wanglab/gogpt-training-data huggingface dataset:
Protein: Glutamate receptor ionotropic, kainate 5 (GluK5) (Excitatory amino acid receptor 2) (EAA2) (Glutamate receptor KA-2) (KA2) (Q16478)
Organism: Homo sapiens (Human)
Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > domoate > L-glutamate >> AMPA >> NMDA = 1S,3R-ACPD.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14511640}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q61626}; Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q61626}; Multi-pass membrane protein {ECO:0000255}. Note=Association with GRIK2 is required for its cell membrane localization and channel activity. {ECO:0000269|PubMed:14511640}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, kainate 3
- Disks large homolog 4
- G-protein coupled receptor 6
- Nuclear receptor subfamily 2 group E member 1
- Metabotropic glutamate receptor 7
- Glutamate receptor ionotropic, delta-2
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MPAELLLLLIVAFASPSCQVLSSLRMAAILDDQTVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPASASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFLISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLILRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYLGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNATTLDINLSQTLANKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWYNPHPCLRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWEGGRCPKEEDHRAKGLGMENIGGIFIVLICGLIIAVFVAVMEFIWSTRRSAESEEVSVCQEMLQELRHAVSCRKTSRSRRRRRPGGPSRALLSLRAVREMRLSNGKLYSAGAGGDAGSAHGGPQRLLDDPGPPSGARPAAPTPCTHVRVCQECRRIQALRASGAGAPPRGLGVPAEATSPPRPRPGPAGPRELAEHE
Protein: Sporulation protein kinase mde3 (EC 2.7.11.1) (Mei4-dependent protein 3) (O43077)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Protein kinase which is essential for spore formation.
Interaction partners:
- Sporulation protein kinase pit1
- DNA replication licensing factor mcm4
- Origin recognition complex subunit 4
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm7
- Cell division control protein 18
- Origin recognition complex subunit 3
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm6
- DNA replication licensing factor mcm2
Sequence:
MSNESIYSVLDLTQVIFEDRYLVKQKLGDGSFGTVYLAQRKEKNGLYETVAVKKLKNSSKPKPKHELLKLRESLALRKISKHPCLIDLLETFMDPYRNIFLVMEFMDCNLFQLFKRRQGRLFTKETAFNILLQIISGIEHIHKHGFMHRDIKPENILVKRISPKPISSRYSIKLGDFGLARPSVSSDPLTEYVSTRWYRAPELLLRSGSYNHSVDLYAFGCIVFEIYSLKPLFPGRNETDQLNRVCEILGNPGIDELDTLHYWSQAKELAKRLGFMLPPTKPYPIQKLLPQNCPEGHAKMIPCLLAWNPDVRPTAKYCKEVFFPLPPSASKSNSVPQKISNPKVEQNLGFPISREDKKSTRRVGWLKKNLSEFVSSVKSVFPDSHGSQPHVKTEKPINAKESTGHLANPIASSNVPAISLKPGELHESVFFSENEQIDYLLTSIDYLPSYKPPSNGSNIAINAFNETVGDRIPSSKDILITEKIPFKKENEIRDSIVPSCSQPDESNKEGVASCLLLQKSGMEMTSVLEYSTPNPAEVQNICNDHAKFETSKSLHLSSP
Protein: Uncharacterized protein C11orf52 (Q96A22)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGNRVCCGGSWSCPSTFQKKKKTGSQTRRTLKPQPQQLQQNLPKGHETTGHTYERVLQQQGSQERSPGLMSEDSNLHYADIQVCSRPHAREVKHVHLENATEYATLRFPQATPRYDSKNGTLV
Protein: Sponge, isoform D (Sponge, isoform H) (B7Z0R2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MWIPSNNKYGVAIHNWHGDVRFGLALDVGDSVDIVEECKHWYRGSCPRKSRAVGLFPKTYIHIKDLSKIDPVVAECTQVLREWSEIWKRLYVDREAYKFQTLRKVMFSILESRRELLSATMTQDQTLELQMVVVSKIDWGNRKLGLDLVPREGPLAVDPHGIGIVKLYNVHVSSADNAKASSSRGTLRRKTQRKILTHHLYFCMRDFGHRIGGDDAEVYFFLYDGSHMRPLSERFLVKISKDGFSNYIERLHSNCTVFTDLGAADLNEELHLVAVVMRVGKIIQSDSIKKIEKSGTLGHGPTFRRPFGVGVLSLGDIAHFDSSLEQSSDEREYNFKLFQCEEKDFHLLPELIIKKSSGKYSPIQASQGTQGIVVSLKLLHGGLGQARQEQPMLFQGSTITRKMGFPDVIMPGDVRNDLFLNLERGEFERGGKNTGKNILVTVVVLDVAGNVLTDCLWGASGMESQPQYRSMILYHQNAPSWNEMLRLSVPIDKFSTAHVRFEFRHCSTRDKTEPKLFAFSFARLMDTGGATLGDGLHELYVYKCEDPAKLQVANYLRLQCRPRDAQAKMDCGGCFSRSSKEVFVLRSLLCSTKLTQNADLLSLLQWRTYPETIQDSLTGVLRLNDEELVKFLQDVLDALFAMFSNEEGNSTQHSGLVFHVLVSIFSLLQSNKFQHFRPVMNEYIENHFAAALVYKGLITSVEHMAVFMTKAEHPDPFQKCFGSLEYIFKLLIQSRKLFARATGGQYEDSFKRDLHSLFTALNGMLAVPSYDVIIPTQEALLNSTGVVLEQLKDTLPAPELGMLARNMLDAIPRGAPIRLIQAKLHAVKDLVSGELFHEDDSRTVVLSVACKHLRMHLSRRDELRLCAEILSEILSQLYDLQKEQREKVTNTLQHDLDSLCKNILGILIRTISIIMEGSNAVLPQLVSCLLGLLQLLDETHYKRYWDELSPNKDPRDLKEFLSKSLLVYEELLTQDWHVFPNDWLVMKLAANDVLRMSLEEFAKPLVYRFLGPQAFDSQLWWSYFSLAVAFLTQPSLQLEQYREPKRLKILHSHGDMRVLMGFQILSMWSQLGEQKLHFIPSMVGPFLEVTLVPEPALRKATLSVFYDMMQCEQAARGSFRLVESELIDKLDLLISENKGDDEYRELFSTILLEKVQVENPNWKEAGIAFIASVTRLLERLLDYRSVMQGEENRDKRMTCTVNLLNFYKNEINRKEMYLRYIYKLHNLHLQAENYTEAGFTLKLYASMLSWDRETQSFAPFDNSGQPEWQRKERLYHEILKYFDKGKCWEKGIPLCKELAHLYETRRFDYNKLSEILIQEAKFFQNILTQLRPEPEYFRVGFYGMGLPLFVRNKQFVYRGLEYERIGAFTQRLQTEFPSAQILGNNSPPDNAILNAPDQYIQISNVRPVGDAQALKTAMVPVPEKIARFYEVNDVTRFIYDRPMYKGTVDKDNEFKSLWIERTILEIASPLPGILRWYEVKQKTMQELTPVEYACEIISNAGKELSELIVQYKRDPKRNINPFSMRLQGTIDANVMGGISKYQEAFFSEQFLKSPQGAGQQANVQRLKVLILEQIQILEQALELHGQLAPSGVQPLHNRLLERFSQLKQSLSGMGRLKRQHSESIVNTPLPPLPTEQRVAPATASSSLNANAHSNYVYDLDEIYTRPGDTVRPVDPLSSYQTLSKESLSIPLEDTAAPPVPNRPRSQNFIGNGSMDSPEVPPKRQPTLNSPNAPPLPPRGITPDKRASNPLIFNDFGSGDAVGRRHSQQQQQHGQKYSVVDISYDDPEADQQPHSLPPNFQDGSGGHLSVCFAPNDFRDSGISTTSSRELNHMNLNNLSEDSSSISTITVQHREHCRISSNGSLDYNAAASMNITQRESSTSSFDVEDFPVPPPPIPPKSLAVSSNGVNFSLDEAHSPHPSTQANTTQLNHIQNPNQNHSTNSHHHLQQQQNGDGDGYSTLQHPMNGLGLPTLPPPPSAVESPMPASAIASSTSSHQHDGGTF
Protein: Dibenzofuran dioxygenase alpha subunit (F2YMG2)
Organism: Rhodococcus sp. p52
Interaction partners:
Sequence:
MEATMLTVNDSGQLVSPNGQTPQAPPLNPALSSLLKELSESEGGLLDRRMFFDPEIYKVELERVFARSWSFLCHESQLAKAGDFFSTYIGADPVVVTRQRDGSISAVLNSCRHRGMKVCRADWGNAKAFTCTYHGWSYSTDGSLVSVPREEYAYYNEIDKSKLGLLRVPQVQSYKGLVFGCFDPEAPSLVDFLGDMTYYLDILLDRVDGGTEVISGVHKWKMRGNWKLAAEQFSGDNYHTISSHISVLLSEFPPEAADAFVNIDGLEINPAEGHGIGVMYSPTGAPFSAGSSEAILRWRDETRQESINRLGKERVEGMSWTHANVFPNFSYLHDSSVLRVWMPKSPTEMEAWSWCIVDKKAPQEVKNAWRTQAIRHFSPGGTWEQDDGENWSYCSGAGGQEGVVTRLSKLHVEMGVGHERSHPTLPGKVSHTYSEQNQCSLYRRWAEFMAAESWKDISVPVRTTEVIDRSDMAKAGES
Protein: LIM/homeobox protein Lhx5 (LIM homeobox protein 5) (Q9H2C1)
Organism: Homo sapiens (Human)
Function: Plays an essential role in the regulation of neuronal differentiation and migration during development of the central nervous system.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cyclin-K
Sequence:
MMVHCAGCERPILDRFLLNVLDRAWHIKCVQCCECKTNLSEKCFSREGKLYCKNDFFRRFGTKCAGCAQGISPSDLVRKARSKVFHLNCFTCMVCNKQLSTGEELYVIDENKFVCKDDYLSSSSLKEGSLNSVSSCTDRSLSPDLQDALQDDPKETDNSTSSDKETANNENEEQNSGTKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLGGRLDESEMLGSTPYTYYGDYQGDYYAPGSNYDFFAHGPPSQAQSPADSSFLAASGPGSTPLGALEPPLAGPHAADNPRFTDMISHPDTPSPEPGLPGTLHPMPGEVFSGGPSPPFPMSGTSGYSGPLSHPNPELNEAAVW
Protein: Ribosome-associated molecular chaperone sks2 (EC 3.6.4.10) (Heat shock cognate protein hsc1) (Hsp70 chaperone Ssb) (Suppressor of K-252a sensitivity protein 2) (Q10284)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone pss1 and fes1 act as nucleotide exchange factors that cause substrate release.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Associated with translating ribosomes. {ECO:0000250|UniProtKB:P11484}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Probable heat shock protein ssa2
- Protein psi1
- Mitochondrial protein import protein mas5
- Probable heat shock protein ssa1
- Zuotin
- Heat shock protein 90 homolog
- Heat shock protein sti1 homolog
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL24
Sequence:
MSEVYEGAIGIDLGTTYSCVAVWETANVEIIPNDQGARTTPSFVAFTETERLVGDAAKNQAAMNPRNTVFDAKRLIGRRYEDPETQKDIKHWPFKVIDNNGIPTIEVNYLGEKKQFTAQEISAMVLTKMKEISEAKLNKRVEKAVITVPAYFSDSQRAATKDAGAIAGLNVLRIINEPTAAAIAYGLDAKSDKPKNVLIFDLGGGTFDVSLLKIQGGVFEVLATAGDTHLGGEDFDNALVEHFIQEFKRKQKIDISDDPRALRRLRSACERAKRALSSVTQTTVEVDSLSNGIDFSSSITRARFEDINATTFKATIDPVAKVLKDSKVPKADVHDIVLVGGSTRIPKVQRLVSDFFDGRALNKSINPDEAVAYGAAVQAAVLTNKADSDKTQDLLLLDVVPLSLGVAMEGNVFGVVCPRNTPIPTIKKRTFTTVADNQTTVTFPVYQGERVNCAENEPLGEFQLTGIPPMPRGQAELEATFELDANGILKVTAVEKTTGRSAHIEITNSVGHLSSTKIQEMIENADKFKQQDKDFAKKLEAKSQLESYISNIETTISEPNVMMKLKRGDKSKIEAQLAECMSQLELEDTNTDALRKAELRLKRTVQKAFASLR
Protein: FI03211p (Spindle B) (O77135)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Rad51 recombinase D
- DNA repair protein RAD51 homolog 3
- Breast cancer type 2 susceptibility protein homolog
- DNA repair and recombination protein RAD54-like
- X-ray repair cross complementing 2
- DNA repair protein Rad51 homolog
- RecQ-like DNA helicase Blm
- Exonuclease 1
- Crossover junction endonuclease MUS81
- Meiotic recombination protein W68
Sequence:
MTNFLDQLPKHIREIAEQVNVLAPEEVLTTPKVRFLDTRQQSLHTIVRKCTPDDVRVLKDAAAKWLAEMPQSADSLFKPLVNVRWSRVSFGCSALDRCTGGGVVTRGITELCGAAGVGKTQLLLQLSLCVQLPRELGGLGKGVAYICTESSFPARRLLQMSKACEKRHPEMELNFLGNIFVENHIEAEPLLACVINRIPRLMQQHGIGLIIIDSVAAIFRLYNDYLERARHMRRLADALLSYADKYNCAVVCVNQVATRDGQDEIPCLGLQWAHLGRTRLRVSRVPKQHRMGDQLITVRKLEILYSPETPNDFAEFLITAEGVVNVPEPSVPSPPAKMRRL
Protein: Aminotransferase class I/classII large domain-containing protein (Q38BR5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRGCAKGIGAIFAADASNHVRGKSVNADESCFGVFQNMHINPFPVRAAIDIGTGGMITMVVARVDAAANAVRNFMYQTQLPLHLESVAAGLGDSSSFVLSEATRADIRNKMRVFHGALRRDNYDGLSERAAVMSWPLCEAADALALAEDLTREFKVDVRVLGKTFNVSMPFCGSVGLSANASQESMEVDVRRGRRCSNACTTAVTGGSESGSVQSFLHHTNRRRKERQAKLDSQREVRTVTDGDRVPNVPAAQQMEQLAFLAHAAVSKCVAPQRLLILAEDCHKGICVLGADTAEPEEVTDDETAANTKGINNNSKDAVTHQGVGSPTGLLVHALPVDLAMAHRLLVTTVQRRSQTTDEGANQRSPNPVLREEFRRLRCLLEEAMHHTLPQWVLDKSNTGGVICGSSFNGGVLNVAARIAQRSSVSLDHLETHAEMHYCGLTDVLMSVNYPNAATVIPCAALASALLRSLDAQRFEYLPEVHIPAALLLQPSLWTYTRRDQVRKALKQKPFYAAGSLRRTFQRPHARENPTAAPTASWQKNKEWNALSYDNSTKGT
Protein: Sphinganine C4-monooxygenase 1 (EC 1.14.18.5) (Sphingoid C4-hydroxylase 1) (Sphingoid base hydroxylase 1) (Q8VYI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in sphingolipid trihydroxy long-chain base (4-hydroxysphinganine) biosynthesis. Can use C18- and C20-sphinganine as substrates to produce C18- and C20-phytosphinganines (D-ribo-2-amino-1,3,4-trihydroxyoctadecane and -eicosane).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18612100}; Multi-pass membrane protein {ECO:0000269|PubMed:18612100}.
Interaction partners:
- 3-dehydrosphinganine reductase TSC10A
- 3-dehydrosphinganine reductase TSC10B
- Alkaline ceramidase
- Sphingosine kinase 1
- Delta
- Delta
- Sphingosine kinase 2
- Dihydroceramide fatty acyl 2-hydroxylase FAH2
- Neutral ceramidase 1
- Neutral ceramidase 3
Sequence:
MMMGFAVSDELLGTVAPIVVYWLYSGIYVALSSLESYRLHSKVEEEEKNLVSKSSVVKGVLVQQVVQAVVAILLFTVTGSDAEADKAQQFSFLVLARQFVTAMIVLDTWQYFMHRYMHQNKFLYKHIHSQHHRLIVPYAYGALYNHPVEGLLLDTIGGALSFLVSGMSPRTSIFFFSFATIKTVDDHCGLWLPGNLFHMVFKNNSAYHDIHHQLYGTKYNFSQPFFVMWDRILGTYMPYSLEKREDGGFEARPTKEFKDD
Protein: K+/Cl-Cotransporter (Potassium chloride cotransporter isoform a) (C0KDV0)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSEPRHTFLYVNPNNEAIRLLDIDEGAERIPLCEQHSPLALYEQDYDTQGQKIGTMLRKLSVYNATEATSVEADEKPKAAAAKMGTIMGVFLPCLQNIFGVLFFIRLAWIIGTAGVFQAFFVVLTCVSVTFLTSISLSAIATNGVVPSGGPYYMISRNLGPELGGAVGILFYLGTTIAASMYITGAIEILLLYIYPQAKLFDDIYHNFRVLGTVLLLILGLIVMAGVKFVNRCALPLVIVVILCILSAILGVFVRYDGSDSLKFCMVGDRPVDLSTYFEKTQVQPNCTADGLQDLFCSTNGTCDHYYDRMKNIKVWKSSGMPAIREERAIKGIASGVFFDNLWPKYLRAGEVLSKDRKDKGDLNRGGHPSYIYAESVTNFMILVGVFFPSATGIMAGSNRSGNLRDAAKSIPLGTLAAQNFSSFIYLLGVVLFGASVSEMFIRDKYGRSAMGKLIISEISWPFPQVILFGCFMSTAGAGMQSLTGAPRLLQAIAADDVLPFLKPFRKMDSRGEPIRAILLTLAICECGILIAVIENITALITQFFLMCYLGVNAACALQSLLKSPGWRPGFRYFHWSLSMIGAILCVAVMFISAWHFALFAIIIGAGVYKYIEYAGAEKEWGDGLRGLGLSAARFALLNLDDKPQHSRNWRPQLLVLAPDVESANTNGILSFVSQLKAGKGLTLVAHCMEGEYADNYLKAQAVQEKLKAVVKKNKIKGFCDVLVTSNVIEGISCLVQTSGLGGMRHNTVVLSWPNDWKAEQEWVVANKFVSAIRAISAAKCAIMVPKYAEKFPANGTKVSGFIDVWWVVHDGGLLMLLPFLLRQHKTWKNTTVRLFAIAQMEDNNVQMKTDLEKFLYHLRIDAAVNVIEMTDSDISDYTYERTMKMEERNQYLKNLNKSDRDKDIQNHLEIVTRERKLSRINEEAPAVVPEQRNLEVVDEEQEDGKSENGSAKIEHKGVRFSDDEDSKEVKVGNGTLERDREERQRKRRYNVHKMHTAVKLNELMRQKSSDAQLVFVNLPGPPDADSDSYYMDFIEALTEGLDRVLLVRGTGAEVVTIYS
Protein: Adenine phosphoribosyltransferase 1, chloroplastic (APRT 1) (AtAPT1) (EC 2.4.2.7) (P31166)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Contributes primarily to the recycling of adenine into adenylate nucleotides, but is also involved in the inactivation of cytokinins by phosphoribosylation. Catalyzes the conversion of cytokinins from free bases (active form) to the corresponding nucleotides (inactive form).
Subcellular location: [Isoform 1]: Plastid, chloroplast {ECO:0000269|PubMed:18431481}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
Interaction partners:
- Adenosine kinase 2
- Adenosine kinase 1
- AMP deaminase
- GMP synthase
- Guanylate kinase 2
- Guanylate kinase 3, chloroplastic
- Guanylate kinase 1
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- Inosine triphosphate pyrophosphatase
Sequence:
MQTIIISPLVSHRLCLARAVPCNRLLNNHHRAPPSIRLSNHRSTTSLRLFSSAAASRDSEMATEDVQDPRIAKIASSIRVIPDFPKPGIMFQDITTLLLDTEAFKDTIALFVDRYKDKGISVVAGVEARGFIFGPPIALAIGAKFVPMRKPKKLPGKVISEEYSLEYGTDTIEMHVGAVEPGERAIIIDDLIATGGTLAAAIRLLERVGVKIVECACVIELPELKGKEKLGETSLFVLVKSAA
Protein: MIP08680p (Phosphatidylinositol transfer protein) (Vibrator, isoform A) (Vibrator, isoform C) (Q9VDY8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQIKEFRVTLPLTVEEYQVAQLFSVAEASKENTGGGEGIEVLKNEPFEDFPLLGGKYNSGQYTYKIYHLQSKVPAYIRLLAPKGSLEIHEEAWNAYPYCRTIITNPKFMKDAFKIIIDTLHVGDAGDSENVHELTPDKLKVREIVHIDIANDPVLPADYKPDEDPTTYQSKKTGRGPLVGSDWKKHVNPVMTCYKLVTCEFKWFGLQTRVENFIQKSERRLFTNFHRQVFCSTDRWYGLTMEDIRAIEDQTKEELDKARQVGEVRGMRADAD
Protein: Serine/threonine-protein kinase SRK2A (EC 2.7.11.1) (Arabidopsis protein SK1) (OST1-kinase-like 7) (SNF1-related kinase 2.4) (SnRK2.4) (P43291)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein phosphatase 2C 37
- Protein phosphatase 2C 56
- Protein phosphatase 2C 16
- Protein phosphatase 2C 77
- Probable protein phosphatase 2C 24
- Probable protein phosphatase 2C 75
- Protein phosphatase 2C 3
- Probable protein phosphatase 2C 78
- Protein phosphatase 2C 7
- ABSCISIC ACID-INSENSITIVE 5-like protein 2
Sequence:
MDKYELVKDIGAGNFGVARLMKVKNSKELVAMKYIERGPKIDENVAREIINHRSLRHPNIIRFKEVVLTPTHLAIAMEYAAGGELFERICSAGRFSEDEARYFFQQLISGVSYCHAMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSLLHSRPKSTVGTPAYIAPEVLSRREYDGKMADVWSCGVTLYVMLVGAYPFEDQEDPKNFRKTIQKIMAVQYKIPDYVHISQDCKNLLSRIFVANSLKRITIAEIKKHSWFLKNLPRELTETAQAAYFKKENPTFSLQTVEEIMKIVADAKTPPPVSRSIGGFGWGGNGDADGKEEDAEDVEEEEEEVEEEEDDEDEYDKTVKEVHASGEVRIS
Protein: Carboxylesterase 20 (AtCXE20) (EC 3.1.1.1) (Q9LVB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carboxylesterase acting on esters with varying acyl chain length.
Interaction partners:
- DEAD-box ATP-dependent RNA helicase 7
- Probable carboxylesterase SOBER1-like
- AP2-like ethylene-responsive transcription factor BBM
- Non-specific lipid-transfer protein 2
- Strigolactone esterase D14
- Carboxylesterase SOBER1
Sequence:
MSEPSPIADPYAYLNIVNNPDGSITRDLSNFPCTAATPDPSPLNPAVSKDLPVNQLKSTWLRLYLPSSAVNEGNVSSQKLPIVVYYHGGGFILCSVDMQLFHDFCSEVARDLNAIVVSPSYRLAPEHRLPAAYDDGVEALDWIKTSDDEWIKSHADFSNVFLMGTSAGGNLAYNVGLRSVDSVSDLSPLQIRGLILHHPFFGGEERSESEIRLMNDQVCPPIVTDVMWDLSLPVGVDRDHEYSNPTVGDGSEKLEKIGRLRWKVMMIGGEDDPMIDLQKDVAKLMKKKGVEVVEHYTGGHVHGAEIRDPSKRKTLFLSIKNFIFSVL
Protein: Alpha-amylase 1 (AtAMY1) (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (Q8VZ56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses alpha-amylase activity in vitro, but seems not required for breakdown of transitory starch in leaves.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:17324226}.
Interaction partners:
- Isoamylase 3, chloroplastic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- Alpha-glucan phosphorylase 2, cytosolic
- Isoamylase 1, chloroplastic
- Alpha-glucan phosphorylase 1
- alpha-D-xyloside xylohydrolase
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
- Isoamylase 2, chloroplastic
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
Sequence:
MTSLHTLLFSSLLFFIVFPTFTFSSTLLFQSFNWESWKKEGGFYNSLHNSIDDIANAGITHLWLPPPSQSVAPEGYLPGKLYDLNSSKYGSEAELKSLIKALNQKGIKALADIVINHRTAERKDDKCGYCYFEGGTSDDRLDWDPSFVCRNDPKFPGTGNLDTGGDFDGAPDIDHLNPRVQKELSEWMNWLKTEIGFHGWRFDYVRGYASSITKLYVQNTSPDFAVGEKWDDMKYGGDGKLDYDQNEHRSGLKQWIEEAGGGVLTAFDFTTKGILQSAVKGELWRLKDSQGKPPGMIGIMPGNAVTFIDNHDTFRTWVFPSDKVLLGYVYILTHPGTPCIFYNHYIEWGLKESISKLVAIRNKNGIGSTSSVTIKAAEADLYLAMIDDKVIMKIGPKQDVGTLVPSNFALAYSGLDFAVWEKK
Protein: Uncharacterized protein orf187 (Q2F977)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MTRILQLQRSICITPEQWTGEGVSFIYGVWKRGRSRIDCYLKKWNGSDYPLASALTLLTTPTLCLLRFLIHVLMSISICMILILQSIYPLVLPIELLSMFFPFREMVAVPNAELAAVPNDQCLWGFPSLQLSPVSPMCWALNTFQDPVLVGRRFFTFVKVVLRWNRTTLLGFRVQRAKLKRISSPLL
Protein: Alanine and proline-rich secreted protein Apa (45 kDa glycoprotein) (45/47 kDa antigen) (Antigen MPT-32) (FAP-B) (Fibronectin attachment protein) (Immunogenic protein MPT32) (P9WIR7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A potent antigen in animals immunized with live bacteria, it induces a strong delayed-type hypersensitivity (DTH) in immunized animals. Elicits a mostly Th1 type of T-cell response in healthy humans; induces IFN-gamma production from CD4(+) and CD8(+) cells. Functions as an adhesin, binds to mouse macrophages via mannose residues. Might interact via host CD209.
Subcellular location: Secreted {ECO:0000269|PubMed:10531201}. Cell surface {ECO:0000269|PubMed:25359607}.
Interaction partners:
- Immunogenic protein MPT64
- Immunogenic protein MPT63
- Molybdenum import ATP-binding protein ModC
- PE-PGRS family protein PE_PGRS61
Sequence:
MHQVDPNLTRRKGRLAALAIAAMASASLVTVAVPATANADPEPAPPVPTTAASPPSTAAAPPAPATPVAPPPPAAANTPNAQPGDPNAAPPPADPNAPPPPVIAPNAPQPVRIDNPVGGFSFALPAGWVESDAAHFDYGSALLSKTTGDPPFPGQPPPVANDTRIVLGRLDQKLYASAEATDSKAAARLGSDMGEFYMPYPGTRINQETVSLDANGVSGSASYYEVKFSDPSKPNGQIWTGVIGSPAANAPDAGPPQRWFVVWLGTANNPVDKGAAKALAESIRPLVAPPPAPAPAPAEPAPAPAPAGEVAPTPTTPTPQRTLPA
Protein: Transcriptional adaptor 2B (D3YW26)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAELGKKYCVYCLAEEDMAAHVGASRTPQEVMEHYVSMYIHGNLGKACIPDTIPNRVTDHTCPSGGPLSPSLTTPLPPLDISVAEQQQLGYMPLRDDYEIEYDQDAETLISGLSVNYDDDDVEIELKRAHVDMYVRKLKERQRRKNIARDYNLVPAFLGKDKKEKEKTLKRKITKEEKELRLKLRPLYQFMSCKEFDDLFENMHKEKMLRAKIRELQRYRRNGITKMEESAEYEAARHKRERRKENKNLASSKRGKEDGKDSEFAAIENLPGFELLSDREKVLCSSLNLSPARYVTVKTIIIKDHLQKRQGIPSKSRLPSYLDKVLKKRILNFLTESGWISRDAS
Protein: Schnurri, isoform A (Schnurri, isoform B) (Schnurri, isoform C) (Schnurri, isoform E) (Q0E9C5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MENATTTTAKHYKTAGKQYKTNKVNNTRRATAAAAAAAAAAATTTVTTAATPTKKRTYRETATATIVTQRSTNKANIAAAIALAAATEATASASASATATATDATLTASKAAATAAATTDAASGNSNSSSKPSTSTRDKLGEVPLPTVDSNHIISNNNNNNNNNNTSNNNNNNHHSDNSISENNYEFKSRDKASLSDSKMTLQQMAAVSSNQEPVAPNVANTMSNSSIINSQQTTVNATPATDEAPLGDRSNISRYLHKKFKRLASTTEVDSWSATNGGGALQASGDAVRTTSLSSNSSLSPPPTTPLANGHHLMTQQQSHQQVQQQQQQQQTPPPSVAIHEFSANFVNSNHVNAIGHEESIISNSGYKAAGRTRTPLANSNSNTNSTSNSNSNHAANATLSPASFAQHQQLTQPTTVSPGIPGGAAAPNPACEKSGRYVCQYCNLICAKPSVLEKHIRAHTNERPYPCDTCGIAFKTKSNLYKHCRSRSHAARARGLEVPADADDGLSDQDAELSNSSSELPSRAGSPYEEPINSPTPSPSTLSAAKSAYIQQPPLPTYMQQLPLGSPAAGTLPPTTADNHHSATAQHRQSIDYKPYKPKFHNASLYSCSSKELQQQQQQLQIQQQQQQHQLAQQKLSIQLPLVQQPSLAHPTLSPSTQMKMKHHINSHQIQLQLQQQQSLLAQQSLLAAMPPGGVYYLGQPSYYNQDTAAAIHQHALAIQQFQIHLAQQQQQQQQQHPPLVKATPPMQQPPSLPPQQLVRANSQISSVATAPATPTPAANLSTFASSSGGKQVNVAKVQEHISKLISQNEAIVENKEILLQKKYPKQLSRSRSFNNANSNNASQHGSNASALHANNSQNNTNAQMPERETKVNLAQAIFQKQQHQLQQQQQQQITQQQQQQLEQQNYYTYIQQQQECQQQQLEPPNGVVKRNAYKPGVVMTTPVKQQQQLPPPPSPLPMQTMQYRQDPATPVTKIEQPTTAVPVMPLNLSAKPKPTLVTVPVSSLSTSSLAPTPTTSTNPTSSSKTAPPPAQVNNSIIKNLLLNARGLAVPIGEGDDAVYSCPICASEFRSADDLKLHNSTYCQDASSSAPMSPASSPFRSNSISLSLPELKSHMANSKNPLSLAKLAWSQLKTKRSSLVLSRLSAAQTPARTSTVTAPTVTASAPAPAVATVTAPSSAPAPQIEALRFVDAPLPSPGPLLGKTPLVDYAQQSTPRKAQDSVVITKMHEDRQFVIEAQPAKRIKTSDLVVASSSQQPTSFNFSFNNQNSSNSVPELQSSKEERLRRFTSSGGSMIPISECPDLDNSPKMIRTPLLSGGSFQDVSVKVNNETGSSSKERKLMALVSGSGLLGVSSGPQHFQFPPINSITAFNPLTLPPMSGGDKTTPVTPIPHVPGMPGPGSLTPQMPLLPPPPQQLQLPIPSSRGRSPNRKQPSPLLLGGGSGELKALSPFGGVQNVPSEFSRQPPTPAQRQALQWNSKEAPKKAPFNFLRMADNVKTTEPEVRHFNLENVISGKQQELPLTPLHVDTPNGNAPEETSPVASASASAKSKFLRPTSLPLKPGTFTPKRHHGITPTANTLPLISPETPRPSKSCVQLYLNGHAYTYLGLKCSTKMFYCTVNCPQPSYVAGMHKLSMYSVWQVCEENQPHPLGFKLKQVMALYDSRQRMLGNGSSTAMAGSGKLSYNLVASQQIVSSPSTSSTSSAFYQGPLKTPPTVTIAALSEANVAAKANEEAQAKKLETSPSGQPLVGGYESHEDYTYIRGRGRGRYVCSECGIRCKKPSMLKKHIRTHTDVRPFTCSHCNFSFKTKGNLTKHMQSKTHFKKCIELGINPGPMPPDSEFLDVDMDFDQQSSTSAGGRTSSMAGESDSDDYSDNESESSDTDESKSRQKEHEAARGLLSLSMTPPIPQSVSPYPQLQDTPLPAASPANSIGSSGSQPKRLVCSFTSPKPPFDYQKQEQYYSNPEESKPKRSVANEESAPMDLTKPRGSILLISPSPVSVPAHDLPKSQAQQMHDVIFGTSGNESGFMKTLISVSDKVRISAEMEEQAKHEAEGEDVQLQTYIKEHALHQAKIKQSQFSRSYLINTLYTAASPVMSSSSTLFTANSRPVMSVNEVPSIEVHEVKTPEAIESPRSAPEQAPVILAQIAQEENEEPNIAEPHNANLPAAVQQPDVNEFTGVLGNPTAPPTSSVTATSVSTTTAAPVAPSSTANSTQPAQRTVIVGEDGFKSSTPTSKSGDLQHVSYGRGVPPAPIAGDARPTCTMCSKTFQRQHQLTLHMNIHYMERKFKCEPCSISFRTQGHLQKHERSEAHKNKVMMTSTFGVPTTSNPRPFECTDCKIAFRIHGHLAKHLRSKTHVQKLECLQKLPFGTYAEIERAGISLTEIDTSDCENSLISLKLLAQKLQEKDPGKLSSYTTPSGMMQLAQDAAGPVSQDSASEDGFSAAIASAIASLDNDSAGNTPKRASSMSEDETVANGLNHSLKRRLPGSFSSTGEESDNPPESSGEKRARSGQELPVPVAVPVAASAAASN