wanglab/gogpt-training-data huggingface dataset:
Protein: Acyl-coenzyme A oxidase-like protein (Acyl-CoA oxidase-like protein) (EC 1.3.3.-) (Q9NUZ1)
Organism: Homo sapiens (Human)
Interaction partners:
- Enoyl-CoA delta isomerase 2
- Hydroxysteroid dehydrogenase-like protein 2
- Peroxisomal acyl-coenzyme A oxidase 2
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit beta
Sequence:
MRALTVQRVKFAMDLPLLKRAGQDLAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDENGSLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEVKIIEHQTQTLRLMPHLATALALTFVSRYAGALLDEDVFQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYTKQYEEKPLFGLLQNWAESVGDKLRTSFLAFNMDTVDDLAFLLKAVKFRERVLQRGLVARIYYKVKTKKEDFFHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQERC
Protein: RQC trigger complex subunit RQT4 homolog (O13855)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probably functions as part of the RQC trigger (RQT) complex that activates the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- RQC trigger complex helicase rqt2
- Mediator of RNA polymerase II transcription subunit 17
- DNA-directed RNA polymerase II subunit rpb1
- Mediator of RNA polymerase II transcription subunit 10
- Uncharacterized protein C15D4.13c
- tRNA endonuclease vms1
- Oxalate--CoA ligase
- Prohibitin-2
- Uncharacterized ABC transporter ATP-binding protein C29A3.09c
- Set1 complex component shg1
Sequence:
MEKWTKENVLKILPVDDESAAMITSTALAVDSSEAAKDYWISLLGDSAETIEFISDFNQKRFHSTHSGNSPSIMKNKKNVTPNNNIRQKNTATSSHPSFYIANNKQKGYDEEMYKVNPASRNKSQSNNISSHEKSSKTTKNVSPGVMTSDLIPEKKSVKHNNSSSNRIEGLADIEKAIRQIEISQNINKAERRVCNCQGRKHPLNEAAPNCLNCGKIICIVEGIGPCTFCDNPVISKAQQLELIQELKHEGSRLKQAANQKRKSKTVSSKNNFQRLQNSSLHSIFLDPKQLEQKAQEAEERKNVLLNFDRTSAQRTRIIDEAADFDPTSLASDTWASPAEKALNLVRMQKAMAKKEKKKKKVLSISLSGKKVVVDQKEASSESSDEDQDELDNLTKVEGQSHSHNPKAPVIRNLPRPIYHQDLHSSHVAVPESILNKINQKWSKVQDDDGMPSML
Protein: Calcitonin gene-related peptide type 1 receptor (CGRP type 1 receptor) (Calcitonin receptor-like receptor) (Q8WN93)
Organism: Sus scrofa (Pig)
Function: Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP2 or RAMP3. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11714898}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16602}.
Interaction partners:
- Receptor activity-modifying protein 1
- Pro-adrenomedullin
- Receptor activity-modifying protein 3
- Receptor activity-modifying protein 2
- Calcitonin receptor-stimulating peptide 1
- Calcitonin receptor-stimulating peptide 2
- Calcitonin receptor-stimulating peptide 3
- Islet amyloid polypeptide
- GNAS complex locus
- Calcitonin
Sequence:
MEKKYILYFLFLLPFFMILVIAETEEENPDDLIQLTVTRNKIMTAQYECYQKIMQDPIQQTEGIYCNRTWDGWLCWNDVAAGTESMQHCPDYFQDFDPSEKVTKICDQDGNWFRHPESNRTWTNYTQCNINTHEKVQTALNLFYLTIIGHGLSIASLLISLGIFFYFKSLSCQRITLHKNLFFSFVCNSIVTIIHLTAVANNQALVATNPVSCKVFQFIHLYLMGCNYFWMLCEGIYLHTLIVVAVFAEKQHLMWYYFLGWGFPLIPACIHAVARRLYYNDNCWISSDTHLLYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESNLYMKAVRATLILVPLLGIEFVLIPWRPEGKIAEEVYDYIMHILVHYQGLLVSTIYCFFNGEVQAILRRNWNQYKIQFGNSFSHSDALRSASYTVSTISDGAGYSHDYPSEHLNGKSIHDMENIVIKPEKLYD
Protein: Cytoplasmic tRNA 2-thiolation protein 1 (EC 2.7.7.-) (Cytoplasmic tRNA adenylyltransferase 1) (Q38AA3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053}.
Interaction partners:
- Cytoplasmic tRNA 2-thiolation protein 2
- tRNA
- Adenylyltransferase and sulfurtransferase MOCS3 homolog
- Putative rRNA methyltransferase
- rRNA methyltransferase, putative
- tRNA
- ATP-dependent DEAD/H RNA helicase, putative
Sequence:
MPPQRQCSHCEKEKAVLKRPRNGKLLCQRCFFNLFEAEVHETIMKEKLFKPGDIVACGASGGKDSTVLIHLMKLLNEQHEYGIQLLLLSIDEGIAGYRDDSLKTVHRNAEVYNLPLRVLSYKELYGWTMDEVVKVTGLRSSCTYCGVFRRQALDRGAAMLGATKVVTGHNADDLAETILMNILRGDLPRLSRCTSAITSGESLLPRVKPLKYAYEKEIVLYAHFKKLDYFTTECTYSKEAFRSEARTLLKNIEILQPRCILDTIRTGEQLRVKEQECATENPPSACTRCGYVTSQSLCRACVLLQGLNMNGPAVCVREQPQPQQQQQQQNVEVEGQ
Protein: Factor in the germline beta (Q810E9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTEVEYTQLQHILYSHMEAADGELEARLGSALLAGPGAGSGAAGSLAPAPPVYPVLCPPLAADAPCLGHVDFQELRMMLLGEAGAAEKTPGGADGTRTRADGVAKEGAGGAGPDGAPEARAKPTVRVRLEDRFNSMPAEPPAPRGAEPAESGVALNNLVTLIRHPSELMNVPLHQQQNKCTTLVKNKTAAATTALQFTYPLFTSACSTGGNASLAQTQSSSNSCSILEAAKHQDIGLPRTFSFCYQQEIESTKQTGGSRNKALPEQVWIKVGEEALCKQAINKRNRSRIRQLDTSVERRALGEIQNVGEGSSTSQGTWQSSESSQSNLGEQTQSGPQGGRSQRRERHNRMERDRRRRIRICCDELNLLVPFCNAETDKATTLQWTTAFLKYIQERHGDSLKKEFESVFCGKTGRRLKLTRPESLVTWPAQGSLQSSPAMEIK
Protein: Protein MONOCULM 1 (Q84MM9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Putative transcription regulator that controls rice tillering by initiating axillary buds and promoting their outgrowth. Rice tiller is a specialized grain-bearing branch that is formed on the unelongated basal internode and grows independently of the mother stem (culm) by means of its own adventitious roots.
Subcellular location: Nucleus {ECO:0000269|PubMed:12687001}.
Interaction partners:
Sequence:
MLRSLHSSSSSDTDNNSGGCKNNGGGGGEAAAAVEGGGDQRAVAAAAPSTRDLLLACADLLQRGDLPAARRAAEIVLAAAASPRGDAADRLAYHFARALALRVDAKAGHGHVVVGGGAARPASSGAYLAFNQIAPFLRFAHLTANQAILEAVDGARRVHILDLDAVHGVQWPPLLQAIAERADPALGPPEVRVTGAGADRDTLLRTGNRLRAFARSIHLPFHFTPLLLSCATTAPHHVAGTSTGAAAAASTAAAATGLEFHPDETLAVNCVMFLHNLAGHDELAAFLKWVKAMSPAVVTIAEREAGGGGGGGDHIDDLPRRVGVAMDHYSAVFEALEATVPPGSRERLAVEQEVLGREIEAAVGPSGGRWWRGIERWGGAARAAGFAARPLSAFAVSQARLLLRLHYPSEGYLVQEARGACFLGWQTRPLLSVSAWQPSSS
Protein: MKIAA0920 protein (Q69ZV5)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}.
Interaction partners:
Sequence:
KPPQLSEDANQLRSKQDNCGDSRLEPAASSLSPDHKNMEIGVSVAECKSVPGVTSTPHSKDHSSPFYSPSHNGLLADHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSVTEAEPTEKASGRQVPPHIELSRSPSDRMAEGERANGHSTDQPQDLLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEEDEREKEQFCVRKVRPSEEMIELEKERRELIRSQAVKKNPGIAAKWWNPPQEKTIEEQLDEEHLESHRKYKERKEKRAQQEQLQLQQQQQQQLQQQQLQQQQLQQQQLQQQLQQQQLSTSQPCTAPAAHKHLDGIEHTKEDVVTEQIDFSAARKQFQLMENSRQTLAKGQSTPRLFSIKPYYKPLGSIHSDKPPTILRPATVGGTLEDGGTQAAKEQKAPCVSESQSAGAGPANAATQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDEDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETPSALQENSLADFSLPQTPQTDNPSEGREGVSKSFSDHGFYSPSSTLGDSPSVDDPLEYQAGLLVQNAIQQAIAEQVDKAEAHTSKEGSEQQEPEATVEEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNLPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGGYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVRQSTPSPRAKNAPSLPSRTTCYKTAPGE
Protein: NAD(P)H-dependent FMN reductase C4B3.06c (FMN reductase C4B3.06c) (EC 1.5.1.39) (Azoreductase C4B3.06c) (FMN reductase [NAD(P)H]) (Q9USJ6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has several reductase activities that are NAD(P)H-dependent and involve FMN as a cofactor. May be involved in ferric iron assimilation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Riboflavin kinase
Sequence:
MTLPEKLLKITPKILVIMGSVRSKRLCPTIATWVGEMGKRETNFDYEKVDLTDWPLSMSDEPGLPIMGIDVYTQEHTKAWGSKIAGADGFVFVTPQYNGGYPAILKNALDHLYHEWNGKPLLIVSYGGHGGGDCASQLKHVAGFLKMRVAPTMPALTLPRDKIVQGVVDPAVEFTKHLGELKKAFGEFSQLFESNPERKP
Protein: Histidine decarboxylase (EC 4.1.1.22) (A0A068Q816)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MEPEEYRRRGKEMVDYICQYLSNVRERRVTPDVQPGYMRAQLPDSAPMDPDSWDNIFGDIEKIIMPGVVHWQSPHMHAYFPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNVMDWLAKMLGLPDKFLHHHPDSVGGGVLQSTVSESTLVALLAARKNKILEMKLSEPDADESSLNSRLIAYASDQAHSSVEKAGLISLVKMKFLPVDENFSLRGETLKKAIAEDRKKGLVPIFVCATLGTTGVCAFDSLSELGPICGAEGLWLHIDAAYAGTAFLCPEFRLFLDGIEYADSFAFNPSKWMMVHFDCTGFWVKDKYKLHQTFSVNPVYLRHPNSGAAVDFMHWQIPLSRRFRSLKLWFVIRSFGVKKLQAHVRHGTETAKFFESLVRSDPLFEIPAKRHLGLVVFRLKGPNWLTEKLLKELSSSGRLFLIPATIHDKFIIRFTVTSQFTTREDILQDWNIIQRTAAQIISQHNELHCVSSGDEAKIPNMISEPSSSVISHASQLYLEGKYKIPSRKIVGQPKKLAASPSTCVVSQQVQGQGDLDDCFPEDVQDVTKHKLTSFLFSYLSVQGKKKTARSLSCNSVPMTDLLEQCNPKTTDSDQKEPHANGRILSRLPEEVMMLKKSAFKKLIKFYSVPSFSECSIQCGLQLPCCPLQAIV
Protein: Glutathione hydrolase 3 (EC 3.4.19.13) (Gamma-glutamyltransferase 3) (Gamma-glutamyltranspeptidase 3) (EC 2.3.2.2) (Gamma-glutamyltranspeptidase 4) (Q9M0G0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in protecting plants from some xenobiotic chemicals by degrading vacuolar glutathione conjugates into cysteine conjugates.
Subcellular location: Vacuole membrane {ECO:0000305|PubMed:17316176}; Single-pass membrane protein {ECO:0000305|PubMed:17316176}.
Interaction partners:
- 5-oxoprolinase 1
- Glutathione synthetase, chloroplastic
- Puromycin-sensitive aminopeptidase
- Leucine aminopeptidase 1
- Gamma-glutamylcyclotransferase 2-2
- Glutamate--cysteine ligase, chloroplastic
- 1-Cys peroxiredoxin PER1
- Leucine aminopeptidase 2, chloroplastic
- Gamma-glutamylcyclotransferase 2-3
- Leucine aminopeptidase 3, chloroplastic
Sequence:
MRDAIIADPLLAIDHETVAEKKKQSKNLKISLLLLLILLATSGYYSFSDNITTVFLSRQAIDDDHSLSLGTISDVVESENGVVAADDARCSEIGASVLRSGGHAVDAAVAITLCVGVVNPMSSGIGGGSFLIVSSQKDSKAEAFDMRETAPLAASKDMYKNDASAKSLGALSMGVPGEIAGLYEAWKRYGRLPWKPLFEPAIKLARDGFVVYPYLGKAISTKVAMILKDPGMRSVFSRNGQVLKTGETCYNPELAQSLETISEQGPGAFYNGTVGEKLVKDVKKAGGIITMDDLRSYKVRVTDAMSVDVMGYTVHGMPPPSGGTVGFSMVMNILDSYSNLYTASGRELGLHRLIEAMKHMFAARMDLGDPEFVNVTNSMNQMLSKAHAEEIQKRIFDNTTFPPEYYMNRWSQLRDQGTSHFCVVDADRNSVSMTSTVNYRFGAGVLSPSTGIVLNNEMDDFSTPTEITPDMLPPAPTNFIEPNKRPLSSMTPLVITKDGEFVAALGGAGGMHIIPAVLQVFLNCFVLNMKPKEAVESARIYHRLIPNVVSYENFTTINGDHIGVSEDTKMFLAERGHELKELSGGAIVQLIVQSFKEEKEEEMIIEIGRKIGKKSKPLKGLLTAVSDPRKDGKPAAV
Protein: Retrotransposon hot spot (RHS) protein, putative (Q57UU8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRPRDEHVAPPPAQPPQMPQRYKRFSDWKMNSTVRDFLLERYATLPKMNLHDFLNQCFSNTYNTVNVSMETFVKNPEDYIKDAEILEDIQGLYEFREYKRIVEKLPETEMWINYLKEEKIFTISDWVNGATPEVKNSISPVARGRLNAVQHAVTESEVWFLPRVSVKSCRDVYDSFYNAKWSYVMSGYDAEPLGMKVFDGRPQRIWTEAELNITPKTADVDARVKEGSNGLEIFVLTSEKGWPYNRFVLGYTERCKTICKHVYIRREIMRVWYIIQRGLKAWWMEATAEGPPIHIIIGTSGIGKTCGLGSFLFYSLLHFNEGMLDVVAYFLEDAAFLIYNREGEGRGTVDEYKRWESAVSAINKMKSESKGHIVMDTRYAMEELYTQLPSDVWSVTFLTFPKSAHFDEWSANKGGHHIIINCDDVRDMKAFMAWKKLSIHTGEKVSNRRRYELKREIEDEWKIVEGRINLIGPLPRYIFGLGCYEWHLKSVYDALRAMKKSDKYCYNDIIEHTADWRNDEVMNKLVKIVRVKGNVGGVESYKCQALSLMIRNMMMN
Protein: 74aa long hypothetical transcriptional regulator (O74091)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Interaction partners:
- Signal recognition particle 54 kDa protein
- Uncharacterized protein
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MFILLVVRPGLENEVYEKLKDRPEVKEIYRLYGDYDIIIRLSVEGIKALDEFHDKVLRKLRGIEISETLIASSY
Protein: Carboxy-terminal processing protease CtpB (C-terminal processing protease) (EC 3.4.21.102) (O35002)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation.
Subcellular location: Forespore intermembrane space {ECO:0000269|PubMed:17557826}. Note=Is expressed in both the mother cell and forespore compartments but that synthesis in the forespore is both necessary and sufficient for the proper timing of pro-sigma-K processing.
Interaction partners:
- Stage IV sporulation protein FA
- SpoIVB peptidase
- Sigma-K factor-processing regulatory protein BofA
- Stage IV sporulation protein FB
- Regulator of sigma-W protease RasP
Sequence:
MNQKIMAVIAAGSMLFGGAGVYAGINLLEMDKPQTAAVPATAQADSERDKAMDKIEKAYELISNEYVEKVDREKLLEGAIQGMLSTLNDPYSVYMDKQTAKQFSDSLDSSFEGIGAEVGMEDGKIIIVSPFKKSPAEKAGLKPNDEIISINGESMAGKDLNHAVLKIRGKKGSSVSMKIQRPGTKKQLSFRIKRAEIPLETVFASEKKVQGHSVGYIAISTFSEHTAEDFAKALRELEKKEIEGLVIDVRGNPGGYLQSVEEILKHFVTKDQPYIQIAERNGDKKRYFSTLTHKKAYPVNVITDKGSASASEILAGALKEAGHYDVVGDTSFGKGTVQQAVPMGDGSNIKLTLYKWLTPNGNWIHKKGIEPTIAIKQPDYFSAGPLQLKEPLKVDMNNEDVKHAQVLLKGLSFDPGREDGYFSKDMKKAVMAFQDQNKLNKTGVIDTRTAETLNQQIEKKKSDEKNDLQLQTALKSLFVN
Protein: Inactive peptidyl-prolyl cis-trans isomerase FKBP6 (Inactive PPIase FKBP6) (36 kDa FK506-binding protein) (FK506-binding protein 6) (Immunophilin FKBP36) (D3ZQF4)
Organism: Rattus norvegicus (Rat)
Function: Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be required together with HSP90 in removal of 16 nucleotide ping-pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Does not localize to pi-bodies. Localizes to meiotic chromosome cores and regions of homologous chromosome synapsis (By similarity). {ECO:0000250}.
Interaction partners:
- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1
- Tudor and KH domain-containing protein
- RNA helicase Mov10l1
- ATP-dependent RNA helicase TDRD9
- piRNA biogenesis protein EXD1
- Mitochondrial cardiolipin hydrolase
- Tudor domain-containing protein 5
- Putative ATP-dependent RNA helicase TDRD12
Sequence:
MSVFSRLRNGIPPSRDDCQSPYERLSQRMLDISGDRGVLKDIIREGAGDPVTPDASVLVKYSGYLEHMDKPFDSNCFRKTPRLMKLGEDITLWGMELGLLSMRRGELARFLFKPTYAYGTLGCPPLIPPNATVLFEIELIDFLDSAESDKFCALSAEQQEQFPLQKVLKVAATEREFGNYLFRQNRFCDAKVRYKRALLLLHRRLAICEEQHLVEPAELLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYEQARDFLVRAQKEQPCNHDINNELKKLSSHYRDYVDREREMCHRMFAPCGSGSSVGGN
Protein: Copper transport protein ctr5 (Copper transporter 5) (Q9P7F9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for high affinity copper (probably reduced Cu I) transport into the cell.
Subcellular location: Membrane {ECO:0000269|PubMed:11274192}; Multi-pass membrane protein {ECO:0000269|PubMed:11274192}.
Interaction partners:
- Copper transport protein ctr6
- Metal-binding regulatory protein cuf1
- Copper transport protein ctr4
- Copper-transporting ATPase ccc2
- Iron transport multicopper oxidase fio1
- Metal homeostasis factor atx1
- Superoxide dismutase 1 copper chaperone
- Uncharacterized protein C140.04
- Copper amine oxidase 1
- Uncharacterized transporter mfc1
Sequence:
MSLSKMSMSGMSGMGMGSSSNSSAATCRMSMLWNWYIHDSCFLAKSWHINTGNKFAGSIIGIFFFAVAIEGLSLVQRMFDRWIVAHSNGKTLSGPLRIFFPSSTVHVTVWQQLIRAAMYSSFYLSATILMLIVMSFNGYAILFGFVGAWIGFFLFASDTYGTPSTGTGCCESR
Protein: Meiotically up-regulated gene 165 protein (O14196)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C16E8.12c
- Uncharacterized protein C24B10.19c
- Histone deacetylase clr6
- Meiotically up-regulated gene 123 protein
- Meiotically up-regulated gene 168 protein
- Transcriptional regulatory protein sds3
- Meiotically up-regulated gene 166 protein
- Phospholipid-transporting ATPase neo1
- Uncharacterized membrane protein C16E9.09c
- Uncharacterized protein C1739.04c
Sequence:
MLEKGEHIEYPNTPPLHSPPESHTFSSQTDDSYFHKPSSTGLFATLVADTNSSVPSASRSPESIASSQSNDSAAIPSYRRKRRKVRKPEIVKPTLRKRGRKPKNISTLEHDKSKPVISSLIDEDANLSQIKARKSVLESRFSRLEEAFRDFYIKNLEKTEDLIRTDSHFVLNKELLSFRNDYEHRRKHYEKYSQCLNKQLDHFFSYKVTTVHKSYQRFATLLRRHLLDKTAKRYHDLCEKRPYKYITTDLLSPSLTCFASDILQTVPEYTSSQSSPVLLPATPSIVTNKQMMDDLTLCNV
Protein: GTPase NRas (EC 3.6.5.2) (Transforming protein N-Ras) (P01111)
Organism: Homo sapiens (Human)
Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}; Lipid-anchor {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}; Cytoplasmic side {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}. Golgi apparatus membrane {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}; Lipid-anchor {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}. Note=Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}.
Interaction partners:
- Serine/threonine-protein kinase B-raf
- RAF proto-oncogene serine/threonine-protein kinase
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Serine/threonine-protein kinase A-Raf
- Neurofibromin
- Son of sevenless homolog 1
- Epidermal growth factor receptor
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Ral guanine nucleotide dissociation stimulator
- Leucine-rich repeat protein SHOC-2
Sequence:
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM
Protein: Drop dead (EC 2.3.1.-) (RE74651p) (Q8IR42)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Neuropathy target esterase sws
Sequence:
MSRMSHMLALLLVLIASSQALEGVVQPTCNLKDNCNLGDNLLAGTNSASDAGDVSADKLESKIASIFEDKVNYSLKLFADDATTTILEYQTANLSQLHAVTPGNYTIHQMEQAEDDDDQVEEDERAYLYNIGKRFLAITQPFDAARNPDASTLCRRQMHQFLNALDNFDLWALKMHDSSGKLNSGILNGNINQPGDFDQCLGIQQRMNQDQDAGQDQDGDSIIRGQYCLAYAQPVLPHNSKRLKSFFKLIQSHGPFKSEFNDPGHRVPRYSLINWGLCVPSGCSARDVEYSVAEYLGNQTASTGITFNVRVEPQMCQVRDQRPWDRNTTWAVRFFLLVLSVAVLSTIYDRSTKSQPKQNPWFTAFSLDKNLRWLFSTSSAPGDIEAVHGIRFLNAIMLIFSHKSMAMFFNPYNNRTAMSESLGQPWTVIGRAASLYTDPFLLFSGMLTSYSLFGRLMKQQPIRLKNEYISRLMRIVPPLAALILFCTYVLPLWGSGPQWNLVVGHHADICKKNWWRNLLFIHNYFGFSEMCLTHTHHLGIDTELFAVAPLLILALWRWPRRGLFALLLLCTVGTAARYYTTIVNQLSNYIYFGTNIQRLFRTADYMYSFPPHRSTVYIMGILLGYVLRKYQNARLSSLQLRLGWLVATVCVLASLLGPAPMGDINYVYNSTHAAIYAAFAPIAWCLFFSWIVFVSHNGYTNKLTKLFAWRGFQVSTKLSYAIYLTQFPVFFFNVGRRRHIHHYYNFVSIILDTNEFISIFLASVALTVLFDAPFQNLKKLLIKRPTAAKVVKDSKAKAAESQDATTTTLASQPSSTALLQSHHPHSD
Protein: Origin recognition complex subunit 3 (Origin recognition complex subunit Latheo) (Q9UBD5)
Organism: Homo sapiens (Human)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3.
Subcellular location: Nucleus {ECO:0000269|PubMed:31160578}. Chromosome {ECO:0000269|PubMed:31160578}.
Interaction partners:
- Origin recognition complex subunit 1
- Origin recognition complex subunit 5
- Origin recognition complex subunit 4
- Origin recognition complex subunit 6
- Cell division control protein 6 homolog
- Origin recognition complex subunit 2
- DNA replication factor Cdt1
- Leucine-rich repeat and WD repeat-containing protein 1
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM2
Sequence:
MATSSMSKGCFVFKPNSKKRKISLPIEDYFNKGKNEPEDSKLRFETYQLIWQQMKSENERLQEELNKNLFDNLIEFLQKSHSGFQKNSRDLGGQIKLREIPTAALVLGVNVTDHDLTFGSLTEALQNNVTPYVVSLQAKDCPDMKHFLQKLISQLMDCCVDIKSKEEESVHVTQRKTHYSMDSLSSWYMTVTQKTDPKMLSKKRTTSSQWQSPPVVVILKDMESFATKVLQDFIIISSQHLHEFPLILIFGIATSPIIIHRLLPHAVSSLLCIELFQSLSCKEHLTTVLDKLLLTTQFPFKINEKVLQVLTNIFLYHDFSVQNFIKGLQLSLLEHFYSQPLSVLCCNLPEAKRRINFLSNNQCENIRRLPSFRRYVEKQASEKQVALLTNERYLKEETQLLLENLHVYHMNYFLVLRCLHKFTSSLPKYPLGRQIRELYCTCLEKNIWDSEEYASVLQLLRMLAKDELMTILEKCFKVFKSYCENHLGSTAKRIEEFLAQFQSLDETKEEEDASGSQPKGLQKTDLYHLQKSLLEMKELRRSKKQTKFEVLRENVVNFIDCLVREYLLPPETQPLHEVVYFSAAHALREHLNAAPRIALHTALNNPYYYLKNEALKSEEGCIPNIAPDICIAYKLHLECSRLINLVDWSEAFATVVTAAEKMDANSATSEEMNEIIHARFIRAVSELELLGFIKPTKQKTDHVARLTWGGC
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (O18645)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta-1
- LD22662p
- Raptor, isoform B
- Serine/threonine-protein kinase STK11
- Gigas, isoform A
- Protein Mo25
- Forkhead box protein O
- Serine/threonine-protein kinase mTor
- LD23779p
- calcium/calmodulin-dependent protein kinase
Sequence:
MPQMRAAAAEAVAAGSANGQPLVKIGHYLLGATLGTGTFGKVKIGEHQITRVKVAVKILNRQKIKSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMIMEYVSGGELFDYIVKHGKLQEHQARRFFQQIISGVDYCHRHMIVHRDLKPENLLLDHNMHVKIADFGLSNMMLDGEFLRTSCGSPNYAAPEVISGKLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFRKIKSGIFPIPEYLNKQVVNLVCQMLQVDPLKRANIEEIKKHEWFQKDLPAYLFPSSIEQDSNVIDTYAVAEVCTKFGVKETEVHNSLLSGDPHDQLAIAYHLIIDNKRFADDAANQINEINNFFVAGSPPPPPPPPVPQSSMDHQAPLATVTVGGGTSASSGTATPVPPVAGGTPSSTIPIRPHPERIAPMRDRQLAMSVQTSGGGAFPEKTARGGTPIKRAKWHLGIRSQSKPNDIMLEVYRAMKALSYEWKIINPYHVRVRRQNVKTGKFSKMSLQLYQVDAKSYLLDFKSLTNDEVEQGDDVIMESLTPPPLSVSGVMPLQPTGHHTMEFFEMCAALIIQLAR
Protein: Cytochrome c oxidase subunit 3 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide III) (P00414)
Organism: Homo sapiens (Human)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Multi-pass membrane protein {ECO:0000269|PubMed:30030519}.
Interaction partners:
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- ATP synthase F
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase chain 2
Sequence:
MTHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSMTLLMLGLLTNTLTMYQWWRDVTRESTYQGHHTPPVQKGLRYGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGGHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASEYFESPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICFIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS
Protein: Transcriptional regulator PltR (B3G2A3)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MKTLGFSDDFDLYISVALTGSFSETGRVFEMPASSVMRRINNLEEKLETRLINRSTKKLVLTETGALFLKHARKISENINQARNEIKEHTSSAVGTLRVSAPVAFGRRHIAPLVSTLLKKNPGLKLDFSLNDRIADPVGEKLDLCIRLGILPDSSLICSKLAGLRRVLCASPEYLLKHGLPRTPEELERHTCLQHNGCSNASLSWQFSSADITRRIRISPVSRLSVNSAELLVEGALQGLGIIHAPTWLVHEEVASGRLVTFLDRHALPEQAQGGIYALRPQGSVVPAKISLFLSELKSAIGETPYWDLPFQQTPAQLAGSF