wanglab/gogpt-training-data huggingface dataset:
Protein: Protein XAP5 CIRCADIAN TIMEKEEPER (Q8H110)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in light regulation of the circadian clock and photomorphogenesis. May play a global role in coordinating growth in response to the light environment. Acts as a light quality sensor directing both negative and positive transcriptional regulation. Inhibits growth in red light but promote growth in blue light. Inhibits clock gene expression in diurnal cycles. Plays no role in the control of flowering time.
Subcellular location: Nucleus {ECO:0000269|PubMed:18515502}.
Interaction partners:
- Regulator of nonsense transcripts UPF3
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- Putative defensin-like protein 12
- AT4g02720/T10P11_1
- Protein COP1 SUPPRESSOR 2
- Serrate RNA effector molecule
- Expressed protein
- 7-dehydrocholesterol reductase-like protein
- At3g05070
- At4g01000
Sequence:
MSGMGDGYVGTAQDAVRIRRLQKQREAERKKIQELKSKSASGNDQSGLLQFGTSSCEILDTAFKKETVGLVTREEYVEKRVNIRNKFEEEEKEKLQKLQQEEEELQLEKRNKKRKIKGSSRLSFAEDFENGSDEDDGENKSSGTGNLRCGKLGKDPSVETNFLPDSEREAEEQAERERLKKQWLREQEQIKNEPLEITYSYWDGTGHRRVIQVRKGDPIGNFLRAVQQQLAPDFREIRTASVENLLYVKEDLIIPHQHSFYELIINKARGKSGPLFHFDVHEDVRTIADATIEKDESHAGKVVERHWYEKNKHIFPASRWEIYDPTKKWERYTVHGD
Protein: Small ribosomal subunit protein mS26 (O60169)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MISRCIKRCYRSGYMIFPPNRLQSTIRSKEEINSSRHKFNIADTSVRKQYNEELVFTKDAKENAEAKKVSSKVKKDRKNHSAAMEGVNINVPGIYRDVYPLPNEDVEMHEAKKKENICKKENLSKTVLVRQLAEIYFANSNKYVVDENGLDDLIQQAFKNPNDVFQPLPSKRDGDNMRLFIETEEEADMTSIKQHAIEVVLQDFQEEQPLEDKRDTIE
Protein: Interleukin-27 subunit beta (IL-27 subunit beta) (IL-27B) (Epstein-Barr virus-induced gene 3 protein homolog) (O35228)
Organism: Mus musculus (Mouse)
Function: Associates with IL27 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q14213}.
Interaction partners:
- Interleukin-27 subunit alpha
- Interleukin-12 subunit alpha
- Interleukin-27 receptor subunit alpha
- Interleukin-6 receptor subunit beta
- Calnexin
- Interleukin-23 subunit alpha
- Interleukin-12 receptor subunit beta-2
- Interleukin-6
- Signal transducer and activator of transcription 1
Sequence:
MSKLLFLSLALWASRSPGYTETALVALSQPRVQCHASRYPVAVDCSWTPLQAPNSTRSTSFIATYRLGVATQQQSQPCLQRSPQASRCTIPDVHLFSTVPYMLNVTAVHPGGASSSLLAFVAERIIKPDPPEGVRLRTAGQRLQVLWHPPASWPFPDIFSLKYRLRYRRRGASHFRQVGPIEATTFTLRNSKPHAKYCIQVSAQDLTDYGKPSDWSLPGQVESAPHKP
Protein: tRNA pseudouridine(55) synthase (EC 5.4.99.25) (Q0WVR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 2-like protein
- H/ACA ribonucleoprotein complex subunit 3-like protein
- Putative H/ACA ribonucleoprotein complex subunit 1-like protein 1
- H/ACA ribonucleoprotein complex subunit 1-like protein 2
- Nucleolar protein 56
- Nucleolar protein 56
- Probable ribosome-binding factor A
- Ribosomal protein L7Ae/L30e/S12e/Gadd45 family protein
- At4g01790
- At4g22380
Sequence:
MAKSLHFTRLMSSSARMSMTSPLFFSSVKPWRNIHKPYLASLFLSTTSTRYPLQYDMIINRPTQSSLSQNRRRPPKAIESGAPDSAEPEFDSWVDNKLAMEREQGRPGSGDPEMDKAKRKYYSKRRKRLYGSDSEDENSSRKSDEGFVELKPEVVEFDRLHQREEELYFYDTFAYPWEKDKHYKMVYQLEKKYYPDQCLDKAFLQPGEVLKKSDDSGKVRGKKKVVAALGGKRSEVKRIGMENCDEDDDKLVFFDEVKEKEEKKKSEDDVVVVTEKKVEQFFKGLTKSPNEKGMASGGGDGEPFLVTRNGELPPRWDGPNGTVLLVNKPKGWTSFTVCGKLRRLVKVKKVGHAGTLDPMATGLLIVCVGKATKVVDRYQGMIKGYSGVFRLGEATSTLDADSPVIQRESWEHIKDDDIKKALTSFLGEIWQVPPMFSAIKVGGEKMYEKARRGETVELSPRRISIFQFDIERSLDDRQNLIFRVICSKGTYIRSLCADLAKALGSCAHLTALRRDSIGEYSANDAWEFNELEAAITKNYF
Protein: BTB/POZ domain-containing protein At1g55760 (Q680K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- RING-type E3 ubiquitin transferase
- Protein kinase superfamily protein
- Probable protein phosphatase 2C 43
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Subtilisin-like protease
- Vacuolar-sorting receptor 4
Sequence:
MTDSAYRVDTISRLAQWRIHNLSSSTYRKSDPFKMGLWNWHLSVEKSKMLLNVKLYPEVSNLTRENPPVASFALRVVSSTGERKALSHPEVIDKRIKTNEDFIWTIEVPLTGKIIIDVEFLDLKVLSQDSGELYSIWANGSTENQSQVTAVTSLGRMLTESIYTDITINASDGSIGAHRAVLAARSPVFRSMFLHDLKEKELSEINVLDMPLDACQAFLSYIYGNIQNEDFLIHRLALLQAAEKYDIADLKEACHLSLLDDIDTKNVLERLQNAYLYQLPELKASCMRYLVKFGKIFEIRDEFNIFMQCADRDLISEIFHEVLSTWKGF
Protein: Protein mago nashi homolog (AtMAGO) (O23676)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGO-Y14 heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading to EJC disassembly in the cytoplasm (By similarity). Can increase in vitro the expression from reporter constructs that contain leader introns required for the expression of different genes. In association with MAGO and PYM, participates in intron-mediated enhancement of gene expression. The MAGO-Y14 heterodimer works synergistically with the NMD pathway to regulate male gametophyte development.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:19435936}. Nucleus speckle {ECO:0000269|PubMed:19435936}. Nucleus {ECO:0000269|PubMed:26867216}. Cytoplasm, P-body {ECO:0000269|PubMed:26867216}. Cytoplasm {ECO:0000250|UniProtKB:P61326}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:P61326}.
Interaction partners:
- RNA-binding protein Y14
- CASC3/Barentsz eIF4AIII binding protein
- Eukaryotic initiation factor 4A-III homolog
- Partner of Y14 and mago
- Regulator of nonsense transcripts UPF3
- THO complex subunit 4A
- THO complex subunit 4B
- THO complex subunit 4D
- THO complex subunit 4C
- Eukaryotic initiation factor 4A-1
Sequence:
MAAEEATEFYLRYYVGHKGKFGHEFLEFEFREDGKLRYANNSNYKNDTIIRKEVFLTPAVLKECKRIVSESEILKEDDNNWPEPDRVGKQELEIVLGNEHISFATSKIGSLVDCQSSNDPEGLRIFYYLVQDLKCLVFSLISLHFKIKPI
Protein: Polyadenylate-binding protein-interacting protein 2B (PABP-interacting protein 2B) (PAIP-2B) (Poly(A)-binding protein-interacting protein 2B) (Q9ULR5)
Organism: Homo sapiens (Human)
Function: Inhibits translation of capped and polyadenylated mRNAs by displacing PABPC1 from the poly(A) tail.
Interaction partners:
- Polyadenylate-binding protein 1
- Sodium/potassium-transporting ATPase subunit beta-3
- Polyadenylate-binding protein-interacting protein 1
- Adenylate cyclase type 6
- Excitatory amino acid transporter 3
Sequence:
MNGSNMANTSPSVKSKEDQGLSGHDEKENPFAEYMWMENEEDFNRQVEEELQEQDFLDRCFQEMLDEEDQDWFIPSRDLPQAMGQLQQQLNGLSVSEGHDSEDILSKSNLNPDAKEFIPGEKY
Protein: Arginine-hydroxylase NDUFAF5, mitochondrial (EC 1.-.-.-) (NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 5) (Putative methyltransferase NDUFAF5) (EC 2.1.1.-) (Q54JW0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1) at early stages. Probably acts as an arginine hydroxylase (By similarity). May also have methyltransferase activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23536703}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase iron-sulfur protein 7
- Iron-sulfur cluster transfer protein NUBPL
- NADH-ubiquinone oxidoreductase subunit 9
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH-ubiquinone oxidoreductase 49 kDa subunit
- NADH-ubiquinone oxidoreductase 23 kDa subunit
- Acyl carrier protein, mitochondrial
- V-type proton ATPase subunit d
- NADH dehydrogenase 1 alpha subcomplex subunit 13
Sequence:
MLRTTFRKGFNLKCFSKDWNQTRQYSNYTKMTIFDTNVKTIQKNNTVTNVDDPKHYDYLMNEVADRLADRILDIKDIKCGNVLDFGSRNGALFKYIQEKGAKIDKYYMVESSKELLYRDDNNVSQENEDDNNNNKVKPTKILVNSLEDKIEGIEDQSLDLIISNLSLHWVNDLPGVFGGLKRLLKPNGVFLASLFGEDTLMELKDSLYLAEIEREGGFSPHVSPFTKISDIGNILSKNRYTLPTVDTEKITINYDNMFVLMRDLQNMGENNAILKRRNYTSKDTFLAASAIYKHLYGNEDNNSIPATFQIIYLIGWAPHESQQKPLQRGSAKKHFSEISGTSSFGYKFDNDSSIPSILTNENNSVTLSQQQQQQGIEPQQSNDDSINEPFPKTDDFVIKRLDYHGNFHFEKQQQQQQQQDQNKESSDEINKNKDDK
Protein: 1,3-beta-glucan synthase component bgs1 (EC 2.4.1.34) (1,3-beta-D-glucan-UDP glucosyltransferase) (Q10287)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS) complex (By similarity). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall (By similarity). Required for the assembly of the division septum and maintenance of cell polarity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15615781}; Multi-pass membrane protein {ECO:0000255}. Cell septum {ECO:0000269|PubMed:15615781}. Note=Localizes to actively growing cell ends. Following nuclear division, relocalizes to the future site of cell division. {ECO:0000269|PubMed:15615781}.
Interaction partners:
- Cell division control protein 15
- Uncharacterized protein P22H7.03
- LIM domain-containing protein C4F6.12
- Glucan 1,3-beta-glucosidase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Cell wall alpha-1,3-glucan synthase ags1
- Glucan 1,3-beta-glucosidase 1
- Glucan 1,3-beta-glucosidase 2
- Myosin regulatory light chain 1
Sequence:
MDQYWREQEGRGLFEDDANSYVSDDDTMSSLTRMIYDKNSSRDALHSDYDSSSFNVDSSSVAYPAWNQAGEEAPVTMEGVQEILLDLTNKLGFQKDNMRNIFDYVMVLLDSRASRMSPSSALLTIHADVIGGEHANFSKWYFASHFNDGHAIGFHDMSSPIVETMTLKEAEQAWRDQMAAFSPHRMMVQVCLYFLCWGEANNVRFVPECLCFIFECAYDYYISSEAKDVDAALPKEFYLDSVITPIYRFIHAQLFEILDGKYVRRERDHSQIIGYDDINQLFWSYKGLQEIMCADKTPLLDLPPFMRYRHLSDVEWKSCFYKSYYEYRSWFHNVTNFSRIWVMHISAYWYYSAYNSPNLYTKNYHIRLNNKPPASCRWTACGLAGAIASFITLAAVVFEYIHVPRRYHSARRLWPSMLLLISTLLLNIAPVVFIFASSTKEQHYASRLVVGIVHFFFSLVCVVYYSITPLRNLVGFTTKRSGKNLANRFFTANFTPTSKTGAFVSWCLWITVLVAKFLESYFFLTLNLADSIRFLGAMRPYDCRDYILGAGLCKAQPKILLSLLYLTDLSLFFLDTYLWYILISTIYSLAYAFCLGISVWTPWRELFYRVPRRIYTKLLYTDDMEIVFKPKVLISQVWNAIIISMYREHLISRTQIQELLYHQVPSEKAGYHTLRAPNFFYSQQVKHYKQDLFPANSEAARRISFFAQSLAESIPKTSSIDAMPTFTVLVPHYSEKILLSLREIIREEDQLSRVTLLEYLKQLYPVEWRNFVDDTKLLADENDSVIGSIDNEKNGVNKAYDLPFYCVGFKSATPEYTLRTRIWASLRTQTLYRTINGFSNYSRAIKLLYRTETPELVEWTNGDPVRLDEELDLMANRKFRFCVSMQRYAKFTKEEAENAEFLLRAYPDLQIAYMDEDPQSRHNDERHLYSVLIDGHCPIMENGKRRPKYRIRLSGNPILGDGKSDNQNMSIPYIRGEYVQMIDANQDNYLEECLKIRSILAEFEQLTPPLHSPYSVNAKAADNHPVAILGAREYIFSENTGMLGDVAAGKEQTFGTLFARILSLIGGKLHYGHPDFINVLFMITRGGVSKAQKGLHVNEDIYAGMIALQRGGRIKHCDYYQCGKGRDLGFGSILNFTTKIGTGMAEQMLSREYFNLGTQLPFDRFLSFFYAHAGFHVNNMVIMFSLQLLMLVIINLGAMYTVVPVCRYRQFDSLTASLYPEGCYQLKPVLEWLKRCILSIFIVFGIAFVPLAVCELGERGAIRMVIRLAKQIFSLSPIFEIFTCQIYAQSLIANLTFGGARYIGTSRGFATVRVPFSLLYSRFSGPSLYFGSRLMYMLLFGSITAWLPHYIYFWITLTALCISPFLYNPHQFAWTDFFVDYREFMRWLFRENSRNQANSWIGNCQLCRTRVTGYKRKIYGKKADKIAMDSPRARITTMFYGEILGPLGTLFFTCIPFLFINSQPGNDDETQSTNAFIRLIIMSVAPLVLSAIIAFFFFCLGIMLRPILGDRSKTYGVYLAGVAHFLFVCVDVVVFEVLGYLEGWSFSKTLLGFVAIISIHRFAHKFFIICFLSREFRHDGANLAWWSGRWNGQGFGYMVLTQPWREFVCKTTELNMFAGDFLLSHLLLFLQAPVILIPYIDKLHSIILFWLVPSRQIRPPIYTIRQNKLRRQIVLRYATLYFSLFIAFFVLLILPFVFGKSAAGTSMDKFNLIQPATKIVYSSTKNSSV
Protein: Profilin (A9P7F0)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- actin
- Actin
- Actin
- Actin
- Actin depolymerizing factor 7
- Actin-depolymerizing factor
- Actin-depolymerizing factor 2-like
Sequence:
MSWQTYVDEHLMCDIDGTGHHLSAAAIVGHDGSIWAQSSNFPKCQPKEITDIMKDFDEPGHLAPTGLHLGGAKFMVIQGEPGAVIRGKKGSGGVTIKKTAQALVFGIYEEPVTPGQCNMVVERLGDYLAEQGL
Protein: Renin receptor (ATPase H(+)-transporting lysosomal accessory protein 2) (ATPase H(+)-transporting lysosomal-interacting protein 2) (Renin/prorenin receptor) (A0A286YA30)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, dendritic spine membrane {ECO:0000256|ARBA:ARBA00029429}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00029429}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000256|ARBA:ARBA00029432}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00029432}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00029430}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00029430}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00029428}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00029428}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004352}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004352}.
Interaction partners:
Sequence:
MLLRHDARRHAAGPGHVTGVARKRSPSENRPEMNRIIMNAVFALIGLLSGVLGDSLTVLRSPQYVTFRDEQWPISGEKIPDLVALTMGFSVREDLDWPGLAAGSLFQRPRANALIVVRGIDSLDFPKNVSSYPLENPVPFTLDSVANTIHTLFADSTPVVLQLAPSEERLYMMGMANTVFEDLPVTLQQIRGRLSQDGSVLTSLPLVSLSRNNEADLLFLSEVQVLYDISALLQKHKHLAKDPAPDLYSLELAGLEEIVRRYGTDSPQYTDAIRILTIALQKFADDVSSVYGNNAVVEVVTVKTFEVPLTRKSRSILESKQMGSRRTNRFKNVPSNPGSPYNLAYKYNFDYAVIFNIVLWLMIVLALAVIAISYNLWNMDPGYDSIIYRMTNQKIRLD
Protein: Exo-beta-1,3-glucanase (EC 3.2.1.58) (Glucan 1,3-beta-glucosidase) (Laminarinase) (SacteLam55A) (G2NFJ9)
Organism: Streptomyces sp. (strain SirexAA-E / ActE)
Function: Exo-beta-1,3-glucanase that specifically hydrolyzes laminarin and laminarioligosaccharides, producing glucose and laminaribiose as end products.
Subcellular location: Secreted {ECO:0000269|PubMed:23301151}.
Interaction partners:
- Coagulation factor 5/8 type domain protein
- chitinase
Sequence:
MHVPPTDPARSAPPASPHRRRRPKALGLTALAAAMLMAVPTTQAAFGSDVRPAAAQEVVGGGDLGPNVLVFDPSTPDIQGKVDEVFRKQESNQFGTDRYALMFKPGTYNDINAQIGFYTSIAGLGLNPDDTTFNGDVTVDAGWFDGNATQNFWRSAENLALNPVNGTNRWAVSQAAPFRRMHVKGGLNLAPDGYGWASGGYIADSKIDGEVGPYSQQQWYTRDSSVGGWGNGVWNMTFSGVEGAPAQSFPEPPYTTLETTPVSREKPFLYLDGDDYKVFVPAKRTNARGTSWGNGTPEGESLPLDQFYVVKPGATAETINAAVDQGLHLLFTPGVYHVDQPIEIDRANTVALGLGLATIIPDNGVTALKVGDVDGVKVAGLLVDAGPVNSETLVEVGSDGASGDHAANPTSLQDVFVRIGGAGPGKATTSIVVNSNDTIIDHTWVWRADHGEGVGWETNRADYGVHVKGDNVLATGLFVEHFNKYDVQWSGENGKTIFYQNEKAYDAPDQAAIQNGDIKGYAAYKVDDSVTTHEGWGMGSYCYFNVNPDIRQQHGFQAPVKPGVKFHDLLVVSLGGKGQYEHVINDIGDPTSGDTTIPSQVVSFP
Protein: Aminoglycoside N(6')-acetyltransferase type 1 (EC 2.3.1.82) (AAC(6')-Il) (Aminoglycoside resistance protein) (P50858)
Organism: Klebsiella aerogenes (Enterobacter aerogenes)
Function: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin.
Interaction partners:
Sequence:
MDSSPLVRPVETTDSASWLSMRCELWPDGTCQEHQSEIAEFLSGKVARPAAVLIAVAPDGEALGFAELSIRPYAEECYSGNVAFLEGWYVVPSARRQGVGVALVKAAEHWARGRGCTEFASDTQLTNSASTSAHLAAGFTEVAQVRCFRKPL
Protein: Branched-chain amino acid ABC transporter, permease protein (Q5LNB8)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid binding protein, putative
- AMP-binding enzyme
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, permease/ATP-binding protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Phenylacetate-CoA ligase, putative
- Branched-chain amino acid ABC transporter, permease protein
Sequence:
MSDQLIFGIEVILNGLMAGVLYALVALGFVLIYKASGIFNYAQGVMALFAAMTLVGIMNGQVPFSHLINAVFGGHITHFGWNVPGFVAILLTMAVMVLLAWAVQQFVMRHLVGQEPIILFMATIGLAYFLEGVADLMWGSEIKTLDVGLPQGLNVWIDDTTYGIFGYGFFIDNLDIVATVIAALLVAALVAFSQYTKQGRAMRAVADDHQAALSVGISLNFIWVLVWSVAGFVALVAGIMWGTKSGVQFSLSLIALKALPVLMLGGFTSIPGAIVGGLIIGVGEKLFEFAIGPMVGGATENWFAYVLALIFLVFRPQGLFGEKIIERV
Protein: M phase phosphoprotein 10 (AtMPP10) (U3 small nucleolar ribonucleoprotein protein MPP10) (Q9FJY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus, nucleolus {ECO:0000269|PubMed:27792779}.
Interaction partners:
- U3 small nucleolar ribonucleoprotein protein IMP3
- Putative U3 small nucleolar ribonucleoprotein
- AT3g56990/F24I3_70
- At4g28200
- Nucleolar-like protein
- Protein NUCLEOLAR FACTOR 1
- Periodic tryptophan protein 2
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
- KRR1 small subunit processome component
- Putative WD-repeat membrane protein
Sequence:
MATVKDSGFEALEKLKATEPPVFLAPSSISEDARSASQYLFMKLKPHNPKCPFDQLSSDGFDAEQIWQQIDMQSQPLLTSLRQEVKRFAKNPEEIRKLGKLALKVSHEDDIDEMDMDGFDSDDVDDEDKEIESNDSEGEDEEEEEEDEEEEEEEEEEEEEEKDGDNEGIEDKFFKIKELEEFLEEGEAEEYGIDHKNKKGVAQRKKQNLSDDEDEEDDDDEEEDVEFDAFAGGDDEETDKLGKARYDDFFGGKKETKMKLKDLSEDEEAEIENKGNEKLSTHERARLKLQSKIEQMEKANLDPKHWTMQGEITAAKRPMNSALEVDLDFEHNARPAPVITEEVTASLEDLIKSRIIEARFDDVQRAPRLPTKGKREAKELDESKSKKGLAEVYEAEYFQKANPAFAPTTHSDELKKEASMLFKKLCLKLDALSHFHFTPKPVIEEMSIPNVSAIAMEEVAPVAVSDAAMLAPEEIFSGKGDIKDESELTQEDRKRRRANKKRKFKAESANEPPKKALDTSTKNP
Protein: Protein BEX6 (Brain-expressed X-linked protein 6 homolog) (Q3TZW7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15958283}.
Interaction partners:
Sequence:
MMSKVKQVIQDLTVEKDKGGEASRHSEEESHLLEEVETKNPGGYVKRKVRRLVCNFRWPTPNRHVDHSEGREDAGRFVGQETEAKRKSQEQWMRFSKWFLTPESDSHYNLGLIP
Protein: Ornithine carbamoyltransferase, mitochondrial (EC 2.1.3.3) (Ornithine transcarbamylase) (OTCase) (P31317)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ornithine carbamoyltransferase involved in the synthesis of arginine from glutamate via ornithine and the urea cycle.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:1313366, ECO:0000305|PubMed:18849471}.
Interaction partners:
- Argininosuccinate synthase
- Protein arg11
- Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial
- Arginine biosynthesis bifunctional protein ArgJ
- Arginase
- Arginase
- Probable acetylornithine aminotransferase, mitochondrial
- Ornithine aminotransferase car2
- Multifunctional protein ura1
- Carbamoyl phosphate synthase arginine-specific small chain
Sequence:
MSFKKFPRHLLSIRDLSRGEIVKLIDRSSEIKQAYKQNFQNRRSVQMSGLSSQNVAMIFSKRSTRTRVSVESAVSCLGGNAMFLGKDDIQLGVNESLYDTSKVISSMVSGIVARVNKYSDVATLAKHASCPVINGLCDTFHPLQALADLLTIKETFKSFDGLKVAWVGDANNVLHDLMIANAKVGIHTSVAKPKDVNVRDDILSIVNEAANENGSTFEIVNDPKVAVKNADIVVTDTWISMGQEAEKEQRLKQFTGFQVTGEIMKLAKPSCKFMHCLPRHPEEVSDEVFYGENSLVFQEAENRKWTTVAVLEALLVNRGEILPPASA
Protein: Dual specificity protein phosphatase, putative (Q586U9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGAALCTDVVPFTLDDIILIPQRVSKSHLAYDVSPVAVDHFSKFQNNLKAFTFRHRDSSASVNGAAARFDPSHVSALPMDLSQAKIELDDTRVYVLVQVQRQPVSPRNAPTGKATLGSPNMFTPRTLEYPLKDCDMNWRWNDVSPSWASVLSDVFTPRGLATPFSTNIGKPPASLSHAGARLFSRGAGCGTECGDGYNYYYSIYILNGVRAHPSLAAVAAVHAGRLEQALINSKETLQCLFFNCNPSRGEKEAAACGREDSLCASIGDVVGSRRPSRRTSFMGEEYQRNAILRSLLSLRKPAPTASVLGTTPTGGRSQENSSRGKSKRQEGAVLYSFEQYQQQKLKGDPLPLPTTKLSNCLIPPITGARPDVENSARKLPPLETIRSKQSVTDAGGAVKESPLPFTARFPNRTANSQVGSERGPSSAASPCLTPKSSSFMSPRFPVISALRLDGALRQQAGDGGLNDSQINPEHDEIRITEEKLQKLKALSPEATEILPWLFVGGEEAARDRSQLLAKGITSVVNTVAFSIENAHEDIFSYLRLNVSDSPDEPIFSLFPVVNQYIEEARLNGGKTFVHCHQGVSRSCSFVIAYVMWYEGLCYEKAYDYVRARRTVCSPNPGFYVSLLLWQDQLARPVLDKAYAYVPYPDYLFPFSYRLALVFRRQKEQQNGSEEGVHIMNQSVRVLDDKCDEFAMDPRLCYGFLLSGCPTPGGSQEPCTVSHFFVGPECAPAIGQQAKEEWEKFVKYSFYHGAVKTTVNNKGECITYTPLPPLQHPVECLLTPAEVVSAVDSNVYKRGETSCGTLRRLTITLVHDSCWDSLLSRSDMVELFTKYVAEVKQQKQAMSGHKRLREKEQQRDLGKLDVGKSKSAPTPREPTGRSFAASSARVGSHRSLQPRRNEPIEHTVESYQEEKNEGVAEREAGGTTPVSHEMEIFAYPFTGTPVRDIIDATDMEAERAYVIILPRSSSGFEQDGRSSPSHRVFIWIGSRCGIEADEAMDAYRASLKSGNDVRLATGAVLKNPVEEVVYDGEEPDELLLALD
Protein: Esterase dbaE (EC 3.1.2.-) (Derivative of benzaldehyde biosynthesis cluster protein E) (Q5AUY1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Esterase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives. The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step. The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA. The roles of dbaB, C, E and F have still to be determined (Probable).
Interaction partners:
Sequence:
MTIRIPSGEEADYTLHLPRILCLHGGGTNARIFRMQCRVLERFLRSTFRFVYAEAPFAAQPGSDVTSVYKDHGPFKAWLRCTAADPDRSAQEVVKKINLSIATAMYDDDMRGATGEWIALLGFSQGAKVAASILYAQQTIQQRLGERAATRPRFRFAVLMAGRGPLVWLLPETSSGPGSIPMGLVDAASPSMLDSEPELPTDSTEHMLRLPTLHVHGLRDPGLSLHRRLLRSYCQSDSVSLVEWEGEHRVPLKTKDVTAVVDQIYALARDTGVLDSWC
Protein: Cell cycle associated protein 1 (GPI-anchored membrane protein 1, isoform CRA_d) (G3V153)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDEVRTDLKQGLNGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKVLKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPAVEDQVPEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFTSGEKEQVDEWTVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQADPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPPVHSESRLAQPNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHATEQRPQKEPIDQIQATISLNTDQTTASSSLPAASQPQVFQAGTSKPLHSSGINVNAAPFQSMQTVFNMNAPVPPVNEPETLKQQNQYQASYNQSFSSQPHQVEQTELQQEQLQTVVGTYHGSPDQSHQVTGNHQQPPQQNTGFPRSNQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRPSFSNTPNSGYTQSQFSAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN