wanglab/gogpt-training-data huggingface dataset:
Protein: Exocyst complex component EXO84B (AtExo80b) (Q9LTB0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. Probable component of an exocyst subcomplex specifically involved in autophagy-related, Golgi-independent membrane traffic to the vacuole. Regulates autophagosome formation and autophagy-related Golgi-independent import into the vacuole. Mediates ABCG36/PEN3 outer-membrane polarity at the periphery of lateral root cap and root epidermal cells.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19895414}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:20870962}. Secreted, cell wall {ECO:0000269|PubMed:20870962}. Cell membrane {ECO:0000269|PubMed:27803190}. Note=Localized to globular structures in the perinuclear region (PubMed:19895414). During cytokinesis, localizes to the nascent cell plate and later to the cell plate insertion site and along the post-cytokinetic wall (PubMed:20870962). Polarized localization at the outermost side of root epidermal and cap cells, in the outer lateral membrane domain facing the environment (PubMed:27803190). {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:27803190}.
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC5A
- Exocyst complex component SEC5B
- Exocyst complex component SEC3A
- Exocyst complex component SEC15B
- Exocyst complex component SEC10a
- Exocyst complex component EXO70A1
- Exocyst complex component SEC3B
- Exocyst complex component EXO70B1
Sequence:
MAAKTARSKATPTKENGVRVEEGLSLFKSDKFDADAYVQSKCSINEKDIKQLCSYLLDLKRASAEEMRRSVYANYPAFIRTSKEISDLEGELSSIRNLLSTQATLIHGLADGVNIDDDKVSDESLANGLLNFEDNGLSDLEKWATEFPDHLDALLAERRVDEALAAFDEGEILVSQANEKHTLSSSVLSSLQFAIAERKQKLADQLAKAACQPSTRGGELRSAIAALKRLGDGPRAHTVLLDAHFQRYQYNMQSLRPSSTSYGGAYTAALSQLVFSAISQASSDSLGIFGKEPAYSSELVTWATKQTEAFSLLVKRHALASSAAAGGLRAAAECAQIALGHCSLLEARGLSLCPVLLKHFKPIVEQALEANLKRIEENTAAMAAADDWVLTSPPAGSRHASTAFQNKLTSSAHRFNLMVQDFFEDVGPLLSMQLGSKALEGLFRVFNSYVDVLVRALPGSIEEEDPNFESSCNKIVQMAETEANQLALLANASLLADELLPRAAMKLSLDQTGQRTDDLRRPLDRQNRNPEQREWKRRLLSTVDKLKDAFCRQHALDLIFTEEGDSHLSADMYVNIDENGEDVDFFPSLIFQELFAKLNRMASLAADMFVGRERFAISLLMRLTETVILWLSGDQSFWDDIEEGPRPLGPLGLRQLYLDMKFVICFASQGRYLSRNLHRGTNEIISKALAAFTATGIDPYSELPEDDWFNDICVDAMERLSGKTKGNNGDVHSPTASVSAQSVSSARSHGSY
Protein: Cell adhesion molecule DSCAML1 (Down syndrome cell adhesion molecule-like protein 1 homolog) (E1C8P7)
Organism: Gallus gallus (Chicken)
Function: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q4VA61}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q4VA61}. Synapse {ECO:0000269|PubMed:18216854}.
Interaction partners:
Sequence:
MWLVTFFLLYSLRKAHTEDVGTSLYFVNDSIQQVTFSSTVGVVIPCPAAGSPSAVLRWYLATGDDIYDVPHIRHVHANGTLQLYPFSPSAFNSFIHDNDYFCTAENSAGKIRSPNIRVKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSIIPENRFFITSYGGLYISDVQKEDALSTYRCITKHKYSGETRQSNGARLSVSDADPAESIPTMLDSFQSREVRAGRLVELPCIASGYPNPAIRWLKDGRPLPADGRWAKRITGLSIADLRVEDSGTYICEVTNTFGSAEVTGTLTVIDPLRVTLTPKKLKTGIGSTVILSCALSGSPEYVIRWYRNTDLVVVDDFISIRGISNETLLITAAQKSHSGAYQCFATRKSQTAQDFSIITLEDGTPRIVSSFSEKVVNPGEQFSLMCAAKGAPPPTVTWALDDEPIPRDNGHRTNQYTMSDGTTVSHMNVTSPQIKDGGVYRCTARNSVGSAEYQARINVRGPPSIRAMKNITAVAGRDTFINCRVIGYPYYSIKWYKDSLLLPDNHRQVVFENGTLKLMDVQKGMDEGEYLCSVLIQPQLSISQSVHVTVKVPPLIQPFEFPPASIGQLLYIPCVVSSGDMPIHITWRKDGHVILSGSGVTIESKEFMSSLQISSVSLKHNGNYTCIASNAAATVSRERQLIVRVPPRFVVQPNNQDGIYGKAGVLNCSVDGYPPPKVMWKHAKGSGNPQQYHPIPLTGRIQILPNSSLLIRHVLEEDIGYYLCQASNGVGTDISKSMFLTVKIPAMITSHPNTTIAIKGQSKELNCTARGERPIIIRWEKGDTVIDPDRNMRYAIATKDNGDEVISTLKLKPADRGDSVFFSCHAINSYGEDRGLIQLTVQEPPDPPELEIREVKARSMNLRWTQRFDGNSIITGFDIEYKNKSDSWDFKQSTRNISPTINQANIVDLHPASVYSIRMYSFNKIGRSEPSKELTISTEEAAPDGPPMDVTLQPMTSQSIQVTWKAPKKELQNGVIRGYQIGYRENSPGSNGQYSIVEMKATGDSEVYTLDNLKKFAQYGVVVQAFNRAGTGPSSSEINATTLEDVPSQPPENVRAISITSDVAVISWSEPPRSTLNGVLKGYRVIFWSLYMDGEWGEMQNITTTRERVELRGMEKFTNYSVQVLAYTQAGDGVRSSVLYIQTKEDIPGPPAGIKAVPSSASSVVVSWLPPAKPNGIIRKYTIFCSSPGSGQPAPSEYETSPDQLFYRIAHLNRGQQYMLWVAAVTSAGRGNISEKVTIEPAGKAPAKIISFGGTVTTPWMKDVRLPCNSVGEPVPAIKWTKDSEDSAIPVTVDGHRLIQANGTLVLRSVKAEDSGYYTCTATNTWGFDTIIINLLVQVPPDQPRLTVSKTSASSITLAWIPGDNGGSSIRGFVLQYSVDNSEEWKDVFISSSERSFKLESLKCGTWYKVKLAAKNSVGAGRISEIIEAKTHGREPSFSKDQHLFTHINSTHARLNLQGWSSGGCPITAIVLEYRPKGNWGWQSLRTNSSGEVFLTELREATWYELRMKACNSAGCGNESTQFATLDYDGSTIPPIKSAQGEGDDVKKLFTIACPIILATLGVALLFIIRKKRKEKRLKRLRDAKSLAEMLISKNNRSFDTPVKGPPQGPRLHIDIPRVQLLIEDKEGIKQLGDDKATIPVTDTEFSQAVNPQSFCTGVSLHHPALIQNTGPLIDMSDIRPGTNPVSRKSVKSAHSTRNRYSSQWTLTKCQASTPARTLTSDWRTVGSQHGITVTESDSYSASLSQDTDKGRNSMVSTESASSTYEELARAYEHAKLEEQLQHAKFEITECFISDSSSDQMTTGTTDNADSMTSMSTPSEPGICRFTASPPKPQDSERGKSVAVPIPHRASKSDYCNLPLYVKSDAFFRKPDSHEPCPVVPPREASIRSLARGYHPPARHLTLDPAAKPPGLPPPSSSSSSTTLPQRTLPMPTAASTAPAPAPAPAAPAEPPANTTTTTTTHSKVGGSRDSLLEMSTSGAGRAQKQGAGAYSKSYTLV
Protein: SLIT-ROBO Rho GTPase activating protein 2 (SRGAP2 protein) (B7ZM87)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVISEPPEEKVTARAGASCPSGGHVADIYLANINKQRKRPESGSIRKTFRSDSHGLSSSLTDSSSPGVGASCRPSSQPIMSQSLPKEGPDKCSISGHGSLNSISRHSSLKNRLDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELRELERQSSVKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSTSPQSTDKSCTV
Protein: RNA polymerase II-associated protein 3 (Q9H6T3)
Organism: Homo sapiens (Human)
Function: Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.
Interaction partners:
- RuvB-like 1
- PIH1 domain-containing protein 1
- RuvB-like 2
- Prefoldin subunit 6
- Dynein axonemal assembly factor 10
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Protein UXT
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- p53 and DNA damage-regulated protein 1
Sequence:
MTSANKAIELQLQVKQNAEELQDFMRDLENWEKDIKQKDMELRRQNGVPEENLPPIRNGNFRKKKKGKAKESSKKTREENTKNRIKSYDYEAWAKLDVDRILDELDKDDSTHESLSQESESEEDGIHVDSQKALVLKEKGNKYFKQGKYDEAIDCYTKGMDADPYNPVLPTNRASAYFRLKKFAVAESDCNLAVALNRSYTKAYSRRGAARFALQKLEEAKKDYERVLELEPNNFEATNELRKISQALASKENSYPKEADIVIKSTEGERKQIEAQQNKQQAISEKDRGNGFFKEGKYERAIECYTRGIAADGANALLPANRAMAYLKIQKYEEAEKDCTQAILLDGSYSKAFARRGTARTFLGKLNEAKQDFETVLLLEPGNKQAVTELSKIKKELIEKGHWDDVFLDSTQRQNVVKPIDNPPHPGSTKPLKKVIIEETGNLIQTIDVPDSTTAAAPENNPINLANVIAATGTTSKKNSSQDDLFPTSDTPRAKVLKIEEVSDTSSLQPQASLKQDVCQSYSEKMPIEIEQKPAQFATTVLPPIPANSFQLESDFRQLKSSPDMLYQYLKQIEPSLYPKLFQKNLDPDVFNQIVKILHDFYIEKEKPLLIFEILQRLSELKRFDMAVMFMSETEKKIARALFNHIDKSGLKDSSVEELKKRYGG
Protein: FMR1-interacting protein NUFIP1 (Nuclear FMRP-interacting protein 1) (Q9QXX8)
Organism: Mus musculus (Mouse)
Function: Binds RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10556305}. Note=Distributed in the nucleus in a dot-like pattern.
Interaction partners:
- Zinc finger HIT domain-containing protein 3
- Box C/D snoRNA protein 1
- PIH1 domain-containing protein 1
- RNA-binding protein FXR1
- Microtubule-associated protein 1 light chain 3 beta
- Nucleolar protein 58
- Fragile X messenger ribonucleoprotein 1
- RNA-binding protein FXR2
- FMR1-interacting protein NUFIP2
- Nucleolar protein 56
Sequence:
MAEPAPAVWPSAPDLTPAPGTPSEAAPPRDNWVYWAMLPPPPPPLSSPVAGSEQSRKGQPHVLPQPPSGALPPFDAQILPAAQPPFDAQAPPDAQSQFSGQQAWNLQASTPWYWGLSPNGFSTYHTSYQSPVTHSYFPRSHDAKFNLPQNRKQKTKKRKEPVFHFFCDTCDRGFKNQEKYDTHMSEHTKCPEVDCSFSAHEKIVQFHWRNMHAPGMKKIKLDTPEEIARWREERRKNYPTLANIERKKKLQLEKAKRGEVLTTTQYGKMKGMSRHSQMAKIRSPGKHHKWRRGGARQRAVVGLGNHARDSKPEVPSKANVDPLGALIHSDSESDKEEKAQRTVVPKEVTPALCSLMSSYGDVSGSDSEPEEAPIKTEAEVLAENHVLHSSPPKSPKQNVQTTGRTVSRSKWENQRNGLRKISLKRKKSHCHPLFEPRTHHPYLLEMLLAPDIRHERNVILQCVRYIIKKDFFGLNTDSVKTEEV
Protein: Late embryogenesis abundant domain-containing protein / LEA domain-containing protein (Similar to late embryogenesis abundant proteins) (Q9ZPW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Late embryogenesis abundant protein 46
- At2g03850 family protein)
- Agamous-like MADS-box protein AGL93
- Late embryogenesis abundant protein 7
- AT3g02480/F16B3_11
- At3g12955
- Pumilio homolog 23
- Large ribosomal subunit protein P2v
- Putative pumilio homolog 8, chloroplastic
Sequence:
MMERRRTALVLFVVVVVLTWQEGVLGKWLESTAKEKTGSWAGWVSDKITTGFGTKKEETGIYQKSKDEARKAAQAAENYAYDKANYVKDSAYDNAGYAKDFAENKAEYAKDFAYDKAGDAKNMAYENAGYAKDFAYDKAGDAKDMAYEKAGHAKDFAYDKAGNAKDMAYETAGYAKDFAYDKGGYAKDVAYDKAGNAKDMAYEKAGNAKDMAYEKAEHIKDFTYDKVGSAYGSAQSMMDSGYDKAGDAKDMAYEKAGIVKDMAYDKAGDAKDVAYEKAGIAKDMAYDKAGNAKDMAYDKVGSAYGSAQKAKDSGYEKAGEAKDYAYKKAGNAKDIAYEKAQDAKDFAYDKAGYGYDKAGDVIRMATDKSGEAYEGAKEKSKSAKDTAGEAMDDSIDYMKDKSHNAKDGATRGFEEAMEKVGEKYGVAKESTKYAYETAKKKASQVAGEIRDRYAEL
Protein: Slit homolog 1a precursor (Slit1a) (Q3S2J2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPARGGCCLLEVCVWVLLLVCKTGSGCPALCTCSGTTVDCHGLGLKNIPRNIPRNTERLELNGNNLTRINRNDFTGLKYLRVLQLMENQIVTVERGAFDEMRELERLRLNRNQLHQLPELLFQKNAALSRLDLSENFIQAIPRKAFRGATDIKNLQLDKNHISCIEDGAFRAMRGLEVLTLNNNNISSIPVSSFNHMPKLRTFRLHSNNLVCDCVLSWLSQWLRERPNIGLFTQCSSPAPLRGLNVAEVQKHEFSCSGQSDSAVGQSCSLSSGSCPAVCSCNNNIVDCRGKGPTLIPSSLPDSMTEIRLEQNSIKSIPPGAFSPYKKLRRIDLSNNQISELAPDAFQGLRSLNSLVLYGNKITDLPRGVFDGLHALQLLLLNANKIHCLRANTFQDLQNLSLLSLYDNKIQTLAKGTFSSLRAIQTLHLAQNPFICDCNLKWLADYLRSNPIETSGARCTSPRRLANKRIGQIKSKKFRCSAKEQYAIPGTEDSRLNNDCNNDPVCPAKCRCESNVVDCSNLRLDRIPEHVPASTTEPRLNNNEITTIEAMGAFKTLTHLKKINLSNNKISEIEDGAFEGASSVNELHLTANQLDLAHSGMFRGLEGLRMLMLRNNRISCIHNNSFTGLHNVRLLSLYDNTLTTIAPGAFDTLQSLSTLNLLANPFNCNCRLAWLSSWLRNRKIVTGNPRCHRPAFLKEIPLQDVAAPDFRCEDDHEDVSCAPPVHCPADCTCLESVVRCSNKHLQALPKGTPRNITELYLDGNQLSTVPKELSSFKSLQLVDLSNNRISSLTNSSFTNMSQLTTLILSYNALRCIPTLAFSGLRSLRLLSLHGNDISELPDGIFSDAQSLSHLAIGANPLHCDCGLRWLSDWVKTGYKEPGIARCASPHGMEGKLLLTTPAKRFECQGEVDSAILAKCNPCASGPCLHQGVCEADQTDSYRCRCADGFKGKNCETVVNACVSEPCKNGGTCHVSTDEDEGYSCSCAAGFEGPSCEVDTDECRDNDCQNGATCIDGINNYTCLCAPFYTGEMCEDLEDMCSSARSPCKQQSTCFITVTGPKCICAAGYVGEDCSVNYDDCKDHRCQNGAQCVDELNGYSCVCQKGYSGQLCEVAPPPRSPCERADCQNNAPCVERAGHPLCQCLEGFGGPRCEKLVSVNFVDRDSYLLLSDLKNWPQANITLQVSTAEDNGILLYNGDNDHIAVEIHEGHVKVSYDPGSQQSHAIYSTETVNDGQFHTVELVTFDQMVNLSIDGGSPTTMDSFGKVQPLRGEAPLYVGGMPVSVHPTAPRVWQIQNSSSFHGCIQNLYINNELQDFTKTQMKPGVVPGCEPCRKIYCLHGICQPNTATGPVCHCQPGWSGQHCDQPLANPCMGSKCVHGRCIPMDMQSYRCECQEGFHGALCNQHEELFNPCRKLQCKHGHCQISDTGDAYCHCEPGYSGDLCDRESECRGEPVRDFYQVQRGYSICQTTRMVSWVECSGVCESGSCCASQRMKRRKYSFECSDGMSFSEEVEKTIKCGCVGCM
Protein: Heme transporter hrg-4 (Heme-responsive gene 4 protein) (CeHRG-4) (Q20106)
Organism: Caenorhabditis elegans
Function: Heme transporter that mediates heme uptake across the plasma membrane.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Heme Responsive protein
- Cadmium-inducible lysosomal protein CDR-5
- Multidrug resistance-associated protein 5
- ADP,ATP carrier protein
- CC domain-containing protein
- Mitochondrial cytochrome c oxidase subunit VIa
- Aspartic protease 10
- NADPH-dependent diflavin oxidoreductase 1
Sequence:
MTAENRGFCQLICHINVRIGWTIFGIVFGISAILTYAIKFHNWSATATTAIATLFACETLYLYWALKKNTIVNWKSSTFQLMIWPNVFIGLLGLLGCLVCYIIAGITHQGAGSIQGWSLFKCSIYFSKFAAMYGENLWFTGSWSLVITKWTWQNAFFARKYLNKIGTASEDGDIDDDDVEVIKS
Protein: Jellein-3 (Jelleine-III) (P84759)
Organism: Apis mellifera (Honeybee)
Function: Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535 and S.saprophyticus, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lacks cytolytic activity and do not induce rat peritoneal mast cell degranulation.
Subcellular location: Secreted {ECO:0000269|PubMed:15203237}.
Interaction partners:
Sequence:
EPFKISIHL
Protein: Sperm microtubule associated protein 2 (Testicular haploid expressed gene protein) (Q9JMB1)
Organism: Mus musculus (Mouse)
Function: May be involved (but not essential) in spermatogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11173852, ECO:0000269|PubMed:12748127}. Note=Localized predominantly in the nucleus of haploid round spermatid.
Interaction partners:
Sequence:
MGELGEHRASLLSNPIPEVKTLGELKQGQNNGNLDLESEPFGSHWLQGSKATTGRTSEEPEEEIPPEEMAGEELPETSNLDGPLQQDLEVEVVEMSHLSITERTPSVSTAKGRKKRSRRLLELAKPKTNWQCLRDRTGRCCKGYAWISPRKTNLQFCLYWPSVYWTERFIEDTTLTITVPVVSQRMEELSRPKRFYQEYYNNNRTTPIWSIPRSTLEYQASNRLKQLATPKVRNNIWSINMSEVSQVSRAAQMAVPTPRTLRLAKPRPPATLLEEWDPMPKPKPYVSDYNRLLQLATPKALSEKCVPDRSPQWEVLDVTKNAVASSRIISLAQPKIRKDLNEGYNPYYISPASLVAQASPRIYELATPKYITKKV
Protein: Protein indeterminate-domain 14 (AtIDD14) (Transcriptional regulator of starch metabolism IDD14) (Q9C9X7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor regulating starch metabolism by binding directly to the promoter of QQS. The IDD14beta isoform attenuates the transcription factor activity by competitively forming heterodimers with reduced DNA-binding capacity. Regulates lateral organ morphogenesis and gravitropic responses. Has a redundant role with IDD16 in directing leaf and floral organ morphogenesis. Involved in the establishment of auxin gradients through the regulation of auxin biosynthesis and transport.
Subcellular location: Nucleus {ECO:0000269|PubMed:21556057, ECO:0000269|PubMed:24039602}.
Interaction partners:
- Probable indole-3-pyruvate monooxygenase YUCCA5
- Protein QUA-QUINE STARCH
- Protein LOW PSII ACCUMULATION 1
- Zinc finger/BTB domain protein, putative
- SH2 domain-containing protein B
- Uncharacterized protein
Sequence:
MIDYERSNTTKNINTHHHNPPPSSSSSDLLPDGNGTAVTQKRKRRPAGTPDPEAEVVSLSPRTLLESDRYVCEICNQGFQRDQNLQMHRRRHKVPWKLLKRETNEEVRKRVYVCPEPTCLHHNPCHALGDLVGIKKHFRRKHSNHKQWICERCSKGYAVQSDYKAHLKTCGTRGHSCDCGRVFSRVESFIEHQDTCTVRRSQPSNHRLHEQQQHTTNATQTASTAENNENGDLSIGPILPGHPLQRRQSPPSEQQPSTLLYPFVTNGSIELQLLPSRNCADETSLSLSIGTMDQKTMSEVEKKSYEKGETSLEREEARRETKRQIEIAELEFAEAKRIRQHARAELHKAHLFREEASRRISATMMQITCHNCKQHFQAPAALVPPPPQTHCTDESTSLAVSYMSSATTEGEKASDRASS
Protein: Cullin-5 (CUL-5) (Cullin-E) (Q54XF7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit (By similarity).
Interaction partners:
- Cullin-associated NEDD8-dissociated protein 1
- RING-box protein 1
- Elongin-C
- Cullin-2
- Cullin-1
- NEDD8-activating enzyme E1 catalytic subunit
- NEDD8-conjugating enzyme Ubc12
- UDP-galactose:fucoside alpha-3-galactosyltransferase
- SCF ubiquitin ligase complex protein SKP1a
- SCF ubiquitin ligase complex protein SKP1b
Sequence:
MSDQITVDELWAECEQTFEDLFLNLKKGLSRKRYMEIYTKIYNYCSSANEKALIDFYIPKVKVLVAQKAVEIMSRSESYPNDALLLFFRNQWNEWKMSSNVLKNLLSPVNKIHSSDKKTTSSSANQNESVVYSDTLNSWRETAFNPLKNKLSVSLLQIIKNDRTGFSTNLQVLSDSLECYVQLGPEKNKLEIYQSCFEQQFLQETETFYKAESADFIEKNGVCEYMRHVYNRIEQETNRVNQYMPISTLEKLTKILNNVLISNYKEQFASKFLDILIEDKSSDLVMMYSLLSRVNHLTPLKNIFSDFIKSEGLKEIESNLKEAQEKPQVLISILLKIYSRFNIMIKECYGNDTDFTTAMDKSFSILVNENPASYDPKKKESNIPVVLSKFCDQILRKGPHHISDEAELEKKLTEAVCLFKYLPDKDIFMLNYQKMLSKRLVEDLSASEDAETLMINKLKNYQGFDYCTKLTRMITDMRLCKDININFQNHLNEKSLTLPYQFNFYVLTNGSWTLTNKQTATPFKPPSEMLSSITYFESFYKKSYQGRVLTFLYDFSRADVDSRQAKGKIYKLTTTAYQMAILLMFNGADKITRFLINDTIGLDETSIRLPLLALIKTGIIECSEPSFKNWNNDTEFTVNSKFSSKKMKVSCNIAVQIGETKQSEGQQTVSEQEIEKERFFKLQAAIVRIMKSKKTMTHNDLTVETTTQVSKWFTPKITAIKKAIEYLIDQEYIRRTTDDNPSARKYEYMA
Protein: Receptor-like protein 42 (AtRLP42) (Protein RESPONSIVENESS TO BOTRYTIS POLYGALACTURONASES 1) (Q9LJS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Recognizes fungal (e.g. B.cinerea and A.niger) endopolygalacturonases (PGs, e.g. BcPG3, BcPG2, BcPG4, BcPG6 and AnPGB) and acts as a microbe-associated molecular pattern (MAMP) receptor to mediate defense response against fungi (e.g. B.cinerea) and oomycetes (e.g. H.arabidopsidis). Functionality seems to depend on the presence of the receptor kinase SOBIR1 as an adapter protein.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Polygalacturonase 1 beta-like protein 2
- Indole-3-acetic acid-amido synthetase GH3.2
- Isovalerate--CoA ligase AAE2
Sequence:
MSKSLLRLTFLLLLLLSCVSPSSFFTFNNPAEGPGACGPHQIQAFTQFKNEFDTRACNHSDPWNGVWCDNSTGAVTMLQLRACLSGTLKPNSSLFQFHHLRSLLLPHNNFTSSSISSKFGMLNNLEVLSLSSSGFLAQVPFSFSNLSMLSALDLSKNELTGSLSFVRNLRKLRVLDVSYNHFSGILNPNSSLFELHHLIYLNLRYNNFTSSSLPYEFGNLNKLEVLDVSSNSFFGQVPPTISNLTQLTELYLPLNDFTGSLPLVQNLTKLSILHLFGNHFSGTIPSSLFTMPFLSSIYLNKNNLSGSIEVPNSSSSSRLEHLYLGKNHLGKILEPIAKLVNLKELDLSFLNTSHPIDLSLFSSLKSLLLLDLSGDWISKASLTLDSYIPSTLEVLRLEHCDISEFPNVFKTLHNLEYIALSNNRISGKFPEWLWSLPRLSSVFITDNLLTGFEGSSEVLVNSSVQILSLDTNSLEGALPHLPLSINYFSAIDNRFGGDIPLSICNRSSLDVLDLSYNNFSGQIPPCLSNLLYLKLRKNNLEGSIPDKYYVDTPLRSFDVGYNRLTGKLPRSLINCSALQFLSVDHNGIKDTFPFYLKALPKLQVLLLSSNEFYGPLSPPNQGPLGFPELRILEIAGNKLTGSLPPDFFVNWKASSHTMNEDLGLYMVYSKVIFGNYHLTYYETIDLRYKGLSMEQENVLTSSATIDLSGNRLEGEIPESLGLLKALIALNLSNNAFTGHIPLSLANLKKIESLDLSSNQLSGTIPNGLGTLSFLAYMNVSHNQLNGEIPQGTQITGQPKSSFEGNAGLCGFPLQESCFGTNAPPAQKPKEEEEAEEDEQELNWKAVAIGYGVGVLLGLAIAQLIASYKPEWLVCLVKSRNPLRSFFGFEY
Protein: WASH complex subunit homolog 3 (Daf-16-dependent longevity protein 1) (O01901)
Organism: Caenorhabditis elegans
Function: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (By similarity). Acts as a component of the DHIC (ddl-1-containing hsf-1 inhibitory complex) which modulates lifespan by sequestering the heat-shock transcription factor hsf-1 to negatively regulate its binding to DNA and its transcriptional activity.
Interaction partners:
- WASH complex subunit homolog 1
- Heat shock factor-binding protein 1
- Heat shock transcription factor hsf-1
- WASH complex subunit strumpellin
- HEPN_LA2681 domain-containing protein
- TPR_REGION domain-containing protein
Sequence:
MNASSRTKPAIDLNKVPPIDHHRTAVTFNCLIMKMTEMLNNFGNKMEDILEKAEQSLDTADRKLRLMESKLAGMSLEDKSTTATPSSAPEIDEIHESNPSSSQIVEETVEEKPEEHTTTVLIKDDPAYSKYFKMLKLGVLEAGVIQKMKSEGVDPSILKRGDEPSRPQAQTSRNYESSGESTASFSDSD
Protein: Antitoxin HigA1 (P9WJA7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone.
Interaction partners:
- SecB-like chaperone Rv1957
- Probable endoribonuclease HigB1
- Putative antitoxin HigA2
- Putative toxin HigB2
Sequence:
MSIDFPLGDDLAGYIAEAIAADPSFKGTLEDAEEARRLVDALIALRKHCQLSQVEVAKRMGVRQPTVSGFEKEPSDPKLSTLQRYARALDARLRLVLEVPTLREVPTWHRLSSYRGSARDHQVRVGADKEILMQTNWARHISVRQVEVA
Protein: Serine protease inhibitor 2 (Q2VMU1)
Organism: Onchocerca volvulus
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MNPFFIFITAFVVLFTYVDADQRKHKCKRPEIWEDCGGCELKCGQSDFAPCALRCNPPGCYCSPFYGLRRDSSGKCISKHQCPTRKHLNAPEDFILETDSVTFRKTL
Protein: Zinc finger and BTB domain-containing protein 9 (Q96C00)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
METPTPLPPVPASPTCNPAPRTIQIEFPQHSSSLLESLNRHRLEGKFCDVSLLVQGRELRAHKAVLAAASPYFHDKLLLGDAPRLTLPSVIEADAFEGLLQLIYSGRLRLPLDALPAHLLVASGLQMWQVVDQCSEILRELETSGGGISARGGNSYHALLSTTSSTGGWCIRSSPFQTPVQSSASTESPASTESPVGGEGSELGEVLQIQVEEEEEEEEDDDDEDQGSATLSQTPQPQRVSGVFPRPHGPHPLPMTATPRKLPEGESAPLELPAPPALPPKIFYIKQEPFEPKEEISGSGTQPGGAKEETKVFSGGDTEGNGELGFLLPSGPGPTSGGGGPSWKPVDLHGNEILSGGGGPGGAGQAVHGPVKLGGTPPADGKRFGCLCGKRFAVKPKRDRHIMLTFSLRPFGCGICNKRFKLKHHLTEHMKTHAGALHACPHCGRRFRVHACFLRHRDLCKGQGWATAHWTYK
Protein: cAMP-dependent protein kinase type II regulatory subunit (P81900)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Mediates membrane association by binding to anchoring proteins, such as Akap200. Might play an essential role in the regulation of neuronal activity in the brain.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10480936, ECO:0000269|PubMed:9196067}. Cell membrane {ECO:0000269|PubMed:12223401}. Note=Localization to the membrane depends on Akap200. {ECO:0000269|PubMed:12223401}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit 1
- cAMP-dependent protein kinase catalytic subunit 2
- UT01108p)
- cAMP-dependent protein kinase catalytic subunit 3
- Ribosomal protein S6 kinase
- FI03282p
- Serine/threonine-protein kinase tricornered
- Protein phosphatase PHLPP-like protein
- cAMP-dependent protein kinase type I regulatory subunit
Sequence:
MSSDSSRRIQVPEELKEVLLQFSISFLVEQPPDVIDYAVEYFTKLQSERPSVSHTDQSTDDQLSVNSQDADAEPPVMASSRRKSVFAEAYDPEADDDDDGATAVFPKTDEQRARLVESVKNVLLFRSLEKEQMNQVLDAMFERKVQPGDFIIRQGDDGDNFYVIESGVYKVYINDKHINTYNHTGLFGELALLYNMPRAATVQAETSGLLWAMDRQTFRRILLKSAFRKRKMYEELLNSVPMLKALQNYERMNLADALVSKSYDNGERIIKQGDAADGMYFIEEGTVSVRMDQDDAEVEISQLGKGQYFGELALVTHRPRAASVYATGGVVKLAFLDVKAFERLLGPCMDIMKRNIDDYESQLVKIFGSKNNITDTR
Protein: Defensin-like protein 255 (Q2V3Q8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MRSISFKLLLLVSLLVVVSRYTLAYEDSCSTDEECRRNCLCDVAYCDKSRDKCDYGFMNRVDVRFPKHPYISKNKDGSGR
Protein: CCT-theta (Q38AE5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
- T-complex protein 1, zeta subunit, putative
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit epsilon
- CCT-beta
- Phosducin domain-containing protein
- Chaperonin HSP60, mitochondrial
- Prefoldin, putative
Sequence:
MSFMQTGPASMLKDGSTFVDDPVIKNIDACRELAKITRSSMGPYGLCKMVINHLNKLFVTHDAATILRELEVEHPAAKLLVQASNAMQEEVGDGTNFVVSLAGELLSQAESLVRMGLHPSEIVEGYKKAGNKSLEILETLTVGTVDDVLLKEQVMAPIRTAIASKQYGHDSFLANLVVEACINACPTNTRSFNVDNVRVAKLDGDCVLGSRNVRGFVIARNPEGVVRHQKKAKIAVYACAVDVPSTETKGTALIETADELLQFSRKEEEAMEEIITNIHKTGVNVIVSNSTFGDLALHYLNRYGIMAVKVPSKFELRRLCAAVGARTLSRLDTPTVEDIGSCDNVDVTDAGGKNIISFVQDKDDSKLSTIVVRGATKNVLDDVERAIDDGVNVFKALTKDKRLVAGAGAVEMELQRKLKLFAETSPGLDQYAIHKFASSFEVVARTLAEVSGFNGTDVVTQLEIDHNAGKVHNGVGVEDGTTIDSLEAGIVEPYLTKYWAINLATEAVVTVLQVNQIIVAKQAGGPKNRPDQARDDD