wanglab/gogpt-training-data huggingface dataset:
Protein: Importin subunit alpha-7 (Importin alpha-S2) (Karyopherin subunit alpha-6) (O35345)
Organism: Mus musculus (Mouse)
Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular location: Cytoplasm.
Interaction partners:
- Importin subunit beta-1
- Importin subunit alpha-5
- Importin subunit alpha-1
- Importin subunit alpha-4
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran, testis-specific isoform
- Exportin-5
- Importin subunit alpha-8
- Importin subunit alpha-3
Sequence:
METMASPGKDNYRMKSYKNNALNPEEMRRRREEEGIQLRKQKREQQLFKRRNVELINEEAAMFDSLLMDSYVSSTTGESVITREMVEMLFSDDSDLQLATTQKFRKLLSKEPSPPIDEVINTPGVVDRFVEFLKRNENCTLQFEAAWALTNIASGTSQQTKIVIEAGAVPIFIELLNSDFEDVQEQAVWALGNIAGDSSLCRDYVLNCSILNPLLTLLTKSTRLTMTRNAVWALSNLCRGKNPPPEFAKVSPCLPVLSRLLFSSDSDLLADACWALSYLSDGPNEKIQAVIDSGVCRRLVELLMHNDYKVASPALRAVGNIVTGDDIQTQVILNCSALPCLLHLLSSSKESIRKEACWTISNITAGNRAQIQAVIDANIFPVLIEILQKAEFRTRKEAAWAITNATSGGTPEQIRYLVSLGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQESKRSGSGVNPYCGLIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGVEDDDSSLAPQVDETQQQFIFQQPEAPMEGFQL
Protein: WD repeat-containing protein 27 (A2RRH5)
Organism: Homo sapiens (Human)
Interaction partners:
- Dynein light chain Tctex-type protein 2
Sequence:
MENPQDIFSSNGGCLSDIVIEKYLVESKESVSHVQLACSMQDCAFPLDGTELCIWNTKDPSHQLLILRGHHQPITAMAFGNKVNPLLICSASLDYVIMWNLDECREKVLQGLVPRGTVMGSLLGKVLCLQLSLDDHVVAVCAGNKIFMLDIETQAVRAELQGHLGPVTAVEFCPWRAGTLISASEDRGFKVWDHCTGSLIYSSSVLSAYPLLSLFIDAESRQLVTGCADGQLWIFSLMDGHHYRRVARVDLRKKTETFSTRRVKSGLCSQPEESQLPSTSALGKGEQVEVTFPVLRLAPCDLSLIPNSACGCLSSENTRCVWIGSSVGLFVFNLANLEVEAALYYKDFQSLSILLAGSCALRNRTADQKVLCLLASLFGGKIAVLEINPAALVRAQQCPSMGQSLSVPASSCVLPTSPLYLGIAKEKSTKAASEQRRAARNVMKDQRLVFHSKVRSSGYASAPHVTMFSPKTNIKSEGKGSSRSRSSCAREAYPVECAVPTKPGPQVAAAPTCTRVCCIQYSGDGQWLACGLANHLLLVFDASLTGTPAVFSGHDGAVNAVCWSQDRRWLLSAARDGTLRMWSARGAELALLLGKDMFSKPIQSAQFYYIDAFILLSSGPEFQLLRYHIDTCKDEIKRYKQKSKSKLICRLSTTGAVDMTSLSAVNDFYSHIVLAAGRNRTVEVFDLNAGCSAAVIAEAHSRPVHQICQNKGSSFTTQQPQAYNLFLTTAIGDGMRLWDLRTLRCERHFEGHPTRGYPCGIAFSPCGRFAACGAEDRHAYVYEMGSSTFSHRLAGHTDTVTGVAFNPSAPQLATATLDGKLQLFLAE
Protein: Cellulosome anchoring protein cohesin region (A3DF10)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Cellulosomal-scaffolding protein A
- Cellulosome-anchoring protein
- Ig domain protein group 2 domain protein
- Arabinogalactan endo-beta-1,4-galactanase
- Endoglucanase D
- Beta-xylanase
- Copper amine oxidase-like domain-containing protein
- Copper amine oxidase-like domain-containing protein
- Copper amine oxidase-like domain-containing protein
- Copper amine oxidase-like domain-containing protein
Sequence:
MRKKKRLISLLLAVFIAVACLPAGIARADKASSIELKFDRNKGEVGDILIGTVRINNIKNFAGFQVNIVYDPKVLMAVDPETGKEFTSSTFPPGRTVLKNNAYGPIQIADNDPEKGILNFALAYSYIAGYKETGVAEESGIIAKIGFKILQKKSTAVKFQDTLSMPGAISGTQLFDWDGEVITGYEVIQPDVLSLGDEPYETPGTDIPISDNPAATPSSTPSVTPSPEVKPTQTPSPAENSAKVELEPVLDNATGEAKAAIDEEKLNKALDEAKKSEDDKLVELNIKKVENADAYIQQLPAKFLIKSDAEYKLRIATEQGIIEVPANMLNTADISKLVKNDSVVEFVIRKVKVDELGAELKEKIGNRPVIDISVVVDGKKVEWSNYKAKVKISIPYKPDAKELENHEHIVVLHIDDAGKAVSVPSGKYEPSLGVVTFETNHLSKYAVSYVYKTFADIGSYAWAKKQIEVLASKGVINGTSDTTFTPQADITRADFMILLVKALGLTAEVTSNFDDVSEKDYYYEYVGIAKELGITTGVGNNKFNPKAKITRQDMMVLTTNALRIAGKISSTGTRADVERFSDKDQIASYAVEGVATLVKEGIVVGSGDIINPRGNASRAELAAIIYKIYYK
Protein: C2 domain-containing protein (PfDOC2) (PfDOC2.1) (Q8I4Z1)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000269|PubMed:24992295}; Peripheral membrane protein {ECO:0000305|PubMed:24992295}. Note=Localizes in a punctate manner reminiscent of vesicles. {ECO:0000269|PubMed:22246776}.
Interaction partners:
Sequence:
MILDKFKNIVNLSNSNTEKEEGKNAEINENNDPNTQLAHEPSIVEADEKTFFDEMLGAPQYTYDEFLQVLKNPIEERGDTEDMKKHWGYPRRWKVILWDLHIQNYMNNDFNAFVDFDFGGNREECRIQRGSTMKIYAKGKTKNCLRTPVVTNVATEQKKNMNFRNVFEYRGSYLDLENEKLRIRVWEYKQFTLNKLEGIYEEPLLSFAVGEIYNETTLYKFIKDSRVKRCRLYFQLYFQELYDFELSFLNWSFSDLLSSSYIQAKSYNYLSNKNNVKKRYIDDTSCNIFPHMCKNFKRFHKKKIYRKVRNYDIDKNFSFNTALSDDSDERKNKNDRTIKNLEKLFVRNLTLMQNIEENEDMSYKNLQNINLPNPRVTITLSHTPKGHEGLNIISIEQKSIRFPIWENLGEIYFRGTLRDLDVSYLNIKVEDMSAPKSAREIGTCQISLKGIVDYPYVMHELEAPSWLVKEAKYEGWENKLNEWKLGTVEGKVIINRVPRYRQRGDIYHIDSKQPYLIVHIFNIDKIITVDNIKELDTYVEVSFDETSRRTRLMKKTLSPNYDSQISIPLRFNNKNDINYENLSKKGLIYIDVWGKSEDIVYIGGISISPYEIFFNEKNVRRNKTKLEHIDLETNVKITYDTVVYRGCKKLCFLHDDQRMSNIHFSIWTYPDILGNSTNQKKIVAPVSFNTTMNFPIKLAEKYNKLKKLFMEVLKTIKSIPENCTDVNTSTRFYNYELINQRKEKHFLPTLITSIKSPYCAESMNAIFHYVRCIPFIHKKENIIFTPDFTLQLKGGNALDHSLLLCSLFLGIPVLAFVCFGTLWDKQKHSWVATFEYNDEKNYGIVKFWETTTGNVYILKKRFIDHNRLKGLELKLKESKYKSHLRNGFLQRYENNTDINYIKEQTKRHIKQLFKNRINDIPIGGPSLPYKTIDLIFNHKNIYVNLQHSSPLNIWYDYWKFDFWFPFSSIEYNLQPSFTIKSFTHKMEDMELDKIAKELRTNIEKNINIYRASRNLSTRWNRDETLEIFLQVGLELLHQLNTSRKEDVLLAKLKIEDWKKALYHKVPQSHRLLGFPYHFNTYKSKFISDKLISTLAILESRDRSLCLSLAVCLYSLPGNFISCYIYIITCVKITQRELRKMEIIKEKAQRMAEIKNSQKKKKSSDDQNIDIKTMDDVEEKETFSSTNLDDTLHDEHTDIDTEKKKHEKDNYKNKKIKNTKLKDANIDNEEKDDHHHITDKKVSKSSDLIHSFDKNDISKNTFDKEEFINNLDKDKKYSSFKKGNVVNKKVSIKNEPSINIYEDHKIYDDENISNNIDNMENNQDEIYNLRQGKTIINEFQQVKKPQKYTINEKRDDIKTKKKRSKEKKKQDKLEFEKLIQSNAYFEQEKKKLQEDIKKLEKDKEQFQKEKIRREEKEKQLLLEEKIKLQKEKELFENEKLERKMSYMLKINELEKKKNERNKMEKSYKRMIQKDKEKKKKKESRDKIRRGEEEKMSADENMKEEQKMREEQKVGEEQKVGEEQKVGEEQKLREEQKMREEQKMREEQKMREEQKMREEQKVREEQKMREEQKMREEQKMREEQKVREEQKLREEQKMREEQKMREEQKMREEEKIREEEQMKREKKMRREEKKKRVQEPIKIDEIQVYDIIKNEKMKKKEEKEEKKRKKKKEDIEDKYKIGKEASLDENNNERQIKSKNIQEISDYEYKNIKENKNLNKFDEKLDLNQIYSKASNFYDNQEKKRRTIKVHANRKENSDSTFSHIDDSIKNKKEYLEDSNIARYLYEKRKHDLIGKGNYNFDEPHYGKKMNNVAYQDIKGSNLFKGFIEEPSSKKSPQKKKIVIVRKN
Protein: Histidine kinase/HSP90-like ATPase domain-containing protein (A0A060XFW6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Stress-induced-phosphoprotein 1
- Stress-induced-phosphoprotein 1
- TBC1 domain family member 7
- SGS domain-containing protein
- Uncharacterized protein
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Prostaglandin E synthase 3
- Prostaglandin E synthase 3
- Prostaglandin E synthase 3
Sequence:
MDTSAQSNTQEGIKISEIPFYFPASESRGDLRYWQHFIQEKSTEQIKMPEEMRQEEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPTKLDNGKELKIDVIPNVEERTLTLIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAERVTVITKHNDDEQYIWESSAGGSFTVKVDTGEPMLRGTKVILHMKEDQTEYVEEKRVKEVVKKHSQFIGYPITLFVEKEREKEISDDEAEEEEKAEKEEKEEKEAEDKPKIEDVGSDDEEDSKDKDKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITMEEYGEFYKSLTNDWEEHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCEELIPEYLNFVRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCMELFGELAEDRENYNKFYDGFSKNLKLGIHEDSQNRKKLSELLRYHSSQSGDELTSLTEYLTRMKDNQKSIYYITGESKDQVANSAFVERVRKRGFEVLYMTEPIDEYCVQQLKEFDGKTLVSVTKEGLELPEDEEEKKKMDEDKTKFENLCKLMKEILDKKVEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKADLDKNDKAVKDLVILLFETALLSSGFSLDDPQTHSNRIYRMIKLGLGIDDDEVIPEEPTSAPAPDEIPPLEGDDDASRMEEVD
Protein: Spondin-1 (F-spondin) (Q7KN04)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- GH18858p
- Glutactin
- FI04421p
Sequence:
MGQSLPLLIRLIVVIWLTISMVTACPRAPTHLNHGRRTRGDNGYKLIVADGPNGYVPGKTYNLLLLGSRTHLKVQHFTHFTITAEAHTGARRPQAASPRRVGRFQLFSDSLTQFNDRCVNTVSEADDLPKTEVQVMWVAPESGSGCVSLSAMVYEGPRAWFADDGNLSTVICERKPDAAAAQKECCACDEAKYSFVFEGIWSNETHPKDYPFAIWLTHFSDVIGASHESNFSFWGENHIATAGFRSLAEWGSPAALETELRANGPKLRTLIKAAGLWYPNVNQNTSSKFRVDRKHPKVSLVSMFGPSPDWVVGISGLDLCTEDCSWKESMDFDLFPWDAGTDSGISYMSPNSETQPPERMYRITTMYPEDPRAPFYNPKSREMTPLAKLYLRREKIVSRNCDDEFLQALQLEVSDDAEEQDTRAECRVGDYSAWSPCSVSCGKGIRMRSRQYLYPAAADQNKCARQLVAKEMCVAAIPECADGPAQSKDRDDDEGENLANSQSLVGSNGEGAGLCKTSPWSVWSECSASCGIGITMRTRTFVNHLGRKRCPHITIVEKNKCMRPDCTYEQVELPDPQCPTSQWSDWSPCSSTCGRGVTIRTRLLLLENGPDKESCTQRMELHQQKECVNPIDCHINAEQAKDICVQAPDPGPCRGTYMRYAYDPQNQHCYSFTYGGCRGNRNNFLTENDCLNTCNVLRSPYSSRVDQPRACVLSDWSVWSPCSVSCGVGVSESRRYVVTEPQNGGQPCSKRLVKSRSCAMPAC
Protein: Glutathione S-transferase P 1 (EC 2.5.1.18) (GST class-pi) (GST-Pi) (XlGSTP1-1) (Q8JFZ2)
Organism: Xenopus laevis (African clawed frog)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Highly active towards 1-chloro-2,4-dinitrobenzene and organic isothiocyanates, but shows no detectable activity towards 1,2-dichloro-4-nitrobenzene, p-nitrobenzylchloride, trans-4-phenyl-3-buten-2-one (tPBO) and ethacrynic acid. May be associated with cellular proliferation.
Subcellular location: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000250}.
Interaction partners:
Sequence:
MPGYVLTYFPVRGRAEPIRLLLADQGISWKEDEVQIPDWFSGKDARKKEAVFGQLPQFQDGDYVLYQSNSILRYLGNKHGLTGANDEERGHIDMVNDGVEDLRQKYGRLIFFEYETGKDKYLKELPSQLDFFERILSKNANGSKFVVGQKISFADYNLLDILQCHLDLCSKSLSAYPLLTAYVERLVARPKISEYLKSDARNKRPITPKHKK
Protein: Attractin (Protein mahogany) (Q9WU60)
Organism: Mus musculus (Mouse)
Function: Involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines (By similarity). May play a role in melanocortin signaling pathways that regulate energy homeostasis and hair color. Low-affinity receptor for agouti. Has a critical role in normal myelination in the central nervous system (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O75882}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75882}.
Interaction partners:
- E3 ubiquitin-protein ligase MGRN1
- Agouti-signaling protein
- Melanocortin receptor 4
Sequence:
MVAVAAAAATEARLRGSTTATAAPAGRKGRQHRPCTATGAWRPGPRARLCLPRVLSRALPPPPLLPLLFSLLLLPLPREAEAAAVAAAVSGSAAAEAKECDRPCVNGGRCNPGTGQCVCPTGWVGEQCQHCGGRFRLTGSSGFVTDGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATECSWDHLYVYDGDSIYAPLIAAFSGLIVPERDGNETAPEVTVTSGYALLHFFSDAAYNLTGFNITYNFDMCPNNCSGRGECKSSNSSSAVECECSENWKGESCDIPHCTDNCGFPHRGICNASDTRGCSCFPHWQGPGCSIPVPANQSFWTREEYSDLKLPRASHKAVVNGNIMWVVGGYMFNHSDYSMVLAYDLTSREWLPLNHSVNSVVVRYGHSLALHKDKIYMYGGKIDSTGNVTNELRVFHIHNESWVLLTPKAKDQYAVVGHSAHIVTLASGRVVMLVIFGHCPLYGYISVVQEYDLEKNTWSILHTQGALVQGGYGHSSVYDDRTKALYVHGGYKAFSANKYRLADDLYRYDVDTQMWTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDTSMSHGAKCFSSDFMAYDIACDRWSVLPRPELHHDVNRFGHSAVLYNSTMYVFGGFNSLLLSDVLVFTSEQCDAHRSEAACVAAGPGIRCLWDTQSSRCTSWELATEEQAEKLKSECFSKRTLDHDRCDQHTDCYSCTANTNDCHWCNDHCVPVNHSCTEGQISIAKYESCPKDNPMYYCNKKTSCRSCALDQNCQWEPRNQECIALPENICGNGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQSSQSMSKLTLTPWVGLRKINVSYWCWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCERPANHSAKQCRTPCALRTACGECTSSSSECMWCSNMKQCVDSNAYVASFPFGQCMEWYTMSSCPPENCSGYCTCSHCLEQPGCGWCTDPSNTGKGKCIEGSYKGPVKMPSQASAGNVYPQPLLNSSMCLEDSRYNWSFIHCPACQCNGHSKCINQSICEKCEDLTTGKHCETCISGFYGDPTNGGKCQPCKCNGHASLCNTNTGKCFCTTKGVKGDECQLCEVENRYQGNPLKGTCYYTLLIDYQFTFSLSQEDDRYYTAINFVATPDEQNRDLDMFINASKNFNLNITWATSFPAGTQTGEEVPVVSKTNIKEYKDSFSNEKFDFRNHPNITFFVYVSNFTWPIKIQIAFSQHSNFMDLVQFFVTFFSCFLSLLLVAAVVWKIKQSCWASRRREQLLREMQQMASRPFASVNVALETDEEPPDLIGGSIKTVPKPIALEPCFGNKAAVLSVFVRLPRGLGGIPPPGQSGLAVASALVDISQQMPIVYKEKSGAVRNRKQQPPAQPGTCI
Protein: NADH-ubiquinone oxidoreductase chain 6 (EC 7.1.1.2) (NADH dehydrogenase subunit 6) (P03923)
Organism: Homo sapiens (Human)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03924}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- Acyl carrier protein, mitochondrial
Sequence:
MMYALFLLSVGLVMGFVGFSSKPSPIYGGLVLIVSGVVGCVIILNFGGGYMGLMVFLIYLGGMMVVFGYTTAMAIEEYPEAWGSGVEVLVSVLVGLAMEVGLVLWVKEYDGVVVVVNFNSVGSWMIYEGEGSGLIREDPIGAGALYDYGRWLVVVTGWTLFVGVYIVIEIARGN
Protein: Prefoldin subunit 4 (Q387H0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Prefoldin subunit, putative
- Prefoldin, putative
- Prefoldin subunit 3
- Prefoldin subunit 2, putative
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit epsilon
- CCT-beta
- T-complex protein 1 subunit delta
Sequence:
MSLLKGKEVEVTQDDQRRICIFARMHRRRKELTATITRLKEQAAKLSDASDELMIADGAMYLFGETFVAIDNDEAGEWLAKEQAQLQRDQETTEEELKLVESQLSDLKAKLYASLGSQVYLEDE
Protein: AP-1 complex subunit mu-1 (Adaptor-related protein complex 1 subunit mu 1) (A0A0R4IRS1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
- AP-1 complex subunit gamma
- AP complex subunit beta
- AP-1 complex subunit gamma.
- AP complex subunit sigma
- AP complex subunit sigma
- AP complex subunit beta
- AP complex subunit sigma
- AP complex subunit beta
- AP-4 complex subunit epsilon
- AP-3 complex subunit sigma-2
Sequence:
MSASAVYVLDLKGKVLICRNYRGDVDMSEIEHFMTLLMDKEEEGTLSPILAHGGVRFMWIKHNNLYLVATSKKNACVSLVFSFLYKIVQVFSEYFKELEEESIRDNFVIIYELLDELMDFGYPQTTDSKILQEYITQEGHKLDTGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIESVNLLVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFENTGRGKSKSVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMIKAKSQFKRRSTANNVEIHIPVPTDADSPKFKTTVGSVKWVPENSEIVWSIKSFPGGKEYLMRAHFGLPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLRTQ
Protein: Probable UDP-arabinopyranose mutase 5 (EC 5.4.99.30) (Reversibly glycosylated polypeptide 5) (AtRGP5) (UDP-L-arabinose mutase 5) (Q9FFD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21478444}. Golgi apparatus {ECO:0000269|PubMed:21478444}. Note=Localized predominantly in the cytosol.
Interaction partners:
- UDP-sugar pyrophosphorylase
- Major facilitator superfamily protein
- UDP-glucose 6-dehydrogenase 3
- 60S ribosomal export protein NMD3
- Lysine-rich arabinogalactan protein 17
- 2-oxoglutarate
- UDP-arabinopyranose mutase 2
Sequence:
MSLAEINKNEVDIVIGALNADLTQFLTSWRPFFSGFHLIVVKDPELKEELNIPEGFDVDVYSKTDMEKVVGASNSTMFSGYSCRYFGYLVSKKKYIVSIDDDCVPAKDPKGFLVDAVTQHVINLENPATPLFFNTLYDPYCEGADFVRGYPFSLRSGVPCAASCGLWLNLADLDAPTQALKTEKRNTAYVDAVMTVPAKAMLPISGINIAFNRELVGPALVPALRLAGEGKVRWETLEDVWCGMCLKHISDHLGYGVKTGLPYVWRNERGDAVESLRKKWEGMKLMEKSVPFFDSLKLPETALKVEDCVIELAKAVKEQLGSDDPAFTQAADAMVKWVQLWNSVNSSA
Protein: Disco-related protein (Q9GSZ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
HAMGGSGAGSGAGVGALELKHGQDYLQRSYLDAGRFEGQRRKLAMENEHTEDEDDDEILEVGIHMAGDDDDDEADGDEDEDDDDPDGIVVVGDEIDSMPLDHENDNDNENENDESDERSTSAVSSLSQTKEQSSPGKVVQSGLEECHTYAHAHAHALTHGHAHSLGHAHALAQMAANKRKRKSQNPVRCPVQSDENSGENSIDYDVAADLSIKKVRLPAQAAASAKESEVGESTKSIPSPPLTPYGDLRPVGLCIKTEQDHEHELDQEQGQERKREQEQEPEPDTVATASKSEMKLEEQETRPADKEDDNEEDEQVSPPVVTTLDLSRAAAAIKLEPLEEINYEADENRYVRIKQELMGGDESLAEESSDKTANHNNNNNNNNNININNSVRRESDNGLEASELEEREPEPETEIEPEHEHEHEPEPETEVEVPEVPIDKENPLKCTACGEIFQNHFHLKTHHQSVHLKLHHKCNIDGCNAAFPSKRSRDRHSSNLNLHRKLLSTSDDHGLLHAPVMPATDPLLELMSLNLNNNKSGFHHSAMVGSSAGGAGGVNPAAVGSIQAEILARICAGAHAHGLNVPLCFEALQHRFAVGHGHAGYPLIAGDGSPPSPRLFLNHGGGASPLLFAGLPRMPRFPQLTPHMLAASAGNTAAAAAAAAAAAAGMGGLSPFCRRTSSDSNSQHSITPPPKRSRSQSKSPDHCVHPAHAGDTTGITEDSGQRQSPDRIS
Protein: Soluble inorganic pyrophosphatase 4 (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase 4) (PPase 4) (Q9LFF9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the irreversible hydrolysis of pyrophosphate (PPi) to phosphate. The MgPPi(2-) complex binds to the enzyme only after a free Mg(2+) ion has bound. No activity with glycerol-3-phosphate, glucose-6-phosphate, p-nitrophenylphosphate, ADP, NADP(+), NAD(+),NADH, NADPH or phosphoribosyl pyrophosphate as substrates.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q93V56}.
Interaction partners:
- Putative ATPase, plasma membrane-like
- ATP synthase subunit b, chloroplastic
- Pyrophosphate-energized vacuolar membrane proton pump 1
- ATPase 6, plasma membrane-type
- ATPase 8, plasma membrane-type
- ATPase 4, plasma membrane-type
- ATPase 11, plasma membrane-type
- ATPase 9, plasma membrane-type
- ATPase 7, plasma membrane-type
- ATPase 3, plasma membrane-type
Sequence:
MAPPIEVSTKSYVEKHVSLPTLNERILSSMSHRSVAAHPWHDLEIGPEAPIIFNCVVEIGKGSKVKYELDKTTGLIKVDRILYSSVVYPHNYGFIPRTLCEDSDPIDVLVIMQEPVIPGCFLRAKAIGLMPMIDQGEKDDKIIAVCADDPEYRHYNDISELPPHRMAEIRRFFEDYKKNENKEVAVNDFLPATAAYDAVQHSMDLYADYVVENLRR
Protein: Ribonucleases P/MRP protein subunit POP6 (EC 3.1.26.5) (RNA-processing protein POP6) (RNases P/MRP 18.2 kDa subunit) (P53218)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribonuclease P/MRP protein subunit RPP1
- Ribonucleases P/MRP protein subunit POP8
- Ribonuclease P protein subunit RPR2
- Ribonucleases P/MRP protein subunit POP1
- Ribonuclease P/MRP protein subunit POP5
- Ribonucleases P/MRP protein subunit POP7
- Ribonuclease MRP protein subunit SNM1
- Ribonuclease MRP protein subunit RMP1
- RNases MRP/P 32.9 kDa subunit
- Telomere replication protein EST3
Sequence:
MINGVYYNEISRDLDISSSTQCLRFLKETVIPSLANNGNNSTSIQYHGISKNDNIKKSVNKLDKQINMADRSLGLQQVVCIFSYGPHIQKMLSILEIFKKGYIKNNKKIYQWNKLTSFDIKREGRNELQEERLKVPILVTLVSDSEIIDLNLHSFTKQ
Protein: Carboxypeptidase E (CPE) (EC 3.4.17.10) (Egg-laying defective protein 21) (O17754)
Organism: Caenorhabditis elegans
Function: During FMRFamide-like peptide (FaRPs or FLP) and neuropeptide-like protein (NLP) precursor processing, catalyzes the removal of Arg or Lys residues from the C-terminus following the initial endoprotease cleavage. By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions. Involved in egg-laying, defecation and locomotion. By processing FLP neuropeptides, regulates the turning step of male mating behavior. Involved in reducing pharyngeal pumping in response to high CO(2) levels.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:12657671}. Perikaryon {ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000303|PubMed:12657671}. Note=Predominantly localizes to axons in the nerve ring. {ECO:0000269|PubMed:12657671}.
Interaction partners:
- Neuroendocrine convertase 2
- Neuroendocrine protein 7B2
- Calcium-dependent secretion activator
- Receptor-type tyrosine-protein phosphatase-like ida-1
- FMRFamide-like neuropeptides 1
Sequence:
MLHAMRPVLLVAALLAVTAHAFLGFGSGSTHKDDAEWGHYHNQAQLEAKLGEINEKCPEITTLYEIGQSVEGRPLVVIQFSTTPGEHIPTKPEVKLIGNMHGNEPIGRELLLRFAETLCNGAINNDKEIVQLLNSTSIHILPSMNPDGFELALGTEPAQRQWLTGRSNINGVDLNRDFPDLDSIFYELQKIGVPKFDHLLSLFEDNVDRQPETIAVGQWTLSLPFVLSANFHEGDLVANYPFDAAIDENSQKTAYSASPDDGTFRWLAKSYADNHAHMSKNDHAPCDGTSQDAFARQGGITNGAKWYSVAGGMQDFNYLATNAMEITLELSCEKMPEGSQLPRFWEDNQKSIFEYVWKSHSGVKGMVVDAMTGEPIKRAVVWIRNGTETVPVKHPVTTWSEGDFYRVLPAGKYEIIVAAEGYDIAAKNVTVENKVRDSALVVNFALSPAADEPSENEQEQIAELVNEIARRR
Protein: Pyridoxal 5'-phosphate synthase subunit PdxT (EC 4.3.3.6) (Pdx2) (Pyridoxal 5'-phosphate synthase glutaminase subunit) (EC 3.5.1.2) (Q8NS90)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit PdxS
- pyridoxal kinase
- pyridoxal kinase
- Transaldolase
- Ribokinase
- Ribokinase
- Ribose-phosphate pyrophosphokinase
- Phosphoglucomutase
- Transketolase
- Ribose-5-phosphate isomerase B
Sequence:
MIVGVLALQGGVEEHLTALEALGATTRKVRVPKDLDGLEGIVIPGGESTVLDKLARTFDVVEPLANLIRDGLPVFATCAGLIYLAKHLDNPARGQQTLAVVDVVVRRNAFGAQRESFDTTVDVSFDGATFPGVQASFIRAPIVTAFGPTVEAIAALNGGEVVGVRQGNIIALSFHPEETGDYRIHQAWLDLVRKHAELAI
Protein: Se6 protein (Q9ICL1)
Organism: Kappapapillomavirus 2
Interaction partners:
Sequence:
MRCTVCGRRLTIPEKIELRARNCTLCCIDKGQYFQWRGHCSSCKLSDQGDLGGYPPSPGSRCGECDECCVPDLTHLTPVDLEELGLYPGPEGTYPDLVDLGPGVFGEEDEEGGGLFDSFEEEDPGPNQCGCFFCTSYPSGTGDTDINQGPAGAAGIALQSDPVCFCENCINFTEFR
Protein: Sp6 transcription factor (D3ZT88)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Acrosomal vesicle protein 1.
- Proprotein convertase subtilisin/kexin type 5
Sequence:
MLTAVCGSLGSQHTDAPHSSPPRLDLQPLQTYQGHTSPEAGDYPSPLQPGELQSLPLGPEVDFSQGYELPGASSRVTCEDLESDSPLAPGPFSKLLQPDMSHHYESWFRPTHPGTEDGSWWDLHPGTSWMDLPHTQGALTSPGHPGALQPALGGYVGDHQLCAPPPHPHPHHLLPAAGGQHLLGPPDGAKVLEAAAPESQGLDSSLDAAARPKGSRRSVPRSSGQTVCRCPNCLEAERLGAPCGPDGGKKKHLHNCHIPGCGKAYAKTSHLKAHLRWHSGDRPFVCNWLFCGKRFTRSDELQRHLQTHTGTKKFPCAVCSRVFMRSDHLAKHMKTHEGAKEEAAAAAQGEGKAGGVVESPGGKGKREAEGSSASSN
Protein: 2-methylcitrate synthase (2-MCS) (mcs) (EC 2.3.3.5) (Citrate synthase) (EC 2.3.3.16) (Q56063)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA or butyryl-CoA but with a lower specificity.
Interaction partners:
- 2-methylcitrate dehydratase
- Propionate--CoA ligase
- 2-methylisocitrate lyase
- Phosphate acetyltransferase
- Acetyl-coenzyme A synthetase
- Isocitrate dehydrogenase
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
- Aconitate hydratase A
- Propanal dehydrogenase
Sequence:
MTDTTILQNNTHVIKPKKSVALSGVPAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLIHGKLPTRDELNAYKSKLKALRGLPANVRTVLEALPAASHPMDVMRTGVSALGCTLPEKEGHTVSGARDIADKLLASLSSILLYWYHYSHNGERIQPETDDDSIGGHFLHLLHGEKPTQSWEKAMHISLVLYAEHEFNASTFTSRVIAGTGSDVYSAIIGAIGALRGPKHGGANEVSLEIQQRYETPDEAEADIRKRVENKEVVIGFGHPVYTIADPRHQVIKRVAKQLSEEGGSLKMYHIADRLETVMWETKKMFPNLDWFSAVSYNMMGVPTEMFTPLFVIARVTGWAAHIIEQRQDNKIIRPSANYTGPEDRPFVSIDDRC