wanglab/gogpt-training-data huggingface dataset:
Protein: L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2) (EC 1.4.3.25) (Interleukin-4-induced protein 1) (IL4-induced protein 1) (hIL4I1) (Protein Fig-1) (hFIG1) (Q96RQ9)
Organism: Homo sapiens (Human)
Function: Secreted L-amino-acid oxidase that acts as a key immunoregulator. Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively. Also has weak L-arginine oxidase activity. Acts as a negative regulator of anti-tumor immunity by mediating Trp degradation via an indole pyruvate pathway that activates the transcription factor AHR. IL4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites (indole-3-acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer. AHR activation by indoles following IL4I1-mediated Trp degradation enhances tumor progression by promoting cancer cell motility and suppressing adaptive immunity. Also has an immunoregulatory function in some immune cells, probably by mediating Trp degradation and promoting downstream AHR activation: inhibits T-cell activation and proliferation, promotes the differentiation of naive CD4(+) T-cells into FOXP3(+) regulatory T-cells (Treg) and regulates the development and function of B-cells. Also regulates M2 macrophage polarization by inhibiting T-cell activation (By similarity). Also has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4(+) and H2O2.
Subcellular location: Secreted {ECO:0000269|PubMed:17356132, ECO:0000269|PubMed:28891065, ECO:0000269|PubMed:32818467}. Lysosome {ECO:0000250|UniProtKB:O09046}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:25767141}. Note=Secreted at the immunological synapse. {ECO:0000269|PubMed:28891065}.
Interaction partners:
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Indoleamine 2,3-dioxygenase 1
- Tryptophan 2,3-dioxygenase
- Aspartate aminotransferase, mitochondrial
- Branched-chain-amino-acid aminotransferase, cytosolic
- Omega-amidase NIT2
- Indoleamine 2,3-dioxygenase 2
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Tyrosine aminotransferase
Sequence:
MAPLALHLLVLVPILLSLVASQDWKAERSQDPFEKCMQDPDYEQLLKVVTWGLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLGLNLTKFTQYDKNTWTEVHEVKLRNYVVEKVPEKLGYALRPQEKGHSPEDIYQMALNQALKDLKALGCRKAMKKFERHTLLEYLLGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVVAMTQGPHDVHVQIETSPPARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEHIEGGHSNTDRPSRMIFYPPPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLWDGTGVVKRWAEDQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYPHGWVETAVKSALRAAIKINSRKGPASDTASPEGHASDMEGQGHVHGVASSPSHDLAKEEGSHPPVQGQLSLQNTTHTRTSH
Protein: Mitochondrial association factor 1 form b1 (MAF1RHb1 allele) (MAF1b) (A0A140H546)
Organism: Toxoplasma gondii
Function: During host cell infection by tachyzoites, required for tethering the parasitophorous vacuole to the host mitochondria. This process, known as host mitochondrial association (HMA), induces the formation of SPOTs (structures positive for outer mitochondrial membrane (OMM)), a cellular response to OMM stress, which leads to the constitutive shedding of OMM vesicles containing proteins such as mitofusins MFN1 and MFN2, which normally restrict parasite growth. Specifically, binds to the host OMM import receptor TOMM70 to interact with SAMM50, a component of host mitochondrial intermembrane space bridging (MIB) complex. By targeting SAMM50, induces the disassembly of the MIB complex, thereby promoting the formation of SPOTs. Inhibits host TOMM70 import activity. Plays a role in the modulation of the host innate immune response to parasite infection.
Subcellular location: Parasitophorous vacuole membrane {ECO:0000269|PubMed:24781109, ECO:0000269|PubMed:26920761, ECO:0000269|PubMed:28567444}; Single-pass type I membrane protein {ECO:0000305|PubMed:24781109}. Cytoplasmic granule membrane {ECO:0000269|PubMed:24781109}; Single-pass type I membrane protein {ECO:0000305|PubMed:24781109}. Note=Localizes to dense granules (PubMed:24781109). Localizes at the interface between the parasitophorous vacuole and the host outer mitochondrial membrane (PubMed:24781109, PubMed:26920761). {ECO:0000269|PubMed:24781109, ECO:0000269|PubMed:26920761}.
Interaction partners:
Sequence:
MWRIWRCRLSFLFATGCLLGALTAGLGSQMSDSVGRNVQAPAGVADASQEAGDVVEERTERTEEQAFALGPPRRHSSESLFPRNASVTARRRRNRRIALIATAVGVAVILAAVYVLRRRRAQRPQDPEPPAPRSVEDPEVLPEEDEASSSLPPPPPPSPPPPPPVEDPLSPESQTVDLSCLSGTTVRFFGPSHHFGGFTPLYDPAPDKRVATVDAGANALFIGGGGLNGQFAKTLLEEAEKHGIRLTPEELSQHSQRIQQSLLRRAVKSPGKLVELDTGVASPVFARSFGFVPVVPGLMWEESEVGPNVGVTFVHILKPEVTPYGNLNNNVMMYTVAPSGAAPDKTYSLAYKTTIAGVIGAAAAYNDTPAGQQYPVQGLRLPLLGGGIFRRNRSLESIGRANAEGTSLAITRYGPNFELQYMYDPSNAALHGLQEAESTYLASMLD
Protein: Envelope glycoprotein L (gL) (F5HCH8)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH (By similarity). In human cytomegalovirus, forms two distincts complexes to mediate viral entry, a trimer and a pentamer at the surface of the virion envelope. The gH-gL-gO trimer is required for infection in fibroblasts by interacting with host PDGFRA. The gH-gL-UL128-UL130-UL131A pentamer is essential for viral entry in epithelial, endothelial and myeloid cells via interaction with host NRP2.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04036}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04036}; Extracellular side {ECO:0000255|HAMAP-Rule:MF_04036}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04036}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04036}; Extracellular side {ECO:0000255|HAMAP-Rule:MF_04036}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04036}. Note=gL associates with the extravirion surface through its binding to gH. During virion morphogenesis, this protein probably accumulates in the host trans-Golgi where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04036}.
Interaction partners:
Sequence:
MCRRPDCGFSFSPGPVILLWCCLLLPIVSSAAVSVAPTAAEKVPAECPELTRRCLLGEVFEGDKYESWLRPLVNVTGRDGPLSQLIRYRPVTPEAANSVLLDEAFLDTLALLYNNPDQLRALLTLLSSDTAPRWMTVMRGYSECGDGSPAVYTCVDDLCRGYDLTRLSYGRSIFTEHVLGFELVPPSLFNVVVAIRNEATRTNRAVRLPVSTAAAPEGITLFYGLYNAVKEFCLRHQLDPPLLRHLDKYYAGLPPELKQTRVNLPAHSRYGPQAVDAR
Protein: Bromodomain adjacent to zinc finger domain protein 2 (Q23590)
Organism: Caenorhabditis elegans
Function: Chromatin reader protein, involved in positively modulating the rate of age-related behavioral deterioration. Positively modulates the level of global trimethylated 'Lys-9' of histone H3 (H3K9me3), but not of H3K9me2 or H3K9me1. May repress the expression of mitochondrial function-related genes by occupying their promoter regions, working in concert with histone methyltransferase, set-6. Involved in modulation of the mitochondrial unfolded protein response (UPR). Negatively regulates expression of bas-1, a serotonin (5-HT) and dopamine synthesizing enzyme (DOPA decarboxylase), with aging. Negatively modulates levels of endogenous 5-HT and dopamine with aging. Involved in modulating longevity, probably as a result of enhanced stress resistance via mechanisms related to dietary restriction and mitochondrial function.
Subcellular location: Nucleus {ECO:0000269|PubMed:32103178}. Chromosome {ECO:0000269|PubMed:32103178}.
Interaction partners:
- Chromatin-remodeling complex ATPase chain isw-1
- DNA polymerase epsilon subunit 3
- Tyrosine-protein kinase receptor ver-4
- Protein ver-1
Sequence:
MSDNSSNQFLLLLAAAQQQQQQQLLQQQLAKIQKATASSPSKSTNGTSASTSAVPSTSGTSSSQNEAAQLQNLAKMQQIQQLAQFGALMAAQKKQQEKAAADKAKEKEKEKQKAAAAAAAAAAKASASTSSASAIPGLSPEMLAAWQQAIQMQALQQMMMTPQKSQMEEAIKKMMDMAKKKPAGVASTSSASTSSSTPSTSSASITSSNNNAANNAASNMMNNVMWQLVAAQMQQKQQQQQKDTQKKADQAKKAKELAKQQQKEQDVKNKQQEEILKFLMAQHQLNHQKKHEKKQADAAALAAKVLAAHRAALESDSPEEGKKTNEAMLRLPLQLGWRRQTCVRSIASAGVKGDVSYFAPCGKKLSTYSEVVRYLTKNSIHYITRDNFLFNTKLVIGEFIVPKQTEADETQQEREFAMFTEDDINKELTRLNVLKFVPKIQASTSNGVHEDDIKMSKIEEPDEPLDPSELNDEFTEELVHSQIMSNGVDECKIREREADDLLVNINDVRHLPDFSRIGNQCLSSQGFADALMVHEFVQNFGHVLGIDLEIAPKLESLCAGLDGDANHAEQTLQLTRQLLRLALEFPGMGNEKRFGQGGGEMGLDRENFSEVMRLFLIDKGKRGEELSQPLLTCNFLSISPEQKASILAFLCDELVCSRNVVTEIDKNLDEISRLKGEKWMREGKARALRSARSKKKNDEKVVVVKEEQNHESDSEPPTRPDTPKKATVAPPTVVSVSPVSAAQQQQRKFTPGLGQCEVLTEQEESMSLQQMDSLIGDLHQEAQNINQKIHDTGLKIRSFPFGTDRFHRNYWMLAHTDKVIIESLATTSVNNPACNANEYASKDPPTLEQRVPGACETIDLDVIACVEDLVDDVVLLRAKADKKTRKRYRRIENHMKRGWWTMQNRDCVESLRSCMLSRGIRERALHRLLTKPWFLNELKFGTITIEPVGEKSDLELVRRQGWTRLNTAIDKLQCHLKMSDVSKPLPSITPFETQKPIVVPPTMALAQIVKDDMAWKVIDEEVDGQELDETIIRQKIIETADMVQPKFWRPKFQKLEDQDTCQLFEDWKSYVSTEAQTTSQLMVALQTLEGMIMWERSSREALCQICKSMDGDEMLVCDGCESGCHMECFRPRMTKVPEGDWFCQRCREEKSGRPMCMFCSRETGNLHQCQRCAYHVHQECSQDGPKEAINPETFICGHCQEMKQMRFVKRLILRSESEERELEDDNHAENGENTKNGHMNGMNGAIAIGVHNQQNGVKGNLKRKLEVPSIGGLPKNMNKELCQLMLDELVVQANALPFLEPVNPKLVPGYKMIISKPMDLKTIRQKNEKLIYETPEDFAEDIELMFANCRQFNIDHSEIGRAGISLHKFFQKRWKQLKYNFTKRLRRLHR
Protein: Signal-regulatory protein beta-1 (SIRP-beta-1) (CD172 antigen-like family member B) (CD antigen CD172b) (O00241)
Organism: Homo sapiens (Human)
Function: Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK. Triggers activation of myeloid cells when associated with TYROBP.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10604985}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Leukocyte surface antigen CD47
- Tyrosine-protein phosphatase non-receptor type substrate 1
- Ig-like domain-containing protein
- High affinity immunoglobulin epsilon receptor subunit gamma
- Tyrosine-protein phosphatase non-receptor type 11
Sequence:
MPVPASWPHLPSPFLLMTLLLGRLTGVAGEDELQVIQPEKSVSVAAGESATLRCAMTSLIPVGPIMWFRGAGAGRELIYNQKEGHFPRVTTVSELTKRNNLDFSISISNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAVRATPEHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPAGDSVSYSIHSTARVVLTRGDVHSQVICEIAHITLQGDPLRGTANLSEAIRVPPTLEVTQQPMRAENQANVTCQVSNFYPRGLQLTWLENGNVSRTETASTLIENKDGTYNWMSWLLVNTCAHRDDVVLTCQVEHDGQQAVSKSYALEISAHQKEHGSDITHEAALAPTAPLLVALLLGPKLLLVVGVSAIYICWKQKA
Protein: HER-1 protein (Hairy-related 1) (Q90463)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVTPKMASRRPTKRILKPVIEKKRRDRINQRLEELRTLLLDNTLDSRLQNPKLEKAEILELAVEYIRTKTATARDQGDSSKDTHDPKPPPLLSRRPQMPCASIPESIQTHNSPSNPIYKAGFKECISRSASFIDCVEPSQRDSFVQGLCHHLDSYSSALPHGRVSSNPTHHPWIPNPELSCRTDVQSIGHMRANPEPYSYANSLYPKSFMHLHPTGQHPYLSPPYSISPPPSPGFSSSSPPFSSSPTYLSVPCQFPFPPSISPHSTDSSSSSTLSTVSLSTTSLPVVPGPHLQVSSPTRVRFSGSVQSSQPRTLRRALFHNQPLWRPW
Protein: Uncharacterized protein (Q381L5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSFRIPNNLLQVLADYTSQALGAAHDISDEFEEDINELDCQAKRICVILRIIRESAHRQSSAEGGNATLGGCESPKPIEVALRGLGHLIHEFTGLPDIGSAPMGREGQRRELTVQPLGKPVSLAEAALELFGHNTKIIFRRKDKRPRDAAIVEGKTERRGTVYSRLATSQRKRRFALYTARVALFPDVFHTPTLSQEGGEGEMRPFVSPAVREFADLNVEAEREMFGSFYRLDTKAELLREWPSLFSTVEHLQGLLRAEGVRFIPSEAMKRENLEGQLRWFEFPFTDNGVVRMIVKHVLAVDFTWELLQSGRWRVLGLHWLLKTRPPPAFLLPLGSGGCEDTSNLWKEKASSLRATTLRVEPAYYEAALRFLTNCFETGLEGGAVGALRLADAVTMEVIETQCRELKENFFVGPLEPSFALDVRPGTHVSLALNWPHNSSFYSTTAPLNEEGGGPLYLKYKLRNGTVVFEKRRGTDTQAAVQSDFYTDCLTIDDGQSVVVVDIERQLWQFICA
Protein: Uncharacterized protein C56F8.15 (Q10263)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein C56F8.13
- Amino-acid permease 1
- Uncharacterized protein C887.16
- Uncharacterized protein C18B11.08c
- Pyridoxal phosphate homeostasis protein
- Putative uncharacterized transmembrane protein SPBC713.13.
- Uncharacterized protein SPBC713.14c
- Telobox protein 1
- Uncharacterized protein C1565.03
- Uncharacterized protein C13E7.11
Sequence:
MFFFLVFSACEVFVGFSLCTLVISVPFFFLQMTPFYSILCFLSFFALLLHLPCSIYSHTLHFFHHFTIACYHYSLCLSLVALLLFYTLYPFQSITLPLMPFLEKTESSILTISHVYSPPTIITFDGFKRLLRMHVPFYTLSFDTFSTHTNFFPRHTFPIFIARVSLHFVKQLSLSI
Protein: Multiple epidermal growth factor-like domains protein 6 (Multiple EGF-like domains protein 6) (Epidermal growth factor-like protein 3) (EGF-like protein 3) (Q80V70)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Microfibrillar-associated protein 5
Sequence:
MPVGVEARASWRVVALTLLLLPAVPAASQPLPPRPLQPSMPHVCAEQKLTLVGHRQPCVQAFSRVVPVWRSGCGQQAWCVGQERRTVYYMSYRQVYATEARTVFRCCPGWSQKPGQEGCLSDVDECANANGGCEGPCCNTVGGFYCRCPPGYQLQGDGKTCQDVDECRSHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRTCLAISSCTLGNGGCQHQCVQLTVTQHRCQCRPQYQLQEDGRRCVRRSPCADGNGGCMHTCQELRGLAHCGCHPGYQLAADRKACEDVDECALGLAQCAHGCLNTQGSFKCVCHAGYELGADGRQCYRIEMEIVNSCEAGNGGCSHGCSHTSTGPLCTCPRGYELDEDQKTCIDIDDCANSPCCQQVCANTPGGYECSCFAGYRLNTDGCGCEDVDECASGHSGCEHHCSNLAGSFQCFCEAGYRLDEDRRGCTPLEESVVDLDGQLPFVRPLPHIAVLGDELPQLFQDDYGAEEEAVAELRGEHTLTEKFVCLDHSFGHDCSLTCDDCRNGGTCFPGLDGCDCPEGWTGIICNETCPPDTFGKNCSSPCICQNGGTCDPVSGACRCPPGVSGAHCEDGCPKGFYGKHCRKKCHCANRGRCHRLYGACLCDPGLYGRFCHLACPPWAFGPGCSEDCLCEQSHTRSCNSKDGSCSCKAGFQGERCEAECEPGSFGPGCRNRCTCRPGVACDPVSGECRTQCPPGYQGEDCGQECPVGTFGVNCSGSCSCVGAPCHRVTGECLCPPGKTGEDCGADCPEGRWGLGCQEICPACEHGASCDPETGTCLCLPGFVGSRCQDACPAGWFGTGCQMRCACANDGHCHPATGRCSCAPGWTGLSCQRACDSGHWGPDCIHPCNCSAGHGNCDAVSGLCLCEAGYEGPQCEQWCRQGYFGPGCEQKCRCEHGATCDHVSGACTCPAGWRGSFCEHACPAGFFGLDCGSACNCSAGAPCDAVTGSCICPAGRWGPHCAQTCPPLTFGLNCSQICTCFNGASCDPVLGQCHCAPGWMGPTCLQACPAGLYGKNCQHSCLCRNGGSCDPILGQCTCPEGWTGLACENECLPGHHGAGCRLNCSCLNGGTCDRLTGHCRCPAGWTGDKCQSPCVSGMFGVHCEEHCACRKGATCHHVTGACLCPPGWRGSHCEQACPRGWFGEACAQRCHCPPGASCHHVSGECHCPPGFTGPGCEQACQPGTFGKDCEHPCQCPGETWACHPASGACVCAAGYHGTDCQQRCPSGRYGPGCEQICKCLNGGTCDPATGACYCPAGFLGADCSLACPQGRFGPSCAHVCTCGQGAACDPVSGTCICPPGKTGGHCERGCPQDRFGKGCEHKCACRNGGLCHATNGSCSCPLGWMGPHCEHACPAGRYGAACLLECSCQNNGSCEPTSGACLCGPGFYGQACEDTCPAGFHGSGCQRVCECQQGAPCDPVSGRCLCPAGFRGQFCERGCKPGFFGDGCLQQCNSPTGVPCDPISGLCLCPPGRAGTTCDLDCRRGRFGPGCALRCDCGGGADCDPISGQCHCVDSYTGPTCREVPTQLSSIRPAPQHSSSKAMKH
Protein: RE36140p (Stepping stone) (Q9VUK7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MIP16918p
- ADP-ribosylation factor-like protein 11
Sequence:
MQLKAPKSRNMASLKDEDQAATTSNSMHNLNNNNNTNNINNNHSSSSNNNKIEDDPKVRKENLEARKQALEQRLSEKSWLLQQIQKQETAIINGNYEHMTVNEFFVQLAQQYKHEQQLQALARENSSILRRKQSTTSRESRDSQMTINNNNRQSETLSNRSSEYDNYQPSSSAGAGDMLVIGVAQQQAQQQPPLVKSALKKRPTPTPSQMQYMRQQHQQQAHLAMNMNYQRSQPDVISMYSANSSNVATLRQPPQVAPQQQPIIVQCDKYYLSPTHQSYNEGGFIKSSQNIKKYVSPMASPSNISYEQQQQRNPLHHQRQLDAISLAPSYVSVDMEAAQHQQQYRWRSQSHIAPLTPPQLGIIEVKSHSSDMLAVPMPPSRYPPHDEISLSSSSTTIEKKPKPKQWLESSLDGPAVIRQMDSQPHSPAGSSNGSSNPGAAAMVSSKPRAKLSSQSMSVAGRHYSMSNQRPTPNYPSASYAVNTSSKALLSQSTSYLNAMEQTLGISVSYPLEPLDIPALRNLPPKPSQMQQPTPPPRPPPANQAHTQNQNLSHSGNGSSSGLAHGNAVQTALVSPPVTVATASLSPEIRIESPKNMTVVQQATFQPYKEVTKPFEMSDFYKYSTKFKQKEGGNPN
Protein: Disks large homolog 5 N-terminal domain-containing protein (Q8C2V6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
GESSGKDASVSAPTTGQLHFMRNCICNIRHHVTAADLNRKTTEASKNLKMLEEEIGFYRNLHSQLRMAQAKLKNKVNMLKQENRRIWGRCATLQQNLEELKMIYKNQLEDTSDPQTQQQQDPERTEELLQDSHKQKKLGIQEKNLAEKQQYYFEVRRKSCFLTELNQLKKKLEMLSQENKEMQGDCALLQHHVEDLKPIYKKQQEEDSDLQTQHQKHMERMEEKLQYMLKKKNMAIKQRELAEKLKYQFEVLQMRFDKLQQEMELAIAQEERVLQKDLLHQEPPAEPHPQKPQDPLGGFALT
Protein: (+)-3-carene synthase 1, chloroplastic (EC 4.2.3.107) (Terpene synthase TPS-Far/Oci) (PgxeTPS-Car1) (F2XF94)
Organism: Picea engelmannii x Picea glauca (Hybrid white spruce)
Function: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (+)-car-3-ene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSVISIVPLVSKPCLYKSFISSTHEPKALRRPISTVGLCRRAKSVTASMSMSSSTALSDDGVQRRIGNHHSNLWDDNFIQSLSSPYGASSYAERAERLIGEVKEIFNRISMANGELVSHVDDLLQHLSMVDNVERLGIDRHFQTEIKVSLDYVYSYWSEKGIGPGRDIVCADLNTTALGFRVLRLHGYTVFPDVFEQFKDQMGRIACSANQTERQISSILNLFRASLIAFPWEKVMEEAEIFSTAYLKEALQTIPVSSLSREIQYVLDYRWHSDLPRLETRTYIDILRENATNETLDMKTEKLLELAKVEFNIFNSLQQNELKCVSRWWKESGSPDLTFIRHRQVEFYTLVSGIDMEPKRSTFRINFVKICHFVTILDDMYDTFGTMDELRLFTAAVKRWDKSATECLPEYMKGVYIDLYETVNELAREAYKSQGRDTLNYARQALEDYLGSYLKEAEWISTGYIPTFEEYLENGKVSSAHRIATLQPILMLDVPFPPHVLQEIDFPSKFNDLAGSILRLRGDTRCYQNDRARGEEASCISCYMKDNPGSTEKEALNHINGMIEKRIKELNWELLKPDKNVPISSKKHAFNISRGLHHFYKYRDGYTVANSETRNLVIKTVLEPVPM
Protein: ATP-dependent helicase fft1 (EC 3.6.4.12) (Fun thirty-related protein 1) (P87114)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for heterochromatin organization.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKRKDNKELICIPSSSPPSTPIREENYYLLTSSPIECSPIQQLDLSGSFKNYSTTSSRANGKKFGQLAMQSRIFFDTTDHKKYVESSYAAYDPHDQPPERDVSLKESSNKINPSNFFDSEQITKINAVKKRFPALDSEMIIATLEKFNWRENITIHKLTFQKLLGRGNSTINKSAQKLNNQPIEKSSVDKENAKRKRYVEEGTKQGQKKKPLRVIELSDEETNEDDLLGQSPTACTTDANIDNSIPENSDKIEEVSIESSGPSEVEDEMSEYDVRVLNFLNESTLQEIVEVSGCESKVVEYFISKRPFPSLEKAEALCQRNAHAATGKRKKSDGRNVGRKLVNSTYEVLQGFDAVDSLIAKCERYGAMISNTMRSWHNLFDDKKMEQFLNTSTGSISYEYNSQQPSSIASGITLKSYQIVGLNWLCLMYKAKLSGILADEMGLGKTCQVISFLASLKEKGIQNRHLVVVPSSTLGNWLREFEKFCPSLRVESYSGTQSERINKRYYLMDTDFDVLVTTYQLASGSRDDRSFLRKQRFDISIFDEGHYLKNRMSERYKHLMNIPANFRLLITGTPLQNNLKELISLLAFMLPKVFDNNMQGLDIIYKIKTTSDGDIERAYLSQERISRAKTIMNPFILRRRKENVLSDLPPKIQHVEYCHMEETQLSLYLSVLELKNLVNANRENILMQLRKAALHQLLFRSQYNLETLSLMSKRILREDAYLDANPQYIFEDMEVMSDFELHKLADQYRHLHPFALKGKPWMDSAKVKKLCSLLKKSRPNERILIFSQFTQVLDILEYVLNTLDLEFLRLDGSTPVETRQQLIDDFHTNENYKVFLLSTKSGGFGINLTCANIVILFDCSFNPFDDMQAEDRAHRVGQTRPVHVYRLITKNTIEENIRRLANTKLTLESSLTTDSEKIQKEISGELMKSLQMDGRVDTMDGSVV
Protein: Microtubule-associated protein (A0A0B4LHS3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU000686}.
Interaction partners:
Sequence:
MADVLEKSSLLDAVPPLGDPHPPLPHQQLQQEAAAAAAANAAPPAPPQQQQPPPHQLQQQQPQQQQLQQKPANARANQDQKEGDNDSGVDESTQEKDRNGPNSPSSPVKTPTSTSSKPDKSGTSRPPSATPSNKSAPKSRSASKNRLLLKTPEPEPVKKVPMNKVQVGHAPSPNLKAVRSKIGSLDNATYKPGGGHVKIESKKIDIKAAPRIEAKNDKYMPKGGEKKIVTTKLQWNAKSKIGSLENAAHKPGGGDKKIETLKMDFKDKAKPKVGSTANVKHQPGGGDIKYWKAPRIQRATTLTSSMSLPAECLVLSVSMPSLNSEPKRPKSAGPKKKPGQAVHSKPFRLY
Protein: Transducin family protein / WD-40 repeat family protein (Q9LVF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Uncharacterized protein At3g06530
- Bystin
- Protein TORMOZ EMBRYO DEFECTIVE
- rRNA biogenesis protein RRP5
- Nucleolar protein
- F18K10.11 protein
- Protein SLOW WALKER 1
- rRNA processing protein-like protein
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
Sequence:
MVKAYQRYDAATSFGVISSVDSNIAYDSTGKYVLAPALEKVGIWHVRQGVCSKTLTPSSSRGGPSLAVTSIASSASSLVAVGYADGSIRIWDTEKGTCEVNFNSHKGAVTALRYNKVGSMLASGSKDNDIILWDVVGESGLFRLRGHRDQVTDLVFLDGGKKLVSSSKDKFLRVWDLETQHCMQIVSGHHSEVWSVDTDPEERYVVTGSADQELRFYAVKEYSSNGSLVSDSNANEIKASEEHSTENKWEILKLFGEIQRQTKDRVARVRFNVSGKLLACQMAGKTIEIFRVLDEAEAKQKAKRRLRRKEKKSSKVGDENSTANGEASAKIELADAVSSPTVLDVFKLLQVIRAGRKISSFSFCPTAPKESLGTLALSLNNNSLEFYSLKSSENAKTVTIEHQGHRSDVRSVTLSEDNTLLMSTSHSEVKIWNPSTGSCLRTIDSGYGLCSLIVPQNKYGIVGTKSGVLEIIDIGSATKVEEVKAHGGTIWSITPIPNDSGFVTVSADHEVKFWEYQVKQKSGKATKKLTVSNVKSMKMNDDVLAVAISPDAKHIAVALLDSTVKVFYMDSLKFYLSLYGHKLPVMCIDISSDGELIVTGSQDKNLKIWGLDFGDCHKSIFAHGDSVMGVKFVRNTHYLFSIGKDRLVKYWDADKFEHLLTLEGHHAEIWCLAISNRGDFLVTGSHDRSMRRWDRSEEPFFLEEEKEKRLEELFESEIDNAADDRHGPMEEIPEEGVAALAGKKTIDVLSAADSIIDALEVAEDETKRHAAYEEEKTKGKVPEYLPNAVMFGLSPSEYVLRAISNVRTNDLEQTLLALPFSDSLKFLCYMKDWSLIPEKVELVSRIATIILQTHHNQLVTTPSARPILSVLRDILYSEIKACKDTIGFNLAAMDHVKQMMDARSDAPFKDAKAKLLEIRSQQAKRMASRGDTKMEKKRKKKQKKLEEGQHGHALF
Protein: Putative ATP synthase subunit f, mitochondrial (Q9W141)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000250}.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase subunit O, mitochondrial
- ATP synthase subunit g
- ATP synthase subunit b, mitochondrial
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit alpha, mitochondrial
- ATP synthase-coupling factor 6, mitochondrial
- Protein stunted
Sequence:
MAFGDYPAEYNPKVHGPYDPARFYGKADVPFGQVKLGEIGAWLGRRNKTPNAVAGAVSRAWWRWQHKYVFPKRAGIAPFFQLTVASMTFFYLINYTKLKHHRNYKYH
Protein: Nucleoprotein (Protein N) (Nucleocapsid protein) (P03418)
Organism: Human respiratory syncytial virus A (strain A2)
Function: Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases. RNA replication depends on the availability of soluble nucleoprotein. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Together with the phosphoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway. May also act as a modulator of the innate immune response by sequestration of host IFIH1/MDA5 and MAVS into IBs.
Subcellular location: Virion {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:17703289, ECO:0000269|PubMed:32878896}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000269|PubMed:17703289, ECO:0000269|PubMed:32878896}.
Interaction partners:
Sequence:
MALSKVKLNDTLNKDQLLSSSKYTIQRSTGDSIDTPNYDVQKHINKLCGMLLITEDANHKFTGLIGMLYAMSRLGREDTIKILRDAGYHVKANGVDVTTHRQDINGKEMKFEVLTLASLTTEIQINIEIESRKSYKKMLKEMGEVAPEYRHDSPDCGMIILCIAALVITKLAAGDRSGLTAVIRRANNVLKNEMKRYKGLLPKDIANSFYEVFEKHPHFIDVFVHFGIAQSSTRGGSRVEGIFAGLFMNAYGAGQVMLRWGVLAKSVKNIMLGHASVQAEMEQVVEVYEYAQKLGGEAGFYHILNNPKASLLSLTQFPHFSSVVLGNAAGLGIMGEYRGTPRNQDLYDAAKAYAEQLKENGVINYSVLDLTAEELEAIKHQLNPKDNDVEL
Protein: Zinc finger protein 705D (P0CH99)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MHSLEKVTFEDVAIDFTQEEWDMMDTSKRKLYRDVMLENISHLVSLGYQISKSYIILQLEQGKELWREGRVFLQDQNPDRESALKKKHMISMHPIIRKDASTSMTMENSLILEDPFEYNDSGEDCTHSSTITQCLLTHSGKKPCVSKQCGKSLRNLLSPKPRKQIHTKGKSYQCNLCEKAYTNCFYLRRHKMTHTGERPYACHLCGKAFTQCSHLRRHEKTHTGERPYKCHQCGKAFIQSFNLRRHERTHLGQKCYECDKSGKAFSQSSGFRGNKIIHIGEKPHACLLCGKAFSLSSDLR
Protein: Tumor protein D53 (hD53) (Tumor protein D52-like 1) (Q16890)
Organism: Homo sapiens (Human)
Interaction partners:
- Tumor protein D52
- Tumor protein D54
- Tumor protein D55
Sequence:
MEAQAQGLLETEPLQGTDEDAVASADFSSMLSEEEKEELKAELVQLEDEITTLRQVLSAKERHLVEIKQKLGMNLMNELKQNFSKSWHDMQTTTAYKKTHETLSHAGQKATAAFSNVGTAISKKFGDMSYSIRHSISMPAMRNSPTFKSFEERVETTVTSLKTKVGGTNPNGGSFEEVLSSTAHASAQSLAGGSRRTKEEELQC