wanglab/gogpt-training-data huggingface dataset:
Protein: Benzyl alcohol O-benzoyltransferase (PhBEBT1) (EC 2.3.1.196) (Acetyl CoA:3-hydroxybenzyl alcohol acetyltransferase) (EC 2.3.1.-) (Acetyl CoA:benzyl alcohol acetyltransferase) (EC 2.3.1.224) (Acetyl CoA:geraniol acetyltransferase) (EC 2.3.1.-) (Benzoyl coenzyme A:benzyl alcohol benzoyl transferase) (Benzyl CoA:benzyl alcohol/phenylethanol benzoyltransferase) (PhBPBT) (Benzyl CoA:(3Z)-hex-3-en-1-ol benzoyltransferase) (EC 2.3.1.-) (Benzyl CoA:2-phenylethanol benzoyltransferase) (EC 2.3.1.-) (Benzyl CoA:3-hydroxybenzyl alcohol benzoyltransferase) (EC 2.3.1.-) (Benzyl CoA:butanol benzoyltransferase) (EC 2.3.1.-) (Benzyl CoA:geraniol benzoyltransferase) (EC 2.3.1.-) (Benzyl CoA:octan-1-ol benzoyltransferase) (EC 2.3.1.-) (Q6E593)
Organism: Petunia hybrida (Petunia)
Function: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta). Acyltransferase that catalyzes the transfer of benzoyl and acetyl moieties to a large variety of potential substrate alcohols, and involved in the formation of volatile esters benzyl benzoate and phenylethyl benzoate from benzoyl-CoA. With acetyl-CoA, mainly active on benzyl alcohol, and, to a lower extent, on 3-hydroxybenzyl alcohol, geraniol, and 2-phenylethanol, but barely active on butanol, 1-octanol, 4-hydroxy-benzyl alcohol, 2-hexanol, cis-3-hexen-1-ol and linalool. With benzoyl-CoA, mainly active on benzyl alcohol, but also efficient on several substrates, including 3-hydroxybenzyl alcohol, 2-phenylethanol, geraniol, butanol, cis-3-hexen-1-ol and 1-octanol.
Interaction partners:
Sequence:
MDSKQSSELVFTVRRQEPELIAPAKPTPRETKFLSDIDDQEGLRFQIPVINFYRKDSSMGGKDPVEVIKKAIAETLVFYYPFAGRLREGNDRKLMVDCTGEGVMFVEANADVTLEEFGDELQPPFPCLEELLYDVPGSAGVLHCPLLLIQVTRLRCGGFIFALRLNHTMSDAPGLVQFMTAVGEMARGATAPSTLPVWCRELLNARNPPQVTCTHHEYEEVPDTKGTLIPLDDMVHRSFFFGPTEVSALRRFVPPHLHNCSTFEVLTAALWRCRTISIKPDPEEEVRVLCIVNARSRFNPQLPSGYYGNAFAFPVAVTTAEKLCKNPLGYALELVKKTKSDVTEEYMKSVADLMVIKGRPHFTVVRTYLVSDVTRAGFGEVDFGWGKAVYGGPAKGGVGAIPGVASFYIPFRNKKGENGIVVPICLPGFAMEKFVKELDSMLKGDAQLDNKKYAFITPAL
Protein: Pentatricopeptide repeat-containing protein At1g07590, mitochondrial (Q940Q2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Small RNA 2'-O-methyltransferase
- Regulator of Vps4 activity in the MVB pathway protein
- Transcription factor bHLH145
- Metallothionein-like protein 1A
- Uncharacterized protein F15D2.6
Sequence:
MRSIIALMRQREYFVQAIRRTTCVASPALNQTNFQASSFLTTLISSKKSPEETCIGSEEEEEEPNKCLSLRIEKLPKGVTVGSALQSWMGDGFPVHGGDVYHAINRLRKLGRNKRALELMEWIIRERPYRLGELEYSYLLEFTVKLHGVSQGEKLFTRVPQEFQNELLYNNLVIACLDQGVIRLALEYMKKMRELGYRTSHLVYNRLIIRNSAPGRRKLIAKDLALMKADKATPHVSTYHILMKLEANEHNIDGVLKAFDGMKKAGVEPNEVSYCILAMAHAVARLYTVAEAYTEEIEKSITGDNWSTLDILMILYGRLGKEKELARTWNVIRGFHHVRSKSYLLATEAFARVGNLDRAEELWLEMKNVKGLKETEQFNSLLSVYCKDGLIEKAIGVFREMTGNGFKPNSITYRHLALGCAKAKLMKEALKNIEMGLNLKTSKSIGSSTPWLETTLSIIECFAEKGDVENSEKLFEEVKNAKYNRYAFVYNALFKAYVKAKVYDPNLFKRMVLGGARPDAESYSLLKLVEQYKP
Protein: Peroxisomal coenzyme A diphosphatase NUDT7 (EC 3.6.1.-) (EC 3.6.1.77) (Nucleoside diphosphate-linked moiety X motif 7) (Nudix motif 7) (Q99P30)
Organism: Mus musculus (Mouse)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Cleaves CoA, CoA esters and oxidized CoA with similar efficiencies. Preferentially hydrolyzes medium-chain acyl-CoAs and bile acid-CoAs. Has no activity toward NDP-sugars, CDP-alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in this organelle in response to metabolic demand. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
Subcellular location: Peroxisome {ECO:0000269|PubMed:11415433, ECO:0000269|PubMed:18799520}.
Interaction partners:
- Acyl-coenzyme A diphosphatase NUDT19
- NAD-capped RNA hydrolase NUDT12
Sequence:
MSRPCGLPEPVRNNLIDDAKARLRKSDVGTRYSHLSSNKFSVLVPLLARGGKLYLMFTVRSDKLKREPGEVCFPGGKRDPVDTDDTATALREAQEEVGLHPHQVEVVSHLVPYVFDNDALVTPVVGFLDHNFQAQPNADEVKEVFFVPLDYFLHPQVYYQKQITQSGRDFIMHCFEYKDPETGVNYLIQGMTSKLAVLVALIILEQSPAFKIDFDLHDLIPSCERTFLWRYSLSKL
Protein: Putative tRNA pseudouridine synthase C25B8.05 (EC 5.4.99.-) (Q9UTB3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Multisubstrate pseudouridine synthase 7
- Cytoplasmic tRNA 2-thiolation protein 2
- Ubiquitin-related modifier 1
- tRNA threonylcarbamoyladenosine dehydratase
- tRNA
- tRNA
- ERAD-associated E3 ubiquitin-protein ligase doa10
- tRNA pseudouridine synthase 4
- Elongator complex protein 3
- Uncharacterized protein C3F10.06c
Sequence:
MPASKYAGWSRDQLISRILELDGKLQKNTNSLPNKEIEGKNEVIKNKNKLDNGNEIEPQHLSQELVLQHALQDASSLPKLKPVRPFQLEKTVFVAFKFAYCGWNYNGLAYQLEPTPLPTVEGKVFEALLRAHLITDPSSCSFSRCGRTDKGVSAMGQVISLNVRHSERRPIIYCDVLNRLLPADIRITGYAFPPEGFDARFSCKQRHYKYLFTKDYPGGSLDIDRMNEAAALYLGEHDFRNFCKIDASKQITNYHRRILSSKVICIDPSTGLYAFDLQGTAFLWHQVRCMMAILFLIGQKLEPASLINDLLDIKKVPTKPIYDMASEYPLILYDCDFDNIEWTLPTDSPTTAPRIAKHTYETIYHQWHSLRIREQIASFMLDIADHNVKRYGKSEESSSTMNVGEGLLKRTKKYIPILSRQRQESVEVVNERYKRKKGLKDSDVKSENIK
Protein: Centrosomal protein of 70 kDa (Cep70) (p10-binding protein) (Q8NHQ1)
Organism: Homo sapiens (Human)
Function: Plays a role in the organization of both preexisting and nascent microtubules in interphase cells. During mitosis, required for the organization and orientation of the mitotic spindle.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:21795687}. Note=Localized at the center of the radial microtubule array in interphase and at the spindle poles during various stages of mitosis.
Interaction partners:
- B-lymphocyte antigen CD19
- Serine/threonine-protein kinase PLK1
- Myeloid cell surface antigen CD33
- Glutamate carboxypeptidase 2
- G-protein coupled receptor family C group 5 member D
Sequence:
MFPVAPKPQDSSQPSDRLMTEKQQEEAEWESINVLLMMHGLKPLSLVKRTDLKDLIIFDKQSSQRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLSRACHQQNKIKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAYLCKRVPHTVLDRQLLCLIDYYESKIRKIHTQRQYKEDESQSEEENDYRNLDASPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLETRPTQHELRLYKQQVKKLEKALKKNVKLQELINHKKAEDTEKKDEPSKYNQQQALIDQRYFQVLCSINSIIHNPRAPVIIYKQTKGGVQNFNKDLVQDCGFEHLVPVIEMWADQLTSLKDLYKSLKTLSAELVPWLNLKKQDENEGIKVEDLLFIVDTMLEEVENKEKDSNMPHFQTLQAIVSHFQKLFDVPSLNGVYPRMNEVYTRLGEMNNAVRNLQELLELDSSSSLCVLVSTVGKLCRLINEDVNEQVMQVLGPEDLQSIIYKLEEHEEFFPAFQAFTNDLLEILEIDDLDAIVPAVKKLKVLSY
Protein: Small conductance calcium-activated potassium channel protein 2 (SK2) (SKCa 2) (SKCa2) (KCa2.2) (P58390)
Organism: Mus musculus (Mouse)
Function: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:20689065}.
Interaction partners:
- A-type voltage-gated potassium channel KCND2
- Calcium-activated potassium channel subunit beta-1
- Calcium-activated potassium channel subunit beta-4
- Small conductance calcium-activated potassium channel protein 1
- Small conductance calcium-activated potassium channel protein 3
- Calcium-activated potassium channel subunit beta-2
- Potassium channel subfamily U member 1 current)
- Intermediate conductance calcium-activated potassium channel protein 4
- Calmodulin-like protein 3
- Protein kinase C gamma type
Sequence:
MPIVLVRPTNRTRRLDSTGAGMGPSSHQQQESPLPTITHCAGCTTAWSPCSFNSSDMETPLQFQRGFFPEQPPPPPRSSHLHCQQQQQSQDKPCAPFAPLPHPHHHPHLAHQQPGSGGSSPCLRCNSCASSGAPAAGAGAGDNLSLLLRTSSPGGAFRTRTSSPLSGSSCCCCCSSRRGSQLNVSELTPSSHASALRQQYAQQPASASQYHQCHSLQPATSPTGSLGSLGSGPPLSHHHHHPHPAHHQHHQPQARRESNPFTEIAMSSCRYNGGVMRPLSNLSSSRRNLQEMDSEAQPLQPPASVVGGGGGASSPSAAAAASSSAPEIVVSKPEHNNSNNLALYGTGGGGSTGGGGGGSGHGSSSGTKSSKKKNQNIGYKLGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGAYDKASLYSLALKCLISLSTIILLGLIIVYHAREIQLFMVDNGADDWRIAMTYERIFFICLEILVCAIHPIPGNYTFTWTARLAFSYAPSTTTADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRFVMKTLMTICPGTVLLVFSISLWIIAAWTVRACERYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPNTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQNIMYDMISDLNERSEDFEKRIVTLETKLETLIGSIHALPGLISQTIRQQQRDFIETQMENYDKHVSYNAERSRSSSRRRRSSSTAPPTSSESS
Protein: Tumor necrosis factor-inducible gene 6 protein (TNF-stimulated gene 6 protein) (TSG-6) (Tumor necrosis factor alpha-induced protein 6) (TNF alpha-induced protein 6) (O08859)
Organism: Mus musculus (Mouse)
Function: Major regulator of extracellular matrix organization during tissue remodeling (By similarity). Catalyzes the transfer of a heavy chain (HC) from inter-alpha-inhibitor (I-alpha-I) complex to hyaluronan. Cleaves the ester bond between the C-terminus of the HC and GalNAc residue of the chondroitin sulfate chain in I-alpha-I complex followed by transesterification of the HC to hyaluronan. In the process, potentiates the antiprotease function of I-alpha-I complex through release of free bikunin (By similarity). Acts as a catalyst in the formation of hyaluronan-HC oligomers and hyaluronan-rich matrix surrounding the cumulus cell-oocyte complex, a necessary step for oocyte fertilization. Assembles hyaluronan in pericellular matrices that serve as platforms for receptor clustering and signaling. Enables binding of hyaluronan deposited on the surface of macrophages to LYVE1 on lymphatic endothelium and facilitates macrophage extravasation. Alters hyaluronan binding to functionally latent CD44 on vascular endothelium, switching CD44 into an active state that supports leukocyte rolling (By similarity). Modulates the interaction of chemokines with extracellular matrix components and proteoglycans on endothelial cell surface, likely preventing chemokine gradient formation. In a negative feedback mechanism, may limit excessive neutrophil recruitment at inflammatory sites by antagonizing the association of CXCL8 with glycosaminoglycans on vascular endothelium (By similarity). Has a role in osteogenesis and bone remodeling. Inhibits BMP2-dependent differentiation of mesenchymal stem cell to osteoblasts. Protects against bone erosion during inflammation by inhibiting TNFSF11/RANKL-dependent osteoclast activation (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P98066}.
Interaction partners:
- Pentraxin-related protein PTX3
- CD44 antigen
- Hyaluronan synthase 2
- Thrombospondin-1
- C-X-C motif chemokine 10
- Interleukin-6
- Versican core protein
Sequence:
MVVLLCLCVLLWEEAHGWGFKNGIFHNSIWLEQAAGVYHREARAGRYKLTYAEAKAVCEFEGGRLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKRIFKSPGFPNEYDDNQVCYWHIRLKYGQRIHLSFLDFDLEHDPGCLADYVEIYDSYDDVHGFVGRYCGDELPEDIISTGNVMTLKFLSDASVTAGGFQIKYVTVDPASKSSQAKNTSTTGNKKFLPGRFSHL
Protein: Nuclear inhibitor of protein phosphatase 1 (NIPP-1) (Protein phosphatase 1 regulatory inhibitor subunit 8) [Includes: Activator of RNA decay (EC 3.1.4.-) (ARD-1)] (Q12972)
Organism: Homo sapiens (Human)
Function: Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.
Subcellular location: Nucleus. Nucleus speckle. Note=Primarily, but not exclusively, nuclear.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm. Note=Found mainly in the cytoplasm.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
- Splicing factor 3B subunit 1
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- DnaJ homolog subfamily C member 8
- RNA-binding protein 39
- Protein phosphatase 1 regulatory subunit 3B
- ATP-dependent RNA helicase A
- RNA-binding protein 5
Sequence:
MAAAANSGSSLPLFDCPTWAGKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLPSAVKGDEKMGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRNMVQTAVVPVKKKRVEGPGSLGLEESGSRRMQNFAFSGGLYGGLPPTHSEAGSQPHGIHGTALIGGLPMPYPNLAPDVDLTPVVPSAVNMNPAPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLI
Protein: Kruppel like factor 7 (C9JX20)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFPSWPTCLELERYLQTEPRRISETFGEDLDCFLHASPPPCIEESFRRLDPLLLPVEAAICEKSSAVDILLSRDKLLSETCLSLQPASSSLDSYTAVNQAQLNAVTSLTPPSSPELSRHLVKTSQTLSAVDGTVTLKLVAKKAALSSVKVGGVATAAAAVTAAGAVKSGQSDSDQ
Protein: Vacuolar protein sorting-associated protein 51 homolog (G8XYY4)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000256|RuleBase:RU368010}.
Interaction partners:
Sequence:
MSSVLDVTKPDFDVEAFVVKLLREKSLDGLVKEEEEMVSAVRRLDSDVHQIVYENYNKFLTATNTVRKIQDEFTQLDSEMKSLSRSMSTISTLIGNLDGVLGEKRDDILQLGSSYKVVNSLKHIFDLPHVLRSEFDERNYGEVLRMFKLAEESLSQYKDVPTVQLVLQKSKKIYDMTENQLMDQLRNPASGAELVSEAVDLLLTIGRDEDEVQKVLLTCSEQSLRVDLKELSANHSDVLDLVDKASESFIPNLTLIATTHDRLFEDKREDLITVLKTEMNSLHALVSKVFLSSSDAKDCSIVVRALDRYFRKISTCRYVIPGLDFLPLTIELINAVSKHEIDLSLTRIKEELKNGLNEVRKALINEEKDLSALASKIEQVFVHQVKTALANLLLFTASDVTFANLPPDEFRQSFSFNAHERLLVQAFHRFSELADEYESGAGEIRFVDPRVHLVFAVALQHLSNKSAVYLLNLCREQFSLSPDDGLTDITVVMSEVKTRAQKLVRCYAEKTGLSMGETLIKGCAMLVQPAATPSAVRASVRRLVEEMNTCDSELTLLLGGDSKPKDSRSSSNHNCSRCRQRFIVV
Protein: Protein-arginine deiminase type-4 (EC 3.5.3.15) (Peptidylarginine deiminase IV) (Protein-arginine deiminase type IV) (Q9Z183)
Organism: Mus musculus (Mouse)
Function: Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci. Required for the formation of neutrophil extracellular traps (NETs); NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription (By similarity). Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UM07}. Nucleus {ECO:0000250|UniProtKB:Q9UM07}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9UM07}. Note=Cytoplasmic granules of eosinophils and neutrophils. {ECO:0000250|UniProtKB:Q9UM07}.
Interaction partners:
- Histone H3.1
- Histone H3.2
- Neutrophil elastase
- Myeloperoxidase
Sequence:
MAQGAVIHVAPEQPTHAVCVVGTATPLDVRGSAPKGYTTFGITASPGVIVDVIHGPPVKKSTMGASKWPLDPELEVTLQVKAASSRTDDEKVRVSYYGPKTSPVQALIYITGVELSLSADVTRTGRVKPAQAGKDQSTWTWGPGGRGAILLVNCDKEDPQASGMDFEDDKILDNKDLQDMSPMTLSTKTPKDFFEKYQLVLEVPKAKMNRVRVFRATRGKLPSRYKVALGPQQFSYCLELPGGQHSTDFYVEGLAFPDADFKGLIPLTISLLDKSNPELPEALVFQDSVTFRVAPWIMTPNTQPPQEVYVCRVSDNEDFLKSLATLTKKAKCKLTVCPEEENIDDQWMQDEMEIGYIQAPHKTLPVVFDSPRDRGLKDFPVKRVMGPNFGYVTRKLYMSELTGLDAFGNLEVSPPVTVRGKEYPLGRILIGNSGYSSSESRDMHQALQDFLSAQQVQAPVRLFSDWLFVGHVDEFLSFVPARDKQGFRLLLSSPRACYQLFQELQSQGHGEATLFEGLKRKRQTINEILSNKKLRDQNAYVESCIDWNRAVLKRELGLAEGDIIDIPQLFKLAGNSRGNSKAQAFFPNMVNMLVLGKYLGIPKPFGPIIDGHCCLEEEVRSHLEPLGLHCTFINDFYTYHVYNGEVHCGTNVRRKPFTFKWWHMVP
Protein: Gastric triacylglycerol lipase (GL) (Gastric lipase) (EC 3.1.1.3) (P07098)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol. Shows a preferential hydrolysis at the sn-3 position of triacylglycerol.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P80035}.
Interaction partners:
- Pancreatic triacylglycerol lipase
- Inactive pancreatic lipase-related protein 1
- Hepatic triacylglycerol lipase
- Lipoprotein lipase
- Bile salt-activated lipase
- Endothelial lipase
- Colipase
- Pancreatic lipase-related protein 3
- Monoglyceride lipase
- Patatin-like phospholipase domain-containing protein 2
Sequence:
MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK
Protein: Clathrin light chain (H0Y9Q6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180, ECO:0000256|RuleBase:RU363137}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180, ECO:0000256|RuleBase:RU363137}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180, ECO:0000256|RuleBase:RU363137}. Membrane, coated pit {ECO:0000256|RuleBase:RU363137}; Peripheral membrane protein {ECO:0000256|RuleBase:RU363137}; Cytoplasmic side {ECO:0000256|RuleBase:RU363137}. Note=Cytoplasmic face of coated pits and vesicles. {ECO:0000256|RuleBase:RU363137}.
Interaction partners:
Sequence:
IAGIENDEGFGAPAGSHAAPAQPGPTSGAGSEDMGTTVNGDVFQEANGPADGYAAIAQADRLTQEPESIRKWREEQRKRLS
Protein: magnesium chelatase (EC 6.6.1.1) (P73020)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Magnesium-protoporphyrin O-methyltransferase
- Magnesium-chelatase subunit ChlD
- Magnesium-chelatase subunit ChlI
- Ferrochelatase
- CobN protein
- Protoporphyrinogen IX oxidase
- Geranylgeranyl diphosphate reductase
- Chlorophyll a synthase
- Light-independent protochlorophyllide reductase subunit B
- Light-independent protochlorophyllide reductase subunit N
Sequence:
MFTNVKSTIRRVDPEALNGRQLLKVVYVVLESQYQSALSAAVRNINRTNSSLAIQLTGYLIEELRDPENYANFKHDVSEANLFIASLIFIEDLADKVVEAVTPYRDNLDAAIVFPSMPQVMRLNKMGSFSMAQLGQSKSAIAQFMKKRKENSSGAGFQDAMLKLLRTLPTVLKYLPVEKAQDARNFMLSFQYWLGGSQENLENFLLMLTDKYVYPDLGLDKLVNYQEPVVYPDMGIWHPLSMQMFENVKDYLEWYNQRPDISEDLKDPLAPCIGLIMQRTHLVTGDDAHYVGMVQELEAMGARVICVFSGGLDFSKPVNEYFWDKSVNGVEPLPIVDAVVSLTGFALVGGPARQDHPRAIESLKKLNRPYMCALPLVFQTTEEWEASDLGLHPIQVALQIAIPELDGAIEPIILSGRDGSTGRAIALQDRLEAIAQRAMKWANLRKKPKLDKKVAITVFSFPPDKGNVGTAAYLDVFGSIYEVMKGLQGNGYDVQDLPGSAKELMEAVIHDAQAQYNSPELNIAHRMSVEQYERLTPYSVRLEENWGKPPGHLNSDGQNLLIYGKEFGNVFIGVQPTFGYEGDPMRLLFSRSASPHHGFAAYYTYLNHIWKADAVLHFGTHGSLEFMPGKQMGMSGECYPDNLIGTIPNLYYYAANNPSEATIAKRRGYASTISYLTPPAENAGLYKGLQELNELIGSYQTLKDSGRGIQIVNTIMDQARICNLDQDVNLPDINAEEMDQGQRDTIVGSVYRKLMEIESRLLPCGLHVIGQPPSAEEAIATLVNIASLDREDEGIWALPTLIAESIGRNMEEIYRNSDKGILADVELLQDITLATRAAVAALVQEQINADGRVSFVSKLNFFKIGKKAPWVKSLCDSGYPNVNEEKLKPLFEYLEFCLEQVCADNEFGGLLQALEGEYVLPGPGGDPIRNPNVLPTGKNIHALDPQSIPTLAAVQSAKVVVDRLLERQRAENGGNYPETIASVLWGTDNIKTYGESLAQIMWMVGAKPVPDALGRVNKIELVPLEELGRPRIDVVVNCSGVFRDLFINQMNLLDQAVKLAAEADEPLEMNFVRKHALEQAEEMGIGVREAATRIFSNASGSYSSNVNLAVENSSWEDESELQEMYLKRKSFAFNSDNPGMMDQNRDMFERALKTADATFQNLDSSEISLTDVSHYFDSDPTKLISTLRDDGKAPAAYIADTTTANAQVRTLSETVRLDARTKLLNPKWYEGMLSHGYEGVRELSKRLVNTMGWSATAGAVDNWVYEDANSTFIKDEEMCKRLMDLNPNSFRRMVSTLLEVNGRGYWETSDENLERLQELYQEVEDRIEGVE
Protein: Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase) (P78780)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Aspartokinase
- Homoserine dehydrogenase
- Protein arg11
- Probable acetolactate synthase small subunit
- Ornithine decarboxylase
- Phosphoglycerate kinase
- Tryptophan synthase
- Acetyl-CoA carboxylase
- Threonine synthase
- Multifunctional tryptophan biosynthesis protein
Sequence:
MAIKKVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSGLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRQENKLDRGCIITNSNCSTAAVVVPLKALQDAFGPIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNSTISGYELTDNVVSAQCNRVPVIDGHLMCISVKFAKTSPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDSTPDRPQPRLDRNNENGYAVSVGRIRSDSIFDIKFVSLVHNTVLGAAGAGILNAEVAVKKGLM
Protein: mRNA export protein mlo3 (RNA-annealing protein mlo3) (Q09330)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the mRNA export process. Interferes with mitotic chromosome segregation when overexpressed.
Subcellular location: Nucleus {ECO:0000269|PubMed:15990877, ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent RNA helicase uap56
- mRNA export factor mex67
- Uncharacterized protein P25A2.03
- THO complex subunit Tho3
- Importin subunit beta-3
- ATP-dependent RNA helicase fal1
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- THO complex subunit tho5
- Uncharacterized protein C126.13c
- THO complex subunit 2
Sequence:
MSMELDQSLDAIIASKPKGGIRKRRARSNKPKPTKNAKPAVNTASALKSVISEESKIIVSNLPTDVTEAQVKELFVKSIGPCKRVSLAYGPNGRSKGIATIIFSRPGDATRAYEQYEGRLVDGTRKMKVEIILDPSRQLNSLAARVSPASNASATASKNGAKSSKRKTTRRRRTPNRPKKSAEELDKEMDDYFGSNEKE
Protein: Probable proton-coupled zinc antiporter SLC30A4 (Solute carrier family 30 member 4) (Zinc transporter 4) (ZnT-4) (O14863)
Organism: Homo sapiens (Human)
Function: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment. Controls zinc deposition in milk (By similarity).
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:O55174}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:17349999}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17349999}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in vesicles within the basal region of epithelial cells. {ECO:0000250|UniProtKB:O55174}.
Interaction partners:
- Zinc transporter ZIP4
- Zinc transporter 6
- Zinc transporter ZIP1
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Sodium/nucleoside cotransporter 2
- Copper-transporting ATPase 2
- Glycine amidinotransferase, mitochondrial
- Zinc transporter ZIP13
- Zinc transporter SLC39A7
- Zinc transporter ZIP6
Sequence:
MAGSGAWKRLKSMLRKDDAPLFLNDTSAFDFSDEAGDEGLSRFNKLRVVVADDGSEAPERPVNGAHPTLQADDDSLLDQDLPLTNSQLSLKVDSCDNCSKQREILKQRKVKARLTIAAVLYLLFMIGELVGGYIANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTKRFTFGFHRLEVLSAMISVLLVYILMGFLLYEAVQRTIHMNYEINGDIMLITAAVGVAVNVIMGFLLNQSGHRHSHSHSLPSNSPTRGSGCERNHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYVFSLLVAFTTFRIIWDTVVIILEGVPSHLNVDYIKEALMKIEDVYSVEDLNIWSLTSGKSTAIVHIQLIPGSSSKWEEVQSKANHLLLNTFGMYRCTIQLQSYRQEVDRTCANCQSSSP