wanglab/gogpt-training-data huggingface dataset:
Protein: Putative 2-dehydro-3-deoxy-D-gluconate aldolase YagE (KDG aldolase YagE) (EC 4.1.2.51) (Putative 2-dehydro-3-deoxy-D-pentonate aldolase YagE) (EC 4.1.2.28) (P75682)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of 2-keto-3-deoxy-gluconate (KDG) from pyruvate and glyceraldehyde. May also function as a 2-dehydro-3-deoxy-D-pentonate aldolase. Overexpression leads to increased growth (over 2 hours) in the presence of the antibiotics norfloxacin, ampicillin and streptomycin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- D-xylonate dehydratase YagF
- D-xylonate dehydratase YjhG
- Probable 2-dehydro-3-deoxy-D-pentonate aldolase YjhH
- 4-hydroxy-tetrahydrodipicolinate reductase
- Lactaldehyde dehydrogenase
- Lactaldehyde reductase
- Glyoxylate/hydroxypyruvate reductase B
- Xylulose kinase
- Xylose isomerase
- Putative glycoside/cation symporter YagG
Sequence:
MPQSALFTGIIPPVSTIFTADGQLDKPGTAALIDDLIKAGVDGLFFLGSGGEFSQLGAEERKAIARFAIDHVDRRVPVLIGTGGTNARETIELSQHAQQAGADGIVVINPYYWKVSEANLIRYFEQVADSVTLPVMLYNFPALTGQDLTPALVKTLADSRSNIIGIKDTIDSVAHLRSMIHTVKGAHPHFTVLCGYDDHLFNTLLLGGDGAISASGNFAPQVSVNLLKAWRDGDVAKAAGYHQTLLQIPQMYQLDTPFVNVIKEAIVLCGRPVSTHVLPPASPLDEPRKAQLKTLLQQLKLC
Protein: Endoribonuclease Dicer homolog 4 (EC 3.1.26.-) (Dicer-like protein 4) (OsDCL4) (Protein SHOOT ORGANIZATION 1) (A7LFZ6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the RNA silencing pathway. Cleaves double-stranded RNA to produce small interfering RNAs (siRNAs) which target the selective destruction of complementary RNAs. Required for the production of 21 nucleotide siRNAs. Regulates shoot apical meristem (SAM) initiation and maintenance, leaf polarization and lemma polarity through the trans-acting siRNAS (ta-siRNAs) pathway, which probably modulate the expression of the ARF2, ARF3, ARF4, ARF14 and ARF15 genes. Can process endogenous 21 nucleotide siRNAs derived from an imperfect inverted repeat. May not be involved in microRNAs (miRNAs) production.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein argonaute 1C
- Protein argonaute 7
- Protein argonaute 2
- Large ribosomal subunit protein bL27c
- Os01g0220300 protein
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL33c
- Protein argonaute 18
- Os07g0658200 protein
- Small ribosomal subunit protein uS9c
Sequence:
MGDAAAAAPAAAAAGPSSTRGEPKDPRTIARKYQLDLCKRAVEENIIVYLGTGCGKTHIAVLLIYELGHLIRKPSREVCIFLAPTIPLVRQQAVVIASSTDFKVQCYYGNGKNSRDHQEWENDMREFEVLVMTPQILLQSLRHCFIKMNSIALLILDECHHAQPQKRHPYAQIMKEFYNSNSVEKFPRVFGMTASPIIGKGVMPSHSFTEKGGRSPCQPLIFFLPKGGSNKLNYTKCINSLEELLHAKVCSVDNEELESVVASPDMEVYFYGPVNHSNLTTICIKELDSLKLQSERMLRASLCDFKDSQKKLKSLWRLHENIIFCLQELGSFGALQAARTFLSFDGDKLDRREVDLNGSTSSFAHHYLNGATSILSRNKTDGSHAGSFDLEKLEEPFFSNKFSVLINVLSRYGLQENMKCIVFVKRITVARAISNILQNLKCLEFWKCEFLVGCHSGSKNMSRNKMDAIVQRFSSGEVNLLVATSVGEEGLDIQTCCLVVRFDLPETVASFIQSRGRARMTKSKYVVLLERENQSHEKLLNGYIAGESIMNEEIDSRTSNDMFDCLEENIYQVDNTGASISTACSVSLLHCYCDNLPRDMFFTPSPVFFYIDGIEGIICRLILPPNAAFRQADGQPCLSKDEAKRDACLKACVKLHKLGALTDFLLPGPGSRKNKVSVTNNSSNNKVEDDSLREELHEMLIPAVLKPSGLKLDSLSNLHFYYVKFIPIPEDRRYQMFGLFVINPLPVEAETLQVDLHLARGRIVKAGIKHLGKIAFEKEKMMLAHKFQEMCLKILLDRSEFTSPHVKLGNDVTLEINSTFYLLLPIKQKCYGDRFMIDWPAVERCLSSPIFKDPIDVSVHASYSSNESLRLLDGIFSKTDVVGSVVFSPHNNIFFFVDGILDEINAWSEHSGATYAEHFKERFRIELSHPEQPLLKAKQIFNLRNLLHNRLPETTESEGRELLEHFVELPPELCSLKVIGFSKDMGSSLSLLPSLMYRLENLLVAIELKDVMLSSFPEASQISASGILEALTTEKCLERISLERFEVLGDAFLKYVVGRHKFITYEGLDEGQLTRRRSDVVNNSHLYELSIRKKLQVYIRDQQFEPTQFFAPGRPCKVVCNTDVEVRLHQMDIHPDNRENCNLRCTRSHHWLHRKVIADVVESLIGAFLVEGGFKAAFAFLHWIGIDVDFNNPALYRVLDSSSINLSLMDYTDIAGLEELIGYKFKHKGLLLQAFVHPSFSQHSGGCYQRLEFLGDAVLEYVITSYLYSTYPDIKPGQITDLRSLAVGNDSLAYAAVEKSIHKHLIKDSNHLTSAISKFEMYVKLSNSEKDLLEEPACPKALGDIVESCIGAVLLDSGFNLNYVWKVMLMLLKPVLTFANMHTNPMRELRELCQCHGFELGLPKPMKADGEYHVKVEVNIKSKIIICTAANRNSKAARKFAAQETLSKLKNYGYKHRNKSLEEILIVARKRESELIGYNEDPIDVEADISVKMKSPHIHEENIPFQNTETSFTRSSKFHNQIIAGSGKHDVNNGRNNQPKLATQSGRLPSEATEKSNKKVYHGDMVHKTARSFLFELCAANYWKPPEFKLCKEEGPSHLRKFTYKVVVEIKGASATLLECHSDGKLQKKAAQEHAAQGALWCLKQLGHLPKEEDVRV
Protein: Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2 (EC 3.1.3.95) (Myotubularin-related protein 2) (Phosphatidylinositol-3-phosphate phosphatase) (D3ZA31)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004220}.
Interaction partners:
- FIG4 phosphoinositide 5-phosphatase.
- Myotubularin-related protein 12
- SET binding factor 1
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol-3-phosphatase SAC1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate-4-phosphatase type I A
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Inositol polyphosphate-5-phosphatase F
Sequence:
MEEPALLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNGLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKVNERYELCDTYPALLAVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATVTRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPKKTVSLWSYINSQLEDFTNPLFGSYSNHVLYPVASMRHLELWVGYYIRWNPRMKPQEPIHSRYKELLAKRTELQRKVEELQREISNRSTSSSERASSPAQCVTPVQTVV
Protein: Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (Macrophage membrane protein MFP150) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (CD antigen CD172a) (P97710)
Organism: Rattus norvegicus (Rat)
Function: Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function. Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Plays a role in antiviral immunity and limits new world arenavirus infection by decreasing virus internalization (By similarity). Receptor for THBS1. Interaction with THBS1 stimulates phosphorylation of SIRPA. In response to THBS1, involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Leukocyte surface antigen CD47
- Tyrosine-protein phosphatase non-receptor type 11
- Triggering receptor expressed on myeloid cells 2
- TYRO protein tyrosine kinase-binding protein
- Tyrosine-protein kinase SYK
- Proto-oncogene tyrosine-protein kinase Src
- OX-2 membrane glycoprotein
- Focal adhesion kinase 1
- Leukocyte surface antigen CD47
- B-cell antigen receptor complex-associated protein beta chain
Sequence:
MEPAGPAPGRLGPLLFCLLLSASCFCAGASGKELKVTQADKSVSVAAGDSATLNCTVSSLTPVGPIKWFKGEGQNRSPIYSFIGGEHFPRITNVSDATKRNNMDFSICISNVTPEDAGTYYCVKFQKGIVEPDTEIKSGGGTTLYVLAKPSSPEVSGPDSRGSPGQTVNFTCKSYGFSPRNITLKWLKDGKELSHLETTISSKSNVSYNISSTVSVKLSPEDIHSRVICEVAHVTLEGRPLNGTANFSNIIRVSPTLKITQQPLTPASQVNLTCQVQKFYPKALQLNWLENGNLSRTDKPEHFTDNRDGTYNYTSLFLVNSSAHREDVVFTCQVEHDSQPAITENHTVRAFAHSSSGGSMETIPDNNAYYNWNVFIGVGVACALLVVLLMAALYLLRIKQKKAKGSTSSTRLHEPEKNAREITQIQDTNDINDITYADLNLPKEKKPAPRVPEPNNHTEYASIETGKLPRPEDTLTYADLDMVHLNRAQPTPKPEPSFSEYASVQVQRK
Protein: V-type proton ATPase 21 kDa proteolipid subunit c'' (V-ATPase 21 kDa proteolipid subunit c'') (Vacuolar proton pump 21 kDa proteolipid subunit c'') (hATPL) (Q99437)
Organism: Homo sapiens (Human)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q2TA24}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit F
- Renin receptor
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit S1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 1
Sequence:
MTGLALLYSGVFVAFWACALAVGVCYTIFDLGFRFDVAWFLTETSPFMWSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVISNMAEPFSATDPKAIGHRNYHAGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQTSRVKMGD
Protein: Transketolase (EC 2.2.1.1) (C8VRQ4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Transaldolase
- Ribulose-phosphate 3-epimerase
- Transaldolase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Fructose-1,6-bisphosphatase
- Fructose-bisphosphate aldolase
- ATP-dependent 6-phosphofructokinase
- Ribose-5-phosphate isomerase
- Fructose-bisphosphate aldolase
Sequence:
MGYTELDQLAINTIRLLAVDATAKANSGHPGAPMGMAPVAHVLFNKFMKFNPKNPEWANRDRFVLSNGHGCMLQYALLHLFGYGISMDDLKAFRQLDSITPGHPEAHDTPGIEVTTGPLGQGFANAVGLAIAQAHSGGVFNKPGYNLFDNYTYCFFGDGCAMEGVASEAASTAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVTKRFEAYGWHVVWVKDGDNDLEGIEAAIKEAQAVKDKPSMIRLTTTIGFGSKLQGTGGVHGNPLKADDIEGVKKRFGFDPAQSFVVPQQVYDLYHKHAEEGAAQEQEWNQLLQKYAGEYPNEHADLTRRLSGKLPEGWEKSLPVYKPSDPAIASRKLSEAVLEKIHSVIPELLSGSADLTGSNNTRWKNAVDFQPPEYGIGEWSGRYLRYGVREHAMAAIMNGLAAYGTVIPAAGTFLNFVSYAAGAVRLSALSRVRAIHVATHDSIGLGEDGPTHQPIETLAHFRALPNCMVWRPADGNETSAAYYSALTAKHTPSILALTRQNLPQLENSSIEAALKGAYPVFEAADAKVTIISTGSEVSICIDAAKYLQEKHGVVARVVSIPCFEVFDAQDKEYRLKVLPDGIPILSVEVCSTMGWERYSHEQFGLNRFGASGPYKEVYAKFEFTPEGISKRALATIDFYKGVPVRSPINRAFQQIL
Protein: Signal transducing adapter molecule 2 (STAM-2) (Hrs-binding protein) (O88811)
Organism: Mus musculus (Mouse)
Function: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10651905, ECO:0000269|PubMed:12551915}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- STAM-binding protein
- Signal transducing adapter molecule 1
- Ubiquitin carboxyl-terminal hydrolase 8
- Tyrosine-protein kinase JAK3
- Tyrosine-protein kinase JAK2
- Tumor susceptibility gene 101 protein
- Non-receptor tyrosine-protein kinase TYK2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Tyrosine-protein phosphatase non-receptor type 23
Sequence:
MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDRVGSTPSGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRSVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGVTFPSAGSQTVAAAAKNGTSLNKNKEDEDIAKAIELSLQEQKQQYTETKALYPPAESQLNNKAARRVRALYDFEAVEDNELTFKHGELITVLDDSDANWWQGENHRGTGLFPSNFVTTDLSTEVETATVDKLNVIDDDVEEIKKSEPEPVYIDEGKMDRALQILQSIDPKESKPDSQDLLDLEDVCQQMGPMIDEKLEEIDRKHSELSELNVKVLEALDLYNKLVNEAPVYSVYSKLHPAHYPPAAAGVPVQTYPVQSHGGNYLGHGIHQVSVAQNYNLGPDPMGSLRSLPPNMNSVTAHTVQPPYLSTGQDTVSNPSYMNQSSRLQAAAGTAAYTQPVGMSTDVSSFQNTASGLPQLAGFPVAVPAPVAAQPQASYHQQPLL
Protein: Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I beta) (GSI beta) (Q3V5W6)
Organism: Pseudomonas taetrolens
Function: Catalyzes the formation of glutamine from glutamate and ammonia. In vitro, can also use hydroxylamine, methylamine and ethylamine, with 32%, 7% and 1% activity compared to ammonia, respectively.
Interaction partners:
- Glutamate synthase large chain
- Bifunctional protein PutA
- Glycine dehydrogenase
- Peptide synthase
- Beta-ketoacyl synthase
- Sarcosine oxidase subunit alpha
- Phosphoribosylformylglycinamidine synthase
- Carbamoyl phosphate synthase small chain
- NADH oxidase
- Iron-sulfur-binding ferredoxin reductase
Sequence:
MSKSVQLIKDHDVKWIDLRFTDTKGTQHHVTMPARDALEDDFFEVGKMFDGSSIAGWKGIEASDMILLPDDDTAVLDPFTEDATLILVCDIIEPSTMQGYDRDPRAIAHRAEEYLKTTGIGDTVFAGPEPEFFIFDEVKFKSDISGSMFKIYSEQGSWMSDQDIEGGNKGHRPGVKGGYFPVPPFDHDHEIRTAMCNALEEMGQTVEVHHHEVATAGQNEIGVKFNTLVKKADEVQTLKYVVHNVADAYGRTATFMPKPLYGDNGSGMHVHMSIAKDGKNTFAGEGYAGLSETALYFIGGIIKHGKALNGFTNPATNSYKRLVPGFEAPVMLAYSARNRSASIRIPYVNSPRGRRIEARFPDPAANPYLAFAALLMAGLDGIQNKIHPGDAADKNLYDLPPEEAKEIPQVCGSLKEALEELDKGRAFLTKGGVFSDDFIDAYIALKSEEEIKVRTFVHPLEYELYYSC
Protein: N-alpha-acetyltransferase 80 (DmNAA80) (EC 2.3.1.-) (Q59DX8)
Organism: Drosophila melanogaster (Fruit fly)
Function: N-alpha-acetyltransferase that acetylates the amino terminal acidic residue of proteins devoid of initiator methionine. Preferentially acts on proteins starting with Asp-Asp-Asp and Glu-Glu-Glu sequences. In vitro, shows high activity towards N-terminal sequences starting with Met-Asp-Glu-Leu, Met-Glu-Glu-Glu and Met-Asp-Asp-Asp.
Interaction partners:
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 20
- Profilin
- N-alpha-acetyltransferase 60
Sequence:
MRYIKSEPYYEGLPPFNVSGSPFNVVPIHNYPELMKDTCALINAEWPRSETARMRSLEASCDSLPCSLVLTTEGMCRVIAHLKLSPINSKKKACFVESVVVDKRHRGQGFGKLIMKFAEDYCRVVLDLKTIYLSTIDQDGFYERIGYEYCAPITMYGPRHCELPSLQNAKKKYMKKVL
Protein: Mitochondrial fusion and transport protein UGO1 (Q03327)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for mitochondrial fusion as well as normal mitochondrial morphology by bridging the essential interaction between FZO1 and MGM1. May coordinate fusion of inner and outer membranes during mitochondrial fusion.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:11257114, ECO:0000269|PubMed:14576278}; Single-pass type II membrane protein {ECO:0000269|PubMed:11257114, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Mitofusin FZO1
- Dynamin-like GTPase MGM1, mitochondrial
- Dynamin-related protein DNM1
- MICOS complex subunit MIC60
- Mitochondrial fission 1 protein
- Mitochondrial import protein 1
- Mitochondrial import receptor subunit TOM40
- CCR4-associated factor 4
- Mitochondrial import receptor subunit TOM70
- Rhomboid protein 1, mitochondrial
Sequence:
MNNNNVTEATSRAQIRPYYDPDSFNAGYSAVFKPDEGVVDPHGYTIASKLNVINSSPTTKRMANALFKSSPMKKLSNSVNDGLSLEGSNGEITGLNNFEWAELVNIQKWRKIFEQLLDMFFRKYFQLLIQQPFDVARLLIQVGEFKIFKTTVDTNKPQAPIILRDEEGDGAAREGEEDAYDEEEIDFFPIERKIAEANSTAPIMAEETDHSHHEPTDISLTIAPQSLHTIDVINALFDQEGIRGLWKANNTTFIYNFLSLSIDTWFTGLLSSFLGVPDPYFMEVINSPDISKSFILALGAGVFTSIILLPVDLIRTRLIVTSFKKKKNVKTDGKNMVTNTRSLRQLIRCWSWRKNGVSIPLDMWSLTILQSINNSFFNKLFDLVIYNQFHIEKYSQTVMYNTMKFFSKSLELFIKLPLENLLRRCQLNYLLNDQRLSFKVDSTELIVKPKKYNGIWDVIRNNSNTNRGQLWNGWKVGVISLICGYGLQMMNKVDINMEQEKF
Protein: Beta-2 adrenergic receptor (Beta-2 adrenoreceptor) (Beta-2 adrenoceptor) (P10608)
Organism: Rattus norvegicus (Rat)
Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P07550}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P07550}. Early endosome {ECO:0000250|UniProtKB:P07550}. Golgi apparatus {ECO:0000250|UniProtKB:P07550}. Note=Colocalizes with VHL at the cell membrane. Activated receptors are internalized into endosomes prior to their degradation in lysosomes. Activated receptors are also detected within the Golgi apparatus. {ECO:0000250|UniProtKB:P07550}.
Interaction partners:
- Beta-arrestin-2
- Beta-arrestin-1
- Na
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Beta-1 adrenergic receptor
- Guanine nucleotide-binding protein G
- Beta-3 adrenergic receptor
- Beta-adrenergic receptor kinase 1
- Guanine nucleotide-binding protein G
Sequence:
MEPHGNDSDFLLAPNGSRAPGHDITQERDEAWVVGMAILMSVIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGASHILMKMWNFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYVAITSPFKYQSLLTKNKARVVILMVWIVSGLTSFLPIQMHWYRATHKQAIDCYAKETCCDFFTNQAYAIASSIVSFYVPLVVMVFVYSRVFQVAKRQLQKIDKSEGRFHAQNLSQVEQDGRSGHGLRSSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIRANLIPKEVYILLNWLGYVNSAFNPLIYCRSPDFRIAFQELLCLRRSSSKTYGNGYSSNSNGRTDYTGEQSAYQLGQEKENELLCEEAPGMEGFVNCQGTVPSLSIDSQGRNCNTNDSPL
Protein: S-acyl fatty acid synthase thioesterase, medium chain (EC 3.1.2.14) (Augmented in rheumatoid arthritis 1) (AURA1) (Oleoyl-ACP hydrolase) (Thioesterase 2) (TE2) (Thioesterase II) (Thioesterase domain-containing protein 1) (Q9NV23)
Organism: Homo sapiens (Human)
Function: Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P08635}.
Interaction partners:
- Fatty acid synthase
- Hydroxysteroid dehydrogenase-like protein 2
- Beta-alanine-activating enzyme
Sequence:
MERGDQPKRTRNENIFNCLYKNPEATFKLICFPWMGGGSTHFAKWGQDTHDLLEVHSLRLPGRESRVEEPLENDISQLVDEVVCALQPVIQDKPFAFFGHSMGSYIAFRTALGLKENNQPEPLHLFLSSATPVHSKAWHRIPKDDELSEEQISHYLMEFGGTPKHFAEAKEFVKQCSPIIRADLNIVRSCTSNVPSKAVLSCDLTCFVGSEDIAKDMEAWKDVTSGNAKIYQLPGGHFYLLDPANEKLIKNYIIKCLEVSSISNF
Protein: Protein ORD (Orientation disrupter protein) (Q24434)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for proper maintenance of sister-chromatid cohesion in both male and female meiosis. Mutations in ord cause premature separation of the sister chromatids in meiosis I and random segregation in both meiotic divisions. Required for chiasma maintenance in female meiosis. Mutations in ord reduce recombination in female meiosis.
Subcellular location: Nucleus. Chromosome. Chromosome, centromere. Note=In male meiosis it assembles onto chromosomes in late G2 of the meiotic cell cycle. It remains at the centromeres after chromosome condensation, through the meiosis I division until the separation of sister chromatids at anaphase II.
Interaction partners:
- Crossover suppressor on 2 of manheim
- Crossover suppressor on 3 of Gowen
- Shugoshin
- Sister chromatid cohesion protein solo
- FI21203p1
- Meiotic recombination protein W68
Sequence:
MYGETTLNKNHVIKFIKLKINNCLGCDEVEINFSKADNVHIIIYSLVTDMAKDLPAVTPVAQAILLLCSLTYPDSDSLETIPQLKIGKGSVSMSFKVYPVNKEEETEPESESDLDEGPSTSKQALERMVQRAERKAKEASTRNVHSKGIYVNVERRFDMYFALDTVSYYINGGKRQSCPLPEFHAKFFVRPQHSINLLRQLHEKCSGNWLKVIQSDGDGDAFKKFKDPDSPFETFVKLFESNPIKPNDMMGKLAKTCLHVNEAVRLTEREFILEVFNQVRHIFEYITAQEYTVWFLVPCLGDKDQLRSKTLEDFDLTKVRTSIRRAGDTSNIWWDHTDHNIKDILLVAFQLDLATHVNQSVLVISHLETLAEFSTMQYVTAFFMNDFYAKKNTEPKWICHRYLERIIDVALFLGVIVIIEYPSAFTLLQEGRHLIKCFQKENADSSRTSQWEIFEDVVKENESDLEFLKEAVGKVQQNV
Protein: Granulysin (Lymphokine LAG-2) (Protein NKG5) (T-cell activation protein 519) (P22749)
Organism: Homo sapiens (Human)
Function: Antimicrobial protein that kills intracellular pathogens. Active against a broad range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.
Subcellular location: Secreted. Note=Located in the cytotoxic granules of T-cells, which are released upon antigen stimulation.
Interaction partners:
- Perforin-1
- Granzyme B
- Granzyme A
- Serrate RNA effector molecule homolog
- Recombining binding protein suppressor of hairless
- Granzyme H
- Protein NKG7
- Tumor necrosis factor ligand superfamily member 6
- Natural killer cells antigen CD94
- T-cell surface glycoprotein CD8 alpha chain
Sequence:
MATWALLLLAAMLLGNPGLVFSRLSPEYYDLARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYRTCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWRDVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPSTGPL
Protein: Uncharacterized protein (Q387M3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLTLGELSDAIASLAEGCSMEQLSGLAQQCESHLANVEGIIDAVENALRTSHGGQRLVLWFFIDRLAKQHVIFLDSLRPRLRSLATTAAPAADGPEWADFKSLLKYSIAVVFGAPLVSLILLEIDPETQKETARNNASASERERGVVALHSCALRTAGAFSTKAVMTERPAGAKHILQVKTIDSQVAMNMASSYAPARPQEIAVPEVQPDADAPQGYMKAVPAEYLKNYQNARRKRLREIMDRNREEMDRRQEAELLNAVRGVAAENGKVPDYSDVVMPLELPRDEHGVKRGFFPLGVRFIREAIRSCGGAVELDVLVNRLSTLASKEVVAEFGDVREFILIHRPTFRVTNEKDRWIVRLAGDENSDPTWESMQCPLCSKVLRGRNLARHVNCRLCVTTQIALGLHGEVRSPISELAFVAKSIIDRANTFDDWDLEHFAECIERAAACRRFKLSSQAKFAPVLKAMRVVRNRWLARKGVAEVADAVVNPGDAAIVNLFRVIGRNVNRLPIPWIDMGDVVDMCSRFSTGVLPPFNPPPRPADPRINLNNEYPGFLLCESEVDDEDEPSDDEDAFSDDDAPTFVFAPPVDLAETLMTAGFERDTKRLQHRMRTAPPLVLQRVLKGDRTQTQRDMYADVVASGNYISATQ
Protein: SD04106p (Q960F2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}.
Interaction partners:
Sequence:
MKVFFVKYNDPIYVKLEKLDIMIRLANQSNIAQVLSELKEYATEVDVDFVRKAVRAIGRCAIKVEPSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESIISTLCENLDTLDEPEARASMVWIIGEYAERIDNADELLDSFLEGFQDENAQVQLQLLTAVVKLFLKRPSDTQELVQHVLSLATQDSDNPDLRDRGFIYWRLLSTDPAAAKEVVLADKPLISEETDLLEPTLLDELICHISSLASVYHKPPTAFVEGRGAGVRKSLPNRAAGSAAGAEQAENAAGSEAMVIPNQESLIGDLLSMDINAPAMPSAPAATSNVDLLGGGLDILLGGPPAEAAPGGATSLLGDIFGLGGATLSVGVQIPKVTWLPAEKGKGLEIQGTFSRRNGEVFMDMTLTNKAMQPMTNFAIQLNKNSFGLVPASPMQAAPLPPNQSIEVSMALGTNGPIQRMEPLNNLQVAVKNNIDIFYFACLVHGNVLFAEDGQLDKRVFLNTWKEIPAANELQYTLSGVIGTTDGIASKMTTNNIFTIAKRNVEGQDMLYQSLKLTNNIWVLLELKLQPGNPEATLSLKSRSVEVANIIFAAYEAIIRSP
Protein: Nucleoporin NUP37 (Q5B9K7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MPSFPSRPLVRARDDGLQLSFQLPHRVYTAQGYPIPAPNGSSVVVYGYEDGLKVIWRGGRSFSNKKLQTKQEKQQKPSRNNDDAVMIIDSDDESMADTQKAEEPVADTYEFEDEDPEVDPAEPYEGVLRQIDIPLGSRVINIAVPRVLPETARSSLDPFPAILDQLIIVSAICADYSTRVVTVPLTPPHPTQTDIAALGIQTFAIGGGFSHQELPQGVSITFTYQESDPQQGGEGRWDLLVATHSAESSGLLVIHRIPITEDKKTTNKVYRLSAEDVESKRRYLPSPAQNIAFNPSSYPAARHSTLLVSFHSGCVKVYSCFSTRPSKSSRRAVAAQNDYETLKTEGEWLISLYPGFEQPLSNLPRRKSITSAEWVLGGRAILVLMADGEWGVWDLEGAGPGSAKGPLQGQSSVQGVTGGSLTAFSVSGRILSFPSGGKSETAVERRPKFAPMTPSTKRIREDTLLKGNVAGTSTSSLRGGISVYQMNSTQDPLPDESILIRHGNQSAVIPSLLTLWRSAVRSTGTLDASNRCRVTPLQDIALMGEPLKGIGHVPAPSRRSHSQIRAFDILVTAEHRLLILAPKLAEPDAASTSRTLVTESPTRAADQLRLRQGELDVDGMDRVLSGMAHNRSLHMGSPIKRTRIFT