wanglab/gogpt-training-data huggingface dataset:
Protein: AT-rich interactive domain-containing protein 5A (ARID domain-containing protein 5A) (Q3U108)
Organism: Mus musculus (Mouse)
Function: DNA-binding protein that may regulate transcription and act as a repressor by binding to AT-rich stretches in the promoter region of target genes (By similarity). May positively regulate chondrocyte-specific transcription such as of COL2A1 in collaboration with SOX9 and positively regulate histone H3 acetylation at chondrocyte-specific genes. May stimulate early-stage chondrocyte differentiation and inhibit later stage differention. Can repress ESR1-mediated transcriptional activation; proposed to act as corepressor for selective nuclear hormone receptors (By similarity). As RNA-binding protein involved in the regulation of inflammatory response by stabilizing selective inflammation-related mRNAs, such as IL6, STAT3 and TBX21. Binds to stem loop structures located in the 3'UTRs of IL6, STAT3 and TBX21 mRNAs; at least for STAT3 prevents binding of ZC3H12A to the mRNA stem loop structure thus inhibiting its degradation activity. Contributes to elevated IL6 levels possibly implicated in autoimmunity processes. IL6-dependent stabilization of STAT3 mRNA may promote differentiation of naive CD4+ T-cells into T-helper Th17 cells. In CD4+ T-cells may also inhibit RORC-induced Th17 cell differentiation independently of IL6 signaling. Stabilization of TBX21 mRNA contributes to elevated interferon-gamma secretion in Th1 cells possibly implicated in the establishment of septic shock. Stabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR; thereby competing with the mRNA-destabilizing functions of RC3H1 and endoribonuclease ZC3H12A.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:21346191}.
Interaction partners:
- Endoribonuclease ZC3H12A
Sequence:
MAAPPAKGNTEQSEEGDLPQLPVSPKPDDEQSRSQSPTQLQDSPEAGGEQEEEQAFLVSLYKFMKERHTPIERVPHLGFKQINLWKIYKAVEKLGAYELVTGRRLWKNVYDELGGSPGSTSAATCTRRHYERLVLPYVRHLKGEDDKPLPPTKPRKQYKMAKELRGDDGTTEKLKKAKDSEERRVEQTTPGKTKSDATGQTQLPCQGSSRDSTEQLGPVSGPSPPLTGASSCPEAYKRLLSSFYCKGAHGIMSPLAKKKLLAQVSKAEALQCQEEGCRHGARSPNKDIQDSPQNLRGPAENSEHQLTPREGLQAPGGSTRMEAQVGPCPTAPMFSGCFHAYPTEVLKPVSQHPRDFFSGLKDRVLLGPPGKEEGPTTKESHLVWGGDANHPSAFHKGSTRKRSFYPKPKACWVSPMAKVPTERPGAPSPHPSSPGLGSKRGLEEEGFAHGGKKLRAVSPFLKEVDSKETGGKPAAPGLAVSCLLGPTPGPTPPEAYRGTMLRCPLNFTGSADPLKGQASLPFSPLVIPAFPAHLLATTGSSPMAASLMHFPPTPYDAVLRNRLGPASSAWHMPPVTTYAAPHFFHLNTKL
Protein: Putrescine--pyruvate aminotransferase (PATase) (EC 2.6.1.113) (Putrescine--pyruvate transaminase) (Q9I6J2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the putrescine catabolism. Catalyzes the transfer of the amino group from putrescine to pyruvate to yield 4-aminobutanal and alanine.
Interaction partners:
- aldehyde dehydrogenase
- Probable aldehyde dehydrogenase
- Probable aldehyde dehydrogenase
- Probable glutamine synthetase
- N-carbamoylputrescine amidohydrolase
- ornithine decarboxylase
- Probable glutamine synthetase
- Spermidine dehydrogenase, SpdH
- Polyamine aminopropyltransferase 2
- Spermidine acetyltransferase
Sequence:
MNSQITNAKTREWQALSRDHHLPPFTDYKQLNEKGARIITKAEGVYIWDSEGNKILDAMAGLWCVNVGYGREELVQAATRQMRELPFYNLFFQTAHPPVVELAKAIADVAPEGMNHVFFTGSGSEANDTVLRMVRHYWATKGQPQKKVVIGRWNGYHGSTVAGVSLGGMKALHEQGDFPIPGIVHIAQPYWYGEGGDMSPDEFGVWAAEQLEKKILEVGEENVAAFIAEPIQGAGGVIVPPDTYWPKIREILAKYDILFIADEVICGFGRTGEWFGSQYYGNAPDLMPIAKGLTSGYIPMGGVVVRDEIVEVLNQGGEFYHGFTYSGHPVAAAVALENIRILREEKIIEKVKAETAPYLQKRWQELADHPLVGEARGVGMVAALELVKNKKTRERFTDKGVGMLCREHCFRNGLIMRAVGDTMIISPPLVIDPSQIDELITLARKCLDQTAAAVLA
Protein: Response regulator protein PilR (Q00934)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system PilS/PilR that regulates the expression of multiple genes including the type IV pilus (T4P) major subunit PilA. Thereby, plays a major role in the regulation of multiple motility pathways. Upon appropriate environmental signals, the histidine kinase PilS transfers the phosphoryl group onto PilR. In turn, PilR functions as a transcriptional activator by direct binding to a cis-acting sequence upstream of the pilin gene promoter leading to its activation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor protein kinase PilS
- RNA polymerase sigma-54 factor
- Fimbrial assembly protein PilQ
- Type IV pilus inner membrane component PilN
- Type IV pilus inner membrane component PilM
- Type IV pilus retractation ATPase PilT
- Type IV pilus assembly ATPase PilB
- Chemotaxis protein CheA
- Type IV pilus inner membrane component PilO
- Type 4 fimbrial biogenesis protein PilZ
Sequence:
MSRQKALIVDDEPDIRELLEITLGRMKLDTRSARNVKEARELLAREPFDLCLTDMRLPDGSGLDLVQYIQQRHPQTPVAMITAYGSLDTAIQALKAGAFDFLTKPVDLGRLRELVATALRLRNPEAEEAPVDNRLLGESPPMRALRNQIGKLARSQAPVYISGESGSGKELVARLIHEQGPRIERPFVPVNCGAIPSELMESEFFGHKKGSFTGAIEDKQGLFQAASGGTLFLDEVADLPMAMQVKLLRAIQEKAVRAVGGQQEVAVDVRILCATHKDLAAEVGAGRFRQDLYYRLNVIELRVPPLRERREDIPLLAERILKRLAGDTGLPAARLTGDAQEKLKNYRFPGNVRELENMLERAYTLCEDDQIQPHDLRLADAPGASQEGAASLSEIDNLEDYLEDIERKLIMQALEETRWNRTAAAQRLGLTFRSMRYRLKKLGID
Protein: CesT family type III secretion system chaperone (Type III secretion system effector chaperone) (A0A0H3NDF5)
Organism: Salmonella typhimurium (strain SL1344)
Interaction partners:
Sequence:
MYSRADRLLRQFSLKLNTDSIVFDENRLCSFIIDNRYRILLTSTNSEYIMIYGFCGKPPDNNNLAFEFLNANLWFAENNGPHLCYDNNSQSLLLALNFSLNESSVEKLECEIEVVIRSMENLYHILQDKGITLDTDYT
Protein: Ribonuclease J 1 (RNase J1) (EC 3.1.-.-) (Q6GHZ6)
Organism: Staphylococcus aureus (strain MRSA252)
Function: An RNase that has 5'-3' exonuclease and possibly endoonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
Interaction partners:
Sequence:
MKQLHPNEVGVYALGGLGEIGKNTYAVEYKDEIVIIDAGIKFPDDNLLGIDYVIPDYTYLVQNQDKIVGLFITHGHEDHIGGVPFLLKQLNIPIYGGPLALGLIRNKLEEHHLLRTAKLNEINEDSVIKSKHFTISFYLTTHSIPETYGVIVDTPEGKVVHTGDFKFDFTPVGKPANIAKMAQLGEEGVLCLLSDSTNSLVPDFTLSEREVGQNVDKIFRNCKGRIIFATFASNIYRVQQAVEAAIKNNRKIVTFGRSMENNIKIGMELGYIKAPPETFIEPNKINTVPKHELLILCTGSQGEPMAALSRIANGTHKQIKIIPEDTVVFSSSPIPGNTKSINRTINSLYKAGADVIHSKISNIHTSGHGSQGDQQLMLRLIKPKYFLPIHGEYRMLKAHGETGVECGVEEDNVFIFDIGDVLALTHDSARKAGRIPSGNVLVDGSGIGDIGNVVIRDRKLLSEEGLVIVVVSIDFNTNKLLSGPDIISRGFVYMRESGQLIYDAQRKIKTDVISKLNQNKDIQWHQIKSSIIETLQPYLFEKTARKPMILPVIMKVNEQKESNNK
Protein: Uncharacterized protein (Q389F9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 30S Ribosomal protein S17, putative
- Methyltransferase
- Dehydrogenase-like protein
- tRNA pseudouridine synthase A-like protein
- Uncharacterized protein
- Ribosomal protein S23 mitochondrial conserved domain-containing protein
- Small ribosomal subunit protein uS5 C-terminal domain-containing protein
- Small ribosomal subunit protein mS41
- Uncharacterized protein
- PROP1-like PPR domain-containing protein
Sequence:
MTDPVRRDPTEFLRVLRRMSRTTSWQKTMLFASKGRMVGYRLTREHYNTVLFSQSLWGRALEIVRVVRAMQEDKVQPNGATYYYIVNGMGNADHGWNYDFRINRRLEKIQHWRVALEALEACEANGFDSTDTMHNSALITLVIPGFNRWQQASLLLQRMLREDRRMHPTMVKFYHDCLVRNNRPREASSLMRLAAERGVHGYEDKWEADVYKGRPLDSEVMNESEGNGLRRQASSLAFASLMLRGDQRPLPENLQALLEEETTRNIEAERSVPVPFSAGLHATEINSVFRPRVYRQLWYKWQHIANRYRPTAALKRRQLAPRDSPTGIPGFYRI
Protein: Npm-A protein (Nucleoplasmin) (Q6GQG6)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein.
- Histone H2B
Sequence:
MASTVSNTSKLEKPVSLIWGCELNEQNKTFEFKVEDDEEKCEHQLALRTVCLGDKAKDEFHIVEIVTQEEGAEKSVPIATLKPSILPMATMVGIELTPPVTFRLKAGSGPLYISGQHVAMEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK
Protein: Colipase (P04118)
Organism: Homo sapiens (Human)
Function: Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pancreatic triacylglycerol lipase
- Inactive pancreatic lipase-related protein 1
- Gastric triacylglycerol lipase
- T-box transcription factor TBX22
- Chymotrypsinogen B2
- Bile salt-activated lipase
- Chymotrypsin-like elastase family member 3A
- Carboxypeptidase A1
- Chymotrypsinogen B
- Lithostathine-1-alpha
Sequence:
MEKILILLLVALSVAYAAPGPRGIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSITNTNFGICHDAGRSKQ
Protein: Protein kinase C-binding protein NELL2 (NEL-like protein 2) (Q62918)
Organism: Rattus norvegicus (Rat)
Function: Required for neuron survival through the modulation of MAPK pathways. Involved in the regulation of hypothalamic GNRH secretion and the control of puberty.
Subcellular location: [Isoform 1]: Secreted {ECO:0000269|PubMed:10548494, ECO:0000269|PubMed:17196548, ECO:0000269|PubMed:18547942}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:17196548}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:19931511}.
Interaction partners:
- Roundabout homolog 3
Sequence:
MHAMESRVLLRTFCVILGLEAVWGLGVDPSLQIDVLSELELGESTAGVRQVPGLHNGTKAFLFQDSPRSIKAPIATAERFFQKLRNKHEFTILVTLKQIHLNSGVILSIHHLDHRYLELESSGHRNEIRLHYRSGTHRPHTEVFPYILADAKWHKLSLAFSASHLILHIDCNKIYERVVEMPSTDLPLGTTFWLGQRNNAHGYFKGIMQDVQLLVMPQGFIAQCPDLNRTCPTCNDFHGLVQKIMELQDILSKTSAKLSRAEQRMNRLDQCYCERTCTMKGTTYREFESWTDGCKNCTCLNGTIQCETLVCPAPDCPAKSAPAYVDGKCCKECKSTCQFQGRSYFEGERSTVFSASGMCVLYECKDQTMKLVENAGCPALDCPESHQIALSHSCCKVCKGYDFCSEKHTCMENSVCRNLNDRAVCSCRDGFRALREDNAYCEDIDECAEGRHYCRENTMCVNTPGSFLCICQTGYIRIDDYSCTEHDECLTNQHNCDENALCFNTVGGHNCVCKPGYTGNGTTCKAFCKDGCRNGGACIAANVCACPQGFTGPSCETDIDECSEGFVQCDSRANCINLPGWYHCECRDGYHDNGMFAPGGESCEDIDECGTGRHSCANDTICFNLDGGYDCRCPHGKNCTGDCVHDGKVKHNGQIWVLENDRCSVCSCQTGFVMCRRMVCDCENPTVDLSCCPECDPRLSSQCLHQNGETVYNSGDTWVQDCRQCRCLQGEVDCWPLACPEVECEFSVLPENECCPRCVTDPCQADTIRNDITKTCLDEMNVVRFTGSSWIKHGTECTLCQCKNGHVCCSVDPQCLQEL
Protein: Large ribosomal subunit protein uL29 (60S ribosomal protein L35) (O74904)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL38A
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL28
Sequence:
MALKTFELRKQSQENLAEQLQELRQELASLRVQKIAGGSGSKLSKIKTTRKDIARILTVINESNRLAAREAYKNKKYIPLDLRQKKTRAIRRALTPYEQSRKTLKQIKKERYFPLRKYALKA
Protein: Storkhead box 1 (A0A2R8Y5I4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARPVQLAPGSLALVLCRLEAQKAAGAAEEPGGRAVFRAFRRANARCFWNARLARAASRLAFQGWLRRGVLLVRAPPACLQVLRDAWRRRALRPPRGFRIRAVGECGTRRGGASRPVQLAPGSLALVLCRLEAQKAAGAAEEPGGRAVFRAFRRANARCFWNARLARAASRLAFQGWLRRGVLLVRAPPACLQVLRDAWRRRALRPPRGFRIRAVGDVFPVQMNPITQSQFVPLGEVLCCAISDMNTAQIVVTQESLLERLMKHYPGIAIPSEDILYTTLGTLIKERKIYHTGEGYFIVTPQTYFITNTTTQENKRMLPSDESRLMPASMTYLVSMESCAESAQENAAPISHCQSCQCFRDMHTQDVQEAPVAAEVTRKSHRGLGESVSWVQNGAVSVSAEHHICESTKPLPYTRDKEKGKKFGFSLLWRSLSRKEKPKTEHSSFSAQFPPEEWPVRDEDDLDNIPRDVEHEIIKRINPILTVDNLIKHTVLMQKYEEQKKYNSQGTSTDMLTIGHKYPSKEGVKKRQGLSAKPQGQGHSRRDRHKARNQGSEFQPGSIRLEKHPKLPATQPIPRIKSPNEMVGQKPLGEITTVLGSHLIYKKRISNPFQGLSHRGSTISKGHKIQKTSDLKPSQTGPKEKPFQKPRSLDSSRIFDGKAKEPYAEQPNDKMEAESIYINDPTVKPINDDFRGHLFSHPQQSMLQNDGKCCPFMESMLRYEVYGGENEVIPEVLRKSHSHFDKLGETKQTPHSLPSRGASFSDRTPSACRLVDNTIHQFQNLGLLDYPVGVNPLRQAARQDKDSEELLRKGFVQDAETTSLENEQLSNDDQALYQNEVEDDDGACSSLYLEEDDISENDDLRQMLPGHSQYSFTGGSQGNHLGKQKVIERSLTEYNSTMERVESQVLKRNECYKPTGLHATPGESQEPNLSAESCGLNSGAQFGFNYEEEPSVAKCVQASAPADERIFDYYSARKASFEAEVIQDTIGDTGKKPASWSQSPQNQEMRKHFPQKFQLFNTSHMPVLAQDVQYEHSHLEGTENHSMAGDSGIDSPRTQSLGSNNSVILDGLKRRQNFLQNVEGTKSSQPLTSNSLLPLTPVINV
Protein: Ariadne RBR E3 ubiquitin protein ligase 2 (C9JZ71)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHH
Protein: Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9) (Q9VNT5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.
Subcellular location: Mitochondrion.
Interaction partners:
- Thioredoxin-2
- cystathionine gamma-lyase
- Thioredoxin reductase 1, mitochondrial
- Selenide, water dikinase 2
- FI04487p
- Inactive selenide, water dikinase-like protein
- dihydrolipoyllysine-residue acetyltransferase
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MSTIKFLRSSTHNALRSSLGWCRLAASRPRYDYDLVVLGGGSAGLACAKEAAGCGARVLCFDYVKPTPVGTKWGIGGTCVNVGCIPKKLMHQASLLGEAVHEAVAYGWNVDDTNIRPDWRKLVRSVQNHIKSVNWVTRVDLRDKKVEYVNSMATFRDSHTIEYVAMPGAEHRQVTSEYVVVAVGGRPRYPDIPGAVELGITSDDIFSYEREPGRTLVVGAGYVGLECACFLKGLGYEPTVMVRSIVLRGFDRQMSELLAAMMTERGIPFLGTTIPKAVERQADGRLLVRYRNTTTQMDGSDVFDTVLWAIGRKGLIEDLNLDAAGVKTHDDKIVVDAAEATSVPHIFAVGDIIYGRPELTPVAILSGRLLARRLFAGSTQLMDYADVATTVFTPLEYSCVGMSEETAIELRGADNIEVFHGYYKPTEFFIPQKSVRHCYLKAVAEVSGDQKILGLHYIGPVAGEVIQGFAAALKTGLTVKTLLNTVGIHPTTAEEFTRLSITKRSGRDPTPASCCS
Protein: Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAT-1) (EC 2.3.1.15) (P97564)
Organism: Rattus norvegicus (Rat)
Function: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipids biosynthesis such as triglycerides, phosphatidic acids and lysophosphatidic acids.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:10924502}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HCL2}. Note=Associated with the mitochondrion outer membrane of hepatic cells via a patch of basic residues. {ECO:0000250|UniProtKB:Q9HCL2}.
Interaction partners:
- 1-acylglycerol-3-phosphate O-acyltransferase 6
- Glycerol-3-phosphate acyltransferase 3
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Glycerol kinase
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- glycerol kinase
Sequence:
MEESSVTIGTIDVSYLPNSSEYSLGRCKHTNEDWVDCGFKPTFFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWERFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYILFVQERDVHKGMFATSITDNVLNSSRVQEAIAEVAAELNPDGSAQQQSKAIQKVKRKARKILQEMVATVSPGMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSSNTIPDILVIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGYVRVDFAQPFSLKEYLEGQSQKPVSAPLSLEQALLPAILPSRPDAAAAEHEDMSSNESRNAADEAFRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIHLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCVTITHTSRKDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSIYAVQNKRGSGGSAGGLGNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCQETVGKFIQYGILTVAEQDDQEDVSPGLAEQQWNKKLPEPLNWRSDEEDEDSDFGEEQRDCYLKVSQAKEHQQFITFLQRLLGPLLEAYSSAAIFVHTFRGPVPESEYLQKLHRYLLTRTERNVAVYAESATYCLVKNAVKMFKDIGVFKETKQKRASVLELSTTFLPQGSRQKLLEYILSFVVL
Protein: Trehalose-6-phosphate synthase (EC 2.4.1.15) (UDP-glucose-glucosephosphate glucosyltransferase) (Q6FNQ8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen [starch] synthase
- Glycogen [starch] synthase
- Trehalase
- Trehalase
- glycogenin glucosyltransferase
- 1,3-beta-glucan synthase
Sequence:
MTQIDKKEVSGNIIVVSNRLPVTISKDDTGKYQYKMSSGGLVTALQGLKKTATFKWYGWPGLEIPDDEKEQVKQDLLEQFNAVPVFLSDEVADLHYNGFSNSILWPLFHYHPGEINFDENAWLAYNEANRAFAEVIFETMQDDDLIWVHDYHLMLLPQMLQEEITKRKLRNVKLGWFLHTPFPSSEIYRILPVRQEILRGVLSCDLLGFHTYDYARHFLSSVQRVLNVNTLPNGVEYQGRFVNVGAFPIGIDVSTFQDGLLKQQVKDRISQLKETFKGQKIIIGVDRLDYIKGVPQKLHAMEVFLSEHPEWRGKVVLVQVAVPSRGDVEEYQYLRSVVNELVGRINGQFGTAEFVPIHFMHKSVPFEELISLYAVSDVCLVSSTRDGMNLVSYEYIACQEETKGSLILSEFAGAAQSLNGAIIVNPWNIDEMSDAINEALTLPEVKREVNWEKLFKYISKYTSAFWGENFVHELYNTSSSSGSIKSSEEKH
Protein: BTB/POZ domain-containing protein KCTD16 (Q5DTY9)
Organism: Mus musculus (Mouse)
Function: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization.
Subcellular location: Presynaptic cell membrane {ECO:0000269|PubMed:20400944}. Postsynaptic cell membrane {ECO:0000269|PubMed:20400944}. Note=Colocalizes with GABBR1. {ECO:0000269|PubMed:20400944}.
Interaction partners:
- Gamma-aminobutyric acid type B receptor subunit 1
Sequence:
MALSGNCSRYYPRDQGAAVPNSFPEVIELNVGGQVYFTRHSTLISIPHSLLWKMFSPKRDTANDLAKDSKGRFFIDRDGFLFRYILDYLRDRQVVLPDHFPERGRLKREAEYFQLPDLVKLLAPEDVKQSPDEFCHSDFEDASQGSDTRICPPSSLLPHDRKWGFITVGYRGSCTLGREGQADAKFRRVPRILVCGRISLAKEVFGETLNESRDPDRAPERYTSRFYLKFKHLERAFDMLSECGFHMVACNSSVTASFVNQYTEDKIWSSYTEYVFYREPSRWSSSHCDCCCKNGKGDKGESGTSCNDLSTSSCDSQSEASSPQETVICGPVTRQSNIQTLDRPIKKGPVQLIQQSEMRRKSDLLRTLTSGSRESNISSKKKAAKEKLSIEEELEKCIQDFLKIKIPDRFPERKHPWQSELLRKYHL
Protein: Eukaryotic translation initiation factor 4E-1 (eIF-4E-1) (eIF4E-1) (Protein cucumovirus multiplication 1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein) (O23252)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm {ECO:0000250|UniProtKB:K0P2S0}.
Interaction partners:
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor isoform 4G-1
- Eukaryotic translation initiation factor isoform 4G-2
- Nuclear cap-binding protein subunit 1
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit B
- Initiation factor eIF-4 gamma, MA3
- Eukaryotic translation initiation factor 2 subunit alpha
- Protein PIR
- Nuclear cap-binding protein subunit 2
Sequence:
MAVEDTPKSVVTEEAKPNSIENPIDRYHEEGDDAEEGEIAGGEGDGNVDESSKSGVPESHPLEHSWTFWFDNPAVKSKQTSWGSSLRPVFTFSTVEEFWSLYNNMKHPSKLAHGADFYCFKHIIEPKWEDPICANGGKWTMTFPKEKSDKSWLYTLLALIGEQFDHGDEICGAVVNIRGKQERISIWTKNASNEAAQVSIGKQWKEFLDYNNSIGFIIHEDAKKLDRNAKNAYTA
Protein: Anion exchange transporter (Solute carrier family 26 member 7) (Q8R2Z3)
Organism: Mus musculus (Mouse)
Function: Acts as a sodium-independent DIDS-sensitive anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport. May play a role in the maintenance of the electrolyte and acid-base homeostasis in the kidney, by acting as a distal excretory segment-specific anion exchanger, specifically chloride. Plays a major role in gastric acid secretion.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946, ECO:0000269|PubMed:19723628, ECO:0000269|PubMed:24810589, ECO:0000269|PubMed:30333321, ECO:0000269|PubMed:32726161}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:16524946}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q8TE54}; Multi-pass membrane protein {ECO:0000255}. Lateral cell membrane {ECO:0000250|UniProtKB:Q8TE54}; Multi-pass membrane protein {ECO:0000255}. Note=Expressed on the basolateral membrane of acid-secreting gastric parietal cells, distal nephron segments and apical domains of proximal tubules and in the glomerulus. Expressed in the cytoplasm in recycling endosomes of kidney outer medullary collecting duct cells and in acid-secreting gastric parietal cells. Targeted to the basolateral membrane in hypertonicity and potassium depletion. {ECO:0000250|UniProtKB:Q8TE54, ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946}.
Interaction partners:
- Anion exchange protein 2
Sequence:
MTGAKRKKRSVLWGKMHTPHREDIKQWCKRRLPILEWAPQYNLKENLLPDTVSGIMLAVQQVAQGLSFAMLSSVHPVFGLYGSLFPAIIYAIFGMGRHVATGTFALTSLISANAVERLVPQSSRNLTTQSNSSVLGLSEFELQRIGVAAAVSFLGGVIQLVMFVLQLGSATFLLTEPVISAMTTGAATHVVTSQVKYLLGIKMPYISGPLGFFYIYAYVFENIKSVQLEALLFSLLSIIVLVLVKELNEQFKRKIKVVLPVDLVLIIAASFACYCTNMENTYGLEVVGHIPNGIPPPRAPPMNILSAVLTEAFGVALVGYVASLALAQGSAKKFKYSVDDNQEFLAHGLSNVIPSFLFCIPSAAAMGRTAGLYSTGAKTQVACLISCIFVLIVIYAIGPLLYWLPMCVLASIIVVGLKGMLIQFRDLKKYWNVDKIDWGIWISTYIFTICFAANVGLLFGVICTIAIVLGRFPRAKTLSITDMKEMELKVKTEMHDETSQQIKIISINNPLVFLNAKKFSADLMKIILKESDSNQPLDDVSKCEQNTLLSSLSNGNCNEEASQPCSSEKCSLVLNCSGLTFFDYTGVSTLVELYLDCKSRSVDVFLANCTASLIKAMTYYGDLDTEKPIFFDSVPAAISIIQSNKNLSKASDHSEV
Protein: Forkhead box E3 (Forkhead box protein E3) (B0UXI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Pituitary homeobox 3
- Paired box protein Pax-6
- Alpha-crystallin A chain
Sequence:
MNLANFSYFTGMCNMTAESQHSPAEAASPVVVSPNVSLDSPVPLPPLALNHQARTKDGILIKAEPQGSSPNTDREEVVSLGQTEEHLPATGSRRRKRPVQRGKPPYSYIALIAMAIANSPERKLTLGGIYKFIMERFPFYRENSKKWQNSIRHNLTLNDCFVKIPREPGRPGKGNYWTLDPAAEDMFDNGSFLRRRKRFKRTDVSTYPGYMQSSSAFTPTPMGRQAYPNTLYPGVTSGYGSQLAGSPHPAMLHHYQASAGVTQGQARMFSIDNIISQQTVMQSGGDLNTQSLGLGAGDLGTMTSSCSVSTSDPTCFQTQAINPTSNMLSRNTGSLASNMTSSYTYPSPTSPSHLSGVTQSGFSPGGSQVYCSGNRISLPPVRSGSCADHTEPLLGLSGPTMNSYNNSYMRQANFASGLERYM