wanglab/gogpt-training-data huggingface dataset:
Protein: Glutamate receptor ionotropic, kainate 1 (GluK1) (Excitatory amino acid receptor 3) (EAA3) (Glutamate receptor 5) (GluR-5) (GluR5) (P39086)
Organism: Homo sapiens (Human)
Function: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P22756}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P22756}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, kainate 5
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, kainate 3
- Disks large homolog 4
- Metabotropic glutamate receptor 7
- Neuropilin and tolloid-like protein 1
- Metabotropic glutamate receptor 5
- Neurochondrin
- Lysine--tRNA ligase
Sequence:
MEHGTLLAQPGLWTRDTSWALLYFLCYILPQTAPQVLRIGGIFETVENEPVNVEELAFKFAVTSINRNRTLMPNTTLTYDIQRINLFDSFEASRRACDQLALGVAALFGPSHSSSVSAVQSICNALEVPHIQTRWKHPSVDNKDLFYINLYPDYAAISRAILDLVLYYNWKTVTVVYEDSTGLIRLQELIKAPSRYNIKIKIRQLPSGNKDAKPLLKEMKKGKEFYVIFDCSHETAAEILKQILFMGMMTEYYHYFFTTLDLFALDLELYRYSGVNMTGFRLLNIDNPHVSSIIEKWSMERLQAPPRPETGLLDGMMTTEAALMYDAVYMVAIASHRASQLTVSSLQCHRHKPWRLGPRFMNLIKEARWDGLTGHITFNKTNGLRKDFDLDIISLKEEGTEKAAGEVSKHLYKVWKKIGIWNSNSGLNMTDSNKDKSSNITDSLANRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFIYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYVLLACLGVSCVLFVIARFTPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQTALVRNSDEGIQRVLTTDYALLMESTSIEYVTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEDNKEASALGVENIGGIFIVLAAGLVLSVFVAIGEFIYKSRKNNDIEQAFCFFYGLQCKQTHPTNSTSGTTLSTDLECGKLIREERGIRKQSSVHTV
Protein: Putative lipase ROG1 (EC 3.1.-.-) (Revertant of glycogen synthase kinase mutation protein 1) (P53118)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- N-alpha-acetyltransferase NAT5
- Protein kinase MCK1
- Ubiquitin ligase-binding protein BUL1
- Ubiquitin ligase-binding protein BUL2
- Monoglyceride lipase
- Protein LST4
Sequence:
MSLTPTNEILFHYKSSVKVGELERYVITYHLYDGEEIPPDLNLNSLWLKVRNMNPLSYRAAYLMGPFMLYCDVKTAQYHHSQKIVASVDYPKFEPNVQTQQDFVAELSVHNIRQKYVWIADVMSQILFTTNTNVTYEVTIGTSKESVENPHDLPSHLGSYSPKLTVNRLTTLDLWNLPVQITTPQKKKHLVVLTHGLHSNVSTDLVYIMEQIYKAQKNYPHEQIVVKGYRGNVCQTEKGVKYLGTRLAEYIIQDLYDESIRKISFVGHSLGGLIQAFAIAYIYEVYPWFFKKVNPINFITLASPLLGIVTDNPAYIKVLLSFGVIGKTGQDLGLENDVEVGKPLLYLLSGLPLIEILRRFKRRTVYANAINDGIVPLYTASLLFLDYNDILEQLQKLKENSKKSPLINDASTPVNQDFFNKTFISPLTKMLSILAPQKFPTENGSEIPKVSFFESASSILLPPLPERAYIMDPDSRDPVIIHDKIYNEDDIPQSEFDIEDGFFGKKNILLQAFFAGKKERAKYRNLEETIARRWHEGMAWRKVVVALKPDAHNNIIVRRKFANAYGWPVIDHLIDVHFNGDDDDDNDENDDINSTQVVEPIQSVTEGKKKYRKAENIPQEYGWLNKVETNGVFDEGPTGMISTVGEIVEALAKRGFSAVIDRRNASEDPNDEVLRFEEMNSDLVQ
Protein: Receptor-like protein tyrosine phosphatase kappa extracellular region (Q9WUL3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MDVPTAAAVAFVALLLLYPWPLLGSVRAQFSAGGCTFDDGPGVCDYHQDLYDDFEWVHVSAQEPHYLPPEMPQGSYMVVDSSNHDPGKKARLQLPTMGENDTHGIDFSYLLYSQKGLNPGTLNILVRVNKQPLANPIWNVTGFGGNDWLRAELAVSTFWPNEYRVIFEAEVSGWRSGYIAIDDIQVLSYPCDKSPHFLRLGDVEVNAGQNATFQCIATGRDAVHNKLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSGVSNFAQLIVREPPRPIAPPQLLGVGPTYLLIQLNANSIIGDGPIILKEVEYRMTSGSWTETHAVNAPTYKLWHLDPDTEYEIRILLTRPGEGGTGLPGPPLITRTKCAEPMRTPKTLKIAEIQARRIAVDWESLGYNITRCHTFNVTICYHYFRGHNESRADCLDMDPKAPQHVVNHLPPYTNVSLKMILTNPEGKKDSEETIIQTDEDVPGTCASQIPPRNIL
Protein: Protein LANA1 (Q9QR71)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Multifunctional protein that plays a role in the replication and long-term persistence of the viral episomal genome in dividing cells. Binds to mitotic chromosomes via its N-terminal region and to a 16-bp imperfect palindrome within the origin of replication (oriP) located in the viral terminal repeat (TR) through its C-terminal. Tethers viral episomes to chromosomes during mitosis. Plays a critical role in the shutdown of lytic gene expression during the early stage of infection by interacting with host TRIM28. Plays also a role in the repression of host NF-kappa-B activity upon TNF-alpha stimulation by promoting the proteasomal degradation of host RELA. Promotes nuclear localization and cleavage of host STAT6 leading to constitutive activation of the IL13/STAT6 signaling pathway to promote viral latency. Interacts with and modulates the histone methyltransferase MLL1 complex activity, leading to its recruitment on viral DNA terminal repeats changing the dynamic of histone H3 methylated 'Lys-4'(H3K4me) profile during the initial hours following infection.
Subcellular location: Host nucleus {ECO:0000269|PubMed:10213686, ECO:0000269|PubMed:10580050, ECO:0000269|PubMed:21697472, ECO:0000269|PubMed:25995248, ECO:0000269|PubMed:27599637, ECO:0000269|PubMed:34850113}. Note=Colocalizes with viral episomes on host chromosomes. {ECO:0000269|PubMed:10213686, ECO:0000269|PubMed:10580050}.
Interaction partners:
Sequence:
MAPPGMRLRSGRSTGAPLTRGSCRKRNRSPERCDLGDDLHLQPRRKHVADSVDGRECGPHTLPIPGSPTVFTSGLPAFVSSPTLPVAPIPSPAPATPLPPPALLPPVTTSSSPIPPSHPVSPGTTDTHSPSPALPPTQSPESSQRPPLSSPTGRPDSSTPMRPPPSQQTTPPHSPTTPPPEPPSKSSPDSLAPSTLRSLRKRRLSSPQGPSTLNPICQSPPVSPPRCDFANRSVYPPWATESPIYVGSSSDGDTPPRQPPTSPISIGSSSPSEGSWGDDTAMLVLLAEIAEEASKNEKECSENNQAGEDNGDNEISKESQVDKDDNDNKDDEEEQETDEEDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEEDEEEDEEEDEEEDEEEEEDEEDDDDEDNEDEEDDEEEDKKEDEEDGGDGNKTLSIQSSQQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQEQQDEQQQDEQQQQDEQEQQEEQEQQEEQQQDEQQQDEQQQDEQQQDEQEQQDEQQQDEQQQQDEQEQQEEQEQQEEQEQQEEQEQQEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQEQELEEVEEQEQEQEEQELEEVEEQEQEQEEQEEQELEEVEEQEEQELEEVEEQEEQELEEVEEQEQQGVEQQEQETVEEPIILHGSSSEDEMEVDYPVVSTHEQIASSPPGDNTPDDDPQPGPSREYRYVLRTSPPHRPGVRMRRVPVTHPKKPHPRYQQPPVPYRQIDDCPAKARPQHIFYRRFLGKDGRRDPKCQWKFAVIFWGNDPYGLKKLSQAFQFGGVKAGPVSCLPHPGPDQSPITYCVYVYCQNKDTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT
Protein: Prepilin leader peptidase/N-methyltransferase [Includes: Leader peptidase (EC 3.4.23.43) (Prepilin peptidase); N-methyltransferase (EC 2.1.1.-)] (P25960)
Organism: Escherichia coli (strain K12)
Function: Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory apparatus.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P22610}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P22610}.
Interaction partners:
- Type II secretion system core protein G
- Putative type II secretion system protein E
- Putative type II secretion system protein F
- Putative type II secretion system protein K
- Putative type II secretion system protein C
- Putative type II secretion system protein L
- Putative type II secretion system protein M
- Type II secretion system protein J
- Putative type II secretion system protein I
- Type II secretion system protein H
Sequence:
MTMLLPLFILVGFIADYFVNAIAYHLSPLEDKTALTFRQVLVHFRQKKYAWHDTVPLILCVAAAIACALAPFTPIVTGALFLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFNAQYGLIDLHDAVYGAVAGYGVLWCVYWGVWLVCHKEGLGYGDFKLLAAAGAWCGWQTLPMILLIASLGGIGYAIVSQLLQRRTITTIAFGPWLALGSMINLGYLAWISY
Protein: Endosialin (Tumor endothelial marker 1) (CD antigen CD248) (Q91V98)
Organism: Mus musculus (Mouse)
Function: May play a role in angiogenesis or vascular function.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Fibronectin
- Collagen alpha-2
- Ubiquitin-associated domain-containing protein 1
- Collagen alpha-1
- GTP-binding protein Rhes
Sequence:
MLLRLLLAWVAAVPALGQVPWTPEPRAACGPSSCYALFPRRRTFLEAWRACRELGGNLATPRTPEEAQRVDSLVGVGPANGLLWIGLQRQARQCQPQRPLRGFIWTTGDQDTAFTNWAQPATEGPCPAQRCAALEASGEHRWLEGSCTLAVDGYLCQFGFEGACPALPLEVGQAGPAVYTTPFNLVSSEFEWLPFGSVAAVQCQAGRGASLLCVKQPSGGVGWSQTGPLCPGTGCGPDNGGCEHECVEEVDGAVSCRCSEGFRLAADGHSCEDPCAQAPCEQQCEPGGPQGYSCHCRLGFRPAEDDPHRCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGISCSPAGAMGAQASQDLRDELLDDGEEGEDEEEPWEDFDGTWTEEQGILWLAPTHPPDFGLPYRPNFPQDGEPQRLHLEPTWPPPLSAPRGPYHSSVVSATRPMVISATRPTLPSAHKTSVISATRPPLSPVHPPAMAPATPPAVFSEHQIPKIKANYPDLPFGHKPGITSATHPARSPPYQPPIISTNYPQVFPPHQAPMSPDTHTITYLPPVPPHLDPGDTTSKAHQHPLLPDAPGIRTQAPQLSVSALQPPLPTNSRSSVHETPVPAANQPPAFPSSPLPPQRPTNQTSSISPTHSYSRAPLVPREGVPSPKSVPQLPSVPSTAAPTALAESGLAGQSQRDDRWLLVALLVPTCVFLVVLLALGIVYCTRCGSHAPNKRITDCYRWVTHAGNKSSTEPMPPRGSLTGVQTCRTSV
Protein: Alanine--glyoxylate aminotransferase (AGT) (SPT) (EC 2.6.1.44) (EC 2.6.1.51) (Serine--pyruvate aminotransferase) (Q6PHK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Threonine aldolase 1
- Phosphoserine phosphatase.
- Novel protein similar to human glyoxylate reductase/hydroxypyruvate reductase
- Glyoxylate reductase/hydroxypyruvate reductase
- Serine hydroxymethyltransferase
- Alanine--glyoxylate aminotransferase 2
- glycine hydroxymethyltransferase
- 4-hydroxy-2-oxoglutarate aldolase, mitochondrial
- Serine dehydratase-like.
- Hydroxyacid oxidase
Sequence:
MMPRTVLSRCARLTQQVPLESALSGKQSVQRGMSSLSVPPPACMLRPLEAPLRYLFGPGPSNVPPRVLAAGGRPIIGHMHSEMFGIMNEIKQGIQYAFQTNNSMTLAMSGSGHTAMECAVFNIVEPGESVLVAVNGIWGERVAEIAERMGAKVHTLAKAPGGHFTNAEIEQALAKHKPVLFFLTHGESSAGLVHPMDGIGDVCRKHNCLLLVDSVASLGAAPLLMDQQKIDILYTGSQKALNAPPGTAPISFNERACQKMFNRKTKPVSYLLDMNYLSNYWGNDGKPDRIYHHTGPVSGFFALRESLAILAETGLENSWRHHTEVAQHLWKGLEDLGLKLFIKDKDLRLPSVTTIAIPEGYNWKELLAYIMKHHQIEFTGGLGPSVGMVLRIGLMGYNCKKTNADKALAALEDGLKQCRKSKA
Protein: Myosin heavy chain 7B (B6RK61)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Myosin light chain 3
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin light chain 4
- Myosin regulatory light chain RLC-A
- Myosin light polypeptide 6
- Myosin regulatory light polypeptide 9
- Myosin regulatory light chain 12B
- Myosin light chain 6B like 1
- Myosin light chain 6B like 1
- Myosin light chain 10
Sequence:
MMDMNELGESACYLRQGYQEMMKVHTVPWDGKKRVWVPDEQDAYVEAEVKTEATGGRVTVETKDQKVLTVRETEMQPMNPPRFDLLEDMAMMTHLNEAAVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTATVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVTTVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFKAGLLGILEELRDQRLAKVLTLLQARSRGRLMRLEYQRMLGGRDALFTIQWNIRAFNAVKNWSWMKLFFKMKPLLRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELNERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEETVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLTDASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLASELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEERADMAETQANKLRARSRDALGPKHKE
Protein: 1-acylglycerol-3-phosphate O-acyltransferase (O53516)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Phosphatidate cytidylyltransferase
- Glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase [NAD
- Putative acyltransferase plsB1
- Diacylglycerol kinase
- Probable CDP-diacylglycerol pyrophosphatase
- Glycerol-3-phosphate dehydrogenase [NAD
- Protein Rv2184c
- Glycerol-3-phosphate dehydrogenase 2
- Glycerol-3-phosphate dehydrogenase 1
Sequence:
MWYYLFKYIFMGPLFTLLGRPKVEGLEYIPSSGPAILASNHLAVADSFYLPLVVRRRIWFLAKSEYFTGTGLKGWINRWFYSVSGQVPIDRTNADSAQGALQTAVVLLGQGKLLGMYPEGTRSPDGRLYKGKTGLARLALHTGVPVIPVAMIGTNVVNPPGRKMLRFGRVTVRFGKPMDFSRFEGLAGNHFIERAVTDEVIYELMGLSGQEYVDIYAASVKDGRNAGGAGANPNSTDAARIPETAAG
Protein: Beta-galactosidase (Q9KGU0)
Organism: Streptococcus pneumoniae
Interaction partners:
Sequence:
MGKGHWNRKRVYSIRKFAVGACSVMIGTCAVLLGGNIAGESVVYADETLITHTAEKPKEEKMIVEEKADKALETKNIVERTEQSEPSSTEAIASEKKEDEAVTPKEEKVSAKPEEKAPRIESQASNQEKPLKEDAKAVTNEEVNQMIEDRKVDFNQNWYFKLNANSKEAIKPDADVSTWKKLDLPYDWSIFNDFDHESPAQNEGGQLNGGEAWYRKTFKLDEKDLKKNVRLTFDGVYMDSQVYVNGQLVGHYPNGYNQFSYDITKYLQKDGRENVIAVHAVNKQPSSRWYSGSGIYRDVTLQVTDKVHVEKNGTTILTPKLEEQQHGKVETHVTSKIVNTDDKDHELVAEYQIVERGGHAVTGLVRTASRTLKAHESTSLDAILEVERPKLWTVLNDKPALYELITRVYRDGQLVDAKKDLFGYRYYHWTPNEGFSLNGERIKFHGVSLHHDHGALGAEENYKAEYRRLKQMKEMGVNSIRTTHNPASEQTLQIAAELGLLVQEEAFDTWYGGKKPYDYGRFFEKDATHPEARKGEKWSDFDLRTMVERGKNNPAIFMWSIGNEIGEANGDAHSLATVKRLVKVIKDVDKTRYVTMGADKFRFGNGSGGHEKIADELDAVGFNYSEDNYKALRAKHPKWLIYGSETSSATRTRGSYYRPERELKHSNGPERNYEQSDYGNDRVGWGKTATASWTFDRDNAGYAGQFIWTGTDYIGEPTPWHNQNQTPVKSSYFGIVDTAGIPKHDFYLYQSQWVSVKKKPMVHLLPHWNWENKELASKVADSEGKIPVRAYSNASSVELFLNGKSLGLKTFNKKQTSDGRTYQEGANANELYLEWKVAYQPGTLEAIARDESGKEIARDKITTAGKPAAVRLIKEDHAIAADGKDLTYIYYEIVDSQGNVVPTANNLVRFQLHGQGQLVGVDNGEQASRERYKAQADGSWIRKAFNGKGVAIVKSTEQAGKFTLTAHSDLLKSNQVTVFTGKKEGQEKTVLGTEVPKVQTIIGEAPEMPTTVPFVYSDGSRAERPVTWSSVDVSKPGIVTVKGMADGREVEARVEVIALKSELPVVKRIAPNTDLNSVDKSVSYVLIDGSVEEYEVDKWEIAEEDKAKLAIPGSRIQATGYLEGQPIHATLVVEEGNPAAPAVPTVTVGGEAVTGLTSQKPMQYRTLAYGAKLPEVTASAKNAAVTVLQASAANGMRASIFIQPKDGGPLQTYAIQFLEEAPKIAHLSLQVEKADSLKEDQTVKLSVRAHYQDGTQAVLPADKVTFSTSGEGEVAIRKGMLELHKPGAVTLNAEYEGAKDQVELTIQANTEKKIAQSIRPVNVVTDLHQEPSLPATVTVEYDKGFPKTHKVTWQAIPKEKLDSYQTFEVLGKVEGIDLEARAKVSVEGIVSVEEVSVTTPIAEAPQLPESVRTYDSNGHVSSAKVAWDAIRPEQYAKEGVFTVNGRLEGTQLTTKLHVRVSAQTEQGANISDQWTGSELPLAFASDSNPSDPVSNVNDKLISYNNQPANRWTNWNRTNPEASVGVLFGDSGILSKRSVDNLSVGFHEDHGVGVPKSYVIEYYVGKTVPTAPKNPSFVGNEDHVFNDSANWKPVTNLKAPAQLKAGEMNHFSFDKVETYAVRIRMVKADNKRGTSITEVQIFAKQVAAAKQGQTRIQVDGKDLANFNPDLTDYYLESVDGKVPAVTASVSNNGLATVVPSVREGEPVRVIAKAENGDILGEYRLHFTKDKSLLSHKPVAAVKQARLLQVGQALELPTKVPVYFTGKDGYETKDLTVEWEEVPAENLTKAGQFTVRGRVLGSNLVAEITVRVTDKLGETLSDNPNYDENSNQAFASATNDIDKNSHDRVDYLNDGDHSENRRWTNWSPTPSSNPEVSAGVIFRENGKIVERTVTQGKVQFFADSGTDAPSKLVLERYVGPEFEVPTYYSNYQAYDADHPFNNPENWEAVPYRADKDIAAGDEINVTFKAIKAKAMRWRMERKADKSGVAMIEMTFLAPSELPQESTQSKILVDGKELADFAENRQDYQITYKGQRPKVSVEENNQVASTVVDSGEDSFPVLVRLVSESGKQVKEYRIHLTKEKPVSEKTVAAVQEDLPKIEFVEKDLAYKTVEKKDSTLYLGETRVEQEGKVGKERIFTAINPDGSKEEKLREVVEVPTDRIVLVGTKPVAQEAKKPQVSEKADTKPIDSSEASQTNKAQLPSTGSAASQAAVAAGLTLLGLSAGLVVTKGKKED
Protein: AB hydrolase superfamily protein C1039.03 (EC 3.-.-.-) (Q9US38)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- S-methyl-5'-thioadenosine phosphorylase
Sequence:
MSQTTTETIIPLDSSVKDKLDPEYVNFYNKYVCSNLPIVKTHTYPVDFLRNNGNVMPGQSELLPVESTEDITIPRKHTKAPSGVPSRIFRPHGTAPEGGWPCFLWFHGGGWVLGNINTENSFATHMCEQAKCVVVNVDYRLAPEDPFPACIDDGWEALLYCYENADTLGINPNKIAVGGSSAGGNIAAVLSHKVAASPANFPPLVLQLLVVPVCDNTANAKTHKSWELFENTPQLPAAKMMWYRRHYLPNEKDWSNPEASPFFYPDSSFKNVCPALICAAGCDVLSSEAIAYNEKLTKAGVESTIKIYEGCPHPVMAMDAVLEKGRILNKDATNALLAAFA
Protein: Peroxisome assembly protein 12 (Peroxin-12) (C8ZEN3)
Organism: Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004585}.
Interaction partners:
Sequence:
MSFYSNLPSAGQSSRGSSTSGRNGVGLEPLYPTIFEIMSSQEIDSLLPASIRYLLANHLVANFPNRYTLRLNKYFFEWFQAIKGFVEWYHLKTYNSTFIDRFYGLQLFSSRDRNLALTQCLNPKGQSEWPQGLQLNQQQKSVIFLEKIILPYITAKLDEILEKISMNNIFSSDETENKWPKRAFLRIYPFIKKLLALSNLLVKLLFLTKRTGSVSLLQYLFKIEYTTVRPLSSELSGLKETKGMDNRLRKTNISSIFALMQGQLSIIPRFLTFMGSQFFPTFIFVLRVYQWWTTQDMTTKLQKRVNDLDEDIPRPPFSSHSDKTEDKEGVSEACPVCEKTVQNPCVLETGYVACYPCAISYLVNNEGHCPVTNKKLLGCTYNKHTNKWEVVTGIRKLLI
Protein: Arabinogalactan protein 1 (OsAGP1) (Q6Z232)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
Subcellular location: Vacuole, aleurone grain membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MARLHLVVVAMAALFAAAAVAQGPSASPTPAPKAQPPVATPPTRPPAVAPVSPPAAQPPVTTPPPVSAPAPVPAPSAAATPSPQASAPTAEPPVLSPPAPAPGSISQSPTEAPTSPPPPSAASGVSPSAAAVVAAWAAVAAVAAFY
Protein: Type II secretion system protein I (T2SS minor pseudopilin I) (Putative general secretion pathway protein I) (Q8VPC3)
Organism: Escherichia coli
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:Q00516}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKRGFTLLEVMLALAIFALSATAVLQIASGALSNQHVLEEKTVAGWVAENQTALLYLMTRGQRAVRQQGESDMAGSRWYWRTTPLSTGNALLQAVDIEVSLHEDFSSVIQSRRAWFSAVGGQQ
Protein: Anthocyanidin reductase (A2IBG2)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MASQIVGTKRACVVGGSGFVASLLVKLLLEKGYAVNTTVRDPDNQKKISHLVTLQELGDLKIFQADLTDEGSFDAPIAGCDLVFHVATPVNFASEDPENDMIKPATQGVVNVLKACAKAKTVKRVVLTSSAAAVSINTLDGTDLVMTEKDWTDIEFLSSAKPPTWGYPASKTLAEKAAWKFAEENNIDLITVIPSLMTGPSLTPIVPSSIGLATSLISGNEFLINALKGMQMLSGSISITHVEDVCRAHVFLAEKESASGRYICSAVNTSVPELAKFLNKRYPDFKVPTDFGDFPSKPKLIISSEKLISEGFSFKYGIEEIYDQTVEYLKSKGLLK
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (P00401)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 COX2 and heme A of COX1 to the active site in COX1, 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 (Probable). COX1 is a catalytic core subunit containing heme A and the active site BNC with heme A3 and the copper atom CU(B).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Multi-pass membrane protein {ECO:0000269|PubMed:30598554}.
Interaction partners:
- Respiratory supercomplex factor 2, mitochondrial
- Cytochrome b
- Cytochrome c oxidase subunit 9, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 7, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
Sequence:
MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNYLLPLMIGATDTAFPRINNIAFWVLPMGLVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTLNMRTNGMTMHKLPLFVWSIFITAFLLLLSLPVLSAGITMLLLDRNFNTSFFEVSGGGDPILYEHLFWFFGHPEVYILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATIHGGSIRLATPMLYAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLNYNEKLAQIQFWLIFIGANVIFFPMHFLGINGMPRRIPDYPDAFAGWNYVASIGSFIATLSLFLFIYILYDQLVNGLNNKVNNKSVIYNKAPDFVESNTIFNLNTVKSSSIEFLLTSPPAVHSFNTPAVQS
Protein: Capsid vertex component 1 (Q6SW50)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04017}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04017}.
Interaction partners:
Sequence:
METHLYSDLAFEARFADDEQLPLHLVLDQEVLSNEEAETLRYVYYRNVDSAGRSAGRVPSGDEDDAPASDDAEDAVGGDRAFDRERRTWQRACFRVLPRPLELLDYLRQSGLTVTLEKEQRVRMFYAVFTTLGLRCPDNRLSGAQTLHLRLVWPDGSYRDWEFLARDLLREEMEANKRDRQHQLATTTNHRRRGGLRNNLDNGSDRRLPEAAVASLETAVSTPFFEIPNGAGTSSANGGGRFSNLEQRVARLLRGDEEFIYHAGPLEPPSKIRGHELVQLRLDVNPDLMYATDPHDRDEVARTDEWKGAGVSRLREVWDVQHRVRLRVLWYVNSFWRSRELSYDDHEVELYRALDAYRARIAVEYVLIRAVRDEIYAVLRRDSGALPQRFACHVPRNMSWRVVWELCRHALALWMDRADVRSCIIKALTPRLSRGAAAAAQRARRQRERSAPKPQELLFGPRNESGPPAERTWYADVVRCVRTQVDLGVEVRAARCPRTGLWIVRDRRGRLRRWLSQPEVCVLYVTPDLDFYWVLPGGFAVSSRVTLHGLAQRALRDRFQNFEAVLARGMHVEAGRQEPETPRVSGRRLPFDDL
Protein: Large ribosomal subunit protein uL3 (60S ribosomal protein L3) (J1 protein) (P27659)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P39023}. Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein uS4
Sequence:
MSHRKFSAPRHGSLGFLPRKRSSRHRGKVKSFPKDDASKPVHLTAFLGYKAGMTHIVREVDRPGSKVNKKEVVEAVTIVETPPMVVVGIVGYVETPRGLRTFKTVFAEHISDECKRRFYKNWHKSKKKAFTKYCKKWQDDTGKKQLEKDFNSMKKYCQVIRIIAHTQMRLLPLRQKKAHLMEIQVNGGTVAEKLDWARERLEQQVPVNQVFGQDEMIDVIGVTKGKGYKGVTSRWHTKKLPRKTHRGLRKVACIGAWHPARVAFSVARAGQKGYHHRTEINKKIYKIGQGYLIKDGKLIKNNASTDYDLSDKSINPLGGFVHYGEVTNDFIMLKGCVVGTKKRVLTLRKSLLVQTKRRALEKIDLKFIDTTSKFGHGRFQTMEEKKAFMGPLKKDRIAKEEGA