wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase BGLF4 (EC 2.7.11.1) (P0C731)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Function: Plays many key roles by phosphorylating several proteins including the viral DNA processivity factor BMRF1, EBNA1 or EBNA2. Modifies the host nuclear envelope structure and induces the redistribution of nuclear envelope-associated proteins by phosphorylating host nucleoporins. Subsequently, promotes the nuclear transport of EBV lytic proteins. Required for efficient lytic DNA replication and release of nucleocapsids from the nucleus. Contributes to the compaction of host cell chromatin in cells undergoing lytic replication, presumably by phosphorylating the host condensin complex and host TOP2A. Induces disassembly of the nuclear lamina by phosphorylating with host LMNA. Phosphorylates substrates involved in capsid assembly and DNA packaging. Facilitates the switch from latent to lytic DNA replication by down-regulating EBNA1 replication function. Phosphorylates the viral immediate-early protein BZLF1 and inhibits its sumoylation by interacting with host SUMO1 and SUMO2. Phosphorylates also host SAMHD1 and thereby counteracts its antiviral effect by reducing its dNTP hydrolase activity.
Subcellular location: Virion tegument {ECO:0000250|UniProtKB:P13288}. Host nucleus {ECO:0000250|UniProtKB:P13288}. Note=the protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs. {ECO:0000250|UniProtKB:P13288}.
Interaction partners:
Sequence:
MDVNMAAELSPTNSSSSGELSVSPEPPRETQAFLGKVTVIDYFTFQHKHLKVTNIDDMTETLYVKLPENMTRCDHLPITCEYLLGRGSYGAVYAHADNATVKLYDSVTELYHELMVCDMIQIGKATAEDGQDKALVDYLSACTSCHALFMPQFRCSLQDYGHWHDGSIEPLVRGFQGLKDAVYFLNRHCGLFHSDISPSNILVDFTDTMWGMGRLVLTDYGTASLHDRNKMLDVRLKSSKGRQLYRLYCQREPFSIAKDTYKPLCLLSKCYILRGAGHIPDPSACGPVGAQTALRLDLQSLGYSLLYGIMHLADSTHKIPYPNPDMGFDRSDPLYFLQFAAPKVVLLEVLSQMWNLNLDMGLTSCGESPCVDVTAEHMSQFLQWCRSLKKRFKESYFFNCRPRFEHPHLPGLVAELLADDFFGPDGRRG
Protein: Formate hydrogenlyase subunit 5 (FHL subunit 5) (Hydrogenase-3 component E) (P16431)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Formate hydrogenlyase subunit 4
- Formate hydrogenlyase subunit 6
- Formate hydrogenlyase subunit 2
- Formate dehydrogenase H
- Formate hydrogenlyase subunit 3
- Formate hydrogenlyase subunit 7
- Hydrogenase 3 maturation protease
- Formate hydrogenlyase maturation protein HycH
- Hydrogenase-4 component E
- Formate hydrogenlyase regulatory protein HycA
Sequence:
MSEEKLGQHYLAALNEAFPGVVLDHAWQTKDQLTVTVKVNYLPEVVEFLYYKQGGWLSVLFGNDERKLNGHYAVYYVLSMEKGTKCWITVRVEVDANKPEYPSVTPRVPAAVWGEREVRDMYGLIPVGLPDERRLVLPDDWPDELYPLRKDSMDYRQRPAPTTDAETYEFINELGDKKNNVVPIGPLHVTSDEPGHFRLFVDGENIIDADYRLFYVHRGMEKLAETRMGYNEVTFLSDRVCGICGFAHSTAYTTSVENAMGIQVPERAQMIRAILLEVERLHSHLLNLGLACHFTGFDSGFMQFFRVRETSMKMAEILTGARKTYGLNLIGGIRRDLLKDDMIQTRQLAQQMRREVQELVDVLLSTPNMEQRTVGIGRLDPEIARDFSNVGPMVRASGHARDTRADHPFVGYGLLPMEVHSEQGCDVISRLKVRINEVYTALNMIDYGLDNLPGGPLMVEGFTYIPHRFALGFAEAPRGDDIHWSMTGDNQKLYRWRCRAATYANWPTLRYMLRGNTVSDAPLIIGSLDPCYSCTDRMTVVDVRKKKSKVVPYKELERYSIERKNSPLK
Protein: Contactin-5 (Neural recognition molecule NB-2) (P68500)
Organism: Mus musculus (Mouse)
Function: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity in the cerebral cortical neurons but not in hippocampal neurons (By similarity). Involved in neuronal activity in the auditory system.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Contactin-associated protein-like 4
- Amyloid-beta precursor protein
- Neuronal cell adhesion molecule
- Amyloid beta precursor like protein 1
- Receptor-type tyrosine-protein phosphatase gamma
Sequence:
MASCWRLILFLSVTRWLSDYSEALSGLSTSYAALLRIKKSSTSPFGSKSRPRFSSPSLGTISVSPPSWRGAAQQYHSPGNLYHSSDAFRQDESVDYGPVFVQEPDDVIFPTDSDEKKVALNCEVRGNPSPSYRWLRNGTEIALESDYRYSLIDGTFIISNPSELRDSGLYQCLATNSFGSILSREATLQFAYLGNFSGRTRSAVSVREGQGVVLMCSPPPHSPEIIYSWVFNEFPSFVAEDSRRFISQETGNLYISKVQTSDVGSYICLVKNAVTNARVLSPPTPLTLRNDGVMGEYEPKIEVHFPFTVTAAKGTTVKMECFALGNPVPTITWMKVNGYIPSKSRLRKSQAVLEIPNLQLDDAGIYECTAENSRGKNSFRGQLQIFTYPHWVQKLNDTQLDSGSPLQWECKATGKPRPTYRWLKNGAPLLPQSRVDTVNGILAIQSVNQSDAGMYQCLAENKYGAIYASAELKILASPPSFELNQVKKSIIVTKDRGVLIECEPQGSPKPAISWRKGDKAVRANKRIAILPDGSLRILNASKADEGKYICQGVNIFGSAEIIASLSVKEPTRIELTPKRTELTVGESIVLNCKAIHDASLDVTFYWTLKGQPIDFEKEGGHFENIRAQASSADLMIRNILLMHAGRYGCRVQTTADSVSDEAELLVRGPPGPPGVVIVEEITESTATLSWSPATDNHSPISSYNLQARSPFSLGWQTVKTVPEVITGDMESAMAVDLNPWVEYEFRVVATNPIGTGDPSIPSRMIRTNEAVPKTAPSNVSGRSGRRHELVIAWEPVSEEFQNGEGFGYIVAFRPNGTRGWKEKMVTSSEASKFIYRDESVPPLTPFEVKVGVYNNKGDGPFSQIVVICSAEGEPTAAPTDVTATSVSVSEIFVVWKHVKESLGRPQGFEISYWKDTEPEDSVETVRTRGNESFVMLTGLEGNTLYHLTVRAYNGAGYGPPSREASTTTKRHPPREPPGNLRWEQQGSQVSLGWEPVRPLANESEVMGYKVFYRQEGHSEGQVIETQKPQAVVPLPEAGVYIIEVRAYSEGGDGTASSQIRVPSYSGGKITSAQSTLHSLSKWSSVTLLLALMLPSSSW
Protein: Ubiquitin-NEDD8-like protein RUB2 [Cleaved into: Ubiquitin; NEDD8-like protein RUB2 (Ubiquitin-related protein 2) (AtRUB2)] (Q8RUC6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- Protein NBR1 homolog
- Cullin-1
- E3 ubiquitin-protein ligase PRT1
- RING-box protein 1a
- E3 ubiquitin-protein ligase UPL3
- Cullin-3A
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1
- COP9 signalosome complex subunit 8
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGTMIKVKTLTGKEIEIDIEPTDTIDRIKERVEEKEGIPPVQQRLIYAGKQLADDKTAKDYAIEGGSVLHLVLALRGGLL
Protein: SH3 and PX domain-containing protein 2A (Adapter protein TKS5) (Five SH3 domain-containing protein) (SH3 multiple domains protein 1) (Tyrosine kinase substrate with five SH3 domains) (Q5TCZ1)
Organism: Homo sapiens (Human)
Function: Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide.
Subcellular location: Cytoplasm. Cell projection, podosome. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.
Interaction partners:
- Actin nucleation-promoting factor WASL
- Src substrate cortactin
- Hematopoietic lineage cell-specific protein
- Growth factor receptor-bound protein 2
- Disintegrin and metalloproteinase domain-containing protein 12
- Actin nucleation-promoting factor WAS
- Disintegrin and metalloproteinase domain-containing protein 15
- Integrin beta-1
- Proto-oncogene tyrosine-protein kinase Src
- Cell division control protein 42 homolog
Sequence:
MLAYCVQDATVVDVEKRRNPSKHYVYIINVTWSDSTSQTIYRRYSKFFDLQMQLLDKFPIEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLKPIDEYCRALVRLPPHISQCDEVFRFFEARPEDVNPPKEDYGSSKRKSVWLSSWAESPKKDVTGADATAEPMILEQYVVVSNYKKQENSELSLQAGEVVDVIEKNESGWWFVSTSEEQGWVPATYLEAQNGTRDDSDINTSKTGEVSKRRKAHLRRLDRRWTLGGMVNRQHSREEKYVTVQPYTSQSKDEIGFEKGVTVEVIRKNLEGWWYIRYLGKEGWAPASYLKKAKDDLPTRKKNLAGPVEIIGNIMEISNLLNKKASGDKETPPAEGEGHEAPIAKKEISLPILCNASNGSAVGVPDRTVSRLAQGSPAVARIAPQRAQISSPNLRTRPPPRRESSLGFQLPKPPEPPSVEVEYYTIAEFQSCISDGISFRGGQKAEVIDKNSGGWWYVQIGEKEGWAPASYIDKRKKPNLSRRTSTLTRPKVPPPAPPSKPKEAEEGPTGASESQDSPRKLKYEEPEYDIPAFGFDSEPELSEEPVEDRASGERRPAQPHRPSPASSLQRARFKVGESSEDVALEEETIYENEGFRPYAEDTLSARGSSGDSDSPGSSSLSLTRKNSPKSGSPKSSSLLKLKAEKNAQAEMGKNHSSASFSSSITINTTCCSSSSSSSSSLSKTSGDLKPRSASDAGIRGTPKVRAKKDADANAGLTSCPRAKPSVRPKPFLNRAESQSQEKMDISTLRRQLRPTGQLRGGLKGSKSEDSELPPQTASEAPSEGSRRSSSDLITLPATTPPCPTKKEWEGPATSYMTCSAYQKVQDSEISFPAGVEVQVLEKQESGWWYVRFGELEGWAPSHYLVLDENEQPDPSGKELDTVPAKGRQNEGKSDSLEKIERRVQALNTVNQSKKATPPIPSKPPGGFGKTSGTPAVKMRNGVRQVAVRPQSVFVSPPPKDNNLSCALRRNESLTATDGLRGVRRNSSFSTARSAAAEAKGRLAERAASQGSDSPLLPAQRNSIPVSPVRPKPIEKSQFIHNNLKDVYVSIADYEGDEETAGFQEGVSMEVLERNPNGWWYCQILDGVKPFKGWVPSNYLEKKN
Protein: Insulin receptor substrate 2a (Zgc:56306) (Q7ZU74)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASPPLKGGPSLSNSNNIHSNNIRKHGYLKKQKHGHRRYFVLKDTSDGLPARLEYHENEKKWKNKSAPKRVIFLDSCLSINKRADAKHRYLIALYTKDEYFAVAAENEQEQESWYGDLTDLLSKGKVCDSTVSNSASSLVGFDEGNYGMITPVNAAYKEVWQVNLKAKGLGQSRNITGVFRLCLTSRTISFVKLNSEVASVTLQLMNIRRCGHSDSFFFIEVGRSASTGPGELWMQADDSVVAQNIHETILEAMKAMKELSEFRPRSKSQSSGSNPISVPTRRNLNNLPPSQTGLVRRSRTDSTAATSPVTKFSSCRIRTASEGEGTMIRPVSISVSENGSPMTVGRNHMSRSNTVSVGCRTSEPSLLNHSRSMSMTMYHSPPSVVSPLSLSSISMNGSISNKAHRPSSCSGSVSGSPNDFGFLTCEDYSSSPGDVRYNLANRSDTPSSLSSTPPLRETSELHSYMVMDRPSNFSQNKTSRDMLDVETYRKRTYSLTTPRQQMAHSQLSSASLDEYMLMRAANSHSGRSTNSASPKLSYPEDYGDIEIGSNCNVGDDGYMPMTPGMAPQSAKNDHYMPMSPMSVSAPKQIINPRSHPQSPGSGCTANSPSSGSLEDSGYMKMWSGSKFSLESSDGKAANGEYVNMSPVDTSISPTPPEYFMGPCEPTQRPSPTQSIRFNKQQVPKRVDDNQYVFMSPQNQNQAEEANSVSSLPPLYRPDVMAQRSKVNRPNRLSLDALRMLPRMTEHPLPCEPKSPGEYINIDFAAATQYSSQSMVTVENQASLSSLRQGSPLSDYMNLNQSSHSSKLCEMSSPLDGLPELAECPPDDGTCFLNEQRNLPCPSVSGKGNYTEMSFNSGSLENQKSASVSPTNRVQRLNLGNQGVSKGIGAFLLAASSVDPNGGAKVIRADPQGRRRHSSETFSSTTTVAPVFPSFAHNVKRHSSASVENISVRSSEGSDEEYESPMCQEMSAGYQNGLNYIALNLMEKQETGNCENLVGFKTGGCCKAGINGLHTTPYVCLGFKETATTVQD
Protein: Lutropin subunit beta (Lutropin beta chain) (Luteinizing hormone subunit beta) (LH-B) (LSH-B) (LSH-beta) (P45646)
Organism: Meleagris gallopavo (Wild turkey)
Function: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MGGAQVLVLMTLLGTPPVTTGTPPVVVDPSVAVVGPPLGLGGGGRPPCRPINVTVAVEKDECPQCMAVTTTACGGYCRTREPVYRSPLGRPPQSSCTYGALRYERWALWGCPIGSDPRVLLPVALSCRCARCPIATSDCTVQGLGPAFCGAPGGFGIGE
Protein: DNA repair protein Rad60 (Q9VCP1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for repair of DNA double strand breaks which occur during replication or are induced by ionizing radiation (IR). Functions with dgrn and downstream of the SMC5-SMC6 complex to regulate strand break repair. Likely functions by stabilizing the association of heterochromatic double strand breaks (DSBs) with the nuclear periphery as part of the homologous recombination (HR) repair process.
Subcellular location: Nucleus {ECO:0000269|PubMed:26502056}. Nucleus, nucleoplasm {ECO:0000269|PubMed:26502056}. Note=Associates with the nuclear pores and localizes to the nuclear periphery. {ECO:0000269|PubMed:26502056}.
Interaction partners:
- Structural maintenance of chromosomes protein 5
- Degringolade, isoform A
- Dorsal interacting protein 4
- SUMO-activating enzyme subunit
- Activator of SUMO 1
- Suppressor of variegation 2-10, isoform I
- E3 SUMO-protein ligase NSE2
- Ubiquitin-like protein NEDD8
- Ran GTPase-activating protein
- Proliferating cell nuclear antigen
Sequence:
MSDDDCDIFSAARKRIPEIALPKNPYNLGNDSFSKEVDYDFIEDLPKKSTKTGKRKNPAATRKNPPKSQDDASPPKQAEHKAVEPEEDMRTERSLSPVSLLILEMEKKNGQQSDVEKHAKENDVGPVARRTRSSLNRSEMAPPPVSPTVEVPTQTKPKKRGQKKRTSLTTTTSNSASMEVSLPSIVGQNNEHISRRWTLAEVAARSKVVDSIDLVSAVAPRVEGFVNLDSEDEGEKEAPPVVEEENIFDNDNPTIEVALSWLGEIQIYKLRQHQKFKHLFKELASRNGIDENDITVDMYYNFVGPEDTPHSIGLKSFHTLTGHPTKSHNNNNVAAKIDYNPEALCRKPKKFQVKVQADKWKHPLVIPMKKTDNFKIIFIKCAEELNCDPRTIKLFFDGDLLDPNDTPNNQDMEGNEVIDLKIKA
Protein: Protein DETOXIFICATION 42 (AtDTX42) (Aluminum-activated citrate transporter) (AtMATE) (FRD-like protein) (Multidrug and toxic compound extrusion protein 42) (MATE protein 42) (Q9SYD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Citrate transporter critical for aluminum tolerance. Responsible for citrate exudation into the rhizosphere to protect roots from aluminum toxicity.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 1
- Aluminum-activated malate transporter 1
- Protein ALUMINUM SENSITIVE 3
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 2
- Protein DETOXIFICATION 19
- MATE efflux family protein
- Protein DETOXIFICATION 20
- Protein DETOXIFICATION 48
- Protein DETOXIFICATION 35
- Protein DETOXIFICATION 30
Sequence:
MMSEDGYNTDFPRNPLYIFFSDFRSVLKFDELGLEIARIALPAALALTADPIASLVDTAFIGQIGPVELAAVGVSIALFNQVSRIAIFPLVSITTSFVAEEDACSSQQDTVRDHKECIEIGINNPTEETIELIPEKHKDSLSDEFKTSSSIFSISKPPAKKRNIPSASSALIIGGVLGLFQAVFLISAAKPLLSFMGVKHDSPMMRPSQRYLSLRSLGAPAVLLSLAAQGVFRGFKDTTTPLFATVIGDVTNIILDPIFIFVFRLGVTGAATAHVISQYLMCGILLWKLMGQVDIFNMSTKHLQFCRFMKNGFLLLMRVIAVTFCVTLSASLAAREGSTSMAAFQVCLQVWLATSLLADGYAVAGQAILASAFAKKDYKRAAATASRVLQLGLVLGFVLAVILGAGLHFGARVFTKDDKVLHLISIGLPFVAGTQPINALAFVFDGVNFGASDFGYAAASLVMVAIVSILCLLFLSSTHGFIGLWFGLTIYMSLRAAVGFWRIGTGTGPWSFLRS
Protein: FI19014p1 (Fimbrin, isoform D) (Q8IQZ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- F-actin-capping protein subunit beta
- Actin-related protein 3
- Drebrin-like protein
- Actin-related protein 2
- Profilin
- Actin-related protein 2/3 complex subunit 5
- Adenylyl cyclase-associated protein
- Survival motor neuron protein
- Actin-42A
- Actin-5C
Sequence:
MADILNVEQHQTVQEFKQNLEELIPNLDANKDGFIDLHELKDALNQVGFKLAGYQVREMIDEYKGKQLTAFQGKLNLEEFEALCLDLKSKDVASTFKTVVSKKENLETLGGMSSISSEGTTHSVRLEEQLAFSDWINSNLGHDKDLQHLLPIDSEGKRLYLSIKDGILLCKIINHSCPDTIDERAINKKNLTVYREFENLTLALVSSQAIGCNIVNIDAHDLAKGKPHLVLGLLWQIIRIGLFSHITLDSCPGLAGLLFDNERLEDLMKMSPEAILLRWVNHHLERAGISRRCTNFQSDIVDSEIYSHLLKQIAGNDADVNLDALRESDLQSRAEIMLQQAAKLNCRSFLTPQDVVNGVYKLNLAFVANLFNNHPGLDKPEQIEGLESIEETREEKTYRNWMNSMGVAPHVNWLYSDLADGLVIFQLFDVIKPGIVNWSRVHKRFSPLRKFMEKLENCNYAVDLGKQLKFSLVGIAGQDLNDGNATLTLALIWQLMRAYTLSILSRLANTGNPIIEKEIVQWVNNRLSEAGKQSQLRNFNDPAIADGKIVIDLIDAIKEGSINYELVRTSGTQEDNLANAKYAISMARKIGARVYALPEDITEVKPKMVMTVFACMMALDYVPNMDSVDQNNHNSSANNSN
Protein: Fibroblast growth factor 18 (FGF-18) (zFGF5) (O89101)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Vascular endothelial growth factor receptor 2
- Beta-klotho
- Decorin
Sequence:
MYSAPSACTCLCLHFLLLCFQVQVLAAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQAELQKPFKYTTVTKRSRRIRPTHPG
Protein: GGPP synthase (Q4W8B2)
Organism: Brevundimonas sp. NBRC 101024
Interaction partners:
Sequence:
MAIVGLRPQPVSDPEPQSPENLRGLVQDRLAETAPSSDGLLALAAREALLGPGKRVRPVVAMLAAAHVGGRAEDALDFGCAVEMAHAASLVLDDLPCMDDAALRRGQPTLHRRHGEDAAVLAAVALLNQSTRLILQSRAPSEARLGALDDLTQAIGFDGLAEGQMRDLRDDPVQRDVVALRRINDLKTGALFVAAARGGGRMGGGDADDLARLAAFGEAVGFAFQLCDDLMDACSTSEALGKDVGQDQGVTTFVDLWGEGRVRAGVRQSLARAAEAVGHDSPLTTYVLHLFRQAELGR
Protein: At5g57460 (Muniscin carboxy-terminal mu-like domain protein) (Q9FKM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AP-2 complex subunit sigma
- AP-2 complex subunit mu
- Calcium-binding EF hand family protein
- Calcium-binding EF hand family protein
- AP-2 complex subunit alpha-1
- Beta-adaptin-like protein B
- Clathrin heavy chain 1
- Calcium sensing receptor, chloroplastic
- Clathrin heavy chain 2
- Transducin/WD40 repeat-like superfamily protein
Sequence:
MSCLALALQPANGSDILLQTREWFPPARALIALSYFRQMRQALASSKQQHQQQSNQKQNQASSSSSSSSSVADPDDATAAEFVGDDPLAASNGQVIVGVESKYRVVYRLVNSIYILGVTVADHDNSINVFECIHIVNQAVSVIVTACRGVEVTPEKLGRKYAEVYMALDIVLRGVSNIRLAAMLGAMHGDGIAKMVHSALDTENKIRGADSWMAVESHAAEHQASVNAFSNARFELPPETVAAGDEFAASLAPVVPESEQLKEEPEPENKDPFAASETINKEKELVGGFKKTKDPSSTDLTLALAGLEVTTLPPAEATQSTHINVEGFEGQYGGIEFSNEQATIGETFESFSDAWGGGLDPSEFMGPKKIQKKEGLGGLELLHTSDPKAVEGKDGVNIDNLVKKPEMKGPEMYISEEIRTEFRESLLARVGVMGVIYLKTMPPKGSGEEKETEFSFRVEGTTAVKRFAMQSSRISSLGNGLFHVRTAPSEEPIPILKYSLQPKLTPLPLRVRMVKRISGTLLSLMIQYVSNPDLPQPLKNVDFILKLPVDPTLLKVSPKAILNRTDRELKWQIPEIPLNGSPGRLRARMPIDSDNSEEEPDIICYVKFSVQGNTSLSGISLRAAAEGNTDFFEVDHRYETGVYMCN
Protein: P2X purinoceptor 3 (P2X3) (ATP receptor) (Purinergic receptor) (P56373)
Organism: Homo sapiens (Human)
Function: Receptor for ATP that acts as a ligand-gated cation channel. Plays a role in sensory perception. Required for normal perception of pain. Required for normal taste perception (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:27626375}; Multi-pass membrane protein {ECO:0000269|PubMed:27626375}. Note=Localizes to neuronal cell body of sensory neurons. {ECO:0000250|UniProtKB:P49654}.
Interaction partners:
- P2X purinoceptor 6
- P2X purinoceptor 2
- P2X purinoceptor 1
- P2X purinoceptor 4
- P2X purinoceptor 5
- P2X purinoceptor 7
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2D
- Glutamate receptor ionotropic, NMDA 2C
Sequence:
MNCISDFFTYETTKSVVVKSWTIGIINRVVQLLIISYFVGWVFLHEKAYQVRDTAIESSVVTKVKGSGLYANRVMDVSDYVTPPQGTSVFVIITKMIVTENQMQGFCPESEEKYRCVSDSQCGPERLPGGGILTGRCVNYSSVLRTCEIQGWCPTEVDTVETPIMMEAENFTIFIKNSIRFPLFNFEKGNLLPNLTARDMKTCRFHPDKDPFCPILRVGDVVKFAGQDFAKLARTGGVLGIKIGWVCDLDKAWDQCIPKYSFTRLDSVSEKSSVSPGYNFRFAKYYKMENGSEYRTLLKAFGIRFDVLVYGNAGKFNIIPTIISSVAAFTSVGVGTVLCDIILLNFLKGADQYKAKKFEEVNETTLKIAALTNPVYPSDQTTAEKQSTDSGAFSIGH
Protein: Large ribosomal subunit protein eL30x (60S ribosomal protein L30-3) (Q9LSA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein uL1y
- Large ribosomal subunit protein uL3z
- Large ribosomal subunit protein uL10x
- Small ribosomal subunit protein uS2z
- Large ribosomal subunit protein uL10y
- Large ribosomal subunit protein eL32z
- Large ribosomal subunit protein eL21x/eL21w
Sequence:
MVAEKKAKKSHEGINSRLALVMKSGKYTLGYKSVLKSLRSSKGKLILISSNCPPLRRSEIEYYAMLAKVGVHRYNGNNVDLGTACGKYFRVSCLSIVDPGDSDIIKTLPGDQ
Protein: Putative E3 ubiquitin-protein ligase RING1b (EC 2.3.2.27) (Polycomb complex protein RING1b) (Protein RING1b) (AtRING1b) (RING-type E3 ubiquitin transferase RING1b) (Ring finger protein 5) (Q0WX00)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:19097900}.
Interaction partners:
- Chromo domain-containing protein LHP1
- E3 ubiquitin protein ligase DRIP2
- Probable E3 ubiquitin protein ligase DRIPH
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- Histone-lysine N-methyltransferase EZA1
- Histone-lysine N-methyltransferase CLF
- E3 ubiquitin protein ligase DRIP1
- Protein EMBRYONIC FLOWER 1
- Zinc finger, C3HC4 type
- Histone-lysine N-methyltransferase MEDEA
Sequence:
MPSLKSFSAAEEEDDQLGRNSEAERFNPEAVEKEEDPDKMDEKDESGDEEDDVKRDQVEAEDEEALGEEEDSKERSQSSSAGELSESEYMVVDLADICKDVQCSICLGIIRKTRTVMECLHRFCRECIDKSMRLGNNECPTCRKHCASRRSLRDDPNFDALIAALFKNIDKFEEEELNFRQDDEARNKQIQASIAQVSQRQSKALVKRKSVGKGTAILSRSRRSGGGSRRRRNCRNIEQDTSEANDDDDQNKRGKDSSSDEPCERQRKKRSATQPSSSNANNNDNCAGNGTEQTHQRDSRVISPVLVWNSELIAWGRGGTRSNTRQGNNNQGAISKRNARLKRLVEYLGSLEGNSVELDIHLKLVSLDTEGLLNLHEPYLCFRPTLLVKQLREYVARHLKLKAEEVELLVSKDGDTVIGNKTSTEKMQSLQDDETVAKLKVDCISSNGYMIVVYRRKQIA
Protein: Uncharacterized protein (G5EB24)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- Carnitine acetyl transferase FacC
Sequence:
MSAAESPASDAVQETVKAAETKAVNQTAAQIRSFAAGGVGGVCAVIVGHPFDLVKVRMQTAAQGVYSGAIDVVKKTVAREGLVRGLYAGVSAPLVGVTPMFAVSFWGYDLGKTLVSNLSEVEVKNNTPQYSIAQVSAAGFFSAIPMTLITAPFERVKVLLQIQGQNPPPPGQKPKYSGGVDVVRQLYKEGGIRSVFRGSAMTLARDGPGSAAYFAAYEYIKRSLTPKDANGNATGDLSLPAVLAAGGAAGIAMWIPVFPVDTVKSRLQSAPGKPTISGTIRTVYAAGGFKAFFPGFGPALARAVPANAATFAGVELAHQFMNKLFD
Protein: Alpha-crystallin B chain (Alpha(B)-crystallin) (P23928)
Organism: Rattus norvegicus (Rat)
Function: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus {ECO:0000250|UniProtKB:P02511}. Secreted {ECO:0000250|UniProtKB:P02511}. Lysosome {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Localizes at the Z-bands and the intercalated disk in cardiomyocytes. Can be secreted; 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. {ECO:0000250|UniProtKB:P02511}.
Interaction partners:
- Alpha-crystallin A chain
- Heat shock protein beta-1
- Caspase-3
- Beta-crystallin B2
- Gamma-crystallin S
- Gamma-crystallin D
- Beta-crystallin A3
- Bcl2-associated athanogene 3.
- DnaJ heat shock protein family
- Heat shock protein HSP 90-beta
Sequence:
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEMRMEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK
Protein: Serine/threonine-protein kinase PKH3 (EC 2.7.11.1) (Pkb-activating kinase homolog 3) (Q03306)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine-protein kinase which may phosphorylate the same targets substrates as PKH1 and PKH2, 2 upstream activators of PKC1.
Interaction partners:
- Protein kinase C-like 1
- Serine/threonine-protein kinase PKH2
- Serine/threonine-protein kinase PKH1
Sequence:
MTSRKRSPHDFIFKEELGHGSYSTVFKALDKKSPNKIYAIKVCSKKHIIKEAKVKYVTIEKNTMNLLAQKHHAGIIKLYYTFHDEENLYFVLDFAPGGELLSLLHKMGTFNDIWTRHFTAQLIDALEFIHSHGIIHRDLKPENVLLDRDGRLMITDFGAAATIDPSLSGDSAKFNSDSNGSKDNQNCASFVGTAEYVSPELLLYNQCGYGSDIWALGCMIYQFVQGQPPFRGENELKTFEKIVALDYPWGPNNRINNSTSPINPLVINLVQKILVIEVNERISLEQIKRHPYFSKVDWNDKIKIWRGIWQSQGQSLQQTTLGLPNIPQNILPTRQLHVIDTPARSIQITKQKRKKPTKISNTTSSIVVWRKRLGISTGKDDLGTVPSTTPAVTAPNDTNVLTNTAAHSTANIALPPNSQSNQVKRAQLVAPNRIPPKVPVINDNVRNKSIPRTKPNVPPLQTSSIPQKLSTSSASSALSAPSTEIRNQDLTHTLDGRNSIDIHVLKQDYVFIYGIPYEHEGPAMSLNSYNKIDNDLITSLVAQHKEELKNSESFLQVLTLKKSGMLSYKNTVMEGNDDQENKEHQMANIEDTDLSMYDFEFNELTRKGFLILEKYKNRIWFISLPSYSTLSKIPFNAVKSSTINNNENWVDCFFRARQLLEEKQILDKISNVSFDSKASSEPSSPPPISRKERPLSIGNNVTTLSYTAKNGSQNNAPQNDNVGEEKPFRIPSSTKDRPGANSTPSSRHPRVLSSNNAGETPKKMNGRLPNSAPSTNTYTNGSVPAFNHRPSTNVGNNKHNILTSKKQGSSVFSPSSSTTKPQIKTTGYRQPTPSPPLPQMEFPTTREKYSAPSNMVISSSRYEVLHTLNNSQTNFDREIASRGASAAFRSLQKSKKKK