wanglab/gogpt-training-data huggingface dataset:
Protein: Inactive serine protease scarface (Q7K5M0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Inactive serine protease that plays a role in germ-band retraction and dorsal closure morphogenesis in embryogenesis; contributes to amnioserosa attachment and epithelial apico-basal polarity by regulating the localization of laminin LanA on the apical side of the amnioserosa epithelium. Contributes to epithelial morphogenesis probably by regulating the bsk/JNK pathway, as part of a negative-feedback loop, and by modulating the cross-talk between the Egfr, bsk/JNK and dpp signal transduction pathways. In larval development, antagonizes the morphogenetic movements controlled by the bsk/JNK signaling including male genitalia formation and thorax development.
Subcellular location: Secreted {ECO:0000269|PubMed:15342518, ECO:0000269|PubMed:20379222, ECO:0000269|PubMed:20530545}.
Interaction partners:
- FI04548p
Sequence:
MSASHFREQLALCITLAVLAAASGDYRANMFLNGQYQNGIKDQKENNLLVNPSTNVFLNHAIISRQASPFQGPTYLPPKEFLKCAPGQQCVRSGQCLNGYFAQQLPKIQNCDPETTVCCTYRPPPTTTTTTTTSVPVANCAYDSDCVTPDNCRNGEISAINYVKKQGPNRCPAPNICCRIPSTTLTEDGYIFNLPEKTFPLPTKPAVLAMPSTQAPFRPQPTTAVPASRPTIEYLPPSTTQHPSYEKVQTSRRPVYLPPSPATESASSLIPKIRPRPEPRPQPTRRPTNEYLPPAAANEIPRFEPDRAPQPSNQKPIYRGEDQLSPQIFPTPQPANVPKHFAKCASALVCTSENFCNAIGVLSETPVELSPMEAAFRVPLTDCLQTENGSPGKCCRDPNYVDPWPVNLAGVCATRNKRTKPTGVKDLDANFAEIPWQAMILRESSKTLICGGAIIGDQFVLSSASCVNGLPVTDIRVKAGEWELGSTNEPLPFQLTGVKTVDVHPDYDPSTNSHDLAIIRLERRLEFASHIQPICISDEDPKDSEQCFTSGWGKQALSIHEEGALMHVTDTLPQARSECSADSSSVCSATKFDSCQFDVGSALACGSGSSVRLKGIFAGENSCGEGQTVRFAKPDIKWINTAFAENNKPLLLKRF
Protein: RNA pseudouridine synthase 6, chloroplastic (EC 5.4.99.-) (RNA pseudouridylate synthase 6) (RNA-uridine isomerase 6) (Q9SVS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Protein Iojap-related
- Pseudouridine synthase family protein
- At4g38020 family protein)
- Short integuments 2, mitochondrial
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
Sequence:
MASPALTGGYRNLTAPVSLLRTLASTRVTTPLFRSNKHSPRFISSPKRFTCLSLLKTDSQNQTTLSSSSNSGYHEYNRLMPCPAYNLPPRIEHMVVLEDDVLVSEFISKQLDLPPLYVADLIRFGAVHYALVCPKPPPTATPEEIILFEEVTSPSVLKKRSSIKGKTVREAQKTFRVTHTNQYAEAGTYLRVHVHPKRSPRCYEIDWKSRIVAVTDSYVILDKPAGTTVGGTTDNIEESCATFASRALDLPEPLKTTHQIDNCTEGCVVFARTKEYCSVFHTKIRNKEVKKLYRALAAAPLPIGIISHYMRPKNMAPRLVAEDSIQGWHLCQLEVLECKKIPWPDAATEKKHDIEDCGWTSKEFAYECTINLLTGKTHQIRAQLAACGAPLVGDSMYMPAAIAEMGNPDTNPYGKAKKHYTMEENQKETAVAEWIDRHGKEPRVGIGLQACQISWDDDDGEHFYEAGTPWWR
Protein: Probable tRNA-splicing endonuclease subunit sen2 (EC 4.6.1.16) (tRNA-intron endonuclease sen2) (Q8TFH7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. This subunit may anchor the endonuclease complex to the nuclear membrane. Probably carries the active site for 5'-splice site cleavage (By similarity).
Interaction partners:
- Probable tRNA-splicing endonuclease subunit sen54
- Probable tRNA-splicing endonuclease subunit sen34
- Probable tRNA-splicing endonuclease subunit sen15
- Uncharacterized protein C6C3.09
- Pre-mRNA-splicing factor cwf5
- Ribonucleases P/MRP protein subunit pop3
- Polynucleotide 5'-hydroxyl-kinase grc3
- Pre-rRNA-processing protein las1
- 5'-3' exoribonuclease 2
- Ribonucleases P/MRP protein subunit pop1
Sequence:
MSKNHEVYKDALPISLAYPLPPIILTNPLTWIPYIYRYLFRKTPRQVQWQCQLHESDLSCVVTDSEAIKKFWTSGFFGKGNLSRSEPTWHTRTKRSLGLLGFDEDLVAEEVTARRRFQRKQFKAQRAYRENRARERQLLLENGKPIPASLEEDAELPEYLTKSLKDFSRVSENPYHITSVPNVEHLQLTFPEAFFLASLGVLRINYENPNFELLPILKLFANIVANSVALTHDYSLQQSHEDPIIEPDNKFLTELAAYFYFRQQGWVVKNGTKFSVDFLLYKKGPVFSHAEFAILLIPCVGNKQKYNMQWHEVHCLNRVIAQVKKSLILCYVQCPSIEDFNKIWKNQASMNEWDWAESVLRQYLIRCVTLRRWVPSRNRD
Protein: Uncharacterized protein B0035.15 (Q17439)
Organism: Caenorhabditis elegans
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Complex I assembly factor TIMMDC1, mitochondrial
- Probable NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- Probable NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 beta subcomplex subunit 3
Sequence:
MKRLWKKVGSGVKNANYLKKSVEEVAKIEKGETKVVPPKYPTEKSREVSEEIKKELAMKNESLVENMNKMYIKSTDPVERWTSTKDLPTRESEFLHRNDPIWEYGFYEPPVERIPKDKLMFKEALEYLRFRQELLSDSSSPAQKKQAAEFVADHVVTSRVNAETLDDIYEYFRPFERKDKQKVVNRHALAALQDHVQGNSDERRILDEAKDVGKKIRHISNNTKFLDEYQRLEDEEKDKVREAIAQLRQEEHERLNKRLGQLGEIEKTAQEAMKKAVEEKKEK
Protein: Thebaine synthase 1 (EC 4.2.99.24) (A0A2U9GHG9)
Organism: Papaver somniferum (Opium poppy)
Function: Catalyzes the formation of thebaine from (7S)-salutaridinol 7-O-acetate at the expense of labile hydroxylated by-products, which are preferentially produced by spontaneous allylic elimination.
Interaction partners:
Sequence:
MDSINSSIYFCAYFRELIIKLLMAPLGVSGLVGKLSTELEVDCDAEKYYNMYKHGEDVQKAVPHLCVDVKVISGDPTRSGCIKEWNVNIDGKTIRSVEETTHNDETKTLRHRVFEGDMMKDFKKFDTIMVVNPKPDGNGCVVTRSIEYEKTNENSPTPFDYLQFGHQAIEDMNKYLRDSE
Protein: Acyl-CoA desaturase 1 (EC 1.14.19.1) (Delta(9)-desaturase 1) (Delta-9 desaturase 1) (Fatty acid desaturase 1) (Stearoyl-CoA desaturase 1) (P13516)
Organism: Mus musculus (Mouse)
Function: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the Delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation. Plays an important role in body energy homeostasis. Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides. Required for normal development of sebaceous glands. Required for the biosynthesis of normal levels of Delta-9 unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the Harderian gland. Required for normal production of meibum, an oily material that prevents drying of the cornea.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16275639, ECO:0000305|PubMed:16443825}; Multi-pass membrane protein {ECO:0000269|PubMed:16275639}. Microsome membrane {ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:16443825}.
Interaction partners:
- Fatty acid synthase
- Acetyl-CoA carboxylase 1
- Diacylglycerol O-acyltransferase 2
- Sterol regulatory element-binding protein 1
- Cytochrome b5 type B
- Cytochrome b5 reductase 4
- Cytochrome b5
- ATP-citrate synthase
- Very long chain fatty acid elongase 6
- Peroxisome proliferator-activated receptor alpha
Sequence:
MPAHMLQEISSSYTTTTTITAPPSGNEREKVKTVPLHLEEDIRPEMKEDIHDPTYQDEEGPPPKLEYVWRNIILMVLLHLGGLYGIILVPSCKLYTCLFGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFILPTLVPWYCWGETFVNSLFVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFPFDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKATVLARIKRTGDGSHKSS
Protein: Mangetout, isoform E (A1Z7F4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTTANIVAAPAAPTISPAITSTATRIGGKAVPTPRLLGSGAANVAQILAKSLDSPSPSSSSGWPVKHAAVLEGDVILGGLMMVHSREDSITCGPIMPQGGIQALEAMLYTLDQVNKQQLLPNVTLGAHLLDDCDKDTYGLEMAVDFIKGSISNIDDAEYHCNKTQVRKVISGVVGAASSVTSIQVANLLRLFRIPQVSYFSTSPELSNKQRFEYFSRTIPSDHYQVKAMVEIVKRMGWSYVSIIYEESNYGIKAFEELEELLARHNICIAIKEKLVKDSGVAEDIAYDNIVQKLLTKPRARGAIIFGSDQEVRQVMRAVRRANATGSFSWIGSDGWSARNLVSDDYEPEVEGTLSVQPQANPVRGFEEYFLSLTVENNQRNPWFVEFWEDHFQCRYPGSTSTPYNNYTKQCTTKERLSRQNTDFEDQLQFVSDAVMAFAYALRDMHRDLCGGGPSLCEAMKPTKGADLLKYLRKVEFEGLSGDEFRFDGNGDGPARYNIIHFKQSQAGQYHWVKVGEYTEGELRLNMTEVKFKRLSPKPPESVCSLPCLVGQAKKYVEGESCCWHCFNCTTYQIRHPDDETHCKLCKLGTLPDAHKQYCRPIPEIYLRPESAWAIGAMAFSATGILVTLFVMGVFVRHNDTPIVRASGRELSYILLAGIFMCYGVTFALVLKPTNIVCAIQRFGVGFCFTVVYAALLTKTNRIARIFKAGKQSAKRPSFISPKSQLVICACLVSVQILINGVWMVIAPSHAMHHYPTREDNLLVCDSYIDASYMIAFSYPIFLIVICTVYAVLTRKIPEAFNESKHIGFTMYTTCVIWLAFVPLYFGTANHVPLRITSMSVTISLSASVTIACLFSPKLYIILIRPERNVRQSMMPPRYGNMHRTAGTGPSSMMAAAVVTAATCAQEEKIQKHITPTNTENSLKTKKLCEMATQTISSIITSLDINAYNQIPYADQYVPNNATTATTTPTDKGSGNGNSNSNSNTNGSSNSNSNSNGDGDVATEQVVANNNKINQRQHGQPAVAFAITSTNNHISGPAATITTTAATGETTTEALVATITTPLATVDGSETMSVAPNNGHGNNGSQRPPVLQTNL
Protein: Eisosome protein sle1 (SEG1-like eisosome protein 1) (O13858)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Important for the biogenesis of filamentous eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on the plasma membrane to cluster specific proteins at sites of membrane invaginations.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:22869600}. Cell tip {ECO:0000269|PubMed:22869600}. Note=Localizes to eisosomes. {ECO:0000269|PubMed:22869600}.
Interaction partners:
- Probable sphingolipid long chain base-responsive protein pil1
- Non-classical export protein 2 homolog
- Inositol-1,4,5-trisphosphate 5-phosphatase 1
Sequence:
MSHASKNYNAQLTAAAASTALHGTKKIYNSNENDRAVNSFLGNRTSYGEAVNGSPQYDYMRSRMSTLGSANQPMAPPSLRNRSSVYLPTPAGPPQIPVNTGKRYTLTSSSANYMTKSERQMRPPKSYDFPPSQQVRPSTSRSPSYASYNSEEVNFQSYQDPRLLPRTSQMYMPDNNYSPAVKSPAAQRRSSSYMVPANSRGSPANYNTPYYPTAIPPPIEEYSPSVSLPTSPVAEESYNNVQRSSTVRNNTTQKSVLKKPSRKMSPAYTSSYRQNSPSSQVPPVSKKHVIIYENKEGSSSSESVYEDVFEDFDPSGSNQASLRSTSTIHYTPSSKRISVIPPNTSNIGSRVVSRSGQNNNQPAQPGQYNQQSQPVQSYQSGQSTQHFQPVQPIQPVQSTQYYQPSSPVQPVQNGVPAPPMQPVQSTQYYQPSSPVQPVQNVKPAQPAQPSLEDAAKRRVEEMLRQMDITPTASSTTANNAYASAEPHPSAFPDDMNSVFSDSSFERERDSGRGRSTNLFSKFKSGRSRSKASGEAPYSYPAPPVPSVNNAGARLTLRDSGAAPEATYSLRQPSNHAYSEGRSYTFTGGQPPSVPTMPYGSRFANDSDSMMGSTADFSSKKKGGKFKAFKKFFKMRF
Protein: GH11495p (Q8MSI9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIIIIRRITICMGFLLRFLESLGISGPLHNKVFVANLDYKVDNKKLKQVFKLAGKVQSVDLSLDKEGNSRGFAVIEYDHPVEAVQAISMLDRQMLFDRRMTVRLDRIPDKNEGIKLPEGLGGVGIGLGPNGEPLRDVAHNLPNGGQSQGQLLGNAQQGSQLGSVGSQPNSSAVSNATTNLLNNLTGVMFGNHAAVQPSPVAPVQKPSLGNNTGSGGLNLNNLNPSILAAVVGNLGNQGGNLSNPLLSSSLSNLGLNLGNSGNDDNLPPSNVGLSNNYSSGGTGGGNSYSSGNNYSGGGGSSNLGYNAYSSSGVMGGGNGGVGVDGNDYNTGNPLDVYGGGSNVGNSNVGSANAVGASRKSDTIIIKNVPITCTWQTLRDKFREIGDVKFAEIRGNDVGVVRFFKERDAELAIALMDGSRLDGRNIKVTYF
Protein: WW domain binding protein 1-like (Outcome predictor in acute leukemia 1) (Q9NX94)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPFLLGLRQDKEACVGTNNQSYICDTGHCCGQSQCCNYYYELWWFWLVWTIIIILSCCCVCHHRRAKHRLQAQQRQHEINLIAYREAHNYSALPFYFRFLPNYLLPPYEEVVNRPPTPPPPYSAFQLQQQQLLPPQCGPAGGSPPGIDPTRGSQGAQSSPLSEPSRSSTRPPSIADPDPSDLPVDRAATKAPGMEPSGSVAGLGELDPGAFLDKDAECREELLKDDSSEHGAPDSKEKTPGRHRRFTGDSGIEVCVCNRGHHDDDLKEFNTLIDDALDGPLDFCDSCHVRPPGDEEEGLCQSSEEQAREPGHPHLPRPPACLLLNTINEQDSPNSQSSSSPS
Protein: 6.6 kDa lipoprotein (Lp6.6 protein) (H7C7L8)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
Sequence:
MTKLMYAIFLSAILFVACETTRISDEMENTSDEDSKVTAPMTDKDMMKSMPDKNTKSMKQPMTKSMKK
Protein: Mitochondrial import inner membrane translocase subunit Tim8 (Q9Y1A3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The Tim8-Tim13 complex mediates the import of some proteins while the predominant Tim9-Tim10 70 kDa complex mediates the import of much more proteins (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim10B
- GEO02620p1
- Mitochondrial import receptor subunit TOM7 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- 10 kDa heat shock protein, mitochondrial
- Mitochondrial import receptor subunit TOM40 homolog 2
Sequence:
MSDFENLSGNDKELQEFLLIEKQKAQVNAQIHEFNEICWEKCIGKPSTKLDHATETCLSNCVDRFIDTSLLITQRFAQMLQKRGGGDL
Protein: Four and a half LIM domains protein 2 (FHL-2) (LIM domain protein DRAL) (Skeletal muscle LIM-protein 3) (SLIM-3) (Q14192)
Organism: Homo sapiens (Human)
Function: May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation. Negatively regulates the calcineurin/NFAT signaling pathway in cardiomyocytes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11813260, ECO:0000269|PubMed:16652157}. Nucleus {ECO:0000269|PubMed:11813260, ECO:0000269|PubMed:16652157}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O35115}.
Interaction partners:
- Catenin beta-1
- Lymphoid enhancer-binding factor 1
- Titin
- TNF receptor-associated factor 6
- Caspase recruitment domain-containing protein 8
- Epidermal growth factor receptor
- TNF receptor-associated factor 2
- Syntaxin-binding protein 2
- Syntaxin-11
- Presenilin-2
Sequence:
MTERFDCHHCNESLFGKKYILREESPYCVVCFETLFANTCEECGKPIGCDCKDLSYKDRHWHEACFHCSQCRNSLVDKPFAAKEDQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFICHRCQQPIGTKSFIPKDNQNFCVPCYEKQHAMQCVQCKKPITTGGVTYREQPWHKECFVCTACRKQLSGQRFTARDDFAYCLNCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI
Protein: Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)] (P50392)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Translocates to membrane vesicles in a calcium-dependent fashion. {ECO:0000250}.
Interaction partners:
- Arachidonate 12-lipoxygenase
- Cytochrome P450, family 4, subfamily F, polypeptide 3
- Prostaglandin-endoperoxide synthase 2a.
- Mitogen-activated protein kinase
- Cytochrome P450 2U1
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phosphoinositide phospholipase C.
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Mitogen-activated protein kinase
- Acyl-CoA 6-desaturase
Sequence:
MSNIIVEHQYSHRLKLTVVRAENVTKGAFGDLLDTPDPYVELSVPTTPESRKRTRHINNDINPKWNETFEFILDPNQSNVLEVTLMDANYVMDETLGTAKYSLSKLKVAQMEHVTLSIGKTTKVFLDLLLEVCASTDLRFSMTLCDQEKLFMQTRRDRVMLSIKKLLKMENPRFLPSSPREVPTIAILGSGGGFRAMVGFSGVMKALYESGVFDCATYVAGLSGSTWYMSMLYSHPEFPAKGPGDINKELMNRVSNNPLKLLLPQNINRYVKALWKKKSAGQPVTFTDIFGMLIGETLIPGRMNIKLSSLKGKINEGQSPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMSPGLFGSKFFMGSVVKQYEENPLHFLMGVWGSAFSILFNRVLGVKETTSSSTMEEELEQIKPEHIVGDDSADNEEETQRGGTESADAEDERQRHAQASWVQRMLTSIMGDTTLFTTREGRAGKVHNFMLGLNLNSTLPFSPFSGITHQTSLEEEVDAVTDPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRCQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDSKVFDREGLKECYVFKPAKGDKNCPTIIHFVLANINFRNFKAPGVPRDSDKDIEFGDFDIFDEPASPYSTFNFKYNNQAFKRLHDLMEFNTLNNIEVIKEAIKDSILLRRENPARCSVSLSLSEIENKKFLKRDNSIAKRPT
Protein: Gasdermin-like protein rcd-1-1 (Regulator of cell death 1-1) (Q7SBA0)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Function: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition). In N.crassa, the rcd-1 locus exists as 2 incompatible alleles, rcd-1-1 (this entry) and rcd-1-2 (AC P0DW10). During the allorecognition process, forms a heterooligomer with rcd-1-2, thereby forming a functional gasdermin-like complex that binds to membranes and forms pores, triggering cell death. Binds negatively charged phospholipids, such as cardiolipin and phosphatidylserine. Also binds to phosphoinositides, preferentially to phosphatidylinositol-3-phosphate (PtdIns-3-P), PtdIns-5-P and PtdIns-3,5-P2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32703806}. Cell membrane {ECO:0000269|PubMed:32703806}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P57764}. Note=Cytoplasmic in the absence of rcd-1-2 (PubMed:32703806). Forms a gasdermin-like pore that associates with the cell membrane in the presence of rcd-1-2 (PubMed:32703806). {ECO:0000269|PubMed:32703806}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MDKCWFTLDNAHYPPPSLDSMRSGHPISPASLGHLIPSLAHLDQIINAKAIEPFPATMDIHGPTIIEDFKWDHSHEYSLSLGGKVPIPLAPAGVPFVDLNVGLGGAFSRSVANYWEFDRLERYIMQPTRSYVQKCIERDEVKRWIAKNKSMMMMGRWEVYMITGIIVARGGGRKKKEKTTGKEFSVEVTVEVPLIVEAGPGGKRNTARQKTWGTSQTGDFVWAVRLAKITKSGLHSDWKMETVFGKTSSFRGQKAIF
Protein: Dolichyldiphosphatase 1 (EC 3.6.1.43) (Dolichyl pyrophosphate phosphatase 1) (Q86YN1)
Organism: Homo sapiens (Human)
Function: Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Dolichol kinase
- Dolichyl-phosphate beta-glucosyltransferase
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Sequence:
MAADGQCSLPASWRPVTLTHVEYPAGDLSGHLLAYLSLSPVFVIVGFVTLIIFKRELHTISFLGGLALNEGVNWLIKNVIQEPRPCGGPHTAVGTKYGMPSSHSQFMWFFSVYSFLFLYLRMHQTNNARFLDLLWRHVLSLGLLAVAFLVSYSRVYLLYHTWSQVLYGGIAGGLMAIAWFIFTQEVLTPLFPRIAAWPVSEFFLIRDTSLIPNVLWFEYTVTRAEARNRQRKLGTKLQ
Protein: B9 domain-containing protein 2 (Q387L3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
- B9 domain-containing protein 1
- C2 domain-containing protein
- Meckelin
- Transmembrane protein
- Transmembrane protein 231
Sequence:
MAELHVIGDLAFGEDFGGKSYFCAFEIVTGEHWRVVEGHTSGCTHIMESDSCGGIAWCFPIDVHYTMGSVEGWPKISMQVWSVDGYGRKDLAGYGVAFVPPPGGEEQEVNVETWKPCFWNPNFFIRLYENLREAVMGGGPVLCDKTMIHTNDERFKLRTISSGSVRLHLNVVARGMERLGVRCA
Protein: Diphthamide biosynthesis protein 4 (J protein type 3) (P47138)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 2-
- 2-
- Diphthine--ammonia ligase
- Pre-mRNA-splicing factor CWC23
- J protein JJJ2
- Auxilin-like clathrin uncoating factor SWA2
- Diphthamide biosynthesis protein 3
- J protein JJJ1
- Diphthine methyl ester synthase
- Mitochondrial protein import protein MAS5
Sequence:
MSLVNSLTHYEILRIPSDATQDEIKKAYRNRLLNTHPDKLSKSIHDTVSNVTINKIQDAYKILSNIKTRREYDRLILENYKRQGFHNCGDGLDEFSLDDFSFDEDKLEFMMNCPRCQFVGGFHFSESLLDECIDNVDAMERSHSGYQLLTQCSACSLWLKVNFDIEEEQEGQ
Protein: Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2) (Q92731)
Organism: Homo sapiens (Human)
Function: Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1/ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:19126643, ECO:0000269|PubMed:20074560}.
Interaction partners:
- Nuclear receptor coactivator 1
- Estrogen receptor
- Nuclear receptor coactivator 3
- Proto-oncogene tyrosine-protein kinase Src
- Nuclear receptor coactivator 2
- Transcription factor Sp1
- Mediator of RNA polymerase II transcription subunit 1
- Caveolin-1
- Nuclear receptor corepressor 1
- Transcription factor Jun
Sequence:
MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ
Protein: Hemophore HasA (Heme acquisition system protein A) (Q54450)
Organism: Serratia marcescens
Function: Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.
Subcellular location: Secreted {ECO:0000269|PubMed:7937909}.
Interaction partners:
- TonB-dependent heme receptor.
- Heme acquisition ABC transporter,ATP-binding/permease protein.
- TonB-like protein.
- Putative iron sensor protein.
Sequence:
MAFSVNYDSSFGGYSIHDYLGQWASTFGDVNHTNGNVTDANSGGFYGGSLSGSQYAISSTANQVTAFVAGGNLTYTLFNEPAHTLYGQLDSLSFGDGLSGGDTSPYSIQVPDVSFGGLNLSSLQAQGHDGVVHQVVYGLMSGDTGALETALNGILDDYGLSVNSTFDQVAAATAVGVQHADSPELLAA