wanglab/gogpt-training-data huggingface dataset:
Protein: Id2 (Inhibitor of DNA binding 2) (Q3LSV1)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKAFSPVRSVRKNGFSEHNLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPSIVSLHHQRPGQNAASRSPLTTLNTDISILSLQAAEFPSELMASDSKALCG
Protein: DUF262 domain-containing protein (O34810)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- DUF1524 domain-containing protein
Sequence:
MMAKIDVELKKLHQILVDRDYFYQVPDYQRPYVWDKDHLGALIDDLVGSYTNNREDEYFCGSIVIVENQKDKRWDVVDGQQRLTSFIILACTILRLYKHSLGQESKDFIEDSIYDRYDKEKERLKFLTAQNYNSIFENTVLNHLEFEDNIKKSELNKKFEENTYLRNAYYFKELLNESVENGSISDIDDFVKWFYEHIVLTRIICFEQDSAMQIFQVLNDRGQPLSPIDILKSSLMQEIKQDSEKRKDFITTWDKLVEACKSVEGVDIDLEDFFNMYLEYADPSTSKKRADKGLKKVFKDSKKDACGFIYEISEFMKAYTALLKKQDRYVYLLRYLPSRYWASILTTALYVKYPDFDALKKLLVSYYYQTWIAGGTITRIKQTSINIIKNVKSNKSVETIKELILNSIDSYNTFDQYLYNLWDSSSVYHSKWVRPVLALANYFMADEEKPHFIAMDAETQVEHILPQTPKRGSQWNADFDKEKREEWVNNIANLTLLKRKKNAHALNGDFDEKRKIYGGKDTSKVISCYDITKELYSNYRKWNEKSLQERYKSLYNTITPVLHIEGQEDDFEDDFDLE
Protein: Methionine aminopeptidase 2B (MAP 2B) (MetAP 2B) (EC 3.4.11.18) (Peptidase M) (Q56Y85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:11060042}.
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Sphingolipid delta
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL23z
- 60S ribosomal export protein NMD3
- At1g28510/F3M18_5
- Large ribosomal subunit protein uL30z
- Large ribosomal subunit protein uL30w
Sequence:
MASESPDVAVVAPVVENGGAESSNGKEEQLESELSKKLEIAEDGQEENDGEEGSKAETSTKKKKKKNKSKKKKELPQQTDPPSIPVVELFPSGEFPEGEIQEYKDDNLWRTTSEEKRELERFEKPIYNSVRRAAEVHRQVRKYVRSIVKPGMLMTDICETLENTVRKLISENGLQAGIAFPTGCSLNWVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGHIIDCAFTVAFNPMFDPLLAASREATYTGIKEAGIDVRLCDIGAAIQEVMESYEVEINGKVFQVKSIRNLNGHSIGPYQIHAGKSVPIVKGGEQTKMEEGEFYAIETFGSTGKGYVREDLECSHYMKNFDAGHVPLRLPRAKQLLATINKNFSTLAFCRRYLDRIGETKYLMALKNLCDSGIVQPYPPLCDVKGSYVSQFEHTILLRPTCKEVLSKGDDY
Protein: Sodium/potassium-transporting ATPase subunit alpha-3 (Na(+)/K(+) ATPase alpha-3 subunit) (EC 7.2.2.13) (Na(+)/K(+) ATPase alpha(III) subunit) (Sodium pump subunit alpha-3) (Q6PIC6)
Organism: Mus musculus (Mouse)
Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit beta-3
- Protein ATP1B4
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit alpha-1
- Mitogen-activated protein kinase 3
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MGDKKDDKSSPKKSKAKERRDLDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTHSKAQEILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNLYLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDLVEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCVEGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILSLILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGTSFDKSSHTWVALSHIAGLCNRAVFKGGQDNIPVLKRDVAGDASESALLKCIELSSGSVKLMRERNKKVAEIPFNSTNKYQLSIHETEDPNDNRYLLVMKGAPERILDRCATILLQGKEQPLDEEMKEAFQNAYLELGGLGERVLGFCHYYLPEEQFPKGFAFDCDDVNFTTDNLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDLKDFTSEQIDEILQNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIMANIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLISMAYGQIGMIQALGGFFSYFVILAENGFLPGNLVGIRLNWDDRTVNDLEDSYGQQWTYEQRKVVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPSWWFCAFPYSFLIFVYDEIRKLILRRNPGGWVEKETYY
Protein: Elongation factor Tu, mitochondrial (EC 3.6.5.3) (Q8BFR5)
Organism: Mus musculus (Mouse)
Function: Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Also plays a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P49411}.
Interaction partners:
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein uL23
- Elongation factor Ts, mitochondrial
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL17m
Sequence:
MAAATLLRATPRFSGLCASPTPFLQGRLRPLKAPASPFLCRGLAVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDVPAMTEEDKNIKWS
Protein: Mitochondrial carrier protein CoAc1 (AtCoAc1) (Mitochondrial coenzyme A transporter CoAc1) (F4HW79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the accumulation of coenzyme A in the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:23590975}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Large ribosomal subunit protein eL18x
- Large ribosomal subunit protein eL18y
- Large ribosomal subunit protein eL18z
Sequence:
MGSSQGSTLSADVMSLVDTLPVLAKTLIAGGAAGAIAKTAVAPLERIKILLQTRTNDFKTLGVSQSLKKVLQFDGPLGFYKGNGASVIRIIPYAALHYMTYEVYRDWILEKNLPLGSGPIVDLVAGSAAGGTAVLCTYPLDLARTKLAYQVSDTRQSLRGGANGFYRQPTYSGIKEVLAMAYKEGGPRGLYRGIGPTLIGILPYAGLKFYIYEELKRHVPEEHQNSVRMHLPCGALAGLFGQTITYPLDVVRRQMQVENLQPMTSEGNNKRYKNTFDGLNTIVRTQGWKQLFAGLSINYIKIVPSVAIGFTVYESMKSWMRIPPRERSKPA
Protein: Gdap1, isoform B (M9PBQ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSEQTKEIEALPPTLQDFKAPDLPANKPVLFFHPYNFHAQKVLMVFYEKKIDFFPYVVDLCNGEQYSNWFLNLNPKGDVPVLQDGALVIPSSTHIINYVESKFRDRSLKPAHNSKEFDQMLIFEQAMARLPVGTLSLGSFIHDDLKLVPKAPFIGPVRQSCLKNNEKVLDLLRHSVDEQATKKAALQHKLDIQLRRHELASSREEFQKVLDAVRHFLLYVEQELTAQAPRVEWLTGDELSVADISLGLLLHRLYQLGFENQFWTFGKLPQVEAYFLRFRQRESFHRLQPSNFAILREMWTRTPGNYKLGAGAGFLGMAMFAAFAHK
Protein: Uncharacterized glycosyl hydrolase C27E2.01 (EC 3.2.1.-) (O13996)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable glucoamylase
- Putative invertase
- Invertase
- Cell wall alpha-1,3-glucan synthase mok12
- Alpha-glucosidase
- Uncharacterized family 31 glucosidase C30D11.01c
Sequence:
MSLDKQIPIIYDFGENYEKNKDIWRRQCIYQILTDRFALDDHCTTAPSTGRMYLGGTWRGIIQKLDYIQSLGCTAVWISPIVKNIEGVTGYGEAYHGYWAEDLTQLNPHFGTKQDLTELVDQLHKRNMLCMIDIVVNHMAHAGDSPIDYSKYAPFNSPSHYHPKRFLHNYDDTWDCEIAWLGDEVVSLMDIRTEDQEVHNFFQNWIRDLIQTYHFDGLRIDTAKHVQKEFYPPFIAAANVFAFGEVYHGDPKFIAKYLEYIPSAANYPLYYQIENTFFPPKQSMNIFYQKAILEARATSMDTTILGNFTENHDVPRFLNRSTDYSLLCNTLTLLLFTDGIPIIFQGQEQMYAGGHDPENRDALWTSNYNQQNPIFQFLKKLIKLRQFLVDNVSGFTTELSNMLFVNEHVYVFRRPGVIIVVSNAGSNSDVDTSAEFSITERESLEFIDVLSGSQFSSLPTEDSSTISMNLEFSFPRVLVHRGLFHSMNELA
Protein: Protein cornichon homolog 3 (CNIH-3) (Cornichon family AMPA receptor auxiliary protein 3) (D0Q0Y7)
Organism: Rattus norvegicus (Rat)
Function: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:19265014}; Multi-pass membrane protein {ECO:0000269|PubMed:19265014}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells).
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 1
- Voltage-dependent calcium channel gamma-8 subunit
- Glutamate receptor 3
- Glutamate receptor 4
- Voltage-dependent calcium channel gamma-2 subunit
- Voltage-dependent calcium channel gamma-3 subunit
- Glutamate receptor ionotropic, kainate 5
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MAFTFAAFCYMLSLVLCAALIFFAIWHIIAFDELRTDFKSPIDQCNPVHARERLRNIERICFLLRKLVLPEYSIHSLFCVMFLCAQEWLTLGLNVPLLFYHFWRYFHCPADSSELAYDPPVVMNADTLSYCQKEAWCKLAFYLLSFFYYLYCMIYTLVSS
Protein: Ribonuclease P protein component 1 (RNase P component 1) (EC 3.1.26.5) (Rpp29) (O59425)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Part of ribonuclease P (RNase P), a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}.
Interaction partners:
- Ribonuclease P protein component 4
- Ribonuclease P protein component 2
- Ribonuclease P protein component 3
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL8
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein eS6
Sequence:
MRRNSKERKNRATRRSQGSYQEIIGRTWIFRGAHRGRVTRRNIIWHELIGLRVRIVGSTHPAFVGIEGYVIDETRNMLVIAGDRIWKVPKDVCIFEFEADDGTKIKIPGERLVGRPEMRLKKRWKKW
Protein: RRM domain-containing protein (Q9U2F5)
Organism: Caenorhabditis elegans
Interaction partners:
- Ras GTPase-activating protein-binding protein gtbp-1
- ATP-dependent RNA helicase cgh-1
- mRNA-decapping enzyme 1
- DRBM domain-containing protein
- Tar DNA-binding protein homolog 1
Sequence:
MATSFYTGGGEDGDGFNPRVHARIAEREGFQLASGSEDPRTLFVANLDPAITDEFLATLFNQIGAVMKAKIIFEGLNDPYAFVEFSDHNQATLALQSHNGRELLEKEMHVTWAFEPREPGENRSKPETSRHFHVFVGDLCSEIDSTKLREAFVKFGEVSEAKIIRDNNTNKGKGYGFVSYPRREDAERAIDEMNGAWLGRRTIRTNWATRKPDEDGERGGDRGDRRGGGGGGRDRYHNQSEKTYDEIFNQAAADNTSVYVGNIANLGEDEIRRAFDRFGPINEVRTFKIQGYAFVKFETKESAARAIVQMNNADIGGQIVRCSWGKSGDSGKPSERGSGGGGGSGNYGYGYGNSGGGGGSGGPGNSQFSNFNQRPPPSGNGGSGGGSGGQNNQYWQYYSQYYNNPHLMQQWNNYWQKDGPPPPPAAAASSTGGN
Protein: GH07919p (Q95TA9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTQSDLESLFSPYGKIITSRILCDNITDEHAAGLSKGVGFIRFDQRFEADRAIKELNGTTPKNSTEPITVKFANNPSSNKNSMQPLAAYIAPQNTRGGRAFPANAAAGAAAAAAAAAIHPNAGRYSSVISRYSPLTSDLITNGMIQGNTIASSGWCIFVYNLAPDTEENVLWQLFGPFGAVQSVKVIRDLQSNKCKGFGFVTMTNYEEAVLAIQSLNGYTLGNRVLQVSFKTNKNKQT
Protein: Protein SPT23 (P35210)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Dosage-dependent suppressor of Ty-induced promoter mutations. May exert its suppression effect through protein-protein interactions since does not present any of the motifs generally found in transcriptional activators or DNA binding proteins.
Interaction partners:
- Cell division control protein 48
- Ubiquitin fusion degradation protein 1
- Protein DOA1
- Ubiquitin thioesterase OTU1
- E3 ubiquitin-protein ligase RSP5
- Acyl-CoA desaturase 1
- Protein MGA2
- Nuclear protein localization protein 4
- CTP-dependent diacylglycerol kinase 1
- UBX domain-containing protein 2
Sequence:
MMSGTGNVSSMLHSYSANIQHNDGSPDLDLLESELLDIALLNSGSSLQDPGLLSLNQEKMITAGTTTPGKEDEGELRDDIASLQGLLDRHVQFGRKLPLRTPYANPLDFININPQSLPLSLEIIGLPKVSRVETQMKLSFRIRNAHARKNFFIHLPSDCIAKDKFFTSSDDPTNLTIPNRDINERTLFLDAFLLCASNNNSNNFKQTYVCNRCINREKRRASRRKSGLNDNSIWQNNENKRAIIFNSKQLFIISNNGLSGNSNCINFDLPTRIVCYCRHHKATNGFVVLFLLRDHNGDILAKTITDPIMIMDKKNASNTTTPTSTSNAQVSPMTNDTRSFSSPQSDLNFPSEFPLPSNSKNFVISTNCMLDSNCNNNNNDNDNKNNIKTNTAMMNNNRHFPSPNSSSEDSNHSFSDIHFSNNNDNNLHRSLDSWSSTGFNSSSNPALTTLTSDFSAASARHTGKRQRSVNEPFMSTPNTFSRLPQKFIDSSKDISNHNSVPVALNNKPSIQRVIPAQGSINGGIEVTLLGSKFKQGLIIKFGENIALSSQCWNESTMVTYLPPSSKPGPVLVTIVDPSETSMRNNSNSSVSTSNSTNDILHLNKYTGEKAIFTYVDDTDRQLIELALQIVGLKMNGKLEDARNIAKRIVGSDSSPSNNNAGLHSQNSSLNSYTNMMRNINDEQLITEVIKSFKRNNNLSTVNLSMCDVRGRTLLHLAAFNNWYSLVSLLIKYGSHLNDQDLFGFTPLHMACINGDLRIIRLLLECNVNIMKKTRNGFIAKQFFLMNYTVNKTRYSNYETSLFDDILTRLTKNTTGSSDTQPFERNVSQSSFNSSLFDDDDADHDYVQERKYLLADSAALAPEQSNCNDNTSFSILDSDSGYDISDCESSSDEIALEFFNTHKIKDFSSKPNEIPKTTKTSIEPDGSLWNRMLTRLNDELPKYEDLFPKKPKNWELGSKSVEIGPDNSAQMTVDDSQTSSEDDELEALQVGFNTIFSKKQNFQNDKMLLFFWIPLTLVLLLCFTLSNLGKDDDMFHNLSKIVQEYLRIGLAKVLLGNERMKTSFKMQLSKFQNNNILNDMRVN
Protein: THAP4 protein (Q9BQ29)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSINEVILSASGACKLIDSLHSYCFSSRQNKSQVCCLREQVEKKNGELKSLRQRVSRSDSQVRKLQEKLDELRRVSVPYPSSLLSPSREPPKMNPVVEPLSWMLGTWLSDPPGAGTYPTLQPFQYLEEVHISHVGQPMLNFSFNSFHPDTRKPMHRECGFIRLKPGSSG
Protein: Expressed protein (Transmembrane protein) (Q9ZPY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAAAEARAVWQRTVNRCFVQEDAKRAPKLTYCQSSSSSTASSTKQVEVSGSSPRVSVEPRTQSSCAGFMPLPRNPNFPDLLPHNTRLWSHPHHQFQVNKKQPLEDEVNNQGVSEKKSELGAGEKQGKSFNSESFQEFIELMETRESYGSTGYDESSEKKLSELSFDPSSPWNLLSSEKAAPWWRTTDKDELASLVAQRSLDYVENCDLPTPQKMKRSYYGSPRGFDSDGLRDYSVSGQTIKGTSKGSSCKNRPEASSESDLSKSELLEALRRSQTRAREAENMAKEAYAEKEHLVKILLKQAAELFGYKQWLQLLQLEALYLQIKNKEIDNKNNDDPGVSIPCWSNGKARKEGRKRRSKRGKPNGAKYAVGLALGMSLVGAGLLLGWTVGWMQMLSF
Protein: FERM and PDZ domain-containing protein 1 (FERM domain-containing protein 2) (Q5SYB0)
Organism: Homo sapiens (Human)
Function: Stabilizes membrane-bound GPSM1, and thereby promotes its interaction with GNAI1.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18566450}. Cell membrane {ECO:0000269|PubMed:18566450}; Peripheral membrane protein {ECO:0000269|PubMed:18566450}; Cytoplasmic side {ECO:0000269|PubMed:18566450}. Note=Found both in the cytoplasm and associated with the cell membrane. {ECO:0000269|PubMed:18566450}.
Interaction partners:
- G-protein-signaling modulator 2
- G-protein-signaling modulator 1
Sequence:
MEELETSLFQTRKAHRIEQMVARWLRRSRDSSARAKVAAADGPARNPTQTLIPVRHTVKIDKDTLLQDYGFHISESLPLTVVAVTAGGSAHGKLFPGDQILQMNNEPAEDLSWERAVDILREAEDSLSITVVRCTSGVPKSSFLTEEKRARLKTNPVKVHFAEEVLISGHSQGNSLLCMPNVLKLYLENGQTKAFKFEANTTVKDIILTVKEKLSIRSIEYFALALEEQYSISRLHLLHEEELIQQVVEREESHDYRCLFRVCFVPKDPLDLLKEDPVAFEYLYLQSCSDVLQERFAVEMKCSSALRLAALHIQERIYACAQPQKISLKYIEKDWGIENFISPTLLRNMKGKDIKKAISFHMKRNQNLLEPRQKQLISAAQLRLNYLQILGELKTYGGRIFNATLMLQDRESYIALLVGAKYGISQVINSKLNIMSTLAEFANISRVELTEESEKVSVVKVYLQDVKVLTLLLESNSAKDLACLIAGYYRLLVDPVTSIFLWPGNKQQAHRVSAEEGYESRACSDSEESSEVDCVLEPLSDRRLVKLAPCRSLIKEEQPPGNSPTPEVARRGPSTCGASSTTDSAESEASDSANTESRGYRTSGSSESMDALEEDDLDTCSSSRSTFFHFGSPGLAESIDSDSQEERSGIETSGFLCLLDLAQRANPQCQKTEFSESAALETFGWAPELSTVRLDPRLYEGSHADYYSLCSSVSPASYLSDSSESTASRQGGAPPAWGQQGWTEAQPSSMLEPLALHPPLAFEDGSSDEEYYDAADKLTPPGPPSGPRDVSTAEPSATSLQNKASTSSPENSLPCGPDGRQPSRRGGVKKYAKTLRKRRSFLQTDYTSQVSFPLVPSASLESVDDVCYYDREPYLALGAPSPTVSSLQDMQGEPGLLETKALGLLAPLRETKSTNPASRVMEMEPETMETKSVIDSRVSSISAIRFRIDPNNKENSGVVPAASSSASTPHCSNPGSSGPDTAQARPSQILPLSQDLDGIAPKEPTIEHGDSSFSLSSGDPNPDRACLASNPGLNNVSQGDTLELQLEPHVQLEMGLESFCTNHIQETAPKYTEPLLSPRDEPRSDECGINPGEKIASIPTKEEPQGQLSLERDREVTNKNGTNVFQEESRKDSGDSPGDVSNNVSQTLDISSPAGKIVTSLSLDAPVTGTEQIPPHPPRDPQGQSREPPGQGCQAQEQKLFVELDLDPDFFLGKQTVSPAVPPEGIKAEAPNHVTGQDIAPRDSPEWVCFNPEPSLPEPLPCPQEDPHLETSNHCLLSEGKSDSSSICLSAEKSFLCFAPESHPEVSASLRVATSLGFAGMNEMVAPRIGMDQCSCQFSYATCFRGPQPETEEEDRDLEAHPMAPLTSPPSAGSPVVLPWRPARAHSCTTAPLSRKSHIWPEYCSRALRQLKATPASTPEGFIQLMESLLELQDILETSWGVGNKHPPEKCTWHFTESRSRLCMGSQKLLSSCRHVIRMDQSPEEMQGAVRDTFQHLVQLAGLCFQFTDCSRCSARHREAAGNLRDVVYTYHQFIEAAKSTCERGYHDLSVKLLARQCTALTAAVFCLTQKFRASTAL
Protein: Protein Bet (O93036)
Organism: Feline foamy virus (FFV) (Feline syncytial virus)
Function: May be implicated in the establishment and/or maintenance of viral persistance. Bet is required for viral replication.
Interaction partners:
Sequence:
MASKYPEEGPITEGVEEDFNSHSTSGLDLTSVGKNPEHPRRILLVLQHLIAYAEATIKKQDVPGPLLPILSPYVMAWDNPQNVVTRLVNLGESWKKYLLSPGWKDCGERDLTMLTRELLVPGIGLVQIAATLTKTYVLMCNGRCITGSRTDPDCDPLFCKLLCWKQNIQDPRECNLEEWCLYSLDPEHDPLWDPKMIVRRHRNLLPYCMRPFLIWMNYISHNPLTQQCIMMKTLNMLWRAQADDPSDVASLYPRVKVFKASHFDIFGSASGNSEERVSWAKENSHRGEYSLLPSSDDEEEEMSEREELLCHINQCQQKLFYPGGTTDVLGMESNVWLTKFVNIKFPKGTKVILPDGRKFIACDPELKPLLQELKFLDRATSESSDSE
Protein: Glycoprotein endo-alpha-1,2-mannosidase (Endo-alpha mannosidase) (Endomannosidase) (rEndo) (EC 3.2.1.130) (Endo-alpha-D-mannosidase) (Enman) (Q5GF25)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15677381}; Single-pass type II membrane protein {ECO:0000269|PubMed:15677381}.
Interaction partners:
Sequence:
MAKFRRRTCIILSLFIVFIFSLMMGLKMLWPNAASFGPPFGLDLLPELRPPNTHLENKADFQRSDRIDMETNTKDLKGAGVTVHPPRASEVNLEELPPLNYFVHAFYYSWYGNPQFDGKYVHWNHPVLEHWDPRIAKNYPQGRHSPPDDIGSSFYPELGSYSSRDPSVIETHMKQMRSASIGVLALSWYPPDASDENGEATDYLVPTILDKAHKYNLKVTFHIEPYSNRDDQNMHQNVKYIIDKYGNHPAFYRYKTRMGHSLPMFYIYDSYITKPKTWANLLTPSGSQSVRGSPYDGLFIALLVEEKHKYDILQSGFDGIYTYFATNGFTYGSSHQNWNKLKSFCEKNNMIFIPSVGPGYIDTSIRPWNTQNTRNRINGKYYEVGLSAALQTQPSLISITSFNEWHEGTQIEKAVPKRTANTVYLDYRPHKPSLYLEITRKWSEKYSKERMTYALDQQLPAS
Protein: E3 ubiquitin-protein ligase TRIM22 (EC 2.3.2.27) (50 kDa-stimulated trans-acting factor) (RING finger protein 94) (RING-type E3 ubiquitin transferase TRIM22) (Staf-50) (Tripartite motif-containing protein 22) (Q8IYM9)
Organism: Homo sapiens (Human)
Function: Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22-dependent ubiquitination of viral proteins. Plays a role in restricting the replication of HIV-1, encephalomyocarditis virus (EMCV) and hepatitis B virus (HBV). Acts as a transcriptional repressor of HBV core promoter. May have E3 ubiquitin-protein ligase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:25683609}. Nucleus {ECO:0000269|PubMed:17156811}. Nucleus speckle. Nucleus, Cajal body. Note=Localizes predominantly to the nucleus, found in cytoplasm to some extent. Forms distinct nuclear bodies that undergo dynamic changes during cell cycle progression. Nuclear bodies start to form in the early G0/G1 phase but become speckle-like in the S-phase and completely dispersed in mitosis. 35% of TRIM22 nuclear bodies overlap or are found adjacent to Cajal bodies.
Interaction partners:
- T-cell receptor-associated transmembrane adapter 1
- Interferon-induced protein 44-like
- Interferon-induced protein 44
- Interferon-induced protein with tetratricopeptide repeats 3
- Signal transducer and activator of transcription 1-alpha/beta
- Gamma-butyrobetaine dioxygenase
- XIAP-associated factor 1
- Probable ATP-dependent RNA helicase DDX60
- 2'-5'-oligoadenylate synthase 2
- Protein mono-ADP-ribosyltransferase PARP9
Sequence:
MDFSVKVDIEKEVTCPICLELLTEPLSLDCGHSFCQACITAKIKESVIISRGESSCPVCQTRFQPGNLRPNRHLANIVERVKEVKMSPQEGQKRDVCEHHGKKLQIFCKEDGKVICWVCELSQEHQGHQTFRINEVVKECQEKLQVALQRLIKEDQEAEKLEDDIRQERTAWKNYIQIERQKILKGFNEMRVILDNEEQRELQKLEEGEVNVLDNLAAATDQLVQQRQDASTLISDLQRRLRGSSVEMLQDVIDVMKRSESWTLKKPKSVSKKLKSVFRVPDLSGMLQVLKELTDVQYYWVDVMLNPGSATSNVAISVDQRQVKTVRTCTFKNSNPCDFSAFGVFGCQYFSSGKYYWEVDVSGKIAWILGVHSKISSLNKRKSSGFAFDPSVNYSKVYSRYRPQYGYWVIGLQNTCEYNAFEDSSSSDPKVLTLFMAVPPCRIGVFLDYEAGIVSFFNVTNHGALIYKFSGCRFSRPAYPYFNPWNCLVPMTVCPPSS
Protein: Small ribosomal subunit protein eS21 (40S ribosomal protein S21) (P49197)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P63220}. Cytoplasm {ECO:0000250|UniProtKB:P63220}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P63221}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P63220, ECO:0000250|UniProtKB:P63221}.
Interaction partners:
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL20
Sequence:
MQNDAGQTVELYVPRKCSSSNRIIGPKDHASVQIDFVDVDPETGRMIPGKSTRYAICGAIRRMGESDDAILRLAQKDGLVPRDDVKSN
Protein: Tryptophan 2,3-dioxygenase (TDO) (EC 1.13.11.11) (Tryptamin 2,3-dioxygenase) (Tryptophan oxygenase) (TO) (TRPO) (Tryptophan pyrrolase) (Tryptophanase) (Q1LK00)
Organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Interaction partners:
- Kynureninase
- Kynurenine formamidase
- Arylformamidase
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- 2-aminobenzoyl-CoA monooxygenase/reductase
Sequence:
MSEFKGCPMGHGAAPQNGDGGDSGDTGNGWHGAQMDFARDMSYGDYLGLDQILSAQHPLSPDHNEMLFIVQHQTTELWMKLMLHELRAARDGVKSDQLQPAFKMLARVSRIMDQLVQAWNVLATMTPPEYSAMRPYLGASSGFQSYQYREIEFILGNKNAAMLRPHAHRPEHLELVETALHTPSMYDEAIRLMARRGFQIDPEVVERDWTQPTQYNASVEAAWLEVYRNPSAHWELYELGEKFVDLEDAFRQWRFRHVTTVERVIGFKRGTGGTEGVSYLRRMLDVVLFPELWKLRTDL
Protein: MDS1 and EVI1 complex locus (E7EUL6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKSEDYPHETMAPDIHEERQYRCEDCDQLFESKAELADHQKFPCSTPHSAFSMVEEDFQQKLESENDLQEIHTIQECKECDQVFPDLQSLEKHMLSHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKHYECENCAKVFTDPSNLQRHIRSQHVGARAHACPECGKTFATSSGLKQHKHIHSSVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHFAAGGFFGQGISLPGTPAMDKTSMVNMSHANPGLADYFGANRHPAGLTFPTAPGFSFSFPGLFPSGLYHRPPLIPASSPVKGLSSTEQTNKSQSPLMTHPQILPATQDILKALSKHPSVGDNKPVELQPERSSEERPFEKISDQSESSDLDDVSTPSGSDLETTSGSDLESDIESDKEKFKENGKMFKDKVSPLQNLASINNKKEYSNHSIFSPSLEEQTAVSGAVNDSIKAIASIAEKYFGSTGLVGLQDKKVGALPYPSMFPLPFFPAFSQSMYPFPDRDLRSLPLKMEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSMGSRSRASGTKLTEPRKNHVFGGKKGSNVESRPASDGSLQHARPTPFFMDPIYRVEKRKLTDPLEALKEKYLRPSPGFLFHPQMSAIENMAEKLESFSALKPEASELLQSVPSMFNFRAPPNALPENLLRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCDRCFGQQTNLDRHLKKHENGNMSGTATSSPHSELESTGAILDDKEDAYFTEIRNFIGNSNHGSQSPRNVEERMNGSHFKDEKALVTSQNSDLLDDEEVEDEVLLDEEDEDNDITGKTGKEPVTSNLHEGNPEDDYEETSALEMSCKTSPVRYKEEEYKSGLSALDHIRHFTDSLKMRKMEDNQYSEAELSSFSTSHVPEELKQPLHRKSKSQEESKA
Protein: E3 ubiquitin-protein ligase RNF133 (EC 2.3.2.27) (Goliath-related E3 ubiquitin-protein ligase 2) (RING finger protein 133) (RING-type E3 ubiquitin transferase RNF133) (Q14B02)
Organism: Mus musculus (Mouse)
Function: Has E3 ubiquitin-protein ligase activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18574499, ECO:0000269|PubMed:35831855}; Single-pass membrane protein {ECO:0000305|PubMed:18574499}.
Interaction partners:
- RING finger protein 148
Sequence:
MNPLQTSTWQNQAPSFWLLRFSFIWLVSQKCCTASAVWTAYMNISFHVGNRMLSELGETGVFGRSSILKRVAGVVVPPEGKIQNACDPNTTFILPRNKEPWIALIERGGCAFTQKIKVASEHGARGVIIYNFPGTGNQVFPMSHQAFEDIVVVMIGNIKGMEILHLIRKGVHVTVMVEVGRKHVIWLNHYFVSFMIVTTATLAYFTFYHIRRLWVARIENRRWKRLTRELKKAFGQLQVRVLKEGDEEVNPNADSCVICFEAYKPNEIVRILTCKHFFHKNCIDPWILAHGTCPMCKCDILKALGIQMDIEDGTDSLQVLMSNELPGTLSPVEEETNYELPPARTSSKVTHVQEHPTSSANAGSQPPEAEETSHPSHGQQVL