wanglab/gogpt-training-data huggingface dataset:
Protein: Nicotinamide phosphoribosyltransferase (NAmPRTase) (EC 2.4.2.12) (W5P316)
Organism: Ovis aries (Sheep)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR005943}. Cytoplasm {ECO:0000256|PIRNR:PIRNR005943}. Secreted {ECO:0000256|PIRNR:PIRNR005943}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide-nucleotide adenylyltransferase.
- protein acetyllysine N-acetyltransferase
- Nicotinamide riboside kinase 1
- NAD-dependent protein deacetylase
- NAD-dependent protein deacetylase sirtuin-2
- NAD-dependent protein deacylase sirtuin-5
- NAD-dependent protein deacetylase sirtuin-7
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
Sequence:
MNAAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKIRKVKYEETVFYGLQYILHKYLKGKVVTKEKIQEAKEVYREHFQDDVFNEKGWNYILEKYDGHLPIEVKAVPEGSVIPRGNVLFTVENTDPECYWLTNWVETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGIALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKTWGEDLRHLIVSRSTEAPLIIRPDSGNPLDTVLKVLDILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKKWSIENVSFGSGGALLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVADPNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGHDLLHTVFKNGKVTKSYSFDEVRKNAQLNIELEAAPH
Protein: LIM domain containing preferred translocation partner in lipoma (C9JXK9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVIPNQPPLTATKKSTLKPQPAPQAGPIPVAPIGTLKPQPQPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAAPSSGQIYGSGPQGYNTQPVPVSGQCPPPSTRGGMDYAYIPPPGLQPEPGYGYAPNQGRYYEGYYAAGPGYGGRNDSDPTYGQQGHPNTWKREPGYTPPGAGNQNPPGMYPVTGPKKTYITDPVSAPCAPPLQPKGGHSGQLGPSSVAPSFRPEDELEHLTKKMLYDMENPPADEYFEC
Protein: Left-right determination factor 2 (Left-right determination factor B) (Protein lefty-2) (Protein lefty-B) (P57785)
Organism: Mus musculus (Mouse)
Function: Required for left-right asymmetry determination of organ systems in mammals.
Subcellular location: Secreted.
Interaction partners:
- Nodal
- Left-right determination factor 1
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
- Teratocarcinoma-derived growth factor
- Cryptic protein
- POU domain, class 5, transcription factor 1
- Homeobox protein NANOG
- Pituitary homeobox 2
- Transcription factor SOX-2
Sequence:
MKSLWLCWALWVLPLAGPGAAMTEEQVLSSLLQQLQLSQAPTLDSADVEEMAIPTHVRSQYVALLQGSHADRSRGKRFSQNFREVAGRFLMSETSTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPRTALRRFERLSPHSARARVTIEWLRVREDGSNRTALIDSRLVSIHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPGTWSAHKLVRFAAQGTPDGKGQGEPQLELHTLDLKDYGAQGNCDPEVPVTEGTRCCRQEMYLDLQGMKWAENWILEPPGFLTYECVGSCLQLPESLTIGWPFLGPRQCVASEMTSLPMIVSVKEGGRTRPQVVSLPNMRVQTCSCASDGALIPRGIDL
Protein: BcDNA.GH03377 (Q9Y153)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- Lysine--tRNA ligase
Sequence:
MLPGVGVFGTGEIANVLVPLLREKGFEVRAIWGRTLKEAKETATTQNVQFHTNVIDDVLLRKDVDLVFIVCQPFLHAEISVKALGIGKHVVCDKPAGLHQQDALKMVRASQYYPTLISLVNHPLRFLPAFTHMRRCLQEELIGSIGDVVLMDVRVQMGTLFPEKYNWMCDAQMGGGALNLVGSVVDLVTFLLQQQAIRVHGVLRSYTKTTPAINGIRQITAPDFCNFQMELASGTLVTVALHSHTVPAKAFSQEVLIYGSKGHLVVRGGDLFVLKEGQPKEEAVYVDVQDLHFATNNSLLPRPYIKGLCKMVGALKEAFGSKESSWVKAPVSTAATFEDGLYVQAVVEAIRKSNETRQWQRVQLSTDSPLNHDQIIRYARMSTM
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (F1MWF1)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000311}.
Interaction partners:
- Vascular endothelial growth factor C
- Cadherin-5
- Platelet endothelial cell adhesion molecule
- Vascular endothelial growth factor A
- Tyrosine-protein kinase
- Vascular endothelial growth factor D
- SHC-transforming protein 1
- SHC adaptor protein 3
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 3-kinase regulatory subunit alpha
Sequence:
MESKALLALALWLCVETRAASVGFSSVSLDPPRLSIQKDILRVMANTTLQITCRGQRDLQWLWPNNQSSSEKRVEVTDCSDGVFCKMLTISEVIGNDTGAYKCFYQDTDMGSVLYVYVQDYRSPFIASVSDQHEVVYITENKNKTVVIPCLGTVSDLNVSLCARYPEKRFVPDGNRISWDSQKGFSIPSYMISYAGVVFCEAKINDESYQSIMYIIVVIGYKIYDVVLSPPHGVELSVGEKLILNCTARTELNVGIDFHWEYPSLKHQHKKLINRDLKTQSGTEMKKFLSTLTIDGVTRSDQGWYICAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRVPVKYLGYPPPEIKWYKNGRPIESNHTVKVGHVLTIMEVSEKDTGNYTVILTNPISKEKQSHMVSLVVNVPPQIGEKSLLSPVDSYQYGTSQTLTCTVYAVPPPSHIRWYWQLETECTYQPTLTALTTNPYTCKEWRNVEDFQGGNKIEVNKNQIALIEGRNKTVSTLVIQAANVSALYKCEAVNKAGRGERVISFHVTRGPEITLQPGIQPTEQENVSLWCSADRTMFENLTWYKLGPQALPIHMGDLPTPVCKNLDALWKMNATMNSNGTNDILILELQNASLQDQGDYVCFAQDRKTKKRHCVARQLTVLERMAPMITGNLENQTTSIGETIEVSCTASGNPSPQITWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIVEGAQEKTNLEVIILVGTAVIAMFFWLLLVIVLRTVKRANGGELKTGYLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCKTVAVKMLKEGATHGEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGAQFRQGKEYVGEITMDPKRRLDSITSSQSSASSGFVEEKSLSDVEEEEVSEDLYKNFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGDPNQRPTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDWTDAQQKQGVCGIRRLKPDERLPVGIPF
Protein: Presenilin (EC 3.4.23.-) (A0A024R6A3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI
Protein: Cysteine desulfurase (m-Nfs1) (EC 2.8.1.7) (Q9Z1J3)
Organism: Mus musculus (Mouse)
Function: Mitochondrial cysteine desulfurase, of the core iron-sulfur cluster (ISC) assembly complex, that catalyzes the desulfuration of L-cysteine to L-alanine, as component of the cysteine desulfurase complex, leading to the formation of a cysteine persulfide intermediate at the active site cysteine residue and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU. The persulfide is then transferred on the flexible Cys loop from the catalytic site of NFS1 to the surface of NFS1 (By similarity). After the NFS1-linked persulfide sulfur is transferred to one of the conserved Cys residues of the scaffold, a reaction assisted by FXN. The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9738949}.
Interaction partners:
- Frataxin, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- LYR motif-containing protein 4
- Adenylyltransferase and sulfurtransferase MOCS3
- Ferredoxin-2, mitochondrial
- Thiosulfate sulfurtransferase
- 3-mercaptopyruvate sulfurtransferase
- Adrenodoxin, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Glutaredoxin-related protein 5, mitochondrial
Sequence:
MVGSVAGNMLLRAAWRRASLAATSLALGRSSVPTRGLRLRVVDHGPHSPVHSEAEAVLRPLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNIMKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMSPLWEMVQDGIDLKSIKWTQH
Protein: Protein deadlock (Q9VIF5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Developmental protein involved in oogenesis. Required for germline maintenance, stability of mitotic spindles, localization of patterning determinants, oocyte growth and fusome biogenesis in males and females. Also required for dorso-ventral and antero-posterior patterning of oocyte and eggshell. May be involved in microtubule function during oogenesis. Part of a rhi-dependent transcription machinery that enables the generation of piRNA precursors from heterochromatin while maintaining the suppression of transposon-encoded promoters and enhancers. Component of the RDC complex (rhi, del and cuff) which binds to repressive H3K9me3 marks in the piRNA clusters. RDC promotes the bidirectional transcription of piRNA clusters at these sites by interacting with Moonshiner which forms a complex with the transcription initiation factors TfIIA-S and Trf2. This mechanism allows transcription to occur in piRNA clusters despite the lack of proper promoter elements and in the presence of the repressive H3K9me3 mark.
Subcellular location: Nucleus {ECO:0000269|PubMed:16616913, ECO:0000269|PubMed:28847004}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16616913}. Chromosome {ECO:0000269|PubMed:24906153}. Note=Colocalizes with the oocyte nucleus at midstages of oogenesis and with the centrosomes of early embryos (PubMed:16616913). Expressed in nuclear foci (PubMed:28847004). All components of the Rhino-Deadlock-Cutoff (RDC) Complex associate with these nuclear foci and are required for their formation. {ECO:0000269|PubMed:16616913, ECO:0000269|PubMed:24906153, ECO:0000269|PubMed:28847004}.
Interaction partners:
- Chromo domain-containing protein rhino
- Moonshiner
Sequence:
MEKLDKIRMSQKLSCWQHILTTLGTSSKTEQEWNTFFKGFLESWRKPYCIQTSCDPSIPLRKELLVRPRKALQENPHGPGSTLPESPVFLEPINSTAPREHPSPSKSHSTGSTGCDPGNGERSPSVSNKNSKYKNPGNSKYAKIWKRSNNHTTSIFSKAQISKRRDKLSSTKKRPDTCAPTDDSRKNREPRACAPNKNIFKTRETNAPNLTKNSCALPNVLILSPNSASKITQRGHSVGQTQDYKASPGKIIKRVPRYSLQCLKKKTEKVHNKIMDKPKNKQQPQTPPPFLLNNEYTESSDDSDDQLPLSELSQKMKSNKLNTLFLSRNEDCSPAPEKVKLKGERPAQNKKEQLTWEPSILTNLTDLGKQVAEPLRKSVKKSAKQQKPRVRAPPQGKKTLPQLQTGLKTQDKQSTHEMISEQAKTISEASGQQTSQVQSSLSPNNIRNNSVKLISAKTLMPAQRSQDYSPNKMQVGQPLGFAIELPSPVDGKEASVEIDTQLVHTSKFLENMTRPSTVEVHKFDLMDIFMGENEKLDYEYDDDDVLSVAASWNGLDDENVPEDEPRKEAKTAEQLPKPEPSTETLKPIEKENAQKMQSIKSFQIPKLNAKNLKTQPSVMRSIYENEELEKNKVLAKPAPPSLVHQPLAESNRNQRDEATAARRAKETFPVFAPLYRVAPESAATLVSANSQQVIPQVYFSTSNQDGVNWIKDVFGIRCMQSVDNKCISINCDHTMNSLGEVQKRLMRMDEDTLLSLYRQTIRSFFLFQTYYTSFVDIFKFRNLWQYLLIMLVDCRLYKSISAPLLAHVYEALSKCGMQKEAVKRIMEHVWLPCKAHKYRDLMLTTLNILSNANWEDYCDKLTQLDKDYNFEIPHKNLITILKSSVDCSDKFANALKLITLHPNSIRTNETIMSILSNASKSYSYMHNESASASQGPPGAASFLAPPAAIQPPHTTVPNFGYLPNPSFHYSNEYAINIHNFD
Protein: Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1) (A7VK01)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
Sequence:
MVYSNCESKEPDSVSASNHLLLNGNDELVEKSHKTGPENNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEEDEWKGKVSYRDSEIELSDASQVEKEVSAAQIAIAGEGVGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPYDIEYQIKSLIKKYICKQETINLVVVPCNVDIATTEALRMAQEVDPEGDRTIGILTKPDLVDKGTEDKIVDVARNLVFHLKKGYMIVKCRGQQDIQDQLSLAKALQKEQAFFENHEHFRDLLEEGRATIPCLAERLTSELIMHICKTLPLLENQIKESHQKITEELQKYGSDIPEDESGKMFFLIDKIDAFNSDITALIQGEELVVEYECRLFTKMRNEFCKWSAVVEKNFKNGYDAICKQIQLFENQYRGRELPGFVNYKTFETIIKKQVSVLEEPAVDMLHTVTDLVRLAFTDVSETNFNEFFNLHRTAKSKIEDIKLEQEKEAETSIRLHFQMEQIVYCQDQVYRGALQKVREKEVEEEKNRKSNQYFLSSPAPSSDPSIAEIFQHLIAYHQEVGKRISSHIPLIIQFFILRTFGQQLQKSMLQLLQNKDQYDWLLRERSDTSDKRKFLKERLMRLTQARQVPRLNRALQAARGLQGTSPGNEDQPPSLTD
Protein: K+/Cl-Cotransporter (S6FWN4)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGDDSSQDKASAPPSAAAAGAAPAGNPQQQPASAIRNKVDVPPGFGRRVSSVEVVKNAMPPTKKASVVIFETPDTPKAERRASSWWRNLVMDDDKTAPVQSDTVISPENAGNGLADHHRNISTASVGDRELYAWGTNKDAGGNHNLALFEEPSMPFFSSYLKAHITPGPLERAQSSSHGGHGAKADLGVLLGVYLPTIQHILGVTMFIRLFWLVGIAGLGQTFLLLFLCCFCTFLTCISISAVATNGVVESGGAYFMISRNLGPEFGSAVGILFYLANTVATSMYLVGGVEILLLYIFPGLTFGGVEGQHDTSMFGTMTNSLRFYSTILLLIEFAIVAMGVKFVQMLAPVSLVCVILSILACYAGGVTKTIYPDSGQYVCMYNDRLLQSSAVLNESIPLDEICNYCNINNTFLADRVCGGRCNSTTIPHVSPFRCINGFPGFQGGQTLLENLGPNYLEKGEAAHGTQADTKSDVYQDVRTSFFVLLAIYFPAVTGIFTGANMSGDLKNPQASIPAGTIAANLTTSFVYFSLAFIFGGAIDNAVLRDKNGQSVGGQMVVALLSWPSPWVLLIGSFLSTFGAALQCLCSAPRLLQAIAKDEVIPLLSPFKKVTANNEPFLGLILTTIIAEIAILMGSMDTIAAVVDFFFLMCYAFVNIICTLHSLLGAPNWRPRFKYYHWFLSLLGAVLCFFIMFSTHWDYAIVACLLCLVIYKYVEWKGAKKEWGDGIRGLALTTAQYSLMKIEDKEPHPKNWRPQLLLLLSMQWSKEIIDVRYLNLLNLASQLKAGKGLTVVTAFLQGDPTSPDDKKKGEQVKARMDFDMNQVRLRGFAKTLVHSEDQVRGSMSTLVQSVGLGGLKPNTMLISWPVHEREEDMTEYNTFIEKVHAASINDMAIVVAKGIIDFPSAVFRMSGMIDVYWIVHDGGLCLLMGYLLKQHKVWRGCKLRVIGIAQESDNNVKMQEDLQKYVYQLRIDAKIMIVELADPEISKNAFERTLLMEERTMMMRDLQKVSGGGMSLSLPPANAPRAPSPLVTSERRANSKDSDEGTPTESEETTEKKSTSTDNEQANQETKTKKERMKALDRSKVSKMHTAVRLNELLLQHSANSQLILLNLPKPPVHKDQQALDDYVHYLEVMTDKLNRVIFVRGTGKEVITESS
Protein: Peptide tarsal-less AA (Peptide polished rice 4) (A3RLR1)
Organism: Drosophila melanogaster (Fruit fly)
Function: One of four peptides (tal-1A, tal-2A, tal-3A and tal-AA) produced from a polycistronic gene that function redundantly in several developmental processes. Required in early stages of leg development for the intercalation of the tarsal segments during the mid-third instar stage and later for tarsal joint formation. Promotes the post-translational modification of ovo isoform B (svb) into its active form which in turn initiates trichome development and promotes tarsal joint development. This is likely due to recruitment of the E3 ubiquitin-protein ligase Ubr3 to svb for ubiquitination of its N-terminus, converting svb into a transcriptional activator. Also enhances interaction of Ubr3 with Diap1. Required for correct wing and leg formation through its regulation of several genes including those in the Notch signaling pathway. Essential for denticle formation and may have a role in the developmental timing of trichome differentiation. Essential for the development of taenidial folds in the trachea.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26383956}. Nucleus {ECO:0000269|PubMed:26383956}.
Interaction partners:
- Transcriptional regulator ovo
- E3 ubiquitin-protein ligase Ubr3
Sequence:
MLDPTGTYRRPRDTQDSRQKRRQDCLDPTGQY
Protein: Intracellular phospholipase A1 (IPLA-1) (PLA(1)) (EC 3.1.1.111) (EC 3.1.1.4) (G5EEM9)
Organism: Caenorhabditis elegans
Function: Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids, being phosphatidylinositol (PI) its major substrate. PI is a versatile lipid that not only serves as a structural component of cellular membranes, but also plays important roles in signal transduction through distinct phosphorylated derivatives of the inositol head group. Catalyzes the hydrolysis of phosphatidylcholine at sn-2 position in vitro. Regulates asymmetric division, an important property of stem cells in C.elegans, by controlling the subcellular localizations of beta-catenin.
Interaction partners:
- Rab-GAP TBC domain-containing protein
- Monensin-resistant homolog 2
- Phospholipid/glycerol acyltransferase domain-containing protein
- Intracellular phospholipase A2
- Phospholipase A2
- Phospholipid/glycerol acyltransferase domain-containing protein
- phospholipase A2
Sequence:
MSGSEEEHLVSLTFRKNEEDMDEDEGKVKQKEKPKEKQMEFVNQNFVESTEDESEVSTPTAVGLPIGTSTPDGDETPTQPDPNGKYTMAQTKDADLSRPSGLPSNGNPGSSTTVPPASKSGPVAPPRPSGTPVAPQRNRRRKVTELKCSEVRWFFQEPKGTLWNPFNGRDSIMLEIKYRKEKGIELDEAMQEIYDESLTHYKMEMKDEPEIENGNIGMEQEKPMVVVMNGQYKVNKDNSKIDPIYWKDDSKEIRRGSWFSPDYQPLEMPLSDQIEKNHLQCFRNQMIPEGTTVFSKSETSNKPVLAELHVDGYDIRWSSVIDISLHQKGNAILRYLWAKSTPLRRGYEKEADWNDAAAEISHLILVVHGIGQKGYENLIAQNANQVRDGVVSAMEKVYPEEKSRPMFLPVEWRSALKLDNGLTDNITIPKMSSMRASLNSTAMDVMYYQSPLFRTEIVRGVVSQLNRTYKLFKANNPQFNGHVSVFGHSLGSVICYDVLTQYSPLMLFDKYVTKSIDEYLKRDDTNASEEARKALEAMKLAREQLRDNLEGGIHKLLVTKEEQLEFKVKYLFAVGSPLGVFLTMRGGESTDLLSKATNVERVFNIFHPYDPVAYRLEPFFAPEYRHIRPIKLFSNTDLRARASYENLPLDVYKHYLKKLKNLNKAKKNKDDKTADARSGGDDENEDEDECDSDEDARSGCSSPRSMTPPPFETAAANAAAAAKETKAVKKGWFSFGTSSNPKKTQSTASLGSVNATSTENIEFAKEAAEELPLAEKILGSGVRVPHRIDFQLQPALTEKSYWSVLKSHFAYWTNADLALFLANVLYCKPLKPEEAKPTWA
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IAK1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MAAAGGGGKDKYKNAQDAKHLLDIIGEDIYKIANDAALKRSGSELKGLLSLAKFEKNPPDKQTPEDPCDLDYKYHTNVTSNVIEPCNKRSGKRFSEVSGAECANNRIKGNKGSNGDACAPFRRLHVCDRNLEQIDPAKITATHNLLVDVCQAAKFEGQSITQDYPKYLATYNDSPSQICTMLARSFADIGDIVRGKDLFRGYDDEEKNRRKKLEQKLKVIFGHIYEELKKHKKLKEEAEERYKKDGDNYYKLREDWWALNRQEIWKAITCGHPGGTYFRQTACGGGTTPTPNKCRCATNDVPTYFDYVPQYLRWFEEWAEDFCRKRKYKLENAIEKCRGKTKGEKYCDLNGFDCTQTASGEKKFVKGHNCHNCSVTCIPFGPWIDNQKKEFLKQRNKYQNEISSNSRKKRSTSNNNYKGYDEEFYKILKEDYGDVEQFLEKLSREGICQSQPTVGNQKADAANFTKDNPAKTFSHTEYCQACPWCGVVCKSGNCTKNPEGSCTEQIRKKVYDDSNTTTIPVLTPEKGKTSILQKYKTFCEKPEKHNQINNWECHYEKTDISNNCILGKWEKFQKGQEVMVYHPFFWKWVTEMLDDSIKWRKELDNCLKNENKQCISKCNGKCDCYKRWVEQKKEKEWTQIKDHFGKQEDMKEQIRGADPGIILEGVLDIEDLFENIKDTYGDVKEIDHIKKLLEEETTVDADNQNKTTIDKLLDHEDKDAKGCLQKQNECKEQERDGGARSDSQEPTPRSEVKPDSEDLDDDDEDDPDEEKSEEVENPEDQGEEEGTKQGSGEKKVDGTEAVQETVAEVTPEKKDEVNPCEIVKTLFEKPENLSDACGLKYGPGGKERYSQWKCIPTKPNSDNKGEVGSAGRVARSAPSGEKGSICVPPRRRRLYVKDLETLGDSEVTQVQLRDAFIKCAAVETFFLWDRYKKEKEKKKPQEGVLQLLGTVGTPPTDDEEDPPEKMLQKGEIPEEFKRQMFYTLADYKDILFGDQEVIKTLKDSGDENIKDISEKIKKTLNGDNNQESGSSPSLSGKKTTPKDWWETYGKDIWEGMVCALTYKNSGDKKIEQVKTADDGEDLFQKLKTQYEYNTVTLKDENSGTEGAKPFTPKTVSSSSGEKNPPKLSDFVLRPPYFRYLEEWGETFCRQRARMLDKIKKDCNVEENDNRPGGGITKQYSGDGESCKDYLPDDPTTLPDLVSSCPKSCSSYRKWINKKKDEFVEQQNAYTEQQNKCQSKSDKAKSDNGFYTRLQNLPDAAAFLKTLGSCSKNDIPEYKIDFDVNGETFRYEKYCGTCPEFKINCTKVKCTSGDMQNGCKDNKINAANFKTMAQSTEINMLVSDNSGNGSQNDLKDCKTSGIFKGFREDVWTCGKVCGYNVCKPKNVNGQNGDGNQILLFNALLKRWVEYFLEDYKKIKHKISHCKNSSEGHTCIKNCVEQWISTKRTEWETIRGRFNDQYKSNDSDVYPVRSFLETWIPKIPVANANNDGKKLIKLSKFDNFCSCSASAHSPNGKDDAIDCMINRLQDKIDKCKEKHPQPSAENQTTCDESTLVEDVDDYEEQNPENKVGKPAICGNVDTTEPVKEEDEEECKAAESPAEPEQAAEEESVPAAETKDTENQPPQAPDVGPPPLAPAPADQPLDPTILQTTIPFGIAIALTSIVFLFLKKKTKSTIDLLRVINIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEELDINDIYVPRAPKYKTLIEVVLEPSGNNTTASGNNTTASDTQNDIQNDIPSDIPKTPSDTPPPITDDEWNQLKDEFISQYLQSEQPKDVPNDYSSGDIPLNTQPNTLYFDKPQEKPFITSIHDRNLYSGEEYNYDMFNSGKNGPYSDKNDLYSGNHDSLSGNRDPTSANHDSYSGNHHPYSGIDLINDSISGNQHIDIYDELLKRKENELFGTNNPKRTSTYSVAKLTNSDPIHNQLELFHTWLDRHRDMCEKWENHHERLAKLKEEWENETHSGNTHPSDSNKTLNTDVSIQIDMDHEKRMKEFTNMDTILEDLDKPFNEPYYYDMYDDDIYYDVNDHDTSTVDSNAMDVPSKVQIEMDVNTKLVKEKYPIGDVWDI
Protein: Calcium-binding protein NCS-1 (Q09711)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Negatively regulates sporulation perhaps by controlling Ca(2+)-dependent desensitization of git3.
Subcellular location: Membrane {ECO:0000269|PubMed:14722091}; Peripheral membrane protein {ECO:0000269|PubMed:14722091}.
Interaction partners:
- Phosphatidylinositol 4-kinase pik1
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Cell division control protein 45 homolog
- Translation factor guf1, mitochondrial
- Peptidyl-prolyl cis-trans isomerase
- Transcriptional regulator prz1
- Stretch-activated cation channel yam8
- Calcium-channel protein cch1
- Dynein heavy chain, cytoplasmic
Sequence:
MGKSQSKLSQDQLQDLVRSTRFDKKELQQWYKGFFKDCPSGHLNKSEFQKIYKQFFPFGDPSAFAEYVFNVFDADKNGYIDFKEFICALSVTSRGELNDKLIWAFQLYDLDNNGLISYDEMLRIVDAIYKMVGSMVKLPEDEDTPEKRVNKIFNMMDKNKDGQLTLEEFCEGSKRDPTIVSALSLYDGLV
Protein: 1,4-dihydroxy-2-naphthoyl-CoA synthase (DHNA-CoA synthase) (EC 4.1.3.36) (A0QRD3)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
Interaction partners:
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- O-succinylbenzoic acid--CoA ligase
- ComA operon protein 2
- o-succinylbenzoate synthase
- isochorismate synthase
- 1,4-dihydroxy-2-naphthoate octaprenyltransferase
- Oxidoreductase, short-chain dehydrogenase/reductase family protein
Sequence:
MSSQAASDNPFDPAMWERVPGFDDLTDITYHRHVLDGARQPTVRVAFDRPEVRNAFRPHTVDELYRVLDHARMSSDVGVILLTGNGPSPKDGGWAFCSGGDQRIRGRTGYQYASGETAETVDPARAGRLHILEVQRLIRFMPKVVICLVNGWAAGGGHSLHVTCDLTLASREHARFKQTDADVGSFDGGFGSAYLARQTGQKFAREIFFLGRAYDAQTMHQMGAVNEVVDHADLEKAGLQYAAEINGKSPQAIRMLKFAFNLIDDGLVGQQVFAGEATRLAYMTDEAVEGRDAFLEKRDPDWSRFPRYF
Protein: Serine/threonine-protein kinase SIK3 (EC 2.7.11.1) (Salt-inducible kinase 3) (SIK-3) (Serine/threonine-protein kinase QSK) (Q6P4S6)
Organism: Mus musculus (Mouse)
Function: Positive regulator of mTOR signaling that functions by triggering the degradation of DEPTOR, an mTOR inhibitor (By similarity). Required for chondrocyte hypertrophy during skeletogenesis. Negatively regulates cAMP signaling pathway possibly by acting on CRTC2/TORC2 and CRTC3/TORC3 (By similarity). Prevents HDAC4 translocation to the nucleus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22318228}. Note=Locates to punctate structures within the cytoplasm on binding to YWHAZ. {ECO:0000250|UniProtKB:Q9Y2K2}.
Interaction partners:
Sequence:
MAAAAASGAGGVAVAGAGGAGPAGRLLPPPAAGPPAAPAAVPPAAVPARPTAPASRGSMAARIGYYEIDRTIGKGNFAVVKRATHLVTKAKVAIKIIDKSQLDEENLKKIFREVQIMKMLCHPHIIRLYQVMETERMIYLVTEYASGGEIFDHLVAHGRMAEKEARRKFKQIVTAVYFCHCRNIVHRDLKAENLLLDANLNIKIADFGFSNLFTPGQLLKTWCGSPPYAAPELFEGKEYDGPKVDIWSLGVVLYVLVCGALPFDGSTLQNLRARVLSGKFRIPFFMSTECEHLIRHMLVLDPNKRLSMEQICRHKWMKLGDADPNFDRLIAECQQLKEERQSDPLNDDVLLAMEDMGLDKERTLQSLRSDAYDHYSAIYSLLCDRHKKHKTLRPGALPSMPQAMTFQAPVNLQAEQTGTAMNLSVPQVQLINPENQIIEPDGAVNLDSDEGEEPSPEALVRYLSMRRHTVGVADPRTEVMEDLQKLLPGFPGVNPQGPFLQVAPNMNFTHNLLPMQSLQPTGQLEYKEQSLLQPPTLQLLNGMGPLGRRASDGGANIQLHAQQLLKRPRGPSPLVTMTPAVPAVTPVDEESSDGEPDQEAVQRYLANRSKRHTLAMTSPTAEIPPDLQRQLGQQSFRSRVWPPHLVPDQHRSTYKDSNTLHLPTERFSPVRRFSDGAASIQAFKAHLEKMGNSSSIKQLQQECEQLQKMYGGQVDERTLEKTQQQHMLYQQEQHHQILQQQIQDSICPPQPSPPLQVACENQPALLTHQLQRLRIQPSSPPPNHPSNHLFRQPSNSPPPVSSAMITSHGATSPSQFQGLPSHGAIFQQQPENCSPPPSVALTCLGLQQASQSQPVTIQLQEPVDMLSNMAGTAAGSAGRSIPISPSASQIQIQHRASLMAPFSYGHRPLSKQLSADSAEAHSLNMNRFSPANYDQAHLHPHLFSDQSRGSPSSYSPSTGVGFPPTQALKVPPLDQFPTFPPSAQQQPPHYTTSALQQALLSPTPPDYPRHQQVPHILQGLLSPRHSLTGHSDIRLPPAEFAQLIKRQQQHRQQQQQQQQQQEYHELFRHMNQGDAVSLAPSLGGQNMTEQQALSYQNADSYHRHHTSPQHILQIRAQDCISQGPSPTPTHGYAHQPPLMHSESMEEDCLCEGLKEGFPDKSSSTLTKGCHNSPLLLCTSGPGDPEPLLGTVSQARELGIHPYGHQPTATTFSRNKVPSRESVLGNCLERSSPGQAMELPDHNGLGYPVRPLVSEHLRSRTLQRHHTIQNSDDAYVQLDTLPGMSLVAGKALSSARMSDAVLSQSSLMGSQQFQDEEDEECGVSLGHEHPGLGDGSQHLNSSRYPATCVTDIMLSHKHPEVSFSMEQAGV