wanglab/gogpt-training-data huggingface dataset:
Protein: Tricyclene synthase TPS4, chloroplastic (EC 4.2.3.105) ((E)-beta-ocimene synthase) (MtEBOS) (MtEbetaOS) (EC 4.2.3.106) (Terpenoid synthase 4) (MtTPS4) (Q5UB07)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Promotes the emission of terpenes volatile organic compounds (VOC) in response to damage mediated by arthropod herbivores (e.g. Spodoptera exigua), probably to attract natural enemies of the herbivores.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:15660362}.
Interaction partners:
Sequence:
MLLNSSFISLPSFFKSQELGRTNLLIHRNGSPLLCYATNTNVSQRKSANYQPNIWNYDILQSLKHDYEDARYVDRSRRLQEEVKRMIKDENVNILELIDTVKQLGLSYHFEEEIGEALDRFLSLEKCSGRNNFGRSLHETALRFRLLREYGYDISPDIFEKFKDHNGNFKACLVQDIKGMLSLYDASFLSYEGEQILDEANAFTSIHLKDLSEGRSSILIDQVNHSLELPLYRRVQSLEARWFIDSYENRKDANKVLLEAAKLNFNIVQSTLQQDLKEMSRWWKGMGLAPRLSFGRDRLMECFFWAAGMTPFEPQFSNIRKGLTKVCSLITLIDDIYDVYGTLDELELFTTAVESWDINAIQILPEYMKIFFLALYTTVNDFTYDTIKETGHDILPYLVKVWSDMLKAFLQEAKWCHNKHMPKFDDYLNNAWVSVSGVVLLTHSYFLLNRNITKEGLGYLENCPMLLQTPSIIFRLCNDLATSSAELERGEGANSIICYMNENGVSEEVAYKHIQNLLDQTWKKMNKDRVINSPSSKYFSETIINLARISHCTYQYGDGHGAPDTLAKNRIKALILEPIN
Protein: Small nuclear ribonucleoprotein U1 subunit 70 (A0A8I5ZV69)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMCKVLLPSSVPLHSHFAPLPRSHVCLFWELEKQSWLTFLATTCQALHLYKAVVGCPDDFDVNSVSSRGVSRPPQAVDHSGDLVNFLPILISHH
Protein: U6 snRNA-associated Sm-like protein LSm5 (Q9VRT7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365055}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm1
- U6 snRNA-associated Sm-like protein LSm3
- Probable small nuclear ribonucleoprotein Sm D2
- Protein associated with topo II related - 1, isoform A
- Small nuclear ribonucleoprotein F
Sequence:
MTAVPPPSNISTLMPLELVDKCIGSRIHIIMKNDKEMVGTLLGFDDFVNMLLDDVTEYENTPDGRRITKLDQILLNGNNITMLVPGGELAE
Protein: Ubiquitin thioesterase OTU1 (EC 3.4.19.12) (DUBA-8) (HIV-1-induced protease 7) (HIN-7) (HsHIN7) (OTU domain-containing protein 2) (Q5VVQ6)
Organism: Homo sapiens (Human)
Function: Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin. May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes. May recruit PLAA, UBXN6 and VCP to damaged lysosome membranes decorated with K48-linked ubiquitin chains and remove these chains allowing autophagosome formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27753622}. Note=Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. {ECO:0000269|PubMed:27753622}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Polyubiquitin-C
- Phospholipase A-2-activating protein
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- UBX domain-containing protein 6
- Nuclear protein localization protein 4 homolog
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin conjugation factor E4 B
Sequence:
MFGPAKGRHFGVHPAPGFPGGVSQQAAGTKAGPAGAWPVGSRTDTMWRLRCKAKDGTHVLQGLSSRTRVRELQGQIAAITGIAPGGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIIEEDQTRPRSSPAFTKRGASSYVRETLPVLTRTVVPADNSCLFTSVYYVVEGGVLNPACAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEARRRRQFTDVNRFTLRCMVCQKGLTGQAEAREHAKETGHTNFGEV
Protein: Kunitz-type serine protease inhibitor Bt-KTI (D8KY58)
Organism: Bombus terrestris (Buff-tailed bumblebee) (Apis terrestris)
Function: Serine protease inhibitor that inhibits plasmin (Ki=2.01 nM) and trypsin. Acts as an antifibrinolytic agent.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MNHKFIALLLVVLCCALSVHQVSAEIPSHCTLPLATGTCRGYFPRFGYNVEMGKCVEFIYGGCDGNANNFRNLEECQQSCSV
Protein: Protein kinase C-binding protein NELL2 (NEL-like protein 2) (Nel-related protein 2) (Q99435)
Organism: Homo sapiens (Human)
Function: Required for neuron survival through the modulation of MAPK pathways (By similarity). Involved in the regulation of hypothalamic GNRH secretion and the control of puberty (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q62918}.
Interaction partners:
- Roundabout homolog 3
- Anoctamin-6
- Anoctamin-5
Sequence:
MESRVLLRTFCLIFGLGAVWGLGVDPSLQIDVLTELELGESTTGVRQVPGLHNGTKAFLFQDTPRSIKASTATAEQFFQKLRNKHEFTILVTLKQTHLNSGVILSIHHLDHRYLELESSGHRNEVRLHYRSGSHRPHTEVFPYILADDKWHKLSLAISASHLILHIDCNKIYERVVEKPSTDLPLGTTFWLGQRNNAHGYFKGIMQDVQLLVMPQGFIAQCPDLNRTCPTCNDFHGLVQKIMELQDILAKTSAKLSRAEQRMNRLDQCYCERTCTMKGTTYREFESWIDGCKNCTCLNGTIQCETLICPNPDCPLKSALAYVDGKCCKECKSICQFQGRTYFEGERNTVYSSSGVCVLYECKDQTMKLVESSGCPALDCPESHQITLSHSCCKVCKGYDFCSERHNCMENSICRNLNDRAVCSCRDGFRALREDNAYCEDIDECAEGRHYCRENTMCVNTPGSFMCICKTGYIRIDDYSCTEHDECITNQHNCDENALCFNTVGGHNCVCKPGYTGNGTTCKAFCKDGCRNGGACIAANVCACPQGFTGPSCETDIDECSDGFVQCDSRANCINLPGWYHCECRDGYHDNGMFSPSGESCEDIDECGTGRHSCANDTICFNLDGGYDCRCPHGKNCTGDCIHDGKVKHNGQIWVLENDRCSVCSCQNGFVMCRRMVCDCENPTVDLFCCPECDPRLSSQCLHQNGETLYNSGDTWVQNCQQCRCLQGEVDCWPLPCPDVECEFSILPENECCPRCVTDPCQADTIRNDITKTCLDEMNVVRFTGSSWIKHGTECTLCQCKNGHICCSVDPQCLQEL
Protein: Corin, serine peptidase (J3KR90)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MKQSPALAPEERCRRAGSPKPVLRADDNNMGNGCSQKLATANLLRFLLLVLIPCICALVLLLVILLSYVGTLQKVYFKSNGSEPLVTDGEIQGSDVILTNTIYNQSTVVSTAHPDQHVPAWTTDASLPGDQSHRNTSACMNITHSQCQMLPYHATLTPLLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDSHGLLPCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTESSNVSRICFSPQQENGKQLLCGRGENFLCASGICIPGKLQCNGYNDCDDWSDEAHCNCSENLFHCHTGKCLNYSLVCDGYDDCGDLSDEQNCACHSQGLVECRNGQCIPSTFQCDGDEDCKDGSDEENCSVIQTSCQEGDQRCLYNPCLDSCGGSSLCDPNNSLNNCSQCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALCEHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCLMPDEYVEECSPSHFKCRSGQCVLASRRCDGQADCDDDSDEENCGCKERDLWECPSNKQCLKHTVICDGFPDCPDYMDEKNCSFCQDDELECANHACVSRDLWCDGEADCSDSSDEWDCVTLSINVNSSSFLMVHRAATEHHVCADGWQEILSQLACKQMGLGEPSVTKLIQEQEKEPRWLTLHSNWESLNGTTLHELLVNGQSCESRSKISLLCTKQDCGRRPAARMNKRILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGRENAAVWKVVLGINNLDHPSVFMQTRFVKTIILHPRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMGNKMPFKLQEGEVRIISLEHCQSYFDMKTITTRMICAGYESGTVDSCMGDSGGPLVCEKPGGRWTLFGLTSWGSVCFSKVLGPGVYSNVSYFVEWIKRQIYIQTFLLN
Protein: GATA transcription factor 15 (OsGATA15) (Protein NECK LEAF 1) (Q6L5E5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor that regulates organogenesis during transition from the vegetative to the reproductive phase. Regulates the expression of CYP78A11/PLA1, HD3A and MADS1 during reproductive development in rice. May act upstream of CYP78A11/PLA1 during panicle development. Acts independently of the photoperiodic and gibberellin signaling pathways.
Interaction partners:
Sequence:
MLHHYYSGGAGHHQDVAAAGSPGDMASSTFSLFFPMSNGQCWPPSTVEESAAYDDHSTVTTSPSSPSSSSTGSVDCTLSLGTPSSRRAEPVAAAAPAANHGAPVPAHYPSLSAATVSWDATAESYYCGQQGRPATGAAKCAAGAGHDALLDRRCANCGTASTPLWRNGPRGPKSLCNACGIRYKKEERRAAATTTTADGAAGCGFITAQRGRGSTAAKAAPAVTTCGEETSPYVVGGGGGGGEVADAAYLAWRLNVVPPAATATAFSVWPERASLYHYN
Protein: Pyrimidine 5'-nucleotidase PynA (EC 3.1.3.5) (Antimutator protein PynA) (House-cleaning nucleotidase) (Non-canonical pyrimidine nucleotide phosphatase) (Nucleoside 5'-monophosphate phosphohydrolase) (Pyrimidine nucleotidase A) (Ribonucleotide monophosphatase) (Q8DPQ3)
Organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Function: Nucleotidase that shows high phosphatase activity toward non-canonical pyrimidine nucleotides and three canonical nucleoside 5'-monophosphates (UMP, dUMP and dTMP), and no activity against IMP, UDP, GMP, AMP, UTP or pNPP. Appears to function as a house-cleaning nucleotidase in vivo, since the general nucleotidase activity of it allows it to protect cells against non-canonical pyrimidine derivatives such as 5-fluoro-2'-deoxyuridine monophosphate (5-FdUMP), and prevents the incorporation of potentially mutagenic nucleotides such as 5-bromo-2'-deoxyuridine (5-BrdU) into DNA. Is strictly specific to pyrimidine substrates with 5'-monophosphates and shows no activity against nucleoside di- and triphosphates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31437335}.
Interaction partners:
- Uncharacterized protein
Sequence:
MFYKFLLFDLDHTLLDFDAAEDVALTQLLKEEGVADIQAYKDYYVPMNKALWKDLELKKISKQELVNTRFSRLFSHFGQEKDGSFLAQRYQFYLAQQGQTLSGAHDLLDSLIERDYDLYAATNGITAIQTGRLAQSGLVPYFNQVFISEQLQTQKPDALFYEKIGQQIAGFSKEKTLMIGDSLTADIQGGNNAGIDTIWYNPHHLENHTQAQPTYEVYSYQDLLDCLDKNILEKITF
Protein: Protein trapped in endoderm-1 (Q9NDM2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for the first active step of germ cell migration: transepithelial migration of germ cells through the posterior midgut (PMG) epithelium.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-1
- G protein beta subunit 5
- G protein alpha i subunit subunit alpha 65A)
Sequence:
MDQDMGMATGYFQDADMQMDEPAAATQSIYPHSATLFAAISACVFVTIGVLGNLITLLALLKSPTIREHATTAFVISLSISDLLFCSFSLPLTAVRFFQESWTFGTTLCKIFPVIFYGNVAVSLLSMVGITLNRYILIACHSRYSQIYKPKFITLQLLFVWAVSFLLLLPPILGIWGEMGLDEATFSCTILKKEGRSIKKTLFVIGFLLPCLVIIVSYSCIYITVLHQKKKIRNHDNFQIAAAKGSSSSGGGSYMTTTCTRKAREDNRLTVMMVTIFLCFLVCFLPLMLANVVDDERNTSYPWLHIIASVMAWASSVINPIIYAASNRNYRVAYYKIFALLKFWGEPLSPMPSRNYHQSKNSKELSGVIRSTPLFHAVQKNSINQMCQTYSV
Protein: Dye-decolorizing peroxidase (DyP) (EC 1.11.1.-) (A0A3T0E4B9)
Organism: Brevibacterium linens
Function: Cargo protein of a type 1 encapsulin nanocompartment. Has both general peroxidase activity and dye-decolorizing activity. Can catalyze the oxidation of both protoporphyrinogen IX and coproporphyrinogen III to their corresponding porphyrins. Also efficiently decolorizes the dyes alizarin red and Cibacron blue F3GA (By similarity). This cargo-loaded encapsulin nanocompartment is probably involved in protection against oxidative damage (By similarity).
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:19172747, ECO:0000269|PubMed:27355101, ECO:0000269|PubMed:29166561}.
Interaction partners:
Sequence:
MTEAFPNGKTPQHVLGPPAPAAVFLVLTVRSGAEAEAKDFLGDIAGVVRSVGFRAREDHLSCVTGIGAELWDRMFDAPRPAGLHPFIEQRGDVHTAPSTPGDLLFHIRARRMDLCFELARQLVGELGDAVSVVDEVHGFRYFDERDIMGFVDGTENPEDQEAVDSVFTPTGGDDPASSTYVIVQKYTHDMAAWEALSVEDQEAAFGRHKLSDMEFPDEDKAPNSHLILNTIEDEDGTEHKIVRDNMVFGSVESGEFGTYFIGYAADVSVTEQMLENMFIGNPRGTYDRILDFSTAQTGGLFFVPSQDFLDDPDGELAAAEPSDAQNDDPASASARIEETDPPNPASADDPAPADDSLGIGSLRRRDQ
Protein: Ras-related protein RABD2c (AtRABD2c) (Ras-related protein Rab1C) (AtRab1C) (Q9SEH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}. Golgi apparatus, trans-Golgi network membrane. Golgi apparatus membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta 1
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Tetratricopeptide repeat
- Geranylgeranyl transferase type-2 subunit beta 2
- Trafficking protein particle complex subunit
- SNARE-like superfamily protein
- Transport protein particle
- DUF506 family protein
Sequence:
MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDSYLDSYISTIGVDFKIRTVEQDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVTYDVTDLESFNNVKQWLNEIDRYASENVNKLLVGNKCDLTSQKVVSTETAKAFADELGIPFLETSAKNATNVEEAFMAMTAAIKTRMASQPAGGSKPPTVQIRGQPVNQQSGCCSS
Protein: Ubiquitin-like modifier HUB1 (Q6Q546)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms conjugate with SPH1 and HBT1. Involved in morphogenesis.
Interaction partners:
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Pre-mRNA-splicing factor 8
- Pre-mRNA-splicing factor CEF1
- U2 snRNP component IST3
- Pre-mRNA-splicing factor ISY1
- Small nuclear ribonucleoprotein G
- 23 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Small nuclear ribonucleoprotein Sm D2
- Pre-mRNA-splicing factor RDS3
- RDS3 complex subunit 10
Sequence:
MIEVVVNDRLGKKVRVKCLAEDSVGDFKKVLSLQIGTQPNKIVLQKGGSVLKDHISLEDYEVHDQTNLELYYL
Protein: DNA replication complex GINS protein psf2 (O94329)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation and is required for bir1 localization.
Subcellular location: Nucleus {ECO:0000269|PubMed:16199877, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm6
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm2
- DNA replication complex GINS protein psf1
- DNA replication complex GINS protein psf3
- DNA replication complex GINS protein sld5
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm7
Sequence:
MALPRELEISFSPEEMEFLAGNEYINIVPSETMDQLPLVSATIPIMKPPKKCRVPLWLALELKKQNLARIVPPEWMEIGKLENIRDDELENETFSELPFRWLETAHLLLNFCADDIEDVEDIRRILLDIREARQSKARTGLEAINEVQLTLDNLGAMEINEIRPIFREVMDRMRKIVQVSQEE
Protein: Serine acetyltransferase (SAT) (EC 2.3.1.30) (P95231)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- O-acetylserine sulfhydrylase
- L-cysteine desulfhydrase Cds1
- Probable cystathionine beta-synthase Rv1077
- L-serine dehydratase
- O-phosphoserine sulfhydrylase
- Cysteine--tRNA ligase
- Phosphoserine phosphatase SerB2
- Serine hydroxymethyltransferase 1
- Serine hydroxymethyltransferase 2
- S-sulfocysteine synthase
Sequence:
MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFIDHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIGQSQPSPGGPFDWRLPDLVGASLDSLLTRVARLEALGGGPQAAGVIRPPEAGIWHGEDFSI
Protein: Monoglucosyldiacylglycerol epimerase (GlcDG epimerase) (EC 5.1.3.34) (P74167)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Involved in the biosynthesis of galactolipids found in the photosynthetic membranes. Catalyzes the isomerization of monoglucosyldiacylglycerol (GlcDG) to yield monogalactosyldiacylglycerol (MGDG).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Slr1508 protein
- Beta-monoglucosyldiacylglycerol synthase
- Sll0545 protein
- UTP--glucose-1-phosphate uridylyltransferase
- Photosystem II reaction center protein L
Sequence:
MAMAWLMGLGLALASVLWVELVRDCYHALAHVWSPLYRLHGWHHRVFRSDLSVVSTEIYQKAHWYNDVPEALVMLAFGIWPPLLTWMWQGFSQWPLILAASAGMVYTLGFLLSAIARGVGLPNADEITDLTHRPGPFLTPPAPWMVNRTYHWRHHFDDPNAYFCGTLTLVDKMLGTALSLKGKKIAVTGASGGFGQALLQELHQQGAKAIAITSCGQEVTVIGAEKTIPIRTEQWCIGQEDQLKDLLAEIDVLVINHGVNVHQRRDGQAIQEAYEVNTFSALRLMELFLATVKTNRHIATKEIWVNTSEAEVNPAFSPLYELSKRALGDVVTLKRLDSPCVIRKLILGPFKSKLNPVGIMSAAWVARQVVKGVKRDSRNIIVTINPITFIAFPVKEFFVSLYFRCFTKKS
Protein: 2,3-dimethylmalate lyase (EC 4.1.3.32) (Q0QLE4)
Organism: Eubacterium barkeri (Clostridium barkeri)
Function: Catalyzes the formation of proponate and pyruvate from (2R,3S)-2,3-dimethylmalate. Has no activity toward dimethylmaleate, malate, citramalate, isocitrate and citrate.
Interaction partners:
- 3-methylitaconate isomerase
- Citrate synthase
- Citrate synthase
- L-serine dehydratase
- 2-methyleneglutarate mutase
- Pyruvate kinase
- Putative repair enzyme for 2-methyleneglutarate mutase
- Malate dehydrogenase
- Pyruvate:ferredoxin oxidoreductase
- Pyruvate:ferredoxin oxidoreductase
Sequence:
MNTAAKMRELLSTKKMVVAPGAHDAMTAKVIGRLGFDAVYMTGYGQSASHLGQPDVGLLTMTEMVARANAIVEAAGVPVIADADTGFGNAVNVMRTVREYEKAGVAVIQLEDQVMPKKCGHMVGREIVSKEEMVGKIKAAVDTRVNPDFMIMARTDARTTKGIDEALERGLAYKEAGADIIFIESPEGEEEMKRINETIPGYTLANMVEGGRTPLLKNAELEALGYNITIYPTASIYVATKAMVDLWTALKNDDTTAGVMDTMVTFSEFNDLMGLEKIREVEHNYATGR
Protein: Beta-ketoacyl synthase PigJ (PKS) (EC 2.3.1.-) (Q5W262)
Organism: Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida)
Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the decarboxylation on the malonyl group attached to PigH to yield a C2 carbanion of acetyl-S-PigH. Then, the heterocyclic pyrrole group of PigG moves to the PigJ active site Cys-525 to generate a transient pyrrolyl-S-cysteinyl PigJ intermediate (acyl donor) whose pyrrolyl group is captured by the C2 carbanion of acetyl-S-PigH to yield the pyrrolyl-beta-ketoacyl-S-PigH.
Interaction partners:
- Non-ribosomal peptide synthetase
- Non-ribosomal peptide synthetase
- Non-ribosomal peptide synthetase
- Malonyl CoA-acyl carrier protein transacylase
- 4'-phosphopantetheinyl transferase
- Non-ribosomal peptide synthetase
- L-proline--[L-prolyl-carrier protein] ligase
- Non-ribosomal peptide synthetase
- Malonyl CoA-acyl carrier protein transacylase
- Aminotransferase PigE
Sequence:
MSNDKHIAPLAVVSMGCVLPGVDHFRALDTIADWETVFQSASPLAWSETSRPIQGRQMDDSGFDFKKFSIPPLFRKAVSRETRLALRAAEDALAGLVLPESLRDCCDQFCAIHLGSDAAYRNATKVGALRALAEKLQAQGCPAAEVRRRLDDYKQPLAESLGCSSHDRVGEMASSIPARIAHFAHTRGKCQTLDGADKGGLRLLQLAQDCFRYHDSQMAVLTSVQCFHHRPQAYMLLEQGVSQDACWLEGAISLVVCPLAVAHEQGWPVLTQLGDIVTTHDGSPQPEADHPAALYFAGANQVFCQIVEMVLRQHQRCEGRSFTGGRWQVNVAQTQSLTPAVDDRVAIVDYQPITGHPLDKTQFWQTLEQGEDALREHSAAHVNAEAFVRTTQQKLSTYIHRTMSFPAHSPSDVALKKPMMPAKKQRLDVTQLYALNSCHSWSEKIRQFERVAIIIASNLSLSADRLQAMRALWSGLPGSEGAIPLPELPSINHWSWYGACGIGTAQLLAQYFGISADCYAVEAACASSLAAVHDAVRALQAGRYDAVIVGGIETATLERDLVLCSAQMMLSVSRIRPFSQGADGFTPGDGGGFVMLTHHPVPRAIATIEAISGSCDSYSMTAPDPLGQALAIKKTLSLTAIDAQTVQYLEAHGTGTELGDRSEVMSLKYSYHRDKHSPLYIGSAKYNFGHCFAGAGALSLCKVLSAFEHERIPPTPVSELNVDLPLGDIPAEVPQQAIPWRLSEDGQRKAAINAFGTGGINYHLVIRQSS
Protein: WHAMM and JMY related, isoform D (WHAMM and JMY related, isoform E) (A0A0B4KH08)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEDYTYAYISEPVEFRQLEGNAIDFRKTFDLRGQGTDEMLQLYLRKANLSDDLERLPAIVRRAYVYDIIRSNKEPGYWVPPSMQVSSDVFAHPPPAVRPPPHYADNVSINASLDGMKSSSSSNSLDRYLGAPPSVALAGPSFATSVLVSSKGSKYEISGPVNFQHVSGDVTRDRTRNAFDLNADPNDKVLRKYMMERGITEADISDMRRQEVIKKIIHSNFTWMPPKSDLQAQPKVQDHARPLLYATISTNNQITPPPSPPPPPIATISRPTEAPNFSNYASLTSRFVDISDMDLPAPTPAAPTPFQPAEVGSVIPVQVQPQQSVKPKVPPPPSAVMAKNTHGYPAAIDIRQVRPSVAPKVANETYATISPQRKVGSMRVPPPAPPKPTIVPHTNSTISNGSLYAVSPVQYAPVAKPAPPAAPAKPTSRSSAVYMTPLSAQKTQISSTPVPVSPPPPTAASVGVPPPPPAPPAGVPPAPPPMPVFGAGGAPPPPPPPSSGMAGVPPPPPMQKSQPKAVSAASTGGDPRDAFLESIRQGVKLKKVDQKAATISGIKPRPERKPVTTDFLSELKLGITLRRVKNPADNPYSEESESQA
Protein: Protein-arginine rhamnosyltransferase (EC 2.4.1.-) (EF-P arginine rhamnosyltransferase) (A0A0T7AQA7)
Organism: Neisseria meningitidis
Function: Protein-arginine rhamnosyltransferase that catalyzes the transfer of a single rhamnose to elongation factor P (EF-P) on 'Lys-32', a modification required for EF-P-dependent rescue of polyproline stalled ribosomes.
Interaction partners:
Sequence:
MNTPPFVCWIFCKVIDNFGDIGVSLRLARVLHRELGWQVHLWTDDVSALRALCPDLPDVPCVHQDIHVRTWHSDAADIDTAPVPDAVIETFACDLPENVLHIIRRHKPLWLNWEYLSAEESNERLHLMPSPQEGVQKYFWFMGFSEKSGGLIRERDYRDAVRFDTEALRQRLMLPEKNAPEWLLFGYRSDVWAKWLEMWQQAGSPMTLLLAGAQIIDSLKQSGIIPQNALQNDGDVFQTASVRLVKIPFVPQQDFDQLLHLADCAVIRGEDSFVRAQLAGKPFFWHIYPQDEHVHLDKLHAFWDKAHGFYTPETASAHRCLSDDLNGGEALSATQRLECWQILQQHQNGWRQGAGAWSRYLFGQPSASEKLAAFVSKHQKIR
Protein: Neuropeptide Y receptor type 1 (NPY1-R) (Q04573)
Organism: Mus musculus (Mouse)
Function: Receptor for neuropeptide Y and peptide YY.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Pro-neuropeptide Y
- Peptide YY
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pancreatic polypeptide prohormone
- Appetite-regulating hormone
- Somatostatin
- Pro-opiomelanocortin
- Oxytocin-neurophysin 1
Sequence:
MNSTLFSKVENHSIHYNASENSPLLAFENDDCHLPLAVIFTLALAYGAVIILGVSGNLALIIIILKQKEMRNVTNILIVNLSFSDLLVAVMCLPFTFVYTLMDHWVFGETMCKLNPFVQCVSITVSIFSLVLIAVERHQLIINPRGWRPNNRHAYIGITVIWVLAVASSLPFVIYQILTDEPFQNVSLAAFKDKYVCFDKFPSDSHRLSYTTLLLVLQYFGPLCFIFICYFKIYIRLKRRNNMMDKIRDSKYRSSETKRINIMLLSIVVAFAVCWLPLTIFNTVFDWNHQIIATCNHNLLFLLCHLTAMISTCVNPIFYGFLNKNFQRDLQFFFNFCDFRSRDDDYETIAMSTMHTDVSKTSLKQASPVAFKKISMNDNEKV
Protein: Synaptosomal-associated protein 29 (SNAP-29) (Golgi SNARE of 32 kDa) (Gs32) (Soluble 29 kDa NSF attachment protein) (Vesicle-membrane fusion protein SNAP-29) (Q9Z2P6)
Organism: Rattus norvegicus (Rat)
Function: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9880331}. Golgi apparatus membrane {ECO:0000269|PubMed:9880331}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:O95721}; Peripheral membrane protein {ECO:0000305}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:O95721}; Peripheral membrane protein {ECO:0000305}. Note=Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic. Localizes to the ciliary pocket from where the cilium protrudes. {ECO:0000250|UniProtKB:O95721}.
Interaction partners:
- Syntaxin-17
- Vesicle-associated membrane protein 8
- Vesicle-associated membrane protein 7
- Beclin 1-associated autophagy-related key regulator
- Syntaxin-6
- Syntaxin-7
- Synaptobrevin homolog YKT6
- Syntaxin-3
- Syntaxin-4
- Syntaxin-16
Sequence:
MSGYPKSYNPFDDDVEDEDTRPAPWKDARDLPDGPDPPIDRQQYLRQEVLRGPSATAASTSRSLFLMYESEKIGVASSEELVRQRGVLEHTEKMVDKMDQDLKMSQKHINSIKSVFGGFINYFKSKPVEPPPEQNGSIVPQPSSRLKEAINTSKDQESKYQASHPNLRRLHDAELDSVPASTVNTEVYPKNSSLRAYHQKIDSNLDELSVGLGRLKDIALGMQTEIEEQDDILDRLTTKVDKLDVNIKSTEKKVRQL
Protein: Prolactin (Q6VLX2)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
HEVLMSLILGLLRSWNDPLYHLVTEVRGMKGAPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARYSAFYNLLHCL