wanglab/gogpt-training-data huggingface dataset:
Protein: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) (Q93619)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Branched-chain-amino-acid aminotransferase, cytosolic
- Probable pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Branched-chain-amino-acid aminotransferase
- 2-oxoacid dehydrogenase acyltransferase catalytic domain-containing protein
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
Sequence:
MSSRAVSLFSKCGSRISQTRGKAHFTFQPSTTLPAGLENLEKTKMNLMQSVNEAMRIAMETDDSAVLFGEDVAFGGVFRCSLDLQKKFGKDRVFNTPLCEQGIAGFGIGVAAAGATAIAEIQFGDYIFPAYDQLVNEAAKFRYRSGNQFDCGKLTVRTTWGAVGHGALYHSQSPEANFTHTPGLKLVVPRGPVQAKGLLLSCIRDPNPCIFFEPKILYRLASEDVPTGDYTIPLGQAETVRSGKDLTLVAWGTQVHVALEAAQLAKEKLNADVEVIDLQTIQPWDEDHVVESVQKTGRLIVTHEAPISSGFGAEIASTVQKRCFLNLESPIDRVAGFDTPFPHVHEPFYLPTVHRVFDAIKKSVNY
Protein: Actin filament-associated protein 1 (110 kDa actin filament-associated protein) (AFAP-110) (Q8VH46)
Organism: Rattus norvegicus (Rat)
Function: Can cross-link actin filaments into both network and bundle structures. May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:12114187}.
Interaction partners:
Sequence:
MEELIVELRLFLELLDHEYLTSTVREKKAVLTNILLRMQSSKGFEVKDHAQKAETNNLPAPPQMPLPEIPQPWLPPDSGPPPLPTSSLPEGYYEEAVPLSPGKAPEYITSNYDSEAMGSSYESYDEEEEDGKGKKTQHQCHHEEASMDLVKDAKICAFLLRKKRFGQWTKLLCVIKDTKLLCYKSSKDQQPQMELPLQGCSITYIPRDSKKKKHELKITQQGTDPLVLAVQSKEQAEQWLKVIKEAYSGCSGPVDPECSPPPSASVPVNKAELEKKLSSERPSSDGEGVVENGVTTCNGKEQAKRKKPSKSEAKGTVSKVTGKKITKIIGLGKKKPSTDEQTSSAEEDVPTCGYLNVLSNSRWRERWCRVKDSKLILHKDRADLKTHIVSIPLRGCEVIPGLDSKHPLTFRLLRNGQEVAVLEASSSEDMGRWIGILLAETGSSTDPGALHYDYIDVEMSANVIQTAKQTFCFMNRRAVSTSPYLGSLSNGYAHPSGTALHYDDVPCVNGSLKNKKPPASSNGLPVKGRAPSSQQKKVESAGGVKRTASNAEQYKYGKNRVEADAKRLQSKEEELLKRKEALRNRLAQLRKERKDLRAAIEVNAGRKTQVALEDKLKRLEEECKQREAERVSLELELTEVKESLKKALAGGVTLGLAIEPKSGTSSPQSPVFRHRTLENSPISSCDTSDAEGPLPVNSAAVLKKSQPSSSSSPCRGHVLQKAREWELKNGT
Protein: Sulfotransferase 1A1 (ST1A1) (EC 2.8.2.1) (Aryl sulfotransferase) (Aryl sulfotransferase IV) (ASTIV) (Minoxidil sulfotransferase) (Mx-ST) (PST-1) (Phenol sulfotransferase) (Sulfokinase) (Tyrosine-ester sulfotransferase) (P17988)
Organism: Rattus norvegicus (Rat)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important roles in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin (By similarity). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil. Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (By similarity). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1513323}.
Interaction partners:
- Carbohydrate sulfotransferase 10
- Sulfotransferase 2A2
- UDP-glucuronosyltransferase 1A1
- Sulfotransferase 4A1
- UDP-glucuronosyltransferase
Sequence:
MEFSRPPLVHVKGIPLIKYFAETIGPLQNFTAWPDDLLISTYPKSGTTWMSEILDMIYQGGKLEKCGRAPIYARVPFLEFKCPGVPSGLETLEETPAPRLLKTHLPLSLLPQSLLDQKVKVIYIARNAKDVVVSYYNFYNMAKLHPDPGTWDSFLENFMDGEVSYGSWYQHVKEWWELRHTHPVLYLFYEDIKENPKREIKKILEFLGRSLPEETVDSIVHHTSFKKMKENCMTNYTTIPTEIMDHNVSPFMRKGTTGDWKNTFTVAQNERFDAHYAKTMTDCDFKFRCEL
Protein: Serine/threonine-protein kinase MPS1 (EC 2.7.12.2) (Monopolar spindle protein 1 homolog) (Q84VX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. Implicated in spindle pole body (SPD) duplication (By similarity). May be a downstream regulator of auxin signaling in the formation of secondary roots (Probable).
Interaction partners:
- Kinetochore protein NDC80 homolog
- Mitotic spindle checkpoint protein MAD2
- Kinetochore protein NUF2 homolog
- Mitotic spindle checkpoint protein BUBR1
- ARM repeat superfamily protein
- Mitotic spindle checkpoint protein MAD1
- At5g05510
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Kinetochore protein SPC25 homolog
- Transcription factor PIF3
Sequence:
MDREDNLPVQPDKPPKSLVRPILNLETTSSSSSSSSSSPELLRHLQAAFKRHRPLSKMQTTSIGPRRSVAPQRQASRNTRLVTAEGQRSQDVVTLSQSLAANTLTQDTTNNLAITSVAGESASITQPTVSEHFNPSDRQMDFGKSAVTSLESNLDVQRKSQSLIGTSQDMEWDATNQAEASHLDACIGSKHQNLPSVDSEVSLKSEYKDSSSLAKIQGQLGEFPNFLNQPRTRCSAVGSSWATTTLIHSSSAPMLNATTHVSRSYVEADSNANPHAVQSQGNLPSCCPSSKVSNILHPNKDATASEMPASTNDPEVRVKETDTSKQQQITTGLEAPVGSSIYGSDGQANARLPEELHTSVSSQPQKSDKHEKVASSKGPSAPRKRNYDPDLFFKVNGKLYQRLGKIGSGGSSEVHKVISSDCTIYALKKIKLKGRDYATAYGFCQEIGYLKKLKGKTNIIQLIDYEVTDKTLLQEVLNGTMSNKDGRVKEDGFIYMVLEYGEIDLAHMLSQKWREIEGSDRTIDENWLRFYWQQILQAVNTIHEERIVHSDLKPANFLLVRGFLKLIDFGIAKAINSDTTNIQRDSQVGTLSYMSPEAFMCNESDENGNTIKCGRPSDIWSLGCILYQMVYGRTPFADYKTFWAKFKVITDPNHEITYNQLSNPWLIDLMKKCLAWDRNQRWRIPELLQHPFLAPPIPHEPQVKTIKLFSLIAESCGSDDDKANSMISQLEQLLSNPAPLPRNDVLDSRDQNQQLLSRVSELCIQLQDRLQGLEGEN
Protein: F-box/WD repeat-containing protein 8 (F-box and WD-40 domain-containing protein 8) (P0DL28)
Organism: Rattus norvegicus (Rat)
Function: Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (By similarity). The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8BIA4}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons (PubMed:21572988). Localizes to the cytosol when phosphorylated at Ser-84, promoting IRS1 ubiquitination (By similarity). {ECO:0000250|UniProtKB:Q8BIA4, ECO:0000269|PubMed:21572988}.
Interaction partners:
- Cullin-7
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase RBX1
- Cullin-1
- Cullin 7
- Glomulin, FKBP associated protein
- Cullin 9
- Obscurin-like protein 1
- Beta-transducin repeat containing E3 ubiquitin protein ligase
Sequence:
MEDHNLEEFRQRWQEELAHSQVLRRRRRLEAGERRPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRTDRKDVSSRSRSPPDRDAAEPEPLVDQLIRDLNEMDDVPFFDVHLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLCRQEGHLPHSRFSDYTCWKLILQECLAPVHLIRPSWMNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGEVRVWDTRTWDYVAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNVWDLRTGRFPIFRFEHDARIQALALSQEKPVVATASAFDVVMLYPNEEGNWHVASEFEVQKLVDYLEIVPNTGRYPVAIATAGDLVYLLKAEDSARTLHYVYGQPATCLDVSASQVAFGVKSLGWVYEGNKILVYSLEAERCLSKLGNALGDFTCVNIRDSPPNLMVSGNMDRRVRLHDLRTDKIALSLSAHQLGVSAVQMDDWKIVSGGEEGLVSVWDYRMNQKLWEVHSRHPVRYISFNSHSLITANVPYEKVLRNSDLDNFACHRRHRGLIHAYEFAVDQLAFQSPLPICRLPRDTVAGYSYDLALSFPYDSI
Protein: Vacuolar protein sorting-associated protein 51 homolog (Protein fat-free) (Q155U0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in retrograde transport from early and late endosomes to the late Golgi. The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. Acts as component of the EARP complex that is involved in endocytic recycling (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:16581006}. Recycling endosome {ECO:0000250|UniProtKB:Q9UID3}. Note=Also localizes in perinuclear region (PubMed:16581006). Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex (By similarity). {ECO:0000250|UniProtKB:Q9UID3, ECO:0000269|PubMed:16581006}.
Interaction partners:
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 53 homolog
- VPS54 subunit of GARP complex.
- Syndetin isoform X3
- VPS50 EARP/GARPII complex subunit.
- EARP-interacting protein homolog
- Syntaxin 16
- Stx6 protein
- Conserved oligomeric Golgi complex subunit 8
- Vacuolar protein sorting-associated protein 45
Sequence:
MSSATTPPDSDPAQRRRVHSMLKLYYGLNEEGKATEQAESLDPCDINGPHFDPEIYLNKLRKECSLTELMDHESCMVKQIRSLDSDMQTLVYENYNKFISATDTIRKMKNDFKKMEDEMDCLSANMAAITEFSARISGTLQDQHAQITKLSGVHTLLRKLQFLFELPARLNKCLELQAYAQAVSSHRRARCVLQQYSHMPSFRGIQDDCHVIMEQLAQQLRQKFRDGGSSAKDLSECVELLLQLDEPAEELCDKFLSHAQSRLEADLQGLEAELKDSAVTDTGAGSVQKTSPGSNPVSPSSSVSNPFLSPAAGTDILEFIDRGCNEFVSNLCLVIASYQELFINRPQESELASKNIPEMANGKLHVFVDTLAARYFSLVERRIQEEKGVGDNSLLVRALDRFHRRLQAISKLLPGSAVPSQGTEIVVRAARERIKQYLSALQTFYHDSLTDVRQALAAPRLSVGGASASGGGALVGGASSKDAPPSLPELLTSLSNFILNQLKSVLASVHLFTAKDITFSNKPYFKGEFCSQGVREGLVVSFIKFICQSSRQYCESAGDRGGSTPPALLLLLSRLCLDYETSTISYILTLTDEQFLVQHHTPVTPVTALCAEAREAAQKLLNHYVKVQGLIISQMLRKSVETRDWVNTIEPRNVRAVMKRVVEDTTSIDVQVGLLYEEGVRKAHSSDSSKRTFSVYSSSRQQIRYAPSYTPSAPMDTNLLSNIHKLFSERIDIFSPVEFNKVSVLTGIIKISLKTFLECVRLRTFGRYGLQQIQVDCHYLQMYLWRFVSDENLVHFLLDEIVGSAAHRCLDPSPMEQSVIEVICERG
Protein: Protein LATERAL BRANCHING OXIDOREDUCTASE 1 (EC 1.14.11.-) (Q9LIF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q94LP4}.
Interaction partners:
- Uncharacterized protein At1g62240
- Transmembrane protein, putative
- Filaggrin-like protein
- CCT motif family protein
- Hyperosmolality-gated Ca2+ permeable channel 1.5
- Hyperosmolality-gated Ca2+ permeable channel 1.6
- Cytochrome P450 711A1
- Strigolactone esterase D14
Sequence:
MAPLPISSIRVGKIDDVQELIKSKPNKVPERFIREEYERGVVVSSLKTHHLHHQIPVIDLSKLSKPDNDDFFFEILKLSQACEDWGFFQVINHGIEVEVVEDIEEVASEFFDMPLEEKKKYPMEPGTVQGYGQAFIFSEDQKLDWCNMFALGVHPPQIRNPKLWPSKPARFSESLEGYSKEIRELCKRLLKYIAISLGLKEERFEEMFGEAVQAVRMNYYPPCSSPDLVLGLSPHSDGSALTVLQQSKNSCVGLQILKDNTWVPVKPLPNALVINIGDTIEVLSNGKYKSVEHRAVTNREKERLTIVTFYAPNYEVEIEPMSELVDDETNPCKYRSYNHGDYSYHYVSNKLQGKKSLDFAKILN
Protein: Transcription factor EB (B0QYS7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSEEDRTFSFGPGTRKLGFMSQLSPACSVTLGKSLPLSGLGVFSSKMDAVPVILASPCQPLCFEEDTCLIYLLPLLIHREPAPAATMASRIGLRMQLMREQAQQEEQRERMQQQAVMHYMQQQQQQQQQQLGGPPTPAINTPVHFQSPPPVPGEVLKVQSYLENPTSYHLQQSQHQKVREYLSETYGNKFAAHISPAQGSPKPPPAASPGVRAGHVLSSSAGNSAPNSPMAMLHIGSNPERELDDVIDNIMRLDDVLGYINPEMQMPNTLPLSSSHLNVYSSDPQVTASLVGVTSSSCPADLTQKRELTDAESRALAKERQKKDNHNLIERRRRFNINDRIKELGMLIPKANDLDVRWNKGTILKASVDYIRRMQKDLQKSRELENHSRRLEMTNKQLWLRIQELEMQARVHGLPTTSPSGMNMAELAQQVVKQELPSEEGPGEALMLGAEVPDPEPLPALPPQAPLPLPTQPPSPFHHLDFSHSLSFGGREDEGPPGYPEPLAPGHGSPFPSLSKKDLDLMLLDDSLLPLASDPLLSTMSPEASKASSRRSSFSMEEGDVL
Protein: AT14664p (Q8MZC1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMKATAWFCPVLLTLLCATRLVCTAQRGAVGTGGAAGGSGAAAGGAEVGGSGRTNRYPLDYPDGTRNSQDDFLLAKRNKPSLSIVNPLDVLRQRLLLEIARRQMKENSRQVELNRAILKNVGKRVVLRGGGGGGGSGAGGLAPKVSRRYRQQWPVERELERERQREREREWDAVREEQLDRQQLLPWKHFPSQLWSYGWALSPYKESSQLQFADSQQSASTGPQSQALPKQLQLLSYAKKPLDVAGMSLARHRVSGNEANETNHENDDGNGASKNPARYVDDGDNEGEDSYNDVGTEGVGLGLGMGVGLGLERFEVLEDKPNWADEEPNELVVVNANDRVPWSFPYRFHKSQHNVN
Protein: Tubulin alpha-1B chain (EC 3.6.5.-) (Alpha-tubulin ubiquitous) (Tubulin K-alpha-1) (Tubulin alpha-ubiquitous chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain] (P81947)
Organism: Bos taurus (Bovine)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:2207090, ECO:0000269|PubMed:6504138, ECO:0000269|PubMed:7704569}.
Interaction partners:
- Doublecortin domain-containing protein
- Tubulin beta-4A chain
- Tubulin beta-4B chain
- Cell division control protein 42 homolog
- Gap junction alpha-1 protein
- Tubulin--tyrosine ligase
- Tubulin beta-2B chain
- Zona occludens protein 1
- MARVEL domain containing 2
- Tubulin beta 4B class IVb
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Protein: LexA repressor (EC 3.4.21.88) (A9BGA3)
Organism: Petrotoga mobilis (strain DSM 10674 / SJ95)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- Sugar-phosphate isomerase, RpiB/LacA/LacB family
- 3-dehydroquinate synthase N-terminal domain-containing protein
- DNA topoisomerase
- Epoxyqueuosine reductase QueH
- Uncharacterized protein
- Competence protein ComEA helix-hairpin-helix repeat protein
- Flagellar Assembly Protein A N-terminal region domain-containing protein
Sequence:
MEELTKRQSQVLDFIKSYMEKNGFAPSIRDIMKHFNFKSPRAAHKHLIILEKKGYIERKNVSRGIKMMPKSGEIFATETLAPVSGKIAAGDAIEAIQTISDYIPIPTNFFPKNYEYFSLRVEGNSMIEAQIKSGDFVLIRKQDYAMDGDIVVALIDGNDATLKRYKRLNEDEVLLIPENKSMKEIKVKADHLKIQGKMVGLIRVL
Protein: cAMP-dependent protein kinase type II-alpha regulatory subunit (C1PIG4)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSHIQIPPGLTELLQGYTVEVLRRQPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDLEPSSGLVTDAIADSESEDDEDLDVPIPSRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIKSKTKANKDGGNQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSMDLIDPGQ
Protein: Zuotin (DnaJ-related protein zuo1) (J protein zuo1) (Ribosome-associated complex subunit zuo1) (Q9Y7I8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Heat shock protein 70 homolog C57A7.12
- Ribosome-associated molecular chaperone sks2
- Probable heat shock protein ssa2
- Probable heat shock protein ssa1
- Eukaryotic peptide chain release factor GTP-binding subunit
- SAGA complex subunit Sgf29
- Large ribosomal subunit protein eL31
- Heat shock protein 104
- Heat shock protein homolog pss1
- Nascent polypeptide-associated complex subunit alpha
Sequence:
MSAGDSIQLFPPTTKQAIEASFVPHGKISPLIKRAVEPVGPLFLAHARRQRHGRTFSEDERLEVKNKVQEEVKEESEDEEEDPAMLRADPKEWKQQDHYAVLGLSKYRYKADTEQIKKAHLKKVLKHHPDKKAASGNINDDSFFKCIQKAYEILSDPVRRRQFDSVDENADVEPPESTTKETFFELWTPVFESEARFSKKQPVPSLGTIESTRAEVDNFYNFWYNFDSWRSFEYLDKDIPDDGESRDNKRFQEKKNRSERQKNKARDNARLRNLVDTALASDPRIKLFKEQEKAAKAARKWEREAGAREAAAAAQKKKEEEERRAAEEAAAKASAAAANKKAKEDKKKAQKRDKKVVKNALKDFNYFSATDVPSAEHVDSVLKDVDVIMSKLGEGELGQLAADINAEKAAGAASVQAVFDKFAKMFIERGSMSSADVVFFAQ
Protein: Ocho, isoform B (Ocho, isoform C) (RT02944p) (Q9VUI5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Enhancer of split m6 protein
- Bearded
- Enhancer of split m4 protein
Sequence:
MSAISKQKTLNTMYKSKVSPSRRLKNLLKPLLGQFFNMKKEQPKRSSYIASEEKEAEFEWLSNDMDNMANEHLEHRLIEEIRQCAKEDAVIVYNENGSGELHTIDQEDYYVPVHFARTNAGTFFWTSVQPKACEPYAIEWNFLDRWAQA
Protein: Transcriptional activator protein (TrAP) (Protein AC2) (Protein AL2) (P03562)
Organism: Tomato golden mosaic virus (strain Yellow vein) (TGMV)
Function: Strong activator of the late viral genes promoters. Enhances the expression of the capsid protein and nuclear shuttle protein. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. Suppresses the host RNA silencing by inhibiting adenosine kinase (ADK), a kinase involved in a general methylation pathway. Also suppresses the host basal defense by interacting with and inhibiting SNF1 kinase, a key regulator of cell metabolism implicated in innate antiviral defense. Determines pathogenicity.
Subcellular location: Host nucleus. Host cytoplasm. Note=The phosphorylated form appears to accumulate almost exclusively in the nucleus, whereas the non-phosphorylated form is found in both nucleus and cytoplasm.
Interaction partners:
Sequence:
MRNSSSSTPPSIKAQHRAAKRRAIRRRRIDLNCGCSIYIHIDCRNNGFTHRGTYHCASSREWRLYLGDNKSPLFQDNQRRGSPLHQHQDIPLTNQVQPQPEESIGSPQGISQLPSMDDIDDSFWENLFK
Protein: Protein NLP4 (AtNLP4) (NIN-like protein 4) (Nodule inception protein-like protein 4) (Q9LE38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00852}.
Interaction partners:
- MOB kinase activator-like 1B
- MOB kinase activator-like 2A
- Putative MOB kinase activator-like 2B
- Rop guanine nucleotide exchange factor 14
- Ferredoxin--nitrite reductase, chloroplastic
Sequence:
MEDSFLQSENVVMDADFMDGLLLDGCWLETTDGSEFLNIAPSTSSVSPFDPTSFMWSPTQDTSALCTSGVVSQMYGQDCVERSSLDEFQWNKRWWIGPGGGGSSVTERLVQAVEHIKDYTTARGSLIQLWVPVNRGGKRVLTTKEQPFSHDPLCQRLANYREISVNYHFSAEQDDSKALAGLPGRVFLGKLPEWTPDVRFFKSEEYPRVHHAQDCDVRGTLAIPVFEQGSKICLGVIEVVMTTEMVKLRPELESICRALQAVDLRSTELPIPPSLKGCDLSYKAALPEIRNLLRCACETHKLPLAQTWVSCQQQNKSGCRHNDENYIHCVSTIDDACYVGDPTVREFHEACSEHHLLKGQGVAGQAFLTNGPCFSSDVSNYKKSEYPLSHHANMYGLHGAVAIRLRCIHTGSADFVLEFFLPKDCDDLEEQRKMLNALSTIMAHVPRSLRTVTDKELEEESEVIEREEIVTPKIENASELHGNSPWNASLEEIQRSNNTSNPQNLGLVFDGGDKPNDGFGLKRGFDYTMDSNVNESSTFSSGGFSMMAEKKRTKADKTITLDVLRQYFAGSLKDAAKNIGVCPTTLKRICRQHGIQRWPSRKIKKVGHSLQKIQRVIDSVQGVSGPLPIGSFYANFPNLVSQSQEPSQQAKTTPPPPPPVQLAKSPVSSYSHSSNSSQCCSSETQLNSGATTDPPSTDVGGALKKTSSEIELQSSSLDETILTLSSLENIPQGTNLLSSQDDDFLRIKVSYGEEKIRLRMRNSRRLRDLLWEIGKRFSIEDMSRYDLKYLDEDNEWVLLTCDEDVEECVDVCRTTPSHTIKLLLQASSHHFPERSSATEYSLWH
Protein: Dipeptidase 1 (EC 3.4.13.19) (Beta-lactamase) (EC 3.5.2.6) (Dehydropeptidase-I) (Microsomal dipeptidase) (Renal dipeptidase) (hRDP) (P16444)
Organism: Homo sapiens (Human)
Function: Hydrolyzes a wide range of dipeptides including the conversion of leukotriene D4 to leukotriene E4. Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation. Possesses also beta lactamase activity and can hydrolyze the beta-lactam antibiotic imipenem.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:28413640}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2168407}. Cell projection, microvillus membrane {ECO:0000269|PubMed:2168407}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2168407}. Note=Brush border membrane. {ECO:0000250|UniProtKB:P31429}.
Interaction partners:
Sequence:
MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTTLAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETFLYVTSSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWADNWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVATMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGARAVGFGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWTEAEVKGALADNLLRVFEAVEQASNLTQAPEEEPIPLDQLGGSCRTHYGYSSGASSLHRHWGLLLASLAPLVLCLSLL
Protein: BHLH transcription factor (Os08g0490000 protein) (cDNA clone:J023030J22, full insert sequence) (Q6ZBQ2)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Os03g0726900 protein
Sequence:
MGLQGNKATHDFLSLYAAAATATDYSPLPRHPDSKPSAPAPPPAQDFFLKTHDFLPQVEKRADQTPPPPPPPPPHAAVTAEKQLLHQHALAAAGAFTINHAVAAAATAVKQEPPFAPWCQPVAAVDPRGHQWSLPFAARAVAVASSRPQQQQQQPPPPERKGGGGFMDAGSRSSGGAGFDDDDGHAARREVSSSLKELTVRVEGKGGSCSGSAGTDQMPNTPRSKHSATEQRRRSKINDRFQLLRDLLPHNDQKRDKASFLLEVIEYIRFLQEKVQKYEVSYPEWNQENAKVVPWTNIYFRSSWKNAQNKGQVPADHSPDPPELLKNGSPYMFPFTGNSDNNNAVETAAASGAQDQAETDPMSRVSYRSVDTPSPNNVADKVTSQPHAQLVRPSPAENHTVNCDKLNNSDLAIDEGTISLSSQYSQELLNKLNHALENSGIDLSQASISVQINLGKRAMKRSTPAATSTSKELTDPASNSQAMGRQLRLGDGAEEHRQASKRHKSDNS
Protein: LD27118p (Magi, isoform A) (Magi, isoform B) (Magi, isoform C) (Q9W2L2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Polychaetoid, isoform O
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MPIITATTTSTAGGGAGVAARGVATAKSPTDYLMLQQQQQQQQQQQQHFNSNHFYQQQQPQQLAPLNASHQHQHSHPHPHPHPVAAATSFATFNGNSNLNSSLANGSSRKFNCSRDNVDDGGDAGEMAAASQTLSSAGTDVVGNGSGHGNGTVTGNGEKSGGLAPPGGHHLRPPPPPALKKSASAVIGNSASREDVASLSGTSSLNSQMSVHNQFISGLPSNGIGSNGVHGGAATGRGGPPNSILKGSKENLLQNTYYNGETGDSSLGSECGVGDVQHQNHESHDDPGDGLGPLPPKWETAYTERGELYFIDHNTGTSHWLDPRLSKYQKKSLEDCCEDELPYGWEKIEDSMYGMYFIDHVNRRTQYENPVLEAKRRAAEQSQQQQQMQQQQQQMQEQRSKTPTALSETMPTEAAEAHEQEEDESPMKLPYKFTRNPAELQGQRINTTLLKSSRGLGFTIVGSDGSAGGDVEEFLQIKTVVPNGPAWLDGQLQTGDVLVYVNDTCVLGYTHHDMVNIFQSILPGERAALEVCRGYPLPFDPNDPNTEVVTTMAVDGRESDKQRRLNMDGNYNFLDLSGEGAKKTSGSGSGFILMKKPEIYTFSIMKGSMGFGFTIADSACGQIVKKILDRNCCTQLMEGDVLLEINGLNVRNKPHFYVVELLKECSQTTPTAVKIQRTPPDPPANNTLAQLNQVGNVAKLRKNFVGSGLFRSKTPTADLYSTQVKEVLPMRPKTPLVDTRRSRVQIQSPNNEVDDEGDGAAAAERKPLQLQTQGKSNSSLQELDDIPYMDPYPKISRLSERLAEVTLQGDANGGIYGMPPSMQPLPLPLAHHESCYCYDCQAQRYRPGYFVQAQQAAMSGTTGQYSPLQTAHLQNERIQRRVNELLSDRRRVGFANLDPPQQMQHSPSWRNGALLDVSEDADQCELTEVTLERQALGFGFRIVGGTEEGSQVTVGHIVPGGAADQDQRINTGDEILSIDGINVLNSSHHKVVSLVGESALRGQVTMILRRRRTPLLQQAPVSTQLRRYPYDVIVSRHENEGFGFVIISSSNHYYGSTIGKLIPGSPADRCGELKVGDRIVAVNRIEIAGMSHGDVVNLIKESGLHVRLTIGVPLKEGGPSPGGSSVGVSSNTPLQASPSLLKAQLSHQQQLPQQHLQQAQLNHHHQHLEMPMSMPVPGHGSYLERPSNNISATLALHQQPQL