wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (EC 2.4.1.15) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase) (P40387)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process. The disaccharide trehalose serves as a storage carbohydrate that is mobilized during nutrient stress and spore germination. Together with ntp1, regulates the level of trehalose as a protectant for cell integrity during thermal and osmotic stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytosolic neutral trehalase
- Trehalose-phosphatase
- Trehalose-phosphatase
- Putative alpha,alpha-trehalose-phosphate synthase 106 kDa subunit
- Putative alpha,alpha-trehalose-phosphate synthase 100 kDa subunit
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Catalase
Sequence:
MSDAHDTIKSLTGDASNSRRLIVVSNRLPITIKRKDNGTYDFSMSSGGLVSALSGLKKLMTFQWLGWCGQEIPEDEKPMIIQRLQDECSAIPVFLDDETADRHYNGFSNSILWPLFHYHPGEINFDEENWEAYRAANYAFAEAIVKNLQDGDLIWVQDYHLMVLPQMLRELIGDKFKDIKIGFFLHTPFPSSEIYRVLPVRNEILEGVLNCDLVGFHTYDYARHFLSACSRILNLSTLPNGVEYNGQMVSVGTFPIGIDPEKFSDALKSDVVKDRIASIERRLQGVKVIVGVDRLDYIKGVPQKFHAFEVFLEQYPEWVGKVVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGRFGTVEYTPIHFLHKSVRFEELVALYNVSDVCLITSTRDGMNLVSYEYICTQQERHGALILSEFAGAAQSLNGSIVINPWNTEELANSIHDALTMPEKQREANENKLFRYVNKYTSQFWGQSFVGELQRIQHYSHPHPRRTNPILRTKSAQVLSMNSSS
Protein: Coronin (A0A0B4KEU5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFRVVRSSKFRHVYGQALKREQCYDNIRVSKSSWDSTFCAVNPKFLAIIVESAGGGAFIVLPHNKVGRMWQVGRIAADHPLVGGHKGPVLDIAWCPHNDNVIASGSEDCVVKVWQIPDGGLSRTLTEPVVDLVFHQRRVGLVLWHPSALNVLLTAGSDNQVVIWNVGTGEILVHIDSHPDIVYSACFNWDGSKLVTTCKDKKIRIYDPRTAELESEAMCHEGSKATRAIFLRHGLIFTTGFNRSSERQYSLRAPDALNEPIVMVELDTSNGVMFPLYDADTNMIYLCGKGDSVIRYFEVTPEPPFVHYINTFQTTEPQRGIGLMPKRGCDVTTCEVAKFYRMNNNGLCQVISMTVPRKSDLFQEDLYPDTLAEDAAITAEEWIDGKDADPITFSLKGGYVSSSVNKSLPAKKAGNILNKPRGDSASSGATSSSAGGGNFASGNNNEASEGGPPAAVLSEKDLRTIQDEIRKLKAIIVKQENRIRALEAKEDARNKNGSDAAPASAGAATSDGKASESANDHASTSAGTSKDED
Protein: 3'-phosphate/5'-hydroxy nucleic acid ligase (EC 6.5.1.8) (Q389M0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA 3'-terminal phosphate cyclase-like protein
Sequence:
MRHAVTKLCIRATAGAGGGGRTDSAVFPGRKCCAVGETDHGSDVEPYTVIREEGSSVDVHAWVSGVEVERSAVEQLLQLSRLGDIIQHPVVAMPDVHTSNGATVGTVIPTTRAIIPASVGVDIGCGMIAVRTSLTQEDLPSSLAALRLAIEVAVPHGRTHNGRSGLDAGSWRNNIPESVAAVWRTQLQKGFEEICCMQKHIETSNHIEHLGTLGGGNHFIELCVDDGRKVDVGESYVEIGNSGSSGATSETSKGVSRQPNIWVMLHSGSRGVGNRIGTIFFELAKKDMGAHLANLPSADLAYLREGSEHFEQYVEAVYWAQLYAKLNREIMLDNVLRAVRKTIGRGFSVDALAINCHHNYVQRMELSAGVHVWLTRKGATSARAGELAVIPGSMGTRSYIVRGKGNPKSYSSCSHGAGRRYSRGEAKRRFTLEQHKTATKGIECRKDADVLDETPMAYKDIDDVMRAQDDLVEVVCVLRQLLCVKG
Protein: Mineralocorticoid receptor (MR) (Nuclear receptor subfamily 3 group C member 2) (Q8VII8)
Organism: Mus musculus (Mouse)
Function: Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:19029984}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Cytoplasmic and nuclear in the absence of ligand; nuclear after ligand-binding. When bound to HSD11B2, it is found associated with the endoplasmic reticulum membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Angiotensinogen
- Heat shock protein HSP 90-beta
- Glucocorticoid receptor
- Angiotensin-converting enzyme
- Renin-1
- Nuclear receptor coactivator 1
- 11-beta-hydroxysteroid dehydrogenase type 2
- Heat shock protein HSP 90-alpha
- Prostaglandin E synthase 3
Sequence:
METKGYHSLPEGLDMERRWSQVSQTLERSSLGPAERTNENSYMEIVNVSCVSGATPNNSTQGSSKEKHELLPCLQQDNSRSGILPSDIKTELESKELSATVAESMGLYMDSVRDAEYTYDQQNQQGSLSPAKIYQNMEQLVKFYKENGHRSSTLSAISRPLRSFMPDSGTSMNGGALRAIVKSPIICHEKSPSVCSPLNMPSSVCSPAGINSMSSSTASFGSFPVHSPITQGTSLTCSPSVENRGSRSHSPVHASNVGSPLSSPLSSMKSPISSPPSHCSVKSPVSSPNNVPLRSSVSSPANLNNSRCSVSSPSNTNNRSTLSSPTASTVGSIGSPISNAFSYTTSGASAGAGAIQDMVPSPDTHEKGAHDVPFPKTEEVEKAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNNKINPSSPFSVPIKQESSKHSCSGASFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDSSCEGSAFPGGIKQEPDDGSYFPETSIPSSAIIGVNSGGQSFHYRIGAQGTISLSRSPRDQSFQHLSSFPPVNALVESWKPHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGLHEEQPQQPPPPPPQSPEEGTTYIAPTKEPSVNSALVPQLASITRALTPSPSMILENIEPEIVYAGYDNSKPDTAESLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMRQISLQFVRLQLTFEEYSIMKVLLLLSTVPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNSSGQSWQRFYQLTKLLDSMHDLVNDLLEFCFYTFRESQALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK
Protein: LIN-46 (MoeA N-terminal and linker domain-containing protein) (G5EF06)
Organism: Caenorhabditis elegans
Interaction partners:
- Molybdopterin synthase catalytic subunit
- Molybdenum cofactor biosynthesis protein moc-5
- Hunchback-like protein
- Protein lin-28
- Putative transcription factor sel-7
- GTP 3',8-cyclase
- molybdopterin molybdotransferase
- sulfite oxidase
- Protein lin-14
- Adenylyltransferase and sulfurtransferase MOCS3
Sequence:
MSSSGLLKPATLDDVFQKLEDLCKLFPPQEKTVNVTSLKTGRILAEDIITEYDIPAQRTSIVDGFAIIVNQLGTKREIVGLSTAVTPYNAELISNECVRITIGGVVPDGADTVVPIENVALLKEEKCIEVLRKPKEGDNIREVGSEAKTGEILLKDGHHLDTMSITLLHALGISQVEIYKKPRVCVLSIGSDLNSNKMYGSFNRSQLLELFQSQGFTAIDAGSSTEHITEVEEKIRTAASFACVLVTVGGAQVIREVAKTLKFKFEIQDVDSTPGNFTVSTGKIDETPVVLSIFPEYHVSSWIGANLFVSPILRAMEGQNSETSHRFKAELTQPISKTSETRFLRARSEVSKGNLISTPLGCEDIFGANSILEVKSNTCFSAGDVVDLRFA
Protein: Zinc finger protein 93 (Zinc finger protein 505) (Zinc finger protein HTF34) (P35789)
Organism: Homo sapiens (Human)
Function: Transcription factor specifically required to repress long interspersed nuclear element 1 (L1) retrotransposons: recognizes and binds L1 sequences and repress their expression by recruiting a repressive complex containing TRIM28/KAP1. Not able to repress expression of all subtypes of L1 elements. Binds to the 5' end of L1PA4, L1PA5 and L1PA6 subtypes, and some L1PA3 subtypes. Does not bind to L1PA7 or older subtypes nor at the most recently evolved L1PA2 and L1Hs. 50% of L1PA3 elements have lost the ZNF93-binding site, explaining why ZNF93 is not able to repress their expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1
Sequence:
MGPLQFRDVAIEFSLEEWHCLDTAQRNLYRNVMLENYSNLVFLGIVVSKPDLIAHLEQGKKPLTMKRHEMVANPSVICSHFAQDLWPEQNIKDSFQKVILRRYEKRGHGNLQLIKRCESVDECKVHTGGYNGLNQCSTTTQSKVFQCDKYGKVFHKFSNSNRHNIRHTEKKPFKCIECGKAFNQFSTLITHKKIHTGEKPYICEECGKAFKYSSALNTHKRIHTGEKPYKCDKCDKAFIASSTLSKHEIIHTGKKPYKCEECGKAFNQSSTLTKHKKIHTGEKPYKCEECGKAFNQSSTLTKHKKIHTGEKPYVCEECGKAFKYSRILTTHKRIHTGEKPYKCNKCGKAFIASSTLSRHEFIHMGKKHYKCEECGKAFIWSSVLTRHKRVHTGEKPYKCEECGKAFKYSSTLSSHKRSHTGEKPYKCEECGKAFVASSTLSKHEIIHTGKKPYKCEECGKAFNQSSSLTKHKKIHTGEKPYKCEECGKAFNQSSSLTKHKKIHTGEKPYKCEECGKAFNQSSTLIKHKKIHTREKPYKCEECGKAFHLSTHLTTHKILHTGEKPYRCRECGKAFNHSATLSSHKKIHSGEKPYECDKCGKAFISPSSLSRHEIIHTGEKP
Protein: Superoxide dismutase [Cu-Zn] 1 (EC 1.15.1.1) (sodCI) (P0CW86)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Periplasm.
Interaction partners:
- Catalase
- Superoxide dismutase
- Superoxide dismutase
- Catalase-peroxidase
- Copper-exporting P-type ATPase
- Alkyl hydroperoxide reductase C
- Fimbrial usher
- Secretion system apparatus protein SsaQ
- Protein MgtC
- Inositol phosphate phosphatase SopB
Sequence:
MKYTILSLVAGALISCSAMAENTLTVKMNDALSSGTGENIGEITVSETPYGLLFTPHLNGLTPGIHGFHVHTNPSCMPGMKDGKEVPALMAGGHLDPEKTGKHLGPYNDKGHLGDLPGLVVNADGTATYPLLAPRLKSLSELKGHSLMIHKGGDNYSDKPAPLGGGGARFACGVIEK
Protein: 1,2-phenylacetyl-CoA epoxidase, subunit C (1,2-phenylacetyl-CoA epoxidase, structural subunit beta) (1,2-phenylacetyl-CoA monooxygenase, subunit C) (P76079)
Organism: Escherichia coli (strain K12)
Function: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit C may be essential for structural integrity of the alpha subunit.
Interaction partners:
- Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- Acyl-coenzyme A thioesterase PaaI
- 1,2-phenylacetyl-CoA epoxidase, subunit E
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- 1,2-epoxyphenylacetyl-CoA isomerase
- Phenylacetate-coenzyme A ligase
- Bifunctional protein PaaZ
- 3-hydroxyadipyl-CoA dehydrogenase
- 2,3-dehydroadipyl-CoA hydratase
Sequence:
MNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALANIGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNLLLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLAAISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAINKLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVFAGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQYLQRVLPGQQW
Protein: Large ribosomal subunit protein uL18y (60S ribosomal protein L5-2) (Ribosomal protein L5 B) (Protein OLIGOCELLULA 7) (P49227)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Seems involved in the regulation of cell proliferation. Essential in leaf polarity establishment, probably having a role for translation in leaf dorsoventral patterning to specify leaf adaxial identity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8LBI1}. Nucleus {ECO:0000250|UniProtKB:Q8LBI1}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8LBI1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8LBI1}.
Interaction partners:
- Large ribosomal subunit protein uL1y
- Probable elongation factor 1-gamma 2
- Large ribosomal subunit protein eL32y
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein eL21z/eL21y
- Large ribosomal subunit protein eL24y
- Large ribosomal subunit protein eL28z
- Large ribosomal subunit protein eL21x/eL21w
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein uL3z
Sequence:
MVFVKSSKSNAYFKRYQVKFRRRRDGKTDYRARIRLINQDKNKYNTPKYRFVVRFTNKDIVAQIVSASIAGDIVKASAYAHELPQYGLTVGLTNYAAAYCTGLLLARRVLKMLEMDDEYEGNVEATGEDFSVEPTDSRRPFRALLDVGLIRTTTGNRVFGALKGALDGGLDIPHSDKRFAGFHKENKQLDAEIHRNYIYGGHVSNYMKLLGEDEPEKLQTHFSAYIKKGVEAESIEEMYKKVHAAIRAEPNHKKTEKSAPKEHKRYNLKKLTYEERKNKLIERVKALNGAGGDDDDEDDEE
Protein: Phosphoribosyl-ATP pyrophosphatase (PRA-PH) (EC 3.6.1.31) (P9WMM9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- ATP phosphoribosyltransferase
- Phosphoribosyl-AMP cyclohydrolase
- Imidazoleglycerol-phosphate dehydratase
- Histidinol dehydrogenase
- Imidazole glycerol phosphate synthase subunit HisF
- Phosphoribosyl isomerase A
- Imidazole glycerol phosphate synthase subunit HisH
- Large ribosomal subunit protein bL31
- Histidinol-phosphate aminotransferase
- Uncharacterized protein Rv3403c
Sequence:
MQQSLAVKTFEDLFAELGDRARTRPADSTTVAALDGGVHALGKKLLEEAGEVWLAAEHESNDALAEEISQLLYWTQVLMISRGLSLDDVYRKL
Protein: Uncharacterized protein (Q57US3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNKQLLQTLPLAKGKDIHNRIAKLALYKECIALASSVSDPLVRQHTIVEVREKWLLSRGDGGQTLQLQLASALDRIAYGRMCVSKQRLRLIPNASEKYDWGVVNPLEHHAQRIQRREERESPDAFPHGAGRRDFVPMTNWGYGNMDPDAVMRHKELTDRQHFMGPHWRNKPKPVLLEDLSFEEQMYVQFQGKPKMKKTPKKHY
Protein: M-phase phosphoprotein 6 homolog (Exosome-associated RNA binding protein Mpp6) (O14076)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99547}. Note=Colocalizes with the nuclear exosome and ribosomes.
Interaction partners:
- Exosome complex component rrp43
- Exosome complex exonuclease rrp6
- Exosome complex protein C1739.07
- Exosome complex component rrp45
- Exosome complex component csl4
- Exosome complex component rrp4
- Exosome complex exonuclease dis3
- Pre-rRNA-processing protein las1
- NURS complex subunit red1
- Exosome complex component rrp46
Sequence:
MSSKLLSMKFMQRARGIDPKQAEEELSKNIVTDEHWSLAGKVDFLPQKMTRNVEYESGYGGLIEENDLESHSNEPNLVQGRASFGLFNKELGEENVDEKDVSKNEEVDVNGTKITDTSELTERERRKQELVSKKAEASRKMEVKAPAKESKKRKVNELSQDVISLHSPKESNARKTKKNKNKKKKKRN
Protein: Probable 2-OH-lauroyltransferase (Q9I7B5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004533}.
Interaction partners:
- 3-deoxy-D-manno-octulosonic acid transferase
- Probable queuosine precursor transporter
- Lipid A biosynthesis acyltransferase
- PilZ domain-containing protein
- DNA-3-methyladenine glycosylase I
- Lipid-A-disaccharide synthase
- UDP-3-O-acylglucosamine N-acyltransferase
- Tetraacyldisaccharide 4'-kinase
- TPR repeat-containing protein PA0015
- Arabinose 5-phosphate isomerase KdsD
Sequence:
MEKFKGALVVGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSETELEKLVGQSLMDIGRTLTESACAWIWPPEKSLRYIREVEGMEVLEEALASGDGLVGITSHLGNWEVLNHFYCSYAKPIIFYRPPKLKAVDELLKKQRVQLGNRVAPSTPEGILSVIKEVKKGGCVGIPADPEPARTAGLFVPYLGTTALISKFVPQLLSRGKARGVFFHAVRLPDGSGYKVILEAAPADMYDKDLEVSVAAMSRELAKYVRAYPSQYMWSMKRFKNRPDGEKKWY
Protein: Baculoviral IAP repeat-containing 3 (F7FLN8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- TNF receptor-associated factor
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Mitogen-activated protein kinase kinase kinase 7
- Myeloid differentiation primary response protein MyD88
- TNF receptor-associated factor
- TNF receptor-associated factor.
- Caspase-9
- Tumor necrosis factor receptor superfamily member 1A
- Diablo IAP-binding mitochondrial protein
Sequence:
MNMVQGSAFLAKLMKSADTFELKYDFSCELYRLSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFSCGLMLDNWKQGDSPIEKHRKLYPSCSFVQTLNPANSLEASPQPPLPSTATSTMPSGFAASESTGYFSGSYSSFPSDPVNFRANQDCPAFSTSPYHFAMNTEKARLLTYQTWPLSFLSPAELAKAGFYYTGPGDRVACFACGGKLSNWDRKDDPLSEHRRHFPSCPFLKDVGQFTSQYTVSNLSMQTHAARVRTFSTWPSSALVHPQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLIRIKGQEFVGQVQAGYPHLLEQLLSTSDSPEDETGEAAIVHLGPGENWEDAVMMNTPVVKAALDMGFSRSLVRQTVQRQILATGENYRTVSDLVIGLLDAEDEMREEQTEQEAEEEESDDLTLIRKNKMVLLQHLTPVTPILDCLLSARVITEQEYDAVKQKPHTLQARTLIDTVLAKGNTAATSFRNSLQEIDPGLYRDIFVRLCLKQNNISLFTALPMEEQLRKLQEERTCKVCMDREVSLVFIPCGHLVVCKECAPSLRKCPICRGTIKGTVRTFLS
Protein: Quaternary amine transport ATP-binding protein (EC 7.6.2.9) (Q9HXC2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|RuleBase:RU369116}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369116}.
Interaction partners:
- Glycine-betaine-binding protein
- Probable permease of ABC transporter
- Probable permease of ABC transporter
- Probable permease of ABC transporter
- Probable ATP-binding component of ABC transporter
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- Probable glycine betaine-binding protein
- Probable permease of ABC transporter
Sequence:
MIELDKLSKTFTQKNGKEFRAVDSVSLTVEKGEICVFLGPSGCGKTTTLKMINRIIPPTSGRVLIDGQDTADLDEVTLRRHIGYVIQQIGLFPNMTIEENIMVVPRLLGWDKARCKEKARELMSMVKLEPKQYLQRYPRELSGGQQQRVGVIRALAADAPLLLMDEPFGAVDPINRESIQNEFFEMQRKLGMTVIMVSHDIDEAIKLGDKVAVFKSGRLLQYDHPDTLLAHPADEFVSAFTGQDSTLKRLLLVRAEDAADSSLVTARPQTPVAEALELMDENDRRYLIVVDDQGKGLGYVRRKDLRRQEGTCAPFVTPFRVTASHDEHLRILLSRMYEFNSSWLPVLDPDQQFLGEVTQESIADYLSSGRSRGGKGLIVSPAEQVGA
Protein: Uncharacterized protein T25D10.1 (Q10017)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- F-box domain-containing protein
- F-box domain-containing protein
- CUB_2 domain-containing protein
- ShKT domain-containing protein
- CUB_2 domain-containing protein
- CUB-like domain-containing protein
- Cytochrome b561 domain-containing protein
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
- Cysteine-rich protein 1
Sequence:
MFLRRRNLNSSRIICIISIIVLLLIIISLYPHKRTQFGRYSRRQKTIRFQHSTGEIGDQLFSLLSHLGVAKTLYRIPVINSANNSKLIDTLSNAMFTRFPSILQQFLIAIEPPTAVNRELGIENSSYEDPLTKFSEDTSSSLMVKGNGFKSFKYFDNLRSDIRLWVLEDAESVLEAQNLITKSQRNNFKICVHATLESNKNCSVKAIAQILNHYTNEYEDVMLIIASPFPEFTRFIFTNSRIRKYKTEKFSLISSSPEMQIIFSRIYCDVVFLTVPYSTHGWWMGYLAKDDNSHVFYFDPDMFPKNRTANQEDYFPPKWKKLSRKIQ
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Q94469)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase
- Transketolase
- Glucose-6-phosphate isomerase
- Probable transaldolase
- Glucose-6-phosphate 1-dehydrogenase
- Hypoxanthine-guanine phosphoribosyltransferase
- Probable 2-ketogluconate reductase
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Sequence:
MVVPIGINGFGRIGRLVLRASLENPECRVLAINEPFMDVKYMVYMFKYDSTHGRFKGTVEDINGEFVVNGNKIHVFAEKDPANIKWSSVGAEYIVESTGLFLSTEKAGVHLKGGAKKVVISAPSTDAPMYVMGVNEETYESSHDVISNASCTTNCLAPLAKIIHENFGIVEGLMTTVHAITATQKTVDGPSGKDWRAGRSALSNIIPASTGAAKAVGKVLPALNGKLTGMSFRVPNCDVSVVDLTVRLEKKATYEEIKKVMKAASESDKYKRYIGYTEDEVVSTDFIGDTHSSIFDAHAGIALNDNFVKLVSWYDNEMGYSTRVIDLLVYISKKN
Protein: Transposase for insertion sequence element IS1557 (P9WKH7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MRNVRLFRALLGVDKRTVIEDIEFEEDDAGDGARVIARVRPRSAVLRRCGRCGRKASWYDRGAGLRQWRSLDWGTVEVFLEAEAPRVNCPTHGPTVVAVPWARHHAGHTYAFDDTVAWLAVACSKTAVCELMRIAWRTVGAIVARVWADTEKRIDRFANLRRIGIDEISYKRHHRYLTVVVDHDSGRLVWAAPGHDKATLGLFFDALGAERAAQITHVSADAADWIADVVTERCPDAIQCADPFHVVAWATEALDVERRRAWNDARAIARTEPKWGRGRPGKNAAPRPGRERARRLKGARYALWKNPEDLTERQSAKLAWIAKTDPRLYRAYLLKESLRHVFSVKGEEGKQALDRWISWAQRCRIPVFVELAARIKRHRVAIDAALDHGLSQGLIESTNTKIRLLTRIAFGFRSPQALIALAMLTLAGHRPTLPGRHNHPQISQ
Protein: Fermitin family homolog 2 (Kindlin-2) (F1Q8X5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling (By similarity). Required for normal embryonic development, including normal heart morphogenesis and normal angiogenesis.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250}. Cell surface {ECO:0000250}. Note=Colocalizes with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes with integrins at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides (By similarity). {ECO:0000250}.
Interaction partners:
- Scaffold protein ILK
- Filamin-binding LIM protein 1.
- Integrin beta.
- Integrin beta
- Integrin beta
- Integrin beta
- Integrin beta
- Integrin beta.
- Integrin beta
- Integrin beta
Sequence:
MALDGIRMPDGCYADGTWELKMHVTDLNRDVSLRVTGEIHIGGVMLKLVEKLDVKKDWSDHALWWEKKKTWLLKTHWTLDKYGIQADARLLFTPQHKLLRLQLPNMKHMRVKVNFSDRVFKAVSDICKTFNIRHPEELSLLRKPRDPKKKKKKLEDAEEETLELEGPLLTPGSGSIYSSPGLYSKTMTPTYDSRDGSPLSPTSAWFGDSPLSEGNPSILAVSQPITSPDILVKMYKPQSLLDKAKINQGWLDSSRSLMEQDVKENEVLLLRFKYHSFFDLNPKYDAIRVNQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMSSDNHMNNSEKEVDEVDAALSDLEITLEGGKTSNTLGDITSIPELADYVKVFKPKKLTLKGYKQYWCTFKDITISCYKSREEAHGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVADGMNEIWLRCDTEKQYAQWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHMNPDPQIIEPITTDINPECLVSPRYLKKYKNKQPGFVRDLISARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFLAKFQGGKKDELIGITYNRLIRMDAGTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEPSLAFICAEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV
Protein: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, mitochondrial (mtHD) (EC 4.2.1.59) (Q9FJI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 3-hydroxyl-[acyl-carrier-protein] (3-hydroxyl-ACP) dehydratase required for mitochondrial fatty acid synthesis (mtFAS). MtFAS are essential for photorespiration and plant development, probably by influencing mitochondrial membrane lipid composition and other lipid metabolic pathways.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:28202596}.
Interaction partners:
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- Peroxisome biogenesis protein 5
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Malate synthase
- Catalase-3
- Catalase-2
Sequence:
MLAKTVFPRGLLVLRSFSSVASKTLLKVGDVLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPGAVYVSQSLHFRSPVYIGDEILGLVQAIALRETKNKYIVKFSTKCFKNHNELVVIDGEATAILPNLDMLQKSPSE