wanglab/gogpt-training-data huggingface dataset:
Protein: Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Bile acid-CoA thioesterase) (Choloyl-CoA hydrolase) (EC 3.1.2.27) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2) (Q91X34)
Organism: Mus musculus (Mouse)
Function: Catalyzes the amidation of bile acids (BAs) with the amino acid taurine. Selective for taurine conjugation of cholyl CoA and only taurine-conjugated BAs are found in bile. Amidation of BAs in the liver with taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (By similarity). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption (By similarity). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (By similarity). In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14032}. Peroxisome {ECO:0000250|UniProtKB:Q63276}.
Interaction partners:
- Long-chain fatty acid transport protein 5
- Acyl-coenzyme A thioesterase 8
- Sterol carrier protein 2
- Cysteine sulfinic acid decarboxylase
- Acyl-coenzyme A amino acid N-acyltransferase 2
- Glutathione hydrolase 6
- Glutathione hydrolase 1 proenzyme
- Acyl-coenzyme A amino acid N-acyltransferase 1
- Glutamate decarboxylase 1
- Glutamate decarboxylase 2
Sequence:
MAKLTAVPLSALVDEPVHIQVTGLAPFQVVCLQASLKDEKGNLFSSQAFYRASEVGEVDLEHDPSLGGDYMGVHPMGLFWSLKPEKLLGRLIKRDVMNSPYQIHIKACHPYFPLQDIVVSPPLDSLTLERWYVAPGVKRIQVKESRIRGALFLPPGEGPFPGVIDLFGGAGGLMEFRASLLASRGFATLALAYWNYDDLPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFVVTNALGLVEFYRTFQETADKDSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKKNWTLLSYPGAGHLIEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLPDLSSQL
Protein: Spindle pole body component 98 (DdSpc98) (Spc98) (Q95ZG4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May be involved in microtubule nucleation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm.
Interaction partners:
- Tubulin gamma chain
- Spindle pole body component 97
- Isobutyryl-CoA dehydrogenase, mitochondrial
- Sun domain-containing protein 1
- Centrosomal protein 224
- FAD dependent oxidoreductase domain-containing protein
- Kinesin-related protein 13
- Mitochondrial outer membrane protein porin
Sequence:
MNSTFVQIPKLNINKQVKKKTDSITANTLLPKLMNDTSIQQPNQQQQQQQPQQPQQVTNGITILQNYQPQQPQPATTTTQQLNSANNTPTLVSTKKSVIGINEIPEHLLIRDIIYVFQGIDGTYIKYNKQSDSFKIDENTSNTLVNGEPAYISKPKRDLVYRLCEFGWLFKKVRLFITNNDFKKTGLTNQSFCSAINDELIELYRIIAILETQVYKKFDMVNYGGGGGGSGGSGSGSGLESPSSVSSGGTTTSTEIPFIDGDSLTLIRLFVWIQSPLKRLKVLGTCVDSITVDMKGGEILSKIDTLSKHGDQDIRILIHNIMFKICQPLFSMIRLWMFKGEINDPYQEFFIRQYESVQLEKTWKEKFAIVARLLPSFISLPLSKRILIIGKSINYMKQFCNNFKEDKNDRYYYYNQEDDDDDDEDHDDNDDDDENENQGEDDEIIERKLLIKESKIIKEKTKELNYINKEVLQEIIELVSRQSSERLLKIVLNRFKFMNHVKALKKYLLLGQGDFIQYLMDLIGEDLLKPTSQIQRHKLVGWMDTAIRNSNAQFEEQDIVNRLDIALLPERPGNIGWDIFSLDYHVDTPLNTILSPNDILRYKKIFHFMWGIKRVEYSLASIWRKIRSSTSLSILSPIGGDIHKSHLIMNEMVHFISNFQYYLMFEVLECSWKNLEKFIDQEATDLDQLIEAHHQYLQDICNKMFLSNSDSCYECFKKLLSIIIKFTLLQTKLINLSIAIQNEKNFNETHQAQVNKEFNSFRNHLNNLYQEYTTSFYKFQSEILKVKVNQDLNPISLQYMLDFNEYYEEKKDN
Protein: Xaa-Pro aminopeptidase ApepP (EC 3.4.11.9) (Aminopeptidase P) (AP-P) (Q9VJG0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11872174}.
Interaction partners:
- Xaa-Pro dipeptidase
- Presequence protease, mitochondrial
Sequence:
MKRSTTQILTRLRELMLRAQVGDSCGISAYIVPSDDAHQSEYQCQHDERRSFVSGFDGSAGTAVITTETALLWTDGRYYQQAEKQLDSNWVLMRDGLSATPSIGAWLAKNLPKGSFVGVDPRLLSFRVWKPIETELSSAECQLVPIEGNLIDEVWGEDQPPQTSNKIITLKLEHSGVTIAKKWDVVRQQLKEKNADALVVSALDEIAWFLNLRGSDIDFNPVFFSYLIVTNDELLLFVDSGKLPTDFVQHQKENNVQISVLPYASIGIEISKIVSTRESKIWIAPTSSYYLTALIPKSRRIQEVTPICVLKAIKNDVEIAGFINSHIRDGVALCQYFAWLEDQVNKGAEVDEMSGADKLESFRSTKDKYMGLSFTTISASGPNGSVIHYHPKKETNRKINDKEIYLCDSGAQYLDGTTDVTRTLHFGEPTEFQKEAYTRVLKGQLSFGSTVFPAKVKGQVLDTLARKALWDVGLDYGHGTGHGVGHFLNVHEGPMGVGIRLMPDDPGLQANMFISNEPGFYQDGEFGIRVEDIVQIVPGQVAHNFSNRGALTFKTITMCPKQTKMIKKELLSDAEVKLLNSYHQQVWDTLSPILSREGDEFTLSWLKKEVQPI
Protein: Interleukin-1 receptor-associated kinase 3 (IRAK-3) (IL-1 receptor-associated kinase M) (IRAK-M) (Inactive IL-1 receptor-associated kinase 3) (Q9Y616)
Organism: Homo sapiens (Human)
Function: Putative inactive protein kinase which regulates signaling downstream of immune receptors including IL1R and Toll-like receptors. Inhibits dissociation of IRAK1 and IRAK4 from the Toll-like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex (By similarity). Upon IL33-induced lung inflammation, positively regulates expression of IL6, CSF3, CXCL2 and CCL5 mRNAs in dendritic cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29686383}. Nucleus {ECO:0000269|PubMed:29686383}. Note=In dendritic cells, translocates into the nucleus upon IL33 stimulation. {ECO:0000250|UniProtKB:Q8K4B2}.
Interaction partners:
- Interleukin-1 receptor-associated kinase 1
- TNF receptor-associated factor 6
- Interleukin-1 receptor-associated kinase-like 2
- Interleukin-1 receptor-associated kinase 4
- Myeloid differentiation primary response protein MyD88
- Tumor necrosis factor receptor superfamily member 16
- Interleukin-1 receptor type 1
- Single Ig IL-1-related receptor
- Toll-like receptor 2
- Toll-like receptor 4
Sequence:
MAGNCGARGALSAHTLLFDLPPALLGELCAVLDSCDGALGWRGLAERLSSSWLDVRHIEKYVDQGKSGTRELLWSWAQKNKTIGDLLQVLQEMGHRRAIHLITNYGAVLSPSEKSYQEGGFPNILFKETANVTVDNVLIPEHNEKGILLKSSISFQNIIEGTRNFHKDFLIGEGEIFEVYRVEIQNLTYAVKLFKQEKKMQCKKHWKRFLSELEVLLLFHHPNILELAAYFTETEKFCLIYPYMRNGTLFDRLQCVGDTAPLPWHIRIGILIGISKAIHYLHNVQPCSVICGSISSANILLDDQFQPKLTDFAMAHFRSHLEHQSCTINMTSSSSKHLWYMPEEYIRQGKLSIKTDVYSFGIVIMEVLTGCRVVLDDPKHIQLRDLLRELMEKRGLDSCLSFLDKKVPPCPRNFSAKLFCLAGRCAATRAKLRPSMDEVLNTLESTQASLYFAEDPPTSLKSFRCPSPLFLENVPSIPVEDDESQNNNLLPSDEGLRIDRMTQKTPFECSQSEVMFLSLDKKPESKRNEEACNMPSSSCEESWFPKYIVPSQDLRPYKVNIDPSSEAPGHSCRSRPVESSCSSKFSWDEYEQYKKE
Protein: Charged multivesicular body protein 4b (Q18886)
Organism: Caenorhabditis elegans
Subcellular location: Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
- Apoptosis-linked gene 2-interacting protein X 1
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 3
- Charged multivesicular body protein 1b
- Charged multivesicular body protein 6
- vesicle-fusing ATPase
- Charged multivesicular body protein 7
- Charged multivesicular body protein 5
- Charged multivesicular body protein 4b
- Coiled-coil and C2 domain-containing protein 1-like
Sequence:
MSLFGKIFGGRKQEAPSTPQESIQKLRETEEMLEKKQEFLEKKVIDEKQNAVKYGTKNKRMALQCLNRKRNFEKQLAHIDGVLSTIGYQREALENASTNAEVLNVMGTASKALKAAHNNMDIDQVHDLMEDIAEQQEVANEIAEAISNPVGFSTAVDDDDLMRELEALEQEELDKELLDARAPPVTLPDTPNIALPAVPASRPRAKEADKDLEDLESWANA
Protein: Transketolase 2 (TK 2) (EC 2.2.1.1) (P33315)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Transketolase 1
- Transaldolase NQM1
- Transaldolase
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate isomerase
- Ribose-5-phosphate isomerase
- Fructose-bisphosphate aldolase
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Fructose-1,6-bisphosphatase
- Triosephosphate isomerase
Sequence:
MAQFSDIDKLAVSTLRLLSVDQVESAQSGHPGAPLGLAPVAHVIFKQLRCNPNNEHWINRDRFVLSNGHSCALLYSMLHLLGYDYSIEDLRQFRQVNSRTPGHPEFHSAGVEITSGPLGQGISNAVGMAIAQANFAATYNEDGFPISDSYTFAIVGDGCLQEGVSSETSSLAGHLQLGNLITFYDSNSISIDGKTSYSFDEDVLKRYEAYGWEVMEVDKGDDDMESISSALEKAKLSKDKPTIIKVTTTIGFGSLQQGTAGVHGSALKADDVKQLKKRWGFDPNKSFVVPQEVYDYYKKTVVEPGQKLNEEWDRMFEEYKTKFPEKGKELQRRLNGELPEGWEKHLPKFTPDDDALATRKTSQQVLTNMVQVLPELIGGSADLTPSNLTRWEGAVDFQPPITQLGNYAGRYIRYGVREHGMGAIMNGISAFGANYKPYGGTFLNFVSYAAGAVRLAALSGNPVIWVATHDSIGLGEDGPTHQPIETLAHLRAIPNMHVWRPADGNETSAAYYSAIKSGRTPSVVALSRQNLPQLEHSSFEKALKGGYVIHDVENPDIILVSTGSEVSISIDAAKKLYDTKKIKARVVSLPDFYTFDRQSEEYRFSVLPDGVPIMSFEVLATSSWGKYAHQSFGLDEFGRSGKGPEIYKLFDFTADGVASRAEKTINYYKGKQLLSPMGRAF
Protein: Matrix metalloproteinase-9 (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (B5X4C7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- CD44 antigen
- CD44 antigen
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 3
- Metalloproteinase inhibitor 3
- Metalloproteinase inhibitor 2
- Kit ligand
- Kit ligand
- Cadherin-1
- B-cadherin-like isoform X1
Sequence:
MRRVLALFVLGMCMLSGWCVPLKKSVSVTFPGDVLKNMTDTELAESYLKKFGYMNVQHRSGFQSMVSTSKALMTMQRQMGLEETGTLDKSTVAAMKAPRCGVPDVRSYQTFEGDLKWDHHDITYRILNYSPDMVASLIDDAFARAFKVWSDVTPLTFTRLFDGTADIMVSFGKADHGDGYPFDGKDGLLAHAFPPGEGIQGDAHFDDDENWTLGKGPAVKTSFGNAEGALCQFPFLFEGKQYSTCTTEGRSDNLPWCATTADYGRDKKFGFCPSELLYTFDGNSDGKACVFPFVFLGETYEGCTTEGRSDGYRWCSTTDNFDQDKKYGFCPNRDTAVIGGNSEGEPCHFPFIFLGKKYDSCTSEGRGDGRLWCATTSDFDTDTKWGFCQDRGYSLFLVAAHEFGHALGLDHSNIRNALMYPMYSYVEDFSLHQDDIEGIHYLYGSKTGPNPSDEPKPEPDTPTTESTTTTTTHPVDPSQNACQIDKFDTITEIDGDLHFFKDRQYWRLSSKTDGKLEGPFSMSKRWPAVPAVVDTAFEDLVTRKIYFFSGTRFWVYTGQSFLGPRSIEKLGLSSTVEKVEGAMQRGKGKVLLFSGENYWRLDVEGQQIDKGYPRLTDQVFGGVPLDAHDVFQFKGNSYFCRDRFYWRMNSKRQVDRVGYVTYDLLNCSDSN
Protein: Gibberellin 20 oxidase 1 (EC 1.14.11.-) (GA 20-oxidase 1) (AtGA20ox1) (Gibberellin C-20 oxidase 1) (Q39110)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA12 to GA9, via a three-step oxidation at C-20 of the GA skeleton. GA53 is less effectively oxidized than GA12 and is only oxidized one step to GA44. Involved in the promotion of the floral transition, fertility and silique elongation, but plays only a minor role in elongation of seedling organs. Acts redundantly with GA20OX2.
Interaction partners:
- Ent-kaurenoic acid oxidase 1
- Ent-kaurenoic acid oxidase 2
- Gibberellin 3-beta-dioxygenase 1
- Gibberellin 3-beta-dioxygenase 2
- Gibberellin 3-beta-dioxygenase 4
- Gibberellin 3-beta-dioxygenase 3
- Ent-kaur-16-ene synthase, chloroplastic
- Auxin transport protein BIG
- DELLA protein GAI
- DELLA protein RGA
Sequence:
MAVSFVTTSPEEEDKPKLGLGNIQTPLIFNPSMLNLQANIPNQFIWPDDEKPSINVLELDVPLIDLQNLLSDPSSTLDASRLISEACKKHGFFLVVNHGISEELISDAHEYTSRFFDMPLSEKQRVLRKSGESVGYASSFTGRFSTKLPWKETLSFRFCDDMSRSKSVQDYFCDALGHGFQPFGKVYQEYCEAMSSLSLKIMELLGLSLGVKRDYFREFFEENDSIMRLNYYPPCIKPDLTLGTGPHCDPTSLTILHQDHVNGLQVFVENQWRSIRPNPKAFVVNIGDTFMALSNDRYKSCLHRAVVNSESERKSLAFFLCPKKDRVVTPPRELLDSITSRRYPDFTWSMFLEFTQKHYRADMNTLQAFSDWLTKPI
Protein: Exopolygalacturonase X-1 (ExoPG) (EC 3.2.1.67) (Galacturan 1,4-alpha-galacturonidase) (Poly(1,4-alpha-D-galacturonide)galacturonohydrolase) (Q5ASG9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Alpha-L-arabinofuranosidase B
- Alpha-L-arabinofuranosidase C
- Probable endopolygalacturonase D
- Endopolygalacturonase AN8327
- Endopolygalacturonase B
- Probable exopolygalacturonase Bgalacturonohydrolase B)
- Exopolygalacturonase X-2
- NAD binding Rossmann fold oxidoreductase, putative
- Probable alpha-L-arabinofuranosidase A
- Exo-1,4-beta-xylosidase bxlB
Sequence:
MKLSHLLTSAVSVLSLGLTVEGHFSRSRNDAVGPKRPFKPLPYSHPRKKVCHVRSHGDGRDDSAFILSALKSCNNGGKVVFAEEKEYTIGTALDLTFLKHVDLEILGRIQFTNDTDYWQANSFKHTFQNATTFFQLGGEDVNVYGGGTLDGNGQIWYDLYAEDPLILRPILFGVIGLHGGTIGPLKLRYSPQWYQLVANSSDVLFDGIDISGYSKSENEAKNTDGWDTYRSKNIVIQNSVINNGDDCVSFKPNSTEILVQNLYCNGSHGISVGSLGQYIGEVDIVKNVLVYNISMYNASDMARIKVWPGVASAMSEDLQGGGGLGSVSNITYEDMYIENVDWAIEITQCYGQKNMTLCNEYPSNLTISDVYISNMYGTTSSARDPNIGTIVCSSPDVCSNIYVENIDVVSPSGTNDFICTNVNESLLQVNCTSG
Protein: Putative ribosomal protein uL13-like (60S ribosomal protein L13a pseudogene 3) (Putative 60S ribosomal protein L13a protein RPL13AP3) (Q6NVV1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLRHKTKRGHASLDCLKVFDGIPPPYDKKKRMVVPAALKVVRLKPTRKFALLGRQAQEVRWKYQAVTATLEEKRKEKAKIHYWKKKQLMRLRKQAEKNVKKN
Protein: Parafibromin (Cell division cycle protein 73 homolog) (Hyperparathyroidism 2 protein) (Q6P1J9)
Organism: Homo sapiens (Human)
Function: Tumor suppressor probably involved in transcriptional and post-transcriptional control pathways. May be involved in cell cycle progression through the regulation of cyclin D1/PRAD1 expression. Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the cleavage and polyadenylation specificity factor (CPSF) complex and the cleavage stimulation factor (CSTF) complex, and with Wnt signaling. Involved in polyadenylation of mRNA precursors.
Subcellular location: Nucleus {ECO:0000269|PubMed:15580289, ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15923622}.
Interaction partners:
- RNA polymerase II-associated factor 1 homolog
- RNA polymerase-associated protein LEO1
- RNA polymerase-associated protein RTF1 homolog
- RNA polymerase-associated protein CTR9 homolog
- Transcription elongation factor SPT5
- Superkiller complex protein 8
- DNA-directed RNA polymerase II subunit RPB1
- Transcription elongation factor SPT4
- FACT complex subunit SPT16
- Transcription elongation factor SPT6
Sequence:
MADVLSVLRQYNIQKKEIVVKGDEVIFGEFSWPKNVKTNYVVWGTGKEGQPREYYTLDSILFLLNNVHLSHPVYVRRAATENIPVVRRPDRKDLLGYLNGEASTSASIDRSAPLEIGLQRSTQVKRAADEVLAEAKKPRIEDEECVRLDKERLAARLEGHKEGIVQTEQIRSLSEAMSVEKIAAIKAKIMAKKRSTIKTDLDDDITALKQRSFVDAEVDVTRDIVSRERVWRTRTTILQSTGKNFSKNIFAILQSVKAREEGRAPEQRPAPNAAPVDPTLRTKQPIPAAYNRYDQERFKGKEETEGFKIDTMGTYHGMTLKSVTEGASARKTQTPAAQPVPRPVSQARPPPNQKKGSRTPIIIIPAATTSLITMLNAKDLLQDLKFVPSDEKKKQGCQRENETLIQRRKDQMQPGGTAISVTVPYRVVDQPLKLMPQDWDRVVAVFVQGPAWQFKGWPWLLPDGSPVDIFAKIKAFHLKYDEVRLDPNVQKWDVTVLELSYHKRHLDRPVFLRFWETLDRYMVKHKSHLRF
Protein: Alpha-3 type IV collagen (Q63122)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
TRMRGFIFTRHSQTTANPSCPEGTQPLYSGFSLLFVQGNEHAHGQDLGTLGSCLQRFTTMPFLFCNVDNVCNFASRNDYSYWLSTPAPMPMDMAPITGRALEPYVSRCTVCEGPAMAIAVHSQTTAIPPCPQGWVSLWKGFSFVMFTSAGSEGAGQALASPGSCLEEFRASPFIECHGRGTCNYYSNSYSFWLASLNPERMFRKPIPSTVKAGDLEKIISRCQVCMKKRH
Protein: Cholera toxin transcriptional activator (A0A0H3AK48)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Interaction partners:
Sequence:
MFGLGHNSKEISMSHIGTKFILAEKFTFDPLSNTLIDKEDSEEIIRLGSNESRILWLLAQRPNEVISRNDLHDFVWREQGFEVDDSSLTQAISTLRKMLKDSTKSPQYVKTVPKRGYQLIARVETVEEEMARENEAAHDISQPESVNEYAESSSVPSSATVVNTPQPANVVANKSAPNLGNRLFILIAVLLPLAVLLLTNPSQSSFKPLTVVDGVAVNMPNNHPDLSNWLPSIELCVKKYNEKHTGGLKPIEVIATGGQNNQLTLNYIHSPEVSGENITLRIVANPNDAIKVCE
Protein: Prostaglandin E synthase (mPGES-1) (EC 5.3.99.3) (Glutathione peroxidase PTGES) (EC 1.11.1.-) (Glutathione transferase PTGES) (EC 2.5.1.18) (Inducible prostaglandin E synthase) (Microsomal prostaglandin E synthase 1) (Q9JHF3)
Organism: Rattus norvegicus (Rat)
Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli. Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:11067848}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}.
Interaction partners:
- Prostaglandin E synthase 3
- Prostaglandin E synthase 2
- Prostaglandin G/H synthase 1
- Prostaglandin G/H synthase 2
- Prostaglandin E synthase 3
- Prostacyclin synthase
- Thromboxane-A synthase
- Hematopoietic prostaglandin D synthase
- Prostaglandin-H2 D-isomerase
- Carbonyl reductase
Sequence:
MTSLGLVMENSQVLPAFLLCSTLLVIKMYAVAVITGQVRLRKKAFANPEDALKRGGLQYCRSDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPLIAWIHFLVVLTGRVVHTVAYLGKMNPRIRSGAYVLAQFACFSMALQILWEVAHHL
Protein: Vacuolar protein sorting-associated protein 54 (Vps54-like protein) (Q9JMK8)
Organism: Rattus norvegicus (Rat)
Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9P1Q0}. Membrane {ECO:0000269|PubMed:31721635}. Note=Associates with membranes in an EIPR1-independent manner. {ECO:0000269|PubMed:31721635}.
Interaction partners:
- Vacuolar protein sorting-associated protein 53 homolog
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 51 homolog
- Syntaxin-16
- EARP and GARP complex-interacting protein 1
- Syntaxin-6
- Syndetin
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 8
- Ras-related protein Rab-6A
Sequence:
MASSHSSSPVPQGSSSDVFFKKEVDPTKHVRPVQSLPDVCPKEPTVTDQHRWTVYHSKVNLPAALNDPTLAKRESDFFTKTWGLGFVDTEVIPSLYLPQISKEHFIAYQQEISQREKIHERCKNICPPKDTFDRTLLHIHDKSRTDLEQVPKIFMKPDFALDDSLTFNSVLPWSHFNTAGGKGNRDAASSKLLQEKLSHYLDIVEVNIAHQISLRSEAFFHAMTSQHELQDYLKKTSQAVKMLRDKIAQIDKVMCEGSLQILRLALTRNNCVKVSNKLKLMATVHQTQPTVQVLLSTSEFVGALDLIATTQEVLQQELQGVHSFRHLGSQLCELEKLIDKMMIAEFSTYSHSDLNRPLEGECQVLEEERLVSLVFGLLEQRKLNFLEIYGEETIITAKNIIKECVINKVAQVEEIDTDAVVKLADQMRMLNFPQWIDLLKDIFSKFTIFLQRVKATLNVIHSVVLSVLDKNQRTRELEEVSQQRSAGKDNSLDTEVAYLTHEGLFISDAFSEAEPASAAVDTTSQRNTSPHSEPCSSDSVSEPECTTDSSSSKEQTPASATLGGVDIIVSEDMRLTDLELGKLASNIQELLCNASDVCHDRAVKFLMSRAKDGFLEKLNSTEFIALSRLMETYIVDTEQICGRKSTSLLGALQSQANKFVNRFHEERRTKLSLLLDNERWKQADVPAEFQDLVDSIADGKIALPDKKPAATEDRKPADVLVVEGHQYAVVGTVLLLIRIILEYCQCVDNIPSVTTDMLTRLTDLLKYFNSRSCQLVLGAGALQVVGLKTITTKNLALSSRCLQLIVHYIPVIRAHFEARLPRKQWSLLRHFDHITKDYHDHIGEISSKLIAIMDSLFDKLLSRCEVEAPAPSPCFRNICKQMTKMHEAIFDLLPKEQTQMLILRINASYKFHLKKQLSHLNVINDGGPQSGFVTADVAFYTGNLQALKGLKDLDLNMAEIWEQKR
Protein: Photosystem I assembly protein Ycf3 (P0C516)
Organism: Oryza sativa (Rice)
Function: Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00439}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00439}.
Interaction partners:
Sequence:
MPRSRINGNFIDKTFSIVANILLRIIPTTSGEKRAFTYYRDGMLAQSEGNYAEALQNYYEAMRLEIDPYDRSYILYNIGLIHTSNGEHTKALEYYFRALERNPFLPQAFNNMAVICHYRGEQAILQGDSEIAEAWFDQAAEYWKQAIALTPGNYIEAQNWLKITKRFEFE
Protein: Cyclin-dependent kinase inhibitor 6 (Cyclin-dependent kinase inhibitor p22ack1) (Inhibitor/interactor of CDK protein 4) (KIP-related protein 6) (Q0WNX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity. Regulates cell division which is crucial for plant growth, development and morphogenesis. May inhibit CDK kinases specifically involved in the G1/S phase transition.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17253089, ECO:0000269|PubMed:18948957, ECO:0000269|PubMed:23617622}. Note=Homogeneously distributed. Present in microspores and accumulates strongly in vegetative cell nuclei immediately after asymmetric division and disappears later.
Interaction partners:
- Cyclin-dependent kinase A-1
- E3 ubiquitin-protein ligase RHF1A
- F-box/LRR-repeat protein 17
- Cyclin-D3-1
- Cyclin-D4-1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B2-2
- E3 ubiquitin-protein ligase RHF2A
Sequence:
MSERKRELAEEASSTSFSPLKKTKLNDSSDSSPDSHDVIVFAVSSSSVASSAALASDECSVTIGGEESDQSSSISSGCFTSESKEIAKNSSSFGVDLEDHQIETETETSTFITSNFRKETSPVSEGLGETTTEMESSSATKRKQPGVRKTPTAAEIEDLFSELESQDDKKKQFIEKYNFDIVNDEPLEGRYKWDRL
Protein: Small ribosomal subunit protein uS11 (30S ribosomal protein S11) (P0A7R9)
Organism: Escherichia coli (strain K12)
Function: Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome (By similarity).
Interaction partners:
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein bS18
- Small ribosomal subunit protein bS20
- Elongation factor G
- Large ribosomal subunit protein bL20
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL14
- DNA-directed RNA polymerase subunit alpha
- Small ribosomal subunit protein bS21
Sequence:
MAKAPIRARKRVRKQVSDGVAHIHASFNNTIVTITDRQGNALGWATAGGSGFRGSRKSTPFAAQVAAERCADAVKEYGIKNLEVMVKGPGPGRESTIRALNAAGFRITNITDVTPIPHNGCRPPKKRRV