wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 536 (Q8K083)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor that negatively regulates neuron differentiation by repressing retinoic acid-induced gene transcription. Binds and interrupts RARA from binding to retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. Recognizes and binds 2 copies of the core DNA sequence 5'-CCCCCA-3' (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19398580}.
Interaction partners:
Sequence:
MEEASLCLGVSSTAPEAEPHLSGPVLNGQYAMSQKLHQITSQLSHAFPELHPRPNPEEKTPAALEEKAHVPMSGQSMGSQMALLANQLGRDVDNSLNGRVDLQQFLNGQNLGIMSQMSDIEDDARKNRKYPCPLCGKRFRFNSILSLHMRTHTGEKPFKCPYCDHRAAQKGNLKIHLRTHKLGNLGKGRGRVREENRLLHELEERAILRDKQMKGSLLQPRSDLKPLAHAQQAPLATCNLALPPNHSVPDVAHPAPSPKPANLQEDSVTPAAGFRCTFCKGKFKKREELDRHIRILHKPYKCTLCDFAASQEEELISHVEKAHITAESAQGQGPNGGGEQSANEFRCEVCGQVFSQAWFLKGHMRKHKDSFEHCCQICGRRFKEPWFLKNHMKVHLNKLSVKNKSPTEPEVAVPMGGLSQEAHANLYSRYLSCLQSGFMAPDKASLNEPSQLYGKGELPAKEKEVLGKLLSPISSMAHSVPEGDKHSLLGCLNLVPPLKSSCIERLQAAAKAAEMDPVNSYQAWQLMARGMAMEHGFLSKEHQLSRNHEDPLANTGVLFDKEKREYVLVGADGSKQKMPADLVHSTKVGNQRDLPNKLDPLEGSREFLSHGLNQTLDYNLQGPGNMKEKPTECPDCGRVFRTYHQVVVHSRVHKRDRKSDEDALHVGVGLEERRGSGSDQESQSVSRSTTPGSSNVTEESGAGGGLSQTGSAQEDSPHPSSPSSSDIGEEAGRAGGVQQQALLRDRNLGSAMKDCPYCGKTFRTSHHLKVHLRIHTGEKPYKCPHCDYAGTQSASLKYHLERHHRERQNGAGPLSGQPPNQEHKDETSSKAPMFIRPDILRGAFKGLPGIDFRGGPASQQWTAGMLSSGDHSGQATGMPSELSSDALKGSDLPSKSSHYSEIGRAYQNIVSNGVNFQGSLQAFMDSFVLSSLKKKDTKDKVPSDAHPMKAHTAEGGEEKASMKPSQRKSEKSQYEPLDLSVRPDAPTLPGSSVTVQDSIAWHGCLFCAFTTSSMELMALHLQANHLGRAKRKDHPTGVTVNCKEQGREASKVSVLPSLQSNKEMALPSAVGVLDSAPEKLAQGPAKETLGDPKSGQWPNHMDPAFCTFPSDFYKQFGVYPAMVGSGAPGSCLNKNTEGKTHPDDDAPILIPETTNKNTTDDLSDIASSEDMDSSKGENNEDEELDTEPEMTSKPLSALSKDGSSEGGDSLLSPGAPQPIQGLVSPLAQAAEEQWHSPGLLPAQDPSAGLPKPERGPPGLEKPMSMLSVLRAYSADGLAAFNGLASSTANSGCIKRPDLCGKF
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial (H7C1Y7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|PIRNR:PIRNR000543}.
Interaction partners:
Sequence:
MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQDKFEVLNYTSIPIFLPEVTIGAHQTDRVLHQFREVFQESEAKRLDVEEVCWKKTPLKDRGEEV
Protein: Diacylglycerol kinase zeta (DAG kinase zeta) (EC 2.7.1.107) (EC 2.7.1.93) (Diglyceride kinase zeta) (DGK-zeta) (Q13574)
Organism: Homo sapiens (Human)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids (Probable). Does not exhibit an acyl chain-dependent substrate specificity among diacylglycerol species. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro but less efficiently and with a preference for alkylacylglycerols containing an arachidonoyl group. The biological processes it is involved in include T cell activation since it negatively regulates T-cell receptor signaling which is in part mediated by diacylglycerol (By similarity). By generating phosphatidic acid, stimulates PIP5KIA activity which regulates actin polymerization. Through the same mechanism could also positively regulate insulin-induced translocation of SLC2A4 to the cell membrane (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11257115, ECO:0000269|PubMed:15157668, ECO:0000269|PubMed:9159104, ECO:0000269|PubMed:9716136}. Cytoplasm, cytosol {ECO:0000269|PubMed:11257115, ECO:0000269|PubMed:22627129}. Cell membrane {ECO:0000269|PubMed:11257115}. Cell projection, lamellipodium {ECO:0000269|PubMed:15157668}.
Interaction partners:
- Sorting nexin-27
- Lipoprotein lipase
- Myristoylated alanine-rich C-kinase substrate
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Dihydroxyacetone phosphate acyltransferase
- Disks large homolog 4
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Phospholipase D2
- Beta-arrestin-1
- Serine/threonine-protein phosphatase 6 regulatory subunit 1
Sequence:
MEPRDGSPEARSSDSESASASSSGSERDAGPEPDKAPRRLNKRRFPGLRLFGHRKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCYVGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSPLMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIPRYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTTSKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRVSMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKLSPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLPTSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
Protein: Large ribosomal subunit protein mL54 (39S ribosomal protein L54, mitochondrial) (L54mt) (MRP-L54) (Q3MHJ5)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11551941}.
Interaction partners:
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL2m
- Small ribosomal subunit protein mS22
- Large ribosomal subunit protein mL46
- Uncharacterized protein.
- Large ribosomal subunit protein uL10m
- Large ribosomal subunit protein uL14m
- Large ribosomal subunit protein mL62
- Small ribosomal subunit protein uS9m
- MRPL41 protein
Sequence:
MAARRLFGATGSWARWRAWELPDPAGSVRLHVRDYAKRPVFKGGKGAKGAAVGETLKDPEVCTDPVQLTTHPMGVNIYKEGQDVVLKPDSEYPEWLFQMNVGPPKKLEELDPETREYWRLLRKHNIWRHNRLSKNQKF
Protein: XO lethal protein 1 (Q23229)
Organism: Caenorhabditis elegans
Function: Sex-determining factor that is required for sexual differentiation and X chromosome dosage compensation to promote male development. High expression during gastrulation triggers male development, while low expression at that time triggers hermaphrodite development. Although related to GHMP kinase, its mode of action remains unclear.
Subcellular location: Nucleus {ECO:0000269|PubMed:7813020}.
Interaction partners:
- Steroid hormone receptor family member cnr14
- Sex determination protein fox-1
- Protein her-1
- T-box transcription factor 18
- Homeobox protein ceh-39
- Sex determination and dosage compensation protein sdc-2
- Sex-determining transformer protein 2
- RNA-binding protein ASD-1
- Lysine-specific demethylase 9
- Chromosome condensation protein dpy-27
Sequence:
MQVEANSERRVKILGIDRSENSPVLTYMETEDDPNFRNSKLAAAPHTVHMMDSGFLAINRQCLVKGKAILAREPKSSNEHMIDDLPKHAHDQHTLSILRDFIDQLKLHNVYEINFYDPLDSSGKLAVIPMLIALWKCMLASETDICDQEVLKSIMNSVIAKFELQIPCKNAVIDATLSGSREEVHIIAEDGSLENSNGTTEHFNKKHDLVFVKTDLHPEDFTPQMFPSQAKAKLLRDAFNNEEDEDTFPDILVPAYMTAHSKNRVRQEDYTCLEVEFDSQVALEKLMNEHEQVEGFEVQQGGILVALKKDSFFDDELIEKIAIAIATESRQSVSSVSFDLLKLGPGASLVTLANSRRFEPECRVVLQIEVKPVSPGETSSEGISDEHHYEEYDEDDIMEEEEAPSARQDDTYDEDEE
Protein: AP2/ERF and B3 domain-containing transcription repressor TEM1 (Protein TEMPRANILLO 1) (RAV1-like ethylene-responsive transcription factor TEM1) (Q9C6M5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional repressor of flowering time on long day plants. Acts directly on FT expression by binding 5'-CAACA-3' and 5'-CACCTG-3 sequences. Functionally redundant with TEM2.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein GIGANTEA
- MADS-box protein SOC1
- Cyclic dof factor 1
- Protein SENSITIVITY TO RED LIGHT REDUCED 1
- Adagio protein 3
- Adagio protein 1
- Inactive protein FRIGIDA
- Gibberellin 3-beta-dioxygenase 2
- BZIP transcription factor, putative
- Agamous-like MADS-box protein AGL8
Sequence:
MEYSCVDDSSTTSESLSISTTPKPTTTTEKKLSSPPATSMRLYRMGSGGSSVVLDSENGVETESRKLPSSKYKGVVPQPNGRWGAQIYEKHQRVWLGTFNEEEEAASSYDIAVRRFRGRDAVTNFKSQVDGNDAESAFLDAHSKAEIVDMLRKHTYADEFEQSRRKFVNGDGKRSGLETATYGNDAVLRAREVLFEKTVTPSDVGKLNRLVIPKQHAEKHFPLPAMTTAMGMNPSPTKGVLINLEDRTGKVWRFRYSYWNSSQSYVLTKGWSRFVKEKNLRAGDVVCFERSTGPDRQLYIHWKVRSSPVQTVVRLFGVNIFNVSNEKPNDVAVECVGKKRSREDDLFSLGCSKKQAIINIL
Protein: Monocopper oxidase-like protein SKS2 (Q9FHN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Probable BOI-related E3 ubiquitin-protein ligase 2
- E3 ubiquitin-protein ligase BOI
Sequence:
MAATDFFFAFVFSFALIFGFSFAGDPYVSYDFTLSYITASPLGVPQQVIAVNGKFPGPVINATTNYNVHVNVLNHLDEPLLLTWPGVQMRRNSWQDGVLGTNCPIPPNWNFTYDFQLKDQIGSYFYSPSLNFQRASGGFGALIINNRDLVPIPFTEPDGEIIFIIGDWYTQNHTALRRILDSGKELGMPDGVLINGKGPFKYNSSVPDGIEHETVNVDPGKTYRIRVHNVGISTSLNFRIQNHKLLLIETEGRYTSQMNFTDFDVHVGQSYSFLVTMDQNATSDYYIVASARFVNETVWQRVTGVGILHYSNSKGPASGPLPVSATDVNHPWSAMNQPRAIKQNTSASGARPNPQGSFHYGQINITRTYILRSLPPTKINGKLRATLNGISFVNPSTPMRLADDHKVKGDYMLDFPDRPLDEKLPRLSSSIINATYKGFIQVIFQNNDTKIQSFHIDGYAFYVVAMDFGIWSEDRNSSYNNWDAVARSTVEVYPGAWTAVLISLDNVGVWNIRVENLDRWYLGQETYMRIINPEENGSTEMDPPENVMYCGALQAMQKEQHHSSATKSMTNGQLILIFSMMMVLLSSFSSFC
Protein: DDRGK domain-containing protein 1 (Q38BR4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- E3 UFM1-protein ligase 1-like N-terminal domain-containing protein
Sequence:
MLLIVFVVGFLLLLTAFVALQLRRSQQFPTFSDATPSRVAARRSETRRSQYNDGDYWSNESSDEGSDDDDNDDCEVGHKREERRKLRGGTSGSAGPLRHRRTRRGAGNAAEADGDGEEDKNGSQTKLSRLQRKKQEKERERQERQQAQEALLENRRVKQEEEQRQQKDREREEREREIAEEAALQELREEKKRQEDEEYAKWVEGIGVVERGEIGDEERKKHDNLVKYLITMAGNGGERQQQRVIDAENFGEGEKVGDETITRGTESSSRGNILILNDVARTHGLSVEVTVQVIEKLLEDGVISGVFDDRGKFVMLSEEHYKQIAEFVKLRGRVSMKELARECNRIIML
Protein: Double-stranded RNA-binding protein 3 (dsRNA-binding protein 3) (AtDRB3) (Q9LJF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds double-stranded RNA.
Interaction partners:
- Endoribonuclease Dicer homolog 3
- Protein argonaute 4
- Dicer-like protein 4
- Protein DCL homolog, chloroplastic
- Endoribonuclease Dicer homolog 2
- Endoribonuclease Dicer homolog 1
- Protein argonaute 7
- Protein argonaute 2
Sequence:
MYKNQLQELAQRSCFSLPSYTCTREGPDHAPRFKASVNFNGEIFESPTYCSTLRQAEHSAAEVALSALSSKGPSKSLTARVLDETGIYKNLLQETAHRAGLDLPVYTSVRSGPGHIPTFSCTVELAGMSFNGESAKTKKQAEKNAAIAAWFSLRKMPRLDPLRGEEKEQEIVARVLSRFRPKEVKRREPNQSRRRTVIRTIRQNTTTTTTTTGDLLCEKLRSINLYTNEASSSSPPPQRFWPSRTNLTQEQSKVKSLLEKCQEYAEKKQSLDDPKPEMRIKTSSPSPLSSSVERNCYSKLLPFPSFVLNHQKLAPAVHIRSVIPVCSAPPPKPNPNPNSSPFITRELGNGSQEKKSLPN
Protein: Proton myo-inositol cotransporter (H(+)-myo-inositol cotransporter) (Hmit) (H(+)-myo-inositol symporter) (Solute carrier family 2 member 13) (Q96QE2)
Organism: Homo sapiens (Human)
Function: H(+)-myo-inositol cotransporter. Can also transport related stereoisomers.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11500374}; Multi-pass membrane protein {ECO:0000269|PubMed:11500374}.
Interaction partners:
- Major facilitator superfamily
- Sodium/myo-inositol cotransporter
Sequence:
MSRKASENVEYTLRSLSSLMGERRRKQPEPDAASAAGECSLLAAAESSTSLQSAGAGGGGVGDLERAARRQFQQDETPAFVYVVAVFSALGGFLFGYDTGVVSGAMLLLKRQLSLDALWQELLVSSTVGAAAVSALAGGALNGVFGRRAAILLASALFTAGSAVLAAANNKETLLAGRLVVGLGIGIASMTVPVYIAEVSPPNLRGRLVTINTLFITGGQFFASVVDGAFSYLQKDGWRYMLGLAAVPAVIQFFGFLFLPESPRWLIQKGQTQKARRILSQMRGNQTIDEEYDSIKNNIEEEEKEVGSAGPVICRMLSYPPTRRALIVGCGLQMFQQLSGINTIMYYSATILQMSGVEDDRLAIWLASVTAFTNFIFTLVGVWLVEKVGRRKLTFGSLAGTTVALIILALGFVLSAQVSPRITFKPIAPSGQNATCTRYSYCNECMLDPDCGFCYKMNKSTVIDSSCVPVNKASTNEAAWGRCENETKFKTEDIFWAYNFCPTPYSWTALLGLILYLVFFAPGMGPMPWTVNSEIYPLWARSTGNACSSGINWIFNVLVSLTFLHTAEYLTYYGAFFLYAGFAAVGLLFIYGCLPETKGKKLEEIESLFDNRLCTCGTSDSDEGRYIEYIRVKGSNYHLSDNDASDVE
Protein: Flagellar motor switch protein FliG (Q44458)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
Subcellular location: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliN
- Flagellar M-ring protein
- Flagellar basal-body rod protein FlgC
- Flagellar hook protein FlgE
- Flagellum-specific ATP synthase
- Flagellar L-ring protein
- Flagellar hook-associated protein 1
- Flagellar biosynthetic protein
- Motility protein A
Sequence:
MMDFEDFGNPLAGKPLSQADKAAAVLLAMGKGVAGKLLKFFTQHELQMIISSAQTLRVIPPDELAQIVAEFEDLFTEGTGLMDNAKAIESILEEGLTPEEVDSLLGRRAAFQAYEASIWDRLQEAEPEFVGKFLLREHPQTIAYILSMLPSSFGAKVLLTIPEEQRADIMNRTVNMKEVSPTAAQIIEKRVVNLINEIEAERNAGGSTKVADLMNELDKPQVDTLLSSLETLSKEAANKVKPKIFLFDDLMFMPQRSRVLLLNDVSADVLTMALRGATVEIKECVLSSISPRQRRMIESDLAVPQASLNTREVAIARRAVAQEAIRLANSGQIQLKDVAAEEQSAAA
Protein: PDZ and LIM domain protein 1 (C-terminal LIM domain protein 1) (Elfin) (LIM domain protein CLP-36) (O70400)
Organism: Mus musculus (Mouse)
Function: Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton (By similarity). Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration and in maintaining cell polarity of fibroblasts (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11596114}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O00151}. Note=Associates with the actin stress fibers (PubMed:11596114).
Interaction partners:
- Alpha-actinin-1
- Alpha-actinin-4
- ENH isoform 1e
Sequence:
MTTQQIVLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAAIANLCIGDLITAIDGEDTSSMTHLEAQNKIKGCADNMTLTVSRSEQKIWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPAPSTRVITNQYNSPTGLYSSENISNFNNAVESKTSASGEEANSRPVVQPHPSGSLIIDKDSEVYKMLQEKQELNEPPKQSTSFLVLQEILESDGKGDPNKPSGFRSVKAPVTKVAASVGNAQKLPICDKCGTGIVGVFVKLRDHHRHPECYVCTDCGINLKQKGHFFVEDQIYCEKHARERVTPPEGYDVVTVFRE
Protein: Receptor protein kinase CLAVATA1 (EC 2.7.11.1) (Q9SYQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the detection of CLV3 and CLV3-like (CLE) peptides, that act as extracellular signals regulating meristem maintenance. Acts with CLV3p as a ligand-receptor pair in a signal transduction pathway coordinating growth between adjacent meristematic regions and controlling the balance between meristem cell proliferation and differentiation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19933383, ECO:0000269|PubMed:21051944}; Single-pass type I membrane protein {ECO:0000269|PubMed:19933383, ECO:0000269|PubMed:21051944}.
Interaction partners:
- Protein CLAVATA 3
- Receptor-like protein CLAVATA2
- Protein phosphatase 2C 70
- CLAVATA3/ESR
- Protein phosphatase 2C 29
- Protein WUSCHEL
- CLAVATA3/ESR
- Serine/threonine-protein kinase-like protein ACR4
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MAMRLLKTHLLFLHLYLFFSPCFAYTDMEVLLNLKSSMIGPKGHGLHDWIHSSSPDAHCSFSGVSCDDDARVISLNVSFTPLFGTISPEIGMLTHLVNLTLAANNFTGELPLEMKSLTSLKVLNISNNGNLTGTFPGEILKAMVDLEVLDTYNNNFNGKLPPEMSELKKLKYLSFGGNFFSGEIPESYGDIQSLEYLGLNGAGLSGKSPAFLSRLKNLREMYIGYYNSYTGGVPPEFGGLTKLEILDMASCTLTGEIPTSLSNLKHLHTLFLHINNLTGHIPPELSGLVSLKSLDLSINQLTGEIPQSFINLGNITLINLFRNNLYGQIPEAIGELPKLEVFEVWENNFTLQLPANLGRNGNLIKLDVSDNHLTGLIPKDLCRGEKLEMLILSNNFFFGPIPEELGKCKSLTKIRIVKNLLNGTVPAGLFNLPLVTIIELTDNFFSGELPVTMSGDVLDQIYLSNNWFSGEIPPAIGNFPNLQTLFLDRNRFRGNIPREIFELKHLSRINTSANNITGGIPDSISRCSTLISVDLSRNRINGEIPKGINNVKNLGTLNISGNQLTGSIPTGIGNMTSLTTLDLSFNDLSGRVPLGGQFLVFNETSFAGNTYLCLPHRVSCPTRPGQTSDHNHTALFSPSRIVITVIAAITGLILISVAIRQMNKKKNQKSLAWKLTAFQKLDFKSEDVLECLKEENIIGKGGAGIVYRGSMPNNVDVAIKRLVGRGTGRSDHGFTAEIQTLGRIRHRHIVRLLGYVANKDTNLLLYEYMPNGSLGELLHGSKGGHLQWETRHRVAVEAAKGLCYLHHDCSPLILHRDVKSNNILLDSDFEAHVADFGLAKFLVDGAASECMSSIAGSYGYIAPEYAYTLKVDEKSDVYSFGVVLLELIAGKKPVGEFGEGVDIVRWVRNTEEEITQPSDAAIVVAIVDPRLTGYPLTSVIHVFKIAMMCVEEEAAARPTMREVVHMLTNPPKSVANLIAF
Protein: Reticulocyte binding protein homologue 4 (C0H496)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNKNILWITFFYFLFFLLDMYQGNDAIPSKEKKNDPEADSKNSQNQHDINKTHHTNNNYDLNIKDKDEKKRKNDNLINNYDYSLLKLSYNKNQDIYKNIQNGQKLKTDIILNSFVQINSSNILMDEIENYVKKYTESNRIMYLQFKYIYLQSLNITVSFVPPNSPFRSYYDKNLNKDINETCHSIQTLLNNLISSKIIFKMLETTKEQILLLWNNKKISQQNYNQENQEKSKMIDSENEKLEKYTNKFEHNIKPHIEDIEKKVNEYINNSDCHLTCSKYKTIINNYIDEIITTNTNIYENKYNLPQERIIKNYNHNGINNDDNFIEYNILNADPDLRSHFITLLVSRKQLIYIEYIYFINKHIVNKIQENFKLNQNKYIHFINSNNAVNAAKEYEYIIKYYTTFKYLQTLNKSLYDSIYKHKINNYSHNIEDLINQLQHKINNLMIISFDKNKSSDLMLQCTNIKKYTDDICLSIKPKALEVEYLRNINKHINKNEFLNKFMQNETFKKNIDDKIKEMNNIYDNIYIILKQKFLNKLNEIIQNHKNKQETKLNTTTIQELLQLLKDIKEIQTKQIDTKINTFNMYYNDIQQIKIKINQNEKEIKKVLPQLYIPKNEQEYIQIYKNELKDRIKETQTKINLFKQILELKEKEHYITNKHTYLNFTHKTIQQILQQQYKNNTQEKNTLAQFLYNADIKKYIDELIPITQQIQTKMYTTNNIEHIKQILINYIQECKPIQNISEHTIYTLYQEIKTNLENIEQKIMQNIQQTTNRLKINIKKIFDQINQKYDDLTKNINQMNDEKIGLRQMENRLKGKYEEIKKANLQDRDIKYIVQNNDANNNNNNIIIINGNNQTGDYNHILFDYTHLWDNAQFTRTKENINNLKDNIQININNIKSIIRNLQNELNNYNTLKSNSIHIYDKIHTLEELKILTQEINDKNVIRKIYDIETIYQNDLHNIEEIIKNITSIYYKINILNILIICIKQTYNNNKSIESLKLKINNLTNSTQEYINQIKAIPTNLLPEHIKQKSVSELNIYMKQIYDKLNEHVINNLYTKSKDSLQFYINEKNYNNNHDDHNDDHNDVYNDIKENEIYKNNKLYECIQIKKDVDELYNIYDQLFKNISQNYNNHSLSFVHSINNHMLSIFQDTKYGKHKNQQILSDIENIIKQNEHTESYKNLDTSNIQLIKEQIKYFLQIFHILQENITTFENQYKDLIIKMNHKINNNLKDITHIVINDNNTLQEQNRIYNELQNKIKQIKNVSDVFTHNINYSQQILNYSQAQNSFFNIFMKFQNINNDINSKRYNVQKKITEIINSYDIINYNKNNIKDIYQQFKNIQQQLNTTETQLNHIKQNINHFKYFYESHQTISIVKNMQNEKLKIQEFNKKIQHFKEETQIMINKLIQPSHIHLHKMKLPITQQQLNTILHRNEQTKNATRSYNMNEEENEMGYGITNKRKNSETNDMINTTIGDKTNVLKNDDQEKGKRGTSRNNNIHTNENNINNEHTNENNINNEHTNEKNINNEHANEKNIYNEHTNENNINYEHPNNYQQKNDEKISLQHKTINTSQRTIDDSNMDRNNRYNTSSQQKNNLHTNNNSNSRYNNNHDKQNEHKYNQGKSSGKDNAYYRIFYAGGITAVLLLCSSTAFFFIKNSNEPHHIFNIFQKEFSEADNAHSEEKEEYLPVYFDEVEDEVEDEVEDEDENENEVENENEDFNDI
Protein: Mitochondrial translation release factor in rescue (Q9H3J6)
Organism: Homo sapiens (Human)
Function: Part of a mitoribosome-associated quality control pathway that prevents aberrant translation by responding to interruptions during elongation. As heterodimer with MTRES1, ejects the unfinished nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for MTRES1 and MTRF during mitoribosome rescue.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:20186120, ECO:0000269|PubMed:20598281}.
Interaction partners:
- Large ribosomal subunit protein mL62
- Mitochondrial transcription rescue factor 1
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL33m
Sequence:
MSTVGLFHFPTPLTRICPAPWGLRLWEKLTLLSPGIAVTPVQMAGKKDYPALLSLDENELEEQFVKGHGPGGQATNKTSNCVVLKHIPSGIVVKCHQTRSVDQNRKLARKILQEKVDVFYNGENSPVHKEKREAAKKKQERKKRAKETLEKKKLLKELWESSKKVH
Protein: Cysteine-rich receptor-like protein kinase 4 (Cysteine-rich RLK4) (EC 2.7.11.-) (Q9LZU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- CDPK-related kinase 7
- CDPK-related kinase 2
- CDPK-related kinase 5
- O-fucosyltransferase 4
- E3 ubiquitin-protein ligase
- CDPK-related kinase 3
Sequence:
MSFFWLFPFLLHLSFADSLSPLSAPVQNFIHLNHSCPSSILTYSRNSTYFTNLKTLLSSLSSRNASYSTGFQTATAGQAPDRVTGLFLCRGDVSQEVCRNCVAFSVKETLYWCPYNKEVVLYYDECMLRYSHRNILSTVTYDGSAILLNGANISSSNQNQVDEFRDLVSSTLNLAAVEAANSSKKFYTRKVITPQPLYLLVQCTPDLTRQDCLRCLQKSIKGMSLYRIGGRFFYPSCNSRYENYSFYNETATRSSSPPSLPPRSTPQQQLKLAPPPLISERGKGRNSSVIIVVVVPIIALLLLFVAFFSLRAKKTRTNYEREPLTEESDDITTAGSLQFDFKAIEAATNKFCETNKLGQGGFGEVYKGIFPSGVQVAVKRLSKTSGQGEREFANEVIVVAKLQHRNLVRLLGFCLERDERILVYEFVPNKSLDYFIFDSTMQSLLDWTRRYKIIGGIARGILYLHQDSRLTIIHRDLKAGNILLGDDMNAKIADFGMARIFGMDQTEANTRRIVGTYGYMSPEYAMYGQFSMKSDVYSFGVLVLEIISGKKNSNVYQMDGTSAGNLVTYTWRLWSNGSPLELVDPSFRDNYRINEVSRCIHIALLCVQEEAEDRPTMSAIVQMLTTSSIALAVPQRPGFFFRSSKHEQVGLVDRLSINTSALCSVDDASITNVTPR
Protein: Collagen alpha-1(V) chain (O88207)
Organism: Mus musculus (Mouse)
Function: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin (By similarity). Transcriptionally activated by CEBPZ, which recognizes a CCAAT-like motif, CAAAT in the COL5A1 promoter.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Fibrillin-1
- Procollagen C-endopeptidase enhancer 1
- Lumican
- Serpin H1
- Collagen alpha-2
- A disintegrin and metalloproteinase with thrombospondin motifs 2
Sequence:
MDVHTRWKAARPGALLLSSPLLLFLLLLWAPPSSRAAQPADLLEMLDFHNLPSGVTKTTGFCATRRSSSEPDVAYRVSKDAQLSMPTKQLYPESGFPEDFSILTTVKAKKGSQAFLVSIYNEQGIQQLGLELGRSPVFLYEDHTGKPGPEEYPLFPGINLSDGKWHRIALSVYKKNVTLILDCKKKITKFLSRSDHPIIDTNGIVMFGSRILDDEIFEGDIQQLLFVSDNRAAYDYCEHYSPDCDTAVPDTPQSQDPNPDEYYPEGEGETYYYEYPYYEDPEDPGKEPAPTQKPVEAARETTEVPEEQTQPLPEAPTVPETSDTADKEDSLGIGDYDYVPPDDYYTPPPYEDFGYGEGVENPDQPTNPDSGAEVPTSTTVTSNTSNPAPGEGKDDLGGEFTEETIKNLEENYYDPYFDPDSDSSVSPSEIGPGMPANQDTIFEGIGGPRGEKGQKGEPAIIEPGMLIEGPPGPEGPAGLPGPPGTTGPTGQMGDPGERGPPGRPGLPGADGLPGPPGTMLMLPFRFGGGGDAGSKGPMVSAQESQAQAILQQARLALRGPAGPMGLTGRPGPMGPPGSGGLKGEPGDMGPQGPRGVQGPPGPTGKPGRRGRAGSDGARGMPGQTGPKGDRGFDGLAGLPGEKGHRGDPGPSGPPGIPGDDGERGDDGEVGPRGLPGEPGPRGLLGPKGPPGPPGPPGVTGMDGQPGPKGNVGPQGEPGPPGQQGNPGAQGLPGPQGAIGPPGEKGPLGKPGLPGMPGADGPPGHPGKEGPPGEKGGQGPPGPQGPIGYPGPRGVKGADGIRGLKGTKGEKGEDGFPGFKGDMGIKGDRGEIGPPGPRGEDGPEGPKGRGGPNGDPGPLGPTGEKGKLGVPGLPGYPGRQGPKGSIGFPGFPGANGEKGGRGTPGKPGPRGQRGPTGPRGERGPRGITGKPGPKGNSGGDGPAGPPGERGPNGPQGPTGFPGPKGPPGPPGKDGLPGHPGQRGETGFQGKTGPPGPPGVVGPQGPTGETGPMGERGHPGPPGPPGEQGLPGAAGKEGTKGDPGPAGLPGKDGPPGLRGFPGDRGLPGPVGALGLKGSEGPPGPPGPAGSPGERGPAGAAGPIGIPGRPGPQGPPGPAGEKGLPGEKGPQGPAGRDGLQGPVGLPGPAGPVGPPGEDGDKGEIGEPGQKGSKGDKGEQGPPGPTGPQGPIGQPGPSGADGEPGPRGQQGLFGQKGDEGSRGFPGPPGPVGLQGLPGPPGEKGETGDVGQMGPPGPPGPRGPSGAPGADGPQGPPGGIGNPGAVGEKGEPGEAGDPGLPGEGGPLGPKGERGEKGEAGPSGAAGPPGPKGPPGDDGPKGSPGPVGFPGDPGPPGEPGPAGQDGPPGDKGDDGEPGQTGSPGPTGEPGPSGPPGKRGPPGPAGPEGRQGEKGAKGEAGLEGPPGKTGPIGPQGAPGKPGPDGLRGIPGPVGEQGLPGSPGPDGPPGPMGPPGLPGLKGDSGPKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGSSGPKGDQGITGPSGPLGPPGPPGLPGPPGPKGAKGSSGPTGPKGEAGHPGLPGPPGPPGEVIQPLPIQASRTRRNIDASQLLDDGAGESYVDYADGMEEIFGSLNSLKLEIEQMKRPLGTQQNPARTCKDLQLCHPDFPDGEYWVDPNQGCSRDSFKVYCNFTAGGSTCVFPDKKSEGARITSWPKENPGSWFSEFKRGKLLSYVDAEGNPVGVVQMTFLRLLSASAHQNVTYNCYQSVAWQDAATGSYDKAIRFLGSNDEEMSYDNNPYIRALVDGCATKKGYQKTVLEIDTPKVEQVPIVDIMFNDFGEASQKFGFEVGPACFLG