wanglab/gogpt-training-data huggingface dataset:
Protein: TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L (TAF5L) (PCAF-associated factor 65 beta) (PAF65-beta) (O75529)
Organism: Homo sapiens (Human)
Function: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (Probable). With TAF6L, acts as an epigenetic regulator essential for somatic reprogramming. Regulates target genes through H3K9ac deposition and MYC recruitment which trigger MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9674425}.
Interaction partners:
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 12
- Transcription initiation protein SPT3 homolog
- Transcriptional adapter 1
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 9B
- Transcription initiation factor TFIID subunit 9
- Transformation/transcription domain-associated protein
- Transcription factor SPT20 homolog
- TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L
Sequence:
MKRVRTEQIQMAVSCYLKRRQYVDSDGPLKQGLRLSQTAEEMAANLTVQSESGCANIVSAAPCQAEPQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFLQNASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHIHLDVQPAKRTDYQLYASGSSSRSENNGLEPPDMPSPILQNEAALEVLQESIKRVKDGPPSLTTICFYAFYNTEQLLNTAEISPDSKLLAAGFDNSCIKLWSLRSKKLKSEPHQVDVSRIHLACDILEEEDDEDDNAGTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRNTYCSAPADGSSSELVGVYTGQMSNVLSVQFMACNLLLVTGITQENQEH
Protein: Interleukin-1 receptor accessory protein-like 1-B (EC 3.2.2.6) (B6ZK77)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. During presynaptic differentiation may regulate both synaptic vesicle accumulation in axon terminals and subsequent axon terminal remodeling.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=May localize to the cell body and growth cones of dendrite-like processes. {ECO:0000269|PubMed:18657618}.
Interaction partners:
- Interleukin-1.
- Protein tyrosine phosphatase receptor type D.
- Mitogen-activated protein kinase 8
Sequence:
MRSRVPLQILLYAAVIRSLKVVSKRGSVDGCTDWSVDYLRYRVLLGEPVRIKCALFYGYIRANYTHAQSAGLSLMWYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQDSGHYSCVLRNSSYCMKVSMALTVAENSSGLCYNSKMRRLEKAELSKSKDILCPDIQDYTPAGSEPHVTWYKECRPKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQFGRFLVRRTTELTVTAPLTDKPPKILQPPEHKLSVMELQLGGPVNLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDETRIRESEIKMVREHLGEQEVSVSLTIDSLQEEDLGNYSCYVENGHGRRHAIIQLSRRELMYTVELAGGLGAILLMLIFLVSLYKCYRIELMLFYRNHFGSEDVDGENKDYDAYVSYTKVDPDQWSQETREEEHFALEILPDMLEKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVSGEIKVILIECSDLRGIMNYQEVEALKHTIKLLTVIRWPGPGSSKPNSRFWKQLQYEMPFRRPEPKLSHEQVLDASEQGPFGELQTVSALSMVSATSTAMATAHPDLRSGFHNTYNTQLRQKHYYRGYEYDIPSSGTLPPLATMGSQHTYCNIPMSLLNGQRPPGQPAHGQQQSLEEQQVNNALLPLLPRETSISSVIW
Protein: Coactosin (C4M4P4)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Actin-binding protein which is involved in F-actin stabilization. May play a role during phagocytosis and pseudopod formation by contributing to the maintenance of F-actin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31095644}. Cell projection, phagocytic cup {ECO:0000269|PubMed:31095644}. Cell projection, pseudopodium {ECO:0000269|PubMed:25210743}. Cell membrane {ECO:0000269|PubMed:25210743}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25210743}. Note=During phagocytosis, recruited to the phagocytic cup by 14-3-3 protein 3 (PubMed:31095644). Co-localizes with F-actin in pseudopods and in phagocytic cups. Localizes to the site of phagocytosis until scission of the cups occurs (PubMed:25210743). {ECO:0000269|PubMed:25210743, ECO:0000269|PubMed:31095644}.
Interaction partners:
Sequence:
MSGFDLSEVAGPVAEVIDDKNEEVEFVVFGVQTQPNKLVVDAKGKGGLEEVKAALKEDALQFAYYRTISGDEESKRVKFVFISWAGEGIKKPKLRAVMSILKGDVKNVINNFHIELHATSLDDLVEDEIAAKIKKAGGADYSFNTTSN
Protein: Palmitoleoyl-protein carboxylesterase NOTUM (EC 3.1.1.98) (Q8R116)
Organism: Mus musculus (Mouse)
Function: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9VUX3}.
Interaction partners:
- Proto-oncogene Wnt-1
- Protein Wnt-2
- Protein Wnt-3a
- Protein Wnt-16
- Protein Wnt-4
- Proto-oncogene Wnt-3
- Protein Wnt-11
- Protein Wnt-6
- Protein Wnt-7b
- Protein Wnt-5a
Sequence:
MGGEVRVLLLLGLLHWVGGSEGRKTWRRRGQQPPQPPPPPPLPQRAEVEPGAGQPVESFPLDFTAVEGNMDSFMAQVKSLAQSLYPCSAQQLNEDLRLHLLLNTSVTCNDGSPAGYYLKESKGSRRWLLFLEGGWYCFNRENCDSRYSTMRRLMSSKDWPHTRTGTGILSSQPEENPHWWNANMVFIPYCSSDVWSGASPKSDKNEYAFMGSLIIQEVVRELLGKGLSGAKVLLLAGSSAGGTGVLLNVDRVAELLEELGYPSIQVRGLADSGWFLDNKQYRRSDCIDTINCAPTDAIRRGIRYWSGMVPERCQRQFKEGEEWNCFFGYKVYPTLRCPVFVVQWLFDEAQLTVDNVHLTGQPVQEGQWLYIQNLGRELRGTLKDVQASFAPACLSHEIIIRSYWTDVQVKGTSLPRALHCWDRSFHDSHKASKTPMKGCPFHLVDSCPWPHCNPSCPTIRDQFTGQEMNVAQFLMHMGFDVQTVAQQQGMEPSKLLGMLSNGN
Protein: Opalin (Oligodendrocytic myelin paranodal and inner loop protein) (Transmembrane protein 10) (Q7M750)
Organism: Mus musculus (Mouse)
Function: Central nervous system-specific myelin protein that increase myelin genes expression during oligodendrocyte differentiation. Promotes oligodendrocyte terminal differentiation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18439243, ECO:0000269|PubMed:18490449, ECO:0000269|PubMed:30837646}; Single-pass type I membrane protein {ECO:0000255}. Note=In the CNS, enriched in the myelin paranodal and inner loop membranes, but not that of the PNS. Enriched in the leading edge of extending processes (PubMed:30837646). {ECO:0000269|PubMed:30837646}.
Interaction partners:
- Ermin
- Myelin-associated oligodendrocyte basic protein
- Myelin-oligodendrocyte glycoprotein
- Myelin-associated glycoprotein
- Plasmolipin
Sequence:
MSFSLNFTLPSNTTSSPVVTSAKATDCGPSIGLAAGIPSLLATALLVALLFTLIQRRRTIDDEPVEETEIPCEISELYDNPKISENPRRSPTHEMNPRGSQEGHIYVKTVSGSEEPLPDTYRPPEELERRRGLWWLVPSLSLE
Protein: Vacuolar protein sorting-associated protein 8 homolog (Q0P5W1)
Organism: Mus musculus (Mouse)
Function: Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Functions predominantly in APPL1-containing endosomes (By similarity).
Interaction partners:
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Transforming growth factor-beta receptor-associated protein 1
- Vacuolar protein sorting-associated protein 33A
- Vam6/Vps39-like protein
- Vacuolar protein sorting-associated protein 33B
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 45
- Vacuolar fusion protein CCZ1 homolog
Sequence:
METEPDQEHLDQNPCARTVEEELSKSFNLEASLSKFSCLDLDKELEFRSDLIDDKEFDIPQVDTPPTLESILNETDDEDESFVLEDPTLLNVDTIDSHSYDTSSVASSDSGDRANLKRKKKLPDSFSLHGSVMRHSLLKGISAQIVSAADKVDAGLPTAIAVSSLIAVGTSHGLALIFDQNQALRLCLGSTSVGGQYGAISALSINNDCSRLLCGFAKGQITMWDLASGKLLRSITDAHPPGTAILHIKFTDDPTLAICNDSGGSVFELTFKRVMGVRTCESRCLFSGSKGEVCCIEPLHSKPELKDHPITQFSLLAMASLTKILVIGLKPSLKVWMTFPYGRMDPSSVPLLAWHFVAVNNSVNPMLAFCRGDMVHFLLVKRDESGAIHVTKQKHLHLYYDLINFTWINSRTVVLLDSVEKLHVIDRQTQEELETMEISEVQLVYNSSHFKSLATGGNVSQALALVGEKACYQSISSYGGQIFYLGTKSVYVMMLRSWRERMDHLLKQDCLTEALALAWSFHEGKAKAVVGLSGDVSKRKAVVADRMVEILFHYADRALKKCPDQGKIQVMEQHFQDTVPVIVDYCLLLQRKDLLFGQMYDKLSENSVAKGVFLECLEPYILSDKLVGITPQVMKDLIVHFQDKKLLENVEALIVHMDITSLDIQQVVLMCWENRLYDAMVYVYNRGMNEFISPMEKLFKVIAPPLNAGKTLTDEQVVMGNKLLVYISCCLAGRAYPLGDIPEDLVPLVKNQVFEFLIRLHSVEASSEEEVYPYVRTLLHFDTREFLNVLALTFEDFKNDKQAVEYQQRIVDILLKVMVENSDFTPSQVGCLFTFLARQLAKPDNTLFVNRTLFDQVLEFLCSPDDDSRHSERQQVLLELLQAGGIVQFEESRLIRMAEKAEFYQICEFMYEREHQYDKIIDCYLHDPLREEEVFNYIHNILSIPGHSAEEKQSVWQKAMNHMEELVSLKPCKAAELVATHFSEQIEVVIGQLQNQLLLFKFLRSLLDPREGVHVNQELLQIPPHITEQFIELLCQFSPDQVIQTLQVLECYRLEETIQITQKYQLHEVTAYLLEKKGDAHGAFLLLLERLQSRLQEMTRQDENTKEDILLKGVEDTMVETIALCQRNSQNLNQQQREALWFPLLEAMMTPQKLSSSAAAPHPHCEALKSLTMQVLNSMAAFIALPSILQRILQDPIYGKGKLGEIQGLILGMLDTFNYEQTLLETTASLLNQDLHWSLCNLRASVSRGLNPKQDYCSICLQQYKRRQEMADEIIVFSCGHLYHSFCLQSKECTLEVEGQTRWACHKCSSSNKAGKLSENPSENKKGRITSSQVKMSPSYHQSKGDPPARKANSEPVLDPQQMQAFDQLCRLYRGSSRLALLTELSQNRGGDSCRPFAGPQSGPAFNSVFQKENFQLQLAPPPVAED
Protein: Protein cholesin (Q9BRJ6)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000269|PubMed:38503280}. Note=Secreted via exosomes, secretion is induced by feeding and cholesterol absorption. {ECO:0000269|PubMed:38503280}.
Interaction partners:
- Surfeit locus protein 6
Sequence:
MAKQKRKVPEVTEKKNKKLKKASAEGPLLGPEAAPSGEGAGSKGEAVLRPGLDAEPELSPEEQRVLERKLKKERKKEERQRLREAGLVAQHPPARRSGAELALDYLCRWAQKHKNWRFQKTRQTWLLLHMYDSDKVPDEHFSTLLAYLEGLQGRARELTVQKAEALMRELDEEGSDPPLPGRAQRIRQVLQLLS
Protein: Translocon-associated protein subunit beta (TRAP-beta) (Signal sequence receptor subunit beta) (SSR-beta) (Q54VI6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Translocon-associated protein subunit gamma
- Translocon-associated protein subunit alpha
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit alpha
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Uncharacterized protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Protein transport protein Sec61 subunit gamma
- J domain-containing protein
Sequence:
MNFKTVISLFLVLFVSFVYCENGAELLFHKKIVEGPVVGKELPIQFIIYNVGSEPAYDISFIDNDFSNAEFEFVSGSSEGKWETLAPNSQVQTNLTVIPKKSGIYSLTSTVLNYRKTQTSSEFTVSSAASYSGMYVESQADYEKRTSLLIKEWITFFVLCAGAIALPYSISTYYKKNYENGIKK
Protein: Putative GTP-binding protein 6 (Pseudoautosomal GTP-binding protein-like) (O43824)
Organism: Homo sapiens (Human)
Interaction partners:
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein bL36m
- Mitochondrial assembly of ribosomal large subunit protein 1
- Large ribosomal subunit protein uL3m
Sequence:
MWALRAAVRPGLRLSRVGRGRSAPRAAAPSCPARALAAVGRRSPGNLEGPWGGGRGLRADGGRSRTGDDEEEPEDADENAEEELLRGEPLLPAGTQRVCLVHPDVKWGPGKSQMTRAEWQVAEATALVHTLDGWSVVQTMVVSTKTPDRKLIFGKGNFEHLTEKIRGSPDITCVFLNVERMAAPTKKELEAAWGVEVFDRFTVVLHIFRCNARTKEARLQVALAEMPLHRSNLKRDVAHLYRGVGSRYIMGSGESFMQLQQRLLREKEAKIRKALDRLRKKRHLLRRQRTRREFPVISVVGYTNCGKTTLIKALTGDAAIQPRDQLFATLDVTAHAGTLPSRMTVLYVDTIGFLSQLPHGLIESFSATLEDVAHSDLILHVRDVSHPEAELQKCSVLSTLRGLQLPAPLLDSMVEVHNKVDLVPGYSPTEPNVVPVSALRGHGLQELKAELDAAVLKATGRQILTLRVRLAGAQLSWLYKEATVQEVDVIPEDGAADVRVIISNSAYGKFRKLFPG
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (F5H7P7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRRTKSAGLDLYLWRQHWPRRGKQPHEVGISNSYLVLEFERVYLDNLPSASMYERSYMHRDVITHVVCTKTDFIITASHDGHVKFWKKIEEGIEFVKHFRSHLGVIESIAVSSEGALFCSVGDDKAMKVFDVVNFDMINMLKLGYFPGQCEWIYCPGDAISSVAASEKSTGKIFIYDGRGDNQPLHIFDKLHTSPLTQIRLNPVYKAVVSSDKSGMIEYWTGPPHEYKFPKNVNWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVFDESLSMFTELQQMRQQLPDMEFGRRMAVERELEKVDAVRLINIVFDETGHFVLYGTMLGIKVINVETNRCVRILGKQENIRVMQLALFQGIAKKHRAATTIEMKASENPVLQNIQADPTIVCTSFKKNRFYMFTKREPEDTKSADSDRDVFNEKPSKEEVMAATQAEGPKRVSDSAIIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPKTDKPYEDVSIINITVK
Protein: H-2 class I histocompatibility antigen, K-K alpha chain (H-2K(K)) (P04223)
Organism: Mus musculus (Mouse)
Function: Involved in the presentation of foreign antigens to the immune system.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MAPCMLLLLLAAALAPTQTRAGPHSLRYFHTAVSRPGLGKPRFISVGYVDDTQFVRFDSDAENPRYEPRVRWMEQVEPEYWERNTQIAKGNEQIFRVNLRTALRYYNQSAGGSHTFQRMYGCEVGSDWRLLRGYEQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGDAERDRAYLEGTCVEWLRRYLQLGNATLPRTDSPKAHVTRHSRPEDKVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPSTVSNTVIIAVLVVLGAAIVTGAVVAFVMKMRRRNTGGKGGDYALAPGSQTSDLSLPDCKVMVHDPHSLA
Protein: ABC transporter B family member 5 (ABC transporter ABCB.5) (Q8T9W2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- ABC transporter B family member 2
- Probable cysteine desulfurase, mitochondrial
Sequence:
MYSINRIGIHGISNKILSRPKFFHSSSSIFSLNQNLNNFKNNNNYILNGYNKITHNHHHQTLFHRHYSNLKQEQENKQQNVGKNSETSPSSTTTTENITTATTATTKTDIKETQNSTMSMLKTVFKYLWPKDNNDSKIRIITSVLLLLSAKVLTVQIPFIFKDIVDSLTTTQSEMLTLPLGLLLAYGAVKITSNGFQELRQTIFSKVAHDAIRDVSCSTFKRLHQLDLTFHLSRQTGSLSRIIDRGGRGINFLLNSILFHVVPTAFEISLVSYVMYTTLGWEYSALSLATIAAYTVFTVKVTKWRTQFRVKMNKMDNEASNKMMDSLINFETVKYFNNDALEVERYHNYLKEYDKASLKTTSSLSFLNFGQALIFSLSMTAMMIMAAQGVVQGNLSVGDLVLVNGLLFQISLPLNFLGTVYREIKQSLVDMDHLFSLLNLNPKISDNKDSKPLKLENGTIVFRDISFKYNDSVQVLNNVSFECEGGKRIAIVGSSGSGKSTLLRLLYRFYDVSSGSIEIDGQDIRGIQLESLRKHIGVVPQDTVLFNDTIYYNIAYGNPNATKEQVENAARAAHIHEVILNMKNGYDTVVGERGLKLSGGEKQRVSIARAILKDSPIVFYDEATSSLDTEKEKLIMDALRELFKGRTTIMIAHRLSTIVDADEIIVLGTGGIILERGNHQQLLELEGKYRSMWLAQQ
Protein: DNA polymerase gamma, catalytic subunit (H0YCV2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XQDVMARACLQKLKGTTELLPKRPQHLPGHPGWYRKLCPRLDDPAWTPGPSLLSLQMRVTPKLMALTWDGFPLHYSERHGWGYLVPGRRDNLAKLPTGTTLESAGVVCPYRAIESLYRKHCLEQGKQQLMPQEAGLAEEFLLTDNSAIWQTVEELDYLEVEAEAKMENLRAAVPGQPLALDGNSCNVGSPFAKDFLPKMEDGTLQAGPGGASGPRALEINKMISFWRNAHKRI
Protein: Type I restriction enzyme EcoKI endonuclease subunit (EcoKI) (R protein) (EC 3.1.21.3) (P08956)
Organism: Escherichia coli (strain K12)
Function: The subtype A restriction (R) subunit of a type I restriction enzyme that recognizes 5'-AACN(6)GTGC-3' and cleaves a random distance away. The R subunit is required for both endonuclease and ATPase activities but not for modification. Has endonucleolytic activity that requires Mg(2+), ATP and S-adenosyl-L-methionine (SAM); ATP can be replaced by dATP, no tested molecule could substitute for SAM. Generates double-stranded DNA with no nicks, by cutting one strand then the other within a few seconds. Cleaves only non-methylated DNA, hemi-methylated and fully methylated DNA are not substrates. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage.
Interaction partners:
- Type I restriction enzyme EcoKI methylase subunit
- Type I restriction enzyme EcoKI specificity subunit
- Small ribosomal subunit protein uS12
- Type IV methyl-directed restriction enzyme EcoKMrr
- Type IV methyl-directed restriction enzyme EcoKMcrB subunit
- ATP synthase subunit beta
- ATP synthase epsilon chain
- ATP synthase subunit c
- Protein RecA
- ATP synthase subunit delta
Sequence:
MMNKSNFEFLKGVNDFTYAIACAAENNYPDDPNTTLIKMRMFGEATAKHLGLLLNIPPCENQHDLLRELGKIAFVDDNILSVFHKLRRIGNQAVHEYHNDLNDAQMCLRLGFRLAVWYYRLVTKDYDFPVPVFVLPERGENLYHQEVLTLKQQLEQQVREKAQTQAEVEAQQQKLVALNGYIAILEGKQQETEAQTQARLAALEAQLAEKNAELAKQTEQERKAYHKEITDQAIKRTLNLSEEESRFLIDAQLRKAGWQADSKTLRFSKGARPEPGVNKAIAEWPTGKDETGNQGFADYVLFVGLKPIAVVEAKRNNIDVPARLNESYRYSKCFDNGFLRETLLEHYSPDEVHEAVPEYETSWQDTSGKQRFKIPFCYSTNGREYRATMKTKSGIWYRDVRDTRNMSKALPEWHRPEELLEMLGSEPQKQNQWFADNPGMSELGLRYYQEDAVRAVEKAIVKGQQEILLAMATGTGKTRTAIAMMFRLIQSQRFKRILFLVDRRSLGEQALGAFEDTRINGDTFNSIFDIKGLTDKFPEDSTKIHVATVQSLVKRTLQSDEPMPVARYDCIVVDEAHRGYILDKEQTEGELQFRSQLDYVSAYRRILDHFDAVKIALTATPALHTVQIFGEPVYRYTYRTAVIDGFLIDQDPPIQIITRNAQEGVYLSKGEQVERISPQGEVINDTLEDDQDFEVADFNRGLVIPAFNRAVCNELTNYLDPTGSQKTLVFCVTNAHADMVVEELRAAFKKKYPQLEHDAIIKITGDADKDARKVQTMITRFNKERLPNIVVTVDLLTTGVDIPSICNIVFLRKVRSRILYEQMKGRATRLCPEVNKTSFKIFDCVDIYSTLESVDTMRPVVVRPKVELQTLVNEITDSETYKITEADGRSFAEHSHEQLVAKLQRIIGLATFNRDRSETIDKQVRRLDELCQDAAGVNFNGFASRLREKGPHWSAEVFNKLPGFIARLEKLKTDINNLNDAPIFLDIDDEVVSVKSLYGDYDTPQDFLEAFDSLVQRSPNAQPALQAVINRPRDLTRKGLVELQEWFDRQHFEESSLRKAWKETRNEDIAARLIGHIRRAAVGDALKPFEERVDHALTRIKGENDWSSEQLSWLDRLAQALKEKVVLDDDVFKTGNFHRRGGKAMLQRTFDDNLDTLLGKFSDYIWDELA
Protein: Auxin-responsive protein IAA26 (Indoleacetic acid-induced protein 26) (Phytochrome-associated protein 1) (Q8LAL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin response factor 18
- Auxin response factor 5
- Auxin response factor 12
- Auxin transporter protein 1
- Auxin response factor 9
- Auxin response factor 7
- Probable indole-3-acetic acid-amido synthetase GH3.1
- Auxin response factor 1
- Auxin response factor 3
Sequence:
MEGCPRNREIGPKLLDLIPQGRKWYQEDKNNTDQEKKLELRLGPPGGDEEDHSAIKKKNTEIRNIKKETEDKSFHCFNGNHFSPSNKTTSVPHISQKRTAPGPVVGWPPVRSFRKNLASTSSSKLGNESSHGGQINKSDDGEKQVETKKEGMFVKINMDGVPIGRKVDLNAYNSYEQLSFVVDKLFRGLLAAQRDISDGQGEEKPIIGLLDGKGEFTLTYEDNEGDKMLVGDVPWQMFVSSVKRLRVIKSSEISSALTFGCSKQEKMMH
Protein: Serine/threonine-protein kinase EDR1 (EC 2.7.11.1) (MAPKK kinase EDR1) (Protein ENHANCED DISEASE RESISTANCE 1) (AtEDR1) (Serine/threonine/tyrosine-protein kinase 10) (Q9FPR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: MAPKKK serine/threonine-protein kinase involved in the regulation of a MAP kinase cascade (probably including MPK3 and MPK6) that negatively regulates salicylic acid- (SA-) dependent defense responses, abscisic acid (ABA) signaling, and ethylene-induced senescence. Modulates also stress response (e.g. drought) signaling and cell death, in an ORE9-dependent manner. Functions at a point of cross talk between ethylene, ABA and SA signaling that impinges on senescence and cell death. On the other hand, it confers sensitivity to various pathogens such as the fungus E.cichoracearum, the oomycete H.parasitica and the bacteria P.syringae pv. tomato DC3000. Required for resistance to some hemibiotrophic/necrotrophic fungal pathogens (e.g. C.gloeosporioides, C.higginsianum and A.brassicicola) through the induction of defensin expression, probably by repressing MYC2, an inhibitor of defensin genes (PDFs). Together with KEG, may regulate endocytic trafficking and/or the formation of signaling complexes on trans-Golgi network (TGN)/ early endosome (EE) vesicles during stress responses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25747881}. Endosome {ECO:0000269|PubMed:25747881}. Nucleus. Endoplasmic reticulum. Golgi apparatus, trans-Golgi network. Early endosome. Note=Displays dynamic movement in cells with accumulation at the plasma membrane around pathogenic fungus penetration site (PubMed:25747881). Excluded from the nucleolus. Targeted to trans-Golgi network and early endosome vesicles via interaction with KEG. {ECO:0000269|PubMed:25747881}.
Interaction partners:
- Protein ENHANCED DISEASE RESISTANCE 4
- Regulatory protein NPR1
- Lipase-like PAD4
- Protein EDS1
- RING-H2 finger protein ATL1
- Protein ENHANCED DISEASE RESISTANCE 2
- Isochorismate synthase 1, chloroplastic
- F12F1.31 protein
- Aspartate--tRNA ligase 1, cytoplasmic
Sequence:
MKHIFKKLHRGGNQEQQNRTNDAAPPSDQNRIHVSANPPQATPSSVTETLPVAGATSSMASPAPTAASNRADYMSSEEEYQVQLALAISASNSQSSEDPEKHQIRAATLLSLGSHQRMDSRRDSSEVVAQRLSRQYWEYGVLDYEEKVVDSFYDVYSLSTDSAKQGEMPSLEDLESNHGTPGFEAVVVNRPIDSSLHELLEIAECIALGCSTTSVSVLVQRLAELVTEHMGGSAEDSSIVLARWTEKSSEFKAALNTCVFPIGFVKIGISRHRALLFKVLADSVRLPCRLVKGSHYTGNEDDAVNTIRLEDEREYLVDLMTDPGTLIPADFASASNNTVEPCNSNGNKFPTAQFSNDVPKLSEGEGSSHSSMANYSSSLDRRTEAERTDSSYPKVGPLRNIDYSSPSSVTSSTQLENNSSTAIGKGSRGAIIECSRTNMNIVPYNQNSEEDPKNLFADLNPFQNKGADKLYMPTKSGLNNVDDFHQQKNNPLVGRSPAPMMWKNYSCNEAPKRKENSYIENLLPKLHRDPRYGNTQSSYATSSSNGAISSNVHGRDNVTFVSPVAVPSSFTSTENQFRPSIVEDMNRNTNNELDLQPHTAAVVHGQQNDESHIHDHRKYTSDDISTGCDPRLKDHESTSSSLDSTSYRNDPQVLDDADVGECEIPWNDLVIAERIGLGSYGEVYHADWHGTEVAVKKFLDQDFSGAALAEFRSEVRIMRRLRHPNVVFFLGAVTRPPNLSIVTEFLPRGSLYRILHRPKSHIDERRRIKMALDVAMGMNCLHTSTPTIVHRDLKTPNLLVDNNWNVKVGDFGLSRLKHNTFLSSKSTAGTPEWMAPEVLRNEPSNEKCDVYSFGVILWELATLRLPWRGMNPMQVVGAVGFQNRRLEIPKELDPVVGRIILECWQTDPNLRPSFAQLTEVLKPLNRLVLPTPQ
Protein: Phosphoinositide phospholipase C 2 (EC 3.1.4.11) (Phosphoinositide phospholipase PLC2) (AtPLC2) (PI-PLC2) (Q39033)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. At physiological calcium concentration, the preferred substrate is phosphatidylinositol 4,5-bisphosphate versus phosphatidylinositol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11377433}; Peripheral membrane protein {ECO:0000269|PubMed:11377433}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Inositol polyphosphate multikinase beta
- Inositol polyphosphate multikinase alpha
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- Type I inositol polyphosphate 5-phosphatase 1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN2A
- Phosphatidylinositol 3-kinase VPS34
- Phosphatidylinositol 4-kinase beta 1
- Phosphatidylinositol-3-phosphatase myotubularin-1
- Phosphatidylinositol-3-phosphatase myotubularin-2
Sequence:
MSKQTYKVCFCFRRRFRYTASEAPREIKTIFEKYSENGVMTVDHLHRFLIDVQKQDKATREDAQSIINSASSLLHRNGLHLDAFFKYLFGDNNPPLALHKVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSNKDDIDVLHGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPVGESLKEFPSPNSLKRRIIISTKPPKEYKEGKDVEVVQKGKDLGDEEVWGREVPSFIQRNKSEAKDDLDGNDDDDDDDDEDKSKINAPPQYKHLIAIHAGKPKGGITECLKVDPDKVRRLSLSEEQLEKAAEKYAKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFDPKATLPVKTTLRVTVYMGEGWYFDFRHTHFDQYSPPDFYTRVGIAGVPGDTVMKKTKTLEDNWIPAWDEVFEFPLTVPELALLRLEVHEYDMSEKDDFGGQTCLPVWELSEGIRAFPLHSRKGEKYKSVKLLVKVEFV