wanglab/gogpt-training-data huggingface dataset:
Protein: ATPase H(+)-transporting accessory protein 2 (Renin homolog receptor) (dPRR) [Cleaved into: ATPase H(+)-transporting accessory protein 2 N-terminal fragment; ATPase H(+)-transporting accessory protein 2 C-terminal fragment] (Q9VHG4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Multifunctional protein which functions as transmembrane receptor in the planar cell polarity (PCP) and is involved in the assembly of the proton-transporting vacuolar (V)-ATPase protein pump. As transmembrane receptor mediates fz/PCP signaling through interaction with fz and stabilizes asymmetric PCP domains through its interaction with stan. Also mediates Wnt/beta-cat signaling through interaction with fz/fz2. Probably by controlling the assembly of the V-ATPase pump and thus the acidification of the endo-lysosomal system, plays a role in many neuronal processes including synapse morphology and synaptic transmission.
Subcellular location: [ATPase H(+)-transporting accessory protein 2]: Cell membrane {ECO:0000269|PubMed:20579879, ECO:0000269|PubMed:20579883}; Single-pass type I membrane protein {ECO:0000269|PubMed:20579883}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20579883, ECO:0000269|PubMed:23292348, ECO:0000269|PubMed:29995586}; Single-pass type I membrane protein {ECO:0000269|PubMed:20579883}. Vesicle {ECO:0000269|PubMed:23292348}. Apical cell membrane {ECO:0000269|PubMed:23292348}; Single-pass type I membrane protein {ECO:0000269|PubMed:23292348}. Golgi apparatus membrane {ECO:0000269|PubMed:29995586}; Single-pass type I membrane protein {ECO:0000269|PubMed:29995586}. Note=Co-localizes at the apical junctions with stan. {ECO:0000269|PubMed:23292348}.; SUBCELLULAR LOCATION: [ATPase H(+)-transporting accessory protein 2 N-terminal fragment]: Secreted {ECO:0000269|PubMed:23292348}. Note=Localization to the planar cell polarity domains depends by stan. {ECO:0000269|PubMed:23292348}.
Interaction partners:
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit B
- V-type proton ATPase subunit H
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit a
- Probable V-type proton ATPase subunit d 2
- VhaAC45-related protein, isoform B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit a
Sequence:
MLRVFVIFSLFIAAINASGEFTVLNRPKAISFKGNDALESHYVGDVLYASMGNAVSGDTNWNGLTINDPFNLAKGVILVHVQGIGHVTTAGNVKTYELTGSGTDASLNALAAELEAANEPVCDINFEQFDDGVQAWKSCFGDFEAPAAKPTKHLNPSLHTADKQFLQEVGFINSAADHLAEMAKPSNVLMLRVSVDGVAKAHGEKSVAVEEANKLLSAAISRLLAASQKSSDSVLFVQTTEKDVAASRAKRDTIAASTTNPYNLAVYYGSDYPVIFNIILWFMVVFGLSLLAICYAIAAMDPGRDSIIYRMTSTRIKKDN
Protein: G-protein coupled receptor 3 (F1STP7)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Phosphodiesterase
Sequence:
MMWGAGSPLAWLSAGPGNVNMSSIGSTEGPTDPDAPLPSPRAWDVVLCISGTLVSCENALVVAIIVGTPAFRAPMFLLVGSLAVADLLAGLGLVMHFAAVFCIGSAEMSLVLVGLMAMAFTASIGSLLAITVDRYLSLYNALTYYSETTVTRTYVMLALVWGGALGLGLLPVLAWNCLDAPATCGVVYPLSKNHLVVLAVAFFMVFGIMLQLYAQICRIVCRHAQQIALQRHLLPASHYVATRKGIATLAVVLGAFAACWLPFTVYCLLGDAQSPPLYTYLTLLPATYNSMINPIIYAFRNQDVQKVLWAVCCCCSSSKIPFRSRSPSDV
Protein: Transient receptor potential melastatin 4a (S5TRY1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MIKMKRVEKESEGCGGGERKAQKDQSWIPKMIKKRVCTTFVEDSCSNGALCQCGGARDLHVSTTADDHVVGQWDRARDTSDYPTDAFGQLEFVGAGRRHCPFLRLSFDTPPDNVYSLMTSQWGLPVPNLVVSMVGGDEKEMAKPWVREVIRQGLVHAAQSTGAWIMTSGLKEGVSRCVGEAVRHHCAMASSLSQAKVIAVGVAPWGLIYQRHQLVNPQGSFPARYYVHDMPSASSCLDNNHQAFLLVDDGSVGHRGSETSFRANLEDFISHQRTGIWGSGSIEIPVLCVLIAGDATMLKRVDLSLKNSTPWLVLAGSGSAADLIAGILKDLSAPLSPPVSPTLQSDSEESSKSSSIELRDRVKERIRKHFPSETELDKLVDQALSIYHNRDLITIFHGDEDGSDDFDTIILKALVRAAKRDSNDASEYTEELKLAVAWNRVDIAKTELFNGDVHWRYEDLEESMTDALVNDKPDFVRLFVESGLNILAYLTYHRLESLYSSLSDCDLVSSFLQRRLQERVGLAASQTRLTPQPDDNSSFKSRATNLTTPSAARDLTLYEVSRVLSEIMEDVCQPFYYTTLGLDHRVNSRKAMKHVNKLLLNESTYRRQRCTSPWISLFIWAVLQNRREMSLYFWKMTGESVLSALAGCKILRELSKLETETETKLSMKELAQTFENLAHDVFSECYQSNEKRSFKLLIRQSPIWGGATCLQMATSADARLFFSHDGVQTLLSEIWWGDMDSNTEVWKLVFSFFLPPFIYTKLINFKVEETDEKAEDFGQGKEFDSTDGAETLADMTNMDEDVEECNALRGKPKASKVIAKKRPFIFHRWRQFWFAPVTSFLGNVLMYFLFLFLFAYVLLIDFKPPPPDGPASLELVLYFWVFTLACEEIRQSFFVGSTTLTQRMKVYIQDIWNKCDITALGLFVLGLLCRMFPWTYNFGRAVMCVDYTVFTLRLIHIFAVHKQLGPKIIIVGKMVKDVFFFLFFLGVWLMAYGVANQALLYSYDSRPGWVARRVFYRPYMHIYGQIPLDEIDADKRHDKRCTDNVTLIHEGAEPCPDSDANWLVLILLSVYLLVTNILLVNLLIAMFSYTFNKVQERSDVYWKFQRYNLIVEYHSRPCLAPPFIIISHLHIFIKRVIQRLPSLKSQHFMLDLTSKETSLLNTWELSLKENLLSTESKKKRESDTERLKRTSTKVDSVLKQMVEIRDHDRRLRKLESEVEYCSTALSWIVEALSQSDLVKQTRPPPYPSKGIASKRPTFSR
Protein: Guanylate kinase (EC 2.7.4.8) (GMP kinase) (Guanylate kinase 1) (Q16774)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of GMP to GDP. Essential enzyme for recycling GMP and indirectly, cyclic GMP (cGMP). Involved in the cGMP metabolism in photoreceptors (By similarity). It may also have a role in the survival and growth progression of some tumors. In addition to its physiological role, GUK1 is essential for convert prodrugs used for the treatment of cancers and viral infections into their pharmacologically active metabolites, most notably acyclovir, ganciclovir, and 6-thioguanine and its closely related analog 6-mercaptopurine.
Subcellular location: Photoreceptor inner segment {ECO:0000250|UniProtKB:Q64520}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q64520}. Note=Colocalizes with RD3 in photoreceptor inner segments and to a lesser extent in the outer plexiform layer. {ECO:0000250|UniProtKB:Q64520}.
Interaction partners:
- GMP synthase
- Adenine phosphoribosyltransferase
- Ribonucleoside-diphosphate reductase large subunit
- Nucleoside diphosphate kinase 3
- Nucleoside diphosphate kinase, mitochondrial
- Nucleoside diphosphate kinase B
- Adenylate kinase 9
- Hypoxanthine-guanine phosphoribosyltransferase
- Nucleoside diphosphate kinase A
- Inosine triphosphate pyrophosphatase
Sequence:
MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEPGLFDVVIINDSLDQAYAELKEALSEEIKKAQRTGA
Protein: Zinc finger C4H2 domain-containing protein (Hepatocellular carcinoma-associated antigen 127 homolog) (Q68FG0)
Organism: Mus musculus (Mouse)
Function: Plays a role in interneurons differentiation. Involved in neuronal development and in neuromuscular junction formation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NQZ6}. Nucleus {ECO:0000250|UniProtKB:Q9NQZ6}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9NQZ6}.
Interaction partners:
- E3 ubiquitin-protein ligase Rnf220
Sequence:
MADEQEIMCKLESIKEIRNKTLQMEKIKARLKAEFEALESEERHLKEYKQEMDLLLQEKMAHVEELRLIHADINVMENTIKQSENDLNKLLESTRRLHDEYKPLKEHVDALRMTLGLQRLPDLCEEEEKLSLDYFEKQKAEWQTEPQEPPIPESLAAAAAAAQQLQVARKQDTRQTATFRQQPPPMKACLSCHQQIHRNAPICPLCKAKSRSRNPKKPKRKQDE
Protein: SID1 transmembrane family member 1 (Q9NXL6)
Organism: Homo sapiens (Human)
Function: In vitro binds long double-stranded RNA (dsRNA) (500 and 700 base pairs), but not dsRNA shorter than 300 bp. Not involved in RNA autophagy, a process in which RNA is directly imported into lysosomes in an ATP-dependent manner, and degraded.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein unc-119 homolog A
- Endoribonuclease Dicer
Sequence:
MRGCLRLALLCALPWLLLAASPGHPAKSPRQPPAPRRDPFDAARGADFDHVYSGVVNLSTENIYSFNYTSQPDQVTAVRVYVNSSSENLNYPVLVVVRQQKEVLSWQVPLLFQGLYQRSYNYQEVSRTLCPSEATNETGPLQQLIFVDVASMAPLGAQYKLLVTKLKHFQLRTNVAFHFTASPSQPQYFLYKFPKDVDSVIIKVVSEMAYPCSVVSVQNIMCPVYDLDHNVEFNGVYQSMTKKAAITLQKKDFPGEQFFVVFVIKPEDYACGGSFFIQEKENQTWNLQRKKNLEVTIVPSIKESVYVKSSLFSVFIFLSFYLGCLLVGFVHYLRFQRKSIDGSFGSNDGSGNMVASHPIAASTPEGSNYGTIDESSSSPGRQMSSSDGGPPGQSDTDSSVEESDFDTMPDIESDKNIIRTKMFLYLSDLSRKDRRIVSKKYKIYFWNIITIAVFYALPVIQLVITYQTVVNVTGNQDICYYNFLCAHPLGVLSAFNNILSNLGHVLLGFLFLLIVLRRDILHRRALEAKDIFAVEYGIPKHFGLFYAMGIALMMEGVLSACYHVCPNYSNFQFDTSFMYMIAGLCMLKLYQTRHPDINASAYSAYASFAVVIMVTVLGVVFGKNDVWFWVIFSAIHVLASLALSTQIYYMGRFKIDLGIFRRAAMVFYTDCIQQCSRPLYMDRMVLLVVGNLVNWSFALFGLIYRPRDFASYMLGIFICNLLLYLAFYIIMKLRSSEKVLPVPLFCIVATAVMWAAALYFFFQNLSSWEGTPAESREKNRECILLDFFDDHDIWHFLSATALFFSFLVLLTLDDDLDVVRRDQIPVF
Protein: ADP-ribosylation factor 2 (P19146)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ADP-ribosylation factor 1
- ARF guanine-nucleotide exchange factor 2
- ARF guanine-nucleotide exchange factor 1
- ADP-ribosylation factor GTPase-activating protein GLO3
- ADP-ribosylation factor GTPase-activating protein GCS1
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
- Kinesin-like protein KAR3
- Phosphatidylinositol 4-kinase PIK1
- Coatomer subunit gamma
- ADP-ribosylation factor 3
Sequence:
MGLYASKLFSNLFGNKEMRILMVGLDGAGKTTVLYKLKLGEVITTIPTIGFNVETVQYKNISFTVWDVGGQDRIRSLWRHYYRNTEGVIFVIDSNDRSRIGEAREVMQRMLNEDELRNAVWLVFANKQDLPEAMSAAEITEKLGLHSIRNRPWFIQSTCATSGEGLYEGLEWLSNNLKNQS
Protein: Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32) (Q9DBX1)
Organism: Mus musculus (Mouse)
Function: Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MKPPSAQSSPAAVAAAAPAMDSAAAADLTDVLCEFDAVLADFASPFHERHFHYEEHLERMKRRSSASVSDSSGFSDSESADSVYRDSFTFSDEKLNSPTNSSPALLPSAVTPRKAKLGDTKELEDFIADLDRTLASM
Protein: Barricade, isoform A (Barricade, isoform C) (LD27763p) (Q7K204)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Splicing factor 3B subunit 1
- Probable ATP-dependent RNA helicase DDX46
- Splicing factor 3A subunit 2
- LD45152p
- Splicing factor 3B subunit 3
- Probable U2 small nuclear ribonucleoprotein A'
- Splicing factor 3A subunit 1
- Splicing factor 3B subunit 6
- Splicing factor 3B subunit 4
- Protein crooked neck
Sequence:
MSDEGGCKSEQLEKSEEAEEKKGDAEGQEAKAPILNPISVPEVDDKPTENKPQSDNHADKTDETPSQDFAAYEEHMTYGADGGAIYTDPSTKQKYKWCATGNNWQPLGVDEDVDGQAEDPYENEHYKWCPKSQQWLPKKQETETEHYKWDDEQKKWVPKHPNPGQEGVCGVDEHGERTYTDKDGVEFFWDATKSAWFPKIDDDFMARYQMNYGFIDNTSAGEKEKAEKEAAEAKRKEEELKRMTAEAEAAMSRDNPASSAAVPTGKRKAQEPPKWFEMDPLQNTKVYVSNLPLDITMDEFADLMGKCGMVMRDPQTQKFKLKLYAEKDGQIKGDGLCDYIKVESVNLALKILDEYNLRGHKIRVQRAQFQMRGEYNPALKPKRKKKDKEKLQKMKEKLFDWRPDKLRGERSKNEKTVIIKNLFTPELFEKEVELILEYQNNLREECSKCGMVRKVVIYDRHPDGVAQINMASPEEADLVIQMMQGRYFGQRQLSAEAWDGKTKYKIEESAVEAHERLSKWDEFLAEEETDKKASEDMKEEDVDSPENQLLPGDATP
Protein: FACT complex subunit spt16 (Facilitates chromatin transcription complex subunit SPT16) (dSPT16) (Q8IRG6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is required for expression of Hox genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:12934007}. Chromosome {ECO:0000269|PubMed:12934007}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
Interaction partners:
- FACT complex subunit Ssrp1
- Transcription elongation factor SPT5
- Transcription elongation factor SPT6
- Transcription elongation factor SPT4
- Hyrax
- RNA polymerase II-associated factor 1 homolog
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB2
- Ctr9, isoform A
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MSSFVLDKEAFVRRVKRLYTEWRAPSIGHDDALRNLDCIMSIVGVEEDVMYSKSMALQLWLLGYELTDTISVFCSDAVYFLTSKKKIEFLKQTQNITEEGFPEINLLVRDRTDKDQGNFEKLIKALQNSKKGKRLGVFAKDAYPGEFSEAWKKSLTASKFEHVDISTIIAYLMCPKDESEINNIRKASLVSMDIFNKYLKDEIMDIIDSDRKVKHNKLSDGCEAAIGEKKYTSGLDPRLLDMAYPPIIQSGGAYSLKFSAVADKNPLHFGVIVCSLGARYKSYCSNISRTFLVNPTEAMQENYTFLVSVQEEILKLLVPGTKLCDVYEKTLDFVKKEKPSMVDNLPKSFGFAMGLEFRENSIVIGPKCQALLKKNMVFNLHVGISNLTNPEATDKEGKNYALFIGDTVLVGEQSPASVMTPSKKKIKNVGIFIKDDSDEEDVDDKKTAKEDQGTEILGRSKRNAVLESKLRNEINTEEKRKEHQRELAQQLNERAKDRLARQGNSKEVEKVRKNTVSYKSISQMPREPEVKELKLYVDKKYETVIMPVFGIQVPFHISTIKNISQSVEGEYTYLRINFFHPGATMGRNEGGLYPQPEATFVKEVTYRSSNVKEHGEVGAPSANLNNAFRLIKEVQKRFKTREAEEREKEDLVKQDTLILSQNKGNPKLKDLYIRPNIVTKRMTGSLEAHSNGFRYISVRGDKVDILYNNIKSAFFQPCDGEMIILLHFHLKYAIMFGKKKHVDVQFYTEVGEITTDLGKHQHMHDRDDLAAEQAERELRHKLKTAFKSFCEKVETMTKSVVEFDTPFRELGFPGAPFRSTVTLQPTSGSLVNLTEWPPFVITLDDVELVHFERVQFHLRNFDMIFVFKEYNKKVAMVNAIPMNMLDHVKEWLNSCDIRYSEGVQSLNWQKIMKTITDDPEGFFEQGGWTFLDPESGSEGENETAESEEDEAYNPTDAESDEESDEDSEYSEASEDSEESDEDLGSDEESGKDWSDLEREAAEEDRNHDYAADDKPRNGKFDSKKHGKSSKHSPSKSSKDKYNSRDKHHSSSSSGNKSSSKDKDRKRSRDDSRDNGHKSKKSRH
Protein: Protein YIPF2 (YIP1 family member 2) (Q9BWQ6)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:27999994}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:27999994}. Late endosome membrane {ECO:0000269|PubMed:27999994}. Note=Mainly localizes within medial-/trans-Golgi and trans-Golgi network (TGN), while less so within cis-Golgi. {ECO:0000269|PubMed:27999994, ECO:0000269|PubMed:28286305}.
Interaction partners:
- Protein YIPF6
- Protein YIPF3
- Protein YIPF4
- Large ribosomal subunit protein mL62
Sequence:
MASADELTFHEFEEATNLLADTPDAATTSRSDQLTPQGHVAVAVGSGGSYGAEDEVEEESDKAALLQEQQQQQQPGFWTFSYYQSFFDVDTSQVLDRIKGSLLPRPGHNFVRHHLRNRPDLYGPFWICATLAFVLAVTGNLTLVLAQRRDPSIHYSPQFHKVTVAGISIYCYAWLVPLALWGFLRWRKGVQERMGPYTFLETVCIYGYSLFVFIPMVVLWLIPVPWLQWLFGALALGLSAAGLVFTLWPVVREDTRLVATVLLSVVVLLHALLAMGCKLYFFQSLPPENVAPPPQITSLPSNIALSPTLPQSLAPS
Protein: tRNA pseudouridine synthase (EC 5.4.99.12) (J3KTG4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVAMQEAAQHLLGTHDFSAFQSAGSPVPSPVRTLRRVSVSPGQASPLVTPEESRKLRFWNLEFESQSFLYRQVRRMTAVLVAVGLGALAPAQVKTILESQDPLGKHQTRVAPAHGLFLKSVLYGN
Protein: Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Q99798)
Organism: Homo sapiens (Human)
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P16276}.
Interaction partners:
- Citrate synthase, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit gamma, mitochondrial
- ATP-citrate synthase
- Frataxin, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Superoxide dismutase, mitochondrial
Sequence:
MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLNRPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPGQDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ
Protein: Multifunctional transport intrinsic membrane protein 2 (Q9LKJ5)
Organism: Lotus japonicus (Lotus corniculatus var. japonicus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGESSAPNGLNGAHEVVVNVNKDASKTIEVSDTNFTVSFLQKVIAELVGTYFFIFAGCASIVVNKNNDNVVTLPGIALVWGLAVMVLVYSLGHISGAHFNPAATIAFASTKRFPWKQVPAYVSAQVLGSTLASGTLRLIFSGKHNQFAGALPTGSNLQAFVIEFIITFFLIFILFGVATDDRAIGEVAGIVVGSTVLLNVLFAGPITGASMNPARSIGSAFVHNEYRGIWIYLLSPTLGAVAGAWVYNIVRYTDKPLREITKNVSFLKGI
Protein: Cytoplasmic filament protein A (Q56336)
Organism: Treponema pallidum (strain Nichols)
Function: Component of the cytoplasmic filaments that run the length of the organism just underneath the cytoplasmic membrane.
Subcellular location: Cytoplasm. Note=An array of 4 to 6 filaments lie in close apposition to the inner membrane and are always localized directly underneath the corresponding group of periplasmic flagella.
Interaction partners:
- Uncharacterized protein TP_0749
Sequence:
MASLDLPKSPNVFHPEKPSAVGSRNSLAQDCRDQQQEVNQLIEEETNKILHHLNTKLPKEVLERLDVMGGLKEKLYNYFNQNYQNMFNRYMVTAEDEMLKKVRGFIDREEMKVLNRYTPKEIAILLDEVAGADKFNTGEIEKSMVNMYGHLQGHIQRGVNELETHTNSLLRQKVDVGAFVRGENAYAVVKCAFKDNLARPKTVTDVKLSINILDSELVSPIFHYQTTVAYLIKDLISNHYIDAIDKEIDRVKDELIDQGKEEMSDSSIIFEKMKMVSDFTDDDCENPDSKRYELISRELMERISNLRAEIDPETFDQLNVRENIKKIVDLENIRNRGFNTAINSITSILDTSRMGYQYIENFKNARELILREYDDTDISNLPDERYQLRLKYLDNAQLIEERKGYEVMLRSFETEVDHLWDVLRTKYDKSKASRFMAKITDFDDLAKVYKKHIKKHYKDKTGEPVYEDIAKVWDEIAFVKPAETEVERMNRTFVYEKDKMRRKLILMRGKLKGMYDYQYPIERRVMEERLAFLESEFNRFDYLVNPFHLQPGLLLDIDITSIKRKKATLDGMANVLNEFLHGISKGFADAAFASFSRRRSTVRADIGQSFASDGSADQKESSGRVAFMDMVNETPALESSVAAEQVDVRSDVGMKTRKAGAVDAGKGRRGRRSAIREL
Protein: methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta) (C8VAZ1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 3-methylcrotonyl-CoA carboxylase biotin-containig subunit3-methylcrotonyl-CoA carboxylase biotin-containing subunit
- Isovaleryl-coenzyme A dehydrogenase
- Putative urea carboxylase
- Mitochondrial methylglutaconyl-CoA hydratase
- Acyl-CoA dehydrogenase, putative
- Enoyl-CoA hydratase/isomerase family protein
- Uncharacterized protein
- Acyl-CoA dehydrogenase NM domain-like protein
- 2-oxoisovalerate dehydrogenase subunit alpha
- 4-hydroxyphenylpyruvate dioxygenase
Sequence:
MRVSVPLHSIRRSCNSSIANAATRLTPQRLYLSYGRRSSIVQAHPRTQARPIASYTHPHHASAISVLSTAVDTSSPDFRENERQMQEVLNRMNSLHSTISQGGPQKAKDKHVARGKMLPRDRVSALIDPGTSFLELSQLAGHEVYPGEDVPAGGIITGIGTVEGVTCMIVANDSTVKGGTYYPVTVKKHLRAQAIAQENKLPCIYLVDSGGANLPHQADVFPDKEHFGRIFFNQARMSSQGIPQISVVMGPCTAGGAYVPAMSDETIIVENQGTIFLAGPPLVKAATGEVVSAEDLGGGQLHSTISGVTDYLAVDDAHAIVLARRSISNLNYPKAKQPLESNDDIKEPLYDPAELNGIVGTNLRRQIPVHEVIARIVDGSEFAEFKRDYGTTLVTGFARIHGHRVGIVANNGILFSESSLKGAHFIELCAQRNIPLVFLQNISGFMVGADAEKGGIAKNGAKLVTAVACADVPKFTVVFGSSAGAGNYGMCGRAYSPRFLFMWPNAKIGVMGSEQLSSVMEAVGRTADPELKARIDRESEATFSSARLWDDGIIPPAHTRHVLGLSLAAALGGKSDKDVQTKFGVFRM
Protein: Protein BANP (BEN domain-containing protein 1) (Btg3-associated nuclear protein) (Scaffold/matrix-associated region-1-binding protein) (Q8N9N5)
Organism: Homo sapiens (Human)
Function: Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell cycle arrest (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16166625, ECO:0000269|PubMed:26080397}. Nucleus speckle {ECO:0000269|PubMed:26080397}. Cytoplasm {ECO:0000269|PubMed:26080397}. Note=Primarily nuclear but translocates to the cytoplasm following MAPK1/MAPK3-mediated phosphorylation. {ECO:0000269|PubMed:26080397}.
Interaction partners:
- Histone deacetylase 1
- Cellular tumor antigen p53
- Histone-lysine N-methyltransferase SETMAR
- E3 ubiquitin-protein ligase Mdm2
- Pre-mRNA-processing factor 19
- Homeobox protein cut-like 1
- Catenin beta-1
Sequence:
MMSEHDLADVVQIAVEDLSPDHPVVLENHVVTDEDEPALKRQRLEINCQDPSIKTICLRLDSIEAKLQALEATCKSLEEKLDLVTNKQHSPIQVPMVAGSPLGATQTCNKVRCVVPQTTVILNNDRQNAIVAKMEDPLSNRAPDSLENVISNAVPGRRQNTIVVKVPGQEDSHHEDGESGSEASDSVSSCGQAGSQSIGSNVTLITLNSEEDYPNGTWLGDENNPEMRVRCAIIPSDMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLTIYGIRCHLFYKFGITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPNSSSYCPSEPMMSTPPPASELPQPQPQPQALHYALANAQQVQIHQIGEDGQVQVGHLHIAQVPQGEQVQITQDSEGNLQIHHVGQDGQLLEATRIPCLLAPSVFKASSGQVLQGAQLIAVASSDPAAAGVDGSPLQGSDIQVQYVQLAPVSDHTAGAQTAEALQPTLQPEMQLEHGAIQIQ
Protein: UDP-3-O-acyl-N-acetylglucosamine deacetylase (UDP-3-O-acyl-GlcNAc deacetylase) (EC 3.5.1.108) (UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase) (P47205)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Interaction partners:
- UDP-3-O-acylglucosamine N-acyltransferase
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Lipid-A-disaccharide synthase
- Tetraacyldisaccharide 4'-kinase
- 2-dehydro-3-deoxyphosphooctonate aldolase
- 3-deoxy-D-manno-octulosonic acid transferase
- Lipid A biosynthesis acyltransferase
- 3-deoxy-manno-octulosonate cytidylyltransferase
- UDP-2,3-diacylglucosamine hydrolase
Sequence:
MIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGIVFCRTDLDPVVEIPARAENVGETTMSTTLVKGDVKVDTVEHLLSAMAGLGIDNAYVELSASEVPIMDGSAGPFVFLIQSAGLQEQEAAKKFIRIKREVSVEEGDKRAVFVPFDGFKVSFEIDFDHPVFRGRTQQASVDFSSTSFVKEVSRARTFGFMRDIEYLRSQNLALGGSVENAIVVDENRVLNEDGLRYEDEFVKHKILDAIGDLYLLGNSLIGEFRGFKSGHALNNQLLRTLIADKDAWEVVTFEDARTAPISYMRPAAAV
Protein: Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I beta) (GSI beta) (P0A9C5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
Interaction partners:
- Sensory histidine kinase/phosphatase NtrB)
- Glutamate synthase large chain
- NADP-specific glutamate dehydrogenase
- Glutamate synthase small chain
- Nitrogen regulatory protein P-II 1
- DNA-binding transcriptional regulator NtrC)
- Bifunctional protein PutA
- Nitrite reductase large subunit
- Nitrogen regulatory protein GlnK
- Ammonium transporter AmtB
Sequence:
MSAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFDGSSIGGWKGINESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRSIAKRAEDYLRSTGIADTVLFGPEPEFFLFDDIRFGSSISGSHVAIDDIEGAWNSSTQYEGGNKGHRPAVKGGYFPVPPVDSAQDIRSEMCLVMEQMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLFAGDKYAGLSEQALYYIGGVIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVSSPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNLYDLPPEEAKEIPQVAGSLEEALNELDLDREFLKAGGVFTDEAIDAYIALRREEDDRVRMTPHPVEFELYYSV
Protein: Uncharacterized protein At5g48480 (Q9LV66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- KH domain-containing protein At4g18375
- Putative H/ACA ribonucleoprotein complex subunit 1-like protein 1
- Endoglucanase 10
Sequence:
MAQEDVTAVATNGAGPVETHLVFTEFKQMLLVEAQKVGDAVTFYKSAFGAIESGHSLYPKRKLDQELPHVLSSELNLAGSSFVVCDVSSLPGFSTAKSEGSGVTFLLGTKDAEAAVAKAVDAGAVKVEVTEAEVELGFKGKVTDPFGVTWIFAEKKTVITDENKEV