/EBP) 1 (Myeloid-restricted CCAAT/enhancer-binding protein 1) (Q90ZW4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSVSDNIFSVHEASSDSSAQTPMDSALYTQTISFTKSPEVMMGYLPYSSCLNNPNTNTERSVQQSSAHTQDFAQFLEPPPASALRLCAQKRGVSKDSAEYRQRRERNNIAVRKSRDKARRRIQMTQQRALQLQDENHRLQVHIQRLLHEVEALRHYLSQRHLQDTSEEH
Protein: AT3G21215 protein (At3g21211) (RNA-binding (RRM/RBD/RNP motifs) family protein) (Q9ASW4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- MLO-like protein 6
- MLO-like protein 12
- MLO-like protein 2
Sequence:
MAGAGIHPYHQQWPPAGAPPPPAAVSSAAPPHPPPIHHHPPPPPVLVDNHNRPPYDELRTIFIAGLPDDVKERELLNLLRWLPGYEASQVNFKGEKPMGFALFSTAQFAMAAKDTLQHMVFDAESKSVIHTEMAKKNLFVKRGIVGDSNAYDQSKRLRTGGDCTHSVYSPSPFHPPPPPVWGPPHGYMAPAPPPYDPYAGYHAPPVPMPTPPPIAAPSSYVPVQNIKDNPPCNTLFIGNLGENINEEELRSLLSAQPGFKQMKILRQERHTVCFIEFEDVNSATNVHHNLQGAVIPSSGSIGMRIQYSKNPYGKRKEGGGYSFFPSPSANGAQGALTYQ
Protein: (+)-caryolan-1-ol synthase (EC 4.2.1.138) ((+)-beta-caryophyllene synthase) (EC 4.2.3.89) (B1W019)
Organism: Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235)
Function: Sesquiterpene cyclase that first catalyzes the cyclization of farnesyl diphosphate (FPP) to the bicyclic sesquiterpene (+)-beta-caryophyllene intermediate, and then its conversion to (+)-caryolan-1-ol via a second cyclization and the addition of a water molecule.
Interaction partners:
Sequence:
MSQITLPAFHMPFQSAGCHPGLAETREAAWEWAAAEGLDLSVPARRKMIRTRPELWISLIFPQATQAHLDLFCQWLFWAFLVDDEFDDGPAGRDPLMCERAIARLVDVFDGAAPNGPMERALAGLRDRTCRGRSPQWNRQFRRDTAAWLWTYYAEAVERAAGQVPSRAEFAKHRRDSVAMQPFLCLHEITAGIDLPDSARSLPAYIALRNAVTDHSGLCNDICSFEKEAALGYEHNAVRLIQRDRGSTLQEAVDEAGIQLARIAERVQRAERELIEEIEAAGIDGPTRTALERCVRDYRGLVRGDFDYHARAERYTRPDLVELDERDSLSRHFAA
Protein: Fe(2+) transporter FeoB (Ferrous iron transport protein B) (P33650)
Organism: Escherichia coli (strain K12)
Function: Transporter of a GTP-driven Fe(2+) uptake system, probably couples GTP-binding to channel opening and Fe(2+) uptake. A guanine nucleotide-binding protein (G proteins) in which the guanine nucleotide binding site alternates between an active, GTP-bound state and an inactive, GDP-bound state. This protein has fast intrinsic GDP release, mediated by the G5 loop (about residues 149-158). Presumably GTP hydrolysis leads to conformational changes and channel closing. A GDP release mechanism involving a conformational change of the G5 loop (and thus the removal of the nucleotide-binding and stabilizing interactions) would significantly reduce the affinity for GDP, and conceivably be sufficient for catalysing nucleotide release.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein.
Interaction partners:
- Fe
- Probable [Fe-S]-dependent transcriptional repressor FeoC
- Divalent metal cation transporter MntH
- Biopolymer transport protein ExbD
- Biopolymer transport protein ExbB
- Zinc transporter ZupT
- Protein TonB
Sequence:
MKKLTIGLIGNPNSGKTTLFNQLTGSRQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHYILSGDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIEIDALSARLGCPVIPLVSTRGRGIEALKLAIDRYKANENVELVHYAQPLLNEADSLAKVMPSDIPLKQRRWLGLQMLEGDIYSRAYAGEASQHLDAALARLRNEMDDPALHIADARYQCIAAICDVVSNTLTAEPSRFTTAVDKIVLNRFLGLPIFLFVMYLMFLLAINIGGALQPLFDVGSVALFVHGIQWIGYTLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYMLGIVMAVLTGLMLKYTIMRGEATPFVMELPVYHVPHVKSLIIQTWQRLKGFVLRAGKVIIIVSIFLSAFNSFSLSGKIVDNINDSALASVSRVITPVFKPIGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAENIQDEEFNPAEFNLGEELFSAIDETWQSLKDTFSLSVLMNPIEASKGDGEMGTGAMGVMDQKFGSAAAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQVASYSQHPTYSLVCILAVILFNIVVIGLLRRARSRVDIELLATRKSVSSCCAASTTGDCH
Protein: Histidine--tRNA ligase (EC 6.1.1.21) (E9QI36)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the aminoacylation of histidyl-tRNA.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:28934368}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000269|PubMed:28934368}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase
- Lysine--tRNA ligase
- Methionine--tRNA ligase, mitochondrial
- Methionyl-tRNA synthetase
- Aspartate--tRNA ligase, mitochondrial
- Glycyl-tRNA synthetase.
- Tryptophanyl tRNA synthetase 2
- Tyrosine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
Sequence:
MADKAQLQEAIKTQGEVVRKLKSEKASKEQIDEEVARLLQLKAQLGGDEGKHVFVLKTAKGTRDYNPKQMAIREKVFNIIINCFKRHGAETIDSPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKITNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAGQYDAMIPDAECLKLVYEILSELDLGDFRIKVNDRRILDGMFAICGVPDEKFRTICSTVDKLDKLAWEEVKKEMVNEKGLSEEVADRIRDYVSMQGGKDLAERLLQDPKLSQSKQACAGITDMKLLFSYLELFQITDKVVFDLSLARGLDYYTGVIYEAILTQANPAPASTPAEQNGAEDAGVSVGSVAGGGRYDGLVGMFDPKGRKVPCVGVSIGIERVFSIMEQKAELSSEKVRTTETQVLVASAQKNLLEERLKLTAELWNAGIKAEVLYKKNPKLLSQLQHCEDTGIPLVAILGEQELKDGVVKLRNVASREEVDVPRAELVDEVKKRTS
Protein: Nucleoid-associated protein At4g30620, chloroplastic (Q9M098)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Transmembrane protein
- Heparanase-like protein 2
- Homeobox-leucine zipper protein HDG7
- Lysine-specific demethylase REF6
Sequence:
MASTATNTDFFKTLLSPFSNGNAAQRSSRQNIVWLNRKQSGNNNRSLRVNGLFGGGKKDNKEDGQSKAGILGNMQNLYETVKKAQMVVQVEAVRVQKELAVAEFDGYCQGELVKVTLSGNQQPIRTDITDAAMELGSEKLSLLVTEAYKDAHSKSVLAMKERMSDLAQSLGMPPGLDGLK
Protein: Another transcription unit protein (Q94546)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RNA polymerase II-associated factor 1 homolog
- Uncharacterized protein
- Hyrax
- FACT complex subunit spt16
- Ctr9, isoform A
- FACT complex subunit Ssrp1
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- Transcription elongation factor SPT6
- Uncharacterized protein
Sequence:
MGSQNSDDDSGSSGSSRSGSRSVTPQGGSAPGSQRSRRSGSGSDRSRSGSRSSRSRSGSGSPRSARSGSAESRHSQLSGSARSKRSRSAHSRRSGSARSRKSGTPESPQSHRSGSLQSRKSGSPQSRRSGSPQSRKSGSTHSRRSGSAHSRRSGSARSRKSGSAQSDRSESRSRSHSGSLKGNEESRSNSPNLQIDVERANSKSGSRSRSRSRSGSRTSRSRSKTGTPSPNRSRSGSASGSGSDVGVPKKKARKASGSDQEKKKSGSDSDIEESPTKAKKSRLIDTDSDSNQDVGKKAPAAADIFGDADDISDDEDEAGPAARKSPVRSKSRSQSKSHSHSRSMSHSRSRSRSRSRDKVESQVESAPKEDEPEPLPETRIDVEIPRISADLGKEQHFIKLPNFLSVVTHPFDPETYEDEIDEEETMDEEGRQRIKLKVSNTIRWREYMNNKGDMVRESNARFVRWSDGSMSLHLGNEIFDAYRQPLLGDHNHLFVRQGTGLQGQSVFRTKLTFRPHSTESFTHKKMTMSLADRSSKTSGIKILTQVGKDPTTDRPTQLREEEAKLRQAMRNQHKSLPKKKKPGAGEPLIGGGTSSYQHDEGSDDENAISLSAIKNRYKKGSGAGQAEVKASTIYSSDEDEGSDFEARRSKKVDKAKASKALRDSDSESDAGSAKSGHSNKSGGEGGSASGSENEGSQKSGGGSSKSASGSGSGSGSGSGSGSDND