wanglab/gogpt-training-data huggingface dataset:
Protein: Tumor necrosis factor receptor superfamily member 1B precursor (Tumor necrosis factor receptor superfamily, member 1B) (F1RAS9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Lymphotoxin-alpha
- TNF receptor-associated factor
- TNF receptor-associated factor
- Lymphotoxin-alpha
- Tumor necrosis factor receptor superfamily, member 1a.
- TNF superfamily member 11
- Interleukin-1.
Sequence:
MLILIARLLLLFMTVVWLMAEGKIPPPFRPEKEQCNNTTSEYYMKQLGLCCSRCKPGTRLSVQCSTASDTICEPCPDGMYSENMNHYPNCFKCPTCREEKGLMYGRNCSADTKAVCVCKPGMYCSKYGLSSACEECKKYKTCKPGEGAQRKGTPTGVVKCAPCPTGTFSDRSGSEPCRPHTECEGSAVLRSGNSTDDTVCVVKPLKATPEIWPMNTISTSTVSVLSSDVKHSSTVTTNAQGTRSNPPPDYMTIIYITGAVVLVLLILVMTVVTCKLRERKGLTKVPITDVNTVEQDPSQSSTPDHQHLLHVDRTQTEPSMSSSDSQSQPDCGQSHSSSEWLERSSQDECPSVSSPVLNLSITATFNCQLNPAATSCSIPINPSTLTPHAEALVPLSQEEVCTSSCQQEDGKEVLKSVQESGPFLY
Protein: Medium/long-chain-fatty-acid--CoA ligase FadD8 (EC 6.2.1.2) (EC 6.2.1.3) (FACL8) (O06417)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA).
Interaction partners:
- o-succinylbenzoate synthase
- Conserved protein
- Possible lipid transfer protein or keto acyl-CoA thiolase Ltp4
- Probable esterase LipO
- Enoyl-CoA hydratase EchA19
- Probable lipid carrier protein or keto acyl-CoA thiolase Ltp3
- Mycocerosic acid synthase-like polyketide synthase
- Mycoketide-CoA synthase
- Phthioceranic/hydroxyphthioceranic acid synthase
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
Sequence:
MSTAGDDAVGVPPACGGRSDAVGVPQLARESGAMRDQDCSGELLRSPTHNGHLLVGALKRHQNKPVLFLGDTRLTGGQLADRISQYIQAFEALGAGTGVAVGLLSLNRPEVLMIIGAGQARGYRRTALHPLGSLADHAYVLNDAGISSLIIDPNPMFVERALALLEQVDSLQQILTIGPVPDALKHVAVDLSAEAAKYQPQPLVAADLPPDQVIGLTYTGGTTGKPKGVIGTAQSIATMTSIQLAEWEWPANPRFLMCTPLSHAGAAFFTPTVIKGGEMIVLAKFDPAEVLRIIEEQRITATMLVPSMLYALLDHPDSHTRDLSSLETVYYGASAINPVRLAEAIRRFGPIFAQYYGQSEAPMVITYLAKGDHDEKRLTSCGRPTLFARVALLDEHGKPVKQGEVGEICVSGPLLAGGYWNLPDETSRTFKDGWLHTGDLAREDSDGFYYIVDRVKDMIVTGGFNVFPREVEDVVAEHPAVAQVCVVGAPDEKWGEAVTAVVVLRSNAARDEPAIEAMTAEIQAAVKQRKGSVQAPKRVVVVDSLPLTGLGKPDKKAVRARFWEGAGRAVG
Protein: G protein-coupled receptor 88 (Striatum-specific G-protein coupled receptor) (Q9EPB7)
Organism: Mus musculus (Mouse)
Function: Probable G-protein coupled receptor implicated in a large repertoire of behavioral responses that engage motor activities, spatial learning, and emotional processing. May play a role in the regulation of cognitive and motor function.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ESP4}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q9GZN0}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9ESP4}. Nucleus {ECO:0000250|UniProtKB:Q9ESP4}. Note=Localized to cilia in ciliated cells; whereas in non-ciliated cells, distributed throughout the cell membrane (By similarity). During cortical lamination, subcellular location shifts, on the day of birth, from expression at the plasma membrane and in the cytoplasm to the nuclei of neurons. This intranuclear localization remains throughout adulthood. {ECO:0000250|UniProtKB:Q9ESP4, ECO:0000250|UniProtKB:Q9GZN0}.
Interaction partners:
- G-protein coupled receptor 6
- G-protein coupled receptor 52
Sequence:
MTNSSSTSTSTTTGGSLLLLCEEEESWAGRRIPVSLLYSGLAIGGTLANGMVIYLVSSFRKLQTTSNAFIVNGCAADLSVCALWMPQEAVLGLLPSGSAEPPGDWDGGGGSYRLLRGGLLGLGLTVSLLSHCLVALNRYLLITRAPATYQVLYQRRHTVGMLALSWALALGLVLLLPPWAPKPGAEPPQVHYPALLAAGALLAQTALLLHCYLGIVRRVRVSVKRVSVLNFHLLHQLPGCAAAAAAFPAAPHAPGPGGAAHPAQPQPLPAALQPRRAQRRLSGLSVLLLCCVFLLATQPLVWVSLASGFSLPVPWGVQAASWLLCCALSALNPLLYTWRNEEFRRSVRSVLPGVGDAAAAAAAATAVPAMSQAQLGTRAAGQHW
Protein: Probable ribonuclease P protein subunit 1 (EC 3.1.26.5) (Q9P7W9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribonuclease P/MRP protein subunit POP5
- Probable ribonuclease P protein subunit 3
- Ribonuclease MRP protein subunit rmp1
- Ribonucleases P/MRP protein subunit pop1
- Ribonuclease P protein subunit rpr2
- Ribonucleases P/MRP protein subunit pop3
- Uncharacterized protein C16C4.19
- Uncharacterized protein C6C3.09
- Ribonucleases P/MRP protein subunit POP7
- Probable ribonucleases P protein subunit pop8
Sequence:
MADPLYSSLKTVNSTSKVTPESLVFQTKILTPEEAKNVINEKIAFKPLLLVPSLNLEKQGDRKESVASKKRKKLSSKEKKKLQLNVVPKIADYSQFKHLHSMWCSYILEVIAGCTGESLMAKLAKAEYQGAYMQVLRSKSTTRVGLEGICIHESKHMLSLITKENRVVRVPKQDSVMKVIVDVPQRKLVFELYTQHLLLRAGDRSNKRFKSKNTIDL
Protein: Precursor of CEP3 (PCEP3) [Cleaved into: C-terminally encoded peptide 3 (CEP3)] (O80460)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signaling peptide that represses primary root growth rate and significantly inhibits lateral root formation. Promotes shoot growth. Modulates leaf morphology. Regulates systemic nitrogen (N)-demand signaling. Mediates systemic up-regulation of genes involved in N uptake and assimilation pathways.
Subcellular location: [C-terminally encoded peptide 3]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.
Interaction partners:
Sequence:
MATINVYVFAFIFLLTISVGSIEGRKLTKFTVTTSEEIRAGGSVLSSSPPTEPLESPPSHGVDTFRPTEPGHSPGIGHSVHN
Protein: Aminoglycoside N(3)-acetyltransferase III (EC 2.3.1.81) (AAC(3)-IIIa) (ACC(3)-III) (Aminocyclitol 3-N-acetyltransferase type III) (Aminoglycoside acetyltransferase (3)-IIIa) (Gentamicin-(3)-N-acetyl-transferase) (P29808)
Organism: Pseudomonas aeruginosa
Function: Resistance to antibiotics containing the 2-deoxy-streptamine ring including dibekacin, gentamicin, kanamycin, sisomicin, tobramycin and neomycin, but not to amikacin or netilmicin. Acetylates a broad range of both 4,5- and 4,6-disubstituted aminoglycosides, including neomycin, paromomycin, ribostamycin, sisomicin, gentamicin, tobramycin and kanamycin, with no preference of one disubstitution over the other. Acetylates sisomicin and kanamycin most and least efficiently, respectively. Does not modify plazomicin.
Interaction partners:
Sequence:
MTDLNIPHTHAHLVDAFQALGIRAGQALMLHASVKAVGAVMGGPNVILQALMDALTPDGTLMMYAGWQDIPDFIDSLPDALKAVYLEQHPPFDPATARAVRENSVLAEFLRTWPCVHRSANPEASMVAVGRQAALLTANHALDYGYGVESPLAKLVAIEGYVLMLGAPLDTITLLHHAEYLAKMRHKNVVRYPCPILRDGRKVWVTVEDYDTGDPHDDYSFEQIARDYVAQGGGTRGKVGDADAYLFAAQDLTRFAVQWLESRFGDSASYG
Protein: LP13385p (Q9W3J9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform E
- LD41913p
Sequence:
MSHKRCLANEVIEFVLPANSDYSDEDNRGNVRVINTSDDATYVLLDNLGNEFEEDIIIVNENGVEKEMLMSKELRDFIVGSRVKDLTDDEQMPQFVVRELDMSEVGDLVEVEPEMEQEADYGDYGDYEHEPSYGHPRDNERVEEDLDMYPPSSPSLPPSPPRPPSPVVQPASKARNSARQIALRSFVSQKNNDDDDGSVKEVKPSEKMLEEFKGPRRYMLFDDLIATIVDFDEDSTPLVEFSMISDIMDEKLPVECGICPDVMHKSKLSKHHKTHLVPGTNRYACIYCTETYRDCKYLAGHARRHMGIRPYVCELCTLYFSTKQDLRVHNQRRHLEKEHICEVCGKTFAQNTQLKRHREATHEKKRRFQCEYCQKAYYKNFSLQEHIRNVHMGKRRMLKCPFCGMQCRDAHKMARHRKEMHLSQGTYVCHLCQEEFTDISYFDAHKRSIQCRSNTRRFVNADGNREGSDSESISGRNMNGQDDDYDGMGPLQEEYDEDDGLLVEDNQPEEQGSPSNRQYLDESEQQYVQLSDYDDQHLLVENAVDAEDGGEDLDELLTEDQYFNAVQQHHQQHQQHHGRGQDYNDELIYEITLKTEDN
Protein: Rhoptry protein 18 (A1E140)
Organism: Toxoplasma gondii
Interaction partners:
Sequence:
MLGRLIQPLTKHYHILQFCTHPSTVCVNVVMFSVQRPSLTCTVVRMGLATLLRKTACLAGLTVALVFLLFQVQDGTGITLRPSKLDSKPTISLDSQQHVANKRGSATVGHYKYSLAGATESTRDVSLLEERAQHGVNTQETNQRRTTFQRLVNRLRRRERDGAVSGFAADSPSRPRLSVRQRLAQLLRRAKSFFTHGIRRYYSQGRNRLRSWWAQRRRSGLVFEKADSGCVIGKRILAHMREQIRQPQALESSQRLDGILTAAAWPPDVPAKFVSLTTGETRTLVRGAPLGSGGFAAVYQVTDVETNEELAVKVIISEKKPTDETMRDLERESFCYKNFSLAKTAKDAQENWRFMVASDVVTLEGQPATTEVVIGSATKWVPNYFLLMMRAETDMSKVISWLFGDASVNNSELGLVVRMHLSSQAIRLVANVQAQGIVHTDIKPPNFLLLKDGRLFLGDFGTYKTNNSVGPAIGTPGYEPPEQPFHSYGVTYTFATDAWQLGITLYCIWCKESPTPADGIWDYLHFADCSSTPELVQDLIRNLLNREPQKRMLPLQALKTAAFNEMDSVVKRAAQNFEQQEHLQTE
Protein: Nudix hydrolase 6 (AtNUDT6) (EC 3.6.1.-) (ADP-ribose pyrophosphatase) (EC 3.6.1.13) (NADH pyrophosphatase) (EC 3.6.1.22) (Q9SJC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear.
Interaction partners:
- Nudix hydrolase 1
- Nudix hydrolase 11
- Nudix hydrolase 4
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Nudix hydrolase 25
- COP9 signalosome complex-related / CSN complex-like protein
- DNAJ heat shock N-terminal domain-containing protein
- Serinc-domain containing serine and sphingolipid biosynthesis protein
- Nudix hydrolase 24, chloroplastic
- Protein NIM1-INTERACTING 1
Sequence:
MDNEDQESLLLQGVPDNYGGVKVNLTEPMTIEDFVPKLRASLVYWSNQGTKGIWLKLADGLDNLIAPAKAEGFVCHHAEREYTMLTSWIADVPSTLPANASHRIGVGAFVLNKKTKEVLVVQEIDGHFKGTGVWKLPTGVVKEGENIWEGALREVEEETGIKTKFVEVLAFRESHQAFLEIKTDIFFLCELEPTTFEIKKQDSEILAAKWMPIEEYVNQPWNQKKELFRFMANICLKRLQEMEYMGFSKVLTTTSSGKESYLYCNTDHANLLNATRGLASTSG
Protein: Endothelial cell-selective adhesion molecule (Q925F2)
Organism: Mus musculus (Mouse)
Function: Can mediate aggregation most likely through a homophilic molecular interaction.
Subcellular location: Cell junction, adherens junction {ECO:0000305}. Cell junction, tight junction {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q96AP7}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Occludin
- Claudin-5
- Cadherin-5
- Tight junction protein 1
- Platelet endothelial cell adhesion molecule
- Roundabout homolog 4
- Claudin-1
- Claudin-3
- Claudin-15
- Intercellular adhesion molecule 2
Sequence:
MILQAGTPETSLLRVLFLGLSTLAAFSRAQMELHVPPGLNKLEAVEGEEVVLPAWYTMAREESWSHPREVPILIWFLEQEGKEPNQVLSYINGVMTNKPGTALVHSISSRNVSLRLGALQEGDSGTYRCSVNVQNDEGKSIGHSIKSIELKVLVPPAPPSCSLQGVPYVGTNVTLNCKSPRSKPTAQYQWERLAPSSQVFFGPALDAVRGSLKLTNLSIAMSGVYVCKAQNRVGFAKCNVTLDVMTGSKAAVVAGAVVGTFVGLVLIAGLVLLYQRRSKTLEELANDIKEDAIAPRTLPWTKGSDTISKNGTLSSVTSARALRPPKAAPPRPGTFTPTPSVSSQALSSPRLPRVDEPPPQAVSLTPGGVSSSALSRMGAVPVMVPAQSQAGSLV
Protein: Exo-1,4-beta-xylosidase xlnD (EC 3.2.1.37) (1,4-beta-D-xylan xylohydrolase xlnD) (Beta-xylosidase A) (Beta-xylosidase xlnD) (Xylobiase xlnD) (Q2UR38)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- xylan 1,4-beta-xylosidase
- Probable exo-1,4-beta-xylosidase bxlB
- Endopolygalacturonase I
- galacturonan 1,4-alpha-galacturonidasegalacturonohydrolase)
- Xylanolytic transcriptional activator xlnR
- Probable endo-1,4-beta-xylanase B
- Alpha-L-arabinofuranosidase B
- Endopolygalacturonase B
- galacturonan 1,4-alpha-galacturonidase
- galacturonan 1,4-alpha-galacturonidase
Sequence:
MPGAASIVAVLAALLPTALGQANQSYVDYNIEANPDLFSECLETGGTSFPDCESGPLSKTLVCDTSAKPHDRAAALVSLLTFEELVNNTANTGHGAPRIGLPAYQVWNEALHGVAHADFSDAGGFSWSTSFPQPISTMAALNRTLIHQIATIISTQGRAFMNAGRYGLDVYSPNINTFRHPVWGRGQETPGEDAYCLASTYAYEYITGIQGGVDANPLKLIATAKHYAGYDIENWDNHSRLGNDMQITQQDLAEYYTPQFLVASRDAKVHSVMCSYNAVNGVPSCSNSFFLQTLLRDTFDFVEDGYVSGDCGAVYNVFNPHGYATNESSAAADSIRAGTDIDCGVSYPRHFQESFHDQEVSRQDLERGVTRLYASLIRAGYFDGKTSPYRNITWSDVVSTNAQNLSYEAAAQSIVLLKNDGILPLTSTSSSTKTIALIGPWANATTQMLGNYYGPAPYLISPLQAFQDSEYKITYTIGTNTTTDPDSTSQSTALTTAKEADLIIFAGGIDNTLETEAQDRSNITWPSNQLSLITKLADLGKPLIVLQMGGGQVDSSALKNNKNVNALIWGGYPGQSGGQALADIITGKRAPAARLVTTQYPAEYAEVFPAIDMNLRPNGSNPGQTYMWYTGTPVYEFGHGLFYTNFTASASASSGTKNRTSFNIDEVLGRPHLGYKLVEQMPLLNFTVDVKNTGDRVSDYTAMAFVNTTAGPAPHPNKWLVGFDRLSAVEPGSAKTMVIPVTVDSLARTDEEGNRVLYPGRYEVALNNEREVVLGFTLTGEKAVLFKWPKEEQLIAPQ
Protein: CDP-diacylglycerol--inositol 3-phosphatidyltransferase (EC 2.7.8.11) (Phosphatidylinositol synthase) (PI synthase) (PtdIns synthase) (O14735)
Organism: Homo sapiens (Human)
Function: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:8110188}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:8110188}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphatidate cytidylyltransferase 1
- Phosphatidate cytidylyltransferase 2
- Phosphatidylinositol 4-kinase alpha
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
- Phosphatidate cytidylyltransferase, mitochondrial
- Inositol monophosphatase 1
- Cardiolipin synthase
- Inositol monophosphatase 2
Sequence:
MPDENIFLFVPNLIGYARIVFAIISFYFMPCCPLTASSFYLLSGLLDAFDGHAARALNQGTRFGAMLDMLTDRCSTMCLLVNLALLYPGATLFFQISMSLDVASHWLHLHSSVVRGSESHKMIDLSGNPVLRIYYTSRPALFTLCAGNELFYCLLYLFHFSEGPLVGSVGLFRMGLWVTAPIALLKSLISVIHLITAARNMAALDAADRAKKK
Protein: Transmembrane protease serine 7 (EC 3.4.21.-) (Matriptase-3) (Q8BIK6)
Organism: Mus musculus (Mouse)
Function: Serine protease which preferentially hydrolyzes peptides with Arg at the P1 position.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15853774}; Single-pass type II membrane protein {ECO:0000269|PubMed:15853774}.
Interaction partners:
Sequence:
MDKEKSDPSCKSSDLKISNISIQVVSVPGKLPGRRPPRKPIGKPRPRKQPKKRAPFWNVQNKIILFTVFLFILAVTAWTLLWLYISKTESKDAFYFVGMFRITNIEFLPEYRQKESREFLSMAKTVQQVVNLVYTTSAFSKFYKQSVVADVSSNNKGGLLVHFWIVFVMPHAKGHIFCEECVAAILKDSIQTSIINRTSVGSLQGLAVDMDSVVLNAGLRSDYSSAVGSDNGCSRYLYADHLTLRYPLEISATSGQLMCHFKLVAIVGYLIRLSIESIQLEADNCITDSLTVYDSLLPIRSAILYRICEPTRTLMSFVSTNNLMLVILKSPYVRRLAGIRAYFEVIPEQKCESTILVKEINSFEGKISSPYYPSYYPPKCKCTWTFQTSLSTLGIALKFYNYSITKKSAKGCEHGWWEINEHMYCGSYMDHETIFRVPSPLVHIQLQCSSRLSDKPLLVEYGGYNISQPCPAGSFRCSSGLCVPQAQRCDGVNDCFDESDELFCVTVKPACNSSSFRQHGPLVCDGFRDCEDGQDEQNCTRSIPCTSRTFKCGNDICFRKQNAQCDGIVDCPDGSDEEGCGCSRSSSFLHRIVGGSDSQEGTWPWQVSLHFVGSAYCGASVISREWLLSAAHCFHGNRLSDPTPWTAHLGMYVQGNAKFISPVRRIVVHEYYNSQTFDYDIALLQLSIAWPETLKQLIQPICIPPAGQKVRSGEKCWVTGWGRRHEADSKGSPVLQQAEVELIDQTVCVSTYGIITSRMLCAGVMSGKSDACKGDSGGPLSCRRKSDGKWILTGIVSWGHGCGRPNFPGVYTRVSSFVPWIHKYVPSLL
Protein: Microtubule-associated proteins 65-1 (F4K3E4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAVTDTESPHLGEITCGTLLEKLQEIWDEVGESDDERDKLLLQIEQECLDVYKRKVEQAAKSRAELLQTLSDANAELSSLTMSLGDKSLVGIPDKSSGTIKEQLAAIAPALEQLWQQKEERVREFSDVQSQIQKICGDIAGGLSNEVPIVDESDLSLKKLDDFQSQLQELQKEKSDRLRKVLEFVSTVHDLCAVLGLDFLSTVTEVHPSLDEDTSVQSKSISNETLSRLAKTVLTLKDDKKQRLQKLQELATQLIDLWNLMDTPDEERELFDHVTCNISSSVDEVTVPGALARDLIEQVIYIALINLPMSSLRNQLLLANIHVKFVKAEVEVDRLDQLKASRMKEIAFKKQSELEEIYARAHVEVNPESARERIMSLIDSGNVEPTELLADMDSQISKAKEEAFSRKDILDRVEKWMSACEEESWLEDYNRDQNRYSASRGAHLNLKRAEKARILVSKIPAMVDTLVAKTRAWEEEHSMSFAYDGVPLLAMLDEYGMLRQEREEEKRRLREQKKVQEQPHVEQESAFSTRPSPARPVSAKKTVGPRANNGGANGTHNRRLSLNANQNGSRSTAKEAGRRETLNRPAAPTNYVAISKEEAASSPVSGAADHQVPASP
Protein: LSDAT_euk domain-containing protein (G5EGJ6)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSLFEHVWQISPPRLIITVHGGTSNFDLQPKLARVFRKGLLKAASTTGAWIITSGCDTGVVKHVAAALEGAQSAQRNKIVCIGIAPWGLLKKREDFIGQDKTVPYYPSSSKGRFTGLNNRHSYFLLVDNGTVGRYGAEVILRKRLEMYISQKQKIFGGTRSVPVVCVVLEGGSCTIRSVLDYVTNVPRVPVVVCDGSGRAADLLAFAHQNVTEDGLLPDDIRRQVLLLVETTFGCSEAAAHRLLHELTVCAQHKNLLTIFRLGEQGEHDVDHAILTALLKGQNLSAADQLALALAWNRVDIARSDVFAMGHEWPQAALHNAMMEALIHDRVDFVRLLLEQGINMQKFLTISRLDELYNTDKGPPNTLFYIVRDVVRVRQGYRFKLPDIGLVIEKLMGNSYQCSYTTSEFRDKYKQRMKRVKHAQKKAMGVFSSRPSRTGSGIASRQSTEGMGGVGGGSSVAGVFGNSFGNQDPPLDPHVNRSALSGSRALSNHILWRSAFRGNFPANPMRPPNLGDSRDCGSEFDEELSLTSASDGSQTEPDFRYPYSELMIWAVLTKRQDMAMCMWQHGEEAMAKALVACRLYKSLATEAAEDYLEVEICEELKKYAEEFRILSLELLDHCYHVDDAQTLQLLTYELSNWSNETCLALAVIVNNKHFLAHPCCQILLADLWHGGLRMRTHSNIKVVLGLICPPFIQMLEFKTREELLNQPQTAAEHQNDMNYSSSSSSSSSSSSSSSSSDSSSFEDDDDENNAHNHDQKRTRKTSQGSAQSLNITSLFHSRRRKAKKNEKCDRETDASACEAGNRQIQNGGLTAEYGTFGESNGVSPPPPYMRANSRSRYNNRSDMSKTSSVIFGSDPNLSKLQKSNITSTDRPNPMEQFQGTRKIKMRRRFYEFYSAPISTFWSWTISFILFITFFTYTLLVKTPPRPTVIEYILIAYVAAFGLEQVRKIIMSDAKPFYEKIRTYVCSFWNCVTILAIIFYIVGFFMRCFGSVAYGRVILACDSVLWTMKLLDYMSVHPKLGPYVTMAGKMIQNMSYIIVMLVVTLLSFGLARQSITYPDETWHWILVRNIFLKPYFMLYGEVYADEIDTCGDEAWDQHLENGGPVILGNGTTGLSCVPGYWIPPLLMTFFLLIANILLMSMLIAIFNHIFDATDEMSQQIWLFQRYKQVMEYESTPFLPPPLTPLYHGVLILQFVRTRLSCSKSQERNPMFDFSLKLFLDNDQIEKLHDFEEDCMEDLARQKLNEKNTSNEQRILRADIRTDQILNRLIDLQAKESMGRDVINDVESRLASVEKAQNEILECVRALLNQNNAPTAIGRCFSPSPDPLVETANGTPGPLLLKLPGTDPILEEKDHDSGENSNSLPPGRIRRNRTATICGGYVSEERNMMLLSPKPSDVSGIPQQRLMSVTSMDPLPLPLAKLSTMSIRRRHEEYTSITDSIAIRHPERRIRNNRSNSSEHDESAVDSEGGGNVTSSPRKRSTRDLRMTPSSQVEESTSRDQIFEIDHPEHEEDEAQADCELTDVITEEEDEEEDDEEDDSHERHHIHPRRKSSRQNRQPSHTLETDLSEGEEVDPLDVLKMKELPIIHQILNEEEQAGAPHSTPVIASPSSSRADLTSQKCSDV
Protein: Photosystem II assembly factor lipoprotein Psb27 (Photosystem II 11 kDa protein) (Q8DG60)
Organism: Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
Function: Plays a role in the repair and/or biogenesis of the calcium-manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of other extrinsic subunits PsbO, PsbU and PsbV, and thus assembly of calcium-manganese-oxide cluster. Psb27-containing complexes lack oxygen evolving activity and an oxidizable calcium-manganese-oxide cluster, but have a normal reaction center.
Subcellular location: Cellular thylakoid membrane {ECO:0000269|PubMed:33846594}; Lipid-anchor {ECO:0000305|PubMed:33846594}; Lumenal side {ECO:0000269|PubMed:33846594}. Note=Associated with PSII on the lumenal side of the thylakoid membrane, its binding site probably overlaps that of PsbO (PubMed:33846594). {ECO:0000269|PubMed:33846594}.
Interaction partners:
- Photosystem II assembly factor Psb28 protein
- Photosystem II extrinsic protein U
- Photosystem II extrinsic protein O
- Photosystem II extrinsic protein V
- Photosystem II CP47 reaction center protein
- Cytochrome b559 subunit alpha
- Cytochrome c-550-like protein
- Photosystem II reaction center protein K
- Photosystem II CP43 reaction center protein
- Photosystem II D2 protein
Sequence:
MKRFWAMVCALFLSVSLLLTSCANVPTGLTGNFREDTLALISSLREAIALPENDPNKKAAQAEARKKLNDFFALYRRDDSLRSLSSFMTMQTALNSLAGHYSSYPNRPLPEKLKARLEQEFKQVELALDREAKS
Protein: Antimicrobial peptide EP-20 (B3A0L3)
Organism: Xenorhabdus budapestensis
Function: The synthetic peptide inhibits growth of fungus P.capsici and partially that of V.dahliae, F.graminearum and F.omysporum.
Subcellular location: Secreted {ECO:0000269|PubMed:22497806}.
Interaction partners:
Sequence:
EGPVGLADPDGPASAPLGAP
Protein: Cytochrome c oxidase subunit 2 (Q8HCP6)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000457}.
Interaction partners:
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 1
- NADH-ubiquinone oxidoreductase chain 1
- Cytochrome b
- NADH-ubiquinone oxidoreductase chain 4
- Cytochrome b
- Cytochrome c oxidase
- NADH-ubiquinone oxidoreductase chain 3
- Heme O synthase
Sequence:
MILRSLECRFLTIALCDAAEPWQLGSQDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHFNEQTNPIPQRIVHGTTIEIIRTIFPSVILLFIAIPSFALLYSMDGVLVDPAITIKAIGHQWYRTYEYSDYNSSDEQSLTFDSYTIPEDDPELGQSRLLEVDNRVVVPAKTHLRMIVTPADVPHSWAVPSSGVKCDAVPGRSNLTSISVQREGVYYGQCSEICGTNHAFTPIVVEAVTLKDYADWVSNQLILQTN
Protein: 52 protein (P88989)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Interaction partners:
Sequence:
MASKKPDKTYEEMVKEVERLKLENKTLKQKVKSSGAVSSDDSILTAAKRESIIVSSSRALGAVAMRKIEAKVRSRAAKAVTEQELTSLLQSLTLRVDVSMEETTVGASGGIGPSSQTETKKRRPRSKSRHRHDHE
Protein: Ribonuclease VapC39 (RNase VapC39) (EC 3.1.-.-) (Toxin VapC39) (P9WF63)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB39.
Subcellular location: Secreted. Note=Following 6 weeks of nutrient starvation. {ECO:0000269|PubMed:23345537}.
Interaction partners:
- Antitoxin VapB39
- Ribonuclease VapC32
- Probable amino acid decarboxylase
- Ribonuclease VapC25
- Ribonuclease VapC28
- Elongation factor P
- Ribonuclease VapC37
- Ribonuclease VapC11
- Ribonuclease VapC33
- Ribonuclease VapC15
Sequence:
MTALLDVNVLIALGWPNHVHHAAAQRWFTQFSSNGWATTPITEAGYVRISSNRSVMQVSTTPAIAIAQLAAMTSLAGHTFWPDDVPLIVGSAGDRDAVSNHRRVTDCHLIALAARYGGRLVTFDAALADSASAGLVEVL
Protein: Polyadenylation and cleavage factor homolog 5 (Q9FIX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cleavage stimulation factor subunit 77
- Protein CLP1 homolog
- Polyadenylation and cleavage factor homolog 1
- Polyadenylation and cleavage factor homolog 4
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage stimulating factor 64
- Cleavage and polyadenylation specificity factor subunit 3-I
- Cleavage stimulation factor subunit 50
- Protein CLP1 homolog 5
- HEAT repeat-containing protein
Sequence:
MASNGSFSAQRNANAGTTMKRRNDNRGYGGGIGCYQEERNRYAPPQKRFRSQLQQQFRSGHNPLYHYGSNTNNNVSRVSSQSYNNYGVDVIASNSSFALPNNDSNTNNYQKPFVVYGNPNPQIVPLPLPYRKLDPLDSLPQWVPNSTPNYPVRSSNFVPNTPDFTNVQNPMNHSNMVSVVSQSMHQPIVLSKELTDLLSLLNNEKEKKTSEASNNDSLPVGLSFDNPSSLNVRHESVIKSLYSDMPRQCTSCGVRFKCQEEHSKHMDWHVRKNRSVKTTTRLGQQPKKSRGWLASASLWLCAPTGGGTVEVASFGGGEMQKKNEKDQVQKQHMVPADEDQKNCALCVEPFEEFFSHEADDWMYKDAVYLTKNGRIVHVKCMPEPRPAKDLREPSRVMSVTVPSVAKAILC
Protein: Nucleoporin NUP42 (NLP-1) (NUP42 homolog) (Nucleoporin hCG1) (Nucleoporin-42) (Nucleoporin-like protein 2) (O15504)
Organism: Homo sapiens (Human)
Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}. Nucleus membrane {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:12228227}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:10358091}.
Interaction partners:
- mRNA export factor GLE1
- Nuclear RNA export factor 1
- Nuclear pore complex protein Nup214
- Exportin-1
- mRNA export factor RAE1
- Nuclear pore complex protein Nup88
- Aladin
- Nucleoporin NUP35
- Nucleoporin SEH1
- E3 SUMO-protein ligase RanBP2
Sequence:
MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQQQPSGNNRRGWNTTSQRYSNVIQPSSFSKSTPWGGSRDQEKPYFSSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRLEYHNFLTSNNLQSYLNSVQRLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFMSPGFPVNNSSSDNAQNFSFKTNSGFAAASSGSPAGFGSSPAFGAAASTSSGISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLPASLATGPVRAPVAPAFGGGSSVAGFGSPGSHSHTAFSKPSSDTFGNSSISTSLSASSSIIATDNVLFTPRDKLTVEELEQFQSKKFTLGKIPLKPPPLELLNV
Protein: NADH dehydrogenase subunit 4L (Q94RD3)
Organism: Oryza sativa (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
TDPIKYFTFSMIISILGIRGILLNRRNILIMSMPIESMLLAVNLNFLVFSVSLDDMMGQSFASLVPTVAAAESAIGLAIFVITFRVRGTIAVEFINCIQG
Protein: RH45818p (Q8SY75)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRSLWLLLGLGLLAVSHVQASTEFSEDLLDEDLDLSDIDENEEEFLRLLEEKNKIKDIERENEIATKLAEVQHNLLNPVVEVDLCETMSCGAGRICQMHDEKPKCVCIPECPEEVDTRRLVCTNTNETWPSDCSVYQQRCWCDSGEPGCTNPDNAHMHIDYYGACHEPRSCEGEDLKDFPRRMRDWLFYVMRDLAERDELTEHYMQMELEAETNNSRRWSNAAVWKWCDLDGDTDRSVSRHELFPIRAPLVSLEHCIAPFLESCDSNKDHRITLVEWGACLELDPEDLKERCDDVQRAQPHLLG