wanglab/gogpt-training-data huggingface dataset:
Protein: phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) (H0YML5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSPADFQRAVDERFPGCMQGRTMYVLPFSMGPVGSPLSRIGVQLTDSAYVVASMRIMTRLGTPVLQALGDGDFVKCLHSVGQPLTGQGEPVSQWPCNPEKTLIGHVPDQREIISFGSGYGGNSLLGKKCFALRIASRLARDEGWLAEHMLILGITSPAGKKRYVAAAFPSACGKTNLAMMRPALPGWKVECVGDDIAWMRFDSEGRLRAINPENGFFGVAPGTSATTNPNAMATIQSNTIFTNVAETSDGGVYWEGIDQPLPPGVTVTSWLGKPWKPGDKEPCAHPNSRFCAPARQCPIMDPAWEAPEGVPIDAIIFGGRRPKGKIIMHDPFAMRPFFGYNFGHYLEHWLSMEGRKGAQLPRIFHVNWFRRDEAGHFLWPGFGENARVLDWICRRLEGEDSARETPIGLVPKEGALDLSGLRAIDTTQLFSLPKDFWEQEVRDIRSYLTEQVNQDLPKEVLAELEALERRVHKM
Protein: Pre-mRNA-splicing factor SLU7 (Synthetic lethal with U2 snRNA protein 17) (Synthetic lethal with U5 snRNA protein 7) (Q02775)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential protein involved in the second catalytic step of pre-mRNA splicing. Involved in the selection of 3'-type splice sites; this selection could be done via a 3'-splice site-binding factor, PRP16.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22
- Pre-mRNA-splicing factor BUD31
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor 8
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing factor 18
- Pre-mRNA-splicing factor CWC22
- Pre-mRNA-splicing factor CWC2
Sequence:
MNNNSRNNENRSTINRNKRQLQQAKEKNENIHIPRYIRNQPWYYKDTPKEQEGKKPGNDDTSTAEGGEKSDYLVHHRQKAKGGALDIDNNSEPKIGMGIKDEFKLIRPQKMSVRDSHSLSFCRNCGEAGHKEKDCMEKPRKMQKLVPDLNSQKNNGTVLVRATDDDWDSRKDRWYGYSGKEYNELISKWERDKRNKIKGKDKSQTDETLWDTDEEIELMKLELYKDSVGSLKKDDADNSQLYRTSTRLREDKAAYLNDINSTESNYDPKSRLYKTETLGAVDEKSKMFRRHLTGEGLKLNELNQFARSHAKEMGIRDEIEDKEKVQHVLVANPTKYEYLKKKREQEETKQPKIVSIGDLEARKVDGTKQSEEQRNHLKDLYG
Protein: Aldehyde dehydrogenase, dimeric NADP-preferring (EC 1.2.1.5) (ALDHIII) (Aldehyde dehydrogenase 3) (Aldehyde dehydrogenase family 3 member A1) (P30838)
Organism: Homo sapiens (Human)
Function: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids. Preferentially oxidizes aromatic aldehyde substrates. Comprises about 50 percent of corneal epithelial soluble proteins (By similarity). May play a role in preventing corneal damage caused by ultraviolet light (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47739}.
Interaction partners:
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Catechol O-methyltransferase
- Acetyl-coenzyme A synthetase, cytoplasmic
- 4-aminobutyrate aminotransferase, mitochondrial
- Aldo-keto reductase family 1 member A1
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Cytochrome P450 2E1
- Transmembrane O-methyltransferase
- Amine oxidase [copper-containing] 2
Sequence:
MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPPSPAKMTQH
Protein: CKLF-like MARVEL transmembrane domain-containing protein 5 (Chemokine-like factor superfamily member 5) (Q9D6G9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Chemokine-like factor
- CKLF-like MARVEL transmembrane domain-containing protein 8
- CKLF-like MARVEL transmembrane domain-containing protein 6
- CKLF-like MARVEL transmembrane domain-containing protein 7
- CKLF-like MARVEL transmembrane domain containing 1
Sequence:
MFSAWDRRERPPEEGAAAGLQGFGVDKTFLSSLKGILLETELALTFIIFICFTASISAYMAAALLEFLITLAFLFLCATQYYQRFDRLNWPCLDFLRCLSAIVIFLVVSFAAVTSREGAAIAAFVFGIILVSVFAYDAFKIYRTELMPSTTEGDQQ
Protein: Gb|AAF24581.1 (Lactoylglutathione lyase / glyoxalase I family protein) (Q9FFR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g57040
- At2g32090/F22D22.16
- Expressed protein
- Probable lactoylglutathione lyase, chloroplastic
- Glyoxylase I 4
Sequence:
MATASFRWILQLHRDVPKAARFYAQGLDFSVNVVTLRWAELHSGPIKLALMQSPSNHVAEKGYSSLLSFTVTDINTTVTKLMALGAELDGTIKYEIHGKVAAMKCPDGYMLGLYEAA
Protein: Mdm2 (A7UKY0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSE
Protein: EFR3 homolog A (A0A1B0GUZ7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKDYVQVPAAELEKPYEFTSTRESPTFLYLRVCCCCSALRPRYKRLVDNIFPEDPKDGLVKTDMEKLTFYAVSAPEKLDRIGSYLAERLSRDVVRHRSGYVLIAMEALDQLLMACHSQSIKPFVESFLHMVAKLLESGEPKLQVLGTNSFVKFANIEEDTPSYHRRYDFFVSRFSAMCHSCHSDPEIRTEIRIAGIRGIQGVVRKTVNDELRATIWEPQHMDKIVPSLLFNMQKIEEVDSRIGPPSSPSATDKEENPAVLAENCFRELLGRATFGNMNNAVRPVFAHLDHHKLWDPNEFAVHCFKIIMYSIQAQYSHHVIQEILGHLDARKKDAPRVRAGIIQVLLEAVAIAAKGSIGPTVLEVFNTLLKHLRLSVEFEANDLQGGSVGSVNLNTSSKDNDEKIVQNAIIQTIGFFGSNLPDYQRSEIMMFIMGKVPVFGTSTHTLDISQLGDLGTRRIQIMLLRSLLMVTSGYKAKTIVTALPGSFLDPLLSPSLMEDYELRQLVLEVMHNLMDRHDNRAKLRGIRIIPDVADLKIKREKICRQDTSFMKKNGQQLYRHIYLGCKEEDNVQKNYELLYTSLALITIELANEEVVIDLIRLAIALQDSAIINEDNLPMFHRCGIMALVAAYLNFVSQMIAVPAFCQHVSKVIEIRTMEAPYFLPEHIFRDKCMLPKSLEKHEKDLYFLTNKIAESLGGSGYSVERLSVPYVPQVTDEDRLSRRKSIVDTVSIQVDILSNNVPSDDVVSNTEEITFEALKKAIDTSGMEEQEKEKRRLVIEKFQKAPFEEIAAQCESKANLLHDRLAQILELTIRPPPSPSGTLTITSGHAQYQSVPVYEMKFPDLCVY
Protein: Geraniol synthase Tps-5031G8, chloroplastic (PsTps-5031G) (EC 3.1.7.11) (C0KWV4)
Organism: Perilla frutescens var. hirtella (Perilla citriodora) (Perilla setoyensis)
Function: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into geraniol.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MCSISQKVVIGLNKAAANNCLQNLDRRGFKTRRVSSSEAASCLRASSSLQLDVKPVEEGRRSGNYQPSIWDFNYVQSLNTPYKEERYLTRHAELIVQVKPLLEKKMEATQQLELIDDLNNLGLSYFFQDRIKQILSFIYDENQCFHSNINDQAEKRDLYFTALGFRLLRQHGFNVSQEVFDCFKNDKGSDFKASLSGNTKGLLQLYEASFLVREGEDTLELARQFATKFLRRKLDEIDDNHLLSRIHHSLEIPLHWRIQRLEARWFLDAYATRHDMNPIILELAKLDFNIIQATHQEELKDVSRWWQNTRLAEKLPFVRDRLVESYFWAIALFEPHQYGYQRRVAAKIITLATSIDDVYDIYGTLDELQLFTDNFRRWDTESLGGLPYSMQLFYMVIHNFVSELAYEILKEKGFIAIPYLQRSWVDLAESFLKEANWYYSGYTPSLEEYIDNGSISIGAVAVLSQVYFTLANSIEKPKIESMYKYHHILRLSGLLVRLHDDLGTSLFEKKRGDVPKAVEICMKERNDTEEEAEEHVKYLIREAWKEMNTATAAAGCPFMDELNVAAANLGRAAQFVYLDGDGHGVQHSKIHQQMGGLMFKPYV
Protein: Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (hLHPP) (EC 3.1.3.-) (EC 3.6.1.1) (Q9H008)
Organism: Homo sapiens (Human)
Function: Phosphatase that hydrolyzes imidodiphosphate, 3-phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16430861}. Nucleus {ECO:0000269|PubMed:16430861}.
Interaction partners:
- Inorganic pyrophosphatase
- Inorganic pyrophosphatase 2, mitochondrial
- Potassium-transporting ATPase alpha chain 2
- Potassium-transporting ATPase alpha chain 1
- Potassium-transporting ATPase subunit beta
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- V-type proton ATPase 116 kDa subunit a 4
- ATP synthase F
- V-type proton ATPase 116 kDa subunit a 2
Sequence:
MAPWGKRLAGVRGVLLDISGVLYDSGAGGGTAIAGSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILKEQGLRPYLLIHDGVRSEFDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLMELEKPVLISLGKGRYYKETSGLMLDVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQAVMIGDDIVGDVGGAQRCGMRALQVRTGKFRPSDEHHPEVKADGYVDNLAEAVDLLLQHADK
Protein: Ferredoxin (B1P759)
Organism: Zea mays (Maize)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|RuleBase:RU364001}.
Interaction partners:
- Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Ribosomal protein L19
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- Histone H2B
- Abscisic acid stress ripening2
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit IV A
Sequence:
MATVLGSPRAPAFFFSPSSLRAAPAPTAVALPAAKVGIMGRSASSRGRLRAQATYNVKLITPEGEVELQVPDDVYILDQAEEDGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSYLDDGQIAAGWVLTCHAYPTSDVVIETHKEEELTGA
Protein: Proline--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.15) (Prolyl-tRNA Synthetase 1) (PRORS1) (Prolyl-tRNA synthetase) (ProRS) (Protein OVULE ABORTION 6) (Q9FYR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16251277}. Mitochondrion {ECO:0000269|PubMed:16251277}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
- ATP binding / aminoacyl-tRNA ligase/ nucleotide binding protein
- Leucine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, chloroplastic/mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MVSSSLRLPSLTSLLFPATTRYPATLRRTVCLRNRPLSGFATAPSGTASPETKSSEVDRLRSDRAVTPRSQDFNAWYLDVIASAELADYGPVRGTMVIRPYGYAIWEAIQDYLNVKFKETGHSNMYFPQFIPYSFIEKEASHVEGFSPELALVTVGGGKELEEKLVVRPTSETIVNHMFTQWIHSYRDLPLMINQWANVTRWEMRTKPFIRTLEFLWQEGHTAHATPEEAEKEAKQMIEIYTRFAFEQTAIPVIPGRKSKLETFAGADITYTIEAMMGDRKALQAGTSHNLGQNFSRAFGTQFADENGERQHVWQTSWAVSTRFVGGIIMTHGDDTGLMLPPKIAPIQVVIVPIWKKDTEKTGVLSAASSVKEALQTAGVRVKLDDTDQRTPGWKFNFWEMKGIPLRIEIGPRDVSSNSVVVSRRDVPGKAGKVFGISMEPSTLVAYVKEKLDEIQTSLLEKALSFRDSNIVDVNSYAELKDAISSGKWARGPWSASDADEQRVKEETGATIRCFPFEQTQGTKTCLMTGNPAEEVAIFAKSY
Protein: D-lactate dehydrogenase (cytochrome) (EC 1.1.2.4) (Q7TPJ4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- L-lactate dehydrogenase B chain
- L-lactate dehydrogenase C chain
- Pyruvate kinase PKM
- Pyruvate kinase PKLR
- L-lactate dehydrogenase A chain
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Hydroxyacylglutathione hydrolase, mitochondrial
- Malic enzyme
- NADP-dependent malic enzyme
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Sequence:
MPGIWSSEQQEALSQQGHVCGFCCLSYDPCTVSPLQGGLSQDFVEALKAVVGSPHVSTASAVRQHHGHDESMHRCRPPDAVVWPQNVDQVSRLASLCYNQGVPIIPFGTGTGVEGGVCAVQGGVCISLTHMDQIMELNTEDFSVVVEPGVTRKALNTHLRNSGLWFPVDPGADASLCGMAATGASGTNAVRYGTMRDNVINLEVVLPDGRLLHTAGRGRHYRKSAAGYNLTGLFVGSEGTLGIITSATLRLHPAPEATVAATCAFPSVQAAVDSTVQILQAAVPVARIEFLDEVMMDACNRHSKLNCPVAPTLFLEFHGSQQALAEQLQRTEAITQDNGGSHFSWAKEAEKRNELWAARHNAWYAALALRPGRVIVGHVGDGNFHCILLVNPDDVEEQRRVKAFAENLGRRALALHGTCTGEHGIGLGKRQLLQEEVGPVGVETMRQLKDTLDPRVSSEKRRMKRKKRKEEEEEEEKEEEEEKDNDDGVKGDHAAAASFLH
Protein: Putrescine hydroxycinnamoyltransferase 3 (OsPHT3) (EC 2.3.1.-) (Q7XXN5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to putrescine, to produce coumaroyl putrescine. Can use feruloyl-CoA and caffeoyl-CoA as acyl donors.
Interaction partners:
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- 4-coumarate--CoA ligase
Sequence:
MEVKVLSSKLVKPAYNGGVAAAPDVEYIPLSIFDKVTYKMQMAIIYAFPPPAPSTAAIEKGLAAVLAQYRAFAGQLGESPDGEAAVVLNDRGARLVEAAVDADLVDMAPAKPTPELLRLHPDLEGELQEVVLLQLTRFRCGSLAVGFTSNHVVADGHATSNFLVAWGRATRGLPMGAPPVHHHAALFKPRPSPHVEHDHRNREYYLPAAGDDSHGHGDGGAADNIVIHKAHFTKDFIAGLRAAASEGRGRPFSRFETILAHLWRTMTRARGLSPDEASTIRLSVDGRHRLGAPAEYFGNLVLWAFPRATVGDLLTRPLKHAAQVIHDEVARVDGAYFRSFLDFALSGAGGDKEGLAPSAVLKDVLCPNAEVDSWLTFPFYELDFGTGSPTYFMPSYFPTEGMLFLVPSYLGDGSVDAFVPVFNHNLEAFKECCYSME
Protein: Side tail fiber protein pb1 (STF-pb1) (EC 3.4.21.-) (LTF-pb1) (Tail protein pb1) [Cleaved into: Mature tail spike protein; Intramolecular chaperone] (P13390)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Assembles together with p132 to form the three L-shaped long tail fibers and the collar structure at the junction between the tail tube and the conical tail tip. The three L-shaped long tail fibers recognize the host lipopolysaccharides that serve as adhesion receptor for virus entry. Each fiber consists of a thin proximal rod of about 30 nm connected by a hinge to a thicker distal part of about 47 nm.
Subcellular location: Virion {ECO:0000269|PubMed:24198424}. Note=Component of the tail. Forms the L-shaped side fibers and are anchored onto the p132 dodecameric ring. {ECO:0000269|PubMed:24198424}.
Interaction partners:
Sequence:
MAITKIILQQMVTMDQNSITASKYPKYTVVLSNSISSITAADVTSAIESSKASGPAAKQSEINAKQSELNAKDSENEAEISATSSQQSATQSASSATASANSAKAAKTSETNANNSKNAAKTSETNAASSASSASSFATAAENSARAAKTSETNAGNSAQAADASKTAAANSATAAKTSETNAKKSETAAKTSETNAKTSENKAKEYLDMASELVSPVTQYDWPVGTNNNSVYVKIAKLTDPGAVSCHLTLMITNGGNYGSSYGNIDFVEISARGLNDARGVTSENITKFLSVRRLGSPNLAWDNQLRYGLVEGDGYFEVWCYQRAFIKETRVAVLAQTGRTELYIPEGFVSQDTQPSGFIESLAARIYDQVNKPTKADLGLENAMLVGAFGLGGNGLSYSSVQSNVDLINKLKANGGQYWRAARESGANVDINDHGSGFYSHCGDTHAAINVQYNTGIVKVLATTDRNLASDIVYANTLYGTANKPSKSDVGLGNVTNDAQVKKAGDVMSGDLDIRKETPSIRLKSTQGNAHLWFMNNDGGERGVIWSPPNNGSLGEIHIRAKTSDGTSTGDFIVRHDGRIEAKDAKISYKISSRTAEFSNDDTNTAATNLRVSGKQHTPIMLVRDSDSNVSVGFKLNNMNAKLLGIDIDGDLAFGENPDHKQNSKIVTRKMMDAGFSVAGLMDFTNGFAGPWEAKNISDQELDLNSLMIKKSDPGSIRVYQCVSAGGGNNITNKPSGIGGNFILYVESIRKVGDTDFTNRQRLFGTDLNREFTRYCSNGTWSAWRESVVSGMNQDVSVKSMSVSGRLSGNELSVGGAGVLNGNLGVGGGATSKMPSSDKGIVIGRGSIVREGGEGRLILSSSGGTDRLLQLRPAGATSLDNQVEISCTSASAGDTKISFGQGAAIRCNNAGSPIISAKAGQMIYFRPNGDGISEGQMILSPNGDLVVKGGVNSKEIDVTASQSLPLKETTATTGIGVNFIGDSATECSFGIENTAGGSAVFHNYTRGASNSVTKNNQLLGGYGSRPWLGSTYTEHSNAALHFLGAGDTSATNHGGWIRLLVTPKGKTISDRVPAFRLSDNGDLWLVPDGAMHSDLGLVRSIETLNAAVPRFNAPSIQDGRGLKIVAPQAPEIDLIAPRGSGASAPAIRAMWCDGSLADTTRYIGATQPGSTFYIGASGHDGEKFDSMRGSVAIKSAGGWGPTSTPTQVVLETCESGSISRLPRWGVDHNGTLMPMADNRYNLGWGSGRVKQVYAVNGTINTSDARLKNDVRAMSDPETEAAKAIAKEIGFWTWKEQADMNDIREHCGLTVQRAIEIMESFGLDPFKYGFICYDKWDEHTVVSEYGPANEDGTENPIYKTIPAGDHYSFRLEELNLFIAKGFEARLSAIEDKLGM
Protein: BICP4 (Q06635)
Organism: bovine alphaherpesvirus 1
Subcellular location: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
Interaction partners:
Sequence:
MSSPGRLELATLDLYDLIESADLGPTGGSEEDPALLDAARRAEARERRRAARAELAELWRMVGGEDAESSEDDGAGDAGATEGAEAEDAEIGEDAGARDAGGAEDADVAECAEAEGAEGAEDADSAWAAARALAVAVEAAAAGAEAAAAEAAVIAAAIEAEAGAAPLKAEAGTEAGGGGALGARTEAGDVGPEDCSDAGSEDSGPEDCSDAGPEDDGGEAREGSTDADAEAEAEAEAGTGAGTRTKAAPREAGAGPGAPRGRAPGPPAPSPPETAPPPPRRQRGRATGARAGYAAAPRDGPPPLEGPLLTPSGEAWPGSAPPPPGRVRFGGAGDTREGLWDCPEIREAAARYAAAAGPAAVFVPEMGDAGKQYAALVDLVYARRDAMAWLQSAKLAGPDLQLARLLQRRVQGCRGHSSFITGSVTAPLPPVGDAMAAQNALWALPHVAACVAMSRRYDCDQKLFLLQSLRRAYAPMAYPEAGAGGSGARAALAELRAVLAGRAAPAPLPPASTARAARERLRELADRCAVACREALEAARRAAGAAGLPVLSAAAGRGLPAAACAPDALAAHPERVLRAAELLGAARDAVERARLQRAAPAALRAEAAAALEAAALAARTVAPLARYSTRGAAARASAWALARALFSPPAEVPARLAAALAALEAAGGGAGAGAAAPGRGPVEVEVEDMRAGAPRADPEDGSEAEDGEDGEDEEAEEEEEEEKEEEEEEEEEEEEEEEGRPGPAAGAPPGPREGRRAEEEEEEEEEEEGDGDGDGEAAALPAAAGGPSGEDDSGPRRRRKAAAADAAGPARREPPLPARVLGPMPPGGPAADGGFRRVPPGDYHTPAPSAAALAAYCRPEVAARLADHPLFPEPWRPALAFDPEALAEIAARRRAGPAGRSPPPLRRRVAWMSQIADPEDVRVVVLYDPLPGEALAAPPGEDERRRPEWPPRRGGLSHALAALGNRLLLSADSHAWAGRWTGAPDVSALGAQGVLLLSTRDLAFRGAVEYLCARLAAARRRLIVLDAVDPENWPRDGPAVGQAHVYLRAAVLPRRSAPRAGPSGALARAVLASRRVFGPGAFARAEAAYARLYPEAPPLRLCRGGNVRYTVATRLGPRTAVPVPPREYRQRVLPALDGRKDMAAQGAALGLGEPDFVEGEAASHRAANRWGLGAPLRPVYLACGRRALELAPDELPAAAVAFCAAALPEPRAEAPPLVLEAAAAPPAAAAPGVDWDADQGPRETLVLLRRAAGGGLVERVPPPAAEAPPARVPAQSSPGAGSGFPAPAGGGRRPRRPRRGPPPRVEVLSSSSSSSSSSSSAASSPASSDDDEAGAAGGGPASP
Protein: V-type proton ATPase subunit d 2 (V-ATPase subunit d 2) (Vacuolar proton pump subunit d 2) (Q8N8Y2)
Organism: Homo sapiens (Human)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). May play a role in coupling of proton transport and ATP hydrolysis (By similarity). Regulator of osteoclast fusion and bone formation (By similarity).
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase 116 kDa subunit a 3
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase subunit F
- V-type proton ATPase subunit E 1
- V-type proton ATPase 116 kDa subunit a 2
Sequence:
MLEGAELYFNVDHGYLEGLVRGCKASLLTQQDYINLVQCETLEDLKIHLQTTDYGNFLANHTNPLTVSKIDTEMRKRLCGEFEYFRNHSLEPLSTFLTYMTCSYMIDNVILLMNGALQKKSVKEILGKCHPLGRFTEMEAVNIAETPSDLFNAILIETPLAPFFQDCMSENALDELNIELLRNKLYKSYLEAFYKFCKNHGDVTAEVMCPILEFEADRRAFIITLNSFGTELSKEDRETLYPTFGKLYPEGLRLLAQAEDFDQMKNVADHYGVYKPLFEAVGGSGGKTLEDVFYEREVQMNVLAFNRQFHYGVFYAYVKLKEQEIRNIVWIAECISQRHRTKINSYIPIL
Protein: Ribosomal RNA-processing protein 8 (EC 2.1.1.-) (Q4GZA6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU365074}.
Interaction partners:
- Importin beta-1 subunit, putative
- Ribosome production factor 2 homolog
- Pumilio/PUF RNA binding protein 8, putative
- RNA-binding protein, putative
- RNA-binding protein, putative
- Ribosome biogenesis protein, putative
- NAD-dependent protein deacylase SIR2rp3
- ATP-dependent DEAD/H RNA helicase, putative
- RNA-binding protein NOB1
- Importin subunit alpha
Sequence:
MSRGGIFGDPRKKGRTATDKYSKKEPPQSKNRTETSSAAKVSKKAGALYGPVVVHSSGCASRDSANDRRGIPFKNKHEEREYKKAKHIPKYAPNPTGGKGENGEPTPRPSGASSAAQRRAIRRVRDDDSVLEHFRTKLSASTFRLLNEQIYNSPISSVAELLRDPSTYADYHNGYRQQIQQWPIKPYDVILQALLEDRRGRFVANKAKSMPGYIPSSWVIADMGCGDAQVAQALCPKGYTVHSFDLHAMNEYVTVANIAHVPLEKKSVDICIFSLSLMSTDYIKCLYEAFRILKPKRLLKIVEVRSRVPHPRRFAELVEGIGFTLDYHDTVGDYFVAYDFIKLDGQESANQHPKYDPQEVLVPSLYKKR
Protein: Nucleosome assembly protein, putative (Q387Z3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Histone H2A
- Histone H2A
Sequence:
MPPKRKSAQHQRDDDDDMSSQWVEGNSTPFQKYFNTKYSSEFMGSLPERIRQRAQVLLYYHEKCERIRKDFEEKETALRRKYDEIYAPLLDKRKEIITGAHLPTDEEVRKGLPSEHEGKVSVTTDADVGKGLPGFWLRVLKHHVLSASMIRDHDEPVLMHLIDVRSGVVDGGYGSIAVAFVFEPNPFFQEETLILKLVQGDDGATVTRTPITWKPGKDVTVRTEKVKKSGKRGQGGKVKTITVPQPSFFNTFKENGGSGAATAHDDDDEDDEDEDEWTEQLLQVLHTSIIPSAVHHYTGEAPDGASDIDTDYDDDDDDDDDDDDDDDDDDDDDIPPQRGRRQQGGAFGRGSGKQSQQQPQQQCKHQ
Protein: Rho guanine nucleotide exchange factor 9 (Collybistin) (Rac/Cdc42 guanine nucleotide exchange factor 9) (A0A0A6YYF8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MTLLITGDSIVSAEAVWDHVTMANRELAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFVRLWVNQEDEVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMSTERHYIKHLKDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNNDDPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQASVLDWEGEDILDRSSELIYTGEMAWIYQPYGRNQQRVFFLFDHQMVLCKKDLIRRDILYYKGRIDMDKYEVVDIEDGRDDDFNVSMKNAFKLHNKETEEIHLFFAKKLEEKIRWLRAFREERKMVQEDEKIGFEISENQKRQAAMTVRKVPKQKGVNSARSVPPSYPPPQDPLNHGQYLVPDGIAQSQVFEFTEPKRSQSPFWQNFSRYCEGIKKPNRSKGVSDYDDAGVDFCSGNILHSGCFFYHWGFPCCSTSGSLQFCI
Protein: Ubiquitin-ribosomal protein eS31 fusion protein (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31 (40S ribosomal protein S27a)] (P62979)
Organism: Homo sapiens (Human)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
Subcellular location: [Small ribosomal subunit protein eS31]: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.; SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein eS10
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL36
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK
Protein: Type IV pilus inner membrane component PilP (G3XCX7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. PilP connects PilO to the secretin PilQ. In turn, the PilM/PilN/PilO/PilP/PilQ complex facilitates transit of the pilus through the periplasm and clamps the pilus in the cell envelope.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:19857645}; Lipid-anchor {ECO:0000255}.
Interaction partners:
- Type IV pilus inner membrane component PilM
- Type IV pilus inner membrane component PilN
- Type IV pilus inner membrane component PilO
- Fimbrial assembly protein PilQ
- Type 4 fimbrial biogenesis protein PilW
- Type IV pilus assembly protein PilF
- Protein PilJ
- Type 4 fimbrial biogenesis protein PilZ
- Type IV pilus biogenesis factor PilY1
- Type IV pilus non-core minor pilin PilE
Sequence:
MRARLILSSLLLASLAGCGGGSDFADLQSYMDEVRARPKGTIEPLPKFQPYEAFTYSAASLRSPFQPPVKIDLTVRQKGNKVIKPDETRVKQFLEGFNIETFEMVGTLSNAQGTFALVKGAGGVHRVRVGDYLGRNDGKVVGISEGKIDVIEIVPDGEGNWLERPRSLTLKERS