wanglab/gogpt-training-data huggingface dataset:
Protein: Required for respiratory growth protein 8, mitochondrial (Q06109)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for respiratory activity and maintenance and expression of the mitochondrial genome.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Genetic interactor of prohibitin 5, mitochondrial
- Protein PET130
- Required for respiratory growth protein 1
- Required for respiratory growth protein 9
- Required for respiratory growth protein 7
- Increased recombination centers protein 19
- Ribonuclease P protein component, mitochondrial
- Uncharacterized protein YDR114C
- Uncharacterized protein YNL184C
Sequence:
MGLPKSAYKKLLIDCPTRVINKNCAQRVKDVSPLITNFEKWSDKRKKLYFKDEEEMVGQFHLENFNLKNNLYGRLLASPMRAEKISKLKSCRELLIPLKVVPSTGKDQHADKDKLKLVPTLDYSKSYKSSYVLNSASIVQDNLAAATSWFPISVLQTSTPKSLEVDSSTFITEYNANLHAFIKARLSVIPNVGPSSINRVLLICDKRKTPPIEIQVVSHGKGLPITQSVFNLGYLHEPTLEAIVSKDAVTNGIYLDADNDKDLIKHLYSTLLFHSVN
Protein: Apidaecin P (C0HKX7)
Organism: Sphecius speciosus (Eastern cicada killer)
Function: Antimicrobial peptide active against many Gram-negative enterobacterial and plant-associated bacterial species. Not active against other bacterial species like H.pylori, P.mirabilis, B.pertussis or N.gonorrhoeae.
Subcellular location: Secreted {ECO:0000269|PubMed:7929322}.
Interaction partners:
Sequence:
NRPTYVPPPPRPPHPRL
Protein: AP-1 complex subunit mu-1-I (Clathrin assembly protein complex 1 mu-1-I medium chain) (Clathrin coat assembly protein AP54) (Clathrin coat-associated protein AP54) (Golgi adaptor AP-1 54 kDa protein) (HA1 54 kDa subunit) (Mu(1)-adaptin) (Mu1-I-adaptin) (Q00776)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin. AP57 is probably a subunit of the Golgi membrane adaptor.
Subcellular location: Cytoplasmic vesicle. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- AP-1 complex subunit sigma-1
- AP-1 complex subunit gamma-1
- AP-1 complex subunit beta-1
- AP-2 complex subunit beta
- Clathrin light chain
- Clathrin heavy chain
- AP-2 complex subunit sigma
- AP-2 complex subunit alpha
- AP-3 complex subunit delta
- AP-3 complex subunit mu
Sequence:
MASAVYFCDHNGKPLLSRRYRDDIPLSAIDKFPILLSDLEEQSNLIPPCLNHNGLEYLFIQHNDLYVVAIVTSLSANAAAIFTFLHKLVEVLSDYLKTVEEESIRDNFVIIYELLDEVMDYGIPQITETKMLKQYITQKSFKLVKSAKKKRNATRPPVALTNSVSWRPEGITHKKNEAFLDIVESINMLMTQKGQVLRSEIIGDVKVNSKLSGMPDLKLGINDKGIFSKYLDDDTNIPSASATTSDNNTETDKKPSITSSSATNKKKVNIELEDLKFHQCVRLSKFENEKIITFIPPDGKFDLMNYRLSTTIKPLIWCDVNVQVHSNSRIEIHCKAKAQIKRKSTATNVEILIPVPDDADTPTFKYSHGSLKYVPEKSAILWKIRSFPGGKEYSMSAELGLPSISNNEDGNRTMPKSNAEILKGPVQIKFQIPYFTTSGIQVRYLKINEPKLQYKSYPWVRYITQSGDDYTIRLT
Protein: Serine protease 43 (Q76HL1)
Organism: Mus musculus (Mouse)
Function: Plays a role in spermatogenesis. Involved in germ cell survival during meiosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23536369}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23536369}.
Interaction partners:
Sequence:
MGGFCGADRGGFLALLVWLQLLQPLFSGTYKPREDSGVMHRPQRPRRPRSDPEAPAQQSRLKSLSISHPSGVPVSVDRTEIPGSGSPSGTTTKITLENRRSSLGGPFFTDTCGHRITEVDPGSLSAGRKWPWQVSLQSQNEHVCGGSLISHRWVLTAAHCIYEQEEYMVMLGDDMLHSESESVTLVPVQDIIFPSNFDIQTMRNDIALALLYFPVNYSSLIQPVCLPEEPFRVKNGTVCWVTGWGQQNEIDAGFASILLQEVQQRILLQKHCNTLFQRQLGTSKNLVIKGMICGLQDSGQSLCWGDSGNPLVCESDNTWTQVGIMSWGINCNGVPVLSVYTDIAEYNEWVSYVLSQASRMDPMGVLVLYLSLVFPLALLVAL
Protein: Cysteine and histidine-rich domain-containing protein 1 (CHORD domain-containing protein 1) (CHORD-containing protein 1) (Chp-1) (Protein morgana) (Q9D1P4)
Organism: Mus musculus (Mouse)
Function: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (By similarity). Involved in stress response. Prevents tumorigenesis (By similarity).
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Activator of 90 kDa heat shock protein ATPase homolog 1
- Heat shock protein 105 kDa
- Serine/threonine-protein phosphatase 5
- Prefoldin subunit 4
- Protein SGT1 homolog
- Activator of 90 kDa heat shock protein ATPase homolog 2
- SHC-transforming protein 4
- Calcyclin-binding protein
Sequence:
MALLCYNRGCGQRFDPEANSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEVKTTEKKELSELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGSEEDKKEEDSDEIKIGTSCKNGGCSKTYQGLQSLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTRGKHVWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSQVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLELPTTKKQEKQKDIAD
Protein: Dysfusion (Q6RZA5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYADNKRGLDKVTAATPPTHALQQQQQQQHPHQQQQHLQHVLQLQQQQQQHLQQQQHHLQHQMHTHHNFQQHETSPTVSQQQHMQQQQPQTTQQQHATQQQQQQQQQTAGMFTRFDANKSTKGASKMRRDLINAEIANLRDLLPLPQSTRQRLSQLQLMALVCVYVRKANYFQQVFKRHNAMHHLHHQTATPNIGFSKALSGFLMMLTQNGKLLYISDNAAEYLGHSMEDLLIHGDSVYDIIDKQDHANIQAELNRNVPPQPGGSSQASSGGAGGAGGAGDSTSSNGSAAGAGGAGGASSLEGEHRMFLCRMNVSRNARRQMRFGDQKVVLVQGHYLSFLPLCSRNEPVFLATCTPIAMPETRECVVQGATNVFTTIHSMDMKIAHIDKNGEFHLGYDKSTLQGTSWYNLIHSDNLTEAQKKHSLIIQSEQDRSCILLVRMQRSSGEYTWVHVVLQVRDSPDSTQQPVIVCTNQVLNDREASIMLANSWLYHYYTVQSKIQFGMPLDSGIRVPPGTPSSGYYSPHSSHPPATPGGATPNLGIASSFGPHHHPHHSHHPHHHHHHHHPATAYHHHPHMGTYGGVYHAKAAIELKEDQPLFCFQEPVDYSQVNSHVNPPNATSTPNPPISKSSTPPPPKKRARKLEPLYLHAERSPAAAITPEPDCYAIHTHPAAAYATSSVVSSDASVIYATIVPTRPRLPNKSLPPDPADFIEQWNPSPPWSESAQKASLDSFGSSHELSPCITTTPPTPTSATPHQSGLGTTQTIGPAFSFEWMSDPLVPVTYQQWPPTGDHHQHLSQHLSQSQNHQNPLQQQQNEQLLLGQQPHLHQQHQHLALHHGRGEHSLEGESQGVVVVPPIPISIPIPTATGHGDAGEPVEDRG
Protein: ODAD1 central coiled coil region domain-containing protein (Q582I1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQAKGDGSGSFTQRSPRIINGEGNENVADTLRRRYVQAELQLRECEDRFRRDCARQEQELELIQFENNKLKVRIEEMRMAENAVDKESSSRSPGGACVAAEHDSKLLKASSQKYRSAREAVERARNELVDLEAQLSAARVRFNELRCRHGSTSSAANASSLQTYRNRREEEEQIEASRARLRGLESHVETESDRLSTLIEEGKAMRLEIDLQITMQNQVDALRQDREGEMVEIMKETSFLIEVCNLLVEERSECEHQLAELRKAAEADAEAYEKAFYELVAVEDRNKIQAQNVREGIDKLTDELAEVVKERTAAEHDLVNKHNETGAAAQDDMDEDGDGLESQLKEFEVYLNRLGKIVGTCDLAEVESYVCDENGERFQLYNVIQSKQSAARELEEERNELMKKLNTLVDGTEKQRQEREEVKRLQSHLKDLQEETEAIEKRSEKTRAVLAESVLHLQKTYTSIGCVAPKLVLTKEGSTPSLHSVHELFAAIERRTEDYLAVWSHDRNGNQAKLMGGRTGPFTAHLLDPMPKFIKEETDTSKPAGLTKPRHEQIGIELDEGYGSGLSSPATARGE
Protein: GM19713p (Klarsicht, isoform C) (A8JNH1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
MGKVSVAVQTDISEMLSATSSTNTSRSSSEQDLLGAWEDLLSWSENASAARKLQQEMSVLKSSLQRLGDKPTPELLDTEPAIQIAVEALKLEQTQLTSYRTNMLRLNASVHSWLTKQERRLQSALEEQEQQQESEQLKQQKLVEEEKGADVQKELASTGAVAITVTDSNGNQVEALATGEASTSTPAWDVHTLMSSEQEFHKHLKNEVSDMYSSWDEADARINTQLEMLTNSLIAWRQLESGLSEFQLALGQDRGTLKGLEGALDKGQATPVELAQNVKLVAKLLSEKVHVSQEQLLAVQQHLDPNHIYHITKFTASNGSLSDSGISDGGATSDGGLSERERRLGVLRRLAKQLELALAPGSEAMRSIAARMESAEADLKHLQNTCRDLIVRTAASHQQKQQIQQNQTQQVSPKANGHIKKQAAKGKAEPQSPGRRGKGARKARQAKKAGEDQQVEEPSLSPEQQKMVLKQLKTLTSGDGGDDPSDDPSLLFNLESSEEDGEGADPAQTSKRGWAWRIARAAVPMQVALFTIFCAACLMQPNCCDNLNNLSMSFTPQLRYIRGPPPI
Protein: C2 NT-type domain-containing protein (Q581A4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- C2 NT-type domain-containing protein
Sequence:
MPEAHIVRFKVLRIDCTALTKGQQYTITYRRGETFRSTPCYVADNNYVDFSPMPEGSAVVHFKSGGLRFLPKWINIRVEEYIRGRARKAVGETRVDCAGVLGASSKTAATTVSVSFSLHGSPAKMTVALLVYPEKHAPLSFNNIIPQPSGGNRDGRGVDQTATGSRGHVKRMATDDVVTLLLALEGLAERRRANIAQGIDKDSPLKARIAELEEKRRAFSGVEGMAQGVVQSRTVDLISAQYLALSQTHRANFTGHVAAYLRQLAASTGVPVTLDISRYTGATIGRGGSSSTVDATQERLQRMQSRIEMLSQQIKKLEGEKTCLDIEQSLSRSQGSAEELKAITAKIESLTSQRQLLQRSCATIEGAGVKPSGSYDHTPVVHEVIGIRARILALSKEEEQLREKVLRMSNVTVGHVLKWARSKDPPMEEVRKDDTGLSGVAQGYHMRKENQSAHPLPQNPVPTQTPQKTEEPEKAAHNSSTQQSSENDSDTDSDGDTAKVAGDGKSSGKSSTRASRITKRFPDWGKIRKSDMYGATGLPSANDFEGGAGSEQQVVSKGSYGDPLAPDLGSSMFSTRRQERAAPQKQEQERKNSSLVVGSDLPQLNFDAPLEDTTTSGHGGFFSSSFADGPTGSIPAIQIVSVDDDAFTYDVGETEGNNFVADDSITYNTFQMEGSSTNEPAFSITPSGLPTYSFESGGENTFSTGGNEGGLPVYNFGSDHLSVSKDKRESGNHTLTFNFGS
Protein: Probable L-galactonate transporter (Galactonate:H(+) symporter) (P39398)
Organism: Escherichia coli (strain K12)
Function: Probably responsible for the transport of L-galactonate from the periplasm across the inner membrane. Is essential for growth on L-galactonate as the sole carbon source.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable HTH-type transcriptional regulator LgoR
- L-galactonate-5-dehydrogenase
Sequence:
MEKENITIDPRSSFTPSSSADIPVPPDGLVQRSTRIKRIQTTAMLLLFFAAVINYLDRSSLSVANLTIREELGLSATEIGALLSVFSLAYGIAQLPCGPLLDRKGPRLMLGLGMFFWSLFQAMSGMVHNFTQFVLVRIGMGIGEAPMNPCGVKVINDWFNIKERGRPMGFFNAASTIGVAVSPPILAAMMLVMGWRGMFITIGVLGIFLAIGWYMLYRNREHVELTAVEQAYLNAGSVNARRDPLSFAEWRSLFRNRTMWGMMLGFSGINYTAWLYLAWLPGYLQTAYNLDLKSTGLMAAIPFLFGAAGMLVNGYVTDWLVKGGMAPIKSRKICIIAGMFCSAAFTLIVPQATTSMTAVLLIGMALFCIHFAGTSCWGLIHVAVASRMTASVGSIQNFASFICASFAPIITGFIVDTTHSFRLALIICGCVTAAGALAYIFLVRQPINDPRKD
Protein: HTH-type transcriptional regulator DctR (P37195)
Organism: Escherichia coli (strain K12)
Function: May act as a transcriptional regulator of dctA.
Interaction partners:
- Outer membrane protein Slp
- Putative magnesium transporter YhiD
- Protein HdeD
- Glutamate decarboxylase alpha
- HTH-type transcriptional regulator GadX
- Acid stress chaperone HdeA
- HTH-type transcriptional regulator GadW
- Transcriptional regulator GadE
- Transcriptional regulatory protein RcsB
- Glutamate decarboxylase beta
Sequence:
MFLIITRDTMFFTAMKNILSKGNVVHIQNEEEIDVMLHQNAFVIIDTLMNNVFHSNFLTQIERLKPVHVIIFSPFNIKRCLGKVPVTFVPRTITIIDFVALINGSYCSVPEAAVSLSRKQHQVLSCIANQMTTEDILEKLKISLKTFYCHKHNIMMILNLKRINELVRHQHIDYLV
Protein: Tiggrin (Q9VMD9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions as a ligand for integrin alpha-PS2/beta-PS. Required in larvae for proper muscle structure and function. Involved in the regulation of cell adhesion during wing development.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20371600, ECO:0000269|PubMed:7924982}. Note=Localizes to the basal surface of the dorsoventral cell layer interface during pupal wing development. {ECO:0000269|PubMed:20371600, ECO:0000269|PubMed:7924982}.
Interaction partners:
- Polypeptide N-acetylgalactosaminyltransferase 3
- Golgi matrix protein 130 kD
- Glutactin
- General vesicular transport factor p115
- Viking, isoform A
- FI03416p
- Golgi SNAP receptor complex member 1
Sequence:
MRALGGITLLLAVAICQGYETYQRSSFRSSSSSSYGGGQTVPQLNSFASAHFNEVRELANQLKQKFNVLSQGSTNFAYTSPWSASILDLSGKSTLQLDQLSSEISRQLVQDMREGITNYHTIAQPNFFEAKAAELLERYSGAESASLQQTVGLGPYQPVDLSGFDEVKNYAYPAEVKVIDGKTYVVHRNCTEATKLSDYGSSGQLNSGFLGHQQTSLPLSSTTTTITRKKTIHDWVRENMEPSVVGYNSVVKLDGQLRNSALNQMVPLSPGSNVVIHRFNKTITTNPDGTSSVGGSEWQQRWQDGKLVYDHQQPFGQSTIPRDEQWKREERERLFWYLTTPQRLDDWQQQQEERLLGVVQRYQVSLPVLKEFHRRELARYEALLGQYQSRVQDTSSWQRQERGRLDWLIHQNGFTVQDIERWQNENARKLAEAARQHGISQNQLQQFQREELQRLYVHFNQVNESLAPQVPSVPQTTYNYQSSSSLTEDNTKEQQRLEELIRQHNATIAALQNSIKTDQQRLKNLSIKYQGDMQSQTQWLRGEVARIGDLIKEQNEQVSKITAWQSSERSRLENILLQHRGSVEEVQQRINMDRNYLQNLATKYQVSVEELEKWQKEELERLQVRGQQQLEEHIKDWQISVSSNLRDIATQNKLTIDEFQNYIINDRSHLEEMARLYKVKVEEIEQWIKSELKKFQSEGLLKGVEQELIQWQQKERERLQAIVQQNSLTVEQLEVRIKNDQDHFFKLADKYKINVEDIQDWLKKELLRLQSEGLVKAETLKEWQQQERAQISLLVQQNKYSLDEFERKMLADRARLQELSNTYNVKVSEIEQWIKSEGDRLQHEGQLRMESQLNNWQKIERQRLLDLINKNNLSIEEIESKISKDQTHLYSLAQQHQVRVEEIEQWIRQQIQKLQDQGLIEMQKLKNWQLEWRGNLTNMVQDRDFTVEEFHKWLLKDREQLQSLAMQHNVQIEEIEQFVKKEEQRFIGMGLLKPSEKLTNWQEVERLHLKNLAQQQYKSTEQLEARLRQDRELLERLARQYSVQVEEIESWMKQELARMRDEGQLQIDNLTSWQLAERERLEALIKQNKQWSAEELRAELEKDREHMQTMAFQYHTSVEEIEKWLQSEIERLKQQGKLNIEQLTAWQRTEQQRILSLLQQHSNITLEQFQAKVHNDRRFLMNLAEQHHVHIEEVDNYVKQVIEDLRKNGQFEIEQLQTWQRVERDYIKSLISEYKNSLSTAEYEEKLLADRAHLKHLADQYRINVEQIEEWMIAELKRLRGSTEETLKSLSAWQVSELERLQNLVKQQNHLTFVEFEMELNQERDRLQKLANQYSVNVVEIEEWLRQQLINLRTTGQAKVENLSKWQVEEQQRLIEMLLKKQQEMPYEQVERELTQDHARLQSLSQTHHVDIDHVDHWLREELRRLQSSGLVQIEQQTQWQQKISNGFNNWLEQQRNGASYQDFVDFLKRDKQRMDGIATDYHVTVEQVEKWVQKEAARLSLIGVIERPENNLKYEDISNIWVGDQTDSWKNELVTRLRSVTRQRPFTRQEFESYLIRNKPIFEQIARQYHVTIEDIHLWLDQSAKNEGLVTTEWQAKERLHIDNLINQQLRKQQRWTIEELELRLNNDQKHLQDAVAQYHVTVEELKVWYKDELNRLLEQRRIDRGSGISWQNIESQRIYLAIVNNPGISRQALENRLFRDVHVRASQYQITVEELRQFILSQLRRFSDMGLIVDNGRQANNWHDQERKRLREVVKGVVITEQELLDFISQDTSFQTQLAQSYQVGLEQLAPVQRIFIGNLAREQLLEQRRLNHLTTWQQRERDRLYEFIGNQNMTQTELKTWQIQDSKLLAEFAKRYEISVQQLSDWQKKELARINQLARYYGMSQSDLQQFREGELRQLAYINHRQLLSAAEAQKWEKRHQWTLSRLQSRYGKFGQELVAWRRTLYLLSQGLIDLPADSGSNGGYVVDAGSTNATAVYKPIFSKDRGDQPPHTYDESFVEGDEPGLEGETARPRPPNPAPIVSTPKPPLPYSRGGPSGGFEYRRQDYTFNVPVGSASASASGGPTGSSASASASLGKWNRASGDEPLQQEVDLGQQQQIEELGWNEKLEDLGQQTQVEDTDWNQQAEDLGQQQQVQVEDDLHFDQTQGHSSSSNSRSQPLQQATKVEVEATSEPSFWEKLKEKLG
Protein: Cytochrome b6-f complex subunit 4 (17 kDa polypeptide) (P0C318)
Organism: Oryza sativa subsp. indica (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01344}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01344}.
Interaction partners:
- Cytochrome b6
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- Photosystem I iron-sulfur center
- Cytochrome f
- Cytochrome b6-f complex subunit 5
- NAD
- NAD
- Photosystem II D2 protein
- Cytochrome b559 subunit alpha
- Cytochrome b559 subunit beta
Sequence:
MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPTGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVALWLGIGATLPIEKSLTLGLF
Protein: Tyrosine--tRNA ligase (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) (TyrTS) (P00952)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGEARAFGLTIPLVTKADGTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRISEALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA
Protein: Vomeronasal type-1 receptor (A0A2I3BRK7)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
Sequence:
MDLISCQQTFIHIMLFFTAGDILHTDIFESMNIENDFKCKTTFYICRVMRGLSICTTCLLSVFQAVTISPNTSLLAKFKHKLKKYTINAFFYIWSFNLSFSSNLIFYVGAYTNVSETNQMKVTKYCSLFPMNYIIRGLILTVTTSRDVFLVGVMLITSTYMVIILFRHQRQCKHLHSIRHLRASPEKKATQTILLLVVFFVVMYWVDFIISSTSVLLWMYDPVILTVQKFVMNAYPTITPLVQISSDNRIINLLKNLQSKCH
Protein: Phosphoenolpyruvate carboxylase kinase 2 (AtPPCK2) (EC 2.7.11.1) (Q93VK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-independent kinase involved in light-dependent phosphoenolpyruvate carboxylase phosphorylation.
Interaction partners:
- Phosphoenolpyruvate carboxylase 3
- Phosphoenolpyruvate carboxylase 1
- Phosphoenolpyruvate carboxylase 2
- Sulfate/thiosulfate import ATP-binding protein, putative
Sequence:
MTREFELENNYQLCDEIGRGRFGTITRCFSPATKEFYACKTIDKRVLIDALDRECIETEPRIMAMLPPHPNIIRIFDLYETEDSLAIVMELVDPPMTIYDRLISAGGRLSESESASYAKQILSALAHCHRCDVVHRDVKPDNVLVDLVSGGVKLCDFGSAVWLGGETAEGVVGTPYYVAPEVVMGRKYDEKVDIWSAGVVIYTMLAGEPPFNGETAEDIFESILRGNLRFPPKKFGSVSSEAKDLLRKMICRDVSRRFSAEDALRHSWMMNVGNLQSN
Protein: Portal protein (Gene product 20) (gp20) (P13334)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the terminase subunits to form the packaging machine. Attaches to the host inner membrane most likely through interaction with host yidC and forms together with chaperone gp40 an initiator complex to form the prohead.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04114, ECO:0000269|PubMed:11162794}. Host cell inner membrane {ECO:0000269|PubMed:22855489}. Note=Located at a unique 5-fold vertex of the icosahedral capsid. Localization at the inner host membrane is likely due to interactions with host membrane proteins such as yidC. {ECO:0000255|HAMAP-Rule:MF_04114, ECO:0000269|PubMed:22855489}.
Interaction partners:
Sequence:
MKFNVLSLFAPWAKMDERNFKDQEKEDLVSITAPKLDDGAREFEVSSNEAASPYNAAFQTIFGSYEPGMKTTRELIDTYRNLMNNYEVDNAVSEIVSDAIVYEDDTEVVALNLDKSKFSPKIKNMMLDEFSDVLNHLSFQRKGSDHFRRWYVDSRIFFHKIIDPKRPKEGIKELRRLDPRQVQYVREIITETEAGTKIVKGYKEYFIYDTAHESYACDGRMYEAGTKIKIPKAAVVYAHSGLVDCCGKNIIGYLHRAVKPANQLKLLEDAVVIYRITRAPDRRVWYVDTGNMPARKAAEHMQHVMNTMKNRVVYDASTGKIKNQQHNMSMTEDYWLQRRDGKAVTEVDTLPGADNTGNMEDIRWFRQALYMALRVPLSRIPQDQQGGVMFDSGTSITRDELTFAKFIRELQHKFEEVFLDPLKTNLLLKGIITEDEWNDEINNIKIEFHRDSYFAELKEAEILERRINMLTMAEPFIGKYISHRTAMKDILQMTDEEIEQEAKQIEEESKEARFQDPDQEQEDF
Protein: Elongation of fatty acids protein (EC 2.3.1.-) (Q4QFR9)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQWIDSWGANHYDGYAFKQWLLDNHDIAIYVAVGYITFVFQAPKLVSKYLNLPANAKSSALVPVINKTWAVWNILLSAFAFYGTTRVVPPLLYNLKTYGLHDTLCTFRPDEFYTSDVGVALGLFTISKVPEFGDTFFLVLKGTKLRFLSWFHHTAMFLYVWLSYETGSSTLICAAAMNYFVHTIMYFYFFLSEAGFKNLARPFAMYITMLQLVQMVGVMFVSGYVIAQKYILAGQGIMDGMEGSCSGTTMATARLQLGIYTAFLYLFGEMFVNNHVRPRVAKKAD
Protein: S-acyl fatty acid synthase thioesterase, medium chain (EC 3.1.2.14) (Medium-chain S-acyl fatty acid synthetase thioester hydrolase) (Oleoyl-ACP hydrolase) (Thioesterase II) (Thioesterase domain-containing protein 1) (P08635)
Organism: Rattus norvegicus (Rat)
Function: Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:3105579}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Fatty acid synthase
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Lipoyl amidotransferase LIPT1, mitochondrial
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
Sequence:
METAVNAKSPRNEKVLNCLYQNPDAVFKLICFPWAGGGSIHFAKWGQKINDSLEVHAVRLAGRETRLGEPFANDIYQIADEIVTALLPIIQDKAFAFFGHSFGSYIALITALLLKEKYKMEPLHIFVSGASAPHSTSRPQVPDLNELTEEQVRHHLLDFGGTPKHLIEDQDVLRMFIPLLKADAGVVKKFIFDKPSKALLSLDITGFLGSEDTIKDIEGWQDLTSGKFDVHMLPGDHFYLMKPDNENFIKNYIAKCLELSSLT
Protein: C-C motif chemokine 17 (ABCD-2) (CC chemokine TARC) (Small-inducible cytokine A17) (Thymus and activation-regulated chemokine) (Q9WUZ6)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000269|PubMed:29871928, ECO:0000269|PubMed:30277599}.
Interaction partners:
Sequence:
MRSLQMLLLAALLLGTFLQHARAARATNVGRECCLDYFKGAIPIRKLVSWYKTSVECSRDAIVFLTVQGKLICADPKDKHVKKAIRLVKNPRP
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (F6PDY7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
Sequence:
MANNSYSGVKNSVAEPNHNGEFGCSLKELRSLMELRGAEGLQKIQETYGDVNGLCNRLKTSAVDGLSGQPSDIEKRKAAFGQNFIPPKKPKTFLQLVWEALQDVTLIILEVAAIVSLGLSFYKPPDAGDKNCVKGTGGEPEEEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQFRGLQSRIEQEQKFSVVRGGQVIQIHVAEIVVGDIAQIKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDAMLLSGTHVMEGSGKIVVTAVGVNSQTGIIFTLLGAGEDDDDEEEKEKKKEKERKKEKKNKKQDGSVENRKKAKAQDGAAMEMQPLNSDEGADGEEKRKANLPKKEKSVLQGKLTKLAVQIGKAGLLMSAITVIILVVLFVVDTFWVDKIPWDSGCIPIYIQFFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQVFIADKHYRKVPEPDVVPASTMDLLIVGISVNCAYTTKIMSPEKEGGLNRQVGNKTECALLGFALDLKKDYQAVRNEIPEEKLYKVYTFNSVRKSMSTVLKNDDGSYRMFSKGASEILLKKCFKILTSTGEAKVFRPRDRDDMVKRVIEPMASEGLRTICLAYRDFPASEGEPDWDNEADILTRLTCVCVVGIEDPVRPEVPDAIRKCQRAGITVRMVTGDNLNTARAIATKCGILQVGDDFLCLEGKEFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTVVEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFSSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASLALATEPPTESLLLRKPYGRNKPLISRTMMKNILGHAVYQLIIIFTLLFAGEKMFNIDSGRYADLHAPPSEHYTIVFNTFVMMQLFNEINARKIHGERNVFEGIFNNMIFCTIVFGTFVIQIVIVQFGGKPFSCVGLNIEQWLWCIFLGFGCLLWGQVISTIPTSRLTFLKTAGHGTQKEEIPDEELEELEDLDEIDHAERELRRGQILWFRGLNRIQTQIRVVNAFRSSLSPYEGLEKPESRTSIHNFMTHPEFRIEDSEPHIPLIDDTDAEDDAPTKRNATPTPPPPPSPNQNNNAVDSGVHLFLDPSKSATPSAPGSPMHSLETSL
Protein: Trafficking protein particle complex subunit 33 (TRAPP subunit 33) (Transport protein particle 33 kDa subunit) (Q99394)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation. Required for sporulation. Has a role late in meiosis following DNA replication.
Subcellular location: Golgi apparatus, cis-Golgi network. Endoplasmic reticulum. Preautophagosomal structure.
Interaction partners:
- Trafficking protein particle complex II-specific subunit 130
- Trafficking protein particle complex subunit 23
- Trafficking protein particle complex subunit BET5
- Trafficking protein particle complex II-specific subunit 120
- Trafficking protein particle complex subunit 20
- Trafficking protein particle complex II-specific subunit 65
- Trafficking protein particle complex III-specific subunit 85
- TRAPP-associated protein TCA17
- Trafficking protein particle complex subunit BET3
- Trafficking protein particle complex subunit 31
Sequence:
MSSTHSNNVGHPQSSPQGPLTEQQRAQQQYQIFENSLPKVSQSVYQMLLNEMVPLAMGIERQISGDVISSDSNVTSENGNINNMIKRLKIEEHHTVDIIRSHNLIHELYKADEEEKEKVLARLRNIGFQIGLKLSELLIFSNNPNLKFKEMDLLLIMKFICRDVWKQIFGKQIDNLKTNHRGTFYLLDYDYRPIQSFSLEEDAKNEELKMIEPFLEIPVGIIRGVLSSLGYSSEEVICLASFIDRPTDRPKTAFPKGVSFHVQVTMPQ
Protein: Odorant receptor (B0FAQ4)
Organism: Apocrypta bakeri (Parasitic fig wasp)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU351113}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU351113}.
Interaction partners:
Sequence:
MKFKHQGLVADLLPNIRVMQGVGHFMFNYYSEGKKFPHRIYCIVTLLLLLLQYGMMAVNLMMESDDVDDLTANTITMLFFLHPIVKMIYFPVRSKIFYKTLAIWNNPNSHPLFAESNARFHALAITKMRRLLFCVAGATIFSVISWTGITFIEDSVKRITDPETNETTIIPIPRLMIRTFYPFNAMSGAGHVFALIYQFYYLVISMAVSNSLDVLFCSWLLFACEQLQHLKAIMKPLMELSATLDTVVPNSGELFKAGSADHLRESQGVQPSGNGDNVLDVDLRGIYSNRQDFTATFRPTAGTTFNGGVGPNGLTKKQEMLVRSAIKYWVERHKHVVRLVTAVGDAYGVALLLHMLTTTITLTLLAYQATKVNGVNVYAATVIGYLLYTLGQVFLFCIFGNRLIEESSSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMSISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK