wanglab/gogpt-training-data huggingface dataset:
Protein: Proteasome subunit alpha type-3 (Proteasome subunit alpha 7) (Q09583)
Organism: Caenorhabditis elegans
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta
- Probable 26S proteasome regulatory subunit 10B
- Proteasome subunit alpha type-2
- Proteasome subunit beta
- Proteasome subunit alpha type-4
- Proteasome subunit beta
- Proteasome subunit beta type-3
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-5
Sequence:
MSSIGTGYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDGFALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTLGISRPFGAGAFFMSWNKQTGGRLFLVEPSGLNYEYKAWAVGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNVQIEMGWVGEQTNGKYEEVPSEVVTAAEEWAIAKLDEDDMDD
Protein: Serine/threonine-protein kinase Nek3 (EC 2.7.11.1) (HSPK 36) (Never in mitosis A-related kinase 3) (NimA-related protein kinase 3) (P51956)
Organism: Homo sapiens (Human)
Function: Protein kinase which influences neuronal morphogenesis and polarity through effects on microtubules. Regulates microtubule acetylation in neurons. Contributes to prolactin-mediated phosphorylation of PXN and VAV2. Implicated in prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells through mechanisms involving RAC1 activation and phosphorylation of PXN and VAV2.
Subcellular location: Cytoplasm {ECO:0000250}. Cell projection, axon {ECO:0000250}.
Interaction partners:
- Putative tyrosine-protein phosphatase TPTE
Sequence:
MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGIVARLVQKCLPPEIIMEYGEEVLEEIKNSKHNTPRKKTNPSRIRIALGNEASTVQEEEQDRKGSHTDLESINENLVESALRRVNREEKGNKSVHLRKASSPNLHRRQWEKNVPNTALTALENASILTSSLTAEDDRGGSVIKYSKNTTRKQWLKETPDTLLNILKNADLSLAFQTYTIYRPGSEGFLKGPLSEETEASDSVDGGHDSVILDPERLEPGLDEEDTDFEEEDDNPDWVSELKKRAGWQGLCDR
Protein: T. brucei spp.-specific protein (Q389C7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRATADKHVSFASELVTASWATANSKTRERNTTSRCGEYPTDGMSLALFHSGSLALQAVDSLRLELELPLVARYRVVNYLWRHCYQSWQEENAATLPPRPASVEHSVDEYLRICRCDGGMAGAISSTSLKLVDGITLHRLTYLADDAGHLHPYSRRLDPVTRPIVRFLRQTCTLQLSRRQNNIICLLPKLVEIIIILCYKLELSAQRYGQWRLPPRHLTSEGRNYRKKGSGGKSEREGGDFSLSRLTHTCNSRSSVSLSWTSRCTWWLARACQRASARPHRLFAHLRALLLDPGPMCHVKAGYLQFLALRFFPDLPSIQYPVATFHPETFVWKSEDGSANGLEETGKTHTLQESLNHKVKLKISPHSNSK
Protein: Autophagy-related 16, isoform F (B7Z0R7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ubiquitin-like-conjugating enzyme ATG3
- Autophagy protein 12-like
- Autophagy protein 5
- Autophagy-related 18b, isoform A
- Autophagy-related 18a, isoform E
- RB1-inducible coiled-coil protein 1
- Autophagy-related 1, isoform B
- Ubiquitin-like modifier-activating enzyme ATG7
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Autophagy-related 8b, isoform A
Sequence:
MSTEEHVWRAHVVRRLRERNRKECDNFKEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAVSTGGTGSNVAIATLEKKLLSQQEELTELHKRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLLERLMQYKSKDADKLNEENESIIRKRLPSIFRKRSAKLKRDLEDAVREPSSSSNAASSPGAASLQRNSSPAQFVGGLIGDEDFDEAAINGAMEAIGLDDNEYISARFTAGEIAENSRASIDTLKATGYLGQANPTKILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIGKNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARVWTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIETKFAGSSCNDLVTTDSLGSTIISGHYDKKIRFWDIRTEKQADDVLMPAKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNEHFKISCDFARASFNSSGLKIACGSADGAIYIWNVNGFLEATLKGHSTAVNAVSWSPNNNMLASVGKNKRCTIYSES
Protein: Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase) (P75089)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Enolase
- Glucose-6-phosphate isomerase
- PTS system fructose-specific EIIABC component
- Probable ATP-dependent 6-phosphofructokinase
- Transketolase
- Putative 1-phosphofructokinase
- PTS system glucose-specific EIICBA component
- L-lactate dehydrogenase
Sequence:
MLVNIKQMLQHAKQHHYAVPHININNYEWAKAVLTAAQQAKSPIIVSTSEGALKYISGHQVVVPMVKGLVDALKITVPVALHLDHGSYEGCKAALQAGFSSIMFDGSHLPFQENFTKSKELIELAKQTNASVELEVGTLGGEEDGIVGQGELANIEECKQIATLKPDALAAGIGNIHGLYPDNWKGLNYELIEAIAKATNLPLVLHGGSGIPEADVKKAIGLGISKLNINTECQLAFAKAIREYVEAKKDLDTHNKGYDPRKLLKSPTQAIVDCCLEKMQLCGSTNKA
Protein: G-protein coupled receptor 37-like 1 (Endothelin B receptor-like protein 2) (ETBR-LP-2) (O60883)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor. Has been shown to bind the neuroprotective and glioprotective factor prosaposin (PSAP), leading to endocytosis followed by an ERK phosphorylation cascade. However, other studies have shown that prosaposin does not increase activity. It has been suggested that GPR37L1 is a constitutively active receptor which signals through the guanine nucleotide-binding protein G(s) subunit alpha. Participates in the regulation of postnatal cerebellar development by modulating the Shh pathway (By similarity). Regulates baseline blood pressure in females and protects against cardiovascular stress in males (By similarity). Mediates inhibition of astrocyte glutamate transporters and reduction in neuronal N-methyl-D-aspartate receptor activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:28688853}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q99JG2}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with the basal membrane of Bergmann glia cell primary cilia. {ECO:0000250|UniProtKB:Q99JG2}.
Interaction partners:
- Prosaposin
- B1 bradykinin receptor
- B2 bradykinin receptor
- Prosaposin receptor GPR37
Sequence:
MRWLWPLAVSLAVILAVGLSRVSGGAPLHLGRHRAETQEQQSRSKRGTEDEEAKGVQQYVPEEWAEYPRPIHPAGLQPTKPLVATSPNPGKDGGTPDSGQELRGNLTGAPGQRLQIQNPLYPVTESSYSAYAIMLLALVVFAVGIVGNLSVMCIVWHSYYLKSAWNSILASLALWDFLVLFFCLPIVIFNEITKQRLLGDVSCRAVPFMEVSSLGVTTFSLCALGIDRFHVATSTLPKVRPIERCQSILAKLAVIWVGSMTLAVPELLLWQLAQEPAPTMGTLDSCIMKPSASLPESLYSLVMTYQNARMWWYFGCYFCLPILFTVTCQLVTWRVRGPPGRKSECRASKHEQCESQLNSTVVGLTVVYAFCTLPENVCNIVVAYLSTELTRQTLDLLGLINQFSTFFKGAITPVLLLCICRPLGQAFLDCCCCCCCEECGGASEASAANGSDNKLKTEVSSSIYFHKPRESPPLLPLGTPC
Protein: Rho-type guanine nucleotide exchange factor, isoform A (Rho-type guanine nucleotide exchange factor, isoform B) (Q9VIN1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}.
Interaction partners:
Sequence:
MDQPLVVQAEYSFMGSNNDELCFQKGDVITVTQREDGGWWEGTLNDKTGWFPSNYVNECKVQLPLTETIRPPEEIQEYRSVVLKDLLDSERAHVAELQGLLENFLEPMQQTQILSQDEYAQLMCNFVEIVRTHEDLLIQIEECNDRVGKLFLTSAPLMKKVHQAYCAAHPKAIVILDKYKDELEKYMERQGAATPGLLVLTTGLSKPFRRLDKYSAMLQELERHMESSHPDRGDTQRSVAVYKDIAATCSATRRQKELELQVLTGPVRGWQGQELSTLGDIIHMGSVAVGADHRDRYFVLFPQTLLFLSVSQRMSAFIYEGKLPLTGIIVNRLEDTDALKNAFEISSPLIDRIVAVCQGPNEANKWVELLNANNPSLPMGIKRQLSNLSNSSLGHLNAAHMSPPSSHILLPPGGRPPATPSSIPAGSSSGGSHSHQGSPATNSMSHHKRSQSFNHHLSYNQYTPTQPPPHHLHPPQPPSLPSHLGASGPRSSSAQTPNSKTAAPLQASSMDASPAIQAAAAAAAAAVGMGVPSARKGSTKANWTISCLRPTPPLRPSLLNATSGSGSGSGGSGGGGSSSSNALASYCSGRKNQPTYEEDALVLRVFEAYCAAYQNNARNTIHSGLENEDMTPTLRQLWTAIRQMQQDMSQIKLQINEERALRADLQQLLMQHLETSSVSSGANTPKC
Protein: SCP domain-containing protein (Q8MQ33)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNYLLTALIALLAPISVAYNVPHGFLTGEAVTSHSGPNDLDGELPATDEVKREKRGYFFPSHFQSDSGLLSRSEHPNEYLKKWITHEHNRYRRMVPASDMNMLYWSDELAASAQRHADTCDFRHSRGRINVGENIWAAPYSNYSDAISIWFNEVHNPRCGCNHAYKHCCGHYVQVVWAKTNLVGCGFSRCRDVQGVWGRGHRNVFVCHYNPQMPAFTWASGDNGKCSNCPANAPACYQGLCYMPKNYEAPTTTTESTTTSTTTEEPTTTCEPDEPEAEGADNNQEEEEENNDGFRMRV
Protein: Coiled-coil domain-containing protein 78 (xCCDC78) (Q66KE8)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for cep152 localization to the deuterosome.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:24075808}. Note=Localizes to centrioles and deuterosome.
Interaction partners:
Sequence:
MDSTEDRETPLKDQIRRLTNENVQLQDRNERLYAKLGELQDKMGKLAGSKTDLSSKLVLSEEEKLKISKELIELQIETNKIREHYEAETFELKNTILTLENRLMSLELQKEKLAGEHESVKERLQAVDANRKELADEYIVLKSNYLALSKEHEKEVAKNDELSMELLNLASRRGQDETYSQSRALVNEATAELDRVKAMVNRLSARNIKPEDLVATEYERQKLERNLLGNQDHIREEIENMKKIHETQQQRLEERIIAMGKELQEAKRAIRNTQHKMAEQSAVLLTSQSQLQETEAQNSHLQLQLKELNEEYRSRLNRYIQDLADYVDGTARSKGDGTRMKHFVDNMLSDIKASHRSREEQLAGAARQYKKRMQNLIKKHQSLLIAYRMQREQLLASGNQDVEPGPPEHHFTITDPELQSQVGLELNRLREDKARLETQIHDLKEKKRLSDAGTSNQHVEHGGKLQEESWAEIRKQLREFTHNTQEELERERSQLLSRALVAEEQVAELQDYVDKHLARYKQEILRLRKLLGNEEQRAVSADAPQSLLIRALRRNSHEM
Protein: UBE2C protein (Ubiquitin-conjugating enzyme E2C) (Q5TZN3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLFKWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP
Protein: F-box protein KIB2 (Protein KINK SUPPRESSED IN BZR1-1D 2) (Q9SU04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Required for brassinosteroid (BR) signal transduction. Mediates ASK7/BIN2/SK21 inactivation both by competing with substrate binding (e.g. BZR1) and by promoting its ubiquitination and subsequent proteasomal degradation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9SU05}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9SU05}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
Sequence:
MAPLNSQAAGEEESNYQCRFPRFMHLSWKRPYLTRVFDLAVIQKKQKKEMSDSEEKKCNDDSKQPVLVLDLLRSILERLSFVDFHRGRCISLEWYSASESCLAVKNPTSPWIILFPSENVESKNDSCKLYNPRDHSSYIVRDLGFDLARSRCLASSGSWFLMLDHRTDFHILNLFTRVRIPLPPLESTGDGNVFKRVYENVSDGSCIKIDNAVLWVDEKRRDYLVVWNISRLFGYHKKGDENYSWKVFKPLKKNDCCIDMAFKENKLYVLSVTRKVTVYDFSGGDSPVKCATFPSLRFRNGYSYNTQGCHYKVAVTLSGEVLIIVAKVEPYPRVECFFAVYKMDHNSSGYERISLGGEALLLDLGITVEANCMKNCIYFSNDQFHRYNGKSLCDDSNKNGICVYHIRSRYVVQVFEHLTASSKIAFKDARSFFPIFGGKWLL
Protein: Syntaxin-1A (Neuron-specific antigen HPC-1) (Q16623)
Organism: Homo sapiens (Human)
Function: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis. Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion. Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm. Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:O35526}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:O35526}. Synapse, synaptosome {ECO:0000250|UniProtKB:O35526}. Cell membrane {ECO:0000250|UniProtKB:P32851}. Note=Colocalizes with KCNB1 at the cell membrane. {ECO:0000250|UniProtKB:P32851}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- Complexin-1
- Vesicle-associated membrane protein 3
- Synaptotagmin-1
- Vesicle-associated membrane protein 2
- Synaptosomal-associated protein 23
- Syntaxin-binding protein 1
- Synaptosomal-associated protein 25
- Syntaxin-binding protein 5
- Vesicle-associated membrane protein 1
- Sodium-dependent dopamine transporter
Sequence:
MKDRTQELRTAKDSDDDDDVAVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIVIASTVGGIFA
Protein: Abscisic acid receptor PYL4 (ABI1-binding protein 2) (PYR1-like protein 4) (Regulatory components of ABA receptor 10) (O80920)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA. Can be activated by both (-)-ABA and (+)-ABA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus {ECO:0000269|PubMed:25465408}. Cell membrane {ECO:0000269|PubMed:25330042, ECO:0000269|PubMed:25465408}. Vacuole {ECO:0000269|PubMed:27495812}. Note=Localizes at the plasma membrane in the presence of a CAR protein (e.g. CAR1) (PubMed:25465408). Localized transiently in the vacuole when in complex with RSL1 (PubMed:27495812). {ECO:0000269|PubMed:25465408, ECO:0000269|PubMed:27495812}.
Interaction partners:
- Protein phosphatase 2C 16
- Protein phosphatase 2C 56
- Protein phosphatase 2C 37
- Protein phosphatase 2C 77
- Probable protein phosphatase 2C 78
- DET1- and DDB1-associated protein 1
- Protein phosphatase 2C 7
- Probable protein phosphatase 2C 24
- Probable protein phosphatase 2C 75
- Protein phosphatase 2C 3
Sequence:
MLAVHRPSSAVSDGDSVQIPMMIASFQKRFPSLSRDSTAARFHTHEVGPNQCCSAVIQEISAPISTVWSVVRRFDNPQAYKHFLKSCSVIGGDGDNVGSLRQVHVVSGLPAASSTERLDILDDERHVISFSVVGGDHRLSNYRSVTTLHPSPISGTVVVESYVVDVPPGNTKEETCDFVDVIVRCNLQSLAKIAENTAAESKKKMSL
Protein: Zygotic DNA replication licensing factor mcm3 (EC 3.6.4.12) (Zygotic minichromosome maintenance protein 3) (zMCM3) (Q7ZXZ0)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P49739}. Chromosome {ECO:0000250|UniProtKB:P49739}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000250|UniProtKB:P49739}.
Interaction partners:
Sequence:
MAAVTELDDQEMREAQREYLDFLDDEEDQGIYQSKVRDMISENQYRLIVNINDLRRKNEKRASLLMNNAFEGLIAFQRALKDFVASIDGTYAKQYEDFYIGLEGSFGSKHVTPRTLTSRFLSSVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERKYTDLTSLEAFPSSAVYPTKDEENNPLETEYGLSIYKDHQTITIQEMPEKAPAGQLPRSVDIILDDDLVDKVKPGDRVQVIGTYRCLPSKQNGYTSASFRTILIACNVIQMSKEVTPVFSADDLAKIKKFSKSHSKDVFEQLSRSLAPSIHGHSYIKKAILCMLLGGVEKVLDNGTRIRGDINVLLIGDPSVAKSQLLRYVLFTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEHDREISDHVLRMHRYRSAGEQDGDALPLGSAVDILATEDPNVTSEEQQELQVYEKHDSLLHGVKKRREKVLSMEFMRKYIHVAKIFKPVLTQEAASFIAEEYTRLRNQDQMSTDVARTSPVTARSLETLIRLSTAHAKVRMSKTVQLQDAEAALELVQYAYFKKVLEKEKKRRRREGESDTEEEQTQPDGEGKKRRKKRRAQDGESHDPYEFSDTEDETPVVHTPKTPVNGQEEMETDSSAKPGLSGDRLKAFKSALLDAFKAAHAQSIAMAAMMEAINKNNDSPFSQAEVKAALELMEEANHIMVSDNIVFLI
Protein: ATPase family gene 2 protein (EC 3.6.4.10) (Diazaborine resistance gene 1 protein) (P32794)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent chaperone which uses the energy provided by ATP hydrolysis to generate mechanical force to disassemble protein complexes. Plays an essential role in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RLP24 from the pre-ribosomal particles. This step facilitates the subsequent release of other shuttling proteins such as NOG1 and allows the transition of the pre-ribosomal particles to later maturation forms that bind REI1. Essential for viability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17646390}.
Interaction partners:
- Ribosome biogenesis protein RLP24
- Probable metalloprotease ARX1
- Nucleolar GTP-binding protein 1
- Bud site selection protein 20
- Eukaryotic translation initiation factor 6
- Ribosome assembly factor MRT4
- Ribosome biogenesis protein NSA2
- Nucleolar GTP-binding protein 2
- Large ribosomal subunit protein uL23
- Cytoplasmic 60S subunit biogenesis factor REI1
Sequence:
MAPKSSSSGSKKKSSASSNSADAKASKFKLPAEFITRPHPSKDHGKETCTAYIHPNVLSSLEINPGSFCTVGKIGENGILVIARAGDEEVHPVNVITLSTTIRSVGNLILGDRLELKKAQVQPPYATKVTVGSLQGYNILECMEEKVIQKLLDDSGVIMPGMIFQNLKTKAGDESIDVVITDASDDSLPDVSQLDLNMDDMYGGLDNLFYLSPPFIFRKGSTHITFSKETQANRKYNLPEPLSYAAVGGLDKEIESLKSAIEIPLHQPTLFSSFGVSPPRGILLHGPPGTGKTMLLRVVANTSNAHVLTINGPSIVSKYLGETEAALRDIFNEARKYQPSIIFIDEIDSIAPNRANDDSGEVESRVVATLLTLMDGMGAAGKVVVIAATNRPNSVDPALRRPGRFDQEVEIGIPDVDARFDILTKQFSRMSSDRHVLDSEAIKYIASKTHGYVGADLTALCRESVMKTIQRGLGTDANIDKFSLKVTLKDVESAMVDIRPSAMREIFLEMPKVYWSDIGGQEELKTKMKEMIQLPLEASETFARLGISAPKGVLLYGPPGCSKTLTAKALATESGINFLAVKGPEIFNKYVGESERAIREIFRKARSAAPSIIFFDEIDALSPDRDGSSTSAANHVLTSLLNEIDGVEELKGVVIVAATNRPDEIDAALLRPGRLDRHIYVGPPDVNARLEILKKCTKKFNTEESGVDLHELADRTEGYSGAEVVLLCQEAGLAAIMEDLDVAKVELRHFEKAFKGIARGITPEMLSYYEEFALRSGSSS
Protein: ADP-ribosylation factor-like protein 11 (Q6P3A9)
Organism: Mus musculus (Mouse)
Function: May play a role in apoptosis. May act as a tumor suppressor (By similarity).
Interaction partners:
- Hypoxia-inducible factor 1-alpha inhibitor
Sequence:
MGSVNSRGHKAEAQVVMMGLDSAGKTTILYKLKGNQLVDTLPTVGFNVEPLEAPGHVSLTLWDIGGQTQLRATWKDYLEGIDLLVYVLDSTDEARLPEAVAELKEVLEDPNMAGVPFLVLANKQEAPGALPLLEIRNRLGLEGFQKHCWELRACSALTGQGLQEALQSLLHLLKSR
Protein: hydroxyacylglutathione hydrolase (EC 3.1.2.6) (Glyoxalase II) (Q8IPU3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- LD44179p
- Uncharacterized protein, isoform B
- IP08061p
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
Sequence:
MLASAWRSVATSVETQLTATYFRGSSSNPTLLLRSWRTIPRADAPGFGAIRRRFLAVPVICPSLVKLQKLRKVGFRGMHSTLEDVQLEGMEIKILPALQDNYMYLIVDTKTREAAVVDPVEPELVIKTVQEQQLTLSKVLTTHHHWDHAGGNEKLLKLWEKELDVYGGDDRIGALNKKVQQDDTFTIGGLHVKCLSTPCHTTGHICYHITAQQGSGEGAVFTGDTLFQGGCGRFFEGTPEEMYEALCTKLSALPDATKVFCGHEYTLQNMSFARHVEPDNEVIQQRIEWAKHRRASQDPTVPSTIGEEKSWNPFMRVHEATVQKHAGGATDPVVTMGKLRKEKDTFKA
Protein: DNA-directed RNA polymerase II subunit RPB7 (RNA polymerase II subunit B7) (DNA-directed RNA polymerase II subunit G) (P62489)
Organism: Rattus norvegicus (Rat)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA. Binds RNA (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62487}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase subunit beta
- RNA polymerase II subunit J
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- Transcription elongation factor SPT5
- General transcription factor IIE subunit 1
Sequence:
MFYHISLEHEILLHPRYFGPNLLNTVKQKLFTEVEGTCTGKYGFVIAVTTIDNIGAGVIQPGRGFVLYPVKYKAIVFRPFKGEVVDAVVTQVNKVGLFTEIGPMSCFISRHSIPSEMEFDPNSNPPCYKTMDEDIVIQQDDEIRLKIVGTRVDKNDIFAIGSLMDDYLGLVS
Protein: Chromosome 19 open reading frame 47 (J3QS80)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEMEGKYVINMPKGTTPRTRKILEQQQAAKGLHRTSVFDRLGAETKADTTTGSKPTGVFSRLGATPETDEDLAWDSDNDSSSSVLQYAGVLKKLGRGPAKASPQPALTVKAKATSSATTAAAPTLRRLALSSRSGLERKPESLSKVSIIKRLGAAALVPEAQDSQASA
Protein: MYCN proto-oncogene, bHLH transcription factor (A0A1W2PPD9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRGAPGNCVGAEQALARRKRAQTVAIRGHPRPPGPPGDTRAESPPDPLQSAGDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC
Protein: Retinal homeobox protein Rx2 (O42357)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a critical role in eye formation by regulating the initial specification of retinal cells and/or their subsequent proliferation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}.
Interaction partners:
- Homeobox protein SIX6b
Sequence:
MHLSPDTMNMVDDGCLSTESYHDLGKGGVSGISGRVHSIDVILGFSKDQDPLLEPSGRHKVDEDQLEEQEKQVNADPYSHLQIPDQTQQQQSVYHDTGLFSTDKCDADLGDPRSNVESDSRSPDIPDEDQPKKKHRRNRTTFTTYQLHELERAFEKSHYPDVYSREELAMKVNLPEVRVQVWFQNRRAKWRRQEKMDTGTMKLHDSPIRSFNRPPMAPNVGPMSNSLPLDPWLSSPLSSATPMHSIPGFMGPGQSLQPTYTAHPGFLNTSPGMMQNIQPMPPPPYQCQPVFNDKYPLEDVDRSSSIAALRMKAKEHIQSMDKTWQPM
Protein: Probable ECF RNA polymerase sigma factor SigI (ECF sigma factor SigI) (Alternative RNA polymerase sigma factor SigI) (RNA polymerase sigma-I factor) (Sigma-I factor) (P9WGH3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor until released, although no anti-sigma factor is known for this protein (By similarity).
Interaction partners:
- AB hydrolase-1 domain-containing protein
- HTH-type transcriptional regulator Rv1931c
- HTH hxlR-type domain-containing protein
- HTH-type transcriptional regulator Cmr
- Probable transcriptional regulatory protein
- Probable transcriptional regulatory protein
- HTH-type transcriptional regulator VirS
- Transcriptional regulatory protein
- Uncharacterized protein Rv0894
- Transcriptional regulatory protein MoaR1
Sequence:
MSQHDPVSAAWRAHRAYLVDLAFRMVGDIGVAEDMVQEAFSRLLRAPVGDIDDERGWLIVVTSRLCLDHIKSASTRRERPQDIAAWHDGDASVSSVDPADRVTLDDEVRLALLIMLERLGPAERVVFVLHEIFGLPYQQIATTIGSQASTCRQLAHRARRKINESRIAASVEPAQHRVVTRAFIEACSNGDLDTLLEVLDPGVAGEIDARKGVVVVGADRVGPTILRHWSHPATVLVAQPVCGQPAVLAFVNRALAGVLALSIEAGKITKIHVLVQPSTLDPLRAELGGG