wanglab/gogpt-training-data huggingface dataset:
Protein: H-N-H endonuclease F-TflIV (EC 3.1.21.-) (HNH endodeoxyribonuclease F-TflIV) (HNH endonuclease F-TflIV) (Q6QGL2)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Endonuclease that introduces double-strand break into pseudo palindromic 17 bp DNA sequence yielding 1 bp extensions with 3'-overhangs.
Interaction partners:
Sequence:
MRTDILDRKEEIAQWIAQGKSKAEIARMLSCSSNTLEAYLGKLGIVVIPTNRQYDNKYKSATEYLYNGSPISSYKLKNKILNEGLKPHKCESCGLESWLDKPIPLELEHKDGNHYNNEWDNLALLCPNCHALTPTHAGKNIGRYTERTVNTCAICHCEISSRATHCKSCTPKGITINPDITVEQIEYWVSKYSWIRASKELGLSDTGLRKRYKSLTGKDPKSIKKNR
Protein: Alkaline phosphatase PhoK (EC 3.1.3.1) (SPAP protein) (A1YYW7)
Organism: Sphingomonas sp
Function: Alkaline phosphatase with broad substrate specificity. Precipitates uranium from alkaline solutions.
Subcellular location: Secreted {ECO:0000269|PubMed:18641147}.
Interaction partners:
Sequence:
MLKHVAAALLLATAMPVVAQSPAPAAAPAPAARSIAATPPKLIVAISVDQFSADLFSEYRQYYTGGLKRLTSEGAVFPRGYQSHAATETCPGHSTILTGSRPSRTGIIANNWFDLDAKREDKNLYCAEDESQPGSSSDKYEASPLHLKVPTLGGRMKAANPATRVVSVAGKDRAAIMMGGATADQVWWLGGPQGYVSYKGVAPTPLVTQVNQAFAQRLAQPNPGFELPAQCVSKDFPVQAGNRTVGTGRFARDAGDYKGFRISPEQDAMTLAFAAAAIENMQLGKQAQTDIISIGLSATDYVGHTFGTEGTESCIQVDRLDTELGAFFDKLDKDGIDYVVVLTADHGGHDLPERHRMNAMPMEQRVDMALTPKALNATIAEKAGLPGKKVIWSDGPSGDIYYDKGLTAAQRARVETEALKYLRAHPQVQTVFTKAEIAATPSPSGPPESWSLIQEARASFYPSRSGDLLLLLKPRVMSIPEQAVMGSVATHGSPWDTDRRVPILFWRKGMQHFEQPLGVETVDILPSLAALIKLPVPKDQIDGRCLDLVAGKDDSCAGQ
Protein: Tubulin beta chain (Beta-tubulin) (P32256)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Probable serine/threonine-protein kinase roco11
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco6
- Dynein heavy chain, cytoplasmic
- Tubulin alpha chain
- Tubulin alpha chain
- Cytoplasmic dynein 1 intermediate chain
- Kinesin-related protein 13
Sequence:
MREIVQIQAGQCGNQIGSKFWEVISEEHGIQSDGFHAGGEDEHLKRLQLERINVYYNEARDGKYVPRSVLVDLEPGTVDTIKASPYGKLFRPDNFIHGQSGAGNNWAKGHYTEGVELVESVLDVVRRETEGCDCLQGFQVTHSIGGGTGSGLGTLLISKIREEFPDRMMCTFSVVPSPKVSLTVVEPYNATLSVHQLVENADEVMCIDNEALHDICFRTLKLTQPNYGDLNHLISSVMSGITCCLRFPGQLNSDLRKLAVNLIPFPRLHFFLVGFAPLTAKGASSYNRITVPELTQQMFDAKNMMAASDPHNGKYLTASALFRGKIFTKEVDEQMHNIQTKNSSYFVEWIPHNIKSSICDIPPKGTPMAVTFIGNNTAIQDLFKRISIHFQAMFRRKAFLHWYTLEGMEELEFTEAESNMNDLVYEYQQYSNQETEEDGGEYQEEHEEHEEQAEN
Protein: Hephaestin (Hp) (EC 1.16.3.1) (Q9Z0Z4)
Organism: Mus musculus (Mouse)
Function: May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1.
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9BQS7}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Ferroportin
- Ferrochelatase, mitochondrial
- Heme oxygenase 1
- Frataxin, mitochondrial
- Heme oxygenase 2
- Ceruloplasmin
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Natural resistance-associated macrophage protein 2
- Hepcidin
- Hepcidin-2
Sequence:
MKAGHLLWALLLMHSLWSIPTDGAIRNYYLGIQDMQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGSSYKKTVYKEYSDGTYTEEIAKPAWLGFLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLTWIYHSHVDAPRDIATGLIGPLITCKRGTLDGNSPPQRKDVDHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKVDSCSMDPPVDQLTGKVRQYFIQAHEIQWDYGPIGYDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERVHQEEETHLGILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYNDGTSHPKVAKSFEKVTYYWTVPPHAGPTAQDPACLTWMYFSAADPTRDTNSGLVGPLLVCKAGALGADGKQKGVDKEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDVHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNVSQCSSHQDSPRQHYQASRVYYIMAEEIEWDYCPDRSWELEWHNTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPRPRSGPEEHLGILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESNTGGPQAAEPGEVLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIKDMYSGLVGPLVICRNGILEPNGGRNDMDREFALLFLIFDENQSWYLKENIATYGPQESSHVNLKDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDTDIHTVHFHAESFLYQNGQSYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETIFTVLSHEEHFSTMTTITKEIGKAVILRDIGGDNVKMLGMNIPIKDVEILSSALIAICVLLLLIALALGGVVWYQHRQRKLRRNRRSILDDSFKLLSLKQ
Protein: HTH-type transcriptional regulator TdcA (Tdc operon transcriptional activator) (P0ACQ7)
Organism: Escherichia coli (strain K12)
Function: Transcriptional activator for the tdcABCDE operon.
Interaction partners:
- Threonine dehydratase operon activator protein
- L-threonine dehydratase catabolic TdcB
- Threonine/serine transporter TdcC
- Uncharacterized HTH-type transcriptional regulator YfiE
- HTH-type transcriptional activator AllS
- HTH-type transcriptional activator AaeR
- HTH-type transcriptional regulator DsdC
- HTH-type transcriptional regulator DmlR
- Propionate kinase
- HTH-type transcriptional regulator YjiE
Sequence:
MSTILLPKTQHLVVFQEVIRSGSIGSAAKELGLTQPAVSKIINDIEDYFGVELVVRKNTGVTLTPAGQLLLSRSESITREMKNMVNEISGMSSEAVVEVSFGFPSLIGFTFMSGMINKFKEVFPKAQVSMYEAQLSSFLPAIRDGRLDFAIGTLSAEMKLQDLHVEPLFESEFVLVASKSRTCTGTTTLESLKNEQWVLPQTNMGYYSELLTTLQRNGISIENIVKTDSVVTIYNLVLNADFLTVIPCDMTSPFGSNQFITIPVEETLPVAQYAAVWSKNYRIKKAASVLVELAKEYSSYNGCRRRQLIEVG
Protein: Multidrug efflux ATP-binding/permease protein Rv0194 (EC 7.6.2.-) (O53645)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Overexpression in M. smegmatis increases resistance to erythromycin, ampicillin, novobiocin and vancomycin. It also reduces accumulation of ethidium bromide in the cell.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein
- Possible two component transcriptional regulatory protein
- Probable transcriptional regulatory protein
- HTH-type transcriptional regulator Cmr
- HTH-type transcriptional regulator VirS
- Transcriptional regulatory protein TcrA
- Possible exported protein
- AB hydrolase-1 domain-containing protein
- Probable transcriptional regulatory protein
- NAD-dependent protein deacylase
Sequence:
MRTNCWWRLSGYVMRHRRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATYLLMYVRRYYGGRIAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTLVDGTKPLSPEARLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYRELLSPAPDLADDLVVAERSPVCRPVAGLGTKAAQHTNVHNPGPHDHPPGPDPLRRLLREFRGPLALSLLLVAVQTCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTPSSPAARPVGTLRGEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLWAAHTRLCSPEITQLQCIDA
Protein: Major capsid protein 1 (MCP1) (Q70LC6)
Organism: Acidianus filamentous virus 1 (isolate United States/Yellowstone) (AFV-1)
Function: Self-assembles to form a helical, filamentous nucleocapsid mesuring 900 nm in length and 24 nm in width (Probable). Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).
Subcellular location: Virion {ECO:0000269|PubMed:19934032}.
Interaction partners:
Sequence:
MAKLNRKLRQDSTDRYKTKLYLWRNLGGLIPEDMAISVTESITADWKQYNDMMSKVRNETLDILKTNKVATEDYIGYIAFAEELAHQVWKNKNSSPDPNTANEASKTDLESKYSDVYGLDVTVLDAIYNAVIPIIMGGGS
Protein: Photosystem II reaction center protein T (PSII-T) (Q6ENE7)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: Seems to play a role in the dimerization of PSII.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00808}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00808}.
Interaction partners:
- Photosystem II reaction center protein L
- Photosystem II reaction center protein J
- Photosystem II reaction center protein I
- Cytochrome b559 subunit beta
- Photosystem II reaction center protein H
- Photosystem II CP43 reaction center protein
- Photosystem II reaction center protein K
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein Z
- Uncharacterized protein
Sequence:
MEALVYTFLLVSTLGIIFFAIFFREPPKVPTKKVK
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (Plasmin receptor) (Plasminogen-binding protein) (P0C0G6)
Organism: Streptococcus pyogenes
Function: Also binds human plasminogen.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Enolase
- Fructose-bisphosphate aldolase
- NADP-dependent glyceraldehyde-3-phosphate dehydrogenase])
- Glucose-6-phosphate isomerase
- L-lactate dehydrogenase
- Chaperone protein DnaK
- Transketolase
- Pyruvate kinase
Sequence:
MVVKVGINGFGRIGRLAFRRIQNIEGVEVTRINDLTDPNMLAHLLKYDTTQGRFDGTVEVKEGGFEVNGNFIKVSAERDPENIDWATDGVEIVLEATGFFAKKEAAEKHLHANGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGASCTTNCLAPMAKALHDAFGIQKGLMTTIHAYTGDQMILDGPHRGGDLRRARAGAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVVTLDKNVSVDEINSAMKAASNDSFGYTEDPIVSSDIVGVSYGSLFDATQTKVMEVDGSQLVKVVSWYDNEMSYTAQLVRTLEYFAKIAK
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q9Y7F6)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Interaction partners:
Sequence:
FHQTPSAMSQVFFDVEYAPVGTAETKVGRIVFNLFDKDVPKTAKNFRELCKRPAGEGYRESTFHRIIPNFMIQGGDFTRGNGTGGRSIYGDKFADENFSRKHDKKGILSMANAGPNTNGSQFFITTAVTSWLDGKHVVFGEVADEKSYSVVKEIEALGSSSGSVRSNTRPKIVNCGEL
Protein: Poly(A) polymerase (EC 2.7.7.19) (G3XAH6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR018425}.
Interaction partners:
Sequence:
MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCVLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKENPDKEEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFEVDMKIAAMHVKRKQLHQLLPNHVLQKKKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTSATKTSPLNSSGSSQGRNSPAPAVTAASVTNIQATEVSVPQVNSSESSGGTSSESIPQTATQPAISPPPKPTVSRVVSSTRLVNPPPRSSGNAATSGNAATKIPTPIVGVKRTSSPHKEESPKKTKTEEEQLDTETSTTQSETIQTAASLLASQKTSSTDLSDIPALPANPIPVIKNSIKLRLNR
Protein: RAS p21 protein activator 1 (Q91YX7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MCGDYYIGGRRFSSLSDLIGYYSHVSCLLKGEKLLYPVAPPEPVEDRRRVRAILPYTKVPDTDEISFLKGDMFIVHNELEDGWMWVTNLRTDEQGLIVEDLVEEVGREEDPHEGKIWFHGKISKQEAYNLLMTVGQVCSFLVRPSDNTPGDYSLYFRTNENIQRFKICPTPNNQFMMGGRYYNSIGDIIDHYRKEQIVEGYYLKEPVPMQDQGQVLNDTVDGKEIYNTIRRKTKDAFYKNIVKKGYLLKKGKGKRWKNLYFILEGSDAQLIYFESEKRATKPKGLIDLSVCSVYVVHDSLFGRPNCFQIVVQHFSEEHYIFYFAGETPEQAEDWMKGLQAFCSLRKSSPGTSNKRLRQVSSLVLHIEEAHKLPVKHFTNPYCNIYLNSVQVAKTHAREGQNPVWSEEFVFDDLPPDINRFEITLSNKTKKSKDPDILFMRCQLSRLQKGHATDEWFLLSSHIPLKGIEPGSLRVRARYSMEKIMPEEEYSEFKELILQKELHVVYALSHVCGQDRTLLASILLKIFLHEKLESLLLCTLNDREISMEDEATTLFRATTLASTLMEQYMKATATQFVHHALKDSILKIMESKQSCELSPSKLEKNEDVNTNLAHLLSILSELVEKIFMASEILPPTLRYIYGCLQKSVQHKWPTNNTMRTRVVSGFVFLRLICPAILNPRMFNIISDSPSPIAARTLTLVAKSVQNLANLVEFGAKEPYMEGVNPFIKSNKHRMIMFLDELGNVPELPDTTEHSRTDLSRDLAALHEICVAHSDELRTLSNERGVQQHVLKKLLAITELLQQKQNQYTKTNDIR
Protein: Ribonuclease H2 subunit B (A0A2R8YEB4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAGVDCGDGVGARQHVFLVSEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKKNSKMTAAQKALAKVDKSGMKSIDTFFGVKNKKKIGKV
Protein: Adapter molecule crk (Proto-oncogene c-Crk) (p38) (Q64010)
Organism: Mus musculus (Mouse)
Function: Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocated to the plasma membrane upon cell adhesion. {ECO:0000250}.
Interaction partners:
- Dedicator of cytokinesis protein 1
- E3 ubiquitin-protein ligase CBL
- Paxillin
- CRK SH3-binding GNRP
- Breast cancer anti-estrogen resistance protein 1
- Tyrosine-protein kinase ABL1
- Proto-oncogene tyrosine-protein kinase Src
- Focal adhesion kinase 1
- Fibroblast growth factor receptor substrate 2
- Epidermal growth factor receptor
Sequence:
MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVARSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS
Protein: Mediator of RNA polymerase II transcription subunit 14 (Mediator complex subunit 14) (Q8IBZ6)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU365082}.
Interaction partners:
- Small ribosomal subunit protein eS30
Sequence:
MMESDEHDEYKDYKCVSYGLLLKKIAKRAINDWFFFCERVDNDSGENFDYLRSALIQYCRHMRECFLKILELDKFRERYKEMNDLIKYILESKQTYEELKTKYNYDIYLTKLKTIPLQINENNILCAIDVLATKRYTRFPLLFKEILKNPNECFLPTLNKYQMNILKKRIIDGFLINYYISNIPKKKVDFIFSRGILDLEIINEVRISLISDFLNVKILDVDILFLDTMNLGKSHNLVLSNLINYHLLQKQQQCYSNYITSQEEINEKMDISTGHMKNMEGAKMFEGDLPPCADMNEDQHVYDKMSDEKYNGSNKSYGINKSYGINKSYGSNKSYGINKSYGSNKSYGSNKSYGINKSYGSNKSYGSNKSYGNNKSYGNNNSYDSDDSHDSDDSRDSDNSHHGDDKNNDLDNFINNILKKEINKERGRYPKNDSIEKHYLENVCTKKVQLQLSDIFYEIYKISHFYCSIQILEFYKGCINQYNSYNYKKKKIQLYKLYKNNNIEYTPSCYNYTLNDNDGILHLDIQLYDMDLTDSIIYTYFKKRKKNASIFINEKNKNKIILKFILNNLNGNIQVFMWPFSYFSNKKKKKKKNIIFKNILSYYEYVICFFMKKKIKNILSYNPYYIHIESWYNKIGYCIVFFLFSILKIFCTCDDDTTLLISRKHVYYLSDSLEKSEYSYKTGVINIHDLLLDYFFDLHFIKDELKCQDTNGNIKYDQMNDHVKNDHTNYYQNNNIFNLLTLIKLKKENENSYILRYTFYNQKIDLFINMINEKLVFKCHWDSDIFINMISLSYNLKLIIYILYLLKYYSSYIYIYNFLKERFQVRPGKIENFVFNKKDLYPNVFFHKLMLYYFLKKSDYSSNLVITKFLEEFFSYIDFYFYIYSGEENNLETQLKRELKRGEIINNIVNDHYDNMNDQGGNMNDHYDNMNNHDDNMNNPDDNMNNHDDNMNNHDDNMNNHDDNMNKHTNYLNDKDNYNSKGTFPENTFDDKKNCSYQKNFVSVFYFTIYVNKNTPLLLCLLIERGYIFCTYIIITFENMKKKSMETQNGGGKYEEDMNSTFKKNNSFIIPLIHKKYFLSSHIHLYFDSLKDVIDNNSNMFINLYNILKVNFYCPLFSDGFDFSTHIMMNGKKSGKKNEMKNLRGTNMEKAEEKRYVENIINNDSHSNVHGDDHNNVHGDSHNNVHGDDHNNVHGDSHSNKPCYIYQFFDKQNYLNFIKQKKKCALDLQYYINKRKNANYYEYPENYINNYILHLYTSFNKKYAMKNEQDMNKDDKNNELMIYLLIKIHSSGSLFFKIPIKGKRYMKINNLDVIKNRELFIYHKCLVINMKLEKKKKKKKYDNGKKNDDMNTICMIDQNKLLDNENKIKMNEIIDTNVMNKDICSNMVDDEKNEQDTSNNTITSNEGKINNWVLIKKMYILLNDESTKLNILDIFSCIIKSCYTFDFSNELYYLENKILCSNFVVRNSHISNIDIVYYSNYNKDITCSISLNFLNNEYDNNNNNNIKNELPKSNEMIQKEEILNNNHNTFKQKNRNDMTTPFSTCNDILKNLLFIDISFNNPIDCINNIFIKEKNNLYLYLEKKKSIYNLLKLICLTYEFHHNFYILINKTNEHLRKTHFLNIMDPSMLFDIQYENLFTINLICKDLYIYNNNNNNNNNNNNLCLCILLHPEYYSQIIIIPYLTCYNNKNVRNDVSFKKKNYFFKNFKYDDHLRNKQQNYNGSFLNIQRDHSKGVLERDGKITRDDLLSSFSVQTYTSLNNQNVFIDNMDEEDLFIYLFLNYCNLINFNITNNNVSQNYNDKISDLNKTKNKNEERSFWSSSLKKLLTKFDEEIFSTNDLRVFEEYEMFISNIKYILKMKNKIISSEVFFFSPYFLPTVLYNLFEFLRTLGVWLTLLGRLKNDYTDINLRNDRNICNVFQYITAKKNSKSWDNQPNPEVKNMNTDENNTTTTKKKKDDNDNQNDDIYIHLIWNIYNVRTLYTERLNNDRKISNAKRKYETFHTNMDDIFNDDNNCINIINVEDNKEENIKDLKYKKLKTNEVEKVDNEFIQVTDNNIIEINPKKKTSTQNEEQHNINTINENGNMYTYSLINSTLTLNNIHMKRWKYLINTYCFNNYIMFFQTTQNKYLLNRRLIKKAFFLRSLKFDDFNDIKSYYKKVKEINYCDNNHKNNKMDTAQQYIHYLKEDQKEKELINFDHIINYMSDNIWVSQIHYLTHGISLYFENVGEEVDEEDAWFYCLQKKKKINGDDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDNKMNGDDNKINGDDNKNCDDNKNCDDNKNCDDNKNCDDNKINCDGEVCGEEYSRKLLILYKDNILKENCEINCSLNIIYKYIRIWLLRLKLQDVDVFFCILNEVINDKKKICEFSSLVFNSVLSYYEHLDFWLSKNTDVLCSPFIETQFTLREEKDVINDSINNVEKSDLFLKYKKNKNKEIKYNDKKFIEIIIPFIIKEKGEEKNLHMDNILKYNKNDIKIDYNDMNNSMDIIKNEDDKEYLSNYINNNIKNIKNIKNNNDVQNSNMNSNYKNIDINMLNALNCSVINYNNIKINYKIWRYMPCPFKIISYNKNKLDILKKNNDSIILSFQISSLPVKNLKDVYINNEPFIKFLVTNHIDLNVAHERVMNILQKYNLKPNYSLVATQTILHISTFELLLNANQKKE
Protein: GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase (EC 2.4.1.346) (Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase) (Alpha-mannosyltransferase) (Alpha-ManT) (Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase) (Phosphatidylinositol alpha-mannosyltransferase) (PI alpha-mannosyltransferase) (Q8NNK8)
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: Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 6 of a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1) to generate phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2). PimB also catalyzes the addition of a mannosyl residue from GDP-Man to the position 6 of phosphatidyl-myo-inositol bearing an acylated alpha-1,2-linked mannose residue (Ac1PIM1) to generate monoacylated phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2) (By similarity). The addition of the second mannosyl residue by PimB preferentially occurs before the acylation of the mannosyl residue transferred by PimA (By similarity). Also able to transfer a mannosyl residue from GDP-Man to the position 6 of a phosphatidyl-myo-inositol (PI), but this reaction is very slow (By similarity).
Interaction partners:
- Cell wall-associated hydrolases
- Lauroyl/myristoyl acyltransferase involved in lipid A biosynthesis
- Alpha-
- Hypothetical membrane protein
- Terminal beta-
- Probable endopeptidase Cgl2188
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Glycosidases
Sequence:
MSASRKTLVVTNDFPPRIGGIQSYLRDFIATQDPESIVVFASTQNAEEAHAYDKTLDYEVIRWPRSVMLPTPTTAHAMAEIIREREIDNVWFGAAAPLALMAGTAKQAGASKVIASTHGHEVGWSMLPGSRQSLRKIGTEVDVLTYISQYTLRRFKSAFGSHPTFEHLPSGVDVKRFTPATPEDKSATRKKLGFTDTTPVIACNSRLVPRKGQDSLIKAMPQVIAARPDAQLLIVGSGRYESTLRRLATDVSQNVKFLGRLEYQDMINTLAAADIFAMPARTRGGGLDVEGLGIVYLEAQACGVPVIAGTSGGAPETVTPATGLVVEGSDVDKLSELLIELLDDPIRRAAMGAAGRAHVEAEWSWEIMGERLTNILQSEPR
Protein: Ground-like domain-containing protein (O18015)
Organism: Caenorhabditis elegans
Interaction partners:
- Ground-like domain-containing protein
- Apple domain-containing protein
- Secreted protein
- dTDP-D-glucose 4,6-dehydratase
- Amine oxidase domain-containing protein
- C6 domain-containing protein
- SUppressor of Pkc-3
- MliC domain-containing protein
- Prion-like-
- WaRThog
Sequence:
MLFRLVSTLLLAQTTSAFFFGGGGGGCGCQQAPACAPHPAPAPCSGGNIVQGYVGAPQQGGYAAAPQYPQQGGYGGAQQGFQAAPAPYQPQGGYQAGPAPVQGYQPQAQVPAGGYQAPVQPAPGPAEVAPAQVQAGGNYQDAPAQVAEVATAQESAPPPSEAAYTGEQEVVASLAREEPNYQNTGTNVIEAAQHASELGNQAAAAAAKVAEVVEEEEEPIKKKDEGKTTHMKTVKAPAAASSTTAAAASTSTEFPVGEEIVADTNEKEVDISELHLTDDPLCNSDDLRKVVIDNIDDQLNSSKRMIQLAAEAQFGGRFDVICANGDFSYVTNTELYCQETKGDISCYTYRQL
Protein: phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (Phosphoribosylglycinamide synthetase) (Q5PPK3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAARVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTASAGKISNAAVSINDHTALARFCKDEKIELVVVGPEAPLAAGIVGDLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPALVVKASGLAAGKGVIVAKSKAEACEAVQEIMQEKSFGAAGETVVVEELLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTGGMGAYCPAPQVPKDLLVKIKNTILQRTVDGMQQEGVPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTFDGLLSESPPVWLENHSAVTVVMASGGYPGAYTKGVEITGFPEAQALGLQVFHAGTALKDAKVVTSGGRVLTVTAVRENLMSALDEARKGLAALKFEGAVYRKDIGFRAVAFLQRPR
Protein: MIP12871p (A1Z951)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFAGIRKRLARKQNEKDCDEDDKEDVLDSMPPPPNYIQISQGRIQLVHQPRTPVESEAGTLSLERHGGSISGSGGCDKSQCGSPTFEKELREQIENMNRIMKSKERKQMQTCRDHKALQTRFARQESLLQSMQQENRSLLTRIRQYEHCLDDVMRKVVDAIVAEDNLREEVSMLKGRVRDLEAQNAALSASPVKGRDEGYCTMSSGQPQPSNGHLEDLPEEPEQWLLPAEPCSTEMEDWSMSQEELAVMTFDDERDPHHPHLQQQRRKRDHDWLWPSSDFINSTTVETDSVADGITQLLQQKIVYSEDEEVACTDFTNDFYKLVNIRSNSSRSLYSYLEGETDDEDEDDDDGEDSSISESQVGPAGRISPTPSEAGRAQLTSCSSSETDELSASQAKKDEEPDYAVIDECRRRVSDIEIEDVPMIVSSTPMKPLDEQQCIAQIIKSELRRPPHVLVKSKSVLEDQEPSCILRHNQRRELESTVVCSDSISCAMMNKLAKEVVPPAPGMVTKLKERMLLRQASTPPTASSWRRSNGWKRVTSPVHPPVAVSPKKKAAKSTEPPKSCLPKAQPTRIPTSIHSSVSSSSSMSSSCSPSPSSPSPQSPQQRSPGQQTQQQQQQQQQRKSKIPPPVPVRRSYAS
Protein: Uncharacterized protein C13G6.15c (Q09791)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin.
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Calcineurin subunit B
Sequence:
MLVFTTSPDHVDELNEFVQQLNPVAFTRVLRGLGKVLASYNDKAVEEDTLKKSSTGSLPSGQQVHCQYVLDDPNHVEGISVDQSLQVPKFEKNWLISPPGSPPVGWEPIVEESPNSQHLAHDIQLKLDELGNALLNDHSAGPQIVISEHNNTKETSPSRQFEH
Protein: Putative protein FAM86C1P (EC 2.1.1.-) (Protein FAM86C) (Q9NVL1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPEENAGSELLLQSFKRRFLAARALRSFRWQSLEAKLRDSSDSELLRDILQKHEAVHTEPLDELYEVLVETLMAKESTQGHRSYLLTCCIAQKPSCRWSGSCGGWLPAGSTSGLLNSTWPLPSATQRCASCSPPSYAGLGSDGKRKLIMTRNCFPTESTWRWQS
Protein: Superoxide dismutase [Fe] 2, chloroplastic (EC 1.15.1.1) (Iron-superoxide dismutase) (Q5VSB7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- superoxide dismutase
- Superoxide dismutase, chloroplastic
- Superoxide dismutase 1
- Superoxide dismutase 2
- Os07g0665300 protein
- Copper chaperone for superoxide dismutase, chloroplastic
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
- Superoxide dismutase 1, chloroplastic
- Os02g0102400 protein
Sequence:
MAAFASALRVLPSPPAAVPRRLRSREQRQGCRSRRYSKVVAYYALTTPPYKLDALEPYISKRTVELHWGKHQQDYVDSLNKQLATSMFYGYTLEELIKEAYNNGNPLPEYNNAAQVWNHHFFWESMQPEGGGSPGRGVLQQIEKDFGSFTNFREEFIRSALSLLGSGWVWLVLKRKERKFSVVHTQNAISPLALGDIPLINLDLWEHAYYLDYKDDRRMYVTNFIDHLVSWDTVTLRMMRAEAFVNLGEPNIPVA
Protein: Outer membrane OMP85 family protein (Q9FFG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000256|ARBA:ARBA00024013}.
Interaction partners:
- Mitochondrial outer membrane import complex protein METAXIN
- Mitochondrial import receptor subunit TOM40-1
- Probable mitochondrial import receptor subunit TOM40-2
- Mitochondrial import receptor subunit TOM9-2
- Mitochondrial import receptor subunit TOM9-1
Sequence:
MENPAEKPDPNPSKPKIESEDEREELGDINGDEEEEEEYEEEDDGKPRTREDAIADRIKAESLFRRMRATPVAVRVHDVIVKGNEKTKDHVIEAEVDVVRQATTLQELLKASKVANFNLQALDIFDSVKITLDSGPPELPGTTNVVIDVVESKSPITGQIGTFTKAEARSSSLEGSLKYKNIFGYGDIWDGSLAYGCDHSAEVGLGMYLPRFRGRPTPFTSRVYLSTQDWLKFSSYKERALGLSLGLIASKYHELAYNIAWRNLIDPSQMASRSIRRQLGHNLVSALKYTFKFDQRNSSLRPTRGYSFISTSQIGGLAPDSRTLRFLRQEIDLRYAVPLGFYRAALNFGIAGGITFPWGSGYKSRASCVPERFFLGGNISPVCSLGGPSALWGFKTRGLGPNEPRREVQDDESGDTYERDFVGGDVAVTAFADLSFDFPLKWFRDRGIHGHVFACAGNMAELSENKYRNFTAPKLLETFRSSVGAGIVVPTSLFRMELNYCHILKKQEHDRAKSGFFMTFSTSS