wanglab/gogpt-training-data huggingface dataset:
Protein: Glucose-6-phosphate isomerase (EC 5.3.1.9) (G8BG61)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- phosphoglucomutase
- Pyruvate kinase
- ATP-dependent 6-phosphofructokinase
- Phosphoglycerate kinase
- Phosphoglycerate mutase
- ATP-dependent 6-phosphofructokinase
- Transketolase
- Transaldolase
Sequence:
MSSFKLASDLPAWKELEQLYKKEGEKFDVRAAFAKDPKRFDEFSRIFTNYDDSKILFDFSKNLINQEILDKLIQLAKEAGVEKLRDEMFAGDHINTTEDRAVYHVALRNVKKHKMPVDGKDTTQEVWDVLNHMKEFSDQVRDGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEALKYYSKPGLNAHFVSNIDGTDIAEVLKKVNPETTLFLIASKTFTTAETITNATSAKKWFLEHAKDTKYIAQHFAALSTNEKEVIKFGIDPKNMFGFESWVGGRYSVWSAIGLSVAIYIGFDNFEKFLAGAEAVDEHFLKTPLENNIPVLGGLISVWYNNFFNAQTHLVVPYDQYLHRFPAYLQQLSMESNGKSVTRANVFTNYQTGTILFGEPATNAQHSFFQLVHQGTKLIPADFILAAQSHNPIENNKHQKMLASNFFAQSEALLKGKSEEQVKAEGTTGGLIPHKEFSGNRPTTSILAQKITPAALGALIAYYEHVTFTEGAIWNINSFDQWGVELGKVLAKVIGTELEDKKSVGSHDPSTNGLINTFKQWE
Protein: DASK1 (Q8I6M5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METAMDVVCVMDTAVGDHLEDRQCALEEIKQAVQSAGANFQRVQFERLDFGETNVLETFYNADVAIIDLSILTQQRPLSYHYGVRESFGMKENILTYNDIDSKQTLSLKLSCANYLFLSYKRNAETNSCHLTSQPNSGNNSKEPNAEGRVPTLQWRLKRKLQDVEIQSKAHMREKFLSDMRTARDTYATNGAKLQSILHEMRKRLDDPHVLSGEVVHSFMCSLRDVQDYDAMVRLVNDLKNIPNTRKYVETGNMSFLYAFALNRRNRKGDREKALESSLKALEKKENHFPDMLCLCGRIYKDIFVESDYTDATSLAHAIKWYRQSFEVQPNEYAGINLATLLVIEGKEFTNTEELQHIGMTLNNLIGKKGSLSSLSEYWDVATFFEISVLANDYAKAIQAAECMFKLKPPNWYLKSTIGNISLIHRFRKKPEERQPPIEEQVFQFWMDFFLEATNTEEVKNSIRFPILILEPQKIYMPSYVTINMDADEKSIQIVNICLAHAKNACKKIHDFLFVASKIKSVSLYKRDDRCAYLYVHHNSDDFQIYFPSTERRQKFYDMILEMTADQVVFVNLSNDDANIEYEYDYDEQNRKMVLGKGTYGTVYAARDKQTQVRIAIKEVPEKNSQDVQPLHEEIKLHSQLRHRNIVRYLGSCSENGFFKIFMEQVPGGSLSDLLETKWGPLKDNESTMAFYSKQILEGLKYLHEQDIVHRDIKGDNVLVNTYSGVVKISDFGTSKRLARINPMTETFTGTLQYMAPEVIDQGVRGYGPAADIWSFGCTNVEMATGKPPFIELGSAHAAMFKVGFYKKHPNIPEELSANAKNFILRCFAISVMDRPSASQLLEDPFLQDKPRKVRPALPINTEFGRSISVPADRFVHKTTPPLSYNTTCNTPTTPELDITHSSSVDIDELPSNQFMLERRNSHGFLLSPEIEPSTPSLRTSISETSETDGFYRLKKDSQRRTTLSKVLALDESKICHIWLKKVDADQNSIAIRKSDLEVLIRGLRDYIMNENEKHLEATINELKQKLNNDAVALDHLHLALYSFQDAVVCVLRYHCIKPHWMFALDNLVKRAVQAAVTIFSPELGANLADKDLSGNDDESLRTSLMQKGSTESQEKQSLEKVLPTSNTREGVGLTPAESGGDALSSSMECARILRDIRDNQQKLQRQLLEQQRQSMRALHNISQELAHIYMGGRKRLRRTINGFNKKCHRMSTSVGGTSGVRPNIAGNPRRQLNKHHFGLHEVDEQLEQWLTQQEIDEFSKTLILNEGFTFDDFIYNMEKLDLMRLGLRVGIEVRLWKLIIQERVCTSSDCVDSPPSTYHKPIGGNSSFALIDNNNTLPSPTTTTPGTPGIKTKIKKSESEYDSCSE
Protein: Uridine phosphorylase A (SmUPa) (EC 2.4.2.3) (G4VGI0)
Organism: Schistosoma mansoni (Blood fluke)
Function: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (Probable).
Interaction partners:
- Putative 2,3-cyclic-nucleotide 2-phosphodiesterase
- Uracil phosphoribosyltransferase homolog
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- Uridine kinase
- Dihydroorotate dehydrogenase
- uridine/cytidine kinase
- Uridine 5'-monophosphate synthase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Putative uridine phosphorylase
Sequence:
MATVQPIVNSHLSELDEDVFHHFGFTTKSFDFKEKFGDVKFVCVCGSSGRIHNFAISMAKLAGLALPVENIAGSHARFVLYKVDHILFADHGMGIPSALIMLHEVTKLLHYAGCKDVLFIRLGTSGGLGVKPGTIVLSDRCVNTKLEPYNELCILGKPVRRQTIVDLNTVNELKKLSENLSLECSVVVGGTIAANDFYEEQGRLDGSICTFSKEEKLAFLQSAYEHGIRNMEMEGTAITSHCYLTGHRAILVCVTAVNRLEGDQITISTDEFTLFAQRPGQLVGEYLKRNNGIIVR
Protein: Uncharacterized protein Rv1899c (P9WK29)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- PE-PGRS family protein PE_PGRS21
- PE-PGRS family protein PE_PGRS19
- PE-PGRS family protein PE_PGRS3
- Bifunctional lipase/adenylate cyclase LipJ
- NAD-dependent protein deacylase
- Uncharacterized PPE family protein PPE58
- Putative lipoprotein LppN
Sequence:
MAAMRAHARRRHPHALMSRAAGLPRLSWFAGLTWFAGGSTGAGCAAHPALAGLTAGARCPAYAAISASTARPAATAGTTPATGASGSARPTDAAGMADLARPGVVATHAVRTLGTTGSRAIGLCPCQPLDCPRSPQATLNLGSMGRSLDGPQWRRARVRLCGRWWRRSNTTRGASPRPPSTCRGDNVSMIELEVHQADVTKLELDAITNAANTRLRHAGGVAAAIARAGGPELQRESTEKAPIGLGEAVETTAGDMPARYVIHAATMELGGPTSGEIITAATAATLRKADELGCRSLALVAFGTGVGGFPLDDAARLMVGAVRRHRPGSLQRVVFAVHGDAAERAFSAAIQAGEDTARR
Protein: Protein charybde (Protein charybdis) (Protein regulated in development and DNA damage response 1) (REDD-1) (Q9VTI8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Inhibits cell growth by regulating the Tor pathway upstream of the Tsc1-Tsc2 complex and downstream of Akt1. Acts as cell death activator during head development.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Gigas, isoform A
- GTP-binding protein Rheb homolog
- GH04846p
- FI21816p1
- Raptor, isoform B
- Ribosomal protein S6 kinase
Sequence:
MKMEVLSVQNHIQGKFGVNKIKDWQASTAPLEEEEELTAGVNGNTAAGEGILDVDVVDGHPASVLHMRQHQALNTRPSATPPSAGGGGPLAGGGSVGMTTPKQATSPVAAASFEAPLSGGSAAAYHHAYMTNVLSSTAQQHHPLPASPLQSTACARFGAADNLDDVSASAVRELSQQLQAQLRDAKRRHLACTEVTLPNDLTQRIAAEIIRMSEREPCGERACTLFIEFESEPNKVKRIAYFKVDPDTVSIFELYLTLRQDKSGWSSLVPQFIKNLTRSNTINISPDFTLTKKKLYSSE
Protein: Abrin-a [Cleaved into: Abrin-a A chain (EC 3.2.2.22) (rRNA N-glycosidase); Linker peptide; Abrin-a B chain] (P11140)
Organism: Abrus precatorius (Indian licorice) (Glycine abrus)
Function: The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. Abrin-a is more toxic than ricin.
Interaction partners:
Sequence:
QDRPIKFSTEGATSQSYKQFIEALRERLRGGLIHDIPVLPDPTTLQERNRYITVELSNSDTESIEVGIDVTNAYVVAYRAGTQSYFLRDAPSSASDYLFTGTDQHSLPFYGTYGDLERWAHQSRQQIPLGLQALTHGISFFRSGGNDNEEKARTLIVIIQMVAEAARFRYISNRVRVSIQTGTAFQPDAAMISLENNWDNLSRGVQESVQDTFPNQVTLTNIRNEPVIVDSLSHPTVAVLALMLFVCNPPNANQSPLLIRSIVEKSKICSSRYEPTVRIGGRDGMCVDVYDNGYHNGNRIIMWKCKDRLEENQLWTLKSDKTIRSNGKCLTTYGYAPGSYVMIYDCTSAVAEATYWEIWDNGTIINPKSALVLSAESSSMGGTLTVQTNEYLMRQGWRTGNNTSPFVTSISGYSDLCMQAQGSNVWMADCDSNKKEQQWALYTDGSIRSVQNTNNCLTSKDHKQGSTILLMGCSNGWASQRWVFKNDGSIYSLYDDMVMDVKGSDPSLKQIILWPYTGKPNQIWLTLF
Protein: Charged multivesicular body protein 2B (A0A8I5Y9Y9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MESGLLRNVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACRVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
Protein: Zinc finger protein 395 (Q7TPT8)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQSHPHRRSRVSSMLSRRLGKRSLLGARVLGPSAAEVPSGATLPLEPQIEVPEGAMSLSPLTSKDPVCQEQPKELLKALGTSCHPQVAFQPGQKVCVWYGGQECKGLVEQHSWAEDKVTVRLLDQKLQ
Protein: Glypican-1 [Cleaved into: Secreted glypican-1] (Q9QZF2)
Organism: Mus musculus (Mouse)
Function: Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling. Binds Cu(2+) or Zn(2+) ions.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Endosome. Note=S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments. Associates with fibrillar APP amyloid-beta peptides in lipid rafts in Alzheimer disease brains.; SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular space.
Interaction partners:
- Syndecan-1
- Syndecan-4
- Fibroblast growth factor 2
- Proheparin-binding EGF-like growth factor
- Syndecan-2
- Slit homolog 2 protein
- Collagen alpha-1
- Epithelial cell adhesion molecule
- Epidermal growth factor receptor
- Basement membrane-specific heparan sulfate proteoglycan core protein
Sequence:
MELRTRGWWLLCAAAALVVCARGDPASKSRSCSEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANHSRMELESALHDSSRALQATLATQLHGIDDHFQRLLNDSERTLQEAFPGAFGDLYTQNTRAFRDLYAELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLPDDYLDCLGKQAEALRPFGDAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLAPECSRAIMKLVYCAHCRGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGPSGAESVIGGVHVWLAEAINALQDNKDTLTAKVIQACGNPKVNPHGSGPEEKRRRGKLALQEKPSTGTLEKLVSEAKAQLRDIQDFWISLPGTLCSEKMAMSPASDDRCWNGISKGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRGAYGGNDVDFQDASDDGSGSGSGGGCPDDTCGRRVSKKSSSSRTPLTHALPGLSEQEGQKTSAATCPEPHSFFLLFLVTLVLAAARPRWR
Protein: Primary amine oxidase, liver isozyme (EC 1.4.3.21) (Amine oxidase [copper-containing]) (Copper amine oxidase) (Serum amine oxidase) (SAO) (Q29437)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Spermine oxidase
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Aldehyde dehydrogenase family 3 member B1
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Aromatic-L-amino-acid decarboxylase
- Amine oxidase
- Amine oxidase [copper-containing] 3
- Amine oxidase
- Catechol O-methyltransferase
Sequence:
MFIFIFLSLWTLLVMGREEGGVGSEEGVGKQCHPSLPPRCPSRSPSDQPWTHPDQSQLFADLSREELTTVMSFLTQQLGPDLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGGQPQPNVTELVVGPLPQPSYMRDVTVERHGGPLPYYRRPVLLREYLDIDQMIFNRELPQAAGVLHHCCSYKQGGQKLLTMNSAPRGVQSGDRSTWFGIYYNITKGGPYLHPVGLELLVDHKALDPADWTVQKVFFQGRYYENLAQLEEQFEAGQVNVVVIPDDGTGGFWSLKSQVPPGPTPPLQFHPQGPRFSVQGNRVASSLWTFSFGLGAFSGPRVFDVRFQGERLAYEISLQEAGAVYGGNTPAAMLTRYMDSGFGMGYFATPLIRGVDCPYLATYMDWHFVVESQTPKTLHDAFCVFEQNKGLPLRRHHSDFLSHYFGGVAQTVLVFRSVSTMLNYDYVWDMVFYPNGAIEVKLHATGYISSAFLFGAARRYGNQVGEHTLGPVHTHSAHYKVDLDVGGLENWVWAEDMAFVPTAIPWSPEHQIQRLQVTRKQLETEEQAAFPLGGASPRYLYLASKQSNKWGHPRGYRIQTVSFAGGPMPQNSPMERAFSWGRYQLAITQRKETEPSSSSVFNQNDPWTPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDQEPSMDSADSIYFREGQDAGSCEINPLACLPQAATCAPDLPVFSHGGYPEY
Protein: Ras-related protein Rab (G5EBF0)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|RuleBase:RU367128}; Lipid-anchor {ECO:0000256|RuleBase:RU367128}.
Interaction partners:
- X-linked retinitis pigmentosa GTPase regulator homolog
- Mss4 protein
- AP-3 complex subunit beta
- E3 ubiquitin-protein ligase rpm-1
- ABC transporter domain-containing protein
- CUP-5L
- AP-3 complex subunit mu
- Ras-related protein Rab-7a
- ABC-type xenobiotic transporter
- Gut granule loss protein 3
Sequence:
MAALTNNDKISYKVLVIGDPGVGKTSIIRRFVHNVFSSNYKTTIGVDFALKILPVDENTVVHLQIWDISGQDRYGVMTRVYYKDAHAAIIVLDSTRERTIEGALRWKTDLDQKVTLADGSPVPAILLANKCDIDNKLGDDKLYDLETNNGFVGSFRTSAKESVGIEEAFKFLANTVISTEQGGQYDVPFMNREGNVNLDDNTTHSRYDSKCC
Protein: Transforming acidic coiled-coil-containing protein 2 (Q9JJG0)
Organism: Mus musculus (Mouse)
Function: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors. May play a role in organizing centrosomal microtubules (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95359}. Nucleus {ECO:0000250|UniProtKB:O95359}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O95359}.
Interaction partners:
- Cytoskeleton-associated protein 5
Sequence:
MGNENSTSDHQRTSSVQSPRSLQPPGKSQSLQKQQGDLPGSCAGSIPGTDDVIQPAAPVDPGHPPLAGIGSNQGEVCTSLQLSYTIVTVQSASPSAARASPAPLAPEHTASAPSAAGPGVEVTPTGSPQHLAKNEPRSSDSEEAFETPESTTPVKAPPAPPPPPPEVTPEPEVIDPPAPEEPGCISEPPVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDKPIASSGTYNLDFDSIELVDNFQSLEPCSADSKGQECKVSTRRKSTESVPPSKSTLSRSLSLQASDFDGASCPGSPEAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKKKQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTESATPEGAGCTLSDDTPLESPAVPTATCPLTLESAEDVSPLVSGGGRVQNSPPVGRKSVPLTTASEAVEVTLSDSGGQEDLPAKGLSVRLEFDYSEDKGSWESQQENAPPTKKIGKKPVAKMPLRRPKMKKTPEKLDNTPASPPRSPTEPSDTPIAKGTYTFDIDKWDDPNFNPFSSTSKMQESPKLSQQSYNFDPDACEESLDPFKASSKTPSSPSKSPASFEIPASTTEADGDGLNKPAKKKKTPLKTMVEDVMSVCSLFDTFRVKKSPKRSPLSDPPSQDPTPAATPEAPSAISTVVHATDEEKLAVTSQKWTCMTVDLDADKQDFPQPSDLSNFVNETKFNSPSEELDYRNSYEIEYMEKLGSSLPQDDDTPKKQALYLMFDTPQESPVKSPPVRMSDSPTPCSGSSFEDTEALVNAATKLQHPVARGLPSSQEPLLQVPEKPSQKELEAMALGTPAEAIEITAPEGAFASADTLLSRLAHPASLCGALGYLEPDLAEKNPPVFAQKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAHPPDVSISKTALYSRIGSTEVEKPPGLLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIPGTERKILSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGKS
Protein: Carbohydrate deacetylase (EC 3.5.1.-) (Q53WD3)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides.
Interaction partners:
Sequence:
MDLLERLGLGGRRVLILHHDDLGLTHAQNGAYQALGLPTGSVMVPGAWASGVKGEDLGVHLVLTSEWPAPRMRPLTEGESLRDEAGYFPESLEALWRKARAEEVERELKAQIQAAAKLFSPTHLDAHQGAVLRPDLAEVYLRLAEAYRLVPLVPESLEGLGVPPPFLPELERLLYETPFPQVRFLDPYGLPPEERLGFYLDLAHLPPGLYYLVHHSALPTPEGRALPDWPTREADYFALSHPEVRRVLAEFHPLTWRAVREALF
Protein: Uncharacterized protein (E7DNB1)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MSQPELVWKPEEFVSNCERYRNKFQVAVITVCEVAATKMEEYAKTHAIWTDRTGNARQKLKGEAAWVSADQIMIAVSHHMDYGFWLELAHGRKYKILEQAVEDNVEELFRALRRLLD
Protein: UvrABC system protein C (Protein UvrC) (Excinuclease ABC subunit C) (P0A8G0)
Organism: Escherichia coli (strain K12)
Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Subcellular location: Cytoplasm.
Interaction partners:
- UvrABC system protein B
- UvrABC system protein A
- DNA helicase II
- Response regulator UvrY
- Holliday junction branch migration complex subunit RuvB
- Holliday junction branch migration complex subunit RuvA
- Crossover junction endodeoxyribonuclease RuvC
- Transcription-repair-coupling factor
- DNA mismatch repair protein MutL
- DNA polymerase I
Sequence:
MSDQFDAKAFLKTVTSQPGVYRMYDAGGTVIYVGKAKDLKKRLSSYFRSNLASRKTEALVAQIQQIDVTVTHTETEALLLEHNYIKLYQPRYNVLLRDDKSYPFIFLSGDTHPRLAMHRGAKHAKGEYFGPFPNGYAVRETLALLQKIFPIRQCENSVYRNRSRPCLQYQIGRCLGPCVEGLVSEEEYAQQVEYVRLFLSGKDDQVLTQLISRMETASQNLEFEEAARIRDQIQAVRRVTEKQFVSNTGDDLDVIGVAFDAGMACVHVLFIRQGKVLGSRSYFPKVPGGTELSEVVETFVGQFYLQGSQMRTLPGEILLDFNLSDKTLLADSLSELAGRKINVQTKPRGDRARYLKLARTNAATALTSKLSQQSTVHQRLTALASVLKLPEVKRMECFDISHTMGEQTVASCVVFDANGPLRAEYRRYNITGITPGDDYAAMNQVLRRRYGKAIDDSKIPDVILIDGGKGQLAQAKNVFAELDVSWDKNHPLLLGVAKGADRKAGLETLFFEPEGEGFSLPPDSPALHVIQHIRDESHDHAIGGHRKKRAKVKNTSSLETIEGVGPKRRQMLLKYMGGLQGLRNASVEEIAKVPGISQGLAEKIFWSLKH
Protein: Zinc finger CCCH domain-containing protein 34 (AtC3H34) (Zinc finger CCCH domain-containing protein ZFN-like 2) (Q9SQU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Probable E3 ubiquitin-protein ligase LUL2
- Probable E3 ubiquitin-protein ligase LUL3
- Probable E3 ubiquitin-protein ligase LUL1
- Probable E3 ubiquitin-protein ligase LOG2
- Probable E3 ubiquitin-protein ligase LUL4
- E3 ubiquitin-protein ligase RHA2A
- E3 ubiquitin-protein ligase SDIR1
Sequence:
MERYGRPGEEGSRSDPSLEWTSHGGETAVEAPMWRLGLSGGGGGGGGGESYPERPDEPDCIYYLRTGVCGYGSRCRFNHPRDRGAVIGGVRGEAGALPERMGHPVCQHFMRTGTCKFGASCKYHHPRQGGGGGSVAPVSLSYLGYPLRPGEKECSYYLRTGQCKFGLTCRFNHPVPLAVQGPPQQPQQQQPQPQPQLQTIYPTLQSQSIPSSQQYGLVLTRPSFLTGSYLQSPYGPPMVLPPGMVPYSGWNPYQASLSAMPSPGTQPSIGSSSIYGLTPLSPSATAYTGTYQSVPSSNSTSKEFPQRPDQPECQYFMRTGDCKFGSSCRYHHPVDAVPPKTGIVLSSIGLPLRPGVAQCTHFAQHGICKFGPACKFDHSMSSSLSYSPSASSLTDMPVAPYPIGSSSLSGSSAPVSSSNEPTKEAVTPAVSSMVSGLSRPEPAETSGDSASVSGSIEAKTSS
Protein: Pathogenesis-related thaumatin-like protein 3.5 (allergen Cry j 3.5) (Q5DWG1)
Organism: Cryptomeria japonica (Japanese cedar) (Cupressus japonica)
Function: May be involved in disease resistance.
Interaction partners:
Sequence:
MASLRLATLAMMVLFGSCRAGATVFTLVNKCSYTVWPGTLSGSGSSVLGEGGFTLAPGQSVPLTASSRWSGRFWGRTDCSFDASGKGSCITGDCGNVLNCAQAGGTPPVSLAEFTLGDKDFYDVSLVDGYNVPLSIAAVGGTGDCRTAGCVSDLRTSCPAELSVTSNGQVIACKSACAAFSTPEYCCTGDHGSPQTCSPSKYSQVFKSACPTAYSYAYDDATSTFTCSNADYTITFCPSS
Protein: Uncharacterized protein (Q38E80)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA damage-binding protein 1
- Cullin 4B, putative
- Cullin family profile domain-containing protein
- Telomerase-associated protein, putative
- Ubiquitin, putative
Sequence:
MGSQIPQQQQQQRPSILSYNTGWLANGVSWSTRENAPFRFAVSSYIQEFKNYVDIVQKNDEGELVCRATWSHSYPPTKVMFAPPKAGSDLIITTADYMRLWEVKEGPPESNERSDERHREVDDPRRVPSKMDHIDSHVSFKMAFEYGKQPNDLCFPVTSCDWNTDDPNVVGCCSVDTTVTIWDLETGKNTRLIAHDKDVYDIAFAKGTHTFASCGADGSVRVFDLREIEHCTILYESSSLFPLLRVAWDNSDRTYISTFGVEGTEVIVIDIRFPAVAVASLKSANPQPINSVCWAPNSMINLCSAGEDGTANIWDLNELPNVEAKCIMSCKVENPINNISWSSQHEQWIAITTGNEAQLLHV
Protein: Plasminogen-binding group A streptococcal M-like protein PAM (P49054)
Organism: Streptococcus pyogenes
Function: Binds to human plasminogen (and plasmin) via its kringle repeats. Also binds to albumin, immunoglobulin G and fibrinogen. Could provide the bacteria with a mechanism for invasion, as streptococcal-bound plasmin could permit tissue penetration.
Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}.
Interaction partners:
Sequence:
RKLKTGTASVAVALTVVGAGLASQTEVKANRADDARNEVLRGNLVRAELWYRQIQENDQLKLENKGLKTDLREKEEELQGLKDDVEKLTADAELQRLKNERHEEAELERLKSERHDHDKKEAERKALEDKLADKQEHLNGALRYINEKEAEAKEKEAEQKKLKEEKQISDASRQGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKGLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSKLAALEKLNKELEESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAEKASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTGETT
Protein: Dihydrofolate reductase (DHFR) (EC 1.5.1.3) (Q60034)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Interaction partners:
- Folylpolyglutamate synthase/dihydrofolate synthase
- Aminomethyltransferase
- Flavin-dependent thymidylate synthase
- Serine hydroxymethyltransferase
- Formate--tetrahydrofolate ligase
- 5-methyltetrahydrofolate S-homocysteine methyltransferase
- Methionyl-tRNA formyltransferase
- Phosphoribosylglycinamide formyltransferase
- Bifunctional purine biosynthesis protein PurH
- ABC transporter, ATP-binding protein
Sequence:
MAKVIFVLAMDVSGKIASSVESWSSFEDRKNFRKITTEIGNVVMGRITFEEIGRPLPERLNVVLTRRPKTSNNPSLVFFNGSPADVVKFLEGKGYERVAVIGGKTVFTEFLREKLVDELFVTVEPYVFGKGIPFFDEFEGYFPLKLLEMRRLNERGTLFLKYSVEKSHR
Protein: S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase (EC 4.1.3.44) (tRNA wybutosine-synthesizing protein 1 homolog) (Q8RXN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Interaction partners:
- tRNA wybutosine-synthesizing protein 2/3/4
- tRNA
- Uncharacterized protein At3g61260
- Protein TIFY 4A
- Threonylcarbamoyladenosine tRNA methylthiotransferase
- Pentatricopeptide repeat-containing protein At5g59600
- CDK5RAP1-like protein
- Cytoplasmic tRNA 2-thiolation protein 1
- Origin of replication complex subunit 1A
- Large ribosomal subunit protein uL1c
Sequence:
MSTTSSVRVRLAFVALLSATTFYCIHKYRRLKHLKNLSLNPSSTLKASRGKIFFISQTGTAKALAQRLHELCASNDIAFDIVDPHSYEPEDLPKETLVLFIASTWDGGKPPKNGEFLVNWLGESAEDFRVGSLLLSDCKFAVFGVGSRAYGESYNAVAKELSSRMIGLGGLEMIPVGEGDVDDGELDRAFQDWCDGVIRVLKGGSAQETNGVSQQIGAVEDDLEYYDSTDEEDEDNDADGGIVDLEDIAGKAPSKRNGVVKVTKVDGKKEMVTPVIRASLTKQGYKIIGSHSGVKICRWTKSQLRGRGGCYKHSFYGIESHRCMETTPSLACANKCVFCWRHHTNPVGKSWQWKMDEPSVIVKGALDLHKNMIKQMKGVPGVTPEKLQEGLNPRHCALSLVGEPIMYPEINALVDELHGRRISTFLVTNAQFPEKILMMKPITQLYVSVDAATKESLKAIDRPLFADFWERFIDSLKALQEKQQRTVYRLTLVKGWNTEELDAYFNLFSIGKPDFIEIKGVTYCGSSATSKLTMENVPWHTDVKAFSEALSLKSNGEYEVACEHAHSCCVLLGRTEKFKVDGKWFTWIDYEKFHDLVASGEPFTSTDYMAQTPSWAVYGAQEGGFDPGQLRYKKERNHPPKPQAVLA
Protein: WD repeat-containing protein 18 (A0A1L8HX76)
Organism: Xenopus laevis (African clawed frog)
Function: Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit (By similarity). May play a role during development (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BV38}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q4VBE8}. Cytoplasm {ECO:0000250|UniProtKB:Q4VBE8}. Dynein axonemal particle {ECO:0000269|PubMed:33263282}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. {ECO:0000250|UniProtKB:Q4VBE8}.
Interaction partners:
- Testis expressed 10 S homeolog isoform X2
- Nucleolar GTP-binding protein 2
- Notchless protein homolog 1
- Polynucleotide 5'-hydroxyl-kinase NOL9
- Protein SDA1
- CDT1 domain-containing protein.
- Nucleolar GTP-binding protein 1
- Proliferation-associated protein 2G4
- CP-type G domain-containing protein.
- CP-type G domain-containing protein.
Sequence:
MAAPLELVLSADAAGQVANCTVWEPVTGSVLLTYRGGNTSHRGLAVLGGQYLLGGQLGKNYINVWELQRRDQLQQKIVCPGPVNCLSASPNGLYLVAGIAESIYLWEVSTGHLLAILNSHYQDVTCLTFTDDSSHIISGAKDSLVLVWGLYSVLQVETSRGPEPRYVWSRHSLPITDVQCGIGGPQARVATSSLDQTIKLWDICSGDLLVSVLFDVRITSVAFDPAEYHLFCGGSDGVIYQVDLYTTPEQRERPFHPEQEMVFKGHRNQVTCLSVSLDGSMLISGSHDETVCVWDIQSKQSLRSVPHRGPVTNVFIIAAPSNMLRAESKPSFPLPHFSKHLQGAEGCEGPESGGVILRLGKQQGSKENTYLQRADQLQSLLGESEGKNLSGLVEQLRSRTSELEEELNVVRKINKDLFDFSARIITKQ
Protein: Collagen IV alpha 5 chain (Q61436)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
GARGLDGPPGPDGLQGPPGPPGTTSVAHGFLITRHSQTTEAPQCPRGTVHIYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASRNDYSYWLSTPEPMPMNMEPLKGQSIQPFISRCAVCEAPAVVIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANSYSFWLATVDMSDMFNKPQSETLKAGDLRTRISRCQVCMKRT