wanglab/gogpt-training-data huggingface dataset:
Protein: Ran-binding protein 17 (Q99NF8)
Organism: Mus musculus (Mouse)
Function: May function as a nuclear transport receptor.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
Interaction partners:
- Exportin-1
- Ran-binding protein 6
Sequence:
MALHFQSLAELEVLCTHLYVGTDLTERIEAEKALLELIDSPECLSKCQLLLEQGTTSYAQLLAATCLSKLVTRINPLPIEQRIDIRNYILNYVASQPKLAPFVIQALIQVIAKLTKLGWFEVQKDEFVFREIIADVKKFLQGTVEHCIIGVIILCELTQEMNLVDYSRPSAKHRKIATSFRDTSLKDILVLACSLLKQVLAKPLNLQDQDQQSLVMQVLKLVLSCLNFDFLGSSADESADDLCTVQIPTTWRTIFLEPETLDLFFNLYHSLPPLLSQLALSCLVQFASTRRSLFSSPERAKYLGNLIKGVKRILENPQGLSDPGNYHEFCRFLARLKTNYQLGELVLVKEYAEVIGLIANFTITSLQHWEFAPNSVHYLLTLWQRMVASVPFVKSAEPHLLDTYAPEITKAFITSRLESVAIVVRDNLEDPLDDTATVFQQLEQLCTVSRCEYEKTCTLLVQLFDQNAQNYQKLLHAAPGLAVDMAIQEGRLAWLIYLVGTVVGGRLTYTSTDEHDAMDGELSCRVFQLISLMDTRLPHCTNEKIELAVLWFLDQFRKTYVGDQLQRTSKVYARMSEVLGITDDNHVLETFMTKIVTNLKYWGRCEPVISRTLQFLSDLSVGYILLKKLVKIDAVKFMLKNHTSEHFPFLGISETYNVGDFRCRTTFYTALTRLLMVDLGEDEDEFENFMLPLTVSFETVLQIFNNNFKQEEVKRMLIGLARDLRGIAFALNTKTSYTMLFDWIYPAYLPVLQRAIERWYGEPACTTPILKLLAELMQNRSQRLNFDVSSPNGILLFREASKMICTYGNQILSLGSLSKDKIYPMKLKGISICYSALKSALCGNYVSFGVFKLYGDNHFDNVLQAFVKMLLSVSHSDLLQYRKLSQSYYPLLECLTQDHMSFITNLEPPVLLYVLTSLSEGLTTLDTVVSSSCCTSLDYMVTYLFKHIAKEGKKPLRSREAMQAGQRLLHFMQQNPDVLQQMMSVLMNTIVFEDCRNQWSVSRPLLGLILLNEKYFSELRASLINSQPLPKQEVLGQCFRNLMEGVEQNLSVKNRDRFTQNLSVFRRDVAEALRSDGHTDLSSLDMMS
Protein: Ribitol-5-phosphate transferase (Q0PIP5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Protein O-mannosyl-transferase 1
- Fukutin.
- Ribitol-5-phosphate xylosyltransferase 1
- Protein O-mannosyl-transferase 2
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Protein O-mannose kinase
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Xylosyl- and glucuronyltransferase LARGE2s
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
Sequence:
MRISFCQALLTGAIILNLLILYYVSRAQQQMMEKRREQGKGLKKASLPVSGLGAMGNLVGGSMVGGVKLGGLEGNMRGPRVTILVREFEDFENYVGDVARSFLRQRPELPFLAVAENSPYPPLALPEGARLLVMSPSPDQPPQTHRPEFNVQTEFSLLVPDGVELDHGRQVERLIRELEGEGGGPVRLVAAPVLTRSSVQCLHLRVNLREWTATYSPAASGSSGSVCTALQGDAVVLIRTEDLFNLSVPLGRPLMSSLFVQTSLRGWKVKLLEGPSFSASHRPLFSSAHNQWKADSRLKDATNHLMRSFGLKRLILPDGRDQWFGCSKETARCFGTVRDDTPEYLYIERWTPPCCLRALRETTKYVINILESSGVRYWLEGGSLLGAARHQDIIPWDYDVDLGIYLEDVPNCDYLKNLDSGSLVDANGYVWERAVEGDFYRVQYSETNHLHVDLWPFYPRNGVMTRDTWTEHKQDVEFSEHFLQPLVPMPFAGITTYGPNNHRAFLELKFGEGVIENPQYPNPAKKRLDRSRTFGS
Protein: Propionyl-CoA carboxylase alpha chain (EC 6.4.1.3) (Q5LUF3)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), the enzyme catalyzing the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then tranfers the carboxyl group from carboxylated biotin to propionyl-CoA (Probable).
Interaction partners:
- Propionyl-CoA carboxylase beta chain
- Propionyl-CoA carboxylase, putative
- methylmalonyl-CoA epimerase
- Methylcrotonyl-CoA carboxylase, beta subunit
- methylmalonate-semialdehyde dehydrogenase
- L-malyl-CoA/beta-methylmalyl-CoA lyase
- Citrate lyase, putative
- Propionate--CoA ligase
- MaoC family protein/phosphate acetyl/butaryl transferase
- Acetyl-coenzyme A synthetase
Sequence:
MFNKILIANRGEIACRVIKTARKMGISTVAIYSDADKQALHVQMADEAVHIGPPPANQSYIVIDKVMAAIRATGAQAVHPGYGFLSENSKFAEALEAEGVIFVGPPKGAIEAMGDKITSKKIAQEANVSTVPGYMGLIEDADEAVKISNQIGYPVMIKASAGGGGKGMRIAWNDQEAREGFQSSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLCDSHGNGIYLGERECSIQRRNQKVVEEAPSPFLDEATRRAMGEQAVALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGVDLVEQMIRVAAGEPLSITQGDVKLTGWAIENRLYAEDPYRGFLPSIGRLTRYRPPAETAAGPLLVNGKWQGDAPSGEAAVRNDTGVYEGGEISMYYDPMIAKLCTWAPTRAAAIEAMRIALDSFEVEGIGHNLPFLSAVMDHPKFISGDMTTAFIAEEYPEGFEGVNLPETDLRRVAAAAAAMHRVAEIRRTRVSGRMDNHERRVGTEWVVTLQGADFPVTIAADHDGSTVSFDDGSSMRVTSDWTPGDQLANLMVDGAPLVLKVGKISGGFRIRTRGADLKVHVRTPRQAELARLMPEKLPPDTSKMLLCPMPGLIVKVDVEVGQEVQEGQALCTIEAMKMENILRAEKKGVVAKINASAGNSLAVDDVIMEFE
Protein: LIM and senescent cell antigen-like-containing domain protein (C0KUC5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|PIRNR:PIRNR038003}. Cell membrane {ECO:0000256|PIRNR:PIRNR038003}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR038003}.
Interaction partners:
Sequence:
MTALQLKELSQSGLYRRRRERPDSLRVNGLPEEELSNMANALASATCERCKGGFDPAEKIVNSNGELYHEQCFVCAQCFQQFPEGLFYEFEGRKYCEHDFQMLFAPCCHQCGEFIIGRVIKAMNNSWHPECFRCDLCQEVLADIGFVKNAGRHLCRPCHNREKARGLGKYICQKCHAIIDEQPLIFKNDPYHPDHFNCANCGKELTADARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNAMGKQWHVEHFVCAKCEKPFLGHRHYERKGLAYCETHYNQLFGDVCFHCNRVIEGDVVSALNKAWCVSCFACSTCNTKLTLKNKFVEFDMKPVCKKCYEKFPLELKKRLKKLSETLGRK
Protein: Transcriptional activator cubitus interruptus (Transcriptional activator ci) (ci form of 155 kDa) (ci-155) (ci full-length protein) (ciFL) [Cleaved into: Transcriptional repressor cubitus interruptus (Transcriptional repressor ci) (ci C-terminally truncated form) (ci form of 75 kDa) (ci-75)] (P19538)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has a dual function as a transcriptional activator and a repressor of the hedgehog (Hh) pathway. The full-length ci form (ciFL), acts as an activator (ciA) while ciR, its C-terminally truncated form, acts as a repressor. Involved in segment polarity. Required for the normal development of the posterior half of each embryonic segment. Engrailed protein directly represses ci expression in posterior compartment cells. Essential component of a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection.
Subcellular location: Nucleus.
Interaction partners:
- Kinesin-like protein costa
- Suppressor of fused homolog
- Protein roadkill
- Supernumerary limbs, isoform B
- Serine/threonine-protein kinase fused
- cAMP-dependent protein kinase catalytic subunit 1
- Protein smoothened
- Cullin homolog 1
- Protein patched
- Cullin 3, isoform F
Sequence:
MDAYALPTYFPLAYSELQFLASRRAAAVAAAATVLPGSPCINQHHPTDVSSSVTVPSIIPTGGTSDSIKTSIQPQICNENTLLGNAGHQHNHQPQHVHNINVTGQPHDFHPAYRIPGYMEQLYSLQRTNSASSFHDPYVNCASAFHLAGLGLGSADFLGSRGLSSLGELHNAAVAAAAAGSLASTDFHFSVDGNRRLGSPRPPGGSIRASISRKRALSSSPYSDSFDINSMIRFSPNSLATIMNGSRGSSAASGSYGHISATALNPMSHVHSTRLQQIQAHLLRASAGLLNPMTPQQVAASGFSIGHMPTSASLRVNDVHPNLSDSHIQITTSPTVTKDVSQVPAAAFSLKNLDDAREKKGPFKDVVPEQPSSTSGGVAQVEADSASSQLSDRCYNNVVNNITGIPGDVKVNSRLDEYINCGSISIPSNEYDCANADTTDIKDEPGDFIETNCHWRSCRIEFITQDELVKHINNDHIQTNKKAFVCRWEDCTRGEKPFKAQYMLVVHMRRHTGEKPHKCTFEGCFKAYSRLENLKTHLRSHTGEKPYTCEYPGCSKAFSNASDRAKHQNRTHSNEKPYICKAPGCTKRYTDPSSLRKHVKTVHGAEFYANKKHKGLPLNDANSRLQQNNSRHNLQEHNIDSSPCSEDSHLGKMLGTSSPSIKSESDISSSNHHLVNGVRASDSLLTYSPDDLAENLNLDDGWNCDDDVDVADLPIVLRAMVNIGNGNASASTIGGSVLARQRFRGRLQTKGINSSTIMLCNIPESNRTFGISELNQRITELKMEPGTDAEIKIPKLPNTTIGGYTEDPLQNQTSFRNTVSNKQGTVSGSIQGQFRRDSQNSTASTYYGSMQSRRSSQSSQVSSIPTMRPNPSCNSTASFYDPISPGCSRRSSQMSNGANCNSFTSTSGLPVLNKESNKSLNACINKPNIGVQGVGIYNSSLPPPPSSHLIATNLKRLQRKDSEYHNFTSGRFSVPSYMHSLHIKNNKPVGENEFDKAIASNARRQTDPVPNINLDPLTNISRFSTTPHSFDINVGKTNNIASSINKDNLRKDLFTVSIKADMAMTSDQHPNERINLDEVEELILPDEMLQYLNLVKDDTNHLEKEHQAVPVGSNVSETIASNHYREQSNIYYTNKQILTPPSNVDIQPNTTKFTVQDKFAMTAVGGSFSQRELSTLAVPNEHGHAKCESFHHQSQKYMNTDIGSKQQSALPSAHQRQTEKSNYNQIIDSSMTSLPELNVDSIYPRNETENIFKVHGDHDNEIQCGIISQSQMSPSTNLNNDGQFSTVNMQPITTSKLFPPEPQKIVCDTQASNTSVMHLDTYQRTLEYVQSCQNWMETNNTSTNQIQSLPGMPVNNTLFPDVSSSTHPYHGTNMVINDMTTSLTSLLEENRYLQMMQ
Protein: Troponin I, fast skeletal muscle (Troponin I, fast-twitch isoform) (P02643)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
Sequence:
MGDEEKRNRAITARRQHLKSVMLQIAATELEKEEGRREAEKQNYLAEHCPPLSLPGSMAEVQELCKQLHAKIDAAEEEKYDMEIKVQKSSKELEDMNQKLFDLRGKFKRPPLRRVRMSADAMLKALLGSKHKVCMDLRANLKQVKKEDTEKERDLRDVGDWRKNIEEKSGMEGRKKMFESES
Protein: Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (mPar-1b) (Q05512)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase. Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Lateral cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7KZI7}. Cytoplasm {ECO:0000250|UniProtKB:Q7KZI7}. Note=Phosphorylation at Thr-593 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm. {ECO:0000250}.
Interaction partners:
- Dystrophin
- Protein S100-A8
Sequence:
MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMLRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKIDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRSSDQAVPAIPTSNSYSKKTQSNNAENKRPEEETGRKASSTAKVPASPLPGLDRKKTTPAPSTNSVLSTSTNRSRNSPLLDRASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSSGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLNEPESKDRVETLRPHVVGSGGTDKDKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL
Protein: Flotillin-1 (O08917)
Organism: Mus musculus (Mouse)
Function: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O75955}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75955}. Endosome {ECO:0000250|UniProtKB:O75955}. Membrane, caveola {ECO:0000269|PubMed:9153235}; Peripheral membrane protein {ECO:0000269|PubMed:9153235}. Melanosome {ECO:0000250|UniProtKB:O75955}. Membrane raft {ECO:0000250|UniProtKB:O75955}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Membrane-associated protein of caveola (PubMed:9153235). {ECO:0000250|UniProtKB:O75955, ECO:0000269|PubMed:9153235}.
Interaction partners:
- Flotillin-2
- CD63 antigen
- CD81 antigen
- Cadherin-1
- Catenin beta-1
- Coronin-1C
- Catenin delta-1
- Catenin alpha-1
- Caveolin-1
- CD9 antigen
Sequence:
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILSRLPESVERLTGVSISQVNHNKPLRTA
Protein: Electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) (EC 1.5.5.1) (Q7JWF1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein subunit beta
- acetyl-CoA C-acyltransferase
- Dihydroorotate dehydrogenase
- Hydroxysteroid dehydrogenase-like protein 2
- Isovaleryl-CoA dehydrogenase, mitochondrial
- HL08109p)
- Decaprenyl diphosphate synthase subunit 2, isoform A
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MSALMKMHRVRRLFSPALARSISDVAKYPRITTHYTLNPREKDERWTEVDMERCVEEVDLVIVGGGPAGMSAAIRAKQLAAEKDQEIRVCVVEKAAEVGGHILSGAVIDPISLNELIPDWQEQGAPLNTPVTKDTFSFLTGSGRISIPVFKGWPMDNHGNYVVRLGHLVKWLGDQAEALGVEIYPGCAASEVLFHEDGSVKGIATNDVGIAKSGAPKDTFARGMELHAKTTIFAEGCRGHLTKQIMQKFGLNEGSEPQAYGIGLKEVWEIAPEKHQPGLVEHTIGWPLDRFTYGGSFLYHLNEPTPTIAVGFVVGLNYKNPWLSPFQEFQRFKTHPKVRDVFEGATRIAYGARAINEGGFQSLPQKLSFPGGCLVGCSAGFLNVPRIKGSHYAMKSGMLAAESAFEAINADAQSTAGVEPTGYAEKIKDSFVWKDLYSVRNVHPSFHNPLGLYGGLVLSGFSIFMGGREPWTLKHGPQDHESLKPASSCPPIVYPKPDGKISFDLLSSVALTGTNHEGDQPAHLTLKDDRIPVDHNLALYEGPEQRFCPAGVYEYVPNEEGGNMKLQINAQNCIHCKTCDIKDPKQNINWVVPEGGGGPAYNGM
Protein: Ankyrin repeat and SOCS box protein 18 (ASB-18) (Q6ZVZ8)
Organism: Homo sapiens (Human)
Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 7
Sequence:
MSNSDYLPDYPLNSDLVKRLKSALDAKDEERVRDLICTEITPVDAVIELANDDWMKDPSAQLPTGMLLGDLDHLKPLMDQFFQDANVVFEINKDEMEWQVKSPATFGLSGLWTLEYKRELTTPLCIAAAHGHTACVRHLLGRGADPDASPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLGCAQALLEHGASVQRVGGTGRDTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETALSAACGAARRPDEHGRCLRLCALLLRRGAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGASPLGRVLQTASCALQASPQRTVQALLNHGSPTVWPDAFPKVLKTCASVPAVIEVLFNSYPQLCLSESWKEVIPEEVFQMHKPFYQSLFALALTPRCLQHLCRCALRRLFGKRCFDLIPLLPLPKPLQNYLLLEPQGVLH
Protein: RIM-binding protein, isoform M (A0A126GUV2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPEEAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNVPAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQPDAGSGLLGGLLGGLFSKPTQNQVNQNGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKNARPASPTLLDNTGHPAPDHQTQGMIGRVGNVGLQQQQQQQQQQQQLQQQQQYGQQQTQMGQQQQQQQQMGQPGMMGQQMGQPMGQQMGQMGQMGQMGQQQMGQQQMGQQQQPPTTQAQTGGLFSGATSLLSGATSAATGGLFGSKQPPKTDPMQPQGGVQPAQQQANAFGAQQPGMGMQQQGGMQSGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQPGMQQQQQQPQQVPPQAQAPPPGPGAGLLGGLKGIAAAAPGGDVLSKGKDLFGKFGFGFGK
Protein: Putative monoglyceride lipase (MGL) (EC 3.1.1.23) (Fatty acid ethyl ester hydrolase) (FAEE hydrolase) (Monoacylglycerol hydrolase) (MAG hydrolase) (MGH) (Monoacylglycerol lipase) (MAG lipase) (MAGL) (O94305)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Has a strong preference for monounsaturated monoglycerides. Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA). Involved in fatty acid ethyl ester (FAEE) catabolism. FAEEs are non-oxidative metabolites of ethanol that are transiently incorporated into lipid droplets (LDs). Their mobilization by LD-resident FAEE hydrolases facilitates a controlled metabolism of these potentially toxic lipid metabolites.
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:P28321}. Cytoplasm {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P28321}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P28321}. Note=Although the protein is identified in the cytoplasm, several membrane systems and lipid droplets, MGL activity is only measured in membrane fractions and lipid droplets. {ECO:0000250|UniProtKB:P28321}.
Interaction partners:
- NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial
- RNA polymerase I-specific transcription initiation factor rrn11
- Diacylglycerol O-acyltransferase 1
- Triacylglycerol lipase ptl1
- Triacylglycerol lipase ptl3
- NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial
- Uncharacterized oxidoreductase C26F1.07
- Glycerol dehydrogenase 1
- Putative lipase atg15
- Putative acyl carrier protein, mitochondrial
Sequence:
MADLYTKDWTDVKDKPVARVVFIHGFGEHVNAYPEFFEALNERNIEVYTFDQRGFGHSRKGGPKKQGCTGGWSLVFPDLDYQILRASDTELPLFLWGHSMGGGLALRYGISGTHRHKLAGVIAQAPMLRCHPDTEPNFLLRKALTLVSKVHPNFLFDSDVQSQHITRDEAVNQRLQDDPLVSSVGSLQVFSDMLNRGTKTIELAPQFFLPLLITHGTDDNVTCSDSSKEFYENAGTKDKTYQSYPGFYHSLHIEKKPEVYEYLDKVAAWIYEHSKPSETVKSEQETAVEHPKPTATTSAPSASPTGVPVEEESHKATSDAVPPAEAKPEPVPASAAERAPTSESTTVPETIVASTTKVISEPAPRVTTAATADIVTNK
Protein: GM15606p (Q8MSF8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAKLLLIFSILTILATIHDSSFVQADLTTKERIKKHQDWLREHRKPKTKKKISTNSYYELANLWHTRKDLSSPKQKPNNKEEYLENETASKISNKSDEKVLKSTTIISLNATNPSTSTFKSVLETTTLPSVTTKDLFESGNVATTRQTPKVEEVLSSPNPPQEATSSTSKKAKKKVYPYPRWDKWSDWSSCSRSCGGGVKYQVRKCINRNLLTNNQLTSNACVGYFKRYQLCNDVPCDEQSPDFRASQCSAYNDKEFHGHRYRWEPYVKDDAECELNCMPFGMKSFATLNESVIDGTPCGHPAEYFRSQFWERAVCVDGACKAVQASGEIDGLYAHSGSVSCGGLLCRPVTGIFTRDPLPEHAYIHVTTLPVGASNISITELKNSINLLVLRTSNELAIFNGENTVSESGSYEAVGAVFDYHRIDGAEDSNGVTEWITSIGPIRDSLQLMVFTKSANNTGVKYGYMLPIVSESEENEMSLESSDGLLRSGMEDTSSSSSSRAGRKRIFNWKVIGFSSCTKSCGGGTQTPIIRCIRKNPLRYYSQRRCTHSVKPVLNENLLHCNTQPCPAYWRFDDWGECRCSSSGGLRRREVSCVQELASGLVIHVDKAACMEDQPPMQKQCECPKNRRRNLSRYRLSGPSESSSNSSQVKRSKIDGSDATAIWLVSDWNQYCSVTCGSGVEYRTVFCDRSKAGEQRCDPSTTPESRRPCEKPACELGDWFTGPWSSCNGDCFDLTRTREVLCIRSQLITEHSECTPELKPQSVEKCSHEEVEYCAARWHYSDWSECTKPCGGGTQRRSVRCLEYDIKMNALRESTHCRYTNREPIYRNCNVQACAEVPKTEVTPVCADKFSNCQWASQAKLCSYDYYRDNCCFSCTGGI
Protein: Salicylate synthetase (YbtS) (Q9Z396)
Organism: Yersinia pestis
Interaction partners:
- Tryptophan biosynthesis protein TrpCF
- Salicyl-AMP ligase YbtE
- Anthranilate synthase component 2
- Anthranilate phosphoribosyltransferase
- Para-aminobenzoate synthase glutamine amidotransferase component II
- Previously sequenced as Yersinia pestis yersiniabactin biosynthetic protein Irp2 TR:Q9Z399
- Irp1 protein
- Tryptophan synthase beta chain
- Putative glycosyl transferase
- Tryptophan synthase alpha chain
Sequence:
MKISEFLHLALPEEQWLPTISGVLRQFAEEECYVYERQPCWYLGKGCQARLHINADGTQATFIDDAGEQKWAVDSIADCARRFMAHPQVKGRRVYGQVGFNFAAHARGIAFNAGEWPLLTLTVPREELIFEKGNVTVYADSADGCRRLCEWVKEAGTTTQNAPLAVDTALNGEAYKQQVARAVAEIRRGEYVKVIVSRAIPLPSRIDMPATLLYGRQANTPVRSFMFRQEGREALGFSPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKEAELLHDSKEVLEHILSVKEAIAELEAVCQPGSVVVEDLMSVRQRGSVQHLGSGVSGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYSGAILLLDDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTETREKLASIAPYLMV
Protein: Lysosome membrane protein 2 (85 kDa lysosomal membrane sialoglycoprotein) (LGP85) (Lysosome membrane protein II) (LIMP II) (Scavenger receptor class B member 2) (O35114)
Organism: Mus musculus (Mouse)
Function: Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}; Multi-pass membrane protein {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}.
Interaction partners:
- Lysosomal acid glucosylceramidase
- CD63 antigen
- Apolipoprotein B-100
- P-selectin glycoprotein ligand 1
- Transferrin receptor protein 1
- AP-3 complex subunit beta-1
- Disabled homolog 2
- Cation-independent mannose-6-phosphate receptor
- Intercellular adhesion molecule 1
Sequence:
MGRCCFYTAGTLSLLLLVTSVTLLVARVFQKAVDQTIEKNMVLQNGTKVFNSWEKPPLPVYIQFYFFNVTNPEEILQGEIPLLEEVGPYTYRELRNKANIQFGENGTTISAVTNKAYVFERNQSVGDPNVDLIRTINIPLLTVVDLAQLTLLRELIEAMLKAYQQKLFVIHTVHELLWGYKDEILSLVHIFKPDVSPNFGLFYERNGTNDGEYVFLTGEDNYLNFSKIVEWNGKTSLDWWTTDTCNMINGTDGDSFHPLISKDEVLYLFPSDLCRSVHITFSSFENVEGLPAFRYKVPAEILANTSENAGFCIPEGNCMDSGVLNISICKNGAPIIMSFPHFYQADEKFVSAIKGMHPNKEEHESFVDINPLTGIILRGAKRFQINTYVRKLDDFVETGDIRTMVFPVMYLNESVLIDKETANQLKSVINTTLVVTNIPYIIMALGVFFGLVFTWLACRGQGSMDEGTADERAPLIRT
Protein: Dynein, axonemal, heavy chain 11 (H3BLD7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
XDYRSIGNIYKGLVQTGAWGCFDEFNRIAVEVLSVVAVQVKMIHDAIRNGRKRFVFLGETIPLKPSVGIFITLNPGYAGRTELPENLKALFRPCAMVAPDTELICEIMLVAEGFVDARSLARKFISLYTLCEELLSKQDHYDWGLRAIKSVLVVAGSLKRGDKNRPEDQVLMRALRDFNMPKIVTDDVPVFLGLVSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVRHSVFVVGNAGTGKSKILRTLNRTYVNMKQKPVWSDLNPKAVTTDELFGFIHHATREWKDGLFSSILREQANLTHDGPTWIVLDGDIDPLWIESLNTVMDDNKVLTLASNERVALKPSMRLLFETHHLRTATPATVSRAGILYVNPQDLGWNPYVASWIDRRRHQSEKANLTILFDKYIPVCLEKLRTSFKAITSVPESSLVQTICTLLECLLTPENIPPDSPKETYEVYFAFACVWTFGGTLLRDQLSDYQADFSRWWHKEMKAVKFPSQGTIFDYYLDHKTKKFLPWTDKVPQFSMDADAPLKTVLVHTPETTRLRYFTELLLCKGKPIMLVGNAGVGKTVFLSNTLASLSENYIVSCVPFNYYTTSAALQRILEKPLEKKAGRNYGPKGNKKLVYFIDDLNMPEVDLYGTIQPHALLRQHIDYGHWYDRHKIMLKEIRNCQYVACMNPMVGSFTVNPRLQRHFTVFAFNFPSLDALTTIYGQIFSFYLQQQAFCPSVLRAGPSLIQATIAFHQMMAESFVPTAIKFHYNFNLRDLSNIFQGILFASPECLKSLEDLARLWLHETSRVYGDRLIDTNDFDLFQRKMLETAHKYFKGVDANALLRQPLVYCHFASGGEDPCYMPVKDWEGLKAVLMEMVDNYNELHSAMHLVLFEDAMQHVCRISRILRIPQGHALLIGVGGSGKQSLSRLAAYICSLEVFQITLTEGYGAQELRVDLANLYVRTGAKNMPTVFLLTDAHVLDESFLVLINDLLASGDIPDLFSDEDMDKIISGIRNEVRGLGLVDSRENCWAFFLARVRQQLKMVFCFSPVGHTLRVRARKFPAIVNCTAIDWFHEWPQEALVSVSRRFIEEIEGIEPQHKDSISLFMAHVHTSVKEVSAWYYQNERRYNYTTPRSFLEQISLFKSLLKKKREEVKQKQEHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIGLQTEKVSREKAIADAEERKVAAIQTEASQKQRECEADLLKAEPALVAAKDALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLAPRGRVPKDRSWKAAKIFMGKVDDFLQALINYDKEHIPENCLKVVNEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIRFYEVYCDVEPKRQALAQTNLDLAAATEKLEAVRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTAAFVSYIGSFTRQYRQELVDCKWIPFLQQKVSIPIAEGLDLIAMLTDDATIATWNNEGLPSDRMSTENATILTHCERWPLMIDPQQQGIKWIKNKYGPDLKVTHLGQKGFLNTIETALAFGDVILIENLKETVDPVLGPLLGRNTTKKGKFIRIGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQIWRG