wanglab/gogpt-training-data huggingface dataset:
Protein: adenine phosphoribosyltransferase (EC 2.4.2.7) (Q57V31)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- GMP synthase
- Adenosine kinase
- Adenosine kinase
- Adenylosuccinate lyase
- Hypoxanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
- Guanine deaminase
- Guanylate kinase, putative
- Guanylate kinase, putative
- Inosine-adenosine-guanosine-nucleoside hydrolase
Sequence:
MSQYDAILTERHPHHFTLADTHPLAKELHANIFGESDLTHANCAHVYDISSLTEKPALFRKVIEFLKCRYETMGDTGPTHIIGVESRGYIIGAPLAVALGIPFVTARVTKRFPSSFVPEGDDLKYLPMSRSIRNDSIPPRARVLIVDDFIGTGSTMLAALRLADIVAAQVVEVLTVCDVASLGGIKIIRESDDEMFKETPIFTLIHFKLSPREAEEQLEFVNSYITRSRL
Protein: Vesicle transport through interaction with t-SNAREs homolog 1A (Q54CK6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers.
Subcellular location: Membrane {ECO:0000269|PubMed:12175335}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12175335}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12175335}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12175335}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q9JI51, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9JI51, ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:12175335}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12175335}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9JI51, ECO:0000255}.
Interaction partners:
- Putative synaptobrevin homolog YKT6
- t-SNARE family protein
- t-SNARE family protein
- Probable syntaxin-8B
- Synaptobrevin domain-containing protein
- Synaptobrevin-A
- Synaptobrevin-B
- Syntaxin-7A
- Vesicle-associated membrane protein 7A
- Syntaxin-8A
Sequence:
MDVFERTEQNFQHVCNSITRRIKQLPNYGGEKKKIAVREVENDIDEALKFISEMEKLAQNHPQRIKLQTKTKQYHSDIQKYKREVQLAQLQSSNQTNSNPWSNAPDDYQSQYDNQRQHLLQGSNMLDSTSDRLLRTHQISAQSEQIGQNILMDLGKQGEQIRGMRDKLHETDDQIKSARKIMTGIARRLATNKVILSIIILLLMGIIALIICLKWLR
Protein: Suppressor of cytokine signaling 2-like (Suppressor of cytokine signaling 2b) (V9Q4K1)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- Elongin-C
- Cullin-5
- Cullin-5
- Cullin-5
- Elongin-B
- Tyrosine-protein kinase receptor
- Growth hormone receptor
- Growth hormone receptor-like isoform X1
- Growth hormone receptor isoform 1
- Somatolactin receptor
Sequence:
MTCHSPESTETIENERTDTESRVVDSDETRIGQAMRDLKNTGWYWGSLTANEAKEILQDASEGTFLVRDSSQRDYLFTISAMTSAGPTNLRIEYKEGKFKLDSVVLIKPKLKQFDSVVHLVEHYVQLSRTTSKGASSGASKSLAPPNGTVQLLLTKPVYTATPSLQHLSRIAINNATRQVQELPLPNRLKNYLTDYSYNV
Protein: Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3) (Q4VA53)
Organism: Mus musculus (Mouse)
Function: Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6TRW4}.
Interaction partners:
- Wings apart-like protein homolog
- Structural maintenance of chromosomes protein 3
- Nipped-B-like protein
- Structural maintenance of chromosomes protein 1A
- Cohesin subunit SA-2
- Cohesin subunit SA-1
- Double-strand-break repair protein rad21 homolog
- Sororin
- Structural maintenance of chromosomes protein 1B
- MAU2 chromatid cohesion factor homolog
Sequence:
MAHSKTRTNDGKITYPPGVKEISDKISKEEMVRRLKMVVKTFMDMDQDSEEEKELYLNLALHLASDFFLKHPDKDVRLLVACCLADIFRIYAPEAPYTSPDKLKDIFMFITRQLKGLEDTKSPQFNRYFYLLENIAWVKSYNICFELEDSNEIFTQLYRTLFSVINNGHNQKVHMHMVDLMSSIICEGDTVSQELLDTVLVNLVPAHKNLNKQAYDLAKALLKRTAQAIEPYITNFFNQVLMLGKTSISDLSEHVFDLILELYNIDSHLLLSVLPQLEFKLKSNDNEERLQVVKLLAKMFGAKDSELASQNKPLWQCYLGRFNDIHVPIRLECVKFASHCLMNHPDLAKDLTEYLKVRSHDPEEAIRHDVIVSIVTAAKKDILLVNDHLLNFVRERTLDKRWRVRKEAMMGLAQIYKKYSLQSAAGKDAAKQISWVKDKLLHIYYQNSIDDRLLVERIFAQYMVPHNLETTERMKCLYYLYATLDLNAVKALNEMWKCQNLLRHQVKDLLDLIKQPKTDASVKAIFSKVMVITRNLPDPGKAQDFMKKFTQVLEDDEKIRKQLEALVSPTCSCKQAEGCVREITKKLGNPKQPTNPFLEMIKFLLERIAPVHIDTESISALIKQVNKSIDGTADDEDEGVPTDQAIRAGLELLKVLSFTHPISFHSAETFESLLACLKMDDEKVAEAALQIFKNTGSKIEEDFPHIRSALLPVLHHKSKKGPPRQAKYAIHCIHAIFSSKETQFAQIFEPLHKSLDPSNLEHLITPLVTIGHIALLAPDQFAAPLKSLVATFIVKDLLMNDRLPGKKTTKLWVPDEEVSPETMVKIQAIKMMVRWLLGMKNNHSKSGTSTLRLLTTILHSDGDLTEQGKISKPDMSRLRLAAGSAIVKLAQEPCYHEIITLEQYQLCALAINDECYQVRQVFAQKLHKGLSRLRLPLEYMAICALCAKDPVKERRAHARQCLVKNITVRREYLKQHAAVSEKLLSLLPEYVVPYTIHLLAHDPDYVKVQDIEQLKDVKECLWFVLEILMAKNENNSHAFIRKMVENIKQTKDAQGPDDTKMNEKLYTVCDVAMNIIMSKSTTYSLESPKDPVLPARFFTQPDKNFSNTKNYLPPEMKSFFTPGKPKTANVLGAVNKPLSSAGKQSQTKSSRMETVSNASSSSNPSSPGRIKGRLDSSEMDHSENEDYTMSSPLPGKKSDKREDPDLSELEKPRSRKKAPVTDPEEKLGMDDLTKLVQEQKPKGSQRGRKRGRTASDSDEQQWPEEKRHKEELLENEDEQNSPPKKGKRGRPPKPLGGGTSKEEPTMKTSKKGNKKKLVPPVVDDDEEEERQIGNTEHKSKSKQHRTSKRAQQRAESPETSAVESTQSTPQKGRGRPSKAPSPSQPPKKIRVGRSKQVATKENDSSEEMDVLQASSPVSDDTTQEGAEEEDISVGNVRRRSSKRERR
Protein: Nuclear migration protein unc-83 (Q0PDL1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTSTLEKSAKKILAERPEAENSVLLRLNTICCAMDQLRVQHNSRMMSGADSDTASSARSSTSSSTGEMRLWLHEVERRLEINEKRIRVEPNLQLLLSDQQALQLEIQHEGQLLVNRLNKQIKDDHDSDSSEEEKRKTCVDAIRKRWHTIYLNSLSLVCRIEELINHQQASEDSESDPDLVGPPIKRARIRTVGHLTASDTEESEADEEDRHSQTETVVTEDDNVLPFAENEYESIMDGRVTVDSCTSSSEDQMVEQSTNKKWESVLQDVGYSSGENSIHEALNTCADHLVPETSDMRRKRIECSPVKAFYRTVQLEDMSDLEVTKAINHDVEEEPNLSDSMYVNHDSTFLATQNLPEYDEVMALMDDDDLPMDMSMTESFNTKWREIHGQKKPLRRASRPSREQMNLIAKSSCDASSEDSSEGENQTNLEDDPEMMSVSFNSAQFDTSSPLKRQRSARGLKNASFLYDSLEMDGSFCSTRSEMLPPCKTRSLARRKLRVRRMPRSMSDGEQLGVVSSKPEGMMTPMIRVSPPSTPVRRLLRKLDEQIRNRDSDTAPEHSDAAQAYEWDEYNPPQKDDSISDRHIQTMTDISDQLMNIDDDFAEHFGTSSAIRLIEESKSHLRVVLKALEESDSNIPQLSNFELIARSNLRQVDEALKIQSGNQPSFLETSTLQDLRSEWANLYESIRSPFARIMHQVKKFAATLQEVSSMASLGDVDIRSKEDVAKTLDAVTAIERRLSSERQELRDLLASSSFRDVAKDLSCEFESVSEGYDDAVDKIGKMAHSLSQVKGEWDAWNSRQNDIRNAMVRIESHLKEGQMDNKMIADEMELCQERMNSLETMCNYLTASLGSIQNESNSKNLPDFKAELSIYSNALARLKDRFNDMIRVPTPPTVQFHPPEPLPSLARSMTTQTAEMESETENEPLTIAEAISSSRLIKFTFALSLLAALAAIFYYHVFGKPFGPHVTYVNGPPPV
Protein: CXXC-type zinc finger protein 1 (F7EKZ5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEGDGSDLEPPDAGEDSKSENGENAPIYCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCRECREKDPKLEIRYRHKKCRERDGSERDGSEPRDEGGGRKRPASDPELQRRAGSGTGVGAMLARGSASPHKSSPQPLVATPSQHHQQQQQQQQQQQIKRSARMCGECEACRRTEDCGHCDFCRDMKKFGGPNKIRQKCRLRQCQLRARESYKYFPSSLSPVTPSEALPRPRRPPPTQQQPQQSQKLGRIREDEGTVLSSVVKEPPEATATPEPLSDEDLALDPDLYQDFCAGAFDDHVPWMSDAEESPFLDPALRKRAVKVKHVKRREKKSEKKKEERYKRHRQKQKHKDKWKHPERADAKDPASLPQCLGPGCVRAAQPGSKYCSDDCGMKLAANRIYEILPQRIQQWQQSPCIAEEHGKKLLERIRREQQSARTRLQEMERRFHELEAIILRAKQQAVREDEENNENDSDDTDLQIFCVSCGHPINPRVALRHMERCYAKVRRLREHPLGPCTPHALRGLPDSSVMSTILRAKHTVRGSRCYVLSTHGTPKCQLMRSVGVHLYAMSLSLQVTSAACPSASVIAITAGRSFGEQKWTWSACGCGTSWTSCLSRNVMFAQP
Protein: U6 snRNA-associated Sm-like protein LSm2 (O94408)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- LSM1-LSM7 complex subunit lsm1
- LSM complex subunit lsm4
- LSM complex subunit lsm5
- Small nuclear ribonucleoprotein Sm D2
- LSM complex subunit lsm7
- LSM complex subunit lsm6
- LSM2-LSM8 complex subunit lsm8
- LSM complex subunit lsm3
- Small nuclear ribonucleoprotein F
- U4/U6 snRNA-associated-splicing factor prp24
Sequence:
MLFYSFFKTLIDTEVTVELKNDMSIRGILKSVDQFLNVKLENISVVDASKYPHMAAVKDLFIRGSVVRYVHMSSAYVDTILLADACRRDLANNKRQ
Protein: Kinesin light chain (H9G2T2)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367020}.
Interaction partners:
- Kinesin heavy chain
- PID domain-containing protein
- Kinesin 1 cargo adaptor alternative variant a
- Calsyntenin-1
- Kinesin like protein
- JNK-interacting protein
- Actin
- Kinesin light chain
- Kinesin-like protein unc-104
- Dynein heavy chain linker domain-containing protein
Sequence:
MAYCLSIPYYVEGLLIPLTVMVISLGDDITTVLKTVQQTLFALRDEHEAATRILEANLINSDSSEPSLPSEKMGLIDESLGKVMDGGDEASLLIMMDKLMQSYDVQLSKNHESIRLLRQENTWLLDELTTTQRKLQESERTVAHLEEERDHYKFQDSMNYLNSDFQHTTSVDATPMMVDTLQELGFGPEEEDQNNNQADQGCRSSSFSNPISNDYQLPTRLQTLQNLVIQYMEQGRFEVAIPLCKQALEDVVKVHGNVHLDVATMLNVLAIVYRNQENFKDAAIYLEKALSIRVQCCGENHHSVAATLNNLAIAYGKRGKYKESEPLCKRALEIRKNLLGPNHPDVAKQLTNLGIVTQQLEKYEETENYFKQALSIYNRAFPENHQNVIKTKNQLASVFLKQGKYQEAEEMYKNILSKVAITGNKPIWRIAEDREERQRNGIPKVDDESFNVNPTTVMDSNVMSTIKNLAAVYRKQGKEEAAGTLEEALGAKKQINGGADHTNSTASSVETSSAVAINPAQSGIKKRIMHFVGLNF
Protein: Splicing factor 3B subunit 10 (Q38DT6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Splicing factor 3B subunit 1, putative
- PHD finger-like domain-containing protein 5A
- G10 protein
- Spliceosome-associated protein, putative
- RNA-binding protein, putative
- Probable eukaryotic initiation factor 4A
- Pre-mRNA-processing factor 19
- Uncharacterized protein
- Splicing factor 3A, putative
- Small nuclear ribonucleoprotein E
Sequence:
MGDPFVRPGLTYQPHIEQALLKNEGTLTLECTKDDWLRYQHRDTAATIILHRDHLEYLSIVENASPVRVERMLLERAVDPTRKRDLHNT
Protein: Kelch repeat-containing protein At3g27220 (Q9LK31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- BTB/POZ domain-containing protein At2g30600
- Pentatricopeptide repeat-containing protein At1g31920
- Probable aspartyl protease At4g16563
- U-box domain-containing protein 45
- At1g14330/F14L17_7
- U-box domain-containing protein 29
- Probable CCR4-associated factor 1 homolog 5
- F-box/kelch-repeat protein At1g15670
- F-box protein PP2-A14
- Duplicated homeodomain-like superfamily protein
Sequence:
MANKPDHHHHHHQSSRRLMLVLYFTSVLGIGFIAAFLCLSSSIPSVSAVFSIWVPVNRPEIQIPIIDSKIVQKRSKQSNDTKDHVRFLSAIFADIPAPELKWEEMESAPVPRLDGYSVQINNLLYVFSGYGSLDYVHSHVDVFNFTDNKWCDRFHTPKEMANSHLGIVTDGRYVYVVSGQLGPQCRGPTSRSFVLDSFTKTWLEFPSLPAPRYAPATQIWRGRLHVMGGSKENRNAVAFDHWSIAVKDGKALDEWREEVPIPRGGPHRACVVANDKLLVIGGQEGDFMAKPNSPIFKCSRRREIFNGEVYMMDEEMKWKMLPPMPKNNSHIESAWIIVNNSIVIVGGTTDWHPVTKRLVLVGEIFRFQLDTLTWSVIGRLPYRVKTAMAGFWNGYLYFTSGQRDRGPDNPQPGKVIGEMWRTKLKF
Protein: H(+)/Cl(-) exchange transporter 5 (Chloride channel protein 5) (ClC-5) (Chloride transporter ClC-5) (P51795)
Organism: Homo sapiens (Human)
Function: Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons. Important for normal acidification of the endosome lumen. May play an important role in renal tubular function. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The absence of conserved gating glutamate residues is typical for family members that function as channels (Probable).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:19019917}; Multi-pass membrane protein {ECO:0000269|PubMed:19019917}. Endosome membrane {ECO:0000269|PubMed:19019917}; Multi-pass membrane protein {ECO:0000269|PubMed:19019917}. Cell membrane {ECO:0000269|PubMed:19019917}; Multi-pass membrane protein {ECO:0000269|PubMed:19019917}.
Interaction partners:
- Inositol polyphosphate 5-phosphatase OCRL
- Low-density lipoprotein receptor-related protein 2
- Cubilin
- Sodium-dependent phosphate transport protein 2C
- Sodium/hydrogen exchanger 3
- Cofilin-2
- Cofilin-1
- Barttin
- H
- ATP-sensitive inward rectifier potassium channel 1
Sequence:
MAMWQGAMDNRGFQQGSFSSFQNSSSDEDLMDIPATAMDFSMRDDVPPLDREVGEDKSYNGGGIGSSNRIMDFLEEPIPGVGTYDDFNTIDWVREKSRDRDRHREITNKSKESTWALIHSVSDAFSGWLLMLLIGLLSGSLAGLIDISAHWMTDLKEGICTGGFWFNHEHCCWNSEHVTFEERDKCPEWNSWSQLIISTDEGAFAYIVNYFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHCFNKYRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFYVEFHTPWHLFELVPFILLGIFGGLWGALFIRTNIAWCRKRKTTQLGKYPVIEVLVVTAITAILAFPNEYTRMSTSELISELFNDCGLLDSSKLCDYENRFNTSKGGELPDRPAGVGVYSAMWQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGVGMEQLAYYHQEWTVFNSWCSQGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADALGREGIYDAHIRLNGYPFLEAKEEFAHKTLAMDVMKPRRNDPLLTVLTQDSMTVEDVETIISETTYSGFPVVVSRESQRLVGFVLRRDLIISIENARKKQDGVVSTSIIYFTEHSPPLPPYTPPTLKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLKHIAQMANQDPDSILFN
Protein: Platelet factor 4 (PF-4) (C-X-C motif chemokine 4) (Iroplact) (Oncostatin-A) [Cleaved into: Platelet factor 4, short form (Endothelial cell growth inhibitor)] (P02776)
Organism: Homo sapiens (Human)
Function: Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.
Subcellular location: Secreted {ECO:0000269|PubMed:7644496}.
Interaction partners:
- Stromal cell-derived factor 1
- Interleukin-8
- C-X-C chemokine receptor type 3
- C-C motif chemokine 5
- C-X-C motif chemokine 11
- C-X-C motif chemokine 10
- C-X-C motif chemokine 9
- C-C motif chemokine 21
- C-C motif chemokine 20
- C-C motif chemokine 2
Sequence:
MSSAAGFCASRPGLLFLGLLLLPLVVAFASAEAEEDGDLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQAPLYKKIIKKLLES
Protein: Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (RA301) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B) (P62997)
Organism: Rattus norvegicus (Rat)
Function: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62995}.
Interaction partners:
- Serine/arginine-rich splicing factor 3
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 7
- Serine/arginine-rich splicing factor 9
- Serine/arginine-rich splicing factor 6
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein A1
- Polypyrimidine tract-binding protein 1
- Serine/arginine-rich splicing factor 2
- Heterogeneous nuclear ribonucleoprotein C
Sequence:
MSDSGEQNYGERESRSASRSGSAHGSGKSARHTPARSRSKEDSRRSRSKSRSRSESRSRSRRSSRRHYTRSRSRSRSHRRSRSRSYSRDYRRRHSHSHSPMSTRRRHVGNRANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHTPTPGIYMGRPTYGSSRRRDYYDRGYDRGYDDRDYYSRSYRGGGGGGGGWRAAQDRDQIYRRRSPSPYYSRGGYRSRSRSRSYSPRRY
Protein: Probable methyltransferase PMT2 (EC 2.1.1.-) (B9DFI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Putative nucleolar protein 5-3
- Receptor-like kinase TMK2
- SAUR-like auxin-responsive protein family
- Bidirectional sugar transporter SWEET5
Sequence:
MALKSSSADGKTRSSVQIFIVFSLCCFFYILGAWQRSGFGKGDSIALEMTNSGADCNIVPSLNFETHHAGESSLVGASEAAKVKAFEPCDGRYTDYTPCQDQRRAMTFPRDSMIYRERHCAPENEKLHCLIPAPKGYVTPFSWPKSRDYVPYANAPYKALTVEKAIQNWIQYEGDVFRFPGGGTQFPQGADKYIDQLASVIPMENGTVRTALDTGCGVASWGAYLWSRNVRAMSFAPRDSHEAQVQFALERGVPAVIGVLGTIKLPYPTRAFDMAHCSRCLIPWGANDGMYLMEVDRVLRPGGYWILSGPPINWKVNYKAWQRPKEDLQEEQRKIEEAAKLLCWEKKYEHGEIAIWQKRVNDEACRSRQDDPRANFCKTDDTDDVWYKKMEACITPYPETSSSDEVAGGELQAFPDRLNAVPPRISSGSISGVTVDAYEDDNRQWKKHVKAYKRINSLLDTGRYRNIMDMNAGFGGFAAALESQKLWVMNVVPTIAEKNRLGVVYERGLIGIYHDWCEAFSTYPRTYDLIHANHLFSLYKNKCNADDILLEMDRILRPEGAVIIRDDVDTLIKVKRIIAGMRWDAKLVDHEDGPLVPEKVLIAVKQYWVTNSTSTH
Protein: Large ribosomal subunit protein eL37B (60S ribosomal protein L37-B) (SP-L27) (P05733)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds to the 23S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL38A
- Large ribosomal subunit protein eL8
Sequence:
MTKGTQSFGMRHNKSHTICRRCGKRSFHIQKSTCACCGYPAAKTRSYNWGAKAKRRRTTGTGRMSYLKKVHRSFKNGFRSGKPAAAVAASA
Protein: Spermidine synthase (EC 2.5.1.16) (Q95Z84)
Organism: Leishmania major
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme
- Putative S-adenosylmethionine decarboxylase proenzyme-like
- ornithine decarboxylase
- Agmatinase-like protein
- S-methyl-5'-thioadenosine phosphorylase
- Trypanothione synthetase
- Arginase
- Putative nitrilase
- Deoxyhypusine hydroxylase
- Putative deoxyhypusine synthase
Sequence:
MPGPGLLPDGWFREESTMWPGQAQGLKVEKVLYDQPTEFQHLTVFESDPSGPWGTVMTLDGAIQLTDYDEFVYHEMLANLSLACHHKPERVLVIGGGDGGVVREVLRHKSEKDGVVQSVELVDIDGAVMQQSKKHFPQVACGFANPCVTATVGDGAAFVRNVPDSVYDVIIIDTTDPKGPASELFGADFYTNVLRILRPGGVVCNQGESVWLHRPLIEKMMGFLKKDIGFATVKYAMIYIPTYPCGSIGTLVCAKSADTDVTVPMRPVESLGFADQLKYYSSDMHKAAFVLPRFAAHLNE
Protein: Fructokinase-like 1, chloroplastic (PEP-associated protein 6) (pfkB-type carbohydrate kinase family protein 2) (Q9M394)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for proper chloroplast development, most likely through regulating plastid-encoded polymerase (PEP) dependent chloroplast transcription. Acts as a component of the transcriptionally active plastid chromosome that is required for plastid gene expression.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:20511297}.
Interaction partners:
- Thioredoxin-like protein CITRX, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 10
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic
- Plastid transcriptionally active 3
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 7
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14
- Protein PEP-RELATED DEVELOPMENT ARRESTED 1, chloroplastic
- PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic
- Probable inactive purple acid phosphatase 1
- Fe
Sequence:
MASLLIFPHLHHFDSSLDRREVLVVRHSQASRRFLTPKASINGSGITNGAAAETTSKPSRKGRKKKQTSTVIEKDNTETDPELNPELADYDDGIEFPYDDPPLVCCFGAVQKEFVPVVRVHDNPMHPDMYSQWKMLQWDPPEFGRAPGGPPSNVAISHVRLGGRAAFMGKVGEDDFGDELVLMMNQERVQTRAVKFDENSKTACTRVKIKFKDGKMMAETVKEPPEDSLFASELNLAVLKEARIFHFNSEVLTSPTMQSTLFTAIQWSKKFGGLIFFDLNLPLPLWRSRNETRKLIKKAWNEANIIEVSQQELEFLLDEDYYERRRNYTPQYFAEDFDQTKNRRDYYHYTPEEIKSLWHDKLKLLVVTDGTLRLHYYTPTFDGVVIGTEDVLITPFTCDRTGSGDAVVAGIMRKLTTCPEMFEDQDVMERQLRFAVAAGIIAQWTIGAVRGFPTESATQNLKEQVYVPSMW
Protein: ferroxidase (EC 1.16.3.1) (Q59PA3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Cysteine desulfurase, mitochondrial
- Iron-sulfur cluster assembly protein
- Complex 1 LYR protein domain-containing protein
- Ferrochelatase
- Adrenodoxin
- Aminotransferase class V domain-containing protein
- GrpE protein homolog
- Mitochondrial thiamine pyrophosphate carrier 1
- Iron-sulfur clusters transporter ATM1, mitochondrial
- Hsp70 family ATPase
Sequence:
MFKRFALNSAKCLSKPACTRQLIYPQTRFITKTLPTVASALRPIGSIRAYSLSTEGEAIDDKIDKLTDNEYAKVSNEYLENLSDSLEELNEDFEQVDSELSQGVLTLTLPPNGTYVINKQPPNKQIWLSSPISGPKRYDLIGGKWVTLRDGSSLTSLLEEEISTAIGQEFKFETVEQ
Protein: N-acetylglucosaminylphosphatidylinositol deacetylase (EC 3.5.1.89) (Q382X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- phosphatidylinositol N-acetylglucosaminyltransferase
- PIG-P domain-containing protein
- PhosphatidylinositolN-acetylglucosaminyltransferase subunit c, putative
- Dolichol phosphate-mannose biosynthesis regulatory protein
Sequence:
MHGALVFGFVVVFLSFLVLWQRASCVSKIHLLGDVLFVFAHPDDEAMFFSPLLDYVRRHGLNAHFLCLSNGNYSGLGTVREKELVASAEYFGVNRRSVRVVDHPDLQDGPDNLWNTEIVQREVLSYLHSVKDIRTVITFDHRGVSSHANHVAVYEGVLLAKKNLPPGILFLSLHTRDLLEKYVGILSTVGYTVGIHRCGGRRNHVILIPPTSLFTSFSAMRKHKTQLVWFRYLFVWFSSYSYVNEVKELGVA
Protein: Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPAT) (Phosphoribosylamidotransferase) (PRAT) (Q27601)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the first step (and regulatory point) of the de novo biosynthesis of purine nucleotides, where it catalyzes the transfer of glutamine amide to 5-phospho-alpha-D-ribose 1-diphosphate.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Multifunctional protein r
- Glutamate synthase
- Phosphoribosylformylglycinamidine synthase
- Glutamine synthetase 1, mitochondrial
- Bifunctional purine biosynthesis protein ATIC
- Glutamine synthetase 2 cytoplasmic
- Adenylosuccinate lyase
- glutamine--fructose-6-phosphate transaminase
- glutamine--fructose-6-phosphate transaminase
Sequence:
MSAPQQQQQSQQKQQQHVRVVEQQQVEPAEAVTSSMESESISASKELTGLTHECGVFGAIACGDWPTQMDIAHVICLGLVALQHRGQESAGIATSEGKCSKNFNVHKGMGMISTLFNDDSMKKLRGNLGIGHTRYSTAGGSGVVNCQPFEVHTTHGALALAHNGELVNNESLRREVLARGVGLSTHSDSELIAQSLCCAPEDVSELDGPNWPARIRHFMMLAPLSYSLVIMLKDKIYAVRDTYGNRPLCIGKIVPINAGHGNNLDTPADGWVVSSESCGFLSIGARYVREVEPGEIVELSRSGYRTVDIVERPDFKRMAFCIFEYVYFARGDSIFEGQMVYTVRLQCGRQLWREAPVEADIVSSVPESGTAAAHGYARESGIEFAEVLCRNRYVGRTFIQPSTRLRQLGVAKKFGALSENVAGKRLVLIDDSIVRGNTIGPIIKLLRDAGAREVHIRIASPPLQYPCYMGINIPTREELIANKLNPDQLARHVGADSLAYLSVEGLVEAVQLKHRDAGDSKSKGTGHCTACLTGEYPGGLPDELSW
Protein: Protein kinase, putative (EC 2.7.1.-) (Q384K4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNNYHIYDEIGKGRHSRVYKGRQRKSIEYYAISSIEKSQRQHVLTNVKFLRSSNHPRIIKFHNWYETNNHLWVITELCTGGDMRQVLHPESRLSEAAVRLYGGDIAEGLMYIHSRGVVYRDLKPSNVLMDSTMAMRFYDFGLSCNFPVNCGGGTIGTAMYMAPELFMKEGVPSIASDLWSFGCVLLEMRTGKPPFDADNLEELITQILTEPYHPHEELSDELNELLGKLLVKNPLERATWEDVVLSPFWQGRLHMPAAPHPPQPAFESLKQKRLASDGGKGDFVMTLEEAKKAVEWTVEVAKRNFILTQPDSDGSALICLGVYDRIDTRDLTGEGEGVRDPTSGSLIGDGNSCASPSSCVARVGCDSNAGRQGDGAAQREGDHNREMVSDIGTAVGGNAAKNSNVKQLVGGGKFSTALIDSLLSHVSDAHVRPLVMNNHIERFVEQKYDAKALGFEPLTKSQLKAYDEEQKARFVTKVYQRLSSSSLSCEDKLNVLCYFESICSESSTANFVVSSSIMTLCLNMAGHRKASSSFRATAASIMGILVRHATFIHPDLAKVNILASIVKMYAEEESSRVRRKLVACYGEFLIYIAVQQERERAVWGVDVPATFNLYRSLLNDPDDVQKHYAIKTIENLASVGNRQIALDAFVNAETISLLLSIHALPPTPTCGEYMRAAAACTALKLAMLREELIPAVLESPYLKLEAYGGVLAAPSPKLAQALLTFVNMTLVKGMVGLRHANITKLGKPDATSPFASSRLTGDKAKGVLTALSGVAEAVVRGLRNGSEHATTAMKGKTLVLFILLGCMDEQLLVRFFTSSRCVAYADGIAKDKDSYVQRCTQGFAVYLSYFFGSQLEGLTHGAPSFMMNNVPSALCNLLGTRHLSSMLQLNDKVFSSIGKCLVMVSSSSRYAAAGTNLHELVELLAQNRELVLRHRLVISSDIFPPYLSMLAESESERRFLSLRILRALIVPFGSESSRQNEEAQKEGAMLDRVMQVVAGMLGDLLKEVEPIPVHGIGLLATCGERRPKTLANLATVELIGELVRYMMRSRQSGVSSPLQLVMLALQTERGGVLMDYLAEQNFPVEVLLNILVMAVEKEVDNLLEPCCELFEHFLKQAVANPNAAALRQSVMSVAPRALETLWLPLCTSPVGTTAKSAAACVLYFTQLSPEVGQELLSDGNVQYIREVLDKCRSPGAVVCVIRTLRLILERGTKHDAQKLMPWLLGSLEAAEQDQKCGGIVALEIRGIKELLRP
Protein: Fructose-bisphosphate aldolase (FBP aldolase) (EC 4.1.2.13) (Q5B9A5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Triosephosphate isomerase
- Triosephosphate isomerase
- Enolase
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase
- ATP-dependent 6-phosphofructokinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-1,6-bisphosphatase
- Glucose-6-phosphate isomerase
- Transaldolase
Sequence:
MGVLEKLSRKTGVIVGDDVLRLFEYAQEHNFAIPAINVTSSSTVVACLEAARDQNCPVILQVSQGGAAFFAGKGVSNDGQAASIAGGIAAAHYIRSIAPSYGIPVVLHTDHCAKKLLPWLDGLLDADEAYFKQHGEPLFSSHMIDLSEEPVDYNIDTTAKYLKRAAPMKQWLEMEIGITGGEEDGVNNESVDNNSLYTQPEDILAIHNALSKISPYFSIAAGFGNVHGVYKPGNVRLHPELLSKHQAYVKEQTGSKKDKPVFFVFHGGSGSSKEEYKEAISYGVVKVNLDTDMQYAYLSGVRDYVLNKKDYLMSTVGNPDGEDKPNKKFFDPRVWIREGEKTMSKRVQVALEDFNTAGKL