wanglab/gogpt-training-data huggingface dataset:
Protein: NADH-quinone oxidoreductase (EC 7.1.1.-) (O25852)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Ferredoxin
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit N
- NADH-ubiquinone oxidoreductase, NQO12 subunit
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit I
- NADH-ubiquinone oxidoreductase, NQO13 subunit
- NADH-ubiquinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit J
Sequence:
MMVRKQSPYEDVQKQSRQHDPYKIIEPTPKKYLEGSAYEVIYNHLSYKHEILDKYIETNTAVFWIKKDDIFSVATILRHLGYECLSEMSAIDLCAKKGHFELFYQFVGFSDSCKNRRRVRVKCVLLPNESVDSLSFLYRSANWSEREAYDMLGIVFDKHPYLKRLIMPHDWVGHPLLRSYPLKGDEFAQWYEVDKIFGKEYREVVGKEQRDSARVDEKDTFNFAKIGYEQGKGEELKEVEEKHAFKKIPFVKDLHKIAPTILKKRL
Protein: Conserved protein (O33249)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable integral membrane protein
- Secreted protein
- Uncharacterized protein
- Probable conserved proline, glycine, valine-rich secreted protein
Sequence:
MSAPERVTGLSGQRYGEVLLVTPGEAGPQATVYNSFPLNDCPAELWSALDPQALATEHKAATALLNGPRYWLMNAIEKAPQGPPVTKTFGGIEMLQQATVLLSSMNPAPYTVSQVSRNTVFVFNAGEEVYELQDPKGQRWVMQTWSQVVDPNLSRADLPKLGERLNLPAGWSYHTRVLTSELRVDTTNREARVLQDDLTNSYSLVTA
Protein: Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (P41811)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit gamma
- Coatomer subunit beta
- Coatomer subunit alpha
- Coatomer subunit epsilon
- Coatomer subunit zeta
- ADP-ribosylation factor GTPase-activating protein GLO3
- ADP-ribosylation factor 1
- Vesicular-fusion protein SEC18
- Protein transport protein BET1
Sequence:
MKLDIKKTFSNRSDRVKGIDFHPTEPWVLTTLYSGRVELWNYETQVEVRSIQVTETPVRAGKFIARKNWIIVGSDDFRIRVFNYNTGEKVVDFEAHPDYIRSIAVHPTKPYVLSGSDDLTVKLWNWENNWALEQTFEGHEHFVMCVAFNPKDPSTFASGCLDRTVKVWSLGQSTPNFTLTTGQERGVNYVDYYPLPDKPYMITASDDLTIKIWDYQTKSCVATLEGHMSNVSFAVFHPTLPIIISGSEDGTLKIWNSSTYKVEKTLNVGLERSWCIATHPTGRKNYIASGFDNGFTVLSLGNDEPTLSLDPVGKLVWSGGKNAAASDIFTAVIRGNEEVEQDEPLSLQTKELGSVDVFPQSLAHSPNGRFVTVVGDGEYVIYTALAWRNKAFGKCQDFVWGPDSNSYALIDETGQIKYYKNFKEVTSWSVPMHSAIDRLFSGALLGVKSDGFVYFFDWDNGTLVRRIDVNAKDVIWSDNGELVMIVNTNSNGDEASGYTLLFNKDAYLEAANNGNIDDSEGVDEAFDVLYELSESITSGKWVGDVFIFTTATNRLNYFVGGKTYNLAHYTKEMYLLGYLARDNKVYLADREVHVYGYEISLEVLEFQTLTLRGEIEEAIENVLPNVEGKDSLTKIARFLEGQEYYEEALNISPDQDQKFELALKVGQLTLARDLLTDESAEMKWRALGDASLQRFNFKLAVEAFTNAHDLESLFLLHSSFNNKEGLVTLAKDAERAGKFNLAFNAYWIAGDIQGAKDLLIKSQRFSEAAFLGSTYGLGDDAVNDIVTKWKENLILNGKNTVSERVCGAEGLPGSSSSGDAQPLIDLDSTPAPEQADENKEAEVEDSEFKESNSEAVEAEKKEEEAPQQQQSEQQPEQGEAVPEPVEEES
Protein: Ervatamin-C (ERV-C) (EC 3.4.22.-) (P83654)
Organism: Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria)
Function: Cysteine proteinase. Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity. Has little or no activity against synthetic substrates.
Subcellular location: Secreted {ECO:0000269|Ref.2, ECO:0000305}.
Interaction partners:
Sequence:
LPEQIDWRKKGAVTPVKNQGSCGSCWAFSTVSTVESINQIRTGNLISLSEQELVDCDKKNHGCLGGAFVFAYQYIINNGGIDTQANYPYKAVQGPCQAASKVVSIDGYNGVPFCNEXALKQAVAVQPSTVAIDASSAQFQQYSSGIFSGPCGTKLNHGVTIVGYQANYWIVRNSWGRYWGEKGYIRMLRVGGCGLCGIARLPYYPTKA
Protein: Ephrin type-A receptor 7 (EC 2.7.10.1) (EPH homology kinase 3) (EHK-3) (P54759)
Organism: Rattus norvegicus (Rat)
Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 and MAPK3 which are phosphorylated upon activation of EPHA7.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Ephrin-A5
- Ephrin A2
- Ephrin-A1
- Ephrin-A4
- Ephrin-A3
- Tyrosine-protein kinase
- Tyrosine-protein kinase.
- Ephrin B2
- Ras GTPase-activating protein 1
- Ephexin-1
Sequence:
MVVQTRYPSWIILCYIWLLGFAHTGEAQAAKEVLLLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIIENLAVFPDTVTGSEFSSLVEVRGTCVSSAEEEAENSPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRRFYKSSSQDLQCSRCPTHSFSDREGSSRCECEDGYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRERTYSTLKTKSTSASINNLKPGTVYVFQIRAFTAAGYGNYSPRLDVATLEEASGKMFEATAVSSEQNPVIIIAVVAVAGTIILVFMVFGFIIGRRHCGYSKADQEGDEELYFHFKFPGTKTYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAGEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEFMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGLSRVIEDDPEAVYTTTGGKIPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKERAERPKFEQIVGILDKMIRNPSSLKTPLGTCSRPISPLLDQSTPDFTAFCSVGEWLQAIKMERYKDNFTAAGYNSLESVARMTIDDVMSLGITLVGHQKKIMSSIQTMRAQMLHLHGTGIQV
Protein: Type 2C protein phosphatase (A0A1D8PEN6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Mitogen-activated protein kinase HOG1
- ESCRT-III subunit protein
- protein-tyrosine-phosphatase
- Protein PNS1
- mitogen-activated protein kinase kinase
- Tyrosine protein phosphatase
Sequence:
MASTDTDNSKTVSSSTSSPSTPTKTATTKTTATPPIQSSLEVPSLANNSNGSSSTSTSSTNASSTGANDSNYDPFAGLSFRVGVAENKNTTFRNKMEDVHTYIANFAERVDWGYFAIFDGHAGKDTARWCGNNLHTLLEEEIDRNSDEGSPPPTPIRGKDDLREDLYKCFVKADELIEKSGQGKSGCTAAVAVLRWESDNEEPVSHTKSQDGGKFDFKPTKNHKRLLYTSNVGDSRIVLCRAGQAYRLSYDHKATDTHEINRIEDNGGLVLKNRVNGVLAVTRSLGDTYMKSLVIGVPFTTATEITADDEFIIIACDGLWDVVSDKHACKLAAESFKQGYSPSQVAKKLCQFAIELSTTDNVTVMVVQLDNDVFS
Protein: ADP ribosylation factor-like 4, isoform B (H9XVM3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- MIP16918p
- RE36140p
- non-specific serine/threonine protein kinase
Sequence:
MGATMVKPLVKNGNILDALPSQVATLHVVMLGLDSAGKTTALYRLKFDQYLNTVPTIGFNCEKVQCTLGKAKGVHFLVWDVGGQEKLRPLWRSYTRCTDGILFVIDSVDTERMEEAKMELMRTAKCPDNQGVPVLILANKQDLPNACGAMELEKLLGLNELYNPVPNISMPSSSDSSPTINLIGCRVSNQSITDKSLEEKKESHLHSSMIHIKPALESKDHNSTLSGGALTAFIYPQSHNNSAVLDQKNPQDVKNGFHNKKMNRSSSNSVQFRGWYIQPTCAITGEGLQEGLDALYDMILKRRKINKSNKRNL
Protein: Kinetoplast DNA-associated protein, putative (Q38A79)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLAGRYCLTTHDAPTRHIEWLPLYFHSRHYLLSFFLFSFLFFFPCVVCVCQTEKGNKAPAMLRVSRLSLAIGTYSLFMKEQKNNPALKGLPVAKRGQATAKLYRELSVTEREELAKRAKAAPSATRKKSVPKTKGKEKVTGGGGKRKASEYTEFVKSNISKYSNLPQRERMTAVAKLWKQQKQMRK
Protein: Catenin beta 1 (A0A2R8Y750)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}.
Interaction partners:
Sequence:
MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL
Protein: Ubiquitin carboxyl-terminal hydrolase isozyme L3 (UCH-L3) (EC 3.4.19.12) (Ubiquitin thioesterase L3) (P15374)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3'', and exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.
Subcellular location: Cytoplasm.
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-like protein NEDD8
- 26S proteasome non-ATPase regulatory subunit 14
- LIM domain only protein 7
- Zinc finger-containing ubiquitin peptidase 1
- Sentrin-specific protease 8
- COP9 signalosome complex subunit 5
Sequence:
MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA
Protein: Ras-related protein Rab-6A (Rab-6) (EC 3.6.5.2) (P35279)
Organism: Mus musculus (Mouse)
Function: Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity. Involved in COPI-independent retrograde transport from the Golgi to the ER. Recruits VPS13B isoform 2 to the Golgi membrane. Plays a role in neuron projection development.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:31218450}; Lipid-anchor {ECO:0000250|UniProtKB:P20340}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:31218450}; Peripheral membrane protein {ECO:0000305}. Note=BICD2 facilitates its targeting to Golgi apparatus membrane. {ECO:0000250|UniProtKB:P20340}.
Interaction partners:
- Kinesin-like protein KIF20A
- DENN domain-containing protein 5A
- Protein bicaudal D homolog 2
- GRIP and coiled-coil domain-containing protein 2
- Rab GDP dissociation inhibitor beta
- Protein bicaudal D homolog 1
- ADP-ribosylation factor-like protein 1
- BICD family-like cargo adapter 1
- Guanine nucleotide exchange factor subunit RIC1
- RAB6-interacting golgin
Sequence:
MSAGGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIIMLVGNKTDLADKRQVSIEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMESTQDRSREDMIDIKLEKPQEQPVNEGGCSC
Protein: Aquaporin NIP1-1 (NOD26-like intrinsic protein 1-1) (ZmNIP1-1) (ZmNIP1;1) (Q9ATN4)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Aquaporin SIP2-1
- Aquaporin SIP1-2
Sequence:
MAGGGDHSQTNGGHVDQRALEEGRKEEFADQGCAAMVVSVPFIQKIIAEIFGTYFLMFAGCGAVTINASKNGQITFPGVAIVWGLAVMVMVYAVGHISGAHFNPAVTLAFATSGRFPWRQLPAYVLAQMLGATLASGTLRLMFGGRHEHFPGTLPTGSEVQSLVIEIITTFYLMFVISGVATDNRAIGELAGLAVGATILLNVLIAGPVSGASMNPARSVGPALVSGEYTSIWVYVVGPVVGAVAGAWAYNLIRFTNKPLREITKSTSFLKSTSRMNSAASA
Protein: Camphor 5-monooxygenase (EC 1.14.15.1) (Cytochrome P450-cam) (Cytochrome P450cam) (P00183)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Involved in a camphor oxidation system.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MTTETIQSNANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNGGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHGVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV
Protein: DnaJ heat shock protein family (Hsp40) member C21 (A0A2R8Y4Q0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIAKEELESVLEEEVDDFPTFGDSQSDYDTVVHPFYAYWQSFCTQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDLYCPACDKSFKTEKAMKNHEKSKKHREMVALLKQQLEEEEENFSRPQIDENPLDDNSEEEMEDAPKQKVKYLTFRFIFALRLSKKQKKKKQKPAQDVPGKDSYLPAAHFQMAWGKKCVLGERRDGESEHKCAKMLLENRQNYDDNFNVNGPGEGVKVDPEDTNLNQDSAKELEDSPQENVSVTEIIKPCDDPKSEAKSVPKPKGKKTKDMKKPVRVPAEPQTMSVLISCTTCHSEFPSRNKLFDHLKATGHARAPSSSSLNSATSSQSKKEKRKNR
Protein: Reticulon-2 (Neuroendocrine-specific protein-like 1) (NSP-like protein 1) (Neuroendocrine-specific protein-like I) (NSP-like protein I) (NSPLI) (Q6WN19)
Organism: Rattus norvegicus (Rat)
Function: Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity (By similarity). Enhances trafficking of the glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to the cell surface. Plays a role in the translocation of SLC2A4/GLUT4 from intracellular membranes to the cell membrane which facilitates the uptake of glucose into the cell (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|RuleBase:RU210713, ECO:0000269|PubMed:18096700}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU210713}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:18096700}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O70622}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O70622}. Note=Localizes to intermediate filaments in mononucleated myoblasts and to Z lines in mature myotubes. {ECO:0000250|UniProtKB:O70622}.
Interaction partners:
- Beta-secretase 1
- Atlastin-1
- Receptor expression-enhancing protein
- Spastin
- Atlastin-3
- Receptor expression-enhancing protein.
- Atlastin GTPase 2
Sequence:
MGQVLPVFAHCKEAPSTASSTPDSTEGGNDDSDFRELHTAREFSEDEEEETTSQDWGTPRELTFSYIAFDGVVGSGGRRDSVVRRPRPQGRSVSEPRDPPPQPSLGDSLESIPSLSQSPEPGRRGDPDTVPPAERPLEELRLRLDQLGWAVRSAGSGEDSATSSSTPLENEEPDGLEASEAGETNLELRLAQPLHLQFEGLTPQLSPSSGIPQAHTPSPQRSQDLNTGPDEPLPNGEGEHWRLLEQEPITAQCLNSTDQSEFTLEPLLLVADLLYWKDTRTSGAIFTGLMASLLCLLHFSIVSVAAHLALLGLCATISLRVYRKVLQAVHRGDGTNPFQAYLDMDLTLTREQTERLSQQIASHVVSTATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLVILGVVALFTVPLLYRQHQAQIDQYVGLVTSQLSHIKAKIRAKIPGTGTLAPAASVSGSKAKAE
Protein: Dimethyladenosine transferase (EC 2.1.1.183) (18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase) (18S rRNA dimethylase) (DIM1 dimethyladenosine transferase 1 homolog) (DIM1 dimethyladenosine transferase 1-like) (S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase) (Q9UNQ2)
Organism: Homo sapiens (Human)
Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:25851604}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:25851604, ECO:0000269|PubMed:34516797}.
Interaction partners:
- Pre-rRNA-processing protein TSR1 homolog
- Bystin
- Periodic tryptophan protein 2 homolog
- Protein LTV1 homolog
- Nucleolar complex protein 4 homolog
- U3 small nucleolar ribonucleoprotein protein IMP4
- WD repeat-containing protein 3
- Nucleolar protein 6
- 18S rRNA
- Serine/threonine-protein kinase RIO2
Sequence:
MPKVKSGAIGRRRGRQEQRRELKSAGGLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVASKLQVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVHNIIIPEDFSIADKIQQILTSTGFSDKRARSMDIDDFIRLLHGFNAEGIHFS
Protein: CENP-ana, isoform A (EC 5.6.1.3) (Q9VKH9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Bub1-related kinase
- Bub1 kinase, isoform A
- Aurora kinase B
- Monopolar spindle 1, isoform B
- Mitotic checkpoint protein BUB3
- Kinetochore protein NDC80
- Protein abnormal spindle
- Aurora kinase
- Kinesin-like protein Klp61F
- Kinesin-like protein
Sequence:
MSTKNASSIQVCIKVRPCEPGLTSLWQVKEGRSIQLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNGIVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSDHSDNDTVKQSVLSLVDLAGSEQVDPADHASSLMIFRNLVKSLSESVDSKPNSFRDSKLPRIMLPSLGGNVLTSIICTITPSFVEESSSTISFGTCAKKIRCKPQVCKIDSETTMMRQLDRGISMLKDKLAKKKIKNESQLVLQELEGRIKRDMLKIVSSASLDDYRLQKRRRTWTLTASGSEGDAPVLALPEPEESRLPRPSKLTNLPKPLFQRRGIAPKAKGICKTLKEKRLQTDNMDTMPGRAKQLGRETASRIPSVMMSKKYQESVPNCDAPQTEISALTASNQVAKETIEKYEEQVKRLKETIERLEMENGKAVNLGEQFETHKAKSKQMEEELLSSISEKDSTIVSLQQSLEELSRDVLRNSKEDQMRSMCPELESSCERICNKCLELERLLPLASASGLDSVACQFDQLRSEIAATRMKLESMLSTFSHASCEVSQKTTDCKRLSEQISTAHDDFGQLQEKYNNLKHKWSSQKLAIDTMQVDYNTIQQKYLQLQDEYRHLELRSDEQCQQLQDENSKLQAEIGTLKERVEEIHSELLEVPNPDTHPEDMELQNQELKKRLSKLQWEFDEIQLNYECLSNELMSTIQECDALREEHKQRTTNSDLESMKSSGVGTECSDPENELDTDLLQQFTKLSKSIQQIELTDYSGGRRLFIYNHAEQDQSVPSLKLCLEPAKYLEGDGKQHDASDSVFLKGFLKCQRFQIVKINQEQNLVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQIETIKNQNAKTKILCEELQTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSSDLLPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREINFRSEKERMDGTISSLLEDKRNLEEKLCTVTELLAKLKRELPALHTQKVNGGDVSIELNSSNGSPTPAAVPATKKPLDCNSAECVPKKSSSLETAERKNRRMTAYDENRKQFC
Protein: Circadian clock oscillator protein KaiA (Q6L8K1)
Organism: Thermostichus vulcanus (Synechococcus vulcanus)
Function: Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII domain during the subjective day yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB during the subjective night to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding on KaiB that sequesters KaiA from KaiC's CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex resulting in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator.
Interaction partners:
Sequence:
MAQSTALTICGLVYSPAIGQELVRLHTSDIDELVYFSSEREFCNYLEARRNSVACLILEWGEGTPQIITYLHHSATLLPAILIFPAAPAPPPAGPHYHIAEVILTTDQLDQLNRQIEEAITGFVKLCPGCAVPPHVLFRLPALKESSNVDPQHRLSQKLKERLGYLGVYYKRDTAFFFRRMSPADKRKLLDELRSIYRTIVLEYFNTDAKVNERIDEFVSKAFFADISVSQVLEIHVELMDTFSKQLKLEGRSEDILLDYRLTLIDVIAHLCEMYRRSIPREV
Protein: Large ribosomal subunit protein uL23B (60S ribosomal protein L25-B) (O74391)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This protein binds to a specific region on the 26S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein uL10
- Elongation factor 3
- Large ribosomal subunit protein eL13
Sequence:
MSVGKAKGAQKTVQKGIHNKVARKVRTSTTFRRPKTLELARKPKYARKSVPHASRLDEYKIIVNPINSESAMKKIEDDNTLVFHVHLKANKFTIKNAVKKLYSVDAVKINTLIRPNGTKKAFVKLSADADALDVANRIGFL
Protein: Mitogen-activated protein kinase 1 (AtMPK1) (MAP kinase 1) (EC 2.7.11.24) (Q39021)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitogen-activated protein kinase kinase 3
- Protein-tyrosine-phosphatase PTP1
- Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein
Sequence:
MATLVDPPNGIRNEGKHYFSMWQTLFEIDTKYMPIKPIGRGAYGVVCSSVNSDTNEKVAIKKIHNVYENRIDALRTLRELKLLRHLRHENVIALKDVMMPIHKMSFKDVYLVYELMDTDLHQIIKSSQVLSNDHCQYFLFQLLRGLKYIHSANILHRDLKPGNLLVNANCDLKICDFGLARASNTKGQFMTEYVVTRWYRAPELLLCCDNYGTSIDVWSVGCIFAELLGRKPIFQGTECLNQLKLIVNILGSQREEDLEFIDNPKAKRYIRSLPYSPGMSLSRLYPGAHVLAIDLLQKMLVFDPSKRISVSEALQHPYMAPLYDPNANPPAQVPIDLDVDEDLREEMIREMMWNEMLHYHPQASTLNTEL