wanglab/gogpt-training-data huggingface dataset:
Protein: R-type basic helix-loop-helix protein (Q948Y2)
Organism: Oryza sativa (Rice)
Interaction partners:
Sequence:
MASAPPVQEEALQPGTNHFRSRLAAAVRSISWSYTIFWSTSTSLPGVLTWNDGFYNGEVKTRKISNLEDLTADQLVLRRSEQLSELYYSLLSGECDHRARKPVAALSPEDIADTEWYYVVCMTYAFRPGQGLPGRSYASNRSVWLCNAQSADSKTFLRALLAKSASIQTIVCIPFMSGVLELGTTDPVSEDPNLVNRIVAYLKELQFPICLEVPSSTPSPDETEDADTVFDGLIEEDQMVILQGEDELGDVVVAECETNGANPETITMETDEFYSLCEELDLDLGSYQLVPTSARETVAAAAAAANDVDGVAYSHASCFVSWKRANPAEKVVAVPMTAGIESQKLLKKAVGGGTAWMSNIDDRGSVAITTTPGSNIKSHVMSERRRREKLNEMFLILKSLLPSVRKVDKASILAETITYLKVLEKRVKELESSSREPSRWRPTEIGQGKAP
Protein: Mitochondrial import inner membrane translocase subunit Tim23 (Q7T2P6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane (By similarity). Plays an essential role in early embryonic development.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O14925}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit Tim21
- Mitochondrial import inner membrane translocase subunit Tim17-B)
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit TIM22
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit tim16
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import receptor subunit TOM40 homolog)
- DnaJ
Sequence:
MDNSTPPPGGFKGGLGSIFGGGTPEYSNTELSGVPLTGMSPLSPYLNVDPRYLIQDTDEFILPTGANKTRGRFELAFFTIGGCCITGAAFGTLNGLRMGLSETRDMPWSKPRNVQILNMVTRQGASWANTLGSVALLYSVFGVAIEKARGAEDDLNTVAAGTLTGMVFKSTGGLKGVARGGLIGLAMSGLYALYNNWDHLKGKSPSHY
Protein: Growth factor receptor-bound protein 2-B (Adapter protein GRB2-B) (SH2/SH3 adapter GRB2-B) (Q6GPJ9)
Organism: Xenopus laevis (African clawed frog)
Function: Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway (By similarity). Promotes meiotic reinitiation during oocyte maturation.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Golgi apparatus {ECO:0000250}.
Interaction partners:
Sequence:
MEAIAKYDFKATADDELSFKRGDVLKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLGKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQVHGGDRATSLPQQPTFVQALFDFDPQEDGELGFRRGDFIQVVDNSDPNWWKGTCLGQTGMFPRNYVTPVNRNM
Protein: Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8) (O73885)
Organism: Gallus gallus (Chicken)
Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (By similarity). May play a role in regulating apoptosis during embryonic development.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11142}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11142}. Cell membrane {ECO:0000250|UniProtKB:P11142}. Lysosome membrane {ECO:0000250|UniProtKB:P11142}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11142}; Cytoplasmic side {ECO:0000250|UniProtKB:P11142}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. {ECO:0000250|UniProtKB:P11142}.
Interaction partners:
- Heat shock protein HSP 90-alpha
- BCL2 associated athano 1
- DnaJ heat shock protein family
- DnaJ homolog subfamily A member 1
- Stress induced phosphoprotein 1.
- Heat shock protein beta-1
- DnaJ homolog subfamily A member 1
- Heat shock cognate protein HSP 90-beta
- BAG cochaperone 2
- DnaJ homolog subfamily A member 2
Sequence:
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDSVVQSDMKHWPFTVVNDAGRPKVQVEYKGETKSFYPEEISSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQGTKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNLLIFDLGGGTFDVSILTIENGIFEVKSTAGDTHLGGEDFDNRLVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEKLNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLDSYAFNMKATVEDEKLPGKILDEDHQNILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
Protein: Ribosome-inactivating protein PMRIPt [Cleaved into: PMRIPt A chain (rRNA N-glycosidase) (EC 3.2.2.22); Linker peptide; PMRIPt B chain] (Q9M653)
Organism: Polygonatum multiflorum (Solomon's seal) (Convallaria multiflora)
Function: GalNAc-specific agglutinin. Behaves as a type-2 ribosome-inactivating protein. Inhibits mammalian ribosomes. 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 (Probable). The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity) (Probable). Involved in plant defense against insects (By similarity). Has very low cytotoxic activity against the human tumor cell lines CEM and Molt4.
Interaction partners:
Sequence:
MRVVAGILYIVVMAICGLGIQGGTLQDYPSVYFQDSTLQQDFPTIFFNILAGETYGDFIADLREIVTRTADTKNGSIPVLLNPAHPVPVRERFVKVHLTGRNGKTVILALDVTNLYVAAFSANNVAYFFRDFSALERENLFSGMLTIRLSFTSNYVSLEHKAGVGRENISLGPTPLDEACTKSLWSGTTVTEASIAKALLVVIQMVSEAARFRHIEERVRRSFTAADHDQLTFRPDGLMLSMENEWPSMSLEVQRSIEGGIFIGVVQLQDESFQPLRVDNFNTLSRYTMVALLLFRCGHPRATAGTSSTTPAAAQIIRMPVDVLAGEEYYDEETCTVGEPTRRISGLDGLCMDVRNESNNDGIPIQLWPCGAQRNQQWTFHTDGTIQSMGKCMTSNGYHPGDYVMIFNCSTAPVPDATKWVVSIDGSITNPHSGLVLTAPQAAQTTILLVVRNTHSAKQGRSVGDDVEPIVTYIVGFKYMCLQGNNENNTRVWLEDCAVDRPQQWWALYSDGTIRVDSDRSLCVTSDGHSSRDAIIILTCDGGINQRLVFNTDGTILNPNAQLVMDVRQSNVALRQIILYQPTGNPNQQWMTMITRTRPSLTS
Protein: MIP10102p (Q9VNL6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MIP13722p
- IP19120p
- FI16876p1
- Mucin 4B, isoform B
- IP19013p
- RE05851p
- Uncharacterized protein
- GEO10309p1
- MIP10846p1
- Chorion protein a at 7F, isoform A
Sequence:
MAGRRVIGLCFGIFLQVLLATAGQDRMSMLCSDDDTPACAQSRENGMYFLFANECDLRKAQRGNLMNGPLYDVTLRFCFPSCEFECSSRYQPVCGISSKSGERKTFRSRCEMLRTACISRSEWMVHRWGVCPKANAVPQISEKPPVPVPCTRIYRPVCAMYAGVKSTFSNECLVNAENIKSQRNWRIVSEGLCGEDSTKMKHSRKQKPKAKPKSDAERTKRSHRGKRLSTQAEDFQIPEDAVEIYAPSTFHTQFISQSGAMEKSYSLPARKPYVVVPPKSKRRIPTKSCVFGNEPVCGNLRGQSRTFSNVCELMEFSQKVGNAWTIAHNGACRRCDKTCPTVYQPICATRNGINHTIVNECYLERVRCKDPKSIWKLSHKGECAKSVSNPRHIYSTGKSRPTSLVPSVLYGKSTTTPRSRFRKPVRRFTTTRTPTTPYKPRQLAMTNFSATSPSLETNNRKIRKIELAAAGFSGLGASSGSNFLSSEEDAFWSSDDSWLVQKTLDNVKGLLGNKPTSLKKEHGEKYPLSYWIVPPRQTSTISTTTAAPPAKLPAILSMASTELLNLDFGNPSSAYEEADHEAMLMLTTKEGTTSTTPVPSTTTPPNITEPSTTELPTSVDVASDSAETVSEDSTTDFGETTDPTTSNDSSTSDAPQSSTTEAEELNSQTTGSESTTTVASDKLSTTTLNADYAVDESFSESSGQTSIYGLDKNSLIMRLLRARSNQNVLI
Protein: Cytochrome P450 monooxygenase helB3 (EC 1.-.-.-) (Helvolic acid biosynthesis cluster protein B3) (Q4WR20)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Interaction partners:
- Acyltransferase helD1
Sequence:
MAVATLISILFAVLALRLCYLLIHALFLSPLRHIPAPFMARVTSKRPLWHLLTGKAEIAARQDYSTFGDIYLCKPNTVYLCDPHDACTVLSSHAFRKTDMYRVFEYEGIPNVSTFTDPAQAQRRRRQLHPFFNNAYLTQMEPVMLKYGIQALKARWDAQLARHKKVEVNYRFDTQLAMFDITGALVFGREFHALETSNLVYTKWVNNTLSYMLVSHYFPWVKRVPLSWLVRGLKQSYDDLVAFSQESIAIRQADLQAGRPKPADLLQALLDAEDPDSKAPMTAREVQAESIAMLVGGSESTSSVISWVIHFLLLYPEHLQAVVAETRANFPADHTITFNESKANLPYLEACIYETLRCIPTASTSFPRVSDQAIILKGYYIPAGTEIATNKCAAHLHQPSWQDPDRFYPPRFLNQETYHETRRNMLSFAYGTRFCIGRNLAWAVMMVTLANLFKDYEVELPEDSRFGPTIVDAAGRPKIMPTKMGVATMPADPERDCRMVLSVRITE
Protein: Uncharacterized protein (Q581T6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMIGVPPEASYLLQRLSRPNKFKSYASARSFEADCADLITLWTNLPLAPGTEEGEDMQRKLVDMWSGFVKNAVSYVMSGNPLLNYRPLLEAILASSAAVESSILTAASCSSAVSTNSECVESLTKAVVDVVAKRTAEIAALIPPLDLLQQVLMFIDLLQEYYHLPGDKMKTTGNCTSLNPILLHPLILNVVKAYTKLVERCATLFVEEVAFPTYWNIGGAPSPACILVDGVHPTIYFCFTTMISLVRAYRNSGLAGDDRSCRQVIAQVWYHGSFAMIAAVETVENSEKRKRQLEIDTLHYVLFARMFREFVGEGYFAPVTRALVKLLVTVGGCVRGGAEKEEASVHVHSCTKFVDDIWNVCPIKELEWLQLGAAARVARRDGSPNDGAFVPWSKAFVRAANVEVAREVPAGWESTCFNKLM
Protein: Kinesin-like protein KIF23 (E9Q5G3)
Organism: Mus musculus (Mouse)
Function: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Midbody, Midbody ring {ECO:0000269|PubMed:19020301}. Note=Localizes to the interzone of mitotic spindles (By similarity). Detected at the midbody during later stages of mitotic cytokinesis. {ECO:0000250}.
Interaction partners:
- Rac GTPase-activating protein 1
- Protein ECT2
- Serine/threonine-protein kinase PLK1
- Abnormal spindle-like microcephaly-associated protein homolog
- Kinesin-like protein KIF11
- Protein regulator of cytokinesis 1
- Inner centromere protein
- Centrosomal protein of 55 kDa
- Chromosome-associated kinesin KIF4
- Centromere-associated protein E
Sequence:
MKSAKAKTVRKPVIKKGSQTNLKDPVGVYCRVRPLSFPDQECCVEVINSTTLQLHTPEGYRLNRNGDYKETQYSFKRVFGTHTTQKELFDVVANPLVDDLIHGKNGLLFTYGVTGSGKTYTMTGSPGSGGLLPRCLNMIFNSIGSFQAKRYVFKSNDRNSMEIQCEVDALLERQKREALPIPKTPSSKRQADPEFADMINVQEFCKAEEVDEDSVYGVFVSYIEIYNNYIYDLLEEVQFDPIKPKLPQSKTLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFSIKLVQAPLDADGDNVLQEKEQITISQLSLVDLAGSERTNRTKAEGNRLREAGNINQSLMTLRTCMEVLRENQTYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEESLQVMRFAEVTQEVEVARPVDKVICGLTPGRRYRNLPRGGPVGDEPLVPEVILQSFPPLPPCKLLDINDEETLPKLADTLEKRHHLRQLMTEDLNKKCLAFKALLKEFDNSLSNKENYVQEKLNEREKVISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELESQNQKLQRQFSDKRRLEARLQGMVTETSMKWQKECERRVAATQLEMQNKLWVKDEKLKQLKAIVTEPKPEKPERPSRERDREKIIPRSVSPSPLPLSSNNIAQISNGQQLMSQPQLHRRSNSCSSISVASCISEWEQKLSPFSTPVNVTSLARHRQQEPGQSKTCIVSDRRRGMCWTEGREMVPTFSSEIGVEEDHCRRNTPIPVRHRRSRSAGSRWVDHKPASNVQTETVMQPHVPHAITVSVANEKALAKCEKYMLTHQELASDGEIQTKVIKGDVYKTRGGGQSVQFTDIETLKQELPTGSRKRRSSTLAPAQPDGTESEWTDVETRCSVAVEMRAGSQLGPGYQHHAQPKRKKP
Protein: Oleate activated transcription factor 3 (P36023)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional inhibitor with a significantly increased number of target genes in response to oleate.
Subcellular location: Cytoplasm. Nucleus. Mitochondrion.
Interaction partners:
- Uracil catabolism protein 2
Sequence:
MGYDSQVRTKKRHRITVVCTNCKKRKSKCDRTKPCGTCVRLGDVDSCVYLTDSSGQPESSPSLNDADPLRKQSTPAERISPGFIKKRRSSQTRQDEDHWQRVRELENQSSLYYLPIHEETPFFIDLIPNGFYLETKRSADNLFGLFTDRAIENRDPYLQAMVTFRSIAIKKMMDKLGSNGNNVKNGSLPKSFEALSTFDADDERHISDDVVGKGNNFRMHQTIHKSLFNKFAQYRENNAKKFSSETILAKDYLPPLKILESEVLALFEEKIYNMIPIFDMKVLRHEITIFYQNIVEKGNPISIKHYDHMVFCIILLIIKICRLSVQFSKLTPYIYPVLQEIDTSKFLALVKHYLFETKVLRKCNLLQLQCLILLRFLHWCAPEDGDGPETQYCQILMGTIISSCKEMGINWYCFSHPEKYSFKINRHTRPSYDIMKPSDYISVFRKIWSYVLFWDRKMCFISGEECQIGKTLQCHFKEEADTPTWYIRMLTLDNLMKKINDTLNDDPGKVDLNLLHRLINDLKRNFHILKSLSKNEKETMRHFDFEMEWIIDLFSLSLLHGEMIFYEYDCNITKFYKSFQDLWDMVIHISEKCYNYFFNSDALEVDSLTKFYTNRIVEIVANKVLVIVPAFILRGDRFKTIQYADKKKMIEFLYGVSSVYFNEFGFEYYRCFRKMFTAKIAYKILNRSCEKDAWRIILKFLLNELKLEDNGDSYIDYNDMRLNDICPIILEFQETVQKYDGYRPDILSIWNNEFYPIGKYNDDMTGFKFQMRIKEMQEFLDMEKYSDRFNIFSSFYDHASSQLAKHTEVDTNISITNEQVAEIPQKELLQQPLAPALPVNDLIVSEFDVIEDIFDPVDFVSFF
Protein: Large ribosomal subunit protein uL2m (39S ribosomal protein L2, mitochondrial) (L2mt) (MRP-L2) (Q2TA12)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279069, ECO:0000269|PubMed:11551941, ECO:0000269|PubMed:16510155}.
Interaction partners:
- Small ribosomal subunit protein uS7m
- Large ribosomal subunit protein bL21m
- Ribosomal protein
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS5m
- Large ribosomal subunit protein uL13m
Sequence:
MALRVVTRALGSLSLTPRIAAVPGPSLLPAAQVTNNVLLQLPSASMLLPSRPLLTSVALSAKFVSWKSRTKYTTMPVKMRKSGGRNHTGRIQVHGIGGGHKQRYRMIDFLRFRPEQESKPGPFEEKVIVVRYDPCRSADIALVAGGNRKRWIIATENMKAGDTILNSDHIGRMAVAAREGDAHPLGALPVGTLINNVESEPGRGAQYIRAAGTCGVLLRKVNGTAIIQLPSKRQMQVLETCTATVGRVSNVDHNKRVIGKAGRNRWLGKRPNSGRWHRKGGWAGRKIRPLPPMKSYVKLPSAAAQN
Protein: GH04589p (Q8MR68)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
FQLGSSHPIQYVYALFIYLFIYNQLLSSPMAAAQVEMHAAPAAPHVDRNPSSDWRQWCRLCAKDDVQGNLNVFLKNEDSGEAASMELATAIGKYFWVNITRGEELPETICSECLSLVTSLVNFSERITRVQKLYCILQSTPSQERPNLHELRSKFGLLDEETQTEVHYVDKKPKLDEQLEFLPEESPYELANPLTPEEKQESVDQEQDQPTEEPDEQDADYEPNEDRVLMSLCDVYGIQEDNSSAGSLDGSSPSTEKAGEDAADSEKRHQCNECLRSYATSKTLQRHLRQDHGQTEPTTEQLQCPDCPKKFRLHYQLERHMKWHVPLPKRKQYACSSCDKKFATSASAQQHEQYMHLDERPRPVICEQCGVGVHSMSALKEHVLKHTDYAPFECEVCKKCFKSANRLKHHKETHDPHKYICPECGMQLNSRTTLNRHRLVHTDQMQHKCDYCGREFKRAKALKNHLILHTGLKPYSCDFCDRTFANGSNCRTHKKKSHPEELAAQEAAGGGRSHNRNIPKLEALKAFTKNKDNLSPVATKQSGCFAFGKKPRPATKDTPASNPAVIQDAQPEPAPDPGGENATQADTPAAAIPTLDNIYNHIMIDYR
Protein: Carotenoid cleavage dioxygenase 8 homolog B, chloroplastic (OsCCD8b) (EC 1.13.11.69) (EC 1.13.11.70) (Protein DWARF-10) (Protein MAX4 homolog) (Q8LIY8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in strigolactones biosynthesis by cleaving the C(27) 9-cis-10'-apo-beta-carotenal produced by CCD7. Produces the C(19) carlactone and a C(8) hydroxyaldehyde. Also shows lower activity with all-trans-10'-apo-beta-carotenal producing a C(9) dialdehyde and the C(18) 13-apo-beta-carotenone. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signal that stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17655651}.
Interaction partners:
- Carotenoid cleavage dioxygenase 7, chloroplastic
- Beta-carotene isomerase D27, chloroplastic
- Carotenoid cleavage dioxygenase 8 homolog A, chloroplastic
Sequence:
MSPAMLQASSLCVSAALSGAASRPGRLASQGHQGKRAVAQPLAASAVTEAAPPAPVVAPPARPVDAPRRRGGRGGGGGGGELVAWKSVRQERWEGALEVDGELPLWLDGTYLRNGPGLWNLGDYGFRHLFDGYATLVRVSFRGGRAVGAHRQIESEAYKAARAHGKVCYREFSEVPKPDNFLSYVGQLATLFSGSSLTDNSNTGVVMLGDGRVLCLTETIKGSIQVDPDTLDTVGKFQYTDKLGGLIHSAHPIVTDTEFWTLIPDLIRPGYVVARMDAGSNERQFVGRVDCRGGPAPGWVHSFPVTEHYVVVPEMPLRYCAKNLLRAEPTPLYKFEWHLESGSYMHVMCKASGKIVASVEVPPFVTFHFINAYEETDEEGRVTAIIADCCEHNANTAILDKLRLHNLRSSSGQDVLPDARVGRFRIPLDGSQFGELETALDPEEHGRGMDMCSINPAHVGREYRYAYACGARRPCNFPNTLTKVDLVERTAKNWHEEGSVPSEPFFVPRPGATEEDDGVAISMVSAKDGSGYALVLDGKTFEEVARAKFPYGLPYGLHCCWVPRKRNSK
Protein: TIM-barrel domain-containing protein (Q2U2K2)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Uncharacterized protein
Sequence:
MPRPTTRQEVLDRLRKTVADGKIIVGAGAGIGLTAKFIEKGGADLILVYNSGRFRMAGRGSLAGMMPYSDANQVVVEMASEVLPIVENTPVLAGVCGTDPFRDMRTFLTELRRLGFIGVQNFPTVGLIDGKFRQNLEETGMGYDREVEMIRIAHEMDLVTTPYAFTVDEGERMARAGADIIVVHVGLTTSGTIGAQTALSLDDCVTIIQEIRDAVVKINPEIIVLCHGGPLAGPKDAEYVLKRTKGVHGFYGASSMERLPVEMAIQENAEAFKKLQVNV
Protein: Ribosome biogenesis protein ALB1 (P47019)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With ARX1, involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Probable metalloprotease ARX1
- Nucleolar GTP-binding protein 2
- Nucleolar GTP-binding protein 1
- Nuclear GTP-binding protein NUG1
- Ribosome biogenesis protein RLP24
- Ribosome assembly factor MRT4
- Ribosome biogenesis protein RPF2
- Ribosome assembly protein 4
- Ribosome biogenesis protein NSA2
- Pre-rRNA-processing protein IPI3
Sequence:
MPSKNSINRPKLTSNLHHKVHSLNKKRAQRERAGLLKPARSSVNSKSGEIKSVALDLYFQNKKNESQNSTAVTLQNASSSPASITTRTLSKKRAKKIERNLKYATQRKLLVDASAKLEDEMDIDLDGGKKVKENEKKSSLTLVKEALWSVIDDTASQGLIIENGQGTTLGGPFFP
Protein: Microtubule-associated protein, putative (Q389U1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
Sequence:
MPGTKGLEADYKWNDPQPYPQRDKERAEVYDCIDIKNKKKSLPHNTENLYMKQQKANKQNYKEILSTMKESYAPIDPAAYKRDMLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDMLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEATGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEATGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESHAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTEESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEATGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEATGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEATGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEATGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEATGPRHVDPSHLRSTTAESYAPIDPAAYKRDVLREEEEATGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHFRSTTAESYAPIDPAAYKRDVLREEEEVTGPRHVDPSHSRSTTAESYAPIDPAAYKRDVLREEVVKVSRRGGDDGHFRTTAKDSYCRYDSSCYKSSCRESSFGDESVMSMRHSFTASSEADAIVVKKVVKGKSDGGVTSKKVDVFTDMKCVASGESNGGAAAAVAATTECAAAAVGDQPTGNGVRVSKWKKAPNVGYSCPCHVDADMYVSTAHRDFKAHGASKPYMPKAAPTVKQSSISMQGVSSEYRNRFIRPEVQCPPRPIGKPAVQVRHVDPSMYVTTNRATFVNHSGRKV
Protein: DNA repair protein RAD5 (EC 3.6.4.-) (Radiation sensitivity protein 5) (Revertibility protein 2) (P32849)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. Seems to be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. Recruits the UBC13-MMS2 dimer to chromatin for DNA repair.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 13
- Ubiquitin-conjugating enzyme variant MMS2
- Postreplication repair E3 ubiquitin-protein ligase RAD18
- ATP-dependent DNA helicase SRS2
- DNA repair protein REV1
- DNA polymerase zeta catalytic subunit
- Ubiquitin-conjugating enzyme E2 2
- DNA repair protein RAD51
- DNA polymerase eta
- Proliferating cell nuclear antigen
Sequence:
MSHIEQEERKRFFNDDLDTSETSLNFKSENKESFLFANSHNDDDDDVVVSVSDTTEGEGDRSIVPVRREIEEEGQNQFITELLRIIPEMPKDLVMELNEKFGSQEEGLSLALSHYFDHNSGTSISKIPSSPNQLNTLSDTSNSTLSPSSFHPKRRRIYGFRNQTRLEDKVTWKRFIGALQVTGMATRPTVRPLKYGSQMKLKRSSEEISATKVYDSRGRKKASMASLVRIFDIQYDREIGRVSEDIAQILYPLLSSHEISFEVTLIFCDNKRLSIGDSFILQLDCFLTSLIFEERNDGESLMKRRRTEGGNKREKDNGNFGRTLTETDEELESRSKRLALLKLFDKLRLKPILDEQKALEKHKIELNSDPEIIDLDNDEICSNQVTEVHNNLRDTQHEEETMNLNQLKTFYKAAQSSESLKSLPETEPSRDVFKLELRNYQKQGLTWMLRREQEFAKAASDGEASETGANMINPLWKQFKWPNDMSWAAQNLQQDHVNVEDGIFFYANLHSGEFSLAKPILKTMIKGGILSDEMGLGKTVAAYSLVLSCPHDSDVVDKKLFDIENTAVSDNLPSTWQDNKKPYASKTTLIVVPMSLLTQWSNEFTKANNSPDMYHEVYYGGNVSSLKTLLTKTKTPPTVVLTTYGIVQNEWTKHSKGRMTDEDVNISSGLFSVNFYRIIIDEGHNIRNRTTVTSKAVMALQGKCKWVLTGTPIINRLDDLYSLVKFLELDPWRQINYWKTFVSTPFESKNYKQAFDVVNAILEPVLLRRTKQMKDKDGKPLVELPPKEVVIKRLPFSKSQDLLYKFLLDKAEVSVKSGIARGDLLKKYSTILVHILRLRQVCCHPGLIGSQDENDEDLSKNNKLVTEQTVELDSLMRVVSERFDNSFSKEELDAMIQRLKVKYPDNKSFQSLECSICTTEPMDLDKALFTECGHSFCEKCLFEYIEFQNSKNLGLKCPNCRNQIDACRLLALVQTNSNSKNLEFKPYSPASKSSKITALLKELQLLQDSSAGEQVVIFSQFSTYLDILEKELTHTFSKDVAKIYKFDGRLSLKERTSVLADFAVKDYSRQKILLLSLKAGGVGLNLTCASHAYMMDPWWSPSMEDQAIDRLHRIGQTNSVKVMRFIIQDSIEEKMLRIQEKKRTIGEAMDTDEDERRKRRIEEIQMLFE