wanglab/gogpt-training-data huggingface dataset:
Protein: Apelin receptor (Angiotensin receptor-like 1) (G-protein coupled receptor APJ) (MSR) (Q9WV08)
Organism: Mus musculus (Mouse)
Function: Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone. May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development. Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P35414}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}. Note=After exposure to apelin (APLN) or apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:Q9JHG3}.
Interaction partners:
- Apelin
- Apelin receptor early endogenous ligand
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
Sequence:
MEDDGYNYYGADNQSECDYADWKPSGALIPAIYMLVFLLGTTGNGLVLWTVFRTSREKRRSADIFIASLAVADLTFVVTLPLWATYTYREFDWPFGTFSCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAVPVMVFRSTDASENGTKIQCYMDYSMVATSNSEWAWEVGLGVSSTAVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDIFLMNVFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCDQSGCKGTPHSSSAEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVD
Protein: Probable magnesium transporter NIPA6 (Q8GWX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited to the cell membrane in response to low extracellular magnesium. {ECO:0000250}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CYP21-1
- AT4g38690/F20M13_250
- At4g34930
- AT4g34920/F11I11_160
- At2g21200
- Dirigent protein 15
- PEARLI 4 protein family protein)
- Protein MANNAN SYNTHESIS-RELATED 2
- Protein MANNAN SYNTHESIS-RELATED 1
- Amidophosphoribosyltransferase 3, chloroplastic
Sequence:
METDNGKGLILAVASSVFIGSSFILKKKGLKRAGAIGTRAGYGGYTYLLEPLWWAGMVTMIVGEAANFVAYIYAPAVLVTPLGALSIIISAVLAHFLLKEKLKKMGVLGCVSCIVGSVVIVIHAPKEQTPNSVEEIWNLATQPAFLIYVAITMSIVLALILHFEPLCGQTNILVYIGICSLMGALTVMSIKAIGIAIKLTMEGVSQIGYPQTWLFVMVAVTCVVTQLIYLNKALDTFNAAIVSPVYYVMFTTLTIVASAIMFKDWSGQDAASVASELCGFITVLTGTMILHGTREEEQQQASSEHVRWYDSRKSMNEEHLVSLYSPEY
Protein: Glucose-6-phosphate 1-epimerase (EC 5.1.3.15) (D-hexose-6-phosphate mutarotase) (Q03161)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P).
Interaction partners:
- Glucose-6-phosphate isomerase
- Phosphoglucomutase 2
- Phosphoglucomutase 1
- Phosphoribomutase
- Hexokinase-2
- Putative glucokinase-2
- N-acetylglucosamine kinase
- Glucokinase-1
- Hexokinase-1
- Mitochondrial nuclease
Sequence:
MPIKETDKEVVLTHPADETTSVHILKYGATVYSWKLKSEEQLWLSTAAKLDGSKPVRGGIPLVFPVFGKNSTDEHLSKLPQHGLARNSTWEFLGQTKENPPTVQFGLKPEIANPELTKLWPMDYLLILTVELGSDYLKTAIEVENTSSSKELKFNWLFHTYFRIEDIEGTMVSNLAGMKLYDQLLKESYVDKHPVVTFNQETDVIYQNVSAERAIQIVDKGVQIHTLKRYNLPDTVVWNPWIEKSQGMADFEPKTGYQQMICIEPGHVHDFISLAPGKKWNAYQLLCKEELKYQAIQ
Protein: BBG-LP43 (Q15K31)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRINRYRDLGTLSNHHSNISSISGINASSNIPAATLISSSIKKTSTEAATTKPAAPQIPGKMELLSSNTGTTTTTTTATHHLHQATTTKQLLVQDYLSYASPPTYSRLPPDGHEFPPNFSEPLIMHSHPLKVTTELSYEIQKGGKDESSAPPLPKTGPPATVPRKVYRQDLVINVEPAPSLTRDYQRSLSGGTPRKPSDWRKDEKSEKSVRDKIAMFSSNNELDAIPPAPATAPISSSFTRKPLNRSSENLLDSCSSSSAPSLKTRAMSVENLNDVQRQYQLAK
Protein: Chymotrypsin-like proteinase (Q8VLY7)
Organism: Treponema denticola
Interaction partners:
Sequence:
MKKKILFFLMTIVLIVSSCNFGMNTAVIGNKDNGAVLNGYTGGLGNSSSVELPNGANYKPDDKDIVDGYFIVKTKDGFDKTLFEKKGFIVKGKISLTDTGFTYWYLNKEGNNKKNLLRAASIEGVLSAEHDYKVVEPDGSKAPNQNDGPVDPSNAGTYDLTKGNYLDDPEANNADYGLSITDALRAYSEIGYGTETVVAGIIGTGINMKHKDFKDENGDSIVLYAKSCATAENGTAITPVRPFTEIPIGDNWDKGAHGTHCSGTIAARGNNNIGIAGVAWKNTKLISYQSLNAGLNGQFGGDTWSVYGALLELTNIVEILRKAKADRSLAEIAALPSYLQTTDFQITQKTVPVNMSLGGSYGTEFAFAVLTNAVKHNILPVIAMGNEGRYTAAYPAAFPGVLAVGATNGKDKKVHFSNSGAWISVSAPGDGIKSCGIYGEDDYETMSGTSMATPFVTGTIAYLLSFTGAHDLTPYQIKALLEKTADKVDGATGFTDRLGHGRVNVYKAAKAIKDGNIPAQNDIYTEAEVTVTVKNNDGHSNDIVPCKITLVDEETHAPLAYVAGTGSNPPAFKGLIKGRSYSVYGAFLGSSSQQTFTAQDVDNPITIQFNKKIVWVSTVPNLHYNSGDDDTDTRIMVYKADASGNLDLNTAQSIVDYDQDLLDTTCFEAETGVKYYVLITGFMKGGVFQGGNYALKIDRTPLNPNGCRYRRYGKKSQQS
Protein: MADA (Q2F7Q5)
Organism: Phycomyces blakesleeanus
Interaction partners:
Sequence:
MDSFSSYPQPAEAQKPFPGHQTQFQDVPSHPFFDVVQEQSQQMVSKAGDPQVDFDLQPGTPVPAPTTTAPLSGFYSSSGFDMIGILSRLVNRPNPQINVGPIDMSCSFLVTDARQYDHPIVYCSPTFEHLTGYKGSEILGRNCRFLQAPDGRVTSGSRRQHTDNQAVYHLKAQMLQSNEHQASIINYRKGGQAFVNLITVIPICNEFNEVAFFVGLQVDLVEQPNAILEKMKDGTYLVNYQQMNMVPYIPGANTASEPVDDYFREIPAVASPASEGLNNQEILDLVQCSGENEQQLQQEWNKLLLEHSEDFIHVLSLKGFFLYCSRSSSDLLEHDPEELVGHSLSSICHPSDIVPVMREIKEAAGNSDKVVNLIYRVRRKYSGYMWMECQGKLHVDQSKGRKCLILAGRERPMYSLPRKELMQYGGAGVGSEFWVKASLSGLYLHVSGTSEDVVGYSSDFLVGASIFRYVLDKEVHEITRALASVKKGEICNLEHTMQNNKGQYVSVVSTFYPGDGSSGNKAPEFALIQIRAKDAAVLAAIKSAADDVAMSDMTEEEVAENMFSELETVRGTSWQYELHQLEVANQKLREQLENLSNPKRRKQKKKKASSAPDVQKMCAQCQSKDSPEWRKGPNGPKELCNACGLRYAKSISAKTTAMET
Protein: Nucleoporin NUP188 (hNup188) (Q5SRE5)
Organism: Homo sapiens (Human)
Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (Probable). Required for proper protein transport into the nucleus.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000305|PubMed:32275884}.
Interaction partners:
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup93
- Nucleoporin NUP35
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup88
- Nuclear pore complex protein Nup85
- Nuclear pore membrane glycoprotein 210
- Nucleoporin SEH1
- Nuclear pore complex protein Nup160
Sequence:
MAAAAGGPCVRSSRELWTILLGRSALRELSQIEAELNKHWRRLLEGLSYYKPPSPSSAEKVKANKDVASPLKELGLRISKFLGLDEEQSVQLLQCYLQEDYRGTRDSVKTVLQDERQSQALILKIADYYYEERTCILRCVLHLLTYFQDERHPYRVEYADCVDKLEKELVSKYRQQFEELYKTEAPTWETHGNLMTERQVSRWFVQCLREQSMLLEIIFLYYAYFEMAPSDLLVLTKMFKEQGFGSRQTNRHLVDETMDPFVDRIGYFSALILVEGMDIESLHKCALDDRRELHQFAQDGLICQDMDCLMLTFGDIPHHAPVLLAWALLRHTLNPEETSSVVRKIGGTAIQLNVFQYLTRLLQSLASGGNDCTTSTACMCVYGLLSFVLTSLELHTLGNQQDIIDTACEVLADPSLPELFWGTEPTSGLGIILDSVCGMFPHLLSPLLQLLRALVSGKSTAKKVYSFLDKMSFYNELYKHKPHDVISHEDGTLWRRQTPKLLYPLGGQTNLRIPQGTVGQVMLDDRAYLVRWEYSYSSWTLFTCEIEMLLHVVSTADVIQHCQRVKPIIDLVHKVISTDLSIADCLLPITSRIYMLLQRLTTVISPPVDVIASCVNCLTVLAARNPAKVWTDLRHTGFLPFVAHPVSSLSQMISAEGMNAGGYGNLLMNSEQPQGEYGVTIAFLRLITTLVKGQLGSTQSQGLVPCVMFVLKEMLPSYHKWRYNSHGVREQIGCLILELIHAILNLCHETDLHSSHTPSLQFLCICSLAYTEAGQTVINIMGIGVDTIDMVMAAQPRSDGAEGQGQGQLLIKTVKLAFSVTNNVIRLKPPSNVVSPLEQALSQHGAHGNNLIAVLAKYIYHKHDPALPRLAIQLLKRLATVAPMSVYACLGNDAAAIRDAFLTRLQSKIEDMRIKVMILEFLTVAVETQPGLIELFLNLEVKDGSDGSKEFSLGMWSCLHAVLELIDSQQQDRYWCPPLLHRAAIAFLHALWQDRRDSAMLVLRTKPKFWENLTSPLFGTLSPPSETSEPSILETCALIMKIICLEIYYVVKGSLDQSLKDTLKKFSIEKRFAYWSGYVKSLAVHVAETEGSSCTSLLEYQMLVSAWRMLLIIATTHADIMHLTDSVVRRQLFLDVLDGTKALLLVPASVNCLRLGSMKCTLLLILLRQWKRELGSVDEILGPLTEILEGVLQADQQLMEKTKAKVFSAFITVLQMKEMKVSDIPQYSQLVLNVCETLQEEVIALFDQTRHSLALGSATEDKDSMETDDCSRSRHRDQRDGVCVLGLHLAKELCEVDEDGDSWLQVTRRLPILPTLLTTLEVSLRMKQNLHFTEATLHLLLTLARTQQGATAVAGAGITQSICLPLLSVYQLSTNGTAQTPSASRKSLDAPSWPGVYRLSMSLMEQLLKTLRYNFLPEALDFVGVHQERTLQCLNAVRTVQSLACLEEADHTVGFILQLSNFMKEWHFHLPQLMRDIQVNLGYLCQACTSLLHSRKMLQHYLQNKNGDGLPSAVAQRVQRPPSAASAAPSSSKQPAADTEASEQQALHTVQYGLLKILSKTLAALRHFTPDVCQILLDQSLDLAEYNFLFALSFTTPTFDSEVAPSFGTLLATVNVALNMLGELDKKKEPLTQAVGLSTQAEGTRTLKSLLMFTMENCFYLLISQAMRYLRDPAVHPRDKQRMKQELSSELSTLLSSLSRYFRRGAPSSPATGVLPSPQGKSTSLSKASPESQEPLIQLVQAFVRHMQR
Protein: Insulin-like growth factor (C5J073)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
MEKINSLSTQLVKCCFCDFLKVKMHTVSYIHFFYLGLCLLTLTSSAAAGPETLCGAELVDALQFVCGDRGFYFSKPTGYGSSSRRLHHKGIVDECCFQSCDLRRLEMYCAPIKPPKSARSVRAQRHTDMPKAQKEVHLKNTSRGNTGNRNYRM
Protein: Homeobox protein knotted-1-like 7 (Protein IRREGULAR XYLEM 11) (Protein KNAT7) (Q9FPQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in secondary cell wall biosynthesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription repressor OFP4
- Transcription factor MYB75
- BEL1-like homeodomain protein 6
- Transcription repressor OFP1
- NAC domain-containing protein 73
- Transcription factor MYB63
- Transcription factor MYB46
- Transcription repressor OFP2
- NAC domain-containing protein 10
- NAC domain-containing protein 12
Sequence:
MQEAALGMMGATVGGDGDTAVVAEQNRQLKGEIATHPMYEQLLAAHVACLRVATPIDQLPIIEAQLSQSHHLLRSYASTAVGYHHDRHELDNFLAQYVMVLCSFKEQLQQHVRVHAVEAVMACREIENNLHSLTGATLGEGSGATMSEDEDDLPMDFSSDNSGVDFSGGHDMTGFGPLLPTESERSLMERVRQELKLELKQGFKSRIEDVREEIMRKRRAGKLPGDTTTVLKNWWQQHCKWPYPTEDDKAKLVEETGLQLKQINNWFINQRKRNWHNNSHSLTSLKSKRKH
Protein: Tubulin gamma-2 chain (Gamma-2-tubulin) (P42271)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. Required for oocyte activation and consequently for organization of the female meiotic spindle. Essential for centrosome organization and assembly of biastral mitotic spindles in embryos. Plays a role in stabilizing the augmin complex on the meiotic spindle.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:9155007}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:9155007}. Note=Embryonic mitotic spindle, female meiotic spindle.
Interaction partners:
- Gamma-tubulin complex component 4 homolog
- Gamma-tubulin complex component
- Gamma-tubulin complex component 2 homolog
- Gamma-tubulin complex component 3
- Grip163
- Grip71
- Gamma-tubulin complex component
- Spindle assembly abnormal 4
- Testis-specific gamma-tubulin ring protein 91
- Protein claret segregational
Sequence:
MPSEIITLQLGQCGNQIGFEFWKRLCLEHGISPDGVLEDFATDGQDRKDVFFYQADDNHYIPRAVLIDLEPRVINNIMTSPYSKLYNQENVFLSKHGGGAGNNWASGFSQGEKVQEEVFDILDREADGSDSLEGFVLCHSIAGGTGSGMGSYVLERLSERFPKKLIQTYSVFPNQDEISDVVVQPYNSILTLKRLTKCADSVVVLDNTALNRIATERLHIQTPTFTQINNLVSTIMSLSTTTLRYPSYMNNNLIGLTASLIPTPQLHFLMTGYTPLMSDCETKTSVRKTTVLDVMRRLLQPKNMMVSALTDKQSRQCFVSILNIIQGEVDPSQVHKSLQRIRERKLANFIPWGPASIQVALPRSSPYVQSAHKVSGLMMANHTGISSLFKRALAQYDKLRKRNAFLDNFRRESMFQDDLTELDIARDTVDCLVQEYEAATQIDYPQWSPAVEASKAG
Protein: Uncharacterized protein Rv1738 (P9WLS3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Putative NAD
- Universal stress protein Rv3134c
- Alpha-crystallin
- Hypoxic response protein 1
- Uncharacterized protein Rv3127
- Dormancy associated translation inhibitor
- Putative NAD
- Ferredoxin
- Universal stress protein Rv2623
- Probable nitrate/nitrite transporter NarK2
Sequence:
MCGDQSDHVLQHWTVDISIDEHEGLTRAKARLRWREKELVGVGLARLNPADRNVPEIGDELSVARALSDLGKRMLKVSTHDIEAVTHQPARLLY
Protein: Peptide deformylase 1A, chloroplastic/mitochondrial (AtDEF1) (AtPDF1A) (PDF 1A) (EC 3.5.1.88) (Polypeptide deformylase) (Q9FV53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
Subcellular location: Plastid, chloroplast stroma. Mitochondrion. Note=Reported to be localized to mitochondria, based on transient GFP expression in a heterologous system (PubMed:11060042), but also shown to be imported and correctly processed in isolated chloroplast (PubMed:11553738). {ECO:0000269|PubMed:11060042, ECO:0000269|PubMed:11553738}.
Interaction partners:
- Trigger factor-like protein TIG, Chloroplastic
- Methionine aminopeptidase 1A
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Large ribosomal subunit protein bL28c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Methionine aminopeptidase 1D, chloroplastic/mitochondrial
- Methionine aminopeptidase 1C, chloroplastic/mitochondrial
- Large ribosomal subunit protein bL21c
- 50S ribosomal protein L33
- Large ribosomal subunit protein bL21m
Sequence:
MGLHRDEATAMETLFRVSLRLLPVSAAVTCRSIRFPVSRPGSSHLLNRKLYNLPTSSSSSLSTKAGWLLGLGEKKKKVDLPEIVASGDPVLHEKAREVDPGEIGSERIQKIIDDMIKVMRLAPGVGLAAPQIGVPLRIIVLEDTKEYISYAPKEEILAQERRHFDLMVMVNPVLKERSNKKALFFEGCLSVDGFRAAVERYLEVVVTGYDRQGKRIEVNASGWQARILQHECDHLDGNLYVDKMVPRTFRTVDNLDLPLAEGCPKLGPQ
Protein: Acidic leucine-rich nuclear phosphoprotein 32 family member E (LANP-like protein) (LANP-L) (Q9BTT0)
Organism: Homo sapiens (Human)
Function: Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1 from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state. Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Histone H2A.Z
- E1A-binding protein p400
- Histone acetyltransferase KAT5
- Transformation/transcription domain-associated protein
- Bromodomain-containing protein 8
- RuvB-like 1
- Histone H2B type 1-J
- Inhibitor of growth protein 3
- RuvB-like 2
- Actin-like protein 6A
Sequence:
MEMKKKINLELRNRSPEEVTELVLDNCLCVNGEIEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYRESIFELLQQITYLDGFDQEDNEAPDSEEEDDEDGDEDDEEEEENEAGPPEGYEEEEEEEEEEDEDEDEDEDEAGSELGEGEEEVGLSYLMKEEIQDEEDDDDYVEEGEEEEEEEEGGLRGEKRKRDAEDDGEEEDD
Protein: Calcium binding protein 39 (A0A8I5Y8Z7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDIASDAFATFKVTFKNLNSKHIYKSDCFPIFFFSEYEKLLHSENYVTKRQSLKLLGELLLDRHNFTIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQTKLIEFLSKFQNDRTEDEQFNDEKTYLVKQIRDLKRAAQQEA
Protein: Structural maintenance of chromosomes protein (Q389U3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
Interaction partners:
- Structural maintenance of chromosomes protein
- Condensin complex subunit 2
- Condensin subunit 1, putative
- Nuclear condensin complex subunit 3 C-terminal domain-containing protein
- SCD domain-containing protein
- Double-strand-break repair protein rad21 homolog, putative
- DNA polymerase eta
- Structural maintenance of chromosomes protein
- Sister chromatid cohesion protein
- RNA-binding protein
Sequence:
MRVKSIVIDGFKSYAHRKVIDDLSPHFNAITGLNGSGKSNIFDAICFVMGITNLKRVRAEDPRELIFRAGTTGVHAARVTIEFINDDPRTAPPGYSCEEYPTITVGRQIKLGGKQQFFLNNTVSVQSKVKRFFESISLNVDNPHFMVLQGTVHKLIGMRSEDILSLIEEAVGTKAFDHRRRTAESLIRSKEKKMEEIDANLETQIGPMLRAMKADQEEYERYVQLSEGIEEMRKFRIAFEYEEHRKRRGELSTRRTSLLSDTAAAKEQLRSFPSVEDETTQRLMQLQSTLAAPAEAAMALHEEESTLKLQLAREEAQLERLDKVLKKLADASRKLEEEKQQQKSRAQQFEAYQEQREKLIRNIHEQKENIAKLKRSLQLNGSGVRAGASGMSLEEERADIERQVIKSSAEARRREERIRELEHQQKSVAEKSEARERTVIRLRNELRSAQDCLDSVTKRYINVKPLEEQARALQEEVARLKAEHWKANDAMLRESAQGGGSGGRGLDLEYDRRACAGIEQYIWGRVVELVSPQEEKYAIALTVGAQSQLMRVVVTSDIVAERIIRHGLRQRTAFLPLNTLTQPKSISDSQLEEAKRMANRMNGFVAVAKDLTVVKDEAHRVIADYVFGNFFICSTLELAQELAYGSAVRCKAVTLDGEVVEPKGLMTGGSKKHIRNVFADVLIYKKRKAPVEALRVTMEKREKELEGLHAQLREHRSLIQEHAKAEEAVSIATHKLQLVENEEEGLSKELQASLKEERQKYEALTTMLNDLQERRARLEKYANLDSDKVRKDLQEQLSAAQKRCAALVHEEESGSAEFERVEAEMTQTAADIEQKLVEVHEQIHQQTKARDEASKSFESTSKSLQEVVDKRCRAEEQRQNIEKEIEETQQELQQLVVKKASLEGFVKNAEVDVREISKSLEELQKLISEAERRNTWIEEKQHLFGPRDGPFYFEDRERTQETLAELREAEVNASTMSKRLNKKALILYEERKKEYDELVQQRSVLGEDRDAIQQCILGIEDKKWRALDRMVEVVSNVFSKLFSTCLPGAAAVLREERNEHGHLSGLQVKVLFNGKERESLSELSGGQRSLLALCLILAILRVRQAPMYILDEVDAALDPSHTQGIGNMLQKHFPSSQFLLVSLKDGMFSNADVLYQVSNTQGYSEITRIQSNRSR
Protein: Ubiquitin carboxyl-terminal hydrolase 5 (EC 3.4.19.12) (Deubiquitinating enzyme 5) (AtUBP5) (Ubiquitin thioesterase 5) (Ubiquitin-specific-processing protease 5) (O22207)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
Interaction partners:
- Plant/protein
- Ubiquitin-like superfamily protein
- Eukaryotic translation initiation factor 6-1
- Proteasome subunit beta type-3-B
- E3 ubiquitin-protein ligase RKP
- Ubiquitin-like protein 5
- Proteasome subunit alpha type-5-A
- Proteasome subunit alpha type-7-B
Sequence:
MAEVSMGSSSSSTDLSPEEERVFIRDIAIAAEANSKEGDTFYLITQRWWQEWIEYVNQDQPCNTNDGSSLSEHCDSPGSSTLKKPSRIDNSDLIYDSSLEDPSNTSEIIETLQEGRDYVLLPQEVWNQLRSWYGGGPTLARRVISSGLSQTELAVEVYPLRLQLLLMPKSDHSAIRISKKETIRELHRRACEIFDLDSEHVRIWDYYGHQKYSLMNDLDKTLDDANLQMDQDILVEVLDINGTLSSAHIQSAQENGLVDGDSTSILIEPSKSSLAAAGGFSSSRNAFRTGSVEVSQSFDNTYSSTGVTTRGSTAGLTGLLNLGNTCFMNSAIQCLVHTPEFASYFQEDYHQEINWQNPLGMVGELALAFGDLLRKLWAPGRTPIAPRPFKAKLARFAPQFSGYNQHDSQELLAFLLDGLHEDLNRVKHKPYINSRDADGRPDEEVADEFWKNHIARNDSIIVDVCQGQYKSTLVCPICNKVSVTFDPFMYLSLPLQFNTTRAITVTVFSCDKTALPSTITVNVSKQGRCRDLIQALTNACSLKQSEELKLAEIRNNFIHRLFEDPLIPLSSIKDDDHLAAYKLSKSSENTTLLRLVLRRRDQKAGERESTVQLKPCGTPLLSSASCGDALTKGKIHCLVQNMLSPFRREESVGKKGNSDSSIPERRSARFNNTEEEDKVGGLKKAKKSNSSDLGASKLSLQLIDEDNKTINLPDNEAEAMKLPSSATVTIYLDWTPELSGMYDITCLESLPEVLKYGPTTKKARSEPLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYSRSMKHKLETFVNFPIHDLDLTKYVANKNLSQPQLYELYALTNHYGGMGSGHYTAHIKLLDDSRWYNFDDSHISHINEDDVKSGAAYVLFYRRKSDAGGKMT
Protein: Envelope glycoprotein (GP1,2) (GP) [Cleaved into: GP1; GP2; Shed GP (GP1,2-delta)] (P87666)
Organism: Zaire ebolavirus (strain Kikwit-95) (ZEBOV) (Zaire Ebola virus)
Function: Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, down-regulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion. Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1. This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes. Down-regulates as well the function of host natural killer cells. Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells. However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation.
Subcellular location: [GP2]: Virion membrane {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein {ECO:0000255}. Note=In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site. {ECO:0000250|UniProtKB:Q05320}.; SUBCELLULAR LOCATION: [GP1]: Virion membrane {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05320}. Host cell membrane {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05320}. Note=GP1 is not anchored to the viral envelope, but forms a disulfid-linked complex with the extravirion surface GP2. In the cell, both GP1 and GP2 localize to the plasma membrane lipid rafts, which probably represent the assembly and budding site. GP1 can also be shed after proteolytic processing. {ECO:0000250|UniProtKB:Q05320}.; SUBCELLULAR LOCATION: [Shed GP]: Secreted {ECO:0000250|UniProtKB:Q05320}. Note=GP2-delta bound to GP1 (GP1,2-delta) is produced by proteolytic cleavage of GP1,2 by host ADAM17 and shed by the virus. {ECO:0000250|UniProtKB:Q05320}.
Interaction partners:
Sequence:
MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTAVSNRAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSPQPPTTKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNDSTASDTPPATTAAGPLKAENTNTSKGTDLLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRARREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYTEGLMHNQDGLICGLRQLANETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF
Protein: Splicing factor 45 (RNA-binding motif protein 17) (Q7PL81)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR031066}.
Interaction partners:
Sequence:
MVFGNKNVTDPAGSKNGCQKTNPEVTCFAPITTVVSKPLISGKALPSILERINRGDWDVADEYDPQRPNEYEKLKEKSNGSDKNRAGVSDREDRDDKEKDRKRGRVGRREFYRDEVSAPNLKLSGFGHRQNDDDMYLPSPGLVAKQGGATIAPPPSLQEMSIDSGCEATNTMPYSASSVAAKIMAKYGFKDGQGLGKSEQGMAIALQVEKTSKRGGRIIHEKDVFLPPLALSPPSIGSQIGTSPSHKAMPPPQMVDTAAESGDIGYSITEIMKSPSKVVLLRNMVGPGDVDEELEPEVKDECNTKYGEVNSVIIHESFGTVPEDAVKIFVEFRRIESAIKAVVDLNGRFFGGRQVRAGFYNYDKFKCFQLH
Protein: Connector protein (Q37995)
Organism: Streptococcus phage Cp-1 (Bacteriophage Cp-1)
Interaction partners:
Sequence:
MSYKNYKRHLGKIELNKETVERNRLAFFEFYFNYFYNIVVNYFTWEGLPNDIDELFIEKKLIENGHVAFFHDDTFGYIAQGGTRGERLNHYDQPLTYQPVNASSMNYFKQMEIAYTENDFRVIEELHKDNPDKIKRPCIVIPNNNFYEPYIGYLELFCEKLADIELTIQLNRNAQITPYFIFADNTNVLSMKNIFNKIANFEPVVYLNKQKDQDGQDSFKQLSDYIQVFRTDAPFLLDKLHDEKLRVMNQLLTFIGINNNPSDKKERLVVSEAISNNGVISANIEVGWKSRRKFVELINKCYGLEISVKPAETIQQFNLDKVALDLAEKEGTIIDPE
Protein: Vitelline membrane-like protein (A8JUV4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000269|PubMed:19540119}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:19540119}. Note=Secreted into the perivitelline space by follicle cells and becomes incorporated into the vitelline membrane. {ECO:0000269|PubMed:19540119}.
Interaction partners:
- IP19021p
- Vitelline membrane protein Vm32E
- Defective chorion protein, FC177 isoform
- Vitelline membrane protein Vm34Ca
Sequence:
MCGRRLLFLAAFGCLLANAFSLPATRNEEFDDGFPESEFDYEERHTREIPAQAYAPPIVYNSQSSYSPAKDQGYSAPAAPVYSPAAPSYSAPAAPSYSAPAAPSYSAPAAPSYSAPAAPSYSAPAAPSYSAPASSSYSAPAAPSYSAPAAPSYSAPAAPSYSAPASSSYSAPAAPSYSAPAAPSYSAPAAPSYSAPAAPSYSAPAAPSYSAPAAPSYSAPSAPSYSAQKTSSYSAPAAPSYHAPAAPASSYSAPAGPSYSAPAAPSYSAPSYSAPASSYSALKAPSYSAPAAPSYSAPAAPSYSSSASPSYSSPASSSYSAPAAPTYSAPKAQSYSAPAAPSYSAPAAPSYSAPASSSYSAPAAPSYSAPAAPSYSAPAAPSYSAPASSSYSAPAAPSYSAPAAPSYSAPASSSYSAPAAPSYSAPAAPSYSAPAAPSYSAPAAPSYSAPASSGYSAARAYSAGSAAPASGYSAPKTSSGYSAPASSGSPAASSYSAPASSTASSGYSAPASKSSGYARSEMDHQILGMARTAGGYGSAAPSAAYGAASLPSPPCPKNYVFSCSSVFTPAPCSQGYGY