wanglab/gogpt-training-data huggingface dataset:
Protein: RE27439p (Q8SYY8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MLVGSHPYLCNGVPAAPAAPNASGQTTTTASKSAAGSATDFSIAAIMAREDASSRESSIRSASPISVEDEVDVDVVDCSDAEEPPTKARRLNHHQHHQHHQHHHNNNNNNNNNNVAHKSRNSGGAVAQTASAESQLNTSSTSSQGRCSTPPQSPGTEDSEERLTPEPVQKAPKIVGSCNCDDLKPVQCHLETKELWDRFHDLGTEMIITKTGRRMFPTVRVSFSGPLRQIQPADRYAVLMDIIPMDSKRYRYAYHRSAWLVAGKADPAPPARLYAHPDSPFSCEALRKQVISFEKVKLTNNEMDKNGQIVLNSMHRYQPRIHLVRLSHGQSIPSNPKELQDLDHKTYVFPETVFTAVTAYQNQLITKLKIDSNPFAKGFRDSSRLTDFDRDPMEALLLEQQLRSPLRLFPDPLMQQFAAQGDPSSMALFEKARQHLQMFGGNSPYAQLMMPQMYQAAAAAAGPPPPPPGLGAFHMFQQQWPQLTAGFLASANQQAAAAQAAAQAQAQTQAAAAAMAANRTPPPPPTASTPSSTSSGSPSPDMRPRQYQRFSPYQLPAVRGHPPLPPVRHPR
Protein: Uncharacterized protein Opa (O16814)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MELPIVLLLVLSVIPFEAQGAVHDELPQCGLHGVYRQRQSLVESPNYPDNYPVNTCWDYVVRSPYRCPTKFHIQFLDFKLELSENCSRDYLAIXEQRWRRHGGLVRSGAGYQKVSTPDGVLRLRFLSDDSPWTTNGGFRLLITRLACEKETCGQGLDDDEEDVHGDTVQVSAKSPPKKLLTQHHHHHLPQQSHQPQLEPAFNYTQPNRLGFNLGLQPGLDYPGGLYPPPAGLPPQYTPPCAPQQQQVLQQQQEQQRFLQQQQLQQQVQVQHPQQLQLSQQRQQLQQELPLISDQYQTTSFQPHAVTLKDYDAQTLQQFGGQLDLCCASSFNQNHFYLSSPGFPRTVLNYLLPNQQRDCVFYIEKSSANVCRLRIQFKFFDFGQNSGGSIGGSFGDGFGGGVSGGLGGGHSGGFGGQHNCNGDFLELDGQRYCGCPSGYVHKSHWDQGRKACACALDNRAAPRPMAFCWRYSRIRTPMAVVKMLAKDLVWACNRSNLKGDWVCGHRGYSLSWACNLSWACNLSWDYPANRTNVAATTWLSWLYQWISPTLFGHSLPNGEKDILCPGIDAQQPSRVVETNSTRKEFYYFDGDEAFARSAVDDEDEDKAHLGVTTQPQSSSQSIVKPESPLVTKAFEQSSCSFDYMRYLNFQSTLSG
Protein: Solute carrier family 22 member 6 (Organic anion transporter 1) (Renal organic anion transporter 1) (ROAT1) (Q6NYN7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one molecule of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). Mediates the sodium-independent uptake of p-aminohippurate (PAH), 2,3-dimercapto-1-propanesulfonic acid (DMPS), cidofovir, adefovir, 9-(2-phosphonylmethoxyethyl) guanine (PMEG), 9-(2-phosphonylmethoxyethyl) diaminopurine (PMEDAP), ochratoxin (OTA), acyclovir (ACV), 3'-azido-3-'deoxythymidine (AZT), cimetidine (CMD), 2,4-dichloro-phenoxyacetate (2,4-D), hippurate (HA), indoleacetate (IA), indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF) and edaravone sulfate. PAH uptake is inhibited by p-chloromercuribenzenesulphonate (PCMBS), diethyl pyrocarbonate (DEPC), indomethacin, sulindac, diclofenac, carprofen, okadaic acid, benzothiazolylcysteine (BTC), S-chlorotrifluoroethylcysteine (CTFC), cysteine S-conjugates S-dichlorovinylcysteine (DCVC), furosemide, steviol, phorbol 12-myristate 13-acetate (PMA), calcium ionophore A23187, benzylpenicillin, bumetamide, losartan, probenecid, phenol red, urate, glutarate and alpha-ketoglutarate (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8VC69}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8VC69}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Solute carrier family 22 member 18.
- Ig-like domain-containing protein.
Sequence:
MAFSDLLEQVGSTGRFQVLHVTLLSMPILMMASHNLLQNFVAAVPPHHCQPHANLSMSSTDAVDVLRATVPLGLNGKLERCKRYTTPQWQILSLNTSESLWDESMAETETQSCEDGWFYNMTEMSSTIITEWDLVCDYRALKQMSQTTYMGGVLVGAIVFGGLSDRFGRRVLLLISNLMMAIGGTCVAFSTSFTMFCVFRVCCGMALSGLVLNSFSLIVEWIPTRVRTVVGTGTGYCYTTGQLILAAVAYCIRDWRWLTLAVSLPFYVSFLYSWWFLESARWLVLTKNPEQAVKNLKTVARINGRSAEGDKIDLEMLQESMKKEMACSKGSYSALDLLRTSTMRTITICLSAVWFSTSFAYYGLSMDLQKFGVSIYLIQIIFGAVDIPAKIIVTICMSMLGRRPSQCGALVLAGIMILINLLVPSDLQMLRTSLAVIGKGCLAASFNCCYLYAGELYPTVIRQSGMGWVSMMARFGAMVAPMVLLLGDDYPWIPGFIYGGAPIVSGIFAFFLPETLSQPLPDTIQDIDDRGLARTNSKRLPEKLDLAMKDPSCVLLKESV
Protein: Putative GM130 protein (Q9NFP0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPDDTQDAKAQKLAAARKKLKEYQQRASNNNGQPGAEEPVAATTQSHSSTVSISSNLSERSDSEINVNGGGAGGTQPPEQSALPTAASYFAQNESEHNGGLADASSLQAIQVIIAEKAQLNAELTKVRLACRERELELEELRILKDQNQLRLEQLQQHCQDQQSTGDDAQLQAQLLQSQAQIKDQQSHLNELEAQLKQSNQHQEELQQQLSQKSNELEMAQLKLRQLSDESSVTTDNRVESLVQTQYMYEQQIRDLQAMVGQLTQDKEQAAGQYQNYVQHQSGEIAKLNERNTELSEVLNSLRERERQLVEHVGALERDIQKNISLQAQFKEASQVQPSKEETSEQKALKDELAVLKEQIENFEFERHEFQLKIKSQDDQLQLKNSALDELEKQLERLQAEQPDQSKLLATMESDKVAASRALTQNVEMKNQLDELQQRFVQLTNDKAELVIRLDSEEFANREIRQNYNSMEQKLQANEERFKFKDEEMIRLSHENVELQRQQLMLQQQLDRLRHYEAKAYHAGEETEKENGADAPENEAEEAKEVGLLHNHSHDHSHQHSDGHCHDNDHDHSHEHNHHNAGDHGHPHDHPHDHTHDHSHSHPHDHQHDHPHDHGQNHAHRQAAETLPTAEAVERLQSRFTTLISQVADLTEEKHSLEHLVLQLQSETETIGEYIALYQTQRRMLKQREYEKAAQMRLLQAEREQLREKIEALNKLVVSLGVELPADAAQAKQPEAAAGSEHTPGEGENSQQIINKIQDIISEIKENTEQPSHNHAGDHLNCCMGKFEVV
Protein: Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog (LPS-induced TNF-alpha factor homolog) (Estrogen-enhanced transcript protein 1) (Eet-1) (P0C0T0)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in endosomal protein trafficking and in targeting proteins for lysosomal degradation. Plays a role in targeting endocytosed EGFR and ERGG3 for lysosomal degradation, and thereby helps down-regulate downstream signaling cascades. Helps recruit the ESCRT complex components TSG101, HGS and STAM to cytoplasmic membranes. Probably plays a role in regulating protein degradation via its interaction with NEDD4. May also contribute to the regulation of gene expression in the nucleus. Binds DNA (in vitro) and may play a synergistic role with STAT6 in the nucleus in regulating the expression of various cytokines. May regulate the expression of numerous cytokines, such as TNF, CCL2, CCL5, CXCL1, IL1A and IL10.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99732}. Nucleus {ECO:0000250|UniProtKB:Q99732}. Lysosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Early endosome membrane {ECO:0000250|UniProtKB:Q99732}. Late endosome membrane {ECO:0000250|UniProtKB:Q99732}. Endosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Cell membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99732}. Note=Associated with membranes of lysosomes, early and late endosomes. Can translocate from the cytoplasm into the nucleus (By similarity). Detected at Schmidt-Lanterman incisures and in nodal regions of myelinating Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q99732, ECO:0000250|UniProtKB:Q9JLJ0}.
Interaction partners:
- SH3 domain and tetratricopeptide repeats 2
- RNA helicase
Sequence:
MSAPGPYQAAAGPSVMPTAPPTYEETVGVNSYYPTPPAPQPGPATGLITGPDGKGMNPPSYYTQPVPVPNANAIAVQTVYVQQPISFYDRPIQMCCPSCNKMIVTQLSYNAGALTWLSCGSLCLLGCVAGCCFIPFCVDALQDVDHYCPNCKALLGTYKRL
Protein: POLDIP3 protein (Q8WUT1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADISLDELIRKRGAAAKGRLNARPGVGGVRSRVGIQQGLLSQSTRTATFQQRFDARQKIGLSDARLKLGVKDAREKLLQKDARFRIKGKVQDAREMLNSRKQQTTVPQKPRQVADAREKISLKRSSPAAFINPPIGTVTPALKLTKTIQNLYDLDEDDDGIASVPTKQMKFAASGGFLHHMAGLSSSKLSMSKALPLTKVVQNDAYTAPALPSSIRTKALPVLTSPGT
Protein: Zinc transporter ZIP5 (Solute carrier family 39 member 5) (Zrt- and Irt-like protein 5) (ZIP-5) (Q9D856)
Organism: Mus musculus (Mouse)
Function: May play a role in polarized cells by carrying out serosal-to-mucosal zinc transport. Seems to play a central role in controlling organismal zinc status. Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (By similarity). Plays a role in eye development (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:15322118, ECO:0000269|PubMed:15358787, ECO:0000269|PubMed:18020946}; Multi-pass membrane protein {ECO:0000269|PubMed:15322118}. Note=Localized to the basolateral surfaces of enterocytes, pancreatic acinar and endoderm cells (PubMed:15358787). During zinc deficiency diet, the basolateral cell membrane localization is lost in the intestine, the visceral yolk sac and acinar cell (PubMed:15358787). During zinc repletion, is relocalized to the basolateral membrane of enterocytes, visceral endoderm cells and pancreatic acinar cells (PubMed:18020946). Zinc can regulate the turnover of protein at the membrane (PubMed:18020946). During zinc deficiency, is internalized and degraded in enterocytes, acinar cells and endoderm cells (PubMed:18020946). Endocytosed through the endolysosomal degradation pathway RAB5A pathway (PubMed:24039764). {ECO:0000269|PubMed:15358787, ECO:0000269|PubMed:18020946, ECO:0000269|PubMed:24039764}.
Interaction partners:
- Zinc transporter ZIP1
- Zinc transporter ZIP11
- Proton-coupled zinc antiporter SLC30A1
- Proton-coupled zinc antiporter SLC30A5
- Zinc transporter 6
- Zinc transporter ZIP9
- Zinc transporter 7
- Probable proton-coupled zinc antiporter SLC30A4
- Proton-coupled zinc antiporter SLC30A2
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
Sequence:
MGPPVHHLLTGLCVGVALGWVGGSVPNLGPAEQEQNHYLAQLFGLYGENGTLTAGGLARLLHSLGLGRVQGLRLGHHEPPTGRAAPTSGDNFTHRLQEPELSVDIWAGMPLGPSGWGDQEESKAPDLHGSGPSSLDLFQRLLLLDHSLADHLNEDCLNGSQLLVNFGLSPVAPLTPRQFALLCPALLYQIDSRVCIKTPAPAPPGDVLSALLHSGLAVLFLSLPAPLSLLLLRLLGPRLLRPVLGFLGALAVGTLCGDALLHLLPHAQGGRHTGPSEQSEEDLGPGLSVLGGLFLLFMLENTLGLVRHRGLRPRCCRNKRDLGEPNPDPEDGSGMVLRPLQAASEPEVQGQRENRQSSPSLAPPGHQGHSHEHRGGSIAWMVLLGDCLHNLTDGLALGAAFSDGFSSGLSTTLAVFCHELPHELGDFAMLLQEGLSFRKLLLLSLVSGALGLGGAALGVGLSLGPVPLTPWVFGTTAGVFLYVALVDMLPTLLRPPEPLPVFHVLLQGLGLLLGGSLMFTIALLEEQLVPTVPDG
Protein: bZIP transcription factor 11 (AtbZIP11) (G-box-binding factor 6) (bZIP transcription factor ATB2) (O65683)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds to the DNA sequence 5'-ACTCAT-3' in target gene promoters. Promotes POX1/PRODH1 expression in response to hypoosmolarity stress. Positively regulates the expression of ASN1 and POX2/PRODH2 genes, which are involved in amino acid metabolism. Regulates several metabolic pathways such as myo-inositol, raffinose and trehalose. Regulates several trehalose metabolism genes, including TRE1, TPP5 and TPP6. Mediates recruitment of the histone acetylation machinery to activate auxin-induced transcription. Interacts with ADA2B adapter protein to promote ADA2B-mediated recruitment of SAGA-like histone acetyltransferase complexes to specific auxin-responsive genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:15047879}.
Interaction partners:
- Basic leucine zipper 8
- Transcriptional adapter ADA2b
- SNF1-related protein kinase catalytic subunit alpha KIN10
- Eukaryotic translation initiation factor 3 subunit H
- Asparagine synthetase 1
- SNF1-related protein kinase catalytic subunit alpha KIN11
- Basic leucine-zipper 75
- Proline dehydrogenase 2, mitochondrial
- Basic leucine zipper 25
- Basic leucine zipper 63
Sequence:
MESSSSGTTSSTIQTSSGSEESLMEQRKRKRMLSNRESARRSRMKKQKLLDDLTAQVNHLKKENTEIVTSVSITTQHYLTVEAENSVLRAQLDELNHRLQSLNDIIEFLDSSNNNNNNNMGMCSNPLVGLECDDFFVNQMNMSYIMNQPLMASSDALMY
Protein: XIAP associated factor 1 (A0A8I5ZLW0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRVSQEDTLPCRWETKRSVASSHFTLHEAHCLRFLVLCPECEEPIPESKMKEHVEAVHQQTKESQQDPAECKFCELAVQLSKLDVHEYHCGSRTEHCPHCNQRVILRVLAQHKDLCLSAKGKPKEGKRAVSPGRKTRCDICKQMIPEHKYASHMKQCSAPRTVTYLRDGRTVVLPSTLPLMNTGNQTSTVSKDVRPKTKNRNSSTKRETKDQSGAVDLPLKSRLQQRTALPKGEETAYDILRKCRQCRILLPLPILNEHQVPGSSRPPNCLPSWLGTCCTPTLG
Protein: xyloglucan O-acetyltransferase 2 (EC 2.3.1.-) (Protein ALTERED XYLOGLUCAN 4-like) (Protein trichome birefringence-like 22) (Q9LRS2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains. Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers. Involved in xyloglucan specific O-acetylation in seeds.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Protein REDUCED WALL ACETYLATION 2
- Uncharacterized GPI-anchored protein At4g28100
- Protein REDUCED WALL ACETYLATION 1
- SAC3 family protein C
- Dynamin-related protein 4C
- Alpha-L-fucosidase 2
- Protein REDUCED WALL ACETYLATION 4
- Calmodulin-like protein 5
- Putative RING-H2 finger protein ATL12
- Xyloglucan galactosyltransferase XLT2
Sequence:
MKSSSSIFRETSEKKSERWMMMNIGRFSPFFLSSFCITLFFTGFFVYQNPFKSIADQNVLSFQPQIDPECDLFKGHWVPDKRGSLYTNSSCATIPDSKNCIKQGRPDKDFLFWRWKPDGCDLPRFNPKAFLSMVRGKKMNFIGDSVARNHMESLLCLLSMEETPKDIYKDGEDRNRIWYFPKHDFTLSTSWTKFLVEERERRDSNNTGTGLFDLDIGKIDEGWFNGLPNTDIAIVSAAHWFFRPIFIHRGDETLGCIYCNLPNMTQISPEEGFKLVYSAVLRQINECEMCKKDLVTVLRTISPAHFENGTWDTGGTCSRTSPFGENKIDLQSNEMKIRKSQIEQLEGITKRGNKAKKFAVLDVTRVMQMRPDGHPNGYWGNKWMKGYNDCVHWCLPGPIDAWNDFLMAIIRQLR
Protein: Aldehyde dehydrogenase, mitochondrial (EC 1.2.1.3) (ALDH class 2) (ALDH-E2) (ALDH1) (P11884)
Organism: Rattus norvegicus (Rat)
Function: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Alcohol dehydrogenase class-3
- Amine oxidase [copper-containing] 3
- All-trans-retinol dehydrogenase [NAD
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Acetyl-coenzyme A synthetase, cytoplasmic
- Acetyl-coenzyme A synthetase
- 4-aminobutyrate aminotransferase, mitochondrial
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
Sequence:
MLRAALSTARRGPRLSRLLSAAATSAVPAPNQQPEVFCNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAAQAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Protein: Serine/threonine-protein kinase greatwall (EC 2.7.11.1) (Microtubule-associated serine/threonine-protein kinase-like) (F1RVK2)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MEPTAGSEMESGGGAATGACVTRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGDRLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFHTPVAEKNLDPANILSTHASETSQLSQGLTCPMSIDQKDITPYSSKLLKSCLETFASHPQMPVKCLTSHLLQSRKRLATSSTSSQSHTFISSVESDCHSSPRWEKDCQESDNTVGSTVMSWNTAEKPSCIHSTNAAESKSFNKRDFELALSPIHNSSAIPAPGNSSVNLAKESSSGNVSWEARELDINNINVAAGTRQSRQWTVDSSGITEEHLGKRSCKRSFELIDSSPCQEIIQNKKNCIEYKHSNEMKDCYTNQRTGLTTEVQDLKLSVYGDQQNDCANKENMGNTFSDKQQTPEKSPIPMIAKNLMCELDDDCDKNSKKDYLSSSFLCSDDDRTPKSIHMDSDSSFPGISMMESPLGRQSLDPDKSIKESSLEGSKIEDLLPTSPSCQEGTLLRGDENPAHQDRNPKMLAPSSEVLKTITSKRNAVAFRSFNSHINASTSSEPSKMSITSSDVMDMSCAYSGSYPMTLTPTQKERSYMPYQTPNQAKSGTPYRTPKSVRRGAAPVDDGRILGTPDYLAPELLLGRTHGSAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILKRDIPWPEGEEKLSDNAQSAVEILLTIDDTKRAGMKELKHHPLFNDVDWENLQHQTMPFIPQPDDETDTSYFEARNTAQHLTVSGFSL
Protein: Urease accessory protein D (AtURED) (E0ZS45)
Organism: Oryza sativa subsp. indica (Rice)
Function: Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter.
Interaction partners:
Sequence:
MEAEAAMAAAAAATGAVRVEKVRGRSAVTRCFAKYPLKLIAPSKAGRASSGAAWLYAITYGGGIVSGDIISCTVAVGDGCAAAMTTQASTKVYKAVDSKCSEQVLEARVGEDALFALIPDPVTCFSMARYHQKQVFHVFPNSNLVVVDWFTSGRYESGEKWNFSFYKSINHILLEDQPLFIDSVLLEQSSNFSIADRMQEYNVVAMVILLGPKLKHIQDQMQDEVKKMMSVQLRPPTSAGGRYSTRSQPLHPQRPPIIASCSPFGRMGTGMVARITAVSTESVYSFLRHHLAALEPFLGACPYPAS
Protein: Uncharacterized protein (Q386J2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA damage-binding protein 1
- Uracil-DNA glycosylase
- Cullin 4B, putative
- Cullin family profile domain-containing protein
- HD domain-containing protein
- HD domain-containing protein
- RING-type domain-containing protein
- RING-type domain-containing protein
Sequence:
MENLQGSRLADGTDHFTTLSVDDAANNMSFNVLNELAERSGEENFEDDIIVSAELVGTLKHIMRRLTKAQKQIKMLKERLRAQARNTSPESQGETIDTESGDKQTLTLLQEYINLELFLWGQLAKILHDEYKRCTDVYASTMSLQDRAPFESLIKTVCNNAPFCEYMGEMINFNVERDDLLSRSEGRSIQSEPILYKSVVRTQSIATYTAFLLVEGSRGNFFDSTPIQDLCKVIIGEKKRQKRLIALSLVFSRLEEDDQAVGEALSQQLPRVLLQRLRHLVHRIFGYPENNGISPSQRWSRSPFRHYSAVIRSELNSPTLSRKTSPEVAAGSSVGVPCVKEAQQVLPQSKQMSLSSHSQFAGSEQASSSPMFDRSTIPIKEVEHESALAEFNQGGGDDLISRPHKKRKFETGEESPRFRKLPDFWQPRRGDRVGRGPMWCFNDQGKKCDFGEVVEVTTAEEVVVRWIRSVDCPPHESEGDRFFRYKYKGPNDQVVPWDHFLNIQTLMPENIDFKMEEFMLCCAVVGALCHQRETVLPALQFQTVESMFYVLSRVDLDAATAAVETEEKKTLGFVLSEDNVEMNADERELLEVRLNWSAELQTTKSHYRKMRELVGRVGWVLNSLFTHKKLALIFLELGGLKQIIKLTDGRLDPVTMYGCCIVLSQLARAAVFENLLRNHGEYFEPILNFILHQWKVASSHDVQGSAGGFLFLALSFPYVVTFFDAHQGPQATLGLIERLLQSSEEQFDVICPGVTLAALKCAYVYLISHLMLATRVIFRKHRFLSVLVTDSAPERSLPRDPATVESVLGYLSAPSATIPDISTETIQSLLTRDRLAAFRFFADNNFHQILLRCAQFYFTQGRWDLLAASLNVLCVLVVVPFFRPLVADAQYPESGVAHLIMIVSELTSAFQNGNASRESHLIPCVATSLQILLNLTRLPADKNDDVCVATFNRVCGMIRANDGVRTLLEVLKVRKDPAMSVKLQLFPVVARALQLMVTLRRYADTRLLFDALGVGSVARELMTQYGDIQKEYLTMMGPRYVASEVHATGRFMENIKCFLFDETNRTTPSVSVDPVELEQRQAVIARSHISYSRESLLELICRHLETEGLLNAASALRRDAPLSCDIAMAQHSANASPDMALSPIGAPTLDGIVRSYLRQQHEKCTNPITTLPQFDLRKGHVYYPLDAPVDQTRNAFNRRLVQKMGLDFSLRTRTNENHFTYRNPGYLFDITGSGDELQGDSVAFCDGGETLVVGTSEGGIALFDTFPDDSTDDKLSEQHLAFDNGSVVGIYVSDDSALLGLVNAEHKVAVMGRNELPAVKYQVEDSRAAMFSCCNTYLLATCDEEHTCRLYDLRAQCEVRHFSDPSWVGENVDNVATFDQFSQLVLSDAVLWDVRCGDRPICRFDRFTNSFCNIFHPFNPLVMIDEKVWDLRTLSILQTVPSFRNSSSFYTSPFRRVIYSFREASALSHTATPVLSVVDSYTFETVFSTEVRPAFRAFAIEPSDRYCAAILDGDAAAVVRVFSTSSGPLPGQQAFSLPQNDRSNDSGAGLAESDDDDEVGNNGSWSGGYDEDDDDGEDDSDSYEWASASDSPEYYSNTETTSDSDSAEVDGGGDGSDTWTMGEEETTESQDEAASRNGENSDDEASLEST
Protein: Lipopolysaccharide glucosyltransferase WaaO (EC 2.4.1.73) (Lipopolysaccharide alpha-1,3 glucosyltransferase) (Lipopolysaccharide glucosyltransferase II) (P27128)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Lipopolysaccharide 1,6-galactosyltransferase
- Lipopolysaccharide core heptose
- Lipopolysaccharide glucosyltransferase WaaG
- Lipopolysaccharide core heptose
- Lipopolysaccharide core biosynthesis protein WaaS
- Lipopolysaccharide 1,2-glucosyltransferase
- Putative lipopolysaccharide heptosyltransferase 4
- Probable 3-deoxy-manno-octulosonic acid transferase
- Lipopolysaccharide heptosyltransferase 3
- O-antigen ligase
Sequence:
MQQVFFQETEFLNSVIDYDHKVETENLCLDIAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQYKTRIKIYLINGDRLRSLPSTKNWTHAIYFRFVIADYFINKAPKVLYLDADIICQGTIEPLINFSFPDDKVAMVVTEGQADWWEKRAHSLGVAGIAKGYFNSGFLLINTAQWAAQQVSARAIAMLNEPEIIKKITHPDQDVLNMLLADKLIFADIKYNTQFSLNYQLKESFINPVTNDTIFIHYIGPTKPWHDWAWDYPVSQAFMEAKNASPWKNTALLKPNNSNQLRYSAKHMLKKHRYLKGFSNYLFYFIEKIKH
Protein: Interferon, alpha-inducible protein 27 (A0A8I5ZTN9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
GLEGTGTPKPISSSHLHHWVWLLSGTHTGPHGIVWHRYAGGFYCLQGGIFSGRGQSRRGGIQHHPSWLNLLAQTALGSGASALGSALGALKAGTVLSSLPASALAVCPIGVKTAVAMLGGAMTVAAVPPVLSAVGFTGSGIAASSLAAKLMSVSAIANGGGVPAGGLVATLQSAGAAGLSMTSKVLVGSTGSAVVASVMGVCKHLYSFL
Protein: Ribulokinase (EC 2.7.1.16) (P08204)
Organism: Escherichia coli (strain K12)
Interaction partners:
- L-arabinose isomerase
- L-ribulose-5-phosphate 4-epimerase AraD
- L-ribulose-5-phosphate 4-epimerase SgbE
- L-ribulose-5-phosphate 4-epimerase UlaF
- L-Rhamnulokinase
- Rhamnulose-1-phosphate aldolase
- Arabinose-proton symporter
- Ribulose-phosphate 3-epimerase
- Arabinose operon regulatory protein
- Xylose isomerase
Sequence:
MAIAIGLDFGSDSVRALAVDCATGEEIATSVEWYPRWQKGQFCDAPNNQFRHHPRDYIESMEAALKTVLAELSVEQRAAVVGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEAEEITRLCHAPGNVDYSRYIGGIYSSEWFWAKILHVTRQDSAVAQSAASWIELCDWVPALLSGTTRPQDIRRGRCSAGHKSLWHESWGGLPPASFFDELDPILNRHLPSPLFTDTWTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGAQPNALVKVIGTSTCDILIADKQSVGERAVKGICGQVDGSVVPGFIGLEAGQSAFGDIYAWFGRVLGWPLEQLAAQHPELKTQINASQKQLLPALTEAWAKNPSLDHLPVVLDWFNGRRTPNANQRLKGVITDLNLATDAPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARKNQVIMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASAVEKTLQPCSEQAQRFEQLYRRYQQWAMSAEQHYLPTSAPAQAAQAVATL
Protein: Tegument protein VP22 (P30022)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Function: Tegument protein that plays different roles during the time course of infection (By similarity). Participates in both the accumulation of viral mRNAs and viral protein translation at late time of infection (By similarity). Modulates the RNase activity of the virion host shutoff protein UL41 probably to ensure necessary levels of key cellular mRNAs and proteins (By similarity). Plays a role in microtubule reorganization that occurs after viral infection by stabilizing microtubule network (By similarity). Plays a role in the inhibition of host innate immune system by targeting the CGAS enzymatic activity which is the principal cytosolic DNA sensor that detects invading viral DNA. Acts by mediating disruption of liquid-like droplets in which CGAS is activated, thereby preventing CGAS activity (By similarity).
Subcellular location: Virion tegument {ECO:0000250|UniProtKB:P10233}. Host cytoplasm {ECO:0000269|PubMed:16140763}. Host nucleus {ECO:0000269|PubMed:16140763}. Host Golgi apparatus {ECO:0000250|UniProtKB:P10233}. Note=One of the most abundant tegument protein (about 2000 copies per virion). Localizes in the cytoplasm at 8 hours postinfection and in the nucleus at 16 hours postinfection. During virion morphogenesis, this protein probably accumulates at the trans-Golgi where secondary envelopment occurs. {ECO:0000250|UniProtKB:P10233}.
Interaction partners:
Sequence:
MARFHRPSEDEDDYEYSDLWVRENSLYDYESGSDDHVYEELRAATSGPEPSGRRASVRACASAAAVQPAARGRDRAAAAGTTVAAPAAAPARRSSSRASSRPPRAAADPPVLRPATRGSSGGAGAVAVGPPRPRAPPGANAVASGRPLAFSAAPKTPKAPWCGPTHAYNRTIFCEAVALVAAEYARQAAASVWDSDPPKSNERLDRMLKSAAIRILVCEGSGLLAAANDILAARAQRPAARGSTSGGESRLRGERARP
Protein: Deneddylase (Q84TH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ubiquitin-NEDD8-like protein RUB1
- At1g28540
- COP9 signalosome complex subunit 8
- NEDD8-specific protease 1
- NEDD8-like protein RUB3
- Cullin-1
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 6a
- Cullin-4
Sequence:
MASISTASSSSSLLFPSRNFKSIPLLPQQRSSVSFVRCFSKNSSTEEDILRFVAESDGKALPCVRTYENNSARLSLVGTVAFDQALTAAAADGGEAADDHLRENVPVMVVETVFPGGSDPKATVSTRLFLPTKKVKERAKRLRRSLSEDLSSGDLSKNILAMTFRQVVLRQLWNFQLVLFAPGAEREMGDFENPREQVSTSFTLSSSDERVISVIAEVICISALQSTEKHFLDDYLGKAKFPFMKWLSKRRRIASRDCSVVLHKLFDDEQNTKLLLEYYQSRKENFKLADTKQRSRWWDLSANSKLEKIGGPGFSSWASEYLPAYRLEMDSTILADLKLEGWRKSSENKWEVLLTHSQMVGLAEALDIYFEDTYSLPRKQLPCDVPGNYANLPNEKKGLSLLKFISVTMASGIFLLAVSAAAQFCLPQKSERKYPGKRQEILWSESELLSHQSSDSSELDSFCGLLVNKLKDAYSWVGEITLESSIGAWIGEVPDYLKETSRAKSVEDHIVTSSSLLEILNEDAKASAQDIATYQVVLSSEGKIIGFQPTSRVAVNHWAANPLARELYGGKKLKPGLIEPGLKSHPPKKVVVLELLMSVNSDRPFALVRPLLPQ