wanglab/gogpt-training-data huggingface dataset:
Protein: G-protein coupled receptor 183 (Epstein-Barr virus-induced G-protein coupled receptor 2) (EBI2) (EBV-induced G-protein coupled receptor 2) (hEBI2) (P32249)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (By similarity). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols. Mediates cell positioning and movement of a number of cells by binding the 7-alpha,25-OHC ligand that forms a chemotactic gradient (By similarity). Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses (By similarity). Guides B-cell movement along the B-cell zone-T-cell zone boundary and later to interfollicular and outer follicular regions (By similarity). Its specific expression during B-cell maturation helps position B-cells appropriately for mounting T-dependent antibody responses (By similarity). Collaborates with CXCR5 to mediate B-cell migration; probably by forming a heterodimer with CXCR5 that affects the interaction between of CXCL13 and CXCR5. Also acts as a chemotactic receptor for some T-cells upon binding to 7-alpha,25-OHC ligand (By similarity). Promotes follicular helper T (Tfh) cells differentiation by positioning activated T-cells at the follicle-T-zone interface, promoting contact of newly activated CD4 T-cells with activated dendritic cells and exposing them to Tfh-cell-promoting inducible costimulator (ICOS) ligand (By similarity). Expression in splenic dendritic cells is required for their homeostasis, localization and ability to induce B- and T-cell responses: GPR183 acts as a chemotactic receptor in dendritic cells that mediates the accumulation of CD4(+) dendritic cells in bridging channels (By similarity). Regulates migration of astrocytes and is involved in communication between astrocytes and macrophages. Promotes osteoclast precursor migration to bone surfaces (By similarity). Signals constitutively through G(i)-alpha, but not G(s)-alpha or G(q)-alpha. Signals constitutively also via MAPK1/3 (ERK1/2) (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:16540462, ECO:0000269|PubMed:18628402, ECO:0000269|PubMed:21673108, ECO:0000269|PubMed:22930711}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Immunoglobulin lambda variable 10-54.
- Early activation antigen CD69
- N-arachidonyl glycine receptor
Sequence:
MDIQMANNFTPPSATPQGNDCDLYAHHSTARIVMPLHYSLVFIIGLVGNLLALVVIVQNRKKINSTTLYSTNLVISDILFTTALPTRIAYYAMGFDWRIGDALCRITALVFYINTYAGVNFMTCLSIDRFIAVVHPLRYNKIKRIEHAKGVCIFVWILVFAQTLPLLINPMSKQEAERITCMEYPNFEETKSLPWILLGACFIGYVLPLIIILICYSQICCKLFRTAKQNPLTEKSGVNKKALNTIILIIVVFVLCFTPYHVAIIQHMIKKLRFSNFLECSQRHSFQISLHFTVCLMNFNCCMDPFIYFFACKGYKRKVMRMLKRQVSVSISSAVKSAPEENSREMTETQMMIHSKSSNGK
Protein: Tumor necrosis factor receptor superfamily member 10B (Death receptor 5) (TNF-related apoptosis-inducing ligand receptor 2) (TRAIL receptor 2) (TRAIL-R2) (CD antigen CD262) (O14763)
Organism: Homo sapiens (Human)
Function: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- FAS-associated death domain protein
- Tumor necrosis factor ligand superfamily member 10
- Caspase-8
- Tumor necrosis factor ligand superfamily member 6
- Tumor necrosis factor receptor superfamily member 10A
- Tumor necrosis factor
- Receptor-interacting serine/threonine-protein kinase 1
- CASP8 and FADD-like apoptosis regulator
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Tumor necrosis factor receptor superfamily member 10D
Sequence:
MEQRGQNAPAASGARKRHGPGPREARGARPGPRVPKTLVLVVAAVLLLVSAESALITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKESGTKHSGEVPAVEETVTSSPGTPASPCSLSGIIIGVTVAAVVLIVAVFVCKSLLWKKVLPYLKGICSGGGGDPERVDRSSQRPGAEDNVLNEIVSILQPTQVPEQEMEVQEPAEPTGVNMLSPGESEHLLEPAEAERSQRRRLLVPANEGDPTETLRQCFDDFADLVPFDSWEPLMRKLGLMDNEIKVAKAEAAGHRDTLYTMLIKWVNKTGRDASVHTLLDALETLGERLAKQKIEDHLLSSGKFMYLEGNADSAMS
Protein: Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)] (P19097)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.
Interaction partners:
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Acetyl-CoA carboxylase
- Long-chain-fatty-acid--CoA ligase 1
- Acetyl-CoA carboxylase, mitochondrial
- Translation machinery-associated protein 17
- Long-chain-fatty-acid--CoA ligase 4
- Long-chain-fatty-acid--CoA ligase 2
- 3-oxoacyl-[acyl-carrier-protein] synthase homolog
- Long-chain-fatty-acid--CoA ligase 3
- 3-oxoacyl-[acyl-carrier-protein] reductase
Sequence:
MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFNTERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILCYSKDAKEIYYTPDPSELAAKEEPAKEEAPAPTPAASAPAPAAAAPAPVAAAAPAAAAAEIADEPVKASLLLHVLVAHKLKKSLDSIPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETPLEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITVARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKAFLDSMAQKYASIVGVDLSSAASASGAAGAGAAAGAAMIDAGALEEITKDHKVLARQQLQVLARYLKMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGVATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDREVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVKTLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNITYSEEPREKVRKLSQYVQEMALGGPITKESQPTIEEDLTRVYKAISAQADKQDISSSTRVEFEKLYSDLMKFLESSKEIDPSQTTQLAGMDVEDALDKDSTKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGDWKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSIGAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAKGSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAIIPFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKKQKSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSLETLFNRWHSESWANQLTVCGAIIGWTRGTGLMSANNIIAEGIEKMGVRTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFVPELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLLDLERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEGCVEMAWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDVKAKYETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEPFEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATLYIPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITLFVLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGSGMGGVSALRGMFKDRFKDEPVQNDILQESFINTMSAWVNMLLISSSGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYDDFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTRNGFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDKIGRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRKRQLVTREAQIKDWVENELEALKLEAEEIPSEDQNEFLLERTREIHNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTIDDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVIGVFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADNVDKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQKGGQAIVVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFHNGMIYNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTFNSKNIQSKDSYINANTIETAKMIENMTKEKVSNGGVGVDVELITSINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWSAKEAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAVELHGNAKKAAEEAGVTDVKVSISHDDLQAVAVAVSTKK
Protein: Protein transport protein SFT2 (P38166)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Nonessential protein required for the fusion of transport vesicles derived from the endocytic pathway with the Golgi complex. Can be partially replaced by GOT1.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10406798}; Multi-pass membrane protein {ECO:0000269|PubMed:10406798}.
Interaction partners:
- Integral membrane protein SED5
- Protein transport protein SFT1
- Protein transport protein GOT1
- Synaptobrevin homolog YKT6
- Golgi SNAP receptor complex member 1
- GTP-binding protein YPT6
- GRIP domain-containing protein RUD3
- Conserved oligomeric Golgi complex subunit 6
- Protein transport protein SEC22
- Autophagy-related protein 29
Sequence:
MSEEPPSDQVNSLRDSLNRWNQTRQQNSQGFNESAKTLFSSWADSLNTRAQDIYQTLPVSRQDLVQDQEPSWFQLSRTERMVLFVCFLLGATACFTLCTFLFPVLAAKPRKFGLLWTMGSLLFVLAFGVLMGPLAYLKHLTARERLPFSMFFFATCFMTIYFAAFSKNTVLTITCALLELVAVIYYAISYFPFGATGLRMLSSAGVNSARGVLRI
Protein: FAD-dependent catabolic D-arginine dehydrogenase DauA (EC 1.4.99.6) (D-arginine dehydrogenase) (DADH) (D-arginine utilization protein A) (Dau) (Q9HXE3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: DauA is highly expressed within the cystic fibrosis (CF) lung, and it is required for virulence via the optimal production of hydrogen cyanide, pyocyanine, pyoverdine, rhamnolipid and alginate during biofilm formation. Involved in the catabolism of D-lysine and D-arginine. Under aerobic conditions, the arginine succinyltransferase (AST) and arginine transaminase (ATA) pathways are 2 major routes for L-arginine utilization as the sole source of carbon and nitrogen. The D-to-L racemization of arginine by DauA and DauB is necessary, before to be channeled into the AST and/or ATA pathways. DauA catalyzes the flavin-dependent oxidative deamination of D-arginine into 2-ketoarginine (2-KA) and ammonia. It has also dehydrogenase activity towards D-lysine, D-tyrosine, D-methionine, D-phenylalanine, D-ornithine, D-histidine and D-leucine as substrates.
Interaction partners:
- NAD
- Transcriptional regulator DauR
- Uncharacterized protein
- RidA family protein
- Sarcosine oxidase alpha subunit
- Sulfate transporter CysZ
Sequence:
MIEADYLVIGAGIAGASTGYWLSAHGRVVVLEREAQPGYHSTGRSAAHYTVAYGTPQVRALTAASRAFFDNPPAGFCEHPLLSPRPEMVVDFSDDPEELRRQYESGKALVPQMRLLDAEQACSIVPVLRRDKVFGATYDPTGADIDTDALHQGYLRGIRRNQGQVLCNHEALEIRRVDGAWEVRCDAGSYRAAVLVNAAGAWCDAIAGLAGVRPLGLQPKRRSAFIFAPPPGIDCHDWPMLVSLDESFYLKPDAGMLLGSPANADPVEAHDVQPEQLDIATGMYLIEEATTLTIRRPEHTWAGLRSFVADGDLVAGYAANAEGFFWVAAQGGYGIQTSAAMGEASAALIRHQPLPAHLREHGLDEAMLSPRRLSP
Protein: Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2) (Q96RT1)
Organism: Homo sapiens (Human)
Function: Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state. Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion.
Subcellular location: Cell junction, hemidesmosome {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:11375975}. Nucleus membrane {ECO:0000250}. Basolateral cell membrane {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
Interaction partners:
- Receptor tyrosine-protein kinase erbB-2
- Nucleotide-binding oligomerization domain-containing protein 2
- Plakophilin-4
- Mothers against decapentaplegic homolog 2
- Leucine-rich repeat protein SHOC-2
- Desmoglein-1
- Epidermal growth factor receptor
- Integrin beta-4
- Dystonin
- Mothers against decapentaplegic homolog 3
Sequence:
MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFIGSLKQLTYLDVSKNNIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQLTNLRTFAADHNYLQQLPPEIGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPSLWEEQRKQRAQVAFECDEDKDEREAPPREGNLKRYPTPYPDELKNMVKTVQTIVHRLKDEETNEDSGRDLKPHEDQQDINKDVGVKTSESTTTVKSKVDEREKYMIGNSVQKISEPEAEISPGSLPVTANMKASENLKHIVNHDDVFEESEELSSDEEMKMAEMRPPLIETSINQPKVVALSNNKKDDTKETDSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTSLCSPVKQTHIDINSKIRQEDENFNSLLQNGDILNSSTEEKFKAHDKKDFNLPEYDLNVEERLVLIEKSVDSTATADDTHKLDHINMNLNKLITNDTFQPEIMERSKTQDIVLGTSFLSINSKEETEHLENGNKYPNLESVNKVNGHSEETSQSPNRTEPHDSDCSVDLGISKSTEDLSPQKSGPVGSVVKSHSITNMEIGGLKIYDILSDNGPQQPSTTVKITSAVDGKNIVRSKSATLLYDQPLQVFTGSSSSSDLISGTKAIFKFDSNHNPEEPNIIRGPTSGPQSAPQIYGPPQYNIQYSSSAAVKDTLWHSKQNPQIDHASFPPQLLPRSESTENQSYAKHSANMNFSNHNNVRANTAYHLHQRLGPARHGEMWAISPNDRLIPAVTRSTIQRQSSVSSTASVNLGDPGSTRRAQIPEGDYLSYREFHSAGRTPPMMPGSQRPLSARTYSIDGPNASRPQSARPSINEIPERTMSVSDFNYSRTSPSKRPNARVGSEHSLLDPPGKSKVPRDWREQVLRHIEAKKLEKKHPQTSSSGDPCQDGIFISGQQNYSSATLSHKDVPPDSLMKMPLSNGQMGQPLRPQANYSQIHHPPQASVARHPSREQLIDYLMLKVAHQPPYTQPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVREVSS
Protein: Syncytin-2 (ERV-FRD provirus ancestral Env polyprotein) (Envelope polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)] (P61555)
Organism: Hylobates moloch (Silvery gibbon)
Function: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process (By similarity).
Subcellular location: [Surface protein]: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000250|UniProtKB:Q9UQF0}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGLLLLVLILTPLLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYQWDPNLKGLMRPANSLLSTVKQDFPDIRQKPPIFGPIFTNINLMGIAPICVTAKRKNGTNVGTLPSTVCNVTFTVDPNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSTRFCQGRPSSCSTRNFWFRPADYNQCLQISNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLGISAVSEFFGNSLTPLFHFHISTCLKTQGAFYICGQSIHQCLPSNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGKSQLPRVRRAIHFIPLLAGLGILAGTGTGIAGITKASLTYSQLSKEIANNIDTMAKTLTTVQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPFIGPFVSLLLLLLFGPCLLNLITQFVSSRLQAIKLQTNLSAGRRPRTIQESPF
Protein: Cadmium/zinc-transporting ATPase HMA2 (EC 7.2.2.12) (EC 7.2.2.21) (Cadmium/zinc-transporting ATPase 3) (Protein HEAVY METAL ATPASE 2) (Q9SZW4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in zinc transport and homeostasis. Could also be involved in cadmium detoxification.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15100400}; Multi-pass membrane protein {ECO:0000269|PubMed:15100400}.
Interaction partners:
- Copper chaperone for superoxide dismutase, chloroplastic/cytosolic
- Metal tolerance protein 1
- Metal transporter Nramp3
- Metal transporter Nramp5
- Metal transporter Nramp4
- Fe
- Fe
- Protein ZINC INDUCED FACILITATOR 1
- Protein PLANT CADMIUM RESISTANCE 2
- Probable magnesium transporter NIPA4
Sequence:
MASKKMTKSYFDVLGICCTSEVPLIENILNSMDGVKEFSVIVPSRTVIVVHDTLILSQFQIVKALNQAQLEANVRVTGETNFKNKWPSPFAVVSGILLLLSFFKYLYSPFRWLAVAAVVAGIYPILAKAVASLARFRIDINILVVVTVGATIGMQDYTEAAVVVFLFTIAEWLQSRASYKASAVMQSLMSLAPQKAVIAETGEEVEVDELKTNTVIAVKAGETIPIDGVVVDGNCEVDEKTLTGEAFPVPKLKDSTVWAGTINLNGYITVNTTALAEDCVVAKMAKLVEEAQNSKTETQRFIDKCSKYYTPAIILISICFVAIPFALKVHNLKHWVHLALVVLVSACPCGLILSTPVATFCALTKAATSGLLIKGADYLETLAKIKIVAFDKTGTITRGEFIVMDFQSLSEDISLQSLLYWVSSTESKSSHPMAAAVVDYARSVSVEPKPEAVEDYQNFPGEGIYGKIDGKEVYIGNKRIASRAGCLSVPDIDVDTKGGKTIGYVYVGETLAGVFNLSDACRSGVAQAMKELKSLGIKIAMLTGDNHAAAMHAQEQLGNAMDIVRAELLPEDKSEIIKQLKREEGPTAMVGDGLNDAPALATADIGISMGVSGSALATETGNIILMSNDIRRIPQAIKLAKRAKRKVVENVVISITMKGAILALAFAGHPLIWAAVLADVGTCLLVILNSMLLLSDKHKTGNKCYRESSSSSVLIAEKLEGDAAGDMEAGLLPKISDKHCKPGCCGTKTQEKAMKPAKASSDHSHSGCCETKQKDNVTVVKKSCCAEPVDLGHGHDSGCCGDKSQQPHQHEVQVQQSCHNKPSGLDSGCCGGKSQQPHQHELQQSCHDKPSGLDIGTGPKHEGSSTLVNLEGDAKEELKVLVNGFCSSPADLAITSLKVKSDSHCKSNCSSRERCHHGSNCCRSYAKESCSHDHHHTRAHGVGTLKEIVIE
Protein: FKBP prolyl isomerase 8 (U3KQ64)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGPDLEMLTGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEEAQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKTIHAELSKLVKKHAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN
Protein: Trans-Golgi network integral membrane protein 2 (Trans-Golgi network glycoprotein 46) (TGN38 homolog) (hTGN46) (Trans-Golgi network glycoprotein 48) (hTGN48) (Trans-Golgi network glycoprotein 51) (hTGN51) (Trans-Golgi network protein 2) (O43493)
Organism: Homo sapiens (Human)
Function: May be involved in regulating membrane traffic to and from trans-Golgi network.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit beta
- AP-2 complex subunit alpha-2
- GRIP and coiled-coil domain-containing protein 1
- Syntaxin-6
- AP-1 complex subunit mu-1
- Vesicle-associated membrane protein 4
- Cation-independent mannose-6-phosphate receptor
- Golgin subfamily A member 1
- Transferrin receptor protein 1
Sequence:
MRFVVALVLLNVAAAGAVPLLATESVKQEEAGVRPSAGNVSTHPSLSQRPGGSTKSHPEPQTPKDSPSKSSAEAQTPEDTPNKSGAEAKTQKDSSNKSGAEAKTQKGSTSKSGSEAQTTKDSTSKSHPELQTPKDSTGKSGAEAQTPEDSPNRSGAEAKTQKDSPSKSGSEAQTTKDVPNKSGADGQTPKDGSSKSGAEDQTPKDVPNKSGAEKQTPKDGSNKSGAEEQGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTEDVEPKEAEDDDTGPEEGSPPKEEKEKMSGSASSENREGTLSDSTGSEKDDLYPNGSGNGSAESSHFFAYLVTAAILVAVLYIAHHNKRKIIAFVLEGKRSKVTRRPKASDYQRLDQKS
Protein: Large ribosomal subunit protein eL36 (60S ribosomal protein L36) (Q6Q415)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3U8}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y3U8}. Note=Detected on cytosolic polysomes. {ECO:0000250|UniProtKB:Q2YGT9, ECO:0000250|UniProtKB:Q9Y3U8}.
Interaction partners:
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS11
- 60S ribosomal protein L7a
- Small ribosomal subunit protein eS25
- Large ribosomal subunit protein eL28
- Ribosomal protein L26
- Large ribosomal subunit protein eL42
Sequence:
MVVRYPMAVGLNKGHKVTKNVSKPKHSRRRGRLTKHAKFARDLIREVCGFAPYERRAMELLKVSKDKRALKFIKKRVGTHIRAKRKREELSNTLAAMRKAAAKKE
Protein: Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (17-beta-hydroxysteroid dehydrogenase 12) (17-beta-HSD 12) (3-ketoacyl-CoA reductase) (KAR) (Estradiol 17-beta-dehydrogenase 12) (EC 1.1.1.62) (Short chain dehydrogenase/reductase family 12C member 1) (Q53GQ0)
Organism: Homo sapiens (Human)
Function: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12482854}; Multi-pass membrane protein {ECO:0000269|PubMed:12482854}.
Interaction partners:
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very long chain fatty acid elongase 1
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (HSD17B8) (KAR alpha subunit) (Estradiol 17-beta-dehydrogenase 8) (Protein Ke6) (Ke6) (Testosterone 17-beta-dehydrogenase 8)
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 17-beta-hydroxysteroid dehydrogenase type 1
- Stearoyl-CoA desaturase
Sequence:
MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWIYLKIVMNMNKSTRAHYLKKTKKN
Protein: Fibroblast growth factor receptor (EC 2.7.10.1) (A0A0G2K210)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Fibroblast growth factor 2
- Fibroblast growth factor 18
- Fibroblast growth factor 1
- Fibroblast growth factor 9
- Fibroblast growth factor
- Fibroblast growth factor
- Fibroblast growth factor 16
- Fibroblast growth factor 7
- Fibroblast growth factor 20
- Fibroblast growth factor 10
Sequence:
MVVPACVLVFCVAVVAGVTSEPPGPEQRVGRRAAEVPGPEPSQQEQVAFGSGDTVELSCHPPGGAPTGPTLWAKDGVGLVASHRILVGPQRLQVLNATHEDAGVYSCQQRLTRRVLCHFSVRVTDAPSSGDDEDGEDVAEDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGKEFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKSWISENVEADARLRLANVSERDGGEYLCRATNFIGVAEKAFWLRVHGPQAAEEELMEVDEAGSVYAGVLSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKVSRFPLKRQQVSLESNSSMNSNTPLVRIARLSSGEGPVLANVSELELPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDRTAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGMDYSFDACRLPEEQLTCKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAVPSQRPTFKQLVEDLDRILTVTSTDEYLDLSVPFEQYSPGGQDTPSSSSSGDDSVFTHDLLPPGPPSNGGPRT