wanglab/gogpt-training-data huggingface dataset:
Protein: Charged multivesicular body protein 7 (Chmp7) (ESCRT III complex subunit Cmp7) (Cmp7) (O94730)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase (By similarity). Plays a role in regulating nuclear envelope (NE) morphology and nuclear integrity, particularly during spindle pole body (SPB) extrusion or insertion through the NE, and perhaps during karyokinesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Vacuolar-sorting protein snf7
- Lap-Emerin-Man domain protein 2
- Vacuolar protein-sorting-associated protein 46
- ESCRT-III complex subunit did4
- Vacuolar protein sorting-associated protein 24
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar protein sorting-associated protein ist1
- Suppressor protein of bem1/bed5 double mutants
Sequence:
MGKKEKVNALEFSVNKGIFTKTRLKSLYSDFTSLFIKNPEGFLANVNTWREAIETSAWSGKLNSRIILVFDETFESAFSSPALGRPLSLGAVAAYWIQQGVWLRKQDFLNDCKKGNLVREDGFSIFSILRWSFQKLGFQNQASSILSNRSPSGQYVIRKNIEKLACLVHNEAMRRCSSYTSAIYTWDFFQDTFGSLYWEEGKLNKDEMECLLNWMCYQKHVLIFDSKIIKFLPNSQIDAQLASIDKSIDGSVADLIQARASIAQRSEFLNEELEQLSQVLNQAVKKGEKTIAITYLRRKKILSKDLERKVSSRLQLDTIISNIDNAVDNKILLIAMSSGSEALDAILAQMGGTEKVEDVLENVNDTLARSEEIDATIQTYNPQNIDLEDEAVEKEWQDLVAEEQKVEDIVSTLGNVSLKTPSDTFTLTNTDSDKKTSKPEKIQAELVEQ
Protein: GST N-terminal domain-containing protein (Q57U23)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQDSVLLSEAFDASHRPWPNRPERKKGVSPSGRDFNMTLYRMKGCPYCERVEWLLRYHLVPFEIVEVGPLTTKGFPDQRFVQVPQIGLEAVADPNNPHAAEKSVAYVADSQHIIAAISAPLGFTKQLSDPRIMETRKWMMERFQAAGFLAINSTWRDAYTTYPHVTPSHYYYQNPIFHVVGATALYALAKYKVAPRFAAEESATSGFPSMENSLQRDPSAWLAAELSGFATRLSGGCHQLHGGKEPDIADVEMYGLTRIIDAHPRLRSALHEGPLKEWCAAMEAALQKRTHVTKK
Protein: Trafficking protein particle complex subunit 4 (Synbindin) (TRS23 homolog) (Q9ES56)
Organism: Mus musculus (Mouse)
Function: Core component of the TRAPP complexes which has a function of guanine nucleotide exchange factor activity for Rab1 GTPase. Plays a role in vesicular transport from endoplasmic reticulum to Golgi and autophagy (By similarity). May play a role in dendrite postsynaptic membrane trafficking.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:11018053}. Golgi apparatus membrane {ECO:0000269|PubMed:11018053}. Endoplasmic reticulum {ECO:0000305}. Vesicle {ECO:0000269|PubMed:11018053}. Note=Associated with postsynaptic membranes and in intracellular cisterns and vesicles (Golgi). {ECO:0000269|PubMed:11018053}.
Interaction partners:
- Trafficking protein particle complex 8
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 6A
- Trafficking protein particle complex subunit 3
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 9
Sequence:
MAIFSVYVVNKAGGLIYQWDSYSPRAEAEKTFSYPLDLLLKLHDERVLVAFGQRDGIRVGHAVLAINGMDVNGKYTADGKEVLEYLGNPANYPVSIRFGRPRLTSNEKLMLASMFHSLFAIGSQLSPEQGSSGIEMLETDTFKLHCFQTLTGIKFVVLADPRQAGIDSLLRKIYEIYSDFALKNPFYSLEMPIRCELFDQNLKLALEVAEKAGTFGPGS
Protein: Enhancer of polycomb homolog 1 (Q9H2F5)
Organism: Homo sapiens (Human)
Function: Component of the NuA4 histone acetyltransferase (HAT) complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR). The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone acetylation is required for histone replacement during the transition from round to elongating spermatids (By similarity). In the NuA4 complex, EPC1 is required to recruit MBTD1 into the complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:10976108}. Cytoplasm {ECO:0000250|UniProtKB:Q8C9X6}.
Interaction partners:
- DNA methyltransferase 1-associated protein 1
- Chromatin modification-related protein MEAF6
- YEATS domain-containing protein 4
- Transformation/transcription domain-associated protein
- Histone acetyltransferase KAT5
- Mortality factor 4-like protein 1
- Inhibitor of growth protein 3
- MRG/MORF4L-binding protein
- Actin-like protein 6A
- RuvB-like 1
Sequence:
MSKLSFRARALDASKPLPVFRCEDLPDLHEYASINRAVPQMPTGMEKEEESEHHLQRAISAQQVYGEKRDNMVIPVPEAESNIAYYESIYPGEFKMPKQLIHIQPFSLDAEQPDYDLDSEDEVFVNKLKKKMDICPLQFEEMIDRLEKGSGQQPVSLQEAKLLLKEDDELIREVYEYWIKKRKNCRGPSLIPSVKQEKRDGSSTNDPYVAFRRRTEKMQTRKNRKNDEASYEKMLKLRRDLSRAVTILEMIKRREKSKRELLHLTLEIMEKRYNLGDYNGEIMSEVMAQRQPMKPTYAIPIIPITNSSQFKHQEAMDVKEFKVNKQDKADLIRPKRKYEKKPKVLPSSAAATPQQTSPAALPVFNAKDLNQYDFPSSDEEPLSQVLSGSSEAEEDNDPDGPFAFRRKAGCQYYAPHLDQTGNWPWTSPKDGGLGDVRYRYCLTTLTVPQRCIGFARRRVGRGGRVLLDRAHSDYDSVFHHLDLEMLSSPQHSPVNQFANTSETNTSDKSFSKDLSQILVNIKSCRWRHFRPRTPSLHDSDNDELSCRKLYRSINRTGTAQPGTQTCSTSTQSKSSSGSAHFAFTAEQYQQHQQQLALMQKQQLAQIQQQQANSNSSTNTSQNLASNQQKSGFRLNIQGLERTLQGFVSKTLDSASAQFAASALVTSEQLMGFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSALLQPSNITQTSSSHSALSHQVTAANSATTQVLIGNNIRLTVPSSVATVNSIAPINARHIPRTLSAVPSSALKLAAAANCQVSKVPSSSSVDSVPRENHESEKPALNNIADNTVAMEVT
Protein: Testin (A1ZAT5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Protein enabled
Sequence:
MSAVSPNSCVETPKAPEWLSKLESRREQLKRSKLGHEAGAGAPCAECKDKCPGLDLHFWRKVCRNCKCPKIQHVCPDDDDATGWAQFEILGQIRAKPAYIKIKALASQPVQLEWVPPNAAPDVVTDYMEKLGTAQIPVAGSDAALKRKMQLELQVPPHDLDAALCDGLTETEAIQLQQYVQKLREQCVGQGVVVRLGDRLNHAQVEHVAPALMPTQEAQQTWQSLGLMPVADDTLNELLANPKVAQALASPASAHPKLLVAFSEPLCESTAQFEENGALRAQTREKLLGISKPALLSLVTHGIVYDKVLGILQEKKLNISRDPKLGPIAEFRKEYVNNPQFRAEINTICPQPPMTPIKSPPGTPFNSPLPLKNPVQIRMGAQMRQDTPMRRVKFGGVSTIVYDCGLPANTDYDRDPVFAQILQAEPLKHAFQEARAGRAPSSVVISNIPAPVASLAELRGLNPATRAQLQSVGLDKNMLQSAVSNAPYYDRLFRSLHDKGISHDQCHLLQPMKQVHDWLLDDDQLLDEIDKVFADMANGCKDISYPKPSLGELPTSQSSDSGFHSKPPTPGYGSEDLTAGQGRFASIPGIEDMNMYPSCAGMPEQFQQLRLHGDEASGKNSTRTILCADCNQPIAMGEVAVKADRAGKEIAWHPGCFKCITCRELLADLVYFFHQGQVFCGRDLAIRLKIPRCRACDELIFTKEYTAAEEATFHIKHFCCYQCDEPLAGQQYIADEKSNMPLCLLCYDRLFAVRCQRCKVAIGPADQGVAWGDVHWHASCFVCAGVQCSKPLIGGRFCVKENMPFCSPTCVRSLIN
Protein: Protein ERGIC-53 (ER-Golgi intermediate compartment 53 kDa protein) (Lectin mannose-binding 1) (Q9TU32)
Organism: Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Function: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins (By similarity).
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAGSRRRGLQARVRPLFCALLLSLSRFVGGDGVGGDPAAGLPHRRFEYKYSFKGPHLVQSDGTVPFWAHAGNAIPSSDQIRVAPSLKSQRGSVWTKAKAAFENWEVEVTFRVTGRGRIGADGLAIWYTENQGLEGPVFGSADLWNGVGIFFDSFDNDGKKNNPAIVIIGNNGQIHYDHQNDGASQALASCQRDFRNKPYPVRAKIIYYQKTLTVMINNGFTPDKNDYEFCAKVENMIIPAQGHFGVSAATGGLADDHDVLSFLTFQLTEPGKEPPTPDKEISEKEKEKYQEEFEHFQQELDKKKEEFQKGHPDLQGQPAEEIFESVGDRELRQVFEGQNRIHLEIKQLNRQLDMILDEQRRYVSSLTEEISKRGAGMPGQHGQISQQELDTVVKTQHEILRQVNEMKNSMSETVRLVSGMQHPGSAGGVYETAQHFADIKEHLHTVKRDIDNLVQRHMLSNEKPKCPELPPFPSCLSTVHFIIFVVVQTVLFIGYIMYRSQQEAAAKKFF
Protein: Transcription factor BHLH089 (Basic helix-loop-helix protein 89) (OsbHLH089) (bHLH transcription factor bHLH089) (Q84T08)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor that may regulate jasmonate-regulated genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MDPAPTLAAELWRTPYLGGGGGGGGGGRGLEAAASGVTEQSNGSRGGGGGGGAGRRRQREAPALEDDSSRIVSTSGGGGGGQDLTDSEAKRFKASKSSGDNSSLRTEAETDSRNASKSGDQNPPPPEPPKQDYIHVRARRGQATDSHSLAERARREKISERMKILQDLVPGCNKVIGKASVLDEIINYIQALQRQVEFLSMKLEAVNAHVNNGIEAFPPKDFGAQVYNTAPGLTFDPQTPREYAQGSTPSEWLHMQIGGTYERVT
Protein: 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-hydroxyanthranilate oxygenase) (3-HAO) (3-hydroxyanthranilic acid dioxygenase) (HAD) (P46953)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03019}.
Interaction partners:
- Kynureninase
- Kynurenine 3-monooxygenase
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Catalase
- Tryptophan 2,3-dioxygenase
- Kynurenine formamidase
- Indoleamine 2,3-dioxygenase 1
- Indoleamine 2,3-dioxygenase 2
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
Sequence:
MERCVRVKSWVEENRASFQPPVCNKLMHREQLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGEHRDVVIRQGEIFLLPARVPHSPQRFANTMGLVIERRRMETELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRTGKPNPDQLLKEPPFPLSTRSVMEPMSLKAWLESHSRELQAGTSLSLFGDSYETQVIAHGQGSSKGPRQDVDVWLWQLEGSSKVTMGGQCVALAPDDSLLVPAGFSYMWERAQGSVALSVTQDPACKKPLG
Protein: Prolyl endopeptidase (PE) (EC 3.4.21.26) (Post-proline cleaving enzyme) (Q9QUR6)
Organism: Mus musculus (Mouse)
Function: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:37189369}.
Interaction partners:
- Thimet oligopeptidase
- Dipeptidyl peptidase 8
- Lysosomal Pro-X carboxypeptidase
- Dipeptidyl peptidase 9
- Dipeptidyl peptidase 4
- Acylamino-acid-releasing enzyme
- Prolyl endopeptidase FAP
- Neprilysin
Sequence:
MLSFQYPDVYRDETSVQEYHGHKICDPYSWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQEPNGITGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNILQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTKEELEPMVFREVTVKGIDAADYQTIQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYGCSDTKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNIEWIQ
Protein: Uncharacterized transporter C460.03 (B5BP47)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Vacuolar amino acid transporter 5
- Uncharacterized amino-acid permease C460.01c
- Putative glutathione S-transferase C460.02c
- Uncharacterized transporter C460.05
- Probable delta-1-pyrroline-5-carboxylate dehydrogenase
- Vacuolar amino acid transporter 3
- Probable L-asparaginase 3
- Putative alpha-ketoglutarate-dependent sulfonate dioxygenase
- Uncharacterized transporter PB10D8.01
Sequence:
MNVQKSNNAEETITPFSEESSLLNSNSYIPATFVDPTTIPQTSTEDIDIHGFNSIFDIPNLAWIEVSLLLNVFLAGFDGTVTASAYTTIGEEFHAANLASWITTSYLITSTTFQPLYGSFSDVLGRRVCLFMASGLFCLGCLWCYFSSGMVSLIFARSFMGIGGGGLITLSTIINSDIIPTRNRGLFQAFQNLLLGFGAICGASFGGVLSEVFSWRLCFLVQVPFSVLSIAVGFFFVKNQSGYSRFHHYCVLFKKIDILGGLLLVSGLTSLLLVLTFGSSRSIQTYRPSQLLLLLGILCIVAFVYVESITEAAPIIPLKLLKGLYSSLVLTTGFLIGLAGYAYLFTLPLFFQLVLGDSPSKAGLRLALPSLSTPIGGLICGILMHRNFRVGKLLFSGVFLMSLGYFLSLFIHPGISPIVLGIFLIPANVGQGIGFPSSLFSFIFAFPQNSHATSTSTLYLIRSIGSLFGVGGLSAVIQLTLRKKMLADLTKFTDLDSKSIQKIIHDVSKSISALYELPEAIQEIVLSDYTFSIRKAQQFTTICCVLALGLCILKDTIKPRTPSGFRY
Protein: SH2 domain-containing protein 3C (Cas/HEF1-associated signal transducer) (SH2 domain-containing Eph receptor-binding protein 1) (Q9QZS8)
Organism: Mus musculus (Mouse)
Function: Acts as an adapter protein that mediates cell signaling pathways involved in cellular functions such as cell adhesion and migration, tissue organization, and the regulation of the immune response. Plays a role in integrin-mediated cell adhesion through BCAR1-CRK-RAPGEF1 signaling and activation of the small GTPase RAP1 (By similarity). Promotes cell migration and invasion through the extracellular matrix. Required for marginal zone B-cell development and thymus-independent type 2 immune responses. Mediates migration and adhesion of B cells in the splenic marginal zone via promoting hyperphosphorylation of NEDD9/CASL. Plays a role in CXCL13-induced chemotaxis of B-cells. Plays a role in the migration of olfactory sensory neurons (OSNs) into the forebrain and the innervation of the olfactory bulb by the OSN axons during development. Required for the efficient tyrosine phosphorylation of BCAR1 in OSN axons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10692442, ECO:0000269|PubMed:17174122, ECO:0000269|PubMed:20956287}. Cell membrane {ECO:0000269|PubMed:10692442}; Peripheral membrane protein {ECO:0000269|PubMed:10692442}. Cell projection, axon {ECO:0000269|PubMed:20881139}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10692442}. Note=Associated with the membrane when EGF-stimulated (PubMed:10692442). Expressed at the cortical actin ring in B cells (PubMed:20956287). {ECO:0000269|PubMed:10692442, ECO:0000269|PubMed:20956287}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:17174122}; Peripheral membrane protein {ECO:0000269|PubMed:17174122}.
Interaction partners:
- Serine protease 57
- Breast cancer anti-estrogen resistance protein 1
- Interferon regulatory factor 3
- Ras GTPase-activating protein-binding protein 2
- Ubiquitin-like protein ISG15
- Enhancer of filamentation 1
- Ras GTPase-activating protein-binding protein 1
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Zinc finger HIT domain-containing protein 2
- Y-box-binding protein 1
Sequence:
MTEMPKKTGRKFKFFKFKGLGSLSNLPRSFSLRRSSASASIRSCPEPDTFEATQDDMVTLPKSPPAYARSSDMYSHMGTMPRPNIKKAQKQQAVQKAQEVSRESHLVSRRLPEPPDLEAAKEAGEGTEALLEDTAPSAVEVDPMRELEDLTVDTEKEQVPGDVSPERTAAELEAAGDYVKFSKEKYILDSSPEKLHKELEEELKLSSTDLRSHAWYHGRIPREVSETLVQRNGDFLIRDSLTSLGDYVLTCRWHNQALHFKINKVVVKAGESYTHIRYLFEQESFDHVPALVRYHVGSRKAVSEQSGAIIYCPVNRTFPLRYLEASYGLSQGSSKTASPASPSGSKGSHMKRRSITMTDGLTTDKVTRSDGCPNSTSLPHPRDSIRNCALSMDQIPDLHSPLSPISESPSSPAYSTVTRVHAPSATPSTSAQPASPVARRSSEPQLCPGNTPKPPGESDRAPHASPSHTLCKASPSPSLSSYSDPDSGHYCQLQPPVRGSREQAAGETPRKARGSGERQKELLENGVSDGEWGKTFTVPVVEATSSFNLATFQSQLIPKENRPLEVALLRKVKELLSEVDARTLARHVTKVDCLVARILGVTKEMQTLMGVRWGMELLTLPHGRQLRLDLLERFHTMSIMLAVDILGCTGSAEERAALLHKTIQLAAELRGTMGNMFSFAAVMGALEMAQISRLEQTWMTLRQRHTEGAILYEKKLKPFLKSLNEGKEGPPLSNTTFPHVLPFITLLECDSAPAEGPEPWGSTEHGVEVVLAHLEAARTVAHHGGLYHTNAEVKLQGFQARPELLEVFSTEFQMRLLWGSQGANSSQAWRYEKFDKVLTALSHKLEPAIRSSEL
Protein: Chromosome segregation in meiosis protein 3 (Q04659)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms a fork protection complex (FPC) with TOF1 which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors and protects stalled replication forks against the fork-releasing activity of RRM3 helicase.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Minichromosome maintenance protein 10
- DNA replication complex GINS protein PSF1
- DNA replication complex GINS protein PSF3
- DNA replication licensing factor MCM2
- DNA replication complex GINS protein SLD5
- Mediator of replication checkpoint protein 1
- Minichromosome maintenance protein 5
- Topoisomerase 1-associated factor 1
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM7
Sequence:
MDQDFDSLLLGFNDSDSVQKDPTVPNGLDGSVVDPTIADPTAITARKRRPQVKLTAEKLLSDKGLPYVLKNAHKRIRISSKKNSYDNLSNIIQFYQLWAHELFPKAKFKDFMKICQTVGKTDPVLREYRVSLFRDEMGMSFDVGTRETGQDLERQSPMVEEHVTSAEERPIVADSFAQDKRNVNNVDYDNDEDDDIYHLSYRNRRGRVLDERGNNETVLNNVVPPKEDLDALLKTFRVQGPVGLEENEKKLLLGWLDAHRKMEKGSMTEEDVQLIQSLEEWEMNDIEGQHTHYDLLPGGDEFGVDQDELDAMKEMGF
Protein: MLX-interacting protein (Transcriptional activator MondoA) (Q2VPU4)
Organism: Mus musculus (Mouse)
Function: Binds DNA as a heterodimer with MLX and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11073985}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11073985}. Mitochondrion outer membrane {ECO:0000269|PubMed:11073985}. Note=Predominantly cytoplasmic but shuttles between cytoplasm and nucleus when associated with MLX. Also associates with the outer mitochondrial membrane and may shuttle between the outer mitochondrial membrane and the nucleus. {ECO:0000250|UniProtKB:Q9HAP2, ECO:0000269|PubMed:11073985}.
Interaction partners:
- Carbohydrate-responsive element-binding protein
- Max-like protein X
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Peroxisome proliferator-activated receptor gamma coactivator 1-beta
- Serine/threonine-protein phosphatase 2A activator
- Thioredoxin-interacting protein
- Max dimerization protein 4
Sequence:
MAADVFMCSPRRPRSRGRSVLLKPQVPEDDDDSDTDEPSPPPPSGVATSARAHASAAPLPPRAGPGREEPPRRQQIIHSGHFMVSSPHREHPPKKGYDFDTVNKQTCQTYSFGKTSSCHLSIDASLTKLFECMTLAYSGKLVSPKWKNFKGLKLQWRDKIRLNNAIWRAWYMQYLEKRRNPVCHFVTPLDGSVDVDEHRRPEAITTEGKYWKSRIEIVIREYHKWRTYFKKRLQQHKDEDLSSLAQDDDMLYWHKHGDGWKTPVPMEEDSLLDTDMLMSEFSDTLFSTLSSHQPVAWPNPREIAHLGNADMIQPGLIPLQPNLDFMDTFEPFQDLFSSSRSIFGSMLPPPSSLPAADPSSPPSQGNILPNTALPPASLPNSLITSSAAPSLDPTEGQGCERTSQTVDPFIQPADFGPSEPPLSVPQPFLPVFTMTLLSPGPAPAPVPTALPLVPSPAPTLNPPTPPAFLQPQKFAGVSKSTPVITHTASATLTHDASATTFSQNQGLVITAHHPTPSSSPCALALSPVPQPPAVGPPQPHLTFIHPKPVSLTGVRHKQPPKIVPAPKPEPVSLVLKNACIAPAAFSGQPQKVIMTSAPLKREGILASTVSPSNVVIASAAITRASGVTEFLSHSTSSQPSPVSRLFSPSTVQDSLVKGEQVSLHGGSPQVPATGSSRDCPNSGQASPCPSEQSPSPQSPQNNCSGKSTDPKNVAALKNRQKHISAEQKRRFNIRMGFNTLNSLISNNSKQTSHAITLQKTMEYITKLQQERMQMQEEARRLREEIEELNTTIISCQQLLPATGVPVNCRQLDHMRDMFDEYVKSRTLQNWKFWIFSMIIKPLFESFKGMVSTSSLEEFHRTALSWLDQHCSLPVLRPMVLSTLRQLSTTTSILTDPSQLPEQASEAVTRMGKRSGES
Protein: Cis-abienol synthase, chloroplastic (NtABS) (EC 4.2.3.140) (G3CCC1)
Organism: Nicotiana tabacum (Common tobacco)
Function: Involved in the biosynthesis of cis-abienol, a labdane diterpene that can be used as synthesis precursor of ambergris substitution fragance products.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
Sequence:
MVLGLRSKIIPLPDHKLGNIKLGSVTNAICHRPCRVRCSHSTASSMEEAKERIRETFGKIELSPSSYDTAWVAMVPSRYSMNQPCFPQCLDWILENQREDGSWGLNPSHPLLVKDSLSSTLASLLALRKWRIGDNQVQRGLGFIETHGWAVDNKDQISPLGFEIIFPCMINYAEKLNLDLPLDPNLVNMMLCERELTIERALKNEFEGNMANVEYFAEGLGELCHWKEMMLRQRHNGSLFDSPATTAAALIYHQYDEKCFGYLNSILKLHDNWVPTICPTKIHSNLFLVDALQNLGVDRYFKTEVKRVLDEIYRLWLEKNEEIFSDVAHCAMAFRLLRMNNYEVSSEELEGFVDQEHFFTTSSGKLMNHVAILELHRASQVAIHERKDHILDKISTWTRNFMEQKLLDKHIPDRSKKEMEFAMRKFYGTFDRVETRRYIESYKMDSFKILKAAYRSSGINNIDLLKFSEHDFNLCQTRHKEELQQMKRWFTDCKLEQVGLSQQYLYTSYFIIAAILFEPEYADARLAYAKYAIIITAVDDFFDCFICKEELQNIIELVERWEGYSTVGFRSERVRIFFLALYKMVEEIAAKAETKQGRCVKDHLINLWIDMLKCMLVELDLWKIKSTTPSIEEYLSVACVTIGVPCFVLTSLYLLGPKLSKDVIESSEVSALCNCTAAVARLINDIHSYKREQAESSTNMVSILITQSQGTISEEEAIRQIKEMMESKRRELLGMVLQNKESQLPQVCKDLFWTTINAAYSIHTHGDGYRFPEEFKNHINDVIYKPLNQYSP
Protein: STING ER exit protein (STEEP) (Q9V412)
Organism: Drosophila melanogaster (Fruit fly)
Function: Stimulates membrane curvature formation and subsequent endoplasmic reticulum exit site (ERES) establishment by recruiting PI3K complex I, leading to COPII vesicle-mediated transport (By similarity). Promotes endoplasmic reticulum (ER) exit of cGAMP-activated STING1 oligomers (By similarity).
Interaction partners:
- DNA polymerase epsilon subunit 2
- Guanylate binding protein 128up
- Citrate transport protein
- Casein kinase II subunit alpha
- Protein Bride of doubletime
- ADP,ATP carrier protein
- ADP/ATP translocase
- AT06125p
- Probable citrate synthase, mitochondrial
- Citrate synthase
Sequence:
MPKVVSRSIVCSDTKDQEEYNEEKPLNIYYCLCNKMALILDCTLEQLPLREVDNARVINANDHANKLTHNPTPRMVYIKRKSRGNGIEKQYRYKCRSCSLPLYYRHSPDSHVTFVMSNALIRNKGESPLTQLLNSEIKGSFKAPAAKPATSAGPDDSGIVDASGKKVVVTRHTKNMGKFSSVTVSTIDEEEDEIEAREIADSYANNARIIEKQLQRKGGKLSDVGIKTKTEDAPPPQKKQRGTLLER
Protein: Uncharacterized protein C1840.08c (O74481)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ERO1-like protein 1
- Tryptophan synthase
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2
Sequence:
MELGAWRSILYIAFLFAITRHAFCKAVNLVHSPEGEEFENILSSVSATVEKKEVNNKLIMPTANRDNQGVREELLVSSFKERKLLNTNSANLRLNSIGSYEMIDFKQINSEFFLSHRQHGFVLFIDSKKKPRQSFYTDSATSIVQLSKKYRNKIKFKSVDCASSLEKCEEIGINSFPSLVYYNNAGQKKVFTAHTPYEVLSKHADLITELDETDGKVYPQSIIRLEEFKNLKANEPVFFLYLHDYGSTPEDFDSLRIFARYLVGFAPLYRTDDEKVIKTLNVTRLPHLVAIRHGVAFSYSERSVSAMRNTFQLIKWASLLKYPLVPELTPAVVENLDSDSYLAIALINPTSQVKASKAISTVQEIGLKWTLKLREVERKQLLTAREKWWDHLRMLKQKGYDDVAFLAAEYSLPLPKNKKVTFVWVNSLQWKTWISHTFHIDPMGPSRFVLMDPSRMFYWDSSAKGLPLTLDDSSLILDTTFRVLAITGEGLPHEFSIPRGYVYLSEIKQYSSLILISLWISLILFVSFLNRRLILHYSFESVHQLKTLTRKFIYSSLLKQD
Protein: Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 (E-NPP 7) (NPP-7) (EC 3.1.4.12) (Alkaline sphingomyelin phosphodiesterase) (Intestinal alkaline sphingomyelinase) (Alk-SMase) (Q5EZ72)
Organism: Rattus norvegicus (Rat)
Function: Choline-specific phosphodiesterase that hydrolyzes sphingomyelin (SM) releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15205117}; Single-pass type I membrane protein {ECO:0000269|PubMed:15205117}. Note=The catalytic domain is released into the extracellular medium when cells are treated with trypsin (PubMed:15205117). Localized at the surface of the microvillar membrane in small intestine enterocytes, and in endosome-like structures situated beneath the microvillar membrane, and in Golgi complex (By similarity). {ECO:0000250|UniProtKB:Q6UWV6, ECO:0000269|PubMed:15205117}.
Interaction partners:
- Sphingomyelin phosphodiesterase 2
- Sphingomyelin phosphodiesterase 4
- Sphingomyelin phosphodiesterase
- Sphingomyelin phosphodiesterase 3
- Ceramide kinase
- Phosphatidylcholine:ceramide cholinephosphotransferase 2
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Ceramide glucosyltransferase
- Ceramide synthase 5
- Phospholipid phosphatase 3
Sequence:
MGHSAVLLSVALVILPACVTGGPVQRQQQHKLLLVSFDGFRWNYDQDVETPNLDSMAQEGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTNKVRLPYHATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHNYKNETEWRANVDTVMKWFTEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLTDSLNLIITSDHGMTTVNKKASDLVEFHKFPNFTFRDIEFELLDYGPNGMLIPKEGMLEKVYSVLKDAHPRLHVYKKEDFPKTFHYANNPRITSLLMYSDLGYVIHGRVNVQFNSGEHGFDNQDMDMKTIFRAVGPSFKAGLEVEPFESVHVYELMCQLLGIVPEPNDGHPGVLQPMLRSGSPLSRQHHLVVVLMGILTGLAKVV