wanglab/gogpt-training-data huggingface dataset:
Protein: Laminin subunit beta-1 (Laminin B1 chain) (Laminin-1 subunit beta) (Laminin-10 subunit beta) (Laminin-12 subunit beta) (Laminin-2 subunit beta) (Laminin-6 subunit beta) (Laminin-8 subunit beta) (P07942)
Organism: Homo sapiens (Human)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.
Interaction partners:
- Laminin subunit gamma-1
- Laminin subunit alpha-5
- Laminin subunit alpha-4
- Laminin subunit alpha-1
- Integrin alpha-6
- Integrin beta-1
- Laminin subunit gamma-3
- Laminin subunit alpha-2
- Laminin subunit alpha-3
- Nidogen-2
Sequence:
MGLLQLLAFSFLALCRARVRAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICNSQDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCEASFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGFNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSISCHFDMAVYLATGNVSGGVCDDCQHNTMGRNCEQCKPFYYQHPERDIRDPNFCERCTCDPAGSQNEGICDSYTDFSTGLIAGQCRCKLNVEGEHCDVCKEGFYDLSSEDPFGCKSCACNPLGTIPGGNPCDSETGHCYCKRLVTGQHCDQCLPEHWGLSNDLDGCRPCDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYYFATLDHYLYEAEEANLGPGVSIVERQYIQDRIPSWTGAGFVRVPEGAYLEFFIDNIPYSMEYDILIRYEPQLPDHWEKAVITVQRPGRIPTSSRCGNTIPDDDNQVVSLSPGSRYVVLPRPVCFEKGTNYTVRLELPQYTSSDSDVESPYTLIDSLVLMPYCKSLDIFTVGGSGDGVVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALLHQTGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPSGCKPCECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWGFPSCQPCQCNGHADDCDPVTGECLNCQDYTMGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDDCASGYFGNPSEVGGSCQPCQCHNNIDTTDPEACDKETGRCLKCLYHTEGEHCQFCRFGYYGDALQQDCRKCVCNYLGTVQEHCNGSDCQCDKATGQCLCLPNVIGQNCDRCAPNTWQLASGTGCDPCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDVIIAELTNRTHRFLEKAKALKISGVIGPYRETVDSVERKVSEIKDILAQSPAAEPLKNIGNLFEEAEKLIKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKNSDIRGALDSITKYFQMSLEAEERVNASTTEPNSTVEQSALMRDRVEDVMMERESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDEGERKCGGPGCGGLVTVAHNAWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTCL
Protein: NAC domain-containing protein 26 (ANAC026) (Protein VASCULAR RELATED NAC-DOMAIN 5) (F4HYV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds to the secondary wall NAC binding element (SNBE), 5'-(T/A)NN(C/T)(T/C/G)TNNNNNNNA(A/C)GN(A/C/T)(A/T)-3', in the promoter of target genes (By similarity). Involved in xylem formation by promoting the expression of secondary wall-associated transcription factors and of genes involved in secondary wall biosynthesis and programmed cell death, genes driven by the secondary wall NAC binding element (SNBE). Triggers thickening of secondary walls.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9C8W9, ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- Transcription factor MYB46
- At5g52380
- Cysteine protease XCP1
- Transcription factor MYB83
- LOB domain-containing protein 15
Sequence:
MNSFSQVPPGFRFHPTDEELVDYYLRKKVASKRIEIDIIKDVDLYKIEPCDLQELCKIGNEEQSEWYFFSHKDKKYPTGTRTNRATKAGFWKATGRDKAIYIRHSLIGMRKTLVFYKGRAPNGQKSDWIMHEYRLETSENGTPQEEGWVVCRVFKKKLAATVRKMGDYHSSPSQHWYDDQLSFMASEIISSSPRQFLPNHHYNRHHHQQTLPCGLNAFNNNNPNLQCKQELELHYNQMVQHQQQNHHLRESMFLQLPQLESPTSNCNSDNNNNTRNISNLQKSSNISHEEQLQQGNQSFSSLYYDQGVEQMTTDWRVLDKFVASQLSNDEEAAAVVSSSSHQNNVKIDTRNTGYHVIDEGINLPENDSERVVEMGEEYSNAHAASTSSSCQIDL
Protein: Kanosamine-6-phosphate phosphatase (EC 3.1.3.92) (O07565)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the dephosphorylation of kanosamine 6-phosphate to yield kanosamine. There is a trace amount of activity using glucosamine-6-phosphate.
Interaction partners:
- 3-oxo-glucose-6-phosphate:glutamate aminotransferase
- Glucose-6-phosphate 3-dehydrogenase
- Glucose/mannose transporter GlcP
Sequence:
MLLSKKSEYKTLSTVEHPQYIVFCDFDETYFPHTIDEQKQQDIYELEDYLEQKSKDGELIIGWVTGSSIESILDKMGRGKFRYFPHFIASDLGTEITYFSEHNFGQQDNKWNSRINEGFSKEKVEKLVKQLHENHNILLNPQTQLGKSRYKHNFYYQEQDEINDKKNLLAIEKICEEYGVSVNINRCNPLAGDPEDSYDVDFIPIGTGKNEIVTFMLEKYNLNTERAIAFGDSGNDVRMLQTVGNGYLLKNATQEAKNLHNLITDSEYSKGITNTLKKLIGS
Protein: Charged multivesicular body protein 5 (Chromatin-modifying protein 5) (SNF7 domain-containing protein 2) (Vacuolar protein sorting-associated protein 60) (Vps60) (hVps60) (Q9NZZ3)
Organism: Homo sapiens (Human)
Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15644320}. Endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Midbody {ECO:0000269|PubMed:17853893}. Note=Localizes to the midbody of dividing cells (PubMed:17853893). Localized in two distinct rings on either side of the Flemming body (PubMed:17853893). {ECO:0000269|PubMed:17853893}.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1 homolog
- Vacuolar protein sorting-associated protein 4A
- IST1 homolog
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 6
- Charged multivesicular body protein 3
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 1b
- Charged multivesicular body protein 1a
- RNF103-CHMP3 readthrough
Sequence:
MNRLFGKAKPKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMREGPAKNMVKQKALRVLKQKRMYEQQRDNLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPELDEDDLEAELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGVLVDEFGLPQIPAS
Protein: Protein RecA (Recombinase A) (Q1IWF2)
Organism: Deinococcus geothermalis (strain DSM 11300 / CIP 105573 / AG-3a)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- DNA polymerase I
- CinA-like protein
- LexA-like repressor
- Regulatory protein RecX
- DNA repair protein RadA
- DNA 3'-5' helicase
- RNA 2',3'-cyclic phosphodiesterase
- DNA topoisomerase 1
- Beta sliding clamp
- ATP-dependent DNA helicase RecQ
Sequence:
MSKDNPKDFGTPSDSKERLKAIETAMTQIEKAFGKGSIMRLGAESKLDVQAVSTGSLSLDLALGVGGIPRGRITEIYGPESGGKTTLALSVIAQAQRAGGTCAFIDAEHALDPVYARSLGVNTDELLVSQPDNGEQALEIMELLVRSGAIDVVVVDSVAALTPRAEIEGEMGDSLPGLQARLMSQALRKLTAILSKTGTAAIFINQVREKIGVMYGNPETTTGGRALKFYASVRLDVRKIGQPVKLGNDAVGNTVKVKTVKNKVAPPFKEVELTLLYGKGFDQLSDLVTLAADMDIIKKAGSFYSYGEERIGQGKEKAIAYIAERPELEQEIRDRVLAAIKEGRDPIAAVPETPALAE
Protein: LD36772p (Q9W158)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH11843p
- Translational regulator orb2
- Uncharacterized protein, isoform B
- Uncharacterized protein, isoform A
- LD31543p
- Quaking related 54B, isoform E
- QKR58E-3
- RNA-binding protein spenito
Sequence:
MFVNSMTFRGNPANYHQQQPALNHHTLAAAHHQQQLHHHAAAAGHLSHVGGGHAASNHLAAAAVLGRHGHNSLGSGHTSTSSHSANVGVGVGGGALASGSTGGSGGNSSPDSGKIYIKNLERSIDNKAVYDTFSVFGNILNCNVAKDEDGNSRGYGFVHFDSEEAARAAIEKVNGMLCNNQKVHVVKFIPRRDREQEKATHFKNLYVKNLSEEFTEQHLREMFEPYGRITSHKLMLDEEGRSRRFGFVAYENPQSALAAVIGLHGKQLGDNKFLYVARALSKAERQQEINRKLEERKRQKAGQIFYY
Protein: NR LBD domain-containing protein (Q22759)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEYIKSRFVSLRDNLMLILDFLSEIGGPSEEQIDNYNIMKIKTNFFIDEIDFHLRGDVTSEQLMEYLGVYAIFYHRSRTELMKLLHEMCPNRHLNW
Protein: Fibroblast growth factor 20 (FGF-20) (Q9ESL9)
Organism: Mus musculus (Mouse)
Function: Neurotrophic factor that regulates central nervous development and function.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Klotho
- Fibroblast growth factor receptor 3
- Pro-epidermal growth factor
- Vascular endothelial growth factor receptor 2
- Decorin
- Beta-klotho
- Vascular endothelial growth factor receptor 3
Sequence:
MAPLTEVGAFLGGLEGLSQQVGSHFLLPPAGERPPLLGERRGALERGARGGPGSVELAHLHGILRRRQLYCRTGFHLQILPDGTVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQFEENWYNTYSSNIYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRPVDPERVPELYKDLLMYT
Protein: Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Fit-1) (Fos-responsive gene 1 protein) (Q62611)
Organism: Rattus norvegicus (Rat)
Function: Receptor for interleukin-33 (IL-33), its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function (By similarity). Upon tissue injury, induces UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages.
Subcellular location: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform B]: Secreted.
Interaction partners:
- Interleukin-33
- Interleukin-1 receptor accessory protein
- Myeloid differentiation primary response protein MyD88
- Thymic stromal lymphopoietin
- TNF receptor-associated factor 6
- Interleukin-1 receptor-associated kinase 1
- Interleukin-13
- Interleukin-1 receptor-associated kinase 4
- Interleukin-1 beta
- Interleukin-1 alpha
Sequence:
MIGKWRMGLWALAILTVPMYFIVTEGRKTSWGLENEALIVRCPQRGGAINPVEWYYSNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRSPESIKTGSLNVTIYKRPPNCKIPDYMMYSTVDGSDKNSKITCPTIALYNWTAPVQWFKNCKALQGPRFRAHMSYLFIDKVSHVDEGDYTCRFTHTENGTNYIVTATRSFTVEEKGFSTFPVITNPPHNYTVEVEIGKTANIACSACFGTASQFVAVLWQINKTRIGSFGKARIQEEKGPNKSSSNGMICLTSLLRITGVTDKDFSLKYDCVAMNHHGVIRHPVRLRRKQPIDHQSTYYIVAGCSLLLMFINVLVIVLKVFWIEVALFWRDIMAPYKTQNDGKLYDAYIIYPRVFRGSAAGTGSVEYFVHYTLPDVLENKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFAYEQEIALHSALIQNNSKVILIEMEPMGEASRLQLGDLQDSLQHLVKMQGTIKWREDHVADKQSLSSKFWKHVRYQMPVPKRPPKMASVAAPLSGKVCLDLKHF
Protein: Caffeine dehydrogenase subunit alpha (EC 1.17.5.2) (Caffeine dehydrogenase large subunit) (D7REY3)
Organism: Pseudomonas sp. (strain CBB1)
Function: Catalyzes the hydrolitical oxidation of 1,3,7-trimethylxanthine (caffeine) by incorporation of an oxygen atom originating from a water molecule into position C-8 to produce 1,3,7-trimethyluric acid (TMU). Coenzyme Q0 is the preferred electron acceptor and coenzyme Q2 can also be used, but oxygen and NADP cannot.
Interaction partners:
Sequence:
MFADINKGDAFGTWVGKSVPRREDADILAGRAEYIADIKLPGMLEAAFLRSPFAHARIVSIDVSQALALPGVYDVMVGADIPDYVKPLPLMITYQNHRETPTSPLARDIVRYAGEPVAVVAAINRYVAEDALELIVVKYEELPVVASIDASLAVDGPRLYEGWPDNVVAKVSSEIGDVDAAMASADLVFEERFEIQRCHPAPLETRGFIAQWDFKGENLNVWNGTQIINQCRDFMSEVLDIPASKIRIRSPRLGGGFGAKFHFYVEEPAIVLLAKRVKAPVRWIEDRLEAFSATVHAREQVIDVKLCAMNDGRITGIVADIKGDLGASHHTMSMGPVWLTSVMMTGVYLIPNARSVAKAIVTNKPPSGSYRGWGQPQANFAVERMVDLLAHKLQLDPAAVRRINYVPEARMPYTGLAHTFDSGRYEVLHDRALKTFGYEAWLERQAAAQAQGRRIGIGMSFYAEVSAHGPSRFLNYVGGRQGGYDIARIRMDTTGDVYVYTGLCDMGQGVTNSLAQIAADALGLNPDDVTVMTGDTALNPYTGWGTGASRSITIGGPAVMRAATRLREKILSIARHWLQADPDTLVLANRGVMVRDDPGRYVSFASIGRAAYCQIIELPEDVEPGLEAVGVFDTVQLAWPYGMNLVAVEVDEDTGAVSFLDCMLVHDMGTIVNPMIVDGQLHGGIAQGIAQALYEELRYDENGQLGTGSFADFLMPTASEIPNMRFDHMVTESPLIPGGMKGVGEGGTIGTPAAVVNAIENALRPITNSKLNRTPVTPDRILTAISAGACA
Protein: ATP phosphoribosyltransferase (ATP-PRT) (ATP-PRTase) (EC 2.4.2.17) (P60757)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Subcellular location: Cytoplasm.
Interaction partners:
- Histidinol-phosphate aminotransferase
- Histidinol dehydrogenase
- Histidine biosynthesis bifunctional protein HisIE
- Imidazole glycerol phosphate synthase subunit HisH
- 1-
- Imidazole glycerol phosphate synthase subunit HisF
- Histidine biosynthesis bifunctional protein HisB
- Ribose-phosphate pyrophosphokinase
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- Histidine--tRNA ligase
Sequence:
MTDNTRLRIAMQKSGRLSDDSRELLARCGIKINLHTQRLIAMAENMPIDILRVRDDDIPGLVMDGVVDLGIIGENVLEEELLNRRAQGEDPRYFTLRRLDFGGCRLSLATPVDEAWDGPLSLNGKRIATSYPHLLKRYLDQKGISFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLREVEVIYRSKACLIQRDGEMEESKQQLIDKLLTRIQGVIQARESKYIMMHAPTERLDEVIALLPGAERPTILPLAGDQQRVAMHMVSSETLFWETMEKLKALGASSILVLPIEKMME
Protein: Potassium voltage-gated channel protein egl-36 (Egg-laying defective protein 36) (G5EFC3)
Organism: Caenorhabditis elegans
Function: Voltage-dependent potassium channel involved in the excitation of muscles operating egg-laying and defecation.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P08510}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08510}.
Interaction partners:
- Ubiquitin-like domain-containing protein
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein eS6
Sequence:
MLDACSFNRFDSNRSSARRFSRRGSDYFGDKGISMDERIVLNVGGVRHETYQATLKKIPATRLSRLTPSLANFDPLLNEYFFDRHPAVFAMILNYYRTGKLHYPTDVCGPLFEEELQYWGLDASDTEPCCWMQLLHAKDTQETLAVLDRMDADHEDDPQLREQDTMKKFGWEEDYFQGKRTRWMKLKPQMWSLFDEPYSSQAAKLIAGISVLFIFISIFSFCLKTHQSFRLPVLIGQNITMPGGVVQPSIERVSTEPLPIFGQIEMLCNIWFTLELIIRFVFCPSKIRFFKSPLNMIDLVATLSFYADAMMVRVVEDEPKDVVEFLSMIRIFRLFKLTQHHQGLQILIHTFRASAKELILLVFFLILGIVIFAALVYYAEKMEANPNNQFQSIPLGLWWAICTMTTVGYGDMTPHTSFGRLVGSLCAVMGVLTIALPVPVIVSNFAMFYSHNQARDKLPKRRRRVLPVEQIRLQARRHAAVLEPSASQGGLGGGQAIRRRNMPILIDQNCCDEENHNHKHREKSENSDEGTNSSSTTGVDTVVKLGPSETAITTTIIS
Protein: Tetranectin (TN) (C-type lectin domain family 3 member B) (Q2KIS7)
Organism: Bos taurus (Bovine)
Function: Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis (By similarity). Plays a role in retinal function (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Plasminogen
- Tumor necrosis factor
Sequence:
MELWGPCVLLCLFSLLTQVTAETPTPKAKKAANAKKDAVSPKMLEELKTQLDSLAQEVALLKEQQALQTVCLKGTKVHMKCFLAFVQAKTFHEASEDCISRGGTLGTPQTGSENDALYEYLRQSVGSEAEVWLGFNDMASEGSWVDMTGGHIAYKNWETEITAQPDGGKVENCATLSGAANGKWFDKRCRDKLPYVCQFAIV
Protein: Ribitol 5-phosphate transferase FKRP (EC 2.7.8.-) (Fukutin-related protein) (Ribitol-5-phosphate transferase) (Q9H9S5)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a ribitol 5-phosphate from CDP-L-ribitol to the ribitol 5-phosphate previously attached by FKTN/fukutin to the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1). This constitutes the second step in the formation of the ribose 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17554798, ECO:0000269|PubMed:21886772, ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:29477842, ECO:0000305|PubMed:26923585}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:19900540}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q8CG64}. Rough endoplasmic reticulum {ECO:0000269|PubMed:15213246}. Cytoplasm {ECO:0000250|UniProtKB:Q8CG64}. Note=According to some studies the N-terminal hydrophobic domain is cleaved after translocation to the Golgi apparatus and the protein is secreted (PubMed:19900540). Localization at the cell membrane may require the presence of dystroglycan (By similarity). At the Golgi apparatus localizes to the middle-to-trans-cisternae, as assessed by MG160 colocalization. Detected in rough endoplasmic reticulum in myocytes (PubMed:17554798, PubMed:21886772). In general, mutants associated with severe clinical phenotypes are retained within the endoplasmic reticulum (PubMed:15213246). {ECO:0000250|UniProtKB:Q8CG64, ECO:0000269|PubMed:15213246, ECO:0000269|PubMed:17554798, ECO:0000269|PubMed:19900540, ECO:0000269|PubMed:21886772}.
Interaction partners:
- Ribitol-5-phosphate transferase FKTN
- Ribitol-5-phosphate xylosyltransferase 1
- Protein O-mannosyl-transferase 2
- Protein O-mannosyl-transferase 1
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Dystroglycan 1
- Laminin subunit alpha-2
- Alpha-sarcoglycan
- Calpain-3
- Anoctamin-5
Sequence:
MRLTRCQAALAAAITLNLLVLFYVSWLQHQPRNSRARGPRRASAAGPRVTVLVREFEAFDNAVPELVDSFLQQDPAQPVVVAADTLPYPPLALPRIPNVRLALLQPALDRPAAASRPETYVATEFVALVPDGARAEAPGLLERMVEALRAGSARLVAAPVATANPARCLALNVSLREWTARYGAAPAAPRCDALDGDAVVLLRARDLFNLSAPLARPVGTSLFLQTALRGWAVQLLDLTFAAARQPPLATAHARWKAEREGRARRAALLRALGIRLVSWEGGRLEWFGCNKETTRCFGTVVGDTPAYLYEERWTPPCCLRALRETARYVVGVLEAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLEDVGNCEQLRGAEAGSVVDERGFVWEKAVEGDFFRVQYSESNHLHVDLWPFYPRNGVMTKDTWLDHRQDVEFPEHFLQPLVPLPFAGFVAQAPNNYRRFLELKFGPGVIENPQYPNPALLSLTGSG
Protein: B-cell receptor-associated protein 29 (BCR-associated protein 29) (Bap29) (Q9UHQ4)
Organism: Homo sapiens (Human)
Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- B-cell receptor-associated protein 31
- tRNA-dihydrouridine
Sequence:
MTLQWAAVATFLYAEIGLILIFCLPFIPPQRWQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIEKSSTSRPDAYEHTQMKLFRSQRNLYISGFSLFFWLVLRRLVTLITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQDRLERGNKKRL
Protein: Squalene synthase (SlSS) (EC 2.5.1.21) (D0VFU8)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Farnesyl pyrophosphate synthase
- squalene monooxygenase
- Squalene monooxygenase
- sterol 14alpha-demethylase
- Beta-amyrin synthase
- Uncharacterized protein
- Uncharacterized protein
- Delta-amyrin synthase
- Terpene cyclase/mutase family member
- Squalene cyclase N-terminal domain-containing protein
Sequence:
MGTLRAILKNPDDLYPLIKLKLAARHAEKQIPPEPHWGFCYLMLQKVSRSFALVIQQLPVELRDAVCIFYLVLRALDTVEDDTSIPTDVKVPILISFHQHVYDREWHFACGTKEYKVLMDQFHHVSTAFLELGKLYQQAIEDITMRMGAGMAKFICKEVETTDDYDEYCHYVAGLVGLGLSKLFHASGKEDLASDSLSNSMGLFLQKTNIIRDYLEDINEVPKCRMFWPREIWSKYVNKLEDLKYEENSVKAVQCLNDMVTNALSHVEDCLTYMFNLHDPAIFRFCAIPQVMAIGTLAMCYDNIEVFRGVVKMRRGLTAKVIDRTKTMADVYGAFFDFSCMLKSKVNNNDPNATKTLKRLDAILKTCRDSGTLNKRKSYIIRNEPNYSPVLIVVIFIILAIILAQLFGSRS
Protein: Rho-related protein racE (Q23862)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Specifically required for cytokinesis.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Formin-A
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- Formin-F
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Protein SCAR
- Mss4-like family protein
- Cofilin-1A
Sequence:
MSEDQGSGATRVKLVVVGDGAVGKTCLLICYAQNDFPVDYVPTVFENYTATRKRGNEDIKVHLWDTAGQEEYDRLRPLSYPGADVVLLCFSTISQSSYEAIRDKWAPEVNHYIPDVPSILVGTKIDLREQQHPDPNSGKFEPITADMGISMQKQIKAKKYLEVSAKTRQGLEEVFSAAIEIVLESRGMDKKSQDGSSSASGVPSGDKPTKGKAGKKKSGCIIL
Protein: 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing] (DCR) (EC 1.3.1.34) (2,4-dienoyl-coenzyme A reductase [NADPH]) (P42593)
Organism: Escherichia coli (strain K12)
Function: Functions as an auxiliary enzyme in the beta-oxidation of unsaturated fatty acids with double bonds at even carbon positions. Catalyzes the NADPH-dependent reduction of the C4-C5 double bond of the acyl chain of 2,4-dienoyl-CoA to yield 2-trans-enoyl-CoA. Acts on both isomers, 2-trans,4-cis- and 2-trans,4-trans-decadienoyl-CoA, with almost equal efficiency. Is not active with NADH instead of NADPH. Does not show cis->trans isomerase activity.
Interaction partners:
- Glutamate synthase large chain
- Fatty acid oxidation complex subunit alpha
- Acyl-coenzyme A dehydrogenase
- Respiratory nitrate reductase 1 beta chain
- 3-ketoacyl-CoA thiolase FadA
- Long-chain acyl-CoA thioesterase FadM
- Respiratory nitrate reductase 2 beta chain
- Long-chain-fatty-acid--CoA ligase
- Putative electron transfer flavoprotein subunit YgcR
- Protein FixA
Sequence:
MSYPSLFAPLDLGFTTLKNRVLMGSMHTGLEEYPDGAERLAAFYAERARHGVALIVSGGIAPDLTGVGMEGGAMLNDASQIPHHRTITEAVHQEGGKIALQILHTGRYSYQPHLVAPSALQAPINRFVPHELSHEEILQLIDNFARCAQLAREAGYDGVEVMGSEGYLINEFLTLRTNQRSDQWGGDYRNRMRFAVEVVRAVRERVGNDFIIIYRLSMLDLVEDGGTFAETVELAQAIEAAGATIINTGIGWHEARIPTIATPVPRGAFSWVTRKLKGHVSLPLVTTNRINDPQVADDILSRGDADMVSMARPFLADAELLSKAQSGRADEINTCIGCNQACLDQIFVGKVTSCLVNPRACHETKMPILPAVQKKNLAVVGAGPAGLAFAINAAARGHQVTLFDAHSEIGGQFNIAKQIPGKEEFYETLRYYRRMIEVTGVTLKLNHTVTADQLQAFDETILASGIVPRTPPIDGIDHPKVLSYLDVLRDKAPVGNKVAIIGCGGIGFDTAMYLSQPGESTSQNIAGFCNEWGIDSSLQQAGGLSPQGMQIPRSPRQIVMLQRKASKPGQGLGKTTGWIHRTTLLSRGVKMIPGVSYQKIDDDGLHVVINGETQVLAVDNVVICAGQEPNRALAQPLIDSGKTVHLIGGCDVAMELDARRAIAQGTRLALEI