wanglab/gogpt-training-data huggingface dataset:
Protein: Homeobox protein Meis2a (Myeloid ecotropic viral integration site 2.2) (Q6PHK8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MAQRYDELAHYGGMDGVGMYGDPHAPRPLPQVHHLNHGPPLHASQHYGTHAPHPNVMPTSMGSAVNDVLKRDKDQIYGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELYNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPASWRDHDDATSTHSAGTPGPSSGGLASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGPMSGMGMNMGMDGQWHYM
Protein: V-type proton ATPase subunit C 1 (V-ATPase subunit C 1) (Vacuolar proton pump subunit C 1) (Q9Z1G3)
Organism: Mus musculus (Mouse)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5FVI6}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q5FVI6}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit E 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit G 2
- V-type proton ATPase subunit H
- Renin receptor
Sequence:
MTEFWLISAPGEKTCQQTWEKLHAATTKNNNLAVSSKFNIPDLKVGTLDVLVGLSDELAKLDAFVEGVVKKVAQYMADVLEDSKDKVQENLLASGVDLVTYITRFQWDMAKYPIKQSLKNISEIIAKGVTQIDNDLKSRASAYNNLKGNLQNLERKNAGSLLTRSLAEIVKKDDFVLDSEYLVTLLVVVPKLNHNDWIKQYETLAEMVVPRSSNVLSEDQDSYLCNVTLFRKAVDDFRHKARENKFIVRDFQYNEEEMKADKEEMTRLSTDKKKQFGPLVRWLKVNFSEAFIAWIHIKALRVFVESVLRYGLPVNFQAMLLQPNKKSVKKLREVLHELYKHLDSSAAAIIDAPMDIPGLNLSQQEYYPYVYYKIDCNLLEFK
Protein: Malolactic enzyme (MLE) (EC 4.1.1.101) (A0A095AMW7)
Organism: Leuconostoc mesenteroides
Function: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate.
Interaction partners:
Sequence:
MNTTGYDILRNPFLNKGTAFSEAERQQLGLTGTLPSQIQTIEEQAEQAYKQFQAKSPLLEKRIFLMNLFNENVTLFYHLMDQHVSEFMPIVYDPVVAESIEQYNEIYTNPQNAAFLSVDRPEDVENALKNAAAGRDIKLVVVTDAEGILGMGDWGVNGVDIAVGKLMVYTAAAGIDPATVLPVSIDAGTNNKELLHNPLYLGNKHERIAGEQYLEFIDKFVTAEQNLFPESLLHWEDFGRSNAQVILDKYKESIATFNDDIQGTGMIVLAGIFGALNISKQKLVDQKFVTFGAGTAGMGIVNQIFSELKQAGLSDDEARNHFYLVDKQGLLFDDTEGLTAAQKPFTRSRKEFVNPEQLINLETIVKELHPTVLIGTSTQPGTFTETIVKSMAENTERPIIFPLSNPTKLAEATAEDLIKWTGGKALVATGIPAADVDYKGVTYKIGQGNNALIYPGLGFGLVASTAKLLTQETISAAIHALGGLVDTDEPGAAVLPPVSNLTDFSQKIAEITAQSVVNQGLNREKIVDPKQAVQDAKWSAEY
Protein: Probable fructokinase-7 (EC 2.7.1.4) (Q9FLH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play an important role in maintaining the flux of carbon towards starch formation.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Sorbitol dehydrogenase
- Hexokinase-4
- Hexokinase-like 1 protein
- Hexokinase-3
- Hexokinase-1
- Hexokinase-2
- Probable hexokinase-like 2 protein
- alpha-D-xyloside xylohydrolase
Sequence:
MGEDAISGNLKNLTIDTRDSETLVVCFGEMLIDFVPTVGGVSLAEAPAFKKAPGGAPANVAVGVSRLGGSSAFIGKVGDDEFGRMLADILRLNNVDNSGMRFDHNARTALAFVTLRGDGEREFLFFRHPSADMLLLESELDKNLIQKAKIFHYGSISLIEEPCRSTQLVAMKIAKAAGSLLSYDPNLRLPLWPSEEAARKEIMSIWNLADVIKISEDEITFLTGGDDPYDDDVVLQKLFHPNLKLLVVSEGPNGCRYYTQEFKGRVGGVKVKPVDTTGAGDAFVSGLLNSLASDLTLLKDEKKLREALLFANACGAITVTERGAIPAMPSMDAVQDLLSSTRS
Protein: Zinc finger protein NUTCRACKER (Protein indeterminate-domain 8) (Q9FFH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds to the DNA sequence 5'-CTTTTGTCC-3'. Regulates photoperiodic flowering by modulating sugar transport and metabolism. Regulates SUS1 and SUS4. Transcription factor that regulates tissue boundaries and asymmetric cell division. Contributes to the sequestration of 'SHORT-ROOT' to the nucleus.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:21265895, ECO:0000269|PubMed:25929516}.
Interaction partners:
- SNF1-related protein kinase catalytic subunit alpha KIN10
- Sucrose transport protein SUC7
- Sucrose transport protein SUC8
- At5g47635
- Putative sucrose transport protein SUC6
Sequence:
MTSEVLQTISSGSGFAQPQSSSTLDHDESLINPPLVKKKRNLPGNPDPEAEVIALSPTTLMATNRFLCEVCGKGFQRDQNLQLHRRGHNLPWKLKQRTSKEVRKRVYVCPEKTCVHHHSSRALGDLTGIKKHFCRKHGEKKWTCEKCAKRYAVQSDWKAHSKTCGTREYRCDCGTIFSRRDSFITHRAFCDALAEETAKINAVSHLNGLAAAGAPGSVNLNYQYLMGTFIPPLQPFVPQPQTNPNHHHQHFQPPTSSSLSLWMGQDIAPPQPQPDYDWVFGNAKAASACIDNNNTHDEQITQNANASLTTTTTLSAPSLFSSDQPQNANANSNVNMSATALLQKAAEIGATSTTTAATNDPSTFLQSFPLKSTDQTTSYDSGEKFFALFGSNNNIGLMSRSHDHQEIENARNDVTVASALDELQNYPWKRRRVDGGGEVGGGGQTRDFLGVGVQTLCHPSSINGWI
Protein: Phosphatidate cytidylyltransferase 3 (EC 2.7.7.41) (CDP-DAG synthase 3) (CDP-DG synthase 3) (CDP-diacylglycerol synthase 3) (CDS3) (CDP-diglyceride pyrophosphorylase 3) (CDP-diglyceride synthase 3) (CTP:phosphatidate cytidylyltransferase 3) (Q1PE48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the synthesis of minor phospholipids and in modulation of IP3-mediated signal transduction.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Cardiolipin synthase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 2
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 1, chloroplastic/mitochondrial
- Phosphatidate phosphatase PAH1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Diacylglycerol kinase 5
- Phospholipase D zeta 1
- Choline/ethanolaminephosphotransferase 1
Sequence:
MAMEKDLSPNSPRIRKLRDTSYPTTPTSRMNTNNQRDNHYPNIPNSPRDYNYTPSSPTARIRHRRRSSENLAEVNRSNVSRVSNLLLGDKNKYRSMWIRTCSSLWMLGGVVFIIYMGHLYIWAMVVVIQIFMAKELFFLRRRAHEERRLPGFWLLNWHFFFTAMLFVYGRIIQQQLVNTVSSDRFIYKLVSGLIKYQMVICYFLYIAGLIWFILTLKNKMYKYQFGQYAWTHMILIVVFTQSSFTVANIFEGIFWFLLPAALIAMNDVAAYFFGFYFGKTPLIKLSPKKTWEGFIGASVATIISAFIFANVLGQFQWLTCPRKDLSTGWLHCDPGPLFRPEYYPFPSWITPFSPWKGISTLPVQWHAFSLGLFASIMAPFGGFFASGFKRAFKIKDFGDSIPGHGGFTDRMDCQMVMAVFAYIYIQSFIVNRDYSVEMILDQISRSLGHEEQKMLYEKLGDILQHKLQGRF
Protein: Biphenyl 2,3-dioxygenase subunit beta (EC 1.14.12.18) (Biphenyl dioxygenase system, oxygenase component subunit beta) (BDO, oxygenase component subunit beta) (Terminal oxygenase component of biphenyl dioxygenase, small subunit) (Q53123)
Organism: Rhodococcus jostii (strain RHA1)
Function: Part of the oxygenase component of the biphenyl dioxygenase system that catalyzes the stereospecific dihydroxylation of the aromatic ring of biphenyl, yielding a dihydrodiol compound. Is likely involved in biphenyl degradation that allows growth of Rhodococcus sp. strain RHA1 on biphenyl as the sole source of carbon and energy. Can also use naphtalene and 4-chlorobiphenyl (4-CB) as substrates, as well as some polychlorinated biphenyls (PCB) such as 2,2'-dichlorobiphenyl, 2,3-dichlorobiphenyl and 2,5,2'-trichlorobiphenyl. Exhibits weak activity toward dibenzofuran and dibenzo-p-dioxin. Electrons are transferred from NADH to the [2Fe-2S] cluster in BphA1 via FAD of BphA4 and [2Fe-2S] cluster of BphA3.
Interaction partners:
Sequence:
MIDAESPTTAFRTKPAPVDPSLQHEIEQFYYWEAKLLNDRRFQEWFDLLAEDIHYFMPIRTTRIMRETAQEYSGAREYAHFDDNAQMMRGRLRKITSDVSWSENPASRTRHVISNVMIVDGEKPGEYHVSSVFIVYRNRLERQLDIFAGERKDILRRTGSEAGFELAKRTILIDQSTILSNNLSFFF
Protein: WD_REPEATS_REGION domain-containing protein (P90757)
Organism: Caenorhabditis elegans
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Intraflagellar transport protein 122 homolog
- WD repeat-containing protein dyf-2
- Anaphase-promoting complex subunit 4-like WD40 domain-containing protein
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 52 C-terminal domain-containing protein
- Intraflagellar transport protein che-13
- Tetratricopeptide repeat protein 21 homolog
- CHE-2 protein
- Intraflagellar transport protein osm-1
- Intraflagellar transport protein 20 homolog
Sequence:
MKPFLIEWAPHCGWICVVTQDETTGEANVAFSDHSGSVQEKGPSKPGSVSCVRWHPKKQFVVVGWKDGGVCFIPKGGNVSHTVVETYPFPNQGVDWSHDGTVLMTLHNPSSVHLYSYMVIGEEISTSNIMQIELNDQITLWCKRLSYDKFKPSKISVTDDDSGVDESPFGSKESLAERRDEKSTVPKGTEFLFAGKSGTIYGVDNDRQRTIHKLDSEILFMGYCETISIIIVFTRDCFIFHLAKGTSEMRCAERVKVKLGGKSEKYSLELDDGILVMCYGEKEIRVWDLIKEENGTIALDVNKGFQPDETINVVTVNGKRGVITAATSLNNIAEWKRKRTDTNVESAWNLSPSTHVDSQVSLIRWSPILSTAALITEEDLVLIGENSLTVKMRGKMAAIQTSSNSFTLLHATSGVSQDLKLSIPSAKGICLGEKQLVVWNEDTVVTYDVQTSLATIQCTSFSCNTTSVAIVNQNLYCIEKDKIFARTLQGTLRQEISLPEIEGDPEILEVNRCWMAVATTNGFIRIYNLSAKDAQQEHNSKYIIENVKNFYKFHTIRINHTGNKVAVSYLEDVSTVAERLLVYDAELDAVSYFSFDRGMTDTQEYETQAELAHTSSGRPVTAAARKMAREQSRFQMMNHRPGAFEWDENDARYLVVECIHVEPESTDQRVLTAFVTSEHGIQLQGMQQKNLHCGKLVSVSVPNFYFVRKSGWDEEDNRDERTIGKTLVAKCLREFLGNENCDESTRKAMMDFSFYLTIGSMDAAFKAIQFIKSDSVWDHMASMSIKTRRLDVAMVCLGHMKNVRGARAVRRSQQNGENDSMKCAALAIELSMLEEALIIYAQNERYDLMNKLYQSQNMWSSAFEIAETKDRIHLRNTHYNYAKYLEARRDQASIEAAIENYEKAGVHAFEVFRMLKDYPKQIEQYVRRKREESLYSWWGAYLESVGELEGAISFYSSAKDYYCMVRVKCIQGKTDEAARLAEESKDKAACYLIGRMYENDGDVVKAVKFFTKARALSSAIRLAKEHDMKDRLANLCLMAGGSELVSAARYYEDLPGYAHKAVMLYHKAGMIGRALDLAFRTEQFSALDLITKDLDAGTDPKILRRAAEFFENNQNYEKAVNFLCLAKEFSGAVQLCKNRNVRVSDKFAELMTPTKDDMPNVQERKQVLETVAELCLQQGAYSAAAKKFTQAGDKLSAMRALLKSGDIQKIRFFANTARNKEIYILAANFLQTTDWQDNQQTMKDIETFYTKSQSFEHLGNFYKSVAIIEAEHLRTLDKSMGALEMAAVCVLEAEQKNMSTTGLDALKEDLKKYVVQLRKLQSVLEVMKNDAADGMRQLTTLAEESIDDDIVPCTRLFALIIEDHASRKNWKPAYRAITGLQKKVPNVDLETFVETSTLDKVCDEMRMERVTKKKKEEVESDGEEVDFSHSLRRQNVS
Protein: Protein tyrosine phosphatase type IVA 1 (EC 3.1.3.48) (PTP(CAAXI)) (Protein-tyrosine phosphatase 4a1) (Protein-tyrosine phosphatase of regenerating liver 1) (PRL-1) (Q93096)
Organism: Homo sapiens (Human)
Function: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:15571731}; Lipid-anchor {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:12235145, ECO:0000269|PubMed:15571731}. Early endosome {ECO:0000269|PubMed:12235145}. Endoplasmic reticulum {ECO:0000269|PubMed:12235145}. Cytoplasm {ECO:0000269|PubMed:12235145}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12235145}. Nucleus {ECO:0000250|UniProtKB:Q78EG7}. Note=And mitotic spindle. {ECO:0000269|PubMed:12235145}.
Interaction partners:
- Metal transporter CNNM2
- Cyclic AMP-dependent transcription factor ATF-7
- Protein tyrosine phosphatase type IVA 2
- 6-pyruvoyl tetrahydrobiopterin synthase
- PHD finger protein 3
- Metal transporter CNNM3
- Lipid droplet-regulating VLDL assembly factor AUP1
- Interleukin-17 receptor D
- Metal transporter CNNM4
- Metal transporter CNNM1
Sequence:
MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (A8K3Y2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSQSKGKKRNPGLKIPKEAFEQPQTSSTPPRDLDSKACISIGNQNFEVKADDLEPIMELGRGAYGVVEKMRHVPSGQIMAVKRIRATVNSQEQKRLLMDLDISMRTVDCPFTVTFYGALFREGDVWICMELMDTSLDKFYKQVIDKGQTIPEDILGKIAVSIVKALEHLHSKLSVIHRDVKPSNVLINALGQVKMCDFGISGYLVDSVAKTIDAGCKPYMAPERINPELNQKGYSVKSDIWSLGITMIELAILRFPYDSWGTPFQQLKQVVEEPSPQLPADKFSAEFVDFTSQCLKKNSKERPTYPELMQHPFFTLHESKGTDVASFVKLILGD
Protein: DNA repair/transcription protein mms19 (Q9UTR1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Key component of the cytosolic iron-sulfur protein assembly (CIA) machinery that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. Acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as rad3/xpd and dna2, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable cytosolic Fe-S cluster assembly factor SPAC806.02c
- MIP18 family protein C144.16
- Cytosolic Fe-S cluster assembly factor NAR1 homolog
- General transcription and DNA repair factor IIH helicase subunit XPD
- NADPH-dependent diflavin oxidoreductase 1
- Fe-S cluster assembly protein dre2
- DNA polymerase epsilon catalytic subunit A
- Rik1-associated factor 2
- Cytosolic Fe-S cluster assembly factor nbp35
- Chromatin modification-related protein rik1
Sequence:
MSSNLVALYLFSIDRSQDEANDVVDRIVEEIVTDRMGIVDLVTSIGEYLTDNNISVRAKAVLLLSQTLGELPKDRLPAKHVSVLLQFYLSRLDDEVTMKENALGIGALLNMQNFPAQKIVDVCKALFSSTDMPKYAQATRLNILKVFETIIDNYLFFISSQTRDAFFSGICSTFAGEKDPRNLMLVFSMLKKILSTFPIDGFEQQFFDITYCYFPITFRAPPDATNLAITSDDLKIALRETLVANDAFSKLLLPALFERLKASTVRIKIDALNIYIEACKTWRVGAYLWSAKDFWESIKQEILNSTDAELQNLALGALNTLASKFYKEEGFSSSFTEFVDMILIQLSQRLLEDVNVKSCGSCAAVFASLASISVETFNYCSCNFLPSVLDLPMVNEPLEKQKGMLVFLEYVYKCLVLLYGKWRSKNQADIDNPLLVYKDKQLSFVSGSLMGTAKDETEIRMLALKVIFLMASIKNFLTESELTMVLQFLDDIAFDFSDPIKKKATECLKDLGLLKPDFLLLTSFPFAFSKLTDDVTAKSSSEETFKQYLSVLVSISEERSLFKALVIRLVEMLKDQFKSKEMSVDLVESIVQSLSVAFKERNDRNEQEIPFFFEELLKQLFTLCFANCESMNVRCLIYVSQTINEIVRVNHFEFQEKFVGQLWKLYMENSNSDLIETEGCEKAAERFTLAASLSDQKFLNLVVLLQGGLNGLSKKLHFIEKLNIELLNLLINVVFVTESPGVKISALRLISSLINKCEKDEDISSFISSKGVTSLWDKVYTGTPKESEAALDVLAWVDKALVSRKHSEGIPLAFKLLDTLNLQNVGDSSVKALSIIIKDDPALSKENSYVEKLLYKQRFYASVSPKILEHISTATGGEKSLYLMLLSNVIGNVPKEIVIPDMPSILPLLLQCLSLSDISVKLSTLNVIHTSVKELTSLLTEYLDTLIPSLLAIPKDMNNPTVVRLLALKCLGSLPEFTPTTNLQLFRDKVIRGLIPCLDDPKRVVRTEASRTRHKWYI
Protein: Probable protein phosphatase 2C 74 (AtPP2C74) (EC 3.1.3.16) (Q9FG61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a protein phosphatase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19021904}.
Interaction partners:
- At4g03260
- Probable protein S-acyltransferase 12
- DNA polymerase I A, chloroplastic/mitochondrial
- N-acetylglucosaminyl transferase component family protein / Gpi1 family protein
- PLATZ transcription factor family protein
Sequence:
MGSCLSSSGGGGSRRSLHGSPHVPGPGRRKRPPKRRPGSCSSSFDNTEEPLLHRIPGRMFLNGSTDTVSLFSQQGKKGPNQDAMIVWENFGSMEDTVFCGVFDGHGPYGHIVAKRVRDLLPLKLGSHLESYVSPEEVLKEISLNTDDRKISEDLVHISANGESRVYNKDYVKDQDMIQMLIGSIVKAYRFMDKELKMQVDVDCFCSGTTAVTMVKQGQHLVIGNIGDSRAVLGVRNKDNKLVPFQLTEDLKPDVPAEAERIKRCRGRIFALRDEPGVARLWLPNHNSPGLAMARAFGDFCLKDFGLISVPDVSYRRLTEKDEFVVLATDGIWDALTNEEVVKIVAKAPTRSSAGRALVEAAVRNWRWKFPTSKVDDCAVVCLFLDSEPNRLSTASFSKEKHINNGVTEPEPDTASSSTPDSGTGSPELNGVNRIDTLVNLPVYVPTKE
Protein: Sodium/potassium-transporting ATPase subunit beta-1 (Sodium/potassium-dependent ATPase subunit beta-1) (P05027)
Organism: Sus scrofa (Pig)
Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and interferon stimulated genes (ISGs). Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of TAK1 and TBK1.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes. Localizes in long striations at the level of Z and M lines. {ECO:0000250|UniProtKB:P14094}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha-1
- FXYD domain-containing ion transport regulator
- Sodium/potassium-transporting ATPase subunit alpha.
- Sodium/potassium-transporting ATPase subunit alpha
- Sodium/potassium-transporting ATPase subunit beta
- cAMP-dependent protein kinase catalytic subunit beta
- Protein ATP1B4
- cAMP-dependent protein kinase catalytic subunit alpha
- Mitogen-activated protein kinase
- cGMP-dependent protein kinase
Sequence:
MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQSQKTEISFRPNDPQSYESYVVSIVRFLEKYKDLAQKDDMIFEDCGNVPSELKERGEYNNERGERKVCRFRLEWLGNCSGLNDETYGYKDGKPCVIIKLNRVLGFKPKPPKNESLETYPVMKYNPYVLPVHCTGKRDEDKEKVGTMEYFGLGGYPGFPLQYYPYYGKLLQPKYLQPLMAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS
Protein: Vacuolar protein sorting-associated protein 28 homolog (B5DEN9)
Organism: Rattus norvegicus (Rat)
Function: Component of the endosomal sorting complex required for transport-I (ESCRT-I) complex, a regulator of vesicular trafficking process. The ESCRT-I complex participates in the sorting of membrane proteins into vesicles that bud into late endosomal compartments called multivesicular bodies, and is also involved in the budding of many viruses.
Subcellular location: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Cell membrane {ECO:0000250}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Tumor susceptibility gene 101 protein
- Ubiquitin-associated protein 1
- VPS37B subunit of ESCRT-I
- Similar to DNA segment, Chr 8, ERATO Doi 531, expressed, isoform CRA_c.
- Multivesicular body subunit 12A
- Vacuolar protein-sorting-associated protein 25
- Multivesicular body subunit 12B
- Charged multivesicular body protein 6
- Charged multivesicular body protein 3
Sequence:
MFHGIPATPGVGALPCSVAAPGNKPELYEEVKLYKNAREREKYDNMAELFAVVKTMQALEKAYIKDCVTPNEYTAACSRLLVQYKAAFRQVQGSEISSIDEFCRKFRLDCPLAMERIKEDRPITIKDDKGNLNRCIADVVSLFITVMDKLRLEIRAMDEIQPDLRELMETMHRMSHLPPDFEGRQTVSQWLQTLSGMSASDELDDSQVRQMLFDLESAYNAFNRFLHS
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q8I621)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Ran-specific GTPase-activating protein 1, putative
- Uncharacterized protein
- Nucleoporin NUP221, putative
- HSP90 co-chaperone p23
- Heat shock protein 90, putative
- Heat shock protein 90, putative
- Heat shock protein 90
- Activator of Hsp90 ATPase, putative
- Activator of Hsp90 ATPase
Sequence:
MNIPNPRVFLDIAIGGRNAGRMIFELFMDKLPITCENFRCLCTGETGLGYYLKPRWYKNSPIHRIVTDFMFQGGDFNFGNGYGGESIYGQYFRNEKFIYKHSKRGILSMCQTRIKHTNNSQFFVTFKSCPWLDKRHVVLGHLEYGFDTLSFIEEQGTLIGKPKKQVFIYNCGVIPLDKIKYKSADNSDDDYIIPDIEKPLLEKDISINENSDFNELRNMYKYNKHF
Protein: Vesicle-associated membrane protein 714 (AtVAMP714) (Q9FMR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}.
Interaction partners:
- Syntaxin-121
- Syntaxin-22
- Syntaxin-23
- Putative SNAP25 homologous protein SNAP30
- Syntaxin-51
- Syntaxin-52
- SNAP25 homologous protein SNAP29
- Vesicle transport v-SNARE 12
- Syntaxin-123
- Syntaxin-21
Sequence:
MAIVYAVVARGTVVLAEFSAVTGNTGAVVRRILEKLSPEISDERLCFSQDRYIFHILRSDGLTFLCMANDTFGRRVPFSYLEEIHMRFMKNYGKVAHNAPAYAMNDEFSRVLHQQMEFFSSNPSVDTLNRVRGEVSEIRSVMVENIEKIMERGDRIELLVDKTATMQDSSFHFRKQSKRLRRALWMKNAKLLVLLTCLIVFLLYIIIASFCGGITLPSCRS
Protein: Stripe, isoform A (Q9VED3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLLTMRRQNELIVGSQQHPSATSSASSSAGATSSPGLSGQNLNLVAGAGAATNSTSANSQDSLNTPTTPLLGLSRNPLQFAPPPAPPIAVPNPAASGPTFGYYQTVNAAPPIHHSPAATSEVSTAPQPPVELDEYVDILQVQQLLLDSSAAAAAAANNPPTTEQSVQQPQQNTVVQPHPHQQQQQQQQQQQPQQQQQQPQQILAKPRPRINLQKATEYAAQLAQAESSSPGSRRVLLDYPSPYLYGNPYHHHTPPGEDLVALWFGSNGTGGVAPGTPSAAMIMEGLETLVAPTHHAFLLTETAAAAHFNVLSFDTCLFKTSTAAQSSGSPSTATYLSPAQFGGSHHGGASTSSNSLNSSSTASSSSTSSSLLHYTTASAAAAAAAAAAASANNSVLRARNQTATPTQGGSPGHVAVQPSATASSGRSSASHLSLLNTSGQHSPTSSAVEQVEAHKQLIEALPGDLNTPVTTSSDIPSFFGPTTVVEPPPITGSIESEDLSLEPQVISVASPVLSHCSPLKEERSTPPALAIVKEESSNNSCNMYPQHNNNNNNNNNTTSSSTTTTSKQTTSESNTECVGSPGNHTQSHQQQQQQLQHNNTSSSNSNCHHSHQQQQQQQQQQHMSSPQQQYQQHQILHQQQQLPNHHHHHHHHHHHHSQLQQLQQQQQQQQQQQQHQQQPLHQQQQLQHQQQQQHHQQHYQQHAIQHQQSQQQASKISYRGIFTTTGNAMNAAAAAAAAAAQQQHQQQQQHQQQLPSPQLGVLAGPMSPPSNSLGNSWGLPSPDKTMFQPPLFSLPAHYATMQQQQQQQQQQQQQQQQQQAAGAAPSPYDDGRAAAAAAAQHAELLGLTMDCTPLLLKQPPPSYAGASAGFPGLGDLHSSHEQQLQQQQYVRSQPKYQWLDSPADYAQQQQQVQQVQQQQQQQQTLVLPGPTSSASSSNAALGVLIPKQENYPDMQPSSNGTGYSGGSGGSSAAAAAAAAAAAAAVQLAEYSPSTSKGHEILSQVYQQSTVPLKLVPVKPRKYPNRPSKTPVHERPYACPVENCDRRFSRSDELTRHIRIHTGQKPFQCRICMRSFSRSDHLTTHIRTHTGEKPFSCDICGRKFARSDEKKRHAKVHLKQRIKKEKVRGEQQQQQQQQQQQQQQQQQQQLQQQQEQHHLSLQQHQQYQQHHLLHSADLAIVTSSASM
Protein: Interleukin-37 (IL-37) (FIL1 zeta) (IL-1X) (Interleukin-1 family member 7) (IL-1F7) (Interleukin-1 homolog 4) (IL-1H) (IL-1H4) (Interleukin-1 zeta) (IL-1 zeta) (Interleukin-1-related protein) (IL-1RP1) (Q9NZH6)
Organism: Homo sapiens (Human)
Function: Immune regulatory cytokine that acts as a suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. Signaling can occur via two mechanisms, intracellularly through nuclear translocation with SMAD3 and extracellularly after secretion and binding to its receptor composed of IL18R1 and IL18RAP. Suppresses, or reduces, pro-inflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A and IL1RN, but spares anti-inflammatory cytokines. Inhibits dendritic cell activation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18390730, ECO:0000269|PubMed:20935647}. Nucleus {ECO:0000269|PubMed:18390730, ECO:0000269|PubMed:20935647, ECO:0000269|PubMed:33674380}. Secreted {ECO:0000269|PubMed:11145836, ECO:0000269|PubMed:18390730, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:33674380}. Note=Stimulation with IL1B leads to colocalization with SMAD3 mostly in perinuclear regions (PubMed:20935647, PubMed:33674380). Only the CASP1-cleaved mature form translocates into the nucleus upon LPS stimulation (PubMed:18390730). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059, PubMed:33674380). {ECO:0000269|PubMed:18390730, ECO:0000269|PubMed:20935647, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:33674380}.
Interaction partners:
- Interleukin-18 receptor 1
- Mothers against decapentaplegic homolog 3
- Interleukin-18-binding protein
- Interleukin-18
- Interleukin-18 receptor accessory protein
- Caspase-1
- Single Ig IL-1-related receptor
- Interleukin-1 beta
- Interleukin-1 alpha
- Interleukin-1 receptor type 1
Sequence:
MSFVGENSGVKMGSEDWEKDEPQCCLEDPAGSPLEPGPSLPTMNFVHTSPKVKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALASSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAAQKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFENRKHIEFSFQPVCKAEMSPSEVSD