wanglab/gogpt-training-data huggingface dataset:
Protein: Transforming acidic coiled-coil-containing protein 3 (ARNT-interacting protein) (Q9JJ11)
Organism: Mus musculus (Mouse)
Function: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (By similarity). May be involved in the control of cell growth and differentiation. May have a role in embryonic development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17920017}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y6A5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9PTG8}. Note=In complex with CKAP5 localized to microtubule plus-ends in mitosis and interphase. In complex with CKAP5 and clathrin localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250|UniProtKB:Q9Y6A5}.
Interaction partners:
- Aurora kinase A
- Targeting protein for Xklp2
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Clathrin heavy chain 1
- Serine/threonine-protein kinase PLK1
- Kinesin-like protein KIF22
- Borealin
- Neurogenic locus notch homolog protein 4
- Neurogenic locus notch homolog protein 3
- Cytoskeleton-associated protein 5
Sequence:
MSLHVLNDENVPNEKSSQCRDFQFLPPELTGRSSVLCLSQKENVPPQSQAKATNVTFQTPPRDPQTHRILSPNMTNKREAPFGLQNDHCVFLQKENQRPLAPVDDAPVVQMAAEILRAEGELQEGILTSSSLSASTSLLDSELVTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQELEPVLESELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPLLEPSHQGLEPVVDLKEESFRDPSEVLGTGAEVDYLEQFGTSSFKESAWRKQSLYVKFDPLLKDSPLRPMPVAPITNSTQDTEEESGSGKPTEAELVNLDFLGDLDVPVSAPTPVWSLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI
Protein: Uncharacterized protein Rv2030c (P9WLM1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- ATP-dependent 6-phosphofructokinase isozyme 2
- Universal stress protein Rv2028c
- Alpha-crystallin
- Putative NAD
- Putative zinc metalloprotease Rip3
- Hypoxic response protein 1
- Putative NAD
- Uncharacterized protein Rv0080
- Uncharacterized protein Rv1813c
- Probable nitrate/nitrite transporter NarK2
Sequence:
MLMTAAADVTRRSPRRVFRDRREAGRVLAELLAAYRDQPDVIVLGLARGGLPVAWEVAAALHAPLDAFVVRKLGAPGHDEFAVGALASGGRVVVNDDVVRGLRITPQQLRDIAEREGRELLRRESAYRGERPPTDITGKTVIVVDDGLATGASMFAAVQALRDAQPAQIVIAVPAAPESTCREFAGLVDDVVCATMPTPFLAVGESFWDFRQVTDEEVRRLLATPTAGPSLRRPAASTAADVLRRVAIDAPGGVPTHEVLAELVGDARIVLIGESSHGTHEFYQARAAMTQWLIEEKGFGAVAAEADWPDAYRVNRYVRGLGEDTNADEALSGFERFPAWMWRNTVVRDFVEWLRTRNQRYESGALRQAGFYGLDLYSLHRSIQEVISYLDKVDPRAAARARARYACFDHACADDGQAYGFAAAFGAGPSCEREAVEQLVDVQRNALAYARQDGLLAEDELFYAQQNAQTVRDAEVYYRAMFSGRVTSWNLRDQHMAQTLGSLLTHLDRHLDAPPARIVVWAHNSHVGDARATEVWADGQLTLGQIVRERYGDESRSIGFSTYTGTVTAASEWGGIAQRKAVRPALHGSVEELFHQTADSFLVSARLSRDAEAPLDVVRLGRAIGVVYLPATERQSHYLHVRPADQFDAMIHIDQTRALEPLEVTSRWIAGENPETYPTGL
Protein: Cyclin-G1 (Cyclin-G) (P39950)
Organism: Rattus norvegicus (Rat)
Function: May play a role in growth regulation. Is associated with G2/M phase arrest in response to DNA damage. May be an intermediate by which p53 mediates its role as an inhibitor of cellular proliferation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase Mdm2
- Cellular tumor antigen p53
- Cyclin G2
- Cyclin-G-associated kinase
- Cyclin-dependent kinase 1
- Cellular tumor antigen p53
- Cyclin-dependent kinase 5
Sequence:
MIEVLTTDSQKLLHQLNTLLEQESRCQPKVCGLKLIESAHDNGLRMTARLRDFEVKDLLSLTQFFGFDTETFSLAVNLLDRFLSKMKVQAKHLGCVGLSCFYLAVKSIEEERNVPLATDLIRISQYRFTVSDLMRMEKIVLEKVCWKVKATTAFQFLQLYYSLIRETLPFERRNDLNFERLEAQLKACHCRIIFSKAKPSVLALAIIALEIQALKYVELTEGVECIQKHSKISGRDLTFWQELVSKCLTEYSSNKCSKPNGQKLKWIVSGRTARQLKHSYYRITHLPTIPETMG
Protein: Retinol binding protein 3 (G3V8Q4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Clusterin-like protein 1
- Rhodopsin
- S-arrestin
- Interphotoreceptor matrix proteoglycan 1
- Opticin
Sequence:
MMREWVLVLSTLLCVLAGPTHLFQPSLVLDMAKVLLDNYCFPENLMGMQAAIEQAMKSHEILGISDPQTLAHVLTVGVQSSLNDPRLFISYEPSTLEAPQQAPALTDLTREELLAQIQRNIRHEVLEDNVGYLRVDDLPGQEVLSELGEFLVSHVWKQLTGTSSLVLDLRHCAGGHVSGIPYVISYLHPGNTVLHVDTIYDRPSNTTTEIWTLPKVLGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGALDLQKLRIGQSDFFLTVPVSRSLGPLGGGGQTWEGSGVLPCVGIPAEQALEKALAILTLRRALPGVVLRLQEALQDYYTLVDRVPGLLHHLASMDYSAVVSEEDLVTKLNAGLQAVSEDPRLLVRATGPRETPSRPETGPNEPPAVTPEVPKEEDARRALVDSVFQVSVLPGNVGYLRFDRFADASVLKTLGPYVLRQVWEPLQDTEHLIMDLRHNPGGPSSAVPLVLSYFQGPEAGPVRLFTTYDRRTNITQEHFSHKELLGQRYGNRRGVYLLTSHRTATAAEEFAFLMQSLSWATLVGEITAGSLLHTCTVPLLDSPEGGLTLTVPVLTFIDNHGEAWLGGGVVPDAIVLAEEALERAQEVLDFHRSLGALVEGTGRLLEAHYARPEIAEQARDLLQSKLAQGAYRTAVDLESLASQLTADLQEVSEDHRLLVFHSPGELVAEEVPLPPPAIPSPEELSYLIEALFKTDVLPGHLGYLRFDAMAELETVKAIGPQLVRLVWQRLVDTAALVVDLRYNPGSYSSAVPLLCSYFFEEEPRQHLYSVFDRATSRVTEIWTLPLVAGQRYGSHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALSVGIYQVDNSPLYASMPTQMALSATTGEAWDLAGVEPDITVPMSEALSTAQDIVALRAKVPTVLQTAGKLVADNYASPELGAKMAAKLSGLQSRYARVTSEGALAEMLGADLQMLSGDPHLKTAHIPEDAKDRIPGIVPMQIPSPEVFEDLIKFSFHTNVFEDNIGYLRFDMFGDCELLIQVSELLVEHIWKKIVHTDALIIDMRFNIGGPTSSISALCSYFFDEAPPVLLDKIYNRPNDSISELWTHSQLTGERYGSKKSVAILTSGVTAGAAEEFTYIMKRLGRALVVGEVTSGGCQPPQTYHVDDTHLYITIPTARSVGATDGSSWEGVGVTPNVVVSSELALTRAKEILQRALRA
Protein: Serine/threonine-protein kinase WNK8 (AtWNK8) (EC 2.7.11.1) (Protein kinase with no lysine 8) (Q944Q0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates flowering time by modulating the photoperiod pathway. Phosphorylates the vacuolar ATPase subunit C (VATC) and RGS1. Regulates EDM2 that, in turn, modulates development processes.
Subcellular location: Nucleus {ECO:0000269|PubMed:20149132}.
Interaction partners:
- Regulator of G-protein signaling 1
- Guanine nucleotide-binding protein subunit gamma 2
- Guanine nucleotide-binding protein subunit gamma 1
- Guanine nucleotide-binding protein alpha-1 subunit
- Protein trichome birefringence-like 26
- Small ribosomal subunit protein RACK1z
- V-type proton ATPase subunit C
- Protein ENHANCED DOWNY MILDEW 2
- Guanine nucleotide-binding protein subunit beta
- Small ribosomal subunit protein RACK1y
Sequence:
MASGSGFLGQISSMEEADFAEKDPSGRYIRYDDVLGRGAFKTVYKAFDEVDGIEVAWNLVSIEDVMQMPGQLERLYSEVHLLKALKHENIIKLFYSWVDEKNKTINMITELFTSGSLRVYRKKHRKVDPKAIKNWARQILKGLNYLHSQNPPVIHRDLKCDNIFVNGNTGEVKIGDLGLATVLQQPTARSVIGTPEFMAPELYEEEYNELVDIYSFGMCMLEMVTCEYPYNECRNQAQIYKKVTSNIKPQSLGKVDDPQVRQFIEKCLLPASSRPTALELSKDPFLARDGGKDSALLASSSTSSKYVRPPQLEHLPMDVDHNENKSVSSNEDYPWSQTIELQRIAENKEFRLRGERSDDVTASMVLRIADPSGKCRIVHFAFYLESDTATAIAEEMVEELHLTSQEVVVIADMIDDFIMQLLSDRTSSHHNQNSPRLTHEDHEAANQQTVNSKDEEAAGQSMKSDISADYYFPYSANDGNAAMEAGRDAESMSSYLDSCSMMSTIYNLSISDNDYPEDLKTELNLIESQFNQSFQDLLKLKEDAIENAKRKWITKKQKAVNIS
Protein: Calsequestrin-1 (Aspartactin) (Calsequestrin, skeletal muscle isoform) (Laminin-binding protein) (P19633)
Organism: Rattus norvegicus (Rat)
Function: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction (By similarity). Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07221}. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P07221}. Mitochondrion matrix {ECO:0000250|UniProtKB:O09165}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells. Preferentially forms linear and round aggregates in the endoplasmic reticulum (ER) of resting cells. In a minority of cells, homogeneously detected in the ER lumen. Colocalizes with STIM1 at endoplasmic reticulum in response to a depletion of intracellular calcium. {ECO:0000250|UniProtKB:P07221, ECO:0000250|UniProtKB:P31415}.
Interaction partners:
- Triadin
- Ryanodine receptor 2
- Inositol 1,4,5-trisphosphate/ryanodine receptor domain-containing protein
- Calsequestrin-2
- Calcium-transporting ATPase
- Ryanodine receptor 1
- Sarcalumenin
- Myosin light chain 1/3, skeletal muscle isoform
- Myozenin 1
- Voltage-dependent L-type calcium channel subunit alpha-1S
Sequence:
MRATDRMGARAVSKLRLALLFVLVLGTPRSGVQGEDGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSVYVFKGDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKSKDSEHYKAYEDAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVSFVEEHRRSTLRKLKPESMYETWEDDLDGIHIVAFAEEADPDGYEFLETLKAVAQDNTENPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSIWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDDDDDDDDDDDDDDD
Protein: Guanine nucleotide-binding protein G(o) subunit alpha (P51875)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. In the 1-cell embryo, probably together with gpa-16, controls nuclear rotation and spindle elongation during mitosis. During the first embryonic cell divisions, plays a role in gpr-1/2 cortical localization and in the proper orientation of EMS blastomere mitotic spindle. Polarity determinants (par genes) may regulate lin-5/gpr-1/gpr-2/goa-1 locally to create the asymmetric forces that drive spindle movement. Involved in chemosensory responses to attractive and repellent odors detected by AWC and AWB sensory neurons, respectively. In ASER neurons, acts downstream of glr-3 to regulate cold avoidance behavior via calcium signaling, and it may also play a role in sensing cold in the intestine. Negatively regulates axon regeneration after injury downstream of the inhibitory compound arachidonoyl ethanolamide (AEA) by antagonizing the activation of the JNK pathway (mlk-1/mek-1/kgb-1). In neurons, may negatively regulate diacylglycerol (DAG) production mediated by egl-30 signaling cascade and thereby negatively regulates acetylcholine release. Couples to the muscarinic acetylcholine receptor gar-2 to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons. Plays a role in the navigational capacity of sperm and the targeting of sperm derived from males to the fertilization site in the uterus of hermaphrodites. Involved in egg-laying and in regulating dopamine-mediated locomotion. Most likely couples to the dopamine receptors dop-2 and dop-3 to positively regulate the dopamine-mediated suppression of crh-1/CREB1 transcription factor activation in cholinergic SIA neurons in the presence of food.
Interaction partners:
- Spindle apparatus protein lin-5
- G-protein regulator 1
- Guanine nucleotide-binding protein subunit beta-1
- Chaperone ric-8
- G-protein regulator 2
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit alpha
- Regulator of G-protein signaling rgs-7
- Tetratricopeptide repeat protein 28
- Regulator of G-protein signaling 7
Sequence:
MGCTMSQEERAALERSRMIEKNLKEDGMQAAKDIKLLLLGAGESGKSTIVKQMKIIHESGFTAEDYKQYKPVVYSNTVQSLVAILRAMSNLGVSFGSADREVDAKLVMDVVARMEDTEPFSEELLSSMKRLWGDAGVQDCFSRSNEYQLNDSAKYFLDDLERLGEAIYQPTEQDILRTRVKTTGIVEVHFTFKNLNFKLFDVGGQRSERKKWIHCFEDVTAIIFCVAMSEYDQVLHEDETTNRMHESLKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICFPEYSGRQDYHEASAYIQAQFEAKNKSANKEIYCHMTCATDTTNIQFVFDAVTDVIIANNLRGCGLY
Protein: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 1) (PDH kinase 1) (Q15118)
Organism: Homo sapiens (Human)
Function: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:22195962}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- [Pyruvate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- L-lactate dehydrogenase A chain
- RAC-alpha serine/threonine-protein kinase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- [Pyruvate dehydrogenase
- Hypoxia-inducible factor 1-alpha
Sequence:
MRLARLLRGAALAGPGPGLRAAGFSRSFSSDSGSSPASERGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLCDLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHANRGVYPPIQVHVTLGNEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTDSIERLPVYNKAAWKHYNTNHEADDWCVPSREPKDMTTFRSA
Protein: Threonine--tRNA ligase (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Q97PI4)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
Interaction partners:
Sequence:
MINITFPDGAVREFESGVTTFEIAQSISNSLAKKALAGKFNGKLIDTTRAITEDGSIEIVTPDHEDALPILRHSAAHLFAQAARRLFPDIHLGVGPAIEDGFYYDTDNTAGQISNEDLPRIEEEMQKIVKENFPSIREEVTKDEAREIFKNDPYKLELIEEHSEDEGGLTIYRQGEYVDLCRGPHVPSTGRIQIFHLLHVAGAYWRGNSDNAMMQRIYGTAWFDKKDLKNYLQMREEAKERDHRKLGKELDLFMISQEVGQGLPFWLPNGATIRRELERYIVNKELVSGYQHVYTPPLASVELYKTSGHWDHYQEDMFPTMDMGDGEEFVLRPMNCPHHIQVFKHHVHSYRELPIRIAEIGMMHRYEKSGALTGLQRVREMSLNDGHLFVTPEQIQEEFQRALQLIIDVYEDFNLTDYRFRLSLRDPQDTHKYFDNDEMWENAQTMLRAALDEMGVDYFEAEGEAAFYGPKLDIQIKTALGKEETLSTIQLDFLLPERFDLKYIGADGEDHRPVMIHRGVISTMERFTAILIENYKGAFPTWLAPHQVTLIPVSNEKHVDYAWEVAKKLRDRGVRADVDERNEKMQFKIRASQTSKIPYQLIVGDKEMEDETVNVRRYGQKETQTVSVDNFVQAILADIANKSRVEK
Protein: AP-3 complex subunit mu (Adaptor-related protein complex 3 subunit mu) (O94669)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000250|UniProtKB:P38153}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P38153}; Peripheral membrane protein {ECO:0000250|UniProtKB:P38153}; Cytoplasmic side {ECO:0000250|UniProtKB:P38153}. Note=Localizes at the cell tip and the barrier septum (PubMed:16823372). Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (By similarity). {ECO:0000250|UniProtKB:P38153, ECO:0000269|PubMed:16823372}.
Interaction partners:
- AP-3 complex subunit beta
- AP-3 complex subunit delta
- AP-3 complex subunit sigma
- AP-1 complex subunit gamma-1
- AP-2 complex subunit alpha
- AP-1 complex subunit sigma-1
- AP-2 complex subunit sigma
- AP-1 complex subunit mu-1
- AP-1 complex subunit beta-1
- AP-2 complex subunit beta
Sequence:
MSTIEAIYLVDTNGALLLQLESRGRTSPITLEHIKNELFRYKLRNEEPPFILHNKNFLIFQELEEDVRLCIPTTCDTEPLYIHDIMRRIVDVVKTFFGGFNASKVEKNVCVIVQLLAEMIDYGYATCMEPNALQDIVPLPSFMNKFMAVTGLQTNTPTLARDTVPWRTAKAKYATNEFFIHVLERVSAVYQPNGKLAFGTVKSDMECKCQISGMPLLLLSLRPGTKLGNVRFHQSVNLKRWKQHPDQIEFIPPDGKFTLASFQTDFATQKSLPVVVEAKNKLDGRFEVRIRNTGKKSVENLKILITIPQALKSVTVTEGNYIFRASKYTHMEEGILEWSVKKLAWTSPALVLTGFLAPLKKDANSTEESSSYSKLEHLDLQYKLQGSTLHNFKVESLKMLNHPDKKSYKGVKHTIIAQNVSFRFR
Protein: Inositol oxygenase (EC 1.13.99.1) (Aldehyde reductase-like 6) (Kidney-specific protein 32) (Myo-inositol oxygenase) (MI oxygenase) (Renal-specific oxidoreductase) (Q9UGB7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Aldo-keto reductase family 1 member A1
- Inositol monophosphatase 1
- Inositol monophosphatase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- UDP-glucuronosyltransferase 1A9
- UDP-glucuronosyltransferase 2B10
- UDP-glucuronosyltransferase 2B7
- demerged
- UDP-glucuronosyltransferase 1A5
- UDP-glucuronosyltransferase 1A1
Sequence:
MKVTVGPDPSLVYRPDVDPEVAKDKASFRNYTSGPLLDRVFTTYKLMHTHQTVDFVRSKHAQFGGFSYKKMTVMEAVDLLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKVLALFGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPRYSTELGMYQPHCGLDRVLMSWGHDEYMYQVMKFNKFSLPPEAFYMIRFHSFYPWHTGRDYQQLCSQQDLAMLPWVREFNKFDLYTKCPDLPDVDKLRPYYQGLIDKYCPGILSW
Protein: Bifunctional purine biosynthesis protein ADE16 [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase) (AICAR transformylase); Inosine 5'-monophosphate cyclohydrolase (IMP cyclohydrolase) (EC 3.5.4.10) (ATIC) (IMP synthase) (Inosinicase)] (J9VJP1)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Also catalyzes the cyclization of FAICAR to IMP.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54113}.
Interaction partners:
Sequence:
MSSEAPIALLSVYDKTGLLPFAKSLKELGFRLLGSGGTAKMIREAGMEIEDVSNITKAPEMLGGRVKTLHPAVHGGILSRDIPSDLADLATNKISPITLVVCNLYPFVLQTAKPDCTLAGAIEEIDIGGVTLLRAAAKNHGRVSIISSPSDYETIVAELRAKGEVSAETRRGLAIKAFEDTKSYDEAISDYFRKVYATPGVEEEMKAGAGVGYQRLGLRYGANPHQKPAQAFVEQGEMPIKVLSGSPGYINLLDALNSWALVKELAAGLDLPAAASFKHVSPAGAAVGLPLDERAAKVFGVEDLKELSPLACAYARARGADRMSSFGDFIALSHTVDTPTAKIISREVSDGVIAPGYEPEALEILSKKKGGKYCVLQMDPTYVPPEIETRQVYGISLQQKRNDCKIDESLFKNVVTANKDLPKSAVTDLVVATLALKYTQSNSVCYALNGTVIGLGAGQQSRIHCTRLAGDKADNWWLRHHPRVLELPFKKGTKRADKANAIDLFVTGQAFEAEGGERAQWESLFETVPEPLTKEEREKHMKELTGVACASDAFFPFPDNVHRAKRSGATYLAAPSGSIMDKECIKAADESNLVFCHTDLRLFHH
Protein: Vacuolar v-SNARE NYV1 (R-SNARE NYV1) (New v-SNARE 1) (Synaptobrevin NYV1) (Q12255)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Vacuolar v-SNARE required for docking. Only involved in homotypic vacuole fusion. Required for Ca(2+) efflux from the vacuolar lumen, a required signal for subsequent membrane fusion events, by inhibiting vacuolar Ca(2+)-ATPase PMC1 and promoting Ca(2+) release when forming trans-SNARE assemblies during the docking step.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Single-pass type IV membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Syntaxin PEP12
- Vacuolar morphogenesis protein 7
- Vacuolar morphogenesis protein 6
- Alpha-soluble NSF attachment protein
- Integral membrane protein SED5
- Golgi SNAP receptor complex member 1
- Syntaxin VAM3
- Protein transport protein BET1
- t-SNARE affecting a late Golgi compartment protein 1
- t-SNARE VTI1
Sequence:
MKRFNVSYVEVIKNGETISSCFQPFQKNENYGTITSANEQITPVIFHNLIMDMVLPKVVPIKGNKVTKMSMNLIDGFDCFYSTDDHDPKTVYVCFTLVDMPKILPIRILSGLQEYESNATNELLSSHVGQILDSFHEELVEYRNQTLNSSGNGQSSNGNGQNTISDIGDATEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQKVKNITLLTFTIILFVSAAFMFFYLW
Protein: Copper transport protein (Q9VHS6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU367022}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367022}.
Interaction partners:
- P-type Cu
- Metal response element-binding transcription Factor-1, isoform C
- Copper transport protein ATOX1
- Metallothionein-2
- RE54080p
- Superoxide dismutase
- Protein Malvolio
Sequence:
MDHGSDDSTSTAKSCPMIMVFHAGHCERILWRGWVASTVTEFVLSALAIFLVSFLYEALKFLRQQLARREARRASEQLAAEQRRKNEAPAAGGCCSEAPLAEPREQTYWQRLFASSHIVQSLLNLLQIVISYLLMLIFMTFNYWLCLAVILGLGLGYFFFGWNKKNPDESECCP
Protein: Flagellar motor switch protein FliG (Q9WY63)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
Subcellular location: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar motor switch protein FliM
- Flagellar M-ring protein
- Flagellum-specific ATP synthase
- Flagellar export/assembly protein
- Motility protein A
- Flagellar basal-body rod protein FlgC
- Flagellar hook-associated protein 1
- Flagellar basal-body rod protein FlgB
- Flagellar hook-basal body complex protein FliE
- Flagellar biosynthesis protein FliQ
Sequence:
MPEKKIDGRRKAAVLLVALGPEKAAQVMKHLDEETVEQLVVEIANIGRVTPEEKKQVLEEFLSLAKAKEMISEGGIEYAKKVLEKAFGPERARKIIERLTSSLQVKPFSFVRDTDPVQLVNFLQSEHPQTIAVVLSYLDPPVAAQILGALPEELQTEVLKRIALLERTSPEVVKEIERNLEKKISGFVSRTFSKVGGIDTAAEIMNNLDRTTEKKIMDKLVQENPELADEIRRRMFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINIIRRLEEAGEIVIARGGGEELIM
Protein: Protein PELOTA 1 (AtPelota1) (Q9ZT87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal chromosome segregation during cell division and genomic stability (By similarity). May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48612}. Nucleus {ECO:0000250|UniProtKB:P48612}.
Interaction partners:
- Small ribosomal subunit protein eS6y
- T10F20.8 protein
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Protein PELOTA 2
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein eS6z
- Large ribosomal subunit protein uL18y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- DExH-box ATP-dependent RNA helicase DExH11
- At4g28210
Sequence:
MKIVRRDFVRNGPGSVKMVAEDSDDLWYAYNLIAVGDSVMAVTFRKVQREIPGGGRDSERVKLKLEVQVEEVDYDKDGSVLRIRGKNILENEHVKIGAFHTLELELKRPFVLRKEMWDSMALDTLKQASDPAASADLAVVLMQEGLAQIFLVGRSVTSSRARIETSIPRKHGPAIAGYESALKKFFENVLQAFVKHVDFSVVRCAVVASPGFTKDQFHRHLLLEAERRQLRPIIENKSRIILVHTNSGYRHSLGEVLHAPNVMNMIKDTKAAKEVKALNDFHNMLSTEPDRACYGPKHVEVANERMAIQTLLITDELFRNSDVKTRKKYVNLVESVKDSGGDAFIFSAMHVSGEQLAQLTGIAALLRFPLPELEDIEM