wanglab/gogpt-training-data huggingface dataset:
Protein: Myelin regulatory factor (EC 3.4.-.-) (Myelin gene regulatory factor) [Cleaved into: Myelin regulatory factor, N-terminal; Myelin regulatory factor, C-terminal] (Q3UR85)
Organism: Mus musculus (Mouse)
Function: Constitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor, N-terminal component that specifically activates transcription of central nervous system (CNS) myelin genes.
Subcellular location: [Myelin regulatory factor]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:30249802}; Single-pass membrane protein.; SUBCELLULAR LOCATION: [Myelin regulatory factor, N-terminal]: Nucleus {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28441531, ECO:0000269|PubMed:30249802}. Cytoplasm {ECO:0000269|PubMed:23966833}. Note=Translocates from the cytoplasm to the nucleus upon autocatalytic cleavage. {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:30249802}.; SUBCELLULAR LOCATION: [Myelin regulatory factor, C-terminal]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:30249802}; Single-pass membrane protein {ECO:0000269|PubMed:23966833}.
Interaction partners:
- Transcription factor SOX-10
- Myelin proteolipid protein
- Transmembrane protein 98
- Oligodendrocyte transcription factor 1
- Oligodendrocyte transcription factor 2
Sequence:
MEVVDETEALQRFFEGHDISGALEPSNIDTSILEEYIGKEDASDLCFPEISAPASTASFPHGPPAIPGSSGLHHLSPPGSGPSPGRHGPLPPPTYGTPLNCNNNNGMGTAPKPFLGGSGPPIKAEPKAPYAPGTLPDSPPDSGSEAYSPQQVNDPHLLRTITPETLCHVGVSSRLEHPPPPPAHLPGPPPPPPPPPHYPVLQRDLYMKAEPPVPPYAAMGPGLVPPELHHTQQTQVLHQLLQQHGAELPPHPSKKRKHSESPPNTLNAQMLNGMIKQEPGTVTALPPHPARAPSPPWPPQGPLSPGTGSLPLSIARAQTPPWHPPGAPSPGLLQDSDSLSGSYLDPNYQSIKWQPHQQNKWATLYDANYKELPMLTYRVDADKGFNFSVGDDAFVCQKKNHFQVTVYIGMLGEPKYVKTPEGLKPLDCFYLKLHGVKLEALNQSINIEQSQSDRSKRPFNPVTVNLPPEQVTKVTVGRLHFSETTANNMRKKGKPNPDQRYFMLVVALQAHAQNQNYTLAAQISERIIVRASNPGQFESDSDVLWQRAQLPDTVFHHGRVGINTDRPDEALVVHGNVKVMGSLMHPSDLRAKEHVQEVDTTEQLKRISRMRLVHYRYKPEFAASAGIEATAPETGVIAQEVKEILPEAVKDTGDVVFANGKTIENFLVVNKERIFMENVGAVKELCKLTDNLETRIDELERWSHKLAKLRRLDSLKSTGSSGAFSHAGSQFSRAGSVPHKKRPPKLANKSSPAVPDQACISQRFLQGTIIALVVVMAFSVVSMSTLYVLSLRSEEDLVDADGSLAVSTSCLLALLRPQDPGGSEAMCPWSSQSFGTTQLRQSSMTTGLPGTQPSLLLVTKSASGPALRALDLCSSQPCPIVCCSPPVSSPATDPALGPTLTPTPSPSSNPKHSGPGQMAPLPVTNIRAKSWGISANGISYSKHSKSLEPLASPVVPFPGGQSKTKNSPSFNLQSRARRGAPQPSPSPAQFTQTQGQLDPAPSLTSIQLLENSMPITSQYCVPEGACRLGNFTYHIPVSSSTPLHLSLTLQMNSSTPVSVVLCSLTSEEEPCEEGGFLQRFHPHQDTQGTSHQWPVTILSFREFTYHFRVTLLGQANCSSEAIVQPATDYYFHFYRLCD
Protein: Helicase required for RNAi-mediated heterochromatin assembly 1 (EC 3.6.4.13) (O74465)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Poly
- RNA-dependent RNA polymerase 1
- Protein argonaute
- Protein Dicer
- RNA-induced transcriptional silencing complex protein tas3
- Chromo domain-containing protein 1
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Chromatin-associated protein swi6
- Argonaute-binding protein 2
- Chromatin modification-related protein rik1
Sequence:
MEQVQDEIWKLSTLDAWEMVNKNTEVVFDEIPEPETLSEMKRHPLYSNIFNADNNTTSFTEQIETSETSKTQDSEGNKVDKNLKENKSIRRKRSIDNDYELSNVKRNDITSGKNREFENEHHPASDTSSWRELPSIPTLEELTSKSVELPSNNIYGGYKSFEDYLSIHYRLLREDAVSPLRESVLRYKVNPNYITGSSLAVYDHVRIDGYTISSSVIAAKLSFSVRAKKKIKWATSRRLISGSLVLLSNDDFQTFRIGTVCARPLSGLNKHPHEIDVKFEDISISLDPREEYVMIEATSGYWEAYKHVLRSLQRLSASTFPMKDYLVHCKSNQETAKHIQNNPRIRINSILKNNSQKIVNALEPFGPGEYILDSSQLKAYQSMLTKRLSIIQGPPGTGKSFVTLKAIETLLENTHSHVLPILVACQTNHAVDQILIRLLHQGASVMRLGSRTKDPEIAAVTIFQKAKHTKHSFKAAYNEIRHKKQRLIKQITNIMHNFNLEFVTLSYLHSKGIITTSQLESLRNNTEWISSVAENGEKTEEELISIWLGDAKVELITPSEITDGFEEELQIDPEKLEEIQKEAEDSGALMEEELRGKFINLRCKYLFSKLTTLHEKEIDTLLTIPNIWDIPEYSRGIIYCRWLESAYAAAEKELNRLYRFYLKVDRERIGFSNKRAAILLRGANVIGMTTTGLNKYRDILERINPKICFIEEAADVLEGPIIPAVFPSLEQLVLIGDHKQLRPGCSTYALRQDPFNLSISMFERLVENDMEYTRLTMQRRMHPQIRRLVSSVYEDLSDYEITKYWPSIPGMGEIRRFFLTHSRIEDNDGFASKINLFEAQMLVQFAVYLINNGVEPQKITCLTFYAAQKDLIERLLSESLNREKHFIKVATVDGYQGEENDVVLLSLVRNNDRTEVGFLSSPHRVCVSLSRARRGLFIFGNAQLVAESNPLWWDAINTLMNDETIQGLGDHLPLFTKDGTIYVNDPVELLDVNMRLTRK
Protein: Peroxisomal membrane protein PMP27 (Peroxin-11) (Q12462)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in peroxisomal proliferation. Promotes peroxisome division and biogenesis.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:14517338, ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14517338, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Peroxisomal membrane protein import receptor PEX19
- Peroxisome biogenesis factor 10
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX25
- Peroxisomal membrane protein PEX27
- Peroxisomal membrane protein PEX14
- Peroxisomal targeting signal receptor
- Peroxisomal biogenesis factor 2
- Peroxisomal biogenesis factor 8
Sequence:
MVCDTLVYHPSVTRFVKFLDGSAGREKVLRLLQYLARFLAVQNSSLLARQLQAQFTTVRKFLRFLKPLNHLQAAAKFYDNKLASDNVVRVCNVLKNIFFAAYLSLDQVNLLRILKVIPVTVLTGKKIPRWSNWCWLFGLLSGLAMDLRKIQTSHAQIAAFVKAKSQSQGDEHEDHKKVLGKAYQDRYTALRRLFWDAADSFIVLNNLGYLSSNEEYVALSGVVTSILGMQDMWKAT
Protein: Transcription initiation factor TFIID subunit 7 (TAFII-67) (TBP-associated factor 67 kDa) (TBP-associated factor 7) (Q05021)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. TAF7 is responsible for the recruitment of BDF1 to TATA element containing promoters.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Bromodomain-containing factor 1
- Transcription initiation factor TFIID subunit 14
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex/transcription factor TFIID complex subunit TAF12
- SAGA complex/transcription factor TFIID complex subunit TAF10
- Transcription initiation factor TFIID subunit 3
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 8
- TATA-box-binding protein
Sequence:
MAVIRIKKPRGPGEKDQPLEGEPKLKRIRIKTKVTDEDIKPKPKLKINLKKKKESADGKEKKNSLKLKLNLKKNEEPVKKIHKAPKLRLKPIRIPGEAYDSEASDIEDDPLIESGVILRILPDIQLEFVKNSLESGDYSGISIKWKNERHAVVTINDVMYGAILVDLPTVIEVNKSVDRKNLLKTFDVSQMLLCIRPIQEEEEVYALEAPDTEDLVVKHFEGIEDEIWENKETFLKGYNGAPLSDMEAKHLKEIALKGYDYKHGISPPLYNVRNRRFRRKMDPNEIDYVEKVVDMLLKQDKQAEEVSYDLVDKSELQARQERVSSWENFKEEPGEPLSRPALKKEEIHTIASAVGKQGAEEEGEEGMEEEEEEDLDLGAAFESEEEGSGAEGDKEQQQEEVGDEVDQDTGGEDDDDDDDGDIEAAGGESESDDEKDENRQHTELLADELNELETTLAHTKHKLSKATNPLLKSRFIDSIKKLEKEAELKRKQLQQTEDSVQKQHQHRSDAETANNVEEEEEEEEEEEEEDEVDEDEEDDEENDEDEDNVHEREHIQENKVVRELDEAPAEETLDQNDLDMMMLFGAEGDE
Protein: Kappa-casein (A1YT10)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
HVTHTHIYLLAFPKENQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTA
Protein: Serine/threonine-protein kinase Nek7 (EC 2.7.11.34) (Never in mitosis A-related kinase 7) (NimA-related protein kinase 7) (Q8TDX7)
Organism: Homo sapiens (Human)
Function: Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression. Phosphorylates RPS6KB1 (By similarity). Acts as an essential activator of the NLRP3 inflammasome assembly independently of its kinase activity. Acts by unlocking NLRP3 following NLRP3 tranlocation into the microtubule organizing center (MTOC), relieving NLRP3 autoinhibition and promoting formation of the NLRP3:PYCARD complex, and activation of CASP1. Serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division: interaction with NEK9 prevents interaction with NLRP3 and activation of the inflammasome during mitosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ES74}. Cytoplasm {ECO:0000269|PubMed:17586473}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19414596}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17101132, ECO:0000269|PubMed:17586473}. Note=Present at centrosome throughout the cell cycle (PubMed:17586473). Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody (PubMed:17586473). Interaction with ANKS3 prevents its translocation to the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9ES74, ECO:0000269|PubMed:17586473}.
Interaction partners:
- Serine/threonine-protein kinase Nek9
- NACHT, LRR and PYD domains-containing protein 3
- Serine/threonine-protein kinase Nek6
- Caspase-1
- Ankyrin repeat and SAM domain-containing protein 3
- Ankyrin repeat and SAM domain-containing protein 6
- Apoptosis-associated speck-like protein containing a CARD
- Gasdermin-D
- Protein bicaudal D homolog 2
- RCC1-like G exchanging factor-like protein
Sequence:
MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASS
Protein: Formin homology 2 domain containing, isoform I (Formin homology 2 domain containing, isoform J) (E1JI78)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Muscle-specific protein 300 kDa, isoform G
- Profilin
Sequence:
MSSYRSYTPWKTSLGSSYKPGSSTYGTSGDSTSRYTSLATPSSYRPSFSGGTYRLKRDPPPPVTTTPVSSYVSRYAKTEPKDAAPSERSSPVKRYTGNTTSSLGKYGRSRDPSPVALEHTNRNKSRDPSPVIDSARSKLGSTYRGGNTPTTSSSSSSATRNAYSSRYGAGSRISGNGSALSYLTTSDFHARTASRAKASREREREKEKEKEKEQEIEEKPSETSNGIDKSPAKQQVEKPENDEEPNETFITISVVTRATSPTLPGSTTVQRTRRIDPAKTIEKTIQRSSKRRETTDQEIQSDRLDDSTRYLRYSAGSSISSTYSPHRDRISSLRYSASPLNSSGSAKSSSVGEGKQIQPIPETVSPARTNGSVSSAKSSEALSPPRTNGNVSSGKSSEALSLPRSNGCSSKSTEAVSPPRTNGSLSSSKSTKSKLSPPKAIRLNSRQSSVENLVNKPPAPPSKADSPTKTCSSSSGSSAVKWPNKDFRKSSLNVGPTDRPRKSRTPSSGGESEDLPNGSSLERSPSAGSDGSLASGSSSKKSSKLSNGKVPGSLKPKSHKSCSETTTGNSSSATASASDSEQRVKSVKKQAKKKTTTKEGGAGKVANANKTNSTTESPPAVVDVVPATQTRLKKLSAVSNFFASRQQDANNEPIFLESSESSGEPEAHSLPVISAISGTSKISKISGISLTTDLRTNEPRTTPSSEAKQSPQTNSPSSSTRCPRETTTETGTRLPSSTTSTTQESSLTTTASLTTSEQDDPSWWQDTSLQINTASALDQNNRGEMPSYRLRHIDSGEEQAWWLRQDENGDDDDTLAEETLNTLDDDLQEPSKSTWWSQDDQDSSSQVKLMPRSRITPEKDAWWLQDEDEAAKSPIENGDLNNNNNSEPHVEVTLRLPSNGSQRSSKSSASKNGSNPKSGGANPWWLSGPARKMFNVQRVESGERAWWQEEAEEPPQEEKESEPPPVKPPTPPPRIIKHWESGERAWWLQDETESNQLPVQASSDDEEQPVLVVINQQESRDEVDLRLAPPTLESQELSNSFNFDAHSERPPPLGQCASPVRCPSPYDNIPRSQLQEPPPPPTTTLTSLQPRFSPQTRRAGEKLFISRHQNIDELLGGACRPLSPLFYGNSNPAESELTPLAGKNMFLLEEVTPDQVRIHDSTAQLPVIQRMQRDVEWLDNGSNFYEPPEQRQHQPPRRIDDAAIQVYKDGDYGAYLDLESSLAEQAEEIEGVNVSRKNSLVVRTQLNVRVQAIIEKLLSAQGSDLRRALFSLKQVFQEDKDLVHAFVALGGLNCLVRVGNCADQNYQNYILRALGQVMLYVDGMNGVMKHEPTMQWLYSLIASNYRSVVKTALKLLLVFVEYAESNCYVLVSAIHAVDASQGTLPWSNIMRLLKDYDNADAELVIYATSLINKTLAGLNDQDSFYDESDLLEQQGMETVIQRYMSKPGTDLDLLDQLQLYEAVLKFEDGESDGQRLPQNSMRKTQRYRPGANTTERRKSRRHSTDNSPASLTKVLPTTVLRMTPTQATVDEDSSGSTNSTEFSGGLFNEKKPRDGAGVTPGLRRRRERAERHKSFLKEQQEAAANGIFAALEQREGLGQIVTAIPATIQTGDSPPQSLQHEVPPCNNISGITNISNNNVSNLSCNDTPNNSLLVMSPSKQLLTGSHSISIINNSFDKASNNNQSEFLTKKNLFRERNSTVINGIMKNIQQTDSAYKKYENEANRLNNYYSQSPKHQIHQPIQPTPEVLLSPKKTLNASGFDFTPAPLSSTPVKCDVPPEPEPLSPVKKPAAAPPPPPPPPPPPPPPPGWWHAPIYNSPQARTLTSTNPELLPHPVDPSDMESEDQQLLLQLKRDHTVKDLTQKLSNLPMSPTQDSANRALVGDMSGLISKAKEGLAKSKSKGEISRSSSVDQDVKKSEPKKSENELHWEELVRNMTRPLNLCDLDFTDLRDDDEKDVLAPRSLGAGIPPPPPPLGGAIAPPPMMPPSLAPPPMYGYGGSLTNSVNSLNGSINGELVNGNNTIKKNKKTVKLFWKEVREDMIPQVVGKTIWDELPDANVDTQKLEHLFESRAKDLMTKKQQELNKSKEIIVLDHKRSNAINIAITKLPPPRAIKTAILKMDATVVTREGIDKLLNMLPTDEERGKIQEAQLSNPELPLGSAEQFLLTLASISELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNGAPVKGFQIEYLAKVPEVKDTVHKHSLLHHLCHMVMESSSDTSDLYSEIGPITRASKADFTDLAHNLNQLEAECKACWDRLKLIAKHDCPPPLKQKLVDFLADCAERIIILQIVHRRVMNRYRKFLLWLGMPQHSVAESRPNEFCRTLSEFALEYRTTRERVQQQLEKKANHRERNKTRGKLIIDMAKFKTKDDVADDELKKLLDTSSADQADGTLTWRRRRAEQLRSPITRQSEEQFTDGDDEILESLVKTATKAPGTRTTPRERKRTRHADRKSLRRTLKNGLTEEEKQHVAALIQTY
Protein: Large ribosomal subunit protein eL18 (60S ribosomal protein L18) (Q9VS34)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein eS10A
- 40S ribosomal protein S27
- 60S ribosomal protein L27
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL15
Sequence:
MGIDINHKYDRKVRRTEPKSQDVYLRLLVKLYRFLQRRTNKKFNRIILKRLFMSKINRPPLSLQRIARFFKAANQPESTIVVVGTVTDDARLLVVPKLTVCALHVTQTARERILKAGGEVLTFDQLALRSPTGKNTLLLQGRRTARTACKHFGKAPGVPHSHTRPYVRSKGRKFERARGRRSSCGYKK
Protein: Innexin (Q23594)
Organism: Caenorhabditis elegans
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}.
Interaction partners:
Sequence:
MFSVPFLTSLTSHLGITAIDDASDTLSCLITAFLFIIAAILTSAQSYVGSAMECWLPQTYSGAWEEFAENYCFLKDTYFYPRQQSMTDIPMYHKERHRLTYYQWSSMYLAVAGIAFMIPKFIWRLSQSTTDMPLIYFCDTANEIKIETTEKRSSKVKEMARFMRSKITTVHTPSIFSCIRMYSVYSIVKMLYLIIAIAQFVILAIFLDQEKDMFWGWTLFMNLLNGITWETTGLFPRVTFCDFEIRETAGNNRAETVECLIGINVFNEKIFLFLWFWLLFLIFSTLVAHIYNATHIAKPYIINSLLHSIRDHGIVDQKELFKEFGEKYLTMDGKIILSFVKAQSDLVASEVAVEMYNDFLEVRDQRIYIISHEFNDIQKTRN
Protein: Ranatuerin-2OK (C0HL07)
Organism: Nidirana okinavana (Kampira Falls frog) (Babina okinavana)
Function: Antimicrobial peptide. Active against Gram-negative bacterium E.coli (MIC=12.5 uM) and against Gram-positive bacterium S.aureus (MIC=50 uM).
Subcellular location: Secreted {ECO:0000269|PubMed:15629529}.
Interaction partners:
Sequence:
SFLNFFKGAAKNLLAAGLDKLKCKISGTQC
Protein: Glutathione S-transferase Mu 4 (EC 2.5.1.18) (GST class-mu 4) (GST-Mu2) (GSTM4-4) (Leukotriene C4 synthase GSTM4) (EC 4.4.1.20) (Q03013)
Organism: Homo sapiens (Human)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4. Can also catalyzes the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8373352}.
Interaction partners:
- Glutathione S-transferase Mu 2
- Glutathione S-transferase Mu 3
- Glutathione S-transferase Mu 5
- Epoxide hydrolase 1
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Glutathione reductase, mitochondrial
- Cytochrome P450 2E1
- Maleylacetoacetate isomerase
- Cytochrome P450 1A2
- Peroxiredoxin-6
Sequence:
MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDFEKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK
Protein: MADS-box transcription factor pvg4 (MADS-box transcription factor 2) (Pyruvylated Gal-beta-1,3-epitope synthesis protein 4) (PvGal synthesis protein 4) (Q9HGP0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts in transcription regulation. May bind to a MEF2-like typee II promoter sequence.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:15173185}.
Interaction partners:
- Galactose-specific cell agglutination protein gsf2
- Mitogen-activated protein kinase sty1
- Uncharacterized transcriptional regulatory protein C15D4.02
- MADS-box transcription factor 1
- Beta-1,3-galactosyltransferase pvg3
- Putative cell agglutination protein pfl8
- Putative cell agglutination protein pfl3
Sequence:
MGRKKISIAPITDDRSRSVTFVKRKQGLYKKAYELAVLADCEVAVTVIDRKGRLHVFCSSDYQRTLQQLNTLSIYELKNRSHFSSSPVEESSTVSPETTTGSFTPLNNKHLKSQDQPLSDSQLDTGDSPATSETTVQDYNPQVQSYCRPEPLSSNHVRSCPPFPPTQHHHPHTRPPHHPPHPHFHNNNYPPPYCFQSPVSPGATVPLQHHSPYPSDNGFPGHRRQTHFAPYYYPQRATSPSLKQVPTYLGTHVLQQDQSTYDQKVLMPPASYLSSPNQYTLKNVSPGNPACPPFLYEHPNPQLTPEMFDVKQGSPIPPTAYSGSSCETSQHTIANTPFLAYDRSPSLTNQEAESSFQDVASISPHSLSDVKY
Protein: Pancreatic adenocarcinoma up-regulated factor (Zymogen granule protein 16 homolog B) (Q96DA0)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000269|PubMed:19302292}. Cytoplasm {ECO:0000269|PubMed:19302292}. Cell membrane {ECO:0000269|PubMed:36232715}. Apicolateral cell membrane {ECO:0000269|PubMed:19302292}. Note=Co-localizes with TLR4 at the cell membrane of pancreatic cancer cells. {ECO:0000269|PubMed:36232715}.
Interaction partners:
Sequence:
MLLLLTLALLGGPTWAGKMYGPGGGKYFSTTEDYDHEITGLRVSVGLLLVKSVQVKLGDSWDVKLGALGGNTQEVTLQPGEYITKVFVAFQAFLRGMVMYTSKDRYFYFGKLDGQISSAYPSQEGQVLVGIYGQYQLLGIKSIGFEWNYPLEEPTTEPPVNLTYSANSPVGR
Protein: Serine/threonine-protein kinase WNK4 (EC 2.7.11.1) (Protein kinase lysine-deficient 4) (Protein kinase with no lysine 4) (Q96J92)
Organism: Homo sapiens (Human)
Function: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D, SGK1, TRPV5 and TRPV6. Regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation which appears to prevent membrane trafficking of SLC12A3. Also inhibits the renal K(+) channel, KCNJ1, via a kinase-independent mechanism by which it induces clearance of the protein from the cell surface by clathrin-dependent endocytosis. WNK4 appears to act as a molecular switch that can vary the balance between NaCl reabsorption and K(+) secretion to maintain integrated homeostasis. Phosphorylates NEDD4L. Acts as a scaffold to inhibit SLC4A4 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:Q80UE6}. Note=Present exclusively in intercellular junctions in the distal convoluted tubule and in both the cytoplasm and intercellular junctions in the cortical collecting duct (By similarity). WNK4 is part of the tight junction complex (By similarity). {ECO:0000250|UniProtKB:Q80UE6}.
Interaction partners:
- Kelch-like protein 3
- ATP-sensitive inward rectifier potassium channel 1
- Solute carrier family 12 member 3
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Cullin-3
- Serine/threonine-protein kinase OSR1
- Kelch-like protein 2
- Solute carrier family 12 member 2
- Epithelial sodium channel subunit beta
- Epithelial sodium channel subunit alpha
Sequence:
MLASPATETTVLMSQTEADLALRPPPPLGTAGQPRLGPPPRRARRFSGKAEPRPRSSRLSRRSSVDLGLLSSWSLPASPAPDPPDPPDSAGPGPARSPPPSSKEPPEGTWTEGAPVKAAEDSARPELPDSAVGPGSREPLRVPEAVALERRREQEEKEDMETQAVATSPDGRYLKFDIEIGRGSFKTVYRGLDTDTTVEVAWCELQTRKLSRAERQRFSEEVEMLKGLQHPNIVRFYDSWKSVLRGQVCIVLVTELMTSGTLKTYLRRFREMKPRVLQRWSRQILRGLHFLHSRVPPILHRDLKCDNVFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDEAVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGRKPNSFHKVKIPEVKEIIEGCIRTDKNERFTIQDLLAHAFFREERGVHVELAEEDDGEKPGLKLWLRMEDARRGGRPRDNQAIEFLFQLGRDAAEEVAQEMVALGLVCEADYQPVARAVRERVAAIQRKREKLRKARELEALPPEPGPPPATVPMAPGPPSVFPPEPEEPEADQHQPFLFRHASYSSTTSDCETDGYLSSSGFLDASDPALQPPGGVPSSLAESHLCLPSAFALSIPRSGPGSDFSPGDSYASDAASGLSDVGEGMGQMRRPPGRNLRRRPRSRLRVTSVSDQNDRVVECQLQTHNSKMVTFRFDLDGDSPEEIAAAMVYNEFILPSERDGFLRRIREIIQRVETLLKRDTGPMEAAEDTLSPQEEPAPLPALPVPLPDPSNEELQSSTSLEHRSWTAFSTSSSSPGTPLSPGNPFSPGTPISPGPIFPITSPPCHPSPSPFSPISSQVSSNPSPHPTSSPLPFSSSTPEFPVPLSQCPWSSLPTTSPPTFSPTCSQVTLSSPFFPPCPSTSSFPSTTAAPLLSLASAFSLAVMTVAQSLLSPSPGLLSQSPPAPPSPLPSLPLPPPVAPGGQESPSPHTAEVESEASPPPARPLPGEARLAPISEEGKPQLVGRFQVTSSKEPAEPLPLQPTSPTLSGSPKPSTPQLTSESSDTEDSAGGGPETREALAESDRAAEGLGAGVEEEGDDGKEPQVGGSPQPLSHPSPVWMNYSYSSLCLSSEESESSGEDEEFWAELQSLRQKHLSEVETLQTLQKKEIEDLYSRLGKQPPPGIVAPAAMLSSRQRRLSKGSFPTSRRNSLQRSEPPGPGIMRRNSLSGSSTGSQEQRASKGVTFAGDVGRM
Protein: ER membrane protein complex subunit 4 (Cell proliferation-inducing gene 17 protein) (Transmembrane protein 85) (Q5J8M3)
Organism: Homo sapiens (Human)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22119785}; Multi-pass membrane protein {ECO:0000305|PubMed:32439656, ECO:0000305|PubMed:32459176}. Note=Could also be a single-pass transmembrane protein with cytosolic N-terminus and lumenal C-terminus. {ECO:0000305|PubMed:32439656, ECO:0000305|PubMed:32459176}.
Interaction partners:
- ER membrane protein complex subunit 5
- Endoplasmic reticulum membrane protein complex subunit 7
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 9
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 8
- Vacuolar protein sorting-associated protein 28 homolog
Sequence:
MTAQGGLVANRGRRFKWAIELSGPGGGSRGRSDRGSGQGDSLYPVGYLDKQVPDTSVQETDRILVEKRCWDIALGPLKQIPMNLFIMYMAGNTISIFPTMMVCMMAWRPIQALMAISATFKMLESSSQKFLQGLVYLIGNLMGLALAVYKCQSMGLLPTHASDWLAFIEPPERMEFSGGGLLL
Protein: UPF0303 protein P4H10.12 (Q9P7D6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Small glutamine-rich tetratricopeptide repeat-containing protein 2
Sequence:
MFSILKRTDHLEESFLKNPNDNLKELENIIIEQEEALRFSSLSYADCYSLGVIVRDLYAKAAYTAPIVIDITLNGHQVFHLAYDGSSPDNDAFIKRKYATVQRFRMSSMRMGLMMAQQGTTMPAKYDVPAEEYGAFGGGFPIKLTSGIQIGVFCISGLRQIQDHCLIARSIAEFLTTKQ