wanglab/gogpt-training-data huggingface dataset:
Protein: 30S ribosome-binding factor (Protein P15B) (Ribosome-binding factor A) (RbfA) (P0A7G2)
Organism: Escherichia coli (strain K12)
Function: One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late maturation steps of the functional core of the 30S subunit. Essential for efficient processing of pre-16S rRNA. Probably part of the 30S subunit prior to or during the final step in the processing of 16S free 30S ribosomal subunits. Probably interacts with the 5'-terminal helix region of 16S rRNA. Has affinity for free ribosomal 30S subunits but not for 70S ribosomes. Overexpression suppresses a cold-sensitive C23U 16S rRNA mutation. Overexpression decreases the lag time following cold-shock by about half, leading to faster adaptation and increased protein synthesis. Overexpression also partially suppresses a rimM deletion mutant and partially rescues its 16S rRNA processing deficiency. Its function overlaps that of Era in ribosome biogenesis. A number of RbfA mutants suppress RsgA/YjeQ deletions, in all cases less RbfA is bound to the 30S ribosome. Released from 30S ribosomes by RsgA; stimulates the ribosome-associated GTPase activity of RsgA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00003, ECO:0000269|PubMed:12963368, ECO:0000269|PubMed:7535280}. Note=About 1/3 associates with free 30S ribosomal subunits at 37 degrees Celsius, 6 hours after a 15 degrees Celsius cold-shock about 4-fold more protein is associated with 30S ribosomes (PubMed:12963368, PubMed:7535280). {ECO:0000269|PubMed:12963368, ECO:0000269|PubMed:7535280}.
Interaction partners:
- tRNA pseudouridine synthase B
- Translation initiation factor IF-2
- Ribosome maturation factor RimP
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS17
- Ribosome maturation factor RimM
- Small ribosomal subunit protein bS18
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS7
Sequence:
MAKEFGRPQRVAQEMQKEIALILQREIKDPRLGMMTTVSGVEMSRDLAYAKVYVTFLNDKDEDAVKAGIKALQEASGFIRSLLGKAMRLRIVPELTFFYDNSLVEGMRMSNLVTSVVKHDEERRVNPDDSKED
Protein: Alpha-tubulin (Q8VXK7)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTSVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKRL
Protein: Tryparedoxin, putative (Q582M8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPSAETLLKDLFGSHTVELLRQDGKMVPATTALEGKKYLLVYFSASWCPPCRVFTPQLATFHELFSAKHNFDVIFVSRDKDESSMSAYFYNPKYSSLSVSGGECSHGDWLALPFTQAQTVGKEIMSRYGLNTIPNILLFDLSTEELVTSEARQLIGSNCRSAEGFPWRGASAPVISFQGLATVFVVFLMLYQFWQSWS
Protein: Translation initiation factor IF-2, putative (Q8IBA3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Small ribosomal subunit protein eS30
- 40S ribosomal protein S3
- 40S ribosomal protein S11
- 60S ribosomal protein L6, putative
- 40S ribosomal protein S19
- 60S ribosomal protein L5, putative
- 40S ribosomal protein S5, putative
- 40S ribosomal protein S11, putative
- 60S ribosomal protein L23
- 60S ribosomal protein L11a, putative
Sequence:
MNKIKIRKFEDPHVWIYENVLLNKTLKLKEIEKKKDNKNVPNALLHEEACKKLKGILKECKKYDKELQEIKNKKESFILKNTLHPNKKINLKFLLNDNQFKVKNEEERKNFKLIFNENKNIYIKNNQKVYNNIINIKRNSQITSTNNMNNNNNNVNINNDNIQPTNNLLNNIKKIQKEKISKLYSVFNNHVNYYDNYLKEKYMKEEYLSNVKYEYVSPHRHNYNDHDIKPDVIYKEDSNVSNTTHNNHNNNNNNNNNSKNKNNFSSSISSSDLLYHTNLGKNNSVSGTNLKLNVHTNNIHILDNKQCYDTLHHNNAYSHDIYGNQENVNTPKDKYITKINNKNVEDMKNVTNNIIFNKLNINNENTQKIFLYNRNDKEHESIKNDKNNSKDYPFDYKKETSYLTTEENCNHIDIYDDNKMCDDNIYVKRNVYHNKNNSVKDLFVKSFNILNTINQTSLYDKQNDDVSNEDANRNVLNGSVLSILNELRENKVKEKNKIGEYKKDNTLHKDDEKVSVSRIHTYEMKQKEVTNVNKNESFYSYGINNNNNNYYYNYNNCNNLKESVVPHKKKENHKNKHIKQYEYLDSNNITINSLSNHLDVDDEKIINVCKYILDNDYIYKYTKIEKEVAELICEELNVSEKLKFSCINLKKRNPIVTILGHVDHGKTTLLDRLRHSNIADNEIGGITQKLGAFEVVCRDDEMKENKNVKEYINDNKKEEHNHYNKKEEHNNYNKKEEHNNYNKKDEHNNYNKKEEHNIYCDNSSNYHNRKITFFDTPGHSVFRTIRKRCVQCSDLIVLVISLDDGIMSETIECIELAKTYNTPLIIAANKIDKFHKNIEELSKSLLNYNIVTNLENGDVPMVPISAKKNINIDILKKQILHVSNKLNLMCDYGSLCSAYILEKKVDPSKGKLLTVICKSGTLKVNTYFIIGHIYGKIKRIYNSNNEIVSQAYPSEVVQIISSIPLSYDNINYGDIMLEMNTLKSAQKVSKYKLKLVQYNLINDHYNMNNTLGEISRNIETNKNNDIHNNDNNLDDNIIDELHNDISIYDGNKKKKNSNKLDINKKYNNNNKKYNNNNNNNNIYNNNIYNNNNIYNIYNNNNNKYYNNHSNDLRNPLNKFNSKNNNLSGSNFNLNSFKLPQIPLILKTCDEGSLEGIMEGIEHFNKNETKEKYCNIHNFIDRNYINKNMLNDDINNISKELFSNWCPLKIINKGLGTFHSTDLKYCEHINPCFLISFNVDIDFKLLQPYIENHNIILRNHNIIYELFNDIENMCNFYFDSLHVYEPVAKMIINKTGYYSIKKNKTKKVVISVDIKEGSFTSNEYFTLKRNKQIIHNKIHILSMQKNKQNTNELNKSCNINAIIFNINSDDFEVGDEIVAYKKVVRSPLFNTIKSFDLS
Protein: methionine--tRNA ligase (EC 6.1.1.10) (Q4QCD2)
Organism: Leishmania major
Interaction partners:
- proline--tRNA ligase
- Putative methionyl-tRNA formyltransferase
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- Methionine synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- arginine--tRNA ligase
- glutamine--tRNA ligase
- asparagine--tRNA ligase
- proline--tRNA ligase
Sequence:
MLKFFTEKANHQALKAVLCAVFVQKPLEVTLGSTYSTPYLQLPKSRALLYSCNEAARLIWSTHAAPLPADNSLEGEAEWLEWESTVLTPALTPLYTHRRITGEAEAALKKLDSTIEEHQGTVAVKGAPSSTSFLVDSVLFASLLPALCEGGLLPAAQAARVPHLVKWFQAFQAEHAELIASAFDVLSVQECGDFLRVPQTYEVSPKKQKVFFATTPIYYVNASPHIGHVYSTLIVDVLGRYHRVKGEEVFVMTGTDEHGQKVAEAAAKQGVSPMDFTTSVSSEFKQCFQEMNYDMNYFIRTTNPTHEKLVQDIWKKLAAKGDIYLGKYEGWYSVSDESFLTAQNVADGVDRDGKPCKVSLESGHVVTWVEEENYMFRLSAFRERLLKYFHDHPNCIVPEFRRREVIKTVEKGLFDLSISRKRESVMNWSIPVPGDERHCIYVWLDALFNYYTGALTRVATDGTETLDEDHHALNRWPADVHVVGKDILKFHAIYWPAFLMSAELPLPERLVSHGWWTKDHKKISKSLGNAFDPVEKAKEFGIDALKYFLMRESNFQDDGDYSDKNMVARLNGELADTLGNLVSRCVAPKINVNGMWPEPAEYSESDKTLIASLNNLAGTVDHYYCLPDIQHALIAIFDVLRSLNAYVTENAPWKLVKMDTARLGTVLYVTMEGLRICTMFLQPVMPQKAKEIMDALGVPEAARVGMENYLFGIVKPGTKIAGLAEGQVVFQKVTLPTEEGERSSKGQ
Protein: DNA polymerase epsilon subunit C (DNA polymerase II subunit C) (C6Y4D0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair (By similarity). The dpb3-dpb4 dimer associates with histone deacetylases, chromatin remodelers, and histones and plays a crucial role in the inheritance of histone hypoacetylation and H3K9 methylation in heterochromatin. The dpb3-dpb4 dimer is also required for the recruitment of sir2 to heterochromatin.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27344}.
Interaction partners:
- DNA polymerase epsilon subunit D
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit B
- Transcriptional activator hap3
- Transcriptional activator hap2
- DNA polymerase zeta processivity subunit
- DNA polymerase delta subunit 4
- DNA polymerase alpha catalytic subunit
- DNA polymerase zeta catalytic subunit
- DNA polymerase subunit delta-2
Sequence:
MEKTYGKTVLPLSRVKRIIKQDEDVHYCSNASALLISVATELFVEKLATEAYQLAKLQKRKGIRYRDVEDVVRKDDQFEFLSDLFSI
Protein: B-related factor 1 (Q9NB72)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTGLKCRNCGSNEIEEDNARGDRVCMNCGSVLEDSLIVSEVQFEEVGHGAAAIGQFVSAESSGGATNYGYGKFQVGSGTESREVTIKKAKKDITLLCQQLQLSQHYADTALNFFKMALGRHLTRGRKSTHIYAACVYMTCRTEGTSHLLIDISDVQQICSYELGRTYLKLSHALCINIPSLDPCLYIMRFANRLQLGAKTHEVSMTALRIVQRMKKDCMHSGRRPTGLCGAALLIAARMHDFSRTMLDVIGVVKIHESTLRKRLSEFAETPSGGLTLEEFMTVDLEREQDPPSFKAARKKDRERIKDMGEHELTELQKEIDAHLEKDLGKYSNSVYRQLTKGKGLSPLSSPSTPNSSSEKDIELEESRQFIEQSNAEVIKELIAKNEDVKKSEPGGLVAGIEGLRPDIEAICRVTQSDLEDVEKAKQPQEQELITDDLNDDELDQYVLTEEESVAKLEMWKNLNAEYLQEQKERDERLAKEREEGKPERKKRKPRKKVIGPSSTAGEAIEKMLQEKKISSKINYEILKTLTDGMGGLTDDSPTTSADTKPSTLEELKHQPVIVEEGPIPSKSRGNRAAYDLPGPSRKRPKLEVGLPVSQAADVEQPETKPAVVVEADDLDEDADDPDVEPEAEPEATLQDMLNTGGDDDEFGYGFDEEEEY
Protein: Uncharacterized transcriptional regulator YjhU (P39356)
Organism: Escherichia coli (strain K12)
Interaction partners:
- PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK
- UPF0761 membrane protein YihY
- UPF0162 protein YchA
- HTH-type transcriptional regulator YjdC
Sequence:
MDRDQTNSSLFNDDPVLHATWLYYQEGKSQTEVAAIMGVSRVTVVKYLQTARENGLVHINLDVNVFGSIDAALQIRDKFNLQRVIIVPDGEHAGKRDDTKLMRTRLSRAGGMYLNQVIENGDVLGVAWGRTIHQMSKTMTPKSCKNVTVIQMLGSMPSQPDLTIIESSSQIAYKLSGRVASLHVPAVVSSARLAMELQAEPIIRSNFDVLTRCTKAFFVVGNALDENPLIRVGVLNKKEMQTYRDLGAVGVICGRFYDKEGMPVVADVDQRILGISLAQLRQIERKIFLAGGERGYDATLGALLGGYVTDLIVDEGTAEFLLACELPH
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q57VN6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
Interaction partners:
- Kinesin, putative
Sequence:
MISPKDTSNYGTLAGRGREKQAFLSTGLTRSDGSVAVEVELEDRIGIGIKGELHTLFSCVGDAKPLYEELGGVEGIAERLGTSITDGIDSFSVENRRAVYGRNELPEEAPLTFWKIFKTAWSDRMIILLTLAACVSLILGLTVPEPGHEKVDYKTGWIEGTAILMAVIAVTSASSIQDYRKELKFRALVEENSAQPISVIRDGHKVTVDVTEIVVGDLVSLSPGLVIPVDGLYVRGLSVVVDESSVTGENDLKKKGAEHPILLSGTVVSTAEDAYILACAVGESSFGGKLLMESRLDGEPRATPLQERSQNLVSFIARVAIISAVLFFIVLCIIEIERIATNKQQFYPKKFLNFLLLCVTIVVIAVPEGLPLVVTIALAYSQSQMQKDNNQVRRLCACETMGNATQICSDKTGTLTQNRMTVVQGYIGMRRFRVSNPGDPSSTVNLEGVSSDAQSLLMLGLALNSSSEKELLPGNVGAESDLLSRWTWRTDKGNKTDQAILDFVDRVLISVPGSCNDKELPHQKLRMTNCSRGFAIFPFTSERKFMTAVVAGADGVVMQYVKGGSDRVLGMCNRYLSSEGREEPLTEEVTEMITEQIRSIAGDANRTIGVAYGRIGTDGAVPEEEPEGPFVWLALLGIQDPLRPEVVDAVRMCQRAGVTVRMCTGDNLDTAVAISRQCGIYNRLRGDLALTGKDFRNLVYDTYGDEANMEKFWPVLDRMMVMGRSQPLDKQLLVLMLMLRGEVVAVTGDGTNDAPALRLANVGFVMRSGTDIAVKSGDIVLLDDNFRSVQRAVVWGRTVNDNIRKFLQLQFTVNLVCFSLTVVGTLVREGKSSPLTTVQLLWVNLLMDTLAAPALATEQPTEDCLNRGPSSPRAPLVSRRMWFTIFSVATVQLTAFFSVLTFGGKYFGEDENGKHLHRTFLFNVFVFGTIFHMLNCRKLYRELNVFEGMGRSVFFIVVVGSCIAFQVLAICTFNDFMGVRPLSIKQWGVSIGIAAISLVVGILSRVVSIREPVFALIPDSRNVDGSASRLIKDVSVAAEQRQRETDGTSDASSLLAGRLRAQSRWRRLQAEHVKKPRVVNAFRRAWTDRDMKRGSTRQLYDTLRMV
Protein: Probable V-type proton ATPase 20 kDa proteolipid subunit (V-ATPase 20 kDa proteolipid subunit) (Vacuolar proton pump 20 kDa proteolipid subunit) (O14046)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P23968}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit d
- V-type proton ATPase subunit E
- V-type proton ATPase subunit F
- V-type proton ATPase subunit a
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
- V-type proton ATPase subunit c
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit G
Sequence:
MSLFSTSLWTTTVMSIIVGLYMLFHNSGESFDFGSFLLDTSPYTWGLLGIASCVAFGIIGAAWGIFICGTSILGGAVKAPRIKTKNLISIIFCEVVAIYSLIIAIVFSAKINDINPAGFYTKSHYYTGFALFWGGITVGLCNLICGVCVGITGSSAALADAQDASLFVKVLVVEIFGSVLGLFGLIVGLLIGGKASDFS
Protein: Neuronal calcium sensor 1 (NCS-1) (Frequenin homolog) (Q8BNY6)
Organism: Mus musculus (Mouse)
Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:P62166}. Postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62166}. Membrane {ECO:0000250|UniProtKB:P62166, ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166}.
Interaction partners:
- D
- Interleukin-1 receptor accessory protein-like 1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Phosphatidylinositol 4-kinase beta
- Rhodopsin kinase GRK1
Sequence:
MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNADGKLTLQEFQEGSKADPSIVQALSLYDGLV
Protein: Septin-2 (Vascular endothelial cell specific protein 11) (Q91Y81)
Organism: Rattus norvegicus (Rat)
Function: Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q15019}. Note=In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes. Found in the sperm annulus (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q15019}.
Interaction partners:
- Septin-8
- Septin-11
- Septin-9
- Septin
- Septin-7
- Septin-5
- Neuronal-specific septin-3
- Septin-10
- Exocyst complex component 8
- Exocyst complex component 2
Sequence:
MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERIIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINSRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHSIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDTDSSTLGHHV
Protein: Isoamylase SU1, chloroplastic (EC 3.2.1.68) (Protein SUGARY 1) (O22637)
Organism: Zea mays (Maize)
Function: Isoamylase starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MAQQLPCVSSPRPLLAVPAGRWRAGVRGRPNVAGLGRGRLSLHAAAARPVAEAVQAEEDDDDDDEEVAEERFALGGACRVLAGMPAPLGATALRGGVNFAVYSSGASAASLCLFAPGDLKADRVTEEVPLDPLLNRTGNVWHVFIHGDQLHGMLYGYRFDGVFAPERGQYYDVSNVVVDPYAKAVVSRGEYGVPAPGGSCWPQMAGMIPLPYNKFDWQGDLPLGYHQKDLVIYEMHLRGFTKHNSSKTKHPGTYIGAVSKLDHLKELGVNCIELMPCHEFNELEYFSSSSKMNFWGYSTINFFSPMARYSSSGIRDSGCGAINEFKAFVREAHKRGIEVIMDVVFNHTAEGNEKGPILSFRGIDNSTYYMLAPKGEFYNYSGCGNTFNCNHPVVREFIVDCLRYWVTEMHVDGFRFDLASILTRGCSLWDPVNVYGSPMEGDMITTGTPLVAPPLIDMISNDPILGNVKLIAEAWDAGGLYQVGQFPHWNVWSEWNGKYRDTVRQFIKGTDGFAGAFAECLCGSPQLYQAGGRKPWHSINFVCAHDGFTLADLVTYNSKYNLSNGEDNRDGENHNLSWNCGEEGEFASLSVRRLRKRQMRNFFVCLMVSQGVPMFYMGDEYGHTKGGNNNTYCHDHYVNYFRWDKKEEQSSDLYRFCRLMTKFRKECESLGLEDFPTSERLKWHGHQPGKPDWSEASRFVAFTMKDETKGEIYVAFNTSHLPVVVGLPERSGFRWEPVVDTGKEAPYDFLTDGLPDRAVTVYQFSHFLNSNLYPMLSYSSIILVLRPDV
Protein: Abscisic acid receptor PYL10 (ABI1-binding protein 8) (PYR1-like protein 10) (Regulatory components of ABA receptor 4) (Q8H1R0)
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) in an ABA-independent manner but more efficiently when activated by ABA. Can be activated by both (-)-ABA and (+)-ABA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus {ECO:0000250|UniProtKB:O49686}. Cell membrane {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.
Interaction partners:
- Protein phosphatase 2C 16
- Protein phosphatase 2C 37
- Protein phosphatase 2C 56
- Protein phosphatase 2C 77
- Probable protein phosphatase 2C 24
- Protein phosphatase 2C 7
- Probable protein phosphatase 2C 78
- Probable protein phosphatase 2C 75
- Protein phosphatase 2C 3
- TIR-NBS-LRR class disease resistance protein
Sequence:
MNGDETKKVESEYIKKHHRHELVESQCSSTLVKHIKAPLHLVWSIVRRFDEPQKYKPFISRCVVQGKKLEVGSVREVDLKSGLPATKSTEVLEILDDNEHILGIRIVGGDHRLKNYSSTISLHSETIDGKTGTLAIESFVVDVPEGNTKEETCFFVEALIQCNLNSLADVTERLQAESMEKKI
Protein: GDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 1) (O-FucT-1) (Protein O-fucosyltransferase 1) (Q18014)
Organism: Caenorhabditis elegans
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6EV70}.
Interaction partners:
- GDP-fucose protein O-fucosyltransferase 2
- Putative extracellular sulfatase Sulf-1 homolog
- Sulfatase N-terminal domain-containing protein
- Alpha-
Sequence:
MRVSKVLTLASFISVCSYSEAKSNETDPNGYIVFCPCMGRFGNQVDQFLGVLAFAKALDRTLVLPNFIEFKHPETKMIPFEFLFQVGTVAKYTRVVTMQEFTKKIMPTVWPPEKRKAFCWTPRQAIYDKSAEPGCHSKEGNPFGPYWDQIDVSFVGDEYFGDIPGGFDLNQMGSRKKWLEKFPSEEYPVLAFSSAPAPFPSKGKVWSIQKYLRWSSRITEQAKKFISANLAKPFVAVHLRNDADWVRVCEHIDTTTNRPLFASEQCLGEGHHLGTLTKEICSPSKQQILEQIVEKVGSIGAKSVFVASDKDHMIDEINEALKPYEIEAHRQEPDDMYTSLAIMGRADLFVGNCVSTFSHIVKRERDHAGQSPRPSAFFGIRAVKRHIDL
Protein: G-protein coupled receptor 84 (Inflammation-related G-protein coupled receptor EX33) (Q9NQS5)
Organism: Homo sapiens (Human)
Function: Receptor for medium-chain free fatty acid (FFA) with carbon chain lengths of C9 to C14. Capric acid (C10:0), undecanoic acid (C11:0) and lauric acid (C12:0) are the most potent agonists. Not activated by short-chain and long-chain saturated and unsaturated FFAs. Activation by medium-chain free fatty acid is coupled to a pertussis toxin sensitive G(i/o) protein pathway. May have important roles in processes from fatty acid metabolism to regulation of the immune system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:35427647}; Multi-pass membrane protein.
Interaction partners:
- Free fatty acid receptor 2
- Free fatty acid receptor 3
- Free fatty acid receptor 4
- Free fatty acid receptor 1
- Glucose-dependent insulinotropic receptor
Sequence:
MWNSSDANFSCYHESVLGYRYVAVSWGVVVAVTGTVGNVLTLLALAIQPKLRTRFNLLIANLTLADLLYCTLLQPFSVDTYLHLHWRTGATFCRVFGLLLFASNSVSILTLCLIALGRYLLIAHPKLFPQVFSAKGIVLALVSTWVVGVASFAPLWPIYILVPVVCTCSFDRIRGRPYTTILMGIYFVLGLSSVGIFYCLIHRQVKRAAQALDQYKLRQASIHSNHVARTDEAMPGRFQELDSRLASGGPSEGISSEPVSAATTQTLEGDSSEVGDQINSKRAKQMAEKSPPEASAKAQPIKGARRAPDSSSEFGKVTRMCFAVFLCFALSYIPFLLLNILDARVQAPRVVHMLAANLTWLNGCINPVLYAAMNRQFRQAYGSILKRGPRSFHRLH
Protein: Non-selective voltage-gated ion channel VDAC2 (Outer mitochondrial membrane protein porin 2) (Q5JSD2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MATHGQTCARPMCIPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFAVGYRTGDFQLHTN
Protein: phosphopyruvate hydratase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (Skeletal muscle enolase) (E5RGZ4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKGRYLGKGVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFYRNGKYDLDFKSPDDPARHITGEKLGELYKSF
Protein: Receptor-like protein 2 (AtRLP2) (Q9SHI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the perception of CLV3 and CLV3-like peptides, that act as extracellular signals regulating meristems maintenance.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Tyrosine-protein phosphatase RLPH2
- Tyrosine-protein phosphatase At3g09960
- Receptor-like kinase
- Wall-associated receptor kinase-like 2
Sequence:
MRSKAKGLVRPLITKPVQPLSSHMHLFLLCILFLSALFLTLSEAVCNLQDRESLIWFSGNVSSSVSPLNWNLSIDCCSWEGITCDDSSDSHVTVISLPSRGLSGTLASSVQNIHRLSRLDLSYNRLSGPLPPGFFSTLDQLMILNLSYNSFNGELPLEQAFGNESNRFFSIQTLDLSSNLLEGEILRSSVYLQGTINLISFNVSNNSFTGPIPSFMCRSSPQLSKLDFSYNDFSGHISQELGRCLRLTVLQAGFNNLSGVIPSEIYNLSELEQLFLPANQLTGKIDNNITRLRKLTSLALYSNHLEGEIPMDIGNLSSLRSLQLHINNINGTVPLSLANCTKLVKLNLRVNQLGGGLTELEFSQLQSLKVLDLGNNSFTGALPDKIFSCKSLTAIRFAGNKLTGEISPQVLELESLSFMGLSDNKLTNITGALSILQGCRKLSTLILAKNFYDETVPSKEDFLSPDGFPKLRIFGVGACRLRGEIPAWLINLNKVEVMDLSMNRFVGSIPGWLGTLPDLFYLDLSDNLLTGELPKELFQLRALMSQKITENNYLELPIFLNPNNVTTNQQYNKLYSFPPTIYIRRNNLTGSIPVEVGQLKVLHILELLGNNLSGSIPDELSNLTNLERLDLSNNNLSGSIPWSLTNLNFLSYFNVANNSLEGPIPSEGQFDTFPKANFEGNPLLCGGVLLTSCKPTRAKENDELNRTFLMGIAIGYFLSFVSILVVRAW
Protein: UBX domain-containing protein 4 (P54730)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cell division control protein 48
- UBX domain-containing protein 5
- Nuclear protein localization protein 4
- UBX domain-containing protein 1
- Ubiquitin fusion degradation protein 1
- UBX domain-containing protein 6
- UBX domain-containing protein 2
- UBX domain-containing protein 7
- ATPase family gene 2 protein
- UBX domain-containing protein 3
Sequence:
MPMVTVKYNFQLFKCKVSLNSTLNDVLHQSIQFFQLHTSSNDWSLIHLDKPVPLDLPWRLLNLPTGVNLELSKSSNFPVANKTNREDIPFNTIKIRFQIPGRDSVVKEMPSDQPIAPILRQMSGAAGDDFKIQVFSKIIEFKTIKDENLTLENLGIQEPSSVRLIFNNTSHSEGISANSAIHPKQTPPTMTNPETVASLPPHELHKPSVFLPSDEPLAVIKDQIEDEEDYELTVEQAKKYQKMLSSKAGTLGGPILTKRLREQSANNLPKKNKAISECLLRVKFPDRSHIQIAFKPNEDMRTVYNVVSQFLIDENMPFTLNQSHPFKPLAKDDKKLLDDLEFGSKTMLLFETNSNSNGPLIKAHLLEDAQKITHETRTTPSVNTINKSNPQGPSDNATSIKKTLNRVPKWMKLSKK