wanglab/gogpt-training-data huggingface dataset:
Protein: Mucolipin-3 (Transient receptor potential channel mucolipin 3) (TRPML3) (Q8TDD5)
Organism: Homo sapiens (Human)
Function: Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity. Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway. Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth (By similarity). Involved in the regulation of autophagy. Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process (By similarity). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19522758, ECO:0000269|PubMed:29106414}; Multi-pass membrane protein {ECO:0000269|PubMed:29106414}. Early endosome membrane {ECO:0000269|PubMed:19497048, ECO:0000269|PubMed:19522758}; Multi-pass membrane protein {ECO:0000269|PubMed:29106414}. Late endosome membrane {ECO:0000269|PubMed:19497048, ECO:0000269|PubMed:19522758}; Multi-pass membrane protein {ECO:0000269|PubMed:29106414}. Lysosome membrane {ECO:0000269|PubMed:19522758}; Multi-pass membrane protein {ECO:0000269|PubMed:29106414}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:19522758}. Note=Recycles between the plasma membrane and intracellular compartments by a dynamin-dependent endocytic pathway (PubMed:19522758). Under normal conditions, only a very minor proportion is present at the cell membrane (PubMed:19522758). In the cochlea located at the base of stereocilia near the position of the ankle links (By similarity). {ECO:0000250|UniProtKB:Q8R4F0, ECO:0000269|PubMed:19522758}.
Interaction partners:
- Mucolipin-2
- Mucolipin-1
- Transient receptor potential cation channel subfamily V member 5
Sequence:
MADPEVVVSSCSSHEEENRCNFNQQTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTIAFKHLFLKGYMDRMDDTYAVYTQSDVYDQLIFAVNQYLQLYNVSVGNHAYENKGTKQSAMAICQHFYKRGNIYPGNDTFDIDPEIETECFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHYMMIFDAFVILTCLVSLILCIRSVIRGLQLQQEFVNFFLLHYKKEVSVSDQMEFVNGWYIMIIISDILTIIGSILKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAAMIYLGYCFCGWIVLGPYHDKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRIYLYSFISLFIYMILSLFIALITDTYETIKQYQQDGFPETELRTFISECKDLPNSGKYRLEDDPPVSLFCCCKK
Protein: Thyroid hormone receptor interactor 11 (B2RY51)
Organism: Mus musculus (Mouse)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
Sequence:
MSSWLGGLGSGLGQSLGQVGGSLASLTGQISNFTKDMLLEGTEDVPADFPNSGREENEATHSVLRSENERLKKLYTDLEEKHEASELQIKQQSSSYRSQLQQKEEEINHLKARQLALQDELLRLQSAAQSAHSGSGSAPAASASSSFSYGVSHRVSAFHEDDMDFGDVISSQQEINRLSNEVSRLESELGHWRHIAQTKVQGAQSSDQTEICKLQNIIKELKQNRSQDLDDHQHELSALQNAHQQKLTEISRRHREELSDYEERIEELENLLQQGGSGVTVTDHSKVYEMQNTIQILQMEKVESTKQIEDLENKIKEIHKRLSSAEHDQEVWKKEQERLEVEKREMTEQCERLKLELSEAQQSALRQSDAAVEEETILPHSSSVAEVLRLQQALTDAENEIMRLRSLNQDISLAEDNQKLQMCVQTLEKEKSLLSQEKEELQISLSKLSSEYEVIKSTASRDLDLFSQVHDLKHNLEAKEQELNQSIHENEILMAELEELDKQNQEATKHVILIKDQLSKQQSEGDSVIKKLKEELAGEKQRTHQLEDDKMNIIKELTVQKEKLTHSEQALSDLQLTKQKLEDKVEDLVDQLSKSEKNNFDIQKENHELREHIRQNEEELSTVRSELTQSQTQGSSRNVKDDLLKERETQVQNLKQNLSEVEQLNEHLEQVAFDLRTENEELLEAYEEVRNQLEESVAGNKQISLEKTAMLEWEKAPLETELCRAEKRVLEEERKYEQTVQELSSACSPDTSALQLEQERLIQLNQEKDFEIAELKKSIEQMDTDHKRTKETLSSSLEEQKQLTQLINEKEICIVKLKEKSSELQKELDKCAQTLRKNETLRQTIEEKDRSLGSMKEENNHLQEELERLREQQSRVVPAPEPRTLDSTTELESELSQLHRIKGHLEEEIKHHQKMIEDQNQSKLQLLQSLQEQKKELDEFKYQHEQMSISHTRLFLEKDEEIKNLQKTIEQIKAQLHEERQDSQTENSDIFQETKVQSLSIEHGSEKHDLSKAETERLVKGIKERELEIKLLNEKNTSLTKQIDQLSKDEVGKLTQIIQQKDLEIQALHARISSASYSQDVVYLQQQLHAYAMEREKVMVILNEKTRENSQLKTEYHKVIDIISAKEAALIKLQDENKKMSTRFESSGQDMFKETIQNLSRIIREKDIEIDALSQKCQTLLTVLQTSGTGSEAGGVNSNQFEELLQERDKLKQQVKKMEEWKQQVMTTVQNMQHESAQLQEELHQLQAQVSVDSDNNSKLQVDYTGLIQSYEQNETKLKNFGQELAQVQHSIGQLCNTKDLLLGKLDIMSPQLSSGSSLTSQAAEPLRASQSSEPHESSQLLQQEVDDLRKSLQEKDATIRTLQENNHRLSDSVAASSEVERKEHEQADSEIKQLKEKQEVLQNLLKEKDLLIKAKSDQLHSSNENLANKVNENELLRQAVTNLKERILILEMDISKLKGENEKIVDASKGKETEYQALQETNMKFSMMLREKEFECHSMREKALAFEQLLKEKEQGKAGELNQLLNAVKSMQEKTVTFQQERDQVMLALKQKQMETSTLQNEVQRLRDKESRLNQELQRLRDHLLESEDSHTREALAAEDREAKLRKKVSVLEEKLVSSSNAMENASHQASVQVESLQEQLNMVSKQRDETALQLSVSQEQVKQYALSLANLQMVLEHFQQEEKAMYSAELEKQNHLLAEWKKKAESLEGKVLSLQERLDEANAALDSASRLTEQLDLKEEQIEELKKQNELHQEMLDDAQKKLMSLVNSTEGKVDKVLMRNLFIGHFHTPKHQRHEVLRLMGSILGVKREEMEQLFAEDQGGVTWWMAGWLGGGSKSVPNTPLRPNQQSVFNSSFSELFVKFLETESHPSVPPPKLSVHGLKPLDSPGRRKADTGIPESFRDTAESRAGRRTDVNPFLAPRSAAVPLINPAGHGPGGPGHLLLKPISDVLPTFTPLPVSPDNSAGVVLKDLLKQ
Protein: Beta,beta-carotene 15,15'-dioxygenase (EC 1.13.11.63) (Beta-carotene dioxygenase 1) (Beta-carotene oxygenase 1) (Q9I993)
Organism: Gallus gallus (Chicken)
Function: Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:10799297}.
Interaction partners:
- Aldehyde dehydrogenase 1A1
- Uncharacterized protein
- NADP-retinol dehydrogenase
- Uncharacterized protein.
- Aldehyde dehydrogenase
- Uncharacterized protein.
- Alcohol dehydrogenase 1
- Uncharacterized protein
- Uncharacterized protein
- Retinal dehydrogenase 2
Sequence:
METIFNRNKEEHPEPIKAEVQGQLPTWLQGVLLRNGPGMHTIGDTKYNHWFDGLALLHSFTFKNGEVYYRSKYLRSDTYNCNIEANRIVVSEFGTMAYPDPCKNIFAKAFSYLSHTIPEFTDNCLINIMKTGDDYYATSETNFIRKIDPQTLETLDKVDYSKYVAVNLATSHPHYDSAGNILNMGTSIVDKGRTKYVLFKIPSSVPEKEKKKSCFKHLEVVCSIPSRSLLQPSYYHSFGITENYIVFIEQPFKLDIVKLATAYIRGVNWASCLSFHKEDKTWFHFVDRKTKKEVSTKFYTDALVLYHHINAYEEDGHVVFDIVAYRDNSLYDMFYLKKLDKDFEVNNKLTSIPTCKRFVVPLQYDKDAEVGSNLVKLPTSATAVKEKDGSIYCQPEILCEGIELPRVNYDYNGKKYKYVYATEVQWSPVPTKIAKLNVQTKEVLHWGEDHCWPSEPIFVPSPDAREEDEGVVLTCVVVSEPNKAPFLLILDAKTFKELGRATVNVEMHLDLHGMFIPQNDLGAETE
Protein: Beta-1,3-galactosyltransferase 2 (Beta-1,3-GalTase 2) (Beta3Gal-T2) (Beta3GalT2) (EC 2.4.1.86) (UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase 2) (O43825)
Organism: Homo sapiens (Human)
Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N-acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 4
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 2
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 3
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- Beta-1,3-galactosyltransferase 5
- Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase
Sequence:
MLQWRRRHCCFAKMTWNAKRSLFRTHLIGVLSLVFLFAMFLFFNHHDWLPGRAGFKENPVTYTFRGFRSTKSETNHSSLRNIWKETVPQTLRPQTATNSNNTDLSPQGVTGLENTLSANGSIYNEKGTGHPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNESLAPGIQITRIFLLGLSIKLNGYLQRAILEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHIPYVMKTDSDMFVNTEYLINKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFSGDLAEKIFKVSLGIRRLHLEDVYVGICLAKLRIDPVPPPNEFVFNHWRVSYSSCKYSHLITSHQFQPSELIKYWNHLQQNKHNACANAAKEKAGRYRHRKLH
Protein: Nitrogenase iron protein (EC 1.18.6.1) (Nitrogenase Fe protein) (Nitrogenase component II) (Nitrogenase reductase) (P22921)
Organism: Rhodospirillum rubrum
Function: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
Interaction partners:
Sequence:
MSALRQIAFYGKGGIGKSTTSQNTLAALVEMGQRILIVGCDPKADSTRLILNTKLQDTVLHLAAEAGSVEDLDVADVVKIGYKGIKCTESGGPEPGVGCAGRGVITAINFLEENGAYDDLDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMALYAANNIAKGILKYAHTGGVRLGGLICNERQTDKEVELAEALAGRLGCRLIHFVPRDNGVQHAELRRQTVIQYAPDSKQAGEYRTLATKIHNNSGQGVVPTPITMEDLEEMLMEFGIMKSDEEALAELEAKESAAAN
Protein: Probable HTH-type transcriptional regulator LeuO (P46924)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Interaction partners:
- Transcriptional regulator
- LuxR/UhpA family transcriptional regulator
- Transcriptional activator of cad operon
- Transcriptional regulator SlyA
- Transcriptional repressor of cel operon
- LysR family transcriptional regulator
- Leucine-responsive regulatory protein
- Putative aminopeptidase SgcX
Sequence:
MPEVKTEKPHLLDMGKPQLRMVDLNLLTVFDAVMQEQNITRAAHTLGMSQPAVSNAVARLKVMFNDELFVRYGRGIQPTARAFQLFGSVRQALQLVQNELPGSGFEPTSSERVFNLCVCSPLDNILTSQIYNRVEKIAPNIHVVFKASLNQNTEHQLRYQETEFVISYEEFRRPEFTSVPLFKDEMVLVASRKHPRISGPLLEGDVYNEQHAVVSLDRYASFSQPWYDTPDKQSSVAYQGMALISVLNVVSQTHLVAIAPRWLAEEFAESLDLQILPLPLKLNSRTCYLSWHEAAGRDKGHQWMEDLLVSVCKR
Protein: RPTOR independent companion of MTOR, complex 2 (A0A8I5ZQ26)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MITVNASLFPSSVANSLIAVGNDGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRINEALITTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLKEDREARFLASKMGIIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTDEFIEALLSVDPGRFQDSWRLSDGFVAAEAKTILPHRARSRPDLMDNYLALILSAFIRNGLLEGLVEVITNSDDHISVRATILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLRASAALNCLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQYLRVQKDIFVLKDTEEALLINLRDSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKPSSKLYASLDLDFAKSKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQWLNASSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVILSKVLTAATDACRLYATKHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAKQLEKWHKEYNSKYVDLIEEQLNEALTTYRKPIDGDNYVRRSNQRLQRPHVYLPIHLYGQLVHHKTGCHLLEVQSIITELCQNVRTPDLDKWEEIKKLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHSWDSVRHSRKHLWPVVPDDVEQLCNELSSVPSTLSLNSESTSSRHNSESESAPSSMFILEDDRFGSSSTSTFFLDINEDAEPAFYDRPGPIKDKNSFPFFASSKLVKNRILNSLTLPTKKHRSSSDPKGGKLSSENKTSNRRIRTFTEPSVDFNHSDDFTNISPAQKTLQLETSFVGNKHLEDTGSTPSIGDNDLKFPKSFGPENHRENTSRERLVVESSAGSHMKIRSQSFNTDTTTSGISSMSSSPSRETVAVDSTTMDTDCGSLSTVVSTKTVKTSHYLTPQANHLSLSKSNSVSLVPPGSSHTLPRRAQSLKAPSIATIKSLADCNFSYTSSRDAFGYATLKRLQQQRMHPSLSHSEALASPAKDVLFTDTITMKANSFESRLTPSRFMKALSYASLDKEDLLSPINQNTLQRSSSVRSMVSSATYGGSDDYIGLALPVDINDIFQVKDIPYFQSKHVPPPDDRGARTFSHDGGGLPSGTGSLVKNSFHLLRQQMSLTEIMNSVHSDASLFLESTEDTGLQEHTDDNCLYCVCIEILGFQPSNQLSSICSHSDLQDIPYSDWCEQPIHNPLEVVPSKFSGISGCSDGASQEEGSASSTKSTELLLGVKTIPDDTPMCRILLRKEVLRLVVNLSSSVSTKCHETGLLTIKEKYPQTFDDICLYSEVSHLLSHCTFRLPCRRFIQELFQDVQFLQMHEEAEAVLAIPPNQPIVDESAES
Protein: Uncharacterized protein, isoform R (M9PER6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVAQWKIINENYKNLEGYKRVAWPPASEERIIREFTPQPQTQSPAPGAGGYYPQAHAPTAAAAAPPQGPIYNNVQPRTTQTPQNAYPSAPQTTSTAYPTNQYPDSYSHQEQQQQQQQQQPVQYTQAQFGRQRSREPVQVSAPSPAPATDPSGYPYQANYQSNYPQEPLQAVNNVGGGWKHIGAPQPKSRSEFTAGNGAYPPFQGSYQQQQQQPQQQYGAPSYDGQQPGAQWQQQQQQQQVPQQQYQPQSQAQAPYQPPQWNQPQQQQQQPSYQASPYQQQQQQQPSYYPQQNGGSTYAQPPYNSYSQPQLPYSQDQTDLQQQQQQQQQQYPGAYAGQDSYRGASPGIITLRKEAPVSQKPAPVYTSQPAAVSYQGGSKLRGDLKWPPPEYKEAAARENEERRQLALGPVCRPRRVNRDYTPFFAKHQLNNGYPSYKVPPGTQHIFG
Protein: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTA/SAH nucleosidase) (EC 3.2.2.9) (5'-methylthioadenosine nucleosidase 2) (AtMTAN2) (MTA nucleosidase 2) (S-adenosylhomocysteine nucleosidase) (AdoHcy nucleosidase) (SAH nucleosidase) (SRH nucleosidase) (Q7XA67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Enzyme of the methionine cycle that catalyzes the irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to a lesser extent, to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Contributes to the maintenance of AdoMet homeostasis and is required to sustain high rates of ethylene synthesis.
Interaction partners:
- Methylthioribose kinase
- 1-aminocyclopropane-1-carboxylate synthase 9
- 1-aminocyclopropane-1-carboxylate synthase 8
- Spermidine synthase 2
- 1-aminocyclopropane-1-carboxylate synthase 11
- 1-aminocyclopropane-1-carboxylate synthase 5
- 1-aminocyclopropane-1-carboxylate synthase 7
- Spermidine synthase 1
- Spermine synthase
- 1-aminocyclopropane-1-carboxylate synthase 4
Sequence:
MEGVMGQVEKRPISTIVFIVAMQKEAQPLINRLRLVEEVNTPFPKEVTWIMFKGMYKDLNINIVCPGKDSTLGVESVGTVPASLVTYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLIKELNLKVGRLSTGDSMDMSPHDEESITANDATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTSEEFLENLAAVTAKLDESLTKVIDFISGKCLSDL
Protein: Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Q04933)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MFRRCFPIFNPYDVVVVGGGPGGYVAAIKAAQLGLKTACVEKRGALGGTCLNVGCIPSKALLHATHMYHDAHANFERYGLMGGAGVTMDVAKMQQQKEKSVNGLTSGVEYLLKKNKVTYYKGEAGFVTPNTLNVKGIDGKDEAIEAKNTIIATGSEPTALPFLPFDEKVVLSSTGALALQQVPKKMVVIGGGVIGLELGSVWARLGSDVTVVEFAPRCAPTLDSDVTDALVGALKRNGEDEVPMTGIEGVNGTNNGSIALTLEVEQAGGQAETLHCDALLVSVGRRPYTAGLGLEKNNVSLNERGFVKIGSHFETNVAGVYAIGDVVDKGPMLAHKAEDEGVACAEILAGRPGHVNYDVIPGVIYTMPEVASVGKTEEELKKAGVAYKVGKFPFNANSRAKAVATEDGFVKVLTDKATDRILGVHIVCSAAGELIAGALLAMEYGASSEDVGRTCHAHPTMSEAVKEACMACFAKTINF
Protein: Hepatocyte nuclear factor 3-beta (HNF-3-beta) (HNF-3B) (Forkhead box protein A2) (Transcription factor 3B) (TCF-3B) (Q9Y261)
Organism: Homo sapiens (Human)
Function: Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). In embryonic development is required for notochord formation. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas and lungs; FOXA1 and FOXA2 seem to have at least in part redundant roles. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; regulates the expression of genes important for glucose sensing in pancreatic beta-cells and glucose homeostasis. Involved in regulation of fat metabolism. Binds to fibrinogen beta promoter and is involved in IL6-induced fibrinogen beta transcriptional activation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:14500912}. Cytoplasm {ECO:0000269|PubMed:14500912}. Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner; in response to insulin signaling via AKT1 is exported from the nucleus.
Interaction partners:
- Pancreas/duodenum homeobox protein 1
- Hepatocyte nuclear factor 6
- Sonic hedgehog protein
- Transcription factor SOX-17
- Ribosomal protein S6 kinase beta-1
- Homeobox protein OTX2
- Ribosomal protein S6 kinase beta-2
- Hepatocyte nuclear factor 1-alpha
- POU domain, class 5, transcription factor 1
- Hypoxia-inducible factor 1-alpha
Sequence:
MLGAVKMEGHEPSDWSSYYAEPEGYSSVSNMNAGLGMNGMNTYMSMSAAAMGSGSGNMSAGSMNMSSYVGAGMSPSLAGMSPGAGAMAGMGGSAGAAGVAGMGPHLSPSLSPLGGQAAGAMGGLAPYANMNSMSPMYGQAGLSRARDPKTYRRSYTHAKPPYSYISLITMAIQQSPNKMLTLSEIYQWIMDLFPFYRQNQQRWQNSIRHSLSFNDCFLKVPRSPDKPGKGSFWTLHPDSGNMFENGCYLRRQKRFKCEKQLALKEAAGAAGSGKKAAAGAQASQAQLGEAAGPASETPAGTESPHSSASPCQEHKRGGLGELKGTPAAALSPPEPAPSPGQQQQAAAHLLGPPHHPGLPPEAHLKPEHHYAFNHPFSINNLMSSEQQHHHSHHHHQPHKMDLKAYEQVMHYPGYGSPMPGSLAMGPVTNKTGLDASPLAADTSYYQGVYSRPIMNSS
Protein: Probable transcriptional regulator (Q9HTQ3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transcriptional regulator
- Probable transcriptional regulator
- FAD dependent oxidoreductase domain-containing protein
Sequence:
MDVGARLQTIRKLKGLSQRELAKRAGVTNSTISMIEKNSVSPSISSLKKVLGGIPMSLVEFFSLDLEQDSHTQVVYKADELIDISSGAVSMRLVGKAHPSRAIAFLDETYPPGSDTGEEMLNHEGEEAGVLVDGRLELTVGSETYVLERGDSYYFESNKPHRFRNPYDVPARLISATTPANF
Protein: Alpha-2-macroglobulin-P (Alpha-2-macroglobulin) (Q6GQT1)
Organism: Mus musculus (Mouse)
Function: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Prolow-density lipoprotein receptor-related protein 1
- Kallikrein 1-related peptidase b8
- Kallikrein 1-related peptidase b5
- Kallikrein 1-related peptidase b9
- Endoplasmic reticulum chaperone BiP
- Apolipoprotein A-I
- Vitamin K-dependent protein C
- Prothrombin
- Albumin
- Transforming growth factor beta-1 proprotein
Sequence:
MGKRWLPSLALLPLPPPLLLLLLLLLPTNASAPQKPIYMVMVPSLLHAGTPEKGCLLFNHLNETVTVKVSMESVRGNQSLFTDLVVDKDLFHCASFIVPQSSSNEVMFLTVQVKGPTHEFRRRSTVLIKTKESLVFAQTDKPIYKPGQMVRFRVVSLDENFHPLNELIPLLYIQDSKKNRIAQWQNFRLEGGLKQLSFPLSSEPTQGSYKVVIRTESGRTVEHPFSVKEFVLPKFEVKVAVPETITILEEEMNVSVCGIYTYGKPVPGHVTVNICRKYSNPSSCFGEESLAFCEKFSQQLDGRGCFSQLVKTKSFQLKRQEYEMQLDVNAKIQEEGTGVEETGKGLTKITRTITKLSFVNVDTHFRQGIPFVGQVLLVDGRGTPIPYEMIFIGADEANQNINTTTDKNGLARFSINTDDIMGTSLTVRAKYKDSNVCYGFRWLTEENVEAWHTANAVFSPSRSFVHLESLPYKLRCEQTLAVQAHYILNDEAVLERKELVFYYLMMAKGGIVRAGTHVLPVTQGHKKGHFSILISMETDLAPVARLVLYTILPNGEVVGDTVKYEIEKCLANKVDLVFHPNIGLPATRAFLSVMASPQSLCGLRAVDQSVLLTKPEAELSASLVYDLLPVKDLTGFPKGVNQQEEDTNGCLKQNDTYINGILYSPVQNTNEEDMYGFLKDMGLKVFTNLNIRKPKVCERLGVNKIPAAYHLVSQGHMDAFLESSESPTETTRSYFPETWIWDLVIVDSTGVAEMEVTVPDTITEWKAGAFCLSNDTGLGLSPVIDFQAFQPFFVDLTMPYSVIRGEAFTLKATVLNYLQTCIRVGVQLEASPDFLATPEEKEQKSHCICMNERHTMSWAVIPKSLGNVNFTVSAEALDSKELCRNEVPVVPERGKKDTIIKSLLVEPEGLENEVTFNSLLCPTGAEVSEQISLKLPSDVVEESARASVTVLGDILGSAMQNTQDLLKMPYGCGEQNMVLFAPNIYVLDYLNETEQLTQEIKTKAITYLNTGYQRQLNYKHRDGSYSTFGDKPGRSHANTWLTAFVLKSFAQARRYIFIDESHITQALTWLSQQQKDNGCFRSSGSLLNNAMKGGVEDEVTLSAYITIALLEMSLPVTHPVVRNALFCLDTAWKSARRGASGNHVYTKALLAYAFALAGNQDTKKEILKSLDEEAVKEDNSVHWTRAQKPRVPADLWYQPQAPSAEVEMTAYVLLAYLTTELVPTREDLTAAMLIVKWLTKQQNSHGGFSSTQDTVVALHALSKYGAATFTRAKKAAHVTIQSSGAFYTKFQVNNDNQLLLQRVTLPTVPGDYTAKVAGEGCVYLQTSLKYSVLPREKEFPFALVVQTLPGTCEDLKAHTTFQISLNISYIGSRSDSNMAIADVKMVSGFIPLKPTVKMLERSVHVSRTEVSNNHVLIYLDKVSNQMLTLFFMVQQDIPVRDLKPAIVKVYDYYEKDEFAVAKYSAPCSAGYGNA
Protein: Kinesin light chain (Q21592)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367020}.
Interaction partners:
Sequence:
MVISLGDDITTVLKTVQQTLFALRDEHEAATRILEANLINSDSSEPSLPSEKMGLIDESLGKVMDGGDEASLLIMMDKLMQSYDVQLSKNHESIRLLRQENTWLLDELTTTQRKLQESERTVAHLEEERDHYKFQDSMNYLNSDFQHTTSVDATPMMVDTLQELGFGPEEEDQNNNQADQGCRSSSFSNPISNDYQLPTRLQTLQNLVIQYMEQGRFEVAIPLCKQALEDVVKVHGNVHLDVATMLNVLAIVYRNQENFKDAAIYLEKALSIRVQCCGENHHSVAATLNNLAIAYGKRGKYKESEPLCKRALEIRKNLLGPNHPDVAKQLTNLGIVTQQLEKYEETENYFKQALSIYNRAFPENHQNVIKTKNQLASVFLKQGKYQEAEEMYKNILSKVAITGNKPIWRIAEDREERQRNGIPKVDDESFNVNPTTVMDSNVMSTIKNLAAVYRKQGKEEAAGTLEEALGAKKQINGGADHTNSTASSVETSSAVAINPAQSGIKKRIMHFVGLNF
Protein: Polychaetoid, isoform O (A0A0B4K6Y7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Canoe, isoform E
- DE-cadherin
- Cortactin, isoform A
- Adherens junction protein p120
- Transcriptional coactivator yorkie
- Atypical protein kinase C
- Vinculin
- Leucine-rich repeat, isoform F
- Patj homolog
- Cdc42 homolog
Sequence:
MKPSTRRRSFKTKPPKSNVYNPLVRYRPTAYVRNGIIGGAEGPGSSGVYQIADRVYTTSKMFLRDGYMYPRQPGQTMDPRFPLELHEFPQQFGATGLQLVSAPKVHIAGEYLASEQQQQQQQQQQQHQQVQEQQQLGRRKAAAAAEINLANQVYWLGKQKTRSRSRSNSVGNRSITSCMGGGGGGGEKERERGGDRDRPYIRNVDDLLQALGKRDGGDNNSNLLETASTHSSSQRRRFKKGDRTTWEYHTVAVTRVPGYGFGIAVSGGRDNPHFANGDPSIAVSDVLKGGPAEDRLQVNDRIISVNGVSLENVEYATAVQVLRDSGNTVQLVVKRRVPLNPINAAGAVQHQHSHSLSSVGLMANGSGGVAPTPITSLSQPNSLNSSLVQNASSGQPIKVTLTKGGKKDDYGVVLGCRLFVKEISSKAREQLNANGYSLQEGDIITRIHNTNCGDTMSLKEAKKIIDGCKERLNLVVLRDITNQTAVSQLNLNNSASHQASGNIYATHQPQVSGCSSSNNNLEDPYLPGGASYSSQNLYVQPPTRTSNGPNINGNGLNDEKSNLTPRGRSRGPIMDGVSLQQLDRPVTPTRGRSAAIDEPPRPPPPRGSSGGAAQEDFYSSRRQLYEERQSAEPRFISFQKEGSVGIRLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQYCKEEYDEVVTNQRGDSFHIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAEELATAQFNATKKEMNANESRGNFFRRRRSTHRRSKSLSRENWDDVVFSDSISKFPAYERVVLRHPGFVRPVVLFGPVSDLARERLAKDFPDKFSTPLQDDDKSAATSGKCRIVRLSNIRDVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLKTDSKHVIKQLRHGLPKAAHKSSKKLLEQCQKLERVWSHIFSTQIALSDEESWYRKLRDSIDLQQSGAVWMSESKPVESLSDDFLFPMTTSRLSYASSPESDLELSPGPSASLSLGNLPQLVKASSDPSIATNQDNLDRDRDIIGEGLPPPYTVPYDHAVPANPNRRQTMDSSKYSIYGTNVPPQQQQPGVGGDTAAVRPQSLYGINAPDLPPRIDRQSKPGDIPLNTSGSSSRNGTLGRSAQERLFGKAVVQDDVQAEYITRNALVGSGAAETLDRQQQQQQQTHASLERQARLNAQLKANGVGAGGGGASTYDSVSSYDSYNNTQMAMQNLGRLGPNAPDDLKSVPNANGRPLPPTGQSHEYGRTPHDHRSFGGPNDLNRQSSPGRPHYHDMNASRNIDPRNGTPQRPSNLGLESSPRKPLVETKTDYGKYSRNNSVTQADYTKLPKTAPHGVVPPPNVSNGQGQMNGSGTPSSNGSGPFKPVPPPKPKNYRPPVQSGGSSGSGGTTPWENGDSGSPRSPNGFYYPPTPSHHHYGQQATPGSPSNGHMQPPPPQQQQPTYGGSNGNYGQAPPPQSYPQANGYNGNGHHYNGGSGTGPYIAPHRGMPPPIGNLPPHTPERHALDLAGSREQRGSAFELYRKPQIGATAGHHHNMSEMEPYDERYDDYYNMPPPAAHPSQGHHMQRSRSAPRYPHERPPHAQDPNYYGHYGTSRGHSQPRQQYSQHHQQQYYDDHGLEMGPPPLPPHKKKKSVLKSPLVALKNALLKSTRPLRRMNSMVEPERKPKGLRRQQSMLERGVQRPYYPDEYPTYPAGFEERAHGGQGMMQPHSQDAYYQRGGHYAPQQQEMMNSTYQNLEGEDIYGNIGNTVPRMPHHQDNGYGYDQYDLYANRACIDLERRQAEAAAASGGRNGRRIVRRHSTTTADRGGNPGPPRRPMISPGYEQDPQEIYQTRNGAYMLPDQRRAPSSEVMTRRRFYPGAANEQTEEEPLYQSRREMQREMQRNHLYQSKREMQERISQGKRDMEREFSPQSSSSQSEASNSEAIYQSRREAKESALKTRSQLRDQIYQTRREALDSMAEPIYVSKRGMGRPAPIYETREESILQSRENETDEKKEKECKTEQIQVEINAQPEEQIEDSTLSRSDLQKSSDTVIENPARAPLVQDEVDDDEEEEVQDQRDPAESSADQTEQPTAIENNLHNEGMVEQSQNDSDDVFEAADKVSPLAPPPAPVQPPTPRSGRAPFHISNILKRTAPPPSSPIGDSCTSIETQYTSQASLPVGPPNATSTPFSSSMSLPIAGPVNNQPSANGRFPTLPREPSTSRGFFDSNGGTLADKLWHVSLQIPPGAIPAGVRQEIYFTVSDPRMGQAVGGPPLDMENGETMLSPLVMCGPQGLEFLVPVTLNIPHCAGRTASLGLALKATDSEKNLHTEWDNIDLPSNAAAHTVSVKVDHF
Protein: Sodium-dependent high-affinity dicarboxylate transporter 2 (Na(+)/dicarboxylate cotransporter 2) (NaDC-2) (ceNaDC2) (P32739)
Organism: Caenorhabditis elegans
Function: High-affinity sodium-dicarboxylate cotransporter that accepts a range of tricarboxylic acid-cycle intermediates with 4-5 carbon atoms. There is no interaction with monocarboxylates (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Facilitated glucose transporter protein 1
Sequence:
MKPSPQRTLIKKLLVLLGPLVAVPLLFFGPEYRCLFSIIFLSTYWIGEAFPIGVTSLFPLALYPILQIVPSKQISPVYFKDSIVLFMCTLIMAMAVEATGLHRRIALKLLTKVGAKQPVMLLGFMCITSFISFFVSDTACTALMCPTAVALLMSMSDAVQHLKEDHRKPKPPPDDATVAEKLRIDDMTPQDAGFCKALILACAHASLIGGTAIITSTGPNLVFRENIHKRYPEGQVTMTYLQWMVFAIPPMFVYLLASYIILVCYFMGPSTFARWFERPSKEEAHLKKLIEKNIQTMYEDLGDVSWGEKSVFVFFILLIGSWISRDPGFTPGWGDLLPHRNFISDSVSGVLISCILFVWPKDPFDPIDPMAPILKWTDMKSKFSWSCTLLIGAGYAISEGVDKSGLSRLISCGMKNIFVGMSSLPLQLTVTTIIVIMTEFASNVSTGSIFIPISLGVAESMGVHPLYLALPTTVACSFAFMLPISTPPNAVVYDTKVISMVEMIVCGFLLNIACILITSLNMNTWTYFIFSLNIFPENIVISSENSSYPVC