wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar heme ABC transmembrane exporter abc3 (Q9P5N0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Iron-regulated vacuolar transporter that mobilizes stored heme from the vacuole to the cytosol in response to iron deficiency.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16849797, ECO:0000269|PubMed:19915076, ECO:0000269|PubMed:28193844}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16849797, ECO:0000269|PubMed:19915076, ECO:0000269|PubMed:28193844}.
Interaction partners:
- ATP-binding cassette transporter abc2
- Iron transport multicopper oxidase fio1
- Ferric reductase transmembrane component 1
- Vacuolar basic amino acid transporter vsb1
Sequence:
MITANKGLSLVLLIPNLFALVSGGLQYVFDVRRRIFRPHFSQFWTIWMKFFSIALVIITQIYVGYKTKNIGWNFFSVVTYCFVLFLQFAEQSTLRVPMASLLIFWLLKVVTSLLILLFSPYIAITSMARLLTLITLFCSLVCFISEVYVPPCNRVWYSDDTNEVEEKGIRPSEVRYANIFSKLSFSWISSFIKFGYTNYLKESDVWLLPPDERSGNLIIGFEDWWIYHSKNKRRSLFLWKLLFFNHWKLVALITITKLIQDVLAFVQPTLIQKTILFISSYTSPNPESPSRGFIIAILVLVANFLQTLLLQQYNQLIMLLGMRWKTELLASIYRKSLLLSSSARQNRSIGDIINYMAVDTQKISDLPIYLFIIVSGPFQIALALSNLYHLMGYSAFTGVAASVILFPCNIIVANVYKKFQSILMKNKDSRSKLMTEIINNIRSIKLYAWETPFLQKLLHIRNTKELSMLKKIGFITAIGDFAWIFTTIIVTTVAFGAFIIFHGKTQALTADIVFPAVSLFNLLQFPLAMLPTVISSLLEASVSVSRIYEFLIAQELDYNGVQRFPATEIPHEICLEIKSGTFSWSKKTLKQQVTPTLRQINFVAKNGELTCIFGKVGAGKSSLLEACMGNMYKNSGSVFQCGSLAYAAQQPWIFDATIRENILFGSEFDPELYEKTIHACCLKRDFEIFTEGDQTEVGQKGASLSGGQKSRISLARAIYSQADIYLLDDVLSSVDQHVSRDLIKNLFGPEGFLRTHCVVLTTNSLNVLKEADSIYILSNGKIVEKGNYEHLFVSTNSELKQQLSEFNDEKDTQPLPEHTTSYPSTQISLAPSIHVEGLETYSSSERKDSSNKYKSRKRNPIRQKVTEDDKGKCVAQTDELVQRGKVKWHVYWMYFKSCSIGLILLYFFFIISGIMMNVATNVWLKHWSEENGKSSSELNPSPYFYLGIYLFFGFLSCAFISSSSLTMTVLCGIRSGRYLHDSMLKTILRAPMGFFETTSSGRILNRFSNDVYKVDEVVSLTFMFFFRNSIQVLFILGVICYSAPLSLLLIVPLFFLYLYNRAYYVRTSRELKRLDNVTRSPLYAHVQESLSGLSTIRAYGMQETFVEENDLRIDTNHRVWFMFFSSSRWQAIRVECIGDLIIFCTAFYGILSAIKGSPNPGLVGFSLSYAIQITQGLSFIVQQSVDAENNTVSVERILEYINVKSEAPEIIPENRPPCEWPTDGAVSFNHYSAKYREDLSFALNNINIEISPREKIGIVGRTGAGKSTLAMALFRIIEPTEGKIEIDNEDITKFGLYDLRSRLSIIPQESQIFEGNIRENLDPNHRLTDKKIWEVLEIASLKNCISQLEDGLYSRVAEGGANFSSGQRQLICLARVLLTSTRILLLDEATASVHAETDAIVQQTIRKRFKDRTILTVAHRINTVMDSDRILVLDHGKVVEFDATKKLLENKDSMFYSLAKESGLI
Protein: Protein TALPID3 (E9PV87)
Organism: Mus musculus (Mouse)
Function: Required for ciliogenesis and sonic hedgehog/SHH signaling. Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1. May play a role in early ciliogenesis in the disappearance of centriolar satellites that preceeds ciliary vesicle formation (By similarity). Involved in regulation of cell intracellular organization. Involved in regulation of cell polarity (By similarity). Required for asymmetrical localization of CEP120 to daughter centrioles.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9BVV6}. Photoreceptor inner segment {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26386247}. Note=In photoreceptor cells localized to the joint between the inner and outer segments, specifically localized at the mother centriole (basal body) and the adjacent centriole as well as between the two centrioles but not in the connecting cilium (PubMed:26386247). {ECO:0000269|PubMed:26386247}.
Interaction partners:
- Centriolar coiled-coil protein of 110 kDa
- Centrosomal protein of 120 kDa
- Centrosomal protein of 290 kDa
Sequence:
MKNVEFSLERGQRLKMPARKLREIVSPNQGNKLAVVEDELPRVPPALAANKRLAVETRTSSNGTLCGSLDLTSARLYHQPLLESPPASKKSDFSKDAVVRQLPLNKTEENNAPKANDIFISQYTMGQKDALRTVLKQKAQSMPVFKAVKVHLFEDTSTEKNTVAQETETPPNRIDSATTVAAATAAAIATAAPLIKVQSDLEAKVNCVGELLTKLQETDKQLQRVTEHQASVQSKQEKVHCHDHDKQMNAFMEQHIRHLEKLQQQQIDIQTHFIDAALKASSLQLGMSTSRAVGKYSGKLGSPSVGSSVFSHNTFVSKRVPLSEDTDFDGQKSPLETPAPRRFAPVPVSRDGKITKRESPTEEKENMEMNSPKGNVRLLEQVLNSNECLTRKTESSDITSLTQPKMGWNLEKRDSTETLHSQIFPSSEERGTAQVPVPKYNDVVHDLGQKKQASDMLQIKQSPVTLRLSDHPHNPALLQTTNTRSVLKDAAKILRGVQNNKKVLEENLEAIVRAKDGAAMYSFINALATNREMSEKIRIRKQVDEWIKIISAEIQDELMRKDYEQKRFDPKNQRNKKALTMSRDIKANNQEKTVNRSVIPRSHYQKQTQEQFTSPPVRNLPASGPQKERSGLLKSATTLQDEDYMLQIYGKPVYQGHRSTLKKGPYLRFSSPSPKAKPQRPRVIELVKGTKVKSAKTQTDFHAASRMKMDSKIQHPITALPHADQQYMVSPSREMPTVSGTLEGHLIPMAILLGQTQSNSDSMPPAGVTVNKPRPVTVTTSIPPASRKGNAGVKKPNVAIVEMKSEKKDPPQLSVQILPSVDIDSVSYSSTDGASSPPSPKEASLPPLHTWIQTPDFMKVDEEEVPLPGTNFDEVIDVIQEEEKRDEIPECSAPMLEFNRSVKVVPTKYNGPSFPPVVSAYHPTTDILDKVIERKETLENSLIQWVEQEIMSRIISGLFPLQQQARLDASVSVSEASEPSASDIVAGTSSGALQRMVDARVPVNSDMVSHFVNEALTETIAVMLADREAERQRAAATSVPGDLSGTETNLLARVCAPVATPQPTPPCSPSPVREHVRVKTPDSSPCESDPDAASSIKEIRVEKGSDMPAVMLVSTPTRTPVATPPPAAALTPTLSETSIDKLKLSSPELPKPWDSGDLPLDEENPNSLQELPHPRAVVMSVANEEPESVDFSAQPAPPEPAPSAPLPEGTKAPSLQRVPSSGSSTLENTLSTVTETETLDRHISEGEILFSCGQNLATKRPGDLFLMNINDSLSSTLQDALEMEDDPPSEGQVIRRPHKKRHEDAIVALLTKQQRELLVSQQEEDLDNSVGELSEGQRLVLKAAEDISAGPSGQMLPPTSPAEPSYQHADPRLVLQQSDMASGNICEDLCASHGPMSLRELELQPDSNLILPITHTTTAVSDGNLPEAAEDFSQYQQKQDSDIKQVEHKPIQRHLTSVRNKPDSTLSQHQGGPADLLLIAHVSPARMSVTLPSANLEDCSQSLSTSSMHGGTESSGTDTF
Protein: Sp1-like factor for pairing sensitive-silencing, isoform B (A0A0B4KHC8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MTOR-associated protein MEAK7
- SD07518p
Sequence:
MLQYKSAASAATSAPPATPLAAGGSSKATIPPNGASAAASQTQVHGAPGTPTMQQIINIHQMPPQFAGGAVAGNGQNAGMPQNMFQIVQPMPMQTVNIDGQEAIFIPNLNAQLATAQAVNFNGQQAFITPNGQILRAPQMAANPAASNCIQLQQLNGLGQEQTQLITIPGTNIQIPVTNLIQQQQQAQQVHQGTVQQQAQGTNASGANGSGVTNSGTAGQLPGSITIPGTNLQIPTSVAAANGLLGNISNISNLLGGGQSIKLENGQLQMRPQLVQFPAPAMPQQQQTVAVQIPVQTANGQTIYQTVHVPVQAAATSSGGLQNLMQAQSLQMPSASQMQIIPQFSQIAQIVTPNGQIQQVQLAMPYPQLPPNANIIHIQNPHQQQQQQVQQQQQQQQAQQQQQAQQQQAQQQQQQQVQAQHQQLLQAISDASAGGQLPPNQPITITNAQGQQLTVIPAQLRPNAPTAPTPAPAGVPTPMQMPNLQALPIQNIPGLGQVQIIHANQLPPNLPANFQQVLTQLPMSHPQVQTQGQVQVMPKQEPQSPTQMITSIKQEPPDTFGPISATGNPPAPASTPNTASPQQQQIKFLHTESNSLSSLSIPASIQITALPQQATNTPNTPATTQPIPVSLPARSKVNAVTTSSTQITIAPTGGQVVSVTTQARGATASIRSTNTSTTTITTPSQSHLNMNISVASVGGAATGGGGGTATGEPKPRLKRVACTCPNCTDGEKHSDKKRQHICHITGCHKVYGKTSHLRAHLRWHTGERPFVCSWAFCGKRFTRSDELQRHRRTHTGEKRFQCQECNKKFMRSDHLSKHIKTHFKSRSGVELIELSIKQETKGGNAPKSISTVNGIVTIEIPGGGSAAAGSGASSVAATVAGSTVTPGGATIVQLPTVEASGGGDSFGDDEDDEEDDELTEEDDEDEELDEDDMDDCEDEEDDEDPELDSGDEVKMTIAVSEPGDNSSNXHSESLFMEQFLFDHFP
Protein: Fibroblast growth factor 7 (FGF-7) (Heparin-binding growth factor 7) (HBGF-7) (Keratinocyte growth factor) (KGF) (P36363)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Pro-epidermal growth factor
- Klotho
- Fibroblast growth factor receptor 3
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Fibroblast growth factor-binding protein 1
- Vascular endothelial growth factor receptor 2
- Decorin
Sequence:
MRKWILTRILPTLLYRSCFHLVCLVGTISLACNDMSPEQTATSVNCSSPERHTRSYDYMEGGDIRVRRLFCRTQWYLRIDKRGKVKGTQEMKNSYNIMEIRTVAVGIVAIKGVESEYYLAMNKEGKLYAKKECNEDCNFKELILENHYNTYASAKWTHSGGEMFVALNQKGIPVKGKKTKKEQKTAHFLPMAIT
Protein: NADPH:adrenodoxin oxidoreductase, mitochondrial (Adrenodoxin reductase) (EC 1.18.1.6) (Mitochondrial ferredoxin reductase) (AtMFDR) (Q8W3L1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Associates in vitro with the adrenodoxin-like protein MFDX1 to form an efficient low potential electron transfer chain that is able to reduce cytochrome C. Functions as accessory mitochondrial protein involved with BIO2 in the plant biotin synthase reaction.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:13677469}.
Interaction partners:
- Adrenodoxin-like protein 1, mitochondrial
- Adrenodoxin-like protein 2, mitochondrial
- Ferredoxin-dependent glutamate synthase 2, chloroplastic
- Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial
- Glutamate synthase 1, chloroplastic
- 2Fe-2S ferredoxin-like superfamily protein
- Electron transfer flavoprotein subunit beta, mitochondrial
- Ferredoxin-3, chloroplastic
- Ferredoxin-2, chloroplastic
- AT4g30750/T10C21_100
Sequence:
MSRYLARYMVSRYFSSASSRPLHVCIVGSGPAGFYTADKVLKAHEGAHVDIIDRLPTPFGLVRSGVAPDHPETKIAINQFSRVAQHERCSFIGNVKLGSDLSLSELRDLYHVVVLAYGAESDKDLGIPGESLSGIYSAREFVWWYNGHPDYSSLKPDLKTSDSAVILGQGNVALDVARILLRPTTELASTDIATHALSALKESSIRKVYLIGRRGPVQAALTAKELREVLGIKNLHIRIKQTDLSVTPADEEEMKTSRARKRIYELLSKAAAAAKTSEADPDQRELHFVFFRQPDQFLESDERKGHVSGVNLQKTILESVGTGKQIAVGTGEFEDLNCSMVLKAIGYKSVPVNGLPFDHKKGVVPNVKGRVVSHTSGDISQTEPGLYVCGWLKRGPVGIIATNLYCAEETVGSISEDIEEGVWKSSKAGSKGLMQLLEKRKVKKVEFSGWEKIDAKEKQMGIERNKPREKLVTWEDLLAAAAN
Protein: MADS-box protein AGL74.2 (Q645J1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQSSNVTDCTMRKRGTKRKIEIEKRMTKQQRSVACSKRRPTLFSKAADLCLLSGANIAVFVTSPDENSDVVYSFSGYSHASEIVDCYLNNKSPPKTTINPESAKFWWEEPDLYRDCDDLSELRIIEDRLMRTKKHLMDYLEKKEKSHSVSKSDQNPNNDTSHHLINLVTW
Protein: TNF-receptor-associated factor 4, isoform E (A8DYU9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPAPPATVKPATGHTTKLNNGKSSNSNSNHTLSNSIAHLSDSRTNLTVNTPTTCQRLSEMFRRSIASSTQSSSRENTYEEIYPGPDPKHIMGSLVFCIHHKQGCKWSDELRKLKGHLNACKHDATQCPNKCGAQIPRIMMTDHLQYTCTMRRTRCEFCQSEFSGAGLEEHNGSCGQEPVYCEAKCGQRILRGRMTLHKSKDCAKRLRRCAHCQREFSADTLPLHAAQCPRAPLACPQRCDAGPIPRGELEAHLRDECQSLAVSCSFKEAGCRFKGPRQMLEAHLESNAAAHLSLMVALSSRQGQQIQMLKSAVSKLSINYTGTLLWKITDWSAKMAEARGKDGLELVSPPFYTSQYGYKLQASMFLNGNGPGENTHVSVYIKVLPGEYDALLKWPFSHSITFTLFEQGAQSGQGGVAESFVPDPTWENFQRPSNEPDQLGFGFPRFISHELLHSRPFIKGDTVFLRVKVDPSKIVAV
Protein: High affinity immunoglobulin epsilon receptor subunit beta (FcERI) (Fc epsilon receptor I beta-chain) (IgE Fc receptor subunit beta) (Membrane-spanning 4-domains subfamily A member 2) (Q01362)
Organism: Homo sapiens (Human)
Function: High affinity receptor that binds to the Fc region of immunoglobulins epsilon. Aggregation of FCER1 by multivalent antigens is required for the full mast cell response, including the release of preformed mediators (such as histamine) by degranulation and de novo production of lipid mediators and cytokines. Also mediates the secretion of important lymphokines. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators responsible for the manifestations of allergy.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit alpha
- High affinity immunoglobulin epsilon receptor subunit gamma
- Tyrosine-protein kinase Lyn
- Tyrosine-protein kinase SYK
- Mast cell carboxypeptidase A
- Immunoglobulin heavy variable 4-38-2
- Tyrosine-protein kinase Fyn
- Membrane-spanning 4-domains subfamily A member 5
- Tryptase alpha/beta-1
- Histidine decarboxylase
Sequence:
MDTESNRRANLALPQEPSSVPAFEVLEISPQEVSSGRLLKSASSPPLHTWLTVLKKEQEFLGVTQILTAMICLCFGTVVCSVLDISHIEGDIFSSFKAGYPFWGAIFFSISGMLSIISERRNATYLVRGSLGANTASSIAGGTGITILIINLKKSLAYIHIHSCQKFFETKCFMASFSTEIVVMMLFLTILGLGSAVSLTICGAGEELKGNKVPEDRVYEELNIYSATYSELEDPGEMSPPIDL
Protein: Bruno 3, isoform B (Q9VU90)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVHIIELVGQPKVEFAQQVTMNRALQLKPAENESRSGCAFVKFGSQQEAQSAITNLHGSQTMPGASSSLVVKYADTEKERQIRRMQQMAGHMNLLNPFVFNQFSPYGAYAQQQQQAALMAAAATAPGSAAAYMNPMAALATQIPHGLNGTGQPPSLPSPTMPNFNMGANTPNGQPGGAAAAAAAAAAADGVFTNGIPQTAFPGHPLHLTIPPQGLPNGDAATLQHAFPGLPPFPGVAFPAVYGQFPQALPPPLAAVAPTQREDFLMFPGCSISGPEGCNLFIYHLPQEFGDAELMQMFLPFGNVISSKVFIDRATNQSKCFGFVSFDNPASAQAAIQAMNGFQIGMKRLKVQLKRPKDASRPY
Protein: Keratin, type II cytoskeletal 2 oral (Keratin-76) (K76) (Type-II keratin Kb9) (Q3UV17)
Organism: Mus musculus (Mouse)
Function: Probably contributes to terminal cornification.
Interaction partners:
Sequence:
MSRQACKKSFSCGSQGFSGHSAVVSGSSRSSCVARSGAASGGACGFRSGAGSLGSHSLYSLGGSKSISISVAAGGSRAGGFSGGRSSCGSGFGSGYGGSLGGSRGMGAGFGGPSGFGGAGGFGRPGSFGPGSCPGGIQEVTINQSLLQPLNVEIDPQIGQVKAQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQTIRSGSGPQNLEPFFESYISCLRKQLDSLLGAKGSLEGELKSMQDLVEDFKKKYEEEINRRTAAENEFVGLKKDVDGAFMNKVELQAKVDSLTDEINFLRTLYDMELSQIQSHVSDTSVVLSMDNNRCLDLDSIIAEVKAQYEDIAQKSKAEAEALYQTKLGELQTTAGRHGDDLRSTKSEIMDLNRMIQRLRAEIENVKKQNTNMQTSIAEAEQRGERALKDADTKFQDLQVALQKAKEDMARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLSGEFQNAVSISVVSNVTSTSSSGSFRGTGGSNYGGDSSGRSGGSSSSSSRGSSSRGSSGSRLGSGGSISVSQQRMGFNSGGSQTSVGSSYKSGRGGSSSVQFSQTTSSSQQRSK
Protein: EG:131F2.2 protein (O76875)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAKGPEQLHPQQQMQQQKRGRNKKPGKWSNNIIDNPNSNHGGSSQQKTCDSSSSSALSSPTSSATTSATSSPTNSPTSYPRANGNRKRIEAALEWRREQELGRQNANFLVPPLRQYEQLEFDDKTVVQQLRRHIIDNHLLRVYGFPVDSVVHEGAIEIFKCMPHMSFAAALAETAQAVTVINYHDGLTNRAEEEVANSTDSGNSSPQSLDSESGGEWSGSECESSNSSSSSAGEAALGLELKYCHFVPVERSLSKPCARCKRHFLVDELTGQYLTHEECQYHSGKYQRYYDGVSHGRWTCCNEGEESSPGCCLGDRHVWSGSVVGVNGPYYDFVRTEHRGSGEDEPAVYALDCEMSYTGRGLDVTKVSLVALNGQLVYEHFVRPVCDIIDYNTQYSGITETDLCSGAKSLAEVQRDLLQLITADTILIGHGLENDLRALRLVHNTLIDTSISFPHCNGFPYRRALRHLTKVHLKRDIQAGDGTTGHSSFEDSRACMELMLWRVNRELDPAWSWDD
Protein: Coatomer subunit delta (Archain) (Delta-coat protein) (Delta-COP) (P48444)
Organism: Homo sapiens (Human)
Function: Component of the coatomer, a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit zeta-1
- Coatomer subunit gamma-1
- Coatomer subunit beta
- Coatomer subunit epsilon
- Coatomer subunit beta'
- Coatomer subunit alpha
- Coatomer subunit gamma-2
- Coatomer subunit zeta-2
- N-terminal kinase-like protein
- Transmembrane emp24 domain-containing protein 10
Sequence:
MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSSMGKRTSEATKMHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIAGQPNDFFPVQVSFVSKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKYEIL
Protein: Mitochondrial inner membrane signal peptidase, putative (Q38BE2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- Protein artemis
- WD repeat protein mio zinc-ribbon like domain-containing protein
- Uncharacterized protein
- Vacuolar membrane-associated protein Iml1 N-terminal domain-containing protein
- Signal peptidase complex subunit 3
- KU70 protein
- DNA ligase, putative
- DNA ligase, putative
- KU80 protein
- Uncharacterized protein
Sequence:
MVMRWGFFSVNRNLPCIFLGAFIGYNVDVCCSVKGRSMYPTLIPGDYVLFIPSFVHLLARELTKMQLVREGDIVVMQISPELRVCKRVVRTTSDASVVQYWNNLQFTVPALVLGGEPSENSGGEEETGAHSDNSSRSHEWDTCLERAGNKSALWLWLEGDNPLESFDSRHTGAMPVECLRGRVLLKIWPSLTRLPSTAPKGGAGEGP
Protein: Lovastatin nonaketide synthase, enoyl reductase component lovC (EC 2.3.1.161) (Lovastatin biosynthesis cluster protein C) (Trans-enoyl reductase lovC) (Q0C8M1)
Organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Interaction partners:
- Lovastatin nonaketide synthase, polyketide synthase component
Sequence:
MGDQPFIPPPQQTALTVNDHDEVTVWNAAPCPILPRDQVYVRVEAVAINPSDTKMRGQFATPWAFLGTDYAGTVVAVGSDVTHIQVGDRVYGAQNEMCPRTPDQGAFSQYTVTRGRVWAKIPKGLSFEQAAALPAGISTAGLAMKLLGLPLPSPSADQPPAHSKPVYVLVYGGSTATATVTMQMLRLSGYIPIATCSPHNFDLAKSRGAEEVFDYRAPNLAQTIRTYTKNNLRYSLDCITNVESTTFCFAAIGRAGGHYVSLNPFPEHAATRKMVTTDWTLGPTIFGEGSTWPAPYGRPGSEEERQFGEDLWRIAGQLVEDGRLAHHPLRVVQGGFDQIKQGMELVRKGELSGEKLVVRLEGP
Protein: 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (EC 1.17.7.3) (1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase) (P9WKG3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Interaction partners:
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 1-deoxy-D-xylulose-5-phosphate synthase
- GCN5-related N-acetyltransferase
- Zinc metalloprotease Rip1
Sequence:
MTVGLGMPQPPAPTLAPRRATRQLMVGNVGVGSDHPVSVQSMCTTKTHDVNSTLQQIAELTAAGCDIVRVACPRQEDADALAEIARHSQIPVVADIHFQPRYIFAAIDAGCAAVRVNPGNIKEFDGRVGEVAKAAGAAGIPIRIGVNAGSLDKRFMEKYGKATPEALVESALWEASLFEEHGFGDIKISVKHNDPVVMVAAYELLAARCDYPLHLGVTEAGPAFQGTIKSAVAFGALLSRGIGDTIRVSLSAPPVEEVKVGNQVLESLNLRPRSLEIVSCPSCGRAQVDVYTLANEVTAGLDGLDVPLRVAVMGCVVNGPGEAREADLGVASGNGKGQIFVRGEVIKTVPEAQIVETLIEEAMRLAAEMGEQDPGATPSGSPIVTVS
Protein: Dikar, isoform B (Dikar, isoform E) (LD29048p) (Q9VRY3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSTFIGLLDIQSWWEIPCISHFCSLFSSAFDLPDIDIEDLESALLSDGTSDEDQVALVPELIVRLLKGCDALQTVAKEITHSNYQMFLRRFLRQQCRLHQTENHFDTDIDFQSLPVRKRLHILHDLCHFRLDSVDVQVILSNLEADSLRVEPLGYDAKNSGYWYFYGTRLYREDKATGGSASSSSGSGSGGAGASTGGASNSKGIGSNGTVWQVICFTEEDWQNLAAKFKTSTNAKERELFNILDDNFLPKLPQLFRERERLRRRKLLQVRNSSRIRNIAELKARQEEERQRRERENLYQDRQNAHWLAPPQQQQQQQQQQQQQQQQSQQRTRRRLARQCS
Protein: Serine/threonine-protein kinase SIK1 (EC 2.7.11.1) (HRT-20) (Myocardial SNF1-like kinase) (Salt-inducible kinase 1) (SIK-1) (Serine/threonine-protein kinase SNF1-like kinase 1) (Serine/threonine-protein kinase SNF1LK) (Q60670)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1 and CRTC2/TORC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1.
Subcellular location: Cytoplasm. Nucleus. Note=Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ.
Interaction partners:
- CREB-regulated transcription coactivator 2
- CREB-regulated transcription coactivator 3
Sequence:
MVIMSEFSAVPSGTGQGQQKPLRVGFYDVERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPNIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARQKFWQILSAVEYCHNHHIVHRDLKTENLLLDSNMDIKLADFGFGNFYKPGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDVWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCETLIRRMLVVDPAKRITIAQIRQHRWMQADPTLLQQDDPAFDMQGYTSNLGDYNEQVLGIMQALGIDRQRTIESLQNSSYNHFAAIYYLLLERLKEHRSAQPSSRPTPAPTRQPQLRSSDLSSLEVPQEILPCDPFRPSLLCPQPQALAQSVLQAEIDCDLHSSLQPLLFPLDTNCSGVFRHRSISPSSLLDTAISEEARQGPSLEEEQEVQEPLPGSTGRRHTLAEVSTHFSPLNPPCIIVSSSATASPSEGTSSDSCLPFSASEGPAGLGSGLATPGLLGTSSPVRLASPFLGSQSATPVLQTQAGLGTAVLPPVSFQEGRRASDTSLTQGLKAFRQQLRKNARTKGFLGLNKIKGLARQVCQSSVRTPRGGMSTFHTPAPSSGLQGCTTSNREGRSLLEEVLHQQRLLQLQHHSSTAAASSGCQQGPQLSPVPYVLAPCDSLLVSGIPLLPTPLLQAGMSPVASAAHLLDTHLHISAGPVALPTGPLPQCLTRLSPGCDPAGLPQGDCEMEDLTSGQRGTFVLVQ
Protein: E3 ubiquitin-protein transferase MAEA (EC 2.3.2.27) (Macrophage erythroblast attacher) (E7ESC7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
Interaction partners:
Sequence:
MAVQESAAQLSMTLKVQEYPTLKVPYETLNKRFRAAQKNIDRETSHVTMVVAELEKTLSGCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAASVWKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKGRQNKHEAKTGRKSRAASSSPKESLDLGMETLKGKPELSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQAMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIKTPQCYKEDGSSKSPDCPVCSRSLNKLAQPLPMAHCANSRLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQDDKVVCPRTKEVFHFSQAEKVYIM