wanglab/gogpt-training-data huggingface dataset:
Protein: S-type anion channel SLAH1 (SLAC1-homolog protein 1) (Q5E930)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Slow, weak voltage-dependent S-type anion efflux channel involved in maintenance of anion homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18305482}; Multi-pass membrane protein {ECO:0000269|PubMed:18305482}.
Interaction partners:
- Protein NRT1/ PTR FAMILY 2.4
- Protein NRT1/ PTR FAMILY 2.5
- Calcium-dependent protein kinase 21
- Chloride channel protein CLC-e
- Aluminum-activated malate transporter 9
- Chloride channel protein CLC-c
- S-type anion channel SLAH3
- Aluminum-activated malate transporter 12
- Putative chloride channel-like protein CLC-g
- Potassium channel GORK channel)
Sequence:
MEIPRQEIHIEIDNSIPSSKEFKTGLADAKPVVLMSALRSLHAGYFRISLSLCSQALLWKIMIAPESPSMSHMHSKLPSMAFHLLWYLALVTQVSLCFLYALKCIFFFDKVKEEFLHYIGVNYLYAPSISWLLMLQSAPMMEPNSVLYQTLFWIFAVPVLTLDIKLYGQWFTTEKRFLSMLANPASQVSVIANLVAARGAAEMGWNECALCMFSLGMVHYLVIFVTLYQRLPGGNNFPAKLRPIFFLFVAAPAMASLAWNSICGTFDAVAKMLFFLSLFIFMSLVCRPNLFKKSMKRFNVAWWAYSFPLTFLALDSVQYAQEVKDPVGSGLMLIFSSISVLIFLGMMVLTAANSNRLLRHDPVLGSATDPKDKQKTLSLNATNQN
Protein: Transmembrane protein 45B (Q96B21)
Organism: Homo sapiens (Human)
Function: Plays a role in innate immunity. Mechanistically, promotes alphaviruses RNA degradation by interacting with the viral polymerase nsP4 and the mRNA-capping enzyme nsP1 and thereby interfering with the interaction between viral RNA and nsP1..
Subcellular location: Endosome membrane {ECO:0000269|PubMed:35938871}; Multi-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:35938871}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:35938871}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MANFKGHALPGSFFLIIGLCWSVKYPLKYFSHTRKNSPLHYYQRLEIVEAAIRTLFSVTGILAEQFVPDGPHLHLYHENHWIKLMNWQHSTMYLFFAVSGIVDMLTYLVSHVPLGVDRLVMAVAVFMEGFLFYYHVHNRPPLDQHIHSLLLYALFGGCVSISLEVIFRDHIVLELFRTSLIILQGTWFWQIGFVLFPPFGTPEWDQKDDANLMFITMCFCWHYLAALSIVAVNYSLVYCLLTRMKRHGRGEIIGIQKLNSDDTYQTALLSGSDEE
Protein: V-type proton ATPase subunit a (Q9JL12)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGSMFRSEEVALVQLLLPTGSAYNCVSQLGELGLVEFRDLNESVSAFQRRFVVDVRRCEELEKTFTFLWEEVQRAGLTLAPPEGTLPAPPPRDLLRIQEETDRLAQELRDVRGNQQALRAQLHQLRLHSAVLGQSHSPPVAADHTEGPFSETTPLLPGTRGPHSDLKVNFVAGAVEPYKAAALERLLWRACRGFLIASFRETEGQLEDPVTGEPATWMTFVISYWGEQIGQKIRKITDCFHCHVFPYLEQEEARFRTLQQLQQQSQELQEVLGETDRFLSQVLGRVQQLLPPWQVQIHKMKAVYLTLNQCSVNTTHKCLIAEVWCAARDLPTVQQALQSGSSEEGVSAVAHRIPCQDMPPTLIRTNRFTSSFQGIVDAYGVGRYREVNPAPYTIITFPFLFAVMFGDVGHGLLMFLFALAMVLTENRPAVKAAQNEIWQTFFGGRYLLLLMGLFSVYTGFIYNECFSRATTIFPSGWSVAAMANQSGWSDEYLSQHSMLTLNPNITGVFLGPYPFGIDPIWSLATNHLSFLNSFKMKMSVILGVTHMAFGVFLSIFNHVHFGQSHRLLLETLPELIFLLGLFGYLVFLIVYKWVNVSAASASSAPSILIHFINMFLFSQNPTNHLLFHGQEVVQYVLVVLALATVPILLLGTPLYLLRQHRHRRNTQRRPAGQQDEDTDKLLASPDASTLENSWSPDEEKAGSPGDEETEFVPSEIFMHQAIHTIEFCLGCISNTASYLRLWALSLAHAQLSEVLWAMVMRIGLGMGREIGVAAVVLVPVFAAFAVLTVAILLVMEGLSAFLHALRLHWVEFQNKFYSGTGYKLSPFTFTVDSD
Protein: Myotubularin (EC 3.1.3.95) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Phosphatidylinositol-3-phosphate phosphatase) (Q9Z2C5)
Organism: Mus musculus (Mouse)
Function: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology (By similarity). Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis. In skeletal muscles, stabilizes MTMR12 protein levels.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12118066}. Cell membrane {ECO:0000250|UniProtKB:Q13496}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13496}. Cell projection, filopodium {ECO:0000269|PubMed:12118066}. Cell projection, ruffle {ECO:0000269|PubMed:12118066}. Late endosome {ECO:0000250|UniProtKB:Q13496}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:23818870}. Note=Localizes as a dense cytoplasmic network. Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles. Predominantly located in the cytoplasm following interaction with MTMR12. Recruited to the late endosome following EGF stimulation (By similarity). In skeletal muscles, co-localizes with MTMR12 in the sarcomere (PubMed:23818870). {ECO:0000250|UniProtKB:Q13496, ECO:0000269|PubMed:23818870}.
Interaction partners:
- Polyphosphoinositide phosphatase
- Phosphatidylinositol-3-phosphatase SAC1
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Myotubularin-related protein 12
- Inositol polyphosphate-4-phosphatase type I A
- Type II inositol 3,4-bisphosphate 4-phosphatase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
Sequence:
MASASASKYNSHSLENESIKKVSQDGVSQDVSETVPRLPGELLITEKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGVISRIEKMGGATSRGENSYGLDITCKDLRNLRFALKQEGHSRRDMFEILVKHAFPLAHNLPLFAFVNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRISFINKCYELCETYPALLVVPYRTSDDDLRRIATFRSRNRLPVLSWIHPENKMVIMRCSQPLVGMSGKRNKDDEKYLDVIRETNKQTSKLMIYDARPSVNAVANKATGGGYESDDAYQNSELSFLDIHNIHVMRESLKKVKDIVYPNIEESHWLSSLESTHWLEHIKLVLTGAIQVADQVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRTIEGFEILVQKEWISFGHKFASRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEGFLITVLDHLYSCRFGTFLFNCDSARERQKLTERTVSLWSLINSNKDKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRVKQQQPNPVEQRYMELLALRDDYIKRLEELQLANSAKLADAPASTSSSSQMVPHVQTHF
Protein: Claspin (O17838)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein timeless homolog
- Protein TIPIN homolog
- Serine/threonine-protein kinase chk-1
- DNA replication complex GINS protein PSF3
- Minichromosome loss protein Mcl1 middle region domain-containing protein
- Probable ubiquitin carboxyl-terminal hydrolase K02C4.3
- DNA replication licensing factor MCM2
- BRCT domain-containing protein
- Cell cycle checkpoint protein hpr-9
- protein-serine/threonine phosphatase
Sequence:
MNSDSCSTKTVSADDTDSPSSLVAEHTMSDSQEQLISSENTEVDKQAEEDRKLRRLNRRKALALERSPLPVPKLGRVLLSANSTIDLTNEDDDPSNKWFKKTFNAEKIPKLAKSPEEAKLFAVPRKISKNAPKSLLTSETLKKKLQASMSAKRRKEQEQRRKMYEEDNEHLKAGSDEEEEEDVVFKKKKGKKPVNEEEYKSEDDEDYEPENSGEEDSDEKNNGRADDEMSVNLLNDSFTYDVFNNVKRSGPGSTVSNFDSRSEADVVEKNGVVQLPTMTEITGGSNDILNLCPGSFGVSQSAGFPDTLQMLIEEDTTERKINLPQNSTSVSSDKPRLEESESEDEDDVGVKRRLPAVKNHRVLDSDEEDDVIEETLPSQDVFGSGTLEDSETIKEICEKSGEFTEKIETVLEEKTELKRVVLSDGEDSDEEAEEAEEEGDDEEEPEEDDIESENDEAETEGVEAPDPNFDDEDDELAILKRLQHQEYKQKIKKRTLFDDEASLSGDDVGSDLEDEEGMENVYEAEEGDADDVPDNDTIRRQNHKLLLKQENDKEQRELAKLQDRLLADGDLGGVETNRQFRFKLREEVQIQMGDDVDGNDGDGEDDEPEEDEQKKKERAEMIKFKYEHAEELMLLDEPKQGDDMFARAGKLFKKTEKTVIEFSEETMFKPRLSKPSLLSKTTLAVTFQEVLNGPGGAAKQMYVQSFEKPTPLSTGHISSPSSRLSTGKRLLKSPESSASAKRVRSSKLSSLE
Protein: Alpha-amylase (EC 3.2.1.1) (Q7SYK9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKLLVVAALVGLCLSQHNTNFKHNRTSIVHLFEWRWADIAKECERYLAPNGYGGVQISPPSESIVLTKPWHPWWQRYQPISYNLCSRSGTEEELKDMIARCNNVGVNIYADAVINHMCGASGGEGTHSSCGTYFNAKNEDFPSVPYSSWDFNDNKCKTANEDIENYSDIFQVRDCRLVSLLDLALEKDYVRGKVAEYMNKLIDIGVAGFRVDACKHMWPGDLSNVYSRLKTLNNTWFSPGTKPFIYQEVIDLGGEPIKASEYVSLGRVTEFKYSAKLGTVIRKWEKEKLCYLKNWGEGWGFMPSDKALVFVDNHDNQRGHGAGGASVLTFWDSRLYKIATGLMLAHPYGVTAVMSSYRWDRHFVNGKDQNDWMGPPSNADGSTKSVPINPDSTCGDNWICEHRWRQIRNMVNFRNVVNGQPLSNWWDNNNNQIAFSRGSKGFIVINNNDWDLNVMLKTGLPSGTYCDIISGDKSGNSCTGKQVTVDSDGQATFSICHTEEDPFMAIHADSKL
Protein: Translation initiation factor IF-2 (P9WKK1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ribosome-binding factor A
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL16
Sequence:
MAAGKARVHELAKELGVTSKEVLARLSEQGEFVKSASSTVEAPVARRLRESFGGSKPAPAKGTAKSPGKGPDKSLDKALDAAIDMAAGNGKATAAPAKAADSGGAAIVSPTTPAAPEPPTAVPPSPQAPHPGMAPGARPGPVPKPGIRTPRVGNNPFSSAQPADRPIPRPPAPRPGTARPGVPRPGASPGSMPPRPGGAVGGARPPRPGAPRPGGRPGAPGAGRSDAGGGNYRGGGVGAAPGTGFRGRPGGGGGGRPGQRGGAAGAFGRPGGAPRRGRKSKRQKRQEYDSMQAPVVGGVRLPHGNGETIRLARGASLSDFADKIDANPAALVQALFNLGEMVTATQSVGDETLELLGSEMNYNVQVVSPEDEDRELLESFDLSYGEDEGGEEDLQVRPPVVTVMGHVDHGKTRLLDTIRKANVREAEAGGITQHIGAYQVAVDLDGSQRLITFIDTPGHEAFTAMRARGAKATDIAILVVAADDGVMPQTVEAINHAQAADVPIVVAVNKIDKEGADPAKIRGQLTEYGLVPEEFGGDTMFVDISAKQGTNIEALEEAVLLTADAALDLRANPDMEAQGVAIEAHLDRGRGPVATVLVQRGTLRVGDSVVAGDAYGRVRRMVDEHGEDVEVALPSRPVQVIGFTSVPGAGDNFLVVDEDRIARQIADRRSARKRNALAARSRKRISLEDLDSALKETSQLNLILKGDNAGTVEALEEALMGIQVDDEVVLRVIDRGVGGITETNVNLASASDAVIIGFNVRAEGKATELASREGVEIRYYSVIYQAIDEIEQALRGLLKPIYEENQLGRAEIRALFRSSKVGLIAGCLVTSGVMRRNAKARLLRDNIVVAENLSIASLRREKDDVTEVRDGFECGLTLGYADIKEGDVIESYELVQKERA
Protein: Zinc finger FYVE domain-containing protein (A2A8R0)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR037289}. Early endosome membrane {ECO:0000256|PIRNR:PIRNR037289}.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Zinc finger FYVE domain-containing protein 16
- Tyrosine-protein phosphatase non-receptor type 23
- Mothers against decapentaplegic homolog 4
- TGF-beta receptor type-2
Sequence:
MENYFQAEAYNLDKVLDEFEQNEDETVSPTLLDTKWNKILDPSSHPLSFNPALASVNEPTVSETGPQLKVFSLAGSAPLTKEDKDPCANGQDCSLNPETDTMWIDENAVTEDQLIKRNYNQDDQFSAVEVGEEKCGSLTCLPDEKNVLVVAVMHNCDKRTLQSDLQDCNNYNSQSLMNSFSCSLDNETRQTDQFSFSMNGSTEKGINSEKQMDALNKPKPERDSVNHLCAASSNSATSISSPSQLKDGENVGRDPSTSTVTSLAVNSSQGMDGGPAIKQQGNYMPDEDLSGMNSSSRTDLGISNSFSHSSGELLIKTEPAEERTAEDSLPSDLSLNLKPDTPALSGRDNCEQSSDCLGSSETRADEDEGNDSQMTNWKLTKLNEMSDSQVNEENQMALQSNQPEDTNSGGECVGMADSDLDFKGTCMNESEGYDFSTVNDAPAANSLSNSCDSYGMQSPIVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNENAEGSGLLLNSTGNVMKKNYLHNFCSQIPSVLGQSSPKIANLQSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDLPANNGNNSKNKNDVLGKAKLGENSAVNACSATLGNISVTDTNGEHLETYEAEISSRPCLALAPDSPDNDLRASQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGTEVPQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVATSPLPTEADTSLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVGSLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLLLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEDPQEQIHIQWVDDDKTVNKGVVSPIDGKSMESITNVKIFHGSEYKANGKVIRWTEVFFLENDDHHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIA
Protein: Varicose, isoform E (M9PDB2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVRWSARSRRQARQDKVELLARNNKVNGEDDTSDNAAFRNSTDLSDHDEIFLKGLLRSNSNTPHKELMLNPTEPQPVPLFLPAHLNNKPICDDIIRKFSPSRRLESRELAKLLAQPHFRALLRAHDEIGALYEQRLKAAGGSTSQLEIASQRQTGGYLFTEDVLNTKMPVETIKMVGLRRDPSKPLGLTVELDEFKQLVVARILAGGVIDKQSMLHVGDVILEVNGTPVRTPDELQVEVSRAKENLTLKIGPNVDEEIKSGRYTVSGGQVKQNGIASLETGKKLTCYMRALFTYNPSEDSLLPCRDIGLPFKSGDILQIINVKDPNWWQAKNITAESDKIGLIPSQELEERRKAFVAPEADYVHKIGICGTRISKRKRKTMYRSVANCEFDKAELLLYEEVTRMPPFRRKTLVLIGVSGVGRRTLKNRLINSDVDKFGAVIPHTSRPKRALEENGSSYWFMDREEMEEAVRNNEFLEYGEHNGNLYGTHLQSIKDVINSGRMCILDCAPNALKILHNSQELMPFVIFVAAPGMEQLKTIYADRRATGSNRNLSDDDLVATVEESSFVQRKYEKYFDMVIVNEDFDETFRQVVETLDQMSHEEQWVPVNWIY
Protein: Peroxisome assembly protein 12 (Peroxin-12) (Q04370)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10. When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:11370741, ECO:0000269|PubMed:35768507}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisomal membrane protein import receptor PEX19
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX17
- Peroxisomal targeting signal receptor
- Peroxisome biogenesis factor 10
- Peroxisomal biogenesis factor 2
- Peroxisomal biogenesis factor 8
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PMP27
- Ubiquitin-conjugating enzyme E2-21 kDa
Sequence:
MSFYSNLPSAGQSSRGSSTSGRNGVGLEPLYPTIFEIMSSQEIDSLLPASIRYLLANHLVANFPNRYTLRLNKYFFEWFQAIKGFVEWYHLKTYNSTFIDRFYGLQLFSSRDRNLALTQCLNPKGQSEWPQGLQLNQQQKSVIFLEKIILPYITAKLDEILEKISMNNIFSSDETENKWPKRAFLRIYPFIKKLLALSNLLVKLLFLTKRTGSVSLLQYLFKIEYTTVRPLSSELSGLKETKGMDNRLRKTNISSIFALMQGQLSIIPRFLTFMGSQFFPTFIFVLRVYQWWTTQDMTTKLQKRVNDLDEDIPRPPFSSHSDKTEDKEGVSEACPVCEKTVQNPCVLETGYVACYPCAISYLVNNEGHCPVTNKKLLGCTYNKHTNKWEVVTGIRKLLI
Protein: Uncharacterized protein (Q584W5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPVRQKYPPVGCNMNDTGYPFRGDYKLQPALNHGHAGAIRKENTTLMLRITGSNLAIEKLQPSKGQKLQCELSIDDGIPKSINFPSGCGVVPVPADGHEYNLTAIVHGAGVKHYCKMSLNGTEGKGIFRLRAPSDSFAAENIRLCADGDVIYPSGGWYAIPIQAKECSLEFVGRQASRLVPTQPLFHAVAESSTVMIQCTAGTTDNAVIYCSGSGESINVVQDRPVRLSLASGPFTLLLPRTTPGAAQVRPSHVPNTPLQPPPSDSSVHRVPEVETSTIDSPEGPNTPPIFVTTADGFMIELTGDNGTSAAGYGRVQLPLPDRMTHRVQIKVSDMTGRIYLRQTAVVPSTQPPPLTFSITKDAAGAHMVKGSTLSQISVDNQPVVSGAVGASITDNARHVVTVREGSASAVFEVVAQPSAAAGPVAVRQEPQPAVPSGGTLLNSETWVNELAKALQCTDINDCRQGVQNIIPRSPEATVILGFVSQNLFKVVPTISFSREGDSVSDIQCPGHTITASINNGAPCTLSGVASIQVPSGHKVTLSALSPSTGRVVASCCAHYPPATQKNLDEHLVARLLELFQRCSLNPEAVLAELQNITQPQSAVGQQLVSYLIGCFRRLLECFQRPINLFAGDTLPNVQLLAYVDDQIPKELTVASPVTVSCANTNVRVSAREPPAAALATRGGVIHKLVEAYRENAPTELMAQLMVISPTDPDERALVDLLSRVLKDYEAKLKRERDNVISSTAADYLQFSCDGVTMENIRTSNPCQLSFEVDGTGFVALEQGGQIPQGYSFPAGSTHCVHVIARDTASGALRAEAYITLKGTKCGPSTMSAPQNEALFLDASVMVVMEEIHLRLLCPPTLSLKCEVDGGGDVVGTKSSEFMARMNASSMHNVNVHLIDEVGNVVFRQRLAVPPIAMVQWALRLDSNSLYVDSTTASCTSFLTSSLNRCPEKELNGPLQLDCSGPQTVVLRKYTLGAVQGRTCVGEMYMMIPPFVDATHLKDLAQIYREASQLQSDELQRRLNEVRAQVPMGLMKDLITVLMENTAGAFNASIRSVGPDRGPRVHFRISGDETKLLSD
Protein: Gem-associated protein 2 (Q568J0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPRLLPVDSCDTEEYTLTEPPRNPQEYLRFVQREASLCPDVVVAQIDPKKLKKQSVNVSITGCLAAPEGFSPSFKWQQQQVSRFSEVRQSVNKHRQHWKAQFLDDNVVMPKTEDEDGWKRFCLGENVCLEIQLKEEDGVNPGLDYVKTGFPPFLSIVSKLSQSTVSAVLEYLINWFEERAFVPQLGRWLYALLACLEKPLLPEAHSLIRQLARRCSAVRANLESKDDDRLSALNLMICIVARYFEQNDLADKE
Protein: Cbp/p300-interacting transactivator 3 (cCITED3) (Q9I8K7)
Organism: Gallus gallus (Chicken)
Function: Acts as transcriptional coactivator. Enhances estrogen-dependent transactivation mediated by estrogen receptors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- CREB binding protein.
- E1A binding protein p300.
- Mannosidase endo-alpha like
- Zinc finger protein 142.
Sequence:
MAEHMMMSMSHGGTGLQSYRMGVSGLQGPPQHGQHVLRTLPAAGQMMPYGGAGMDGAMRPRPNLSGQMSHHQMQNAMMFNGPSQQQQQYMGPVGTQQLMASMHLQKLNTQYQGHPLGMSNGPMGAGAQQYRVGPSQHPGMQHMPSPALTLNVMDTDLIDEEVLTSLVLELGLDRIQELPELFLGQNEFDFISDFVSKQQPSAISC
Protein: Dihydrodipicolinate synthase/N-acetylneuraminate lyase (EC 4.3.3.7) (Q8NMD2)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- Putative N-acetylmannosamine-6-phosphate 2-epimerase
- 4-hydroxy-tetrahydrodipicolinate reductase
- Aspartate-semialdehyde dehydrogenase
- Homoserine dehydrogenase
- 4-hydroxy-tetrahydrodipicolinate synthase
- Glucosamine-6-phosphate deaminase
- Transcriptional regulators
- Transcriptional regulators
- Aspartokinase
- ABC-type transporter, periplasmic component
Sequence:
MASATFTGVIPPVMTPLHADGSVDVESLRKLVDHLINGGVDGLFALGSSGEAAFLTRAQRKLALTTIIEHTAGRVPVTAGVIETTTARVIELVEDALEAGAEGLVATAPFYTRTHDVEIEEHFRKIHAAAPELPLFAYNIPVSVHSNLNPVMLLTLAKDGVLAGTKDSSGNDGAIRSLIEARDDAGLTEQFKILTGSETTVDFAYLAGADGVVPGLGNVDPAAYAALAKLCLDGKWAEAAALQKRINHLFHIVFVGDTSHMSGSSAGLGGFKTALAHLGIIESNAMAVPHQSLSDEETARIHAIVDEFLYTA
Protein: Protein TIC 20-I, chloroplastic (Translocon at the inner envelope membrane of chloroplasts 20-I) (AtTIC20-I) (Q8GZ79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope. Seems to be specific for photosynthesis-related pre-proteins. Partially redundant with TIC20-IV, but not with TIC20-II or TIC20-V.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:11910011, ECO:0000269|PubMed:21395885, ECO:0000269|PubMed:23372012}; Multi-pass membrane protein {ECO:0000269|PubMed:11910011, ECO:0000269|PubMed:21395885}.
Interaction partners:
- Protein TIC 56, chloroplastic
- Protein TIC 100
- Protein TIC 20-II, chloroplastic
- Protein TIC 20-v, chloroplastic
- Protein TOC75-3, chloroplastic
- Protein TIC 214
- YlmG homolog protein 1-1, chloroplastic
- Translocase of chloroplast 33, chloroplastic
- YlmG homolog protein 1-2, chloroplastic
- Translocase of chloroplast 34, chloroplastic
Sequence:
MITGYSTPSAHVLMSSRAFKSSSYRAAAGQTQHYLARSSLPVVKNSWGSPPSPFNELPRVSRGVPLSYLSASSSLLLNGEQGSLSGTLPVLPVRRKTLLTPRASKDVPSSFRFPPMTKKPQWWWRTLACLPYLMPLHETWMYAETAYHLHPFLEDFEFLTYPFLGAIGRLPSWFLMAYFFVAYLGIVRRKEWPHFFRFHVVMGMLLEIALQVIGTVSKWMPLGVYWGKFGMHFWTAVAFAYLFTVLESIRCALAGMYADIPFVCDAAYIQIPYD
Protein: Spectrin repeat containing nuclear envelope protein 1 (F8WAI0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus outer membrane {ECO:0000256|ARBA:ARBA00046312}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046312}.
Interaction partners:
Sequence:
MVVAEDLSALRMAEDSCVDADLPDCNCDVTRVKKLKETLVAVQQLDKNMSSLRTWLAHIESELAKPIVYDSCNSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQKFLDDYSRFEDWLKSSERTAAFPSSSGVIYTVAKEELKKFEAFQRQVHECLTQLELINKQYRRLARENRTDSACSLKQMVHEGNQRWDNLQKRVTSILRRLKHFIGQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPLDAAIIEEELDELRRYCQEVFGRVERYHKKLIRLPLPDDEHDLSDRELELEDSAALSDLHWHDRSADSLLSPQPSSNLSLSLAQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESAMSRALPSEDEEGQDDKDFYLRGAVGLSDVMIPESPEAYVKLTENAIKNTSGDHSALESQIRQLGKALDDSRFQIQQTENIIRSKTPTGPELDTSYKGYMKLLGECSSSIDSVKRLEHKLKEEEESLPGFVNLHSTETQTAGVIDRWELLQAQALSKELRMKQNLQKWQQFNSDLNSIWAWLGDTEEELEQLQRLELSTDIQTIELQIKKLKELQKAVDHRKAIILSINLCSPEFTQADSKESRDLQDRLSQMNGRWDRVCSLLEEWRGLLQDALMQCQGFHEMSHGLLLMLENIDRRKNEIVPIDSNLDAEILQDHHKQLMQIKHELLESQLRVASLQDMSCQLLVNAEGTDCLEAKEKVHVIGNRLKLLLKEVSRHIKELEKLLDVSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKTPRGKCSLSQPGPSVSSPHSRSTKGGSDSSLSEPGPGRSGRGFLFRVLRAALPLQLLLLLLIGLACLVPMSEEDYSCALSNNFARSFHPMLRYTNGPPPL
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) (P46406)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with CHP1 to small punctate structures along the microtubules tracks. {ECO:0000250|UniProtKB:P04797}.
Interaction partners:
- Triosephosphate isomerase
- Large ribosomal subunit protein uL13
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase A
- Peroxidasin
- Peroxidasin like
- Amyloid-beta precursor protein
- Fructose-bisphosphate aldolase
- GDH/6PGL endoplasmic bifunctional protein
- Fructose-bisphosphate aldolase B
Sequence:
MVKVGVNGFGRIGRLVTRAAFNSGKVDVVAINDPFIDLHYMVYMFQYDSTHGKFHGTVKAENGKLVINGKAITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDHFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKAAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSATHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMVHMASKE
Protein: Cytosolic sulfotransferase 18 (AtSOT18) (EC 2.8.2.38) (Desulfo-glucosinolate sulfotransferase B) (Sulfotransferase 5B) (AtST5b) (Q9C9C9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of the glucosinolate core structure. Preferred substrate are the long-chain desulfo-glucosinolates, 7-methylthioheptyl and 8-methylthiooctyl, derived from methionine. Substrate preference is desulfo-benzyl glucosinolate > desulfo-4-methylthiobutyl glucosinolate > desulfo-6-methylthiohexyl glucosinolate > desulfo-3-methylthiopropyl glucosinolate > desulfo-indol-3-yl methyl glucosinolate > desulfo-singrin > desulfo-3-butenyl glucosinolate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15234990, ECO:0000269|PubMed:16367753}.
Interaction partners:
- Cytosolic sulfotransferase 17
- Cytochrome P450 83A1
- S-alkyl-thiohydroximate lyase SUR1
- Methylthioalkylmalate synthase 1, chloroplastic
- UDP-glycosyltransferase 74B1
- Transcription factor MYB28
- Dihomomethionine N-hydroxylase
- Cytosolic sulfotransferase 16
- Methylthioalkylmalate synthase 3, chloroplastic
- Methionine aminotransferase BCAT4
Sequence:
MESETLTAKATITTTTLPSHDETKTESTEFEKNQKRYQDLISTFPHEKGWRPKEPLIEYGGYWWLPSLLEGCIHAQEFFQARPSDFLVCSYPKTGTTWLKALTFAIANRSRFDDSSNPLLKRNPHEFVPYIEIDFPFFPEVDVLKDKGNTLFSTHIPYELLPDSVVKSGCKMVYIWREPKDTFISMWTFLHKERTELGPVSNLEESFDMFCRGLSGYGPYLNHILAYWKAYQENPDRILFLKYETMRADPLPYVKSLAEFMGHGFTAEEEEKGVVEKVVNLCSFETLKNLEANKGEKDREDRPGVYANSAYFRKGKVGDWSNYLTPEMAARIDGLMEEKFKGTGLLEHGK