wanglab/gogpt-training-data huggingface dataset:
Protein: Histone H2A type 1-B/E (Histone H2A.2) (Histone H2A/a) (Histone H2A/m) (P04908)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H4
- Histone H2B type 2-E
- Histone H3.1
- Histone H2B type 1-J
- Histone H2B type 1-B
- Histone H3-like centromeric protein A
- Histone H2B type 1-K
- Histone H3.2
- Histone H3.1t
- Histone H3.3
Sequence:
MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
Protein: LD23375p (RE72238p) (Zinc transporter 86D) (Q9VGS1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Zinc transporter ZIP11
- IP18018p
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Protein catecholamines up
- FI23527p1
- RE15841p
- Zinc/iron regulated transporter-related protein 42C.2
- Zinc/iron regulated transporter-related protein 102B, isoform E
- Zinc transporter ZIP13 homolog
- FI18611p1
Sequence:
MIPLSHKDRSSLGYRIREKLNSWKRLIFSDRNSRNLFLFLLLNLSFAFVELFYGIVTNSLGLISDSFHMFFDCTGLLAGLAASVITKWKANDKFSYGYVRAEVLAGFVNSLFLLFIAFFILSEGVERLIEPPEVKHERLFVVSVLGLLVNLVGIYAFNHGGHGHSHGGHGHSHGGGHGHGHSHGHTDAGNHNHQAITLDNGHGHSHDHDSHGHSHGDMSGSNSQIMRGVFLHILADTLGSVGVIISAVLMHMFGWMIADPICSIFIALLIALSVLSLIKESIMILMQRQPADLDRSLPQCYQKVTGLAGVYAVQEPHFWTLCSDVYVGALKLEVSKNVDPKYVVTHTRMIFEAVGVKQIYIQLDYV
Protein: ATP-dependent RecD2 DNA helicase (EC 5.6.2.3) (DNA 5'-3' helicase RecD2) (Q9RT63)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Function: DNA-dependent ATPase (ssDNA better than dsDNA) and ATP-dependent 5'-3' DNA helicase. Appears to move along DNA in single base steps, powered by hydrolysis of 1 molecule of ATP. Has low processivity; short (20 bp) substrates with 5'-overhangs or forked ends are the best substrates, is much less efficient on 52 or 76 bp substrates with 5'- overhangs. The presence of single-stranded DNA-binding protein (SSB) increases unwinding 4-5 fold. Has no activity on blunt DNA or DNA with 3'-overhangs. Requires at least 10 bases of 5'-ssDNA for helicase activity.
Interaction partners:
- Beta sliding clamp
- Protein RecA
Sequence:
MSAALPAEPFRVSGGVNKVRFRSDTGFTVMSATLRNEQGEDPDATVIGVMPPLDVGDTFSAEVLMEEHREYGYQYRVVNMVLEAMPADLSEEGVAAYFEARVGGVGKVLAGRIAKTFGAAAFDLLEDDPQKFLQVPGITESTLHKMVSSWSQQGLERRLLAGLQGLGLTINQAQRAVKHFGADALDRLEKDLFTLTEVEGIGFLTADKLWQARGGALDDPRRLTAAAVYALQLAGTQAGHSFLPRSRAEKGVVHYTRVTPGQARLAVETAVELGRLSEDDSPLFAAEAAATGEGRIYLPHVLRAEKKLASLIRTLLATPPADGAGNDDWAVPKKARKGLSEEQASVLDQLAGHRLVVLTGGPGTGKSTTTKAVADLAESLGLEVGLCAPTGKAARRLGEVTGRTASTVHRLLGYGPQGFRHNHLEPAPYDLLIVDEVSMMGDALMLSLLAAVPPGARVLLVGDTDQLPPVDAGLPLLALAQAAPTIKLTQVYRQAAKNPIIQAAHGLLHGEAPAWGDKRLNLTEIEPDGGARRVALMVRELGGPGAVQVLTPMRKGPLGMDHLNYHLQALFNPGEGGVRIAEGEARPGDTVVQTKNDYNNEIFNGTLGMVLKAEGARLTVDFDGNVVELTGAELFNLQLGYALTVHRAQGSEWGTVLGVLHEAHMPMLSRNLVYTALTRARDRFFSAGSASAWQIAAARQREARNTALLERIRAH
Protein: Potassium channel subfamily K member 4 (TWIK-related arachidonic acid-stimulated potassium channel protein) (TRAAK) (G3V8V5)
Organism: Rattus norvegicus (Rat)
Function: Voltage-insensitive potassium channel. Channel opening is triggered by mechanical forces that deform the membrane, and by raising the intracellular pH to basic levels. The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius. Plays a role in the perception of pain caused by heat (By similarity). Plays a role in the sensory perception of pain caused by pressure (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11374070}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:31630908}. Note=Localizes at the Ranvier nodes of myelinated afferent nerves. {ECO:0000269|PubMed:31630908}.
Interaction partners:
- Potassium channel subfamily K member 12
- Potassium channel subfamily K member 13
- Calcium-activated potassium channel subunit alpha-1
- Transient receptor potential cation channel subfamily M member 8
- Potassium channel subfamily K member 9 channel 3)
- Piezo-type mechanosensitive ion channel component 1
Sequence:
MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQVQKDLEDGRDQFLKDHPCVSQKNLEGFIKLVAEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIALHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAVFLKWHVPPGLVRMLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVAEPAHRPGSPAPAEKVETPPPTASALDYPSENLAFIDESSDTQSERGCALPRAPRGRRRPNPTKKPSRPRGPGRLRDKAVPV
Protein: ATP-dependent RNA helicase SUB2 (EC 3.6.4.13) (Q6FL17)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: ATP-binding RNA helicase involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome A complete sequence
- THO complex subunit 2
- RNA helicase
- Pre-mRNA-splicing factor CWC22
- Candida glabrata strain CBS138 chromosome J complete sequence
- Pre-mRNA-splicing factor SLU7
- Candida glabrata strain CBS138 chromosome K complete sequence
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor SYF2
- Candida glabrata strain CBS138 chromosome J complete sequence
Sequence:
MSHEGEEDLLEYSDNEQEIQVDNKETAVEGTTENEATQENGEADKKGSYVGIHSTGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVSVVVICNARELAYQIRNEYLRFSKYMPDVRTAVFYGGTPIAKDAELLKNKDTAPHIVVATPGRLKALVRDKMIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEEREKNRKLAQLLDDLEFNQVIIFVKSTSRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDLLNEADQYLHRVGRAGRFGTKGLAISFVSNKEDEEVLSKIQERFDVKIAEFPEEGIDPSTYLNN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8LDB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MQIFSCFCCGKGFDRQKKVKTEPSWRIFSLKELHAATNSFNYDNKLGEGRFGSVYWGQLWDGSQIAVKRLKAWSSREEIDFAVEVEILARIRHKNLLSVRGYCAEGQERLIVYDYMPNLSLVSHLHGQHSSESLLDWTRRMNIAVSSAQAIAYLHHFATPRIVHGDVRASNVLLDSEFEARVTDFGYDKLMPDDGANKSTKGNNIGYLSPECIESGKESDMGDVYSFGVLLLELVTGKRPTERVNLTTKRGITEWVLPLVYERKFGEIVDQRLNGKYVEEELKRIVLVGLMCAQRESEKRPTMSEVVEMLMIESKEKMAQLEANPLFNGNNDGEVIDESSEIISEVRDHQ
Protein: Serine/threonine protein phosphatase 2A regulatory subunit (Q0KI58)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDNEALDPTIKSSTSAATPTAAASETTTTAASSVVETTTTIAAATASAAESKNETTATNNNSNTSGSISSSSSNNIVIPASATNGIKESNSNLSTTTTAAAVAAATTVEGVAPAITSTIVVTGGTPPLSSLANKLKDNTPPYDAPPPTPISKVLNITGTPIVRKEKRQTSARYNASKNCELTALIPLNEKTAASEREELFIQKIQQCCTLFDFSEPLSDLKFKEVKRAALHEMVDFLTNQNGVITEVIYPEAINMFAVNLFRTLPPSSNPNGAEFDPEEDEPTLESSWPHLQLVYELFLRFLESPDFQPSMAKRFIDHQFVLQLLDLFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNVFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKQFLLKVLLPLHKAKSLSVYHPQLTYCVVQFLEKDPSLSEAVIKSLLKFWPKTHSPKEVMFLNELEELLDVIEPAEFQKVMVPLFRQIAKCVSSPHFQVAERALYYWNNEYIMSLITDNSAVILPIMFPALNRNSKTHWNKTIHGLIYNALKLFMEIDQRLFDECSKNYKQEKQMEREKLSQREELWQQVESLAKTNPEWTKARRFNDCLPVSDSRALCDQYSENSDSAYDQSEQRARQPPPPLPPQKQAHQEPREVRQALATLTTLNNY
Protein: Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase) (P03958)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity). Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ T-cell differentiation and proliferation (By similarity). Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (By similarity). Stimulates plasminogen activation (By similarity). Plays a role in male fertility (By similarity). Plays a protective role in early postimplantation embryonic development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P00813}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:8783262}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:P00813}. Note=Colocalized with DPP4 at the cell surface. {ECO:0000250|UniProtKB:P00813}.
Interaction partners:
- Dipeptidyl peptidase 4
- Adenosine kinase
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- 5'-nucleotidase
- Deoxycytidine kinase
- Double-stranded RNA-specific adenosine deaminase
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- Cytosolic purine 5'-nucleotidase
- Cytosolic 5'-nucleotidase 3A
Sequence:
MAQTPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSLEVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNINAAKSSFLPEEEKKELLERLYREYQ
Protein: Myb family transcription factor APL (AtAPL) (Protein ALTERED PHLOEM DEVELOPMENT) (Protein FE) (Protein PHOSPHATE STARVATION RESPONSE 2) (AtPHR2) (Protein PHR1-LIKE 14) (Protein WOODY) (Q9SAK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor required for phloem identity. Has a dual role both in promoting phloem differentiation and in repressing xylem differentiation during vascular development. Regulates the expression of the transcription factor NAC045 (AC A4VCM0). May activate the transcription of specific genes involved in phosphate uptake or assimilation. Promotes flowering through transcriptional activation of both FT and its transport machinery component, FTIP1.
Subcellular location: Nucleus {ECO:0000269|PubMed:14614507}.
Interaction partners:
- Ac-like transposase
- HAT family dimerization domain-containing protein
- Protein NEN2
- Protein NEN1
- Trihelix transcription factor GT-2
Sequence:
MFHAKKPSSMNGSYENRAMCVQGDSGLVLTTDPKPRLRWTVELHERFVDAVAQLGGPDKATPKTIMRVMGVKGLTLYHLKSHLQKFRLGKQPHKEYGDHSTKEGSRASAMDIQRNVASSSGMMSRNMNEMQMEVQRRLHEQLEVQRHLQLRIEAQGKYMQSILERACQTLAGENMAAATAAAAVGGGYKGNLGSSSLSAAVGPPPHPLSFPPFQDLNIYGNTTDQVLDHHNFHHQNIENHFTGNNAADTNIYLGKKRPNPNFGNDVRKGLLMWSDQDHDLSANQSIDDEHRIQIQMATHVSTDLDSLSEIYERKSGLSGDEGNNGGKLLERPSPRRSPLSPMMNPNGGLIQGRNSPFG
Protein: CTD kinase subunit alpha (CTDK-I subunit alpha) (EC 2.7.11.23) (CTD kinase 58 kDa subunit) (CTD kinase subunit 1) (Q03957)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and through PTI1, pre-mRNA 3'-end processing. Participates in both positive and negative regulation of CTD phosphorylation. Required for DNA damage induced transcription, including the expression of the RNR genes, and reprogramming of gene expression upon amino acid starvation. Required for SET2 mediated H3K36 methylation. Also regulates H3K4 methylation. Controls the maintenance of suppressive chromatin in the coding regions of genes by both promoting H3K36 methylation, which leads to histone deacetylation, and catalyzing phosphorylation of the CTD required to localize H3K4 chromatin modification specifically to the 5' ends of genes, thereby creating a boundary for H3K4 methylation that prevents a mark associated with transcriptional initiation from spreading into the bodies of genes. Involved in RNA polymerase I transcription. Involved in telomere maintenance. Acts together with SNF1 to induce GSY2 transcription in response to glucose limitation. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus. Functions in translation elongation by enhancing decoding fidelity. Needed for translational accuracy by phosphorylating RPS2.
Subcellular location: Nucleus, nucleolus. Cytoplasm.
Interaction partners:
- CTD kinase subunit gamma
- CTD kinase subunit beta
- DNA-directed RNA polymerase II subunit RPB1
- Protein BUR2
- Transcription elongation factor SPT5
- Serine/threonine-protein kinase KIN28
- RNA polymerase II holoenzyme cyclin-like subunit
- Cyclin CCL1
- Cell division control protein 73
- RNA polymerase-associated protein RTF1
Sequence:
MSYNNGNTYSKSYSRNNKRPLFGKRSPNPQSLARPPPPKRIRTDSGYQSNMDNISSHRVNSNDQPGHTKSRGNNNLSRYNDTSFQTSSRYQGSRYNNNNTSYENRPKSIKRDETKAEFLSHLPKGPKSVEKSRYNNSSNTSNDIKNGYHASKYYNHKGQEGRSVIAKKVPVSVLTQQRSTSVYLRIMQVGEGTYGKVYKAKNTNTEKLVALKKLRLQGEREGFPITSIREIKLLQSFDHPNVSTIKEIMVESQKTVYMIFEYADNDLSGLLLNKEVQISHSQCKHLFKQLLLGMEYLHDNKILHRDVKGSNILIDNQGNLKITDFGLARKMNSRADYTNRVITLWYRPPELLLGTTNYGTEVDMWGCGCLLVELFNKTAIFQGSNELEQIESIFKIMGTPTINSWPTLYDMPWFFMIMPQQTTKYVNNFSEKFKSVLPSSKCLQLAINLLCYDQTKRFSATEALQSDYFKEEPKPEPLVLDGLVSCHEYEVKLARKQKRPNILSTNTNNKGNGNSNNNNNNNNDDDDK
Protein: 4'-phosphopantetheinyl transferase B, mitochondrial (PPTase B) (EC 2.7.8.7) (Acyl-carrier-protein synthase pptB) (Phosphopantetheine:protein transferase pptB) (Q4W9R0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Acyl-carrier-protein synthase transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi-domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). PptB is specific for the mitochondrial acyl carrier protein acpA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21195204}.
Interaction partners:
- Dephospho-CoA kinase, putative
- 4'-phosphopantetheinyl transferase A
Sequence:
MKLIPFPYPLNIGTDVVHLPRILRLINRPDYFHRFTRRILHEQEQRDFRTRFSLPPPSSGAEKTGLNPITPDMARWLAGRFAAKEAARKAAPAGASSLGWKDVIVRVGEADKGRPEIVYLDPMGCGETGGGRVGKLSISHDGDYVVATVLAAG
Protein: Snake venom metalloproteinase BleucMP (SVMP) (EC 3.4.24.-) (P0DJJ6)
Organism: Bothrops leucurus (Whitetail lancehead)
Function: Snake venom zinc metalloprotease that has fibrino(geno)lytic activities. Hydrolyzes the alpha-chain (FGA) and more slowly the beta-chain of fibrinogen (FGB), without affecting the gamma-chain. Preferentially hydrolyzes the beta-chain (FGB) of fibrin. In vivo, shows a low edema-inducing effect. This action may be attributed to degradation of proteins in the cell membrane and consequent release of inflammatory mediators and leukocyte infiltrate.
Subcellular location: Secreted.
Interaction partners:
Sequence:
TLTSFGEWR
Protein: Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3E (Semaphorin-3E precursor) (Q1LYS1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Plexin D1.
- Neuropilin-1a
- Plexin-A4
- Plexin A3
- Plexin-A2
- Plexin A1a.
- Plexin-B1
- Vascular endothelial growth factor receptor kdr-like
- Plexin C1
- Neuropilin 1b.
Sequence:
MAWGVWTFTLCLVFWISSATQSTKSVYPRLRLSHKELWELNRTWVFQAGEGRLQQYTMLLDETQERLIIGGKDVLYSLNLERITAPHKRIVWSSSQEQVEDCLMQGREKPECANYIKLVQHYNSTHLLACGTGAFSPVCAYIRVSRGAEQEREFRLESDHIESGRGRVPFHPNSPLASTVYRGELFVGLYTDYWENDAALYRLGNHSFIRTEVGDRQQLNEPKFVGSAVIPDNDDPADDKVYYFFTERVADVEGGNKAVYTRVARVCANDQGGQRMLVNRWSSFLKTRLICSVAGPNGIDTHFDELEDVFVLRKKDEKNPEIFGLFSTTSAVFKGYAVCMYNMDDIRAAFNGPFAHRERTDHHWKVYDGKVPYPRPGSCASKINGGHFSSSKEYSDEVLRFARSHPLMFQAVQPVHRRPILLDTEGGRKLTQLAVDRVEAEDGHYNVLFIGTDNSVVLKMITIYNKEADTVEEVLLEELQVFKVPVPITEILISTKRQQLYVGSELGVTQIRVHQCGLYGSACADCCLARDPYCAWDGFTCSRYYPAGLYTKRRFRRQDVRHGNAVQQCNGLQLSEEQSISEKLVYGVENNSTLLECRPRSLQASVTWYIEHGLDMEEVKSDDRMIQTPHGLLLLRIMKSDAGVYVCQSTEHGFIQTLLRVTLEVLEEGKVEALLHKPEEEDSDLPHRAAPPCSFPSLPSTSSKLWYKDFMQLIGYSNFQRVEQYCEKVWCVADRKRKKLKGMTPKWRLTAGGEQRARARAPRHTPGQ
Protein: Toll-like receptor 12 (Toll-like receptor 11) (Q6QNU9)
Organism: Mus musculus (Mouse)
Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Plays a role in preventing infection of internal organs of the urogenital system.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Profilin-3
- Profilin-4
- Profilin
- Profilin-2
- Profilin-1
- Toll-like receptor 11
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 3
Sequence:
MGRYWLLPGLLLSLPLVTGWSTSNCLVTEGSRLPLVSRYFTFCRHSKLSFLAACLSVSNLTQTLEVVPRTVEGLCLGGTVSTLLPDAFSAFPGLKVLALSLHLTQLLPGALRGLGQLQSLSFFDSPLRRSLFLPPDAFSDLISLQRLHISGPCLDKKAGIRLPPGLQWLGVTLSCIQDVGELAGMFPDLVQGSSSRVSWTLQKLDLSSNWKLKMASPGSLQGLQVEILDLTRTPLDAVWLKGLGLQKLDVLYAQTATAELAAEAVAHFELQGLIVKESKIGSISQEALASCHSLKTLGLSSTGLTKLPPGFLTAMPRLQRLELSGNQLQSAVLCMNETGDVSGLTTLDLSGNRLRILPPAAFSCLPHLRELLLRYNQLLSLEGYLFQELQQLETLKLDGNPLLHLGKNWLAALPALTTLSLLDTQIRMSPEPGFWGAKNLHTLSLKLPALPAPAVLFLPMYLTSLELHIASGTTEHWTLSPAIFPSLETLTISGGGLKLKLGSQNASGVFPALQKLSLLKNSLDAFCSQGTSNLFLWQLPKLQSLRVWGAGNSSRPCLITGLPSLRELKLASLQSITQPRSVQLEELVGDLPQLQALVLSSTGLKSLSAAAFQRLHSLQVLVLEYEKDLMLQDSLREYSPQMPHYIYILESNLACHCANAWMEPWVKRSTKTYIYIRDNRLCPGQDRLSARGSLPSFLWDHCPQTLELKLFLASSALVFMLIALPLLQEARNSWIPYLQALFRVWLQGLRGKGDKGKRFLFDVFVSHCRQDQGWVIEELLPALEGFLPAGLGLRLCLPERDFEPGKDVVDNVVDSMLSSRTTLCVLSGQALCNPRCRLELRLATSLLLAAPSPPVLLLVFLEPISRHQLPGYHRLARLLRRGDYCLWPEEEERKSGFWTWLRSRLG
Protein: Ferric reductase transmembrane component 5 (EC 1.16.1.9) (Ferric-chelate reductase 5) (Q08908)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable ferric reductase transmembrane component 8
- Facilitator of iron transport 3
- Facilitator of iron transport 2
- Iron-regulated transcriptional activator AFT1
- ATP-dependent RNA helicase SUB2
- Uncharacterized protein YOR385W
- Siderophore iron transporter ARN2
- Siderophore iron transporter ENB1
- Siderophore iron transporter 1
- Siderophore iron transporter ARN1
Sequence:
MLFARLVLLLVYLAPGSLAKPASTKKRTQWDQIAIDACAKELESHKFDTDVKGRHATLCTYEPALGSWLHCAKDVLDSRKKSKKIFEKTFSKINQYCHDYHKDEVVSNEEYYRIFANASLFIRPLDEVKENIRYPVTPNKASLDRWVWAYFGPLDNIDKGNVYGVTICLYWIGVLFIAAVYHFLNFSRLKQTVFKNKVSAFLRGHYVLPALVHNHAMSVGRWFFIGLVPTRLETLVLFGYVLLHGFLLSSYNFDHNELLSDRRSQVLIFLSDRAGILAFAHFPLIVLFGGKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAIGYTYHAYIENYWKYVKYSDLWTSGRHAMIIVGILVFFSFFFFRRHYYELFVITHIILAIGFFHACWKHCYKLGWGEWIMACALFWIADRILRLIKIAIFGMPWAKLKLCGESMIEVRISKSSKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDSLVEDGELVVVITVKNGLTKKLQEYLLESEGYTEMRVLAEGPYGQSTRTHLFESLLFIAGGAGVPGPLSMAIKAGRQVKSNDSHQMIKFVWSVRNLDLLEVYRKEIMVLKELNIDTKIYFTGERKDESNTEEGAIANMSTEGRLLTTSKSAEMITDFGRPNIDEIIEEAVSGAKSLLVTCCGSEGFVDKTRELTAKRVLEHGDKWIEYVEEFQNW
Protein: Uncharacterized protein, isoform L (H9XVM9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Bent, isoform F
- Uncharacterized protein, isoform A
- Myosin light chain alkali
- RE68558p
Sequence:
MDSTLNIENVNDPTSIASDLSAENTKADLVSLNEPKTYEPTTIAPDLKMENTKNSIPSPIKPNVNDQTSSASDLTAENTKADHDSLNKPKDFNNQILNIISDIDINIKAQEKITQLKEQELKLIQKQNDLANEIHKQQILAKQLSAQNQLKQNECQSGELDLHSQYQNERGGPTSTLYQEKNIASKQIPVVHNNMNCTVEKKRGYRPSDLIDPSKRQYLLSLSKKLWQEKKESANVSKTVDLRKIFTPATDAAEILPKNRKLYASSAFYSPTLHPTVEDQVELARRISHSLSDISNQTSKGQSMYVNRKKRSDKWVHEGGSQGNDAINPFKENSETKSTMEVAKLEKIPLKLIMNPNGKVRDYNSLKDLINVEAGLLSPDNCAELITALQLHQGRGAELFAKRRRKADNWVVDESHSGTQYHPSGIPDFQQYQQRPVLSPNILPAYSDAGKHRVQLNIHQNQLIEKYSKPGLQVVQSPWKAALQTGSASSAFLEDTKSFSPPALTPIPSSQAGSKDWTDANEPMPHGSSRRNTNAVASSPRSVIVPSNPQRDLAYTPCVAQGWGGRSVELPKDSFQSNESQSSWQTEPHIGRADDSNPSFNNYIFGERLTSNFAFDVQNRLHSLENFQKYFLEYQRLELEILRNRESSRVLQHDAYESLLDFTPQNEFKVISGEDLKVNCDLDEKVNVRELIQSFEKQNTTDLRHDAAPIEGLYVPKEISLSSYAAPSQQCEIHSKHFERPYEDTFPRTFPRNNYSANNNFPGNDGIGEFPLSKPTGLTTGTLHQQPYSPTSYKKTVPGLEKVENFARYEQPDRKRLTSGSPQYLNALQNSQVRNASPIPFGTSLNEQTSWPPRSVLLQGGSPSPLPNHVQTFNKCAKGWGSIPVKQQSYSSQYNLPGNLPYSDF
Protein: Mucolipin TRP cation channel 1 (A0A8I6AQ69)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}.
Interaction partners:
Sequence:
ELVEAGWRGETEQLLTPNPGYGTQAGTSPAPTTPPEEEDLRRRLKYFFMSPCDKFRAKGRKPCKLMLQVVKILVVTVQLILFGLSNQLVVTFREENTIAFRHLFLLGYSDGSDDTFAAYTREQLYQAIFYAVDQYLTLPEISLGRYAYVRGGGGPWANGSALALCQRYYHRGHVDPANDTFDIDPRVVTDCIQVDPPDRPPDIPSEDLDFLDGSTSYKNITLKFHKLINVTIHFQLKTINLQSLINNEIPDCYTFSILITFDNKAHSGRIPIRLETQTHIQECKHPSVSRHGDNSFRLLFDVVVILTCSLSFLLCARSLLRGFLLQNEFVVFMWRRRGREISLWERLEFVNGWYILLVTSDVLTISGTIMKIGIEAKNLASYDVCSILLGTSTLLVWVGVIRYLTFFHKYNILIATLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQAQQGRSSLVWLFSQLYLYSFISLFIYMVLSLFIALITGAYDTIKHPGGTGTEKSELQAYIEQCQDSPTSGKFRRGSGSTCSLLCCCGRNSPEDHSLLVN