wanglab/gogpt-training-data huggingface dataset:
Protein: T-cell ecto-ADP-ribosyltransferase 2 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 2) (ARTC2) (Alloantigen Rt6.2) (Mono(ADP-ribosyl)transferase 2B) (NAD(+) glycohydrolase) (EC 3.2.2.5) (T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2) (T-cell mono(ADP-ribosyl)transferase 2) (T-cell surface protein Rt6.2) (P20974)
Organism: Rattus norvegicus (Rat)
Function: Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity (to a lesser extent).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Nicotinamide phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NAD-dependent protein deacetylase sirtuin-7
- NAD kinase 2, mitochondrial
- NAD-dependent protein deacylase sirtuin-5, mitochondrial
Sequence:
MPSNICKFFLTWWLIQQVTGLTGPLMLDTAPNAFDDQYEGCVNKMEEKAPLLLQEDFNMNAKLKVAWEEAKKRWNNIKPSRSYPKGFNDFHGTALVAYTGSIAVDFNRAVREFKENPGQFHYKAFHYYLTRALQLLSNGDCHSVYRGTKTRFHYTGAGSVRFGQFTSSSLSKKVAQSQEFFSDHGTLFIIKTCLGVYIKEFSFRPDQEEVLIPGYEVYQKVRTQGYNEIFLDSPKRKKSNYNCLYSSAGARESCVSLFLVVLPSLLVQLLCLAEP
Protein: Lon protease homolog, mitochondrial (EC 3.4.21.53) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15) (Q59HJ6)
Organism: Bos taurus (Bovine)
Function: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters (By similarity). Endogenous substrates include oxidized aconitase.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- Caseinolytic mitochondrial matrix peptidase chaperone subunit.
- Mitochondrial disaggregase
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Stress-70 protein, mitochondrial
- 60 kDa heat shock protein, mitochondrial
- Mitochondrial-processing peptidase subunit alpha
- GrpE protein homolog 1, mitochondrial
- GrpE protein homolog 2, mitochondrial
- ATP-dependent zinc metalloprotease YME1L1
Sequence:
MAGGTGCVRLWGAARCWTLRRPLLAAAGGRVPTAARAWLPRGRRACDASPPWALWGQSPAAAGHWRGLWEANNRSGGGAFSGGEDASEGGAEDGASGVGGSAGGGEGPVITALTPMMIPDVFPHLPLIAVTRNPVFPRFIKIVEVKNKKLVELLRRKVHLAQPYAGVFLKKDDNNESDVVENLDEIYHTGTFVQIHEMQDLGDKLRMIVMGHRRVHINRQLEVEPEEPEGENKQKLRKKPKRGKKEAEEDGATKRPLEVVVGPGPSPAGEVLMVEVENVAHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGHRVVDNPIYLSDMGAALTGAESHELQEVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKHSDENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANITETIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAEFVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPRDRDSDKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHDSANKFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALDRPVRQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPEERAEALAVER
Protein: Catenin delta 1 (A0A669KB05)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANPLMANGTLTRRHQDHSHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETSDDGTTRRTETTVKKVVKTVTTRTVQPVAMGPDGLPVDASSVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYSRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRSYEDMIGEEVPSDQYYWAPLAQHERGSLASLDSLRKGGPPPPNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPVLVGLLDHPKKEVHLGACGALKNISFGRDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDALIFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEAAPNVANNTGPHAASCFGAKKGKDEWFSRGKKPIEDPANDTVDFPKRTSPARGYELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAIADLLTNEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVISILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKELRKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIQMSNMGSNTKSLDNNYSTPNERGDHNRTLDRSGDLGDMEPLKGTTPLMQKI
Protein: Trichohyalin (Q3V203)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
GFREEKLQRAELQDSLLDEEQRRLQEERREPNRSRQLREESQRRRTLYAKPSQRQRREEELREERLLQEEQRQQRERKHRREEDLQQEEKRLQQDEEQLQRERRRLQRERQYQEEDLQQEEERLQQEEERLQRERRRLQQERQYQEEDLQRLRDEDQRRDLKWQWQPRKENEVRSNRLFTKRRGDEEPIQQLEDSQERERRQDRRPLQDEEEEKRELEQERRRRQQRDRQILEEEQFQREHQREARRRDETFQEEEQLQGESRRRQQEREGKFLEEERQLRTEREEQRRRQEQEREFQEEEEHLQEREKELRQECDRKSREQERRQQREEEQLRRQERDQRFRREQERHLEREEEQLRDRPSRREQERHQEREEEQLRDRPSRREQERHQEREEEQLRDRPSRREQERHQEREEEQLRDRPFRREQERRLEREEEQLRDRPSRREQERHQEREEEQLRDRPSRREQERRLEREEEQLRDRSFRREQELRRDRKFHEEEERREELEEEQRGQERDRLRVEEQLRGQREEEQRRRQECDRKLHRELEVRQELEEERLRDRKLRREQELRRDRKFHEEEERRHEEFEEKQLRLQEPDRRFRREQELRQECVEEERLRDSKIRREQELRREREEERLRDRKIRRDQELRQGLEEEQLRRQELDRKFREEQELDQELEEERLRDRKIRREQELRREQELRREQEFRREQELRREQEFRREQELRQEREEERLRDRKIRRDQELRQGLEEEQLRRQERDRKVREEQELDQELEEERLRDRKIRREQELRREQELRREQEFRREQGLRREREEERLRDRKIRRDQELRQGLEEEQLRRQERDRKFREEQELGQELEEERLRDRKIRREQELRREREQEQRRRLEREEEQQRLHEREEEQRRRQEREQEQQRCLEREEEQFRFEEQQRRRQEREQQLRQERDRRVLEEEELRQEREELLHRQVGGRKFREEERLRLEREEQQRRLQERDNRRFREEVELRQEREGQQLRQERDRKFREVEELRQEEQRRRQERDRKFREEKHPREEREEQQLRREKRDGQYLAEEQFARDTIRRQEQELRQEEEQRRRQERERKFQEEQIRRRQEEQRRRQILEPGTRQFANVPVRSSPLYEYIQEQRSQYRP
Protein: Tektin-like protein 1 (Coiled-coil domain-containing protein 105) (Q8IYK2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9D4K7}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS13
- Elongation factor Tu, mitochondrial
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS19
Sequence:
MRVLVPPAERSQDTRVGAPAWREAAQAMARTAHILTDRCGQEAVTMWQPKDSVLDPNVAHHLGRAAYIQPWRFRVEMIKGGGTLEKPPPGEGVTLWKGKMKPPAWYARLPLPLHRKARALQTTEVVHAHARGARLTAARLGRAQHQINGRVRQLLRQREVTDHRLSEVRKGLLINQQSVKLRGYRPKSEKVPDKADSMLTWEKEELKSMKRKMERDMEKSEVLLKTLASCRDTLNFCFKERLQAVDLMNQPLDKVLEQARRHSWVNLSRAPTPRTQGQKTPPPDPVGTYNPACALALNEAKRLLVESKDTLVEMAKNEVDVREQQLQISDRVCASLAQKASETLELKERLNMTLGLMRGTILRCTKYNQELYTTHGLIKGPLSKVHLETAEKLDRPLVRMYQRHVGTQLPEAARLAQGTDKLQCHITYLEKNLDELLATHKNLSWGLNCKNIGHEVDGNVVRLRLRQRQPHVCYEQAQRLVKDWDPRTPPPRSKSSADP
Protein: Opsin 5, mammalian type (B3XZF5)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSGMASDCNSSSQEEYLPHYVQQEDPFASKLSREADIIAGFYLTVIGILSTLGNGYVIFMSSKRKKKLRPAEIMTVNLAVCDLGISVVGKPFSIISFFSHRWIFGWMGCRWYGWAGFFFGCGSLITMTAVSLDRYLKICHLAYGTWLKRHHAFICLALIWAYATFWATVPFAGVGSYAPEPFGTSCTLDWWLAQASVAGQAFVLSILFFCLLFPTAVIVFSYVKIILKVKSSTKEVAHYDTRIQNSHILEMKLTKVAMLICAGFLIAWIPYAVVSVWSAFGQPDSVPIQFSVVPTLLAKSAAMYNPIIYQVIDCKFACCRSGGPKTLQKKSSLKESRMYTLSSHRDSAALSGTQLEV
Protein: Interferon promoter stimulating protein 1 (D1GEL4)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MSSFSREKLSLHLRRRMGVFVTRVKATELIIYLPCLTPSDKEEILAKKDFSGNYAAMQLLLDYVQKRMNWPEELMSALEMLEHQDLADELKAEWNKHNQNNPYPPSAAATTAVRTPVHPIPSTSSEGSPSSLVLPAQPAPPEVAAPPEASLPPEVAPEALPPPVVAPQPEAPPSSVPDAPKAAVSPEIASEAAPSPVVVLKAEPQATPPSPVSAEEPTVISEPSASSQPGPIETVSLEDNSSHSDAPTQIALSETTPTSSGSDLIPAVTQIPLAVSHLALSQTESTPAALARFQSPERLPVQDTLSHTVKVTTFHQEAVEDSDPTQVTEDDQHTELSQSQHFSPATASASPPVDTSTNEDDVNFSKPEVLRSEVMDSQPYSGDSTRLQRSVSDLVLATDGVNRPVVVPDPFTTSTHLPCQENGVPEEINEPLSHNEPQEDTFESSWLSSLGDREVLHNVVHVSEDASIQNNDGQTPNIVVHVSEESCIWNQDGQTQSMLGTKNVGVSGTPRPVPNRNGQSQGLIMIVNGDDASPSTKHPDAPTGSVAVGSSSAEKRHPLEPMGTEIPMEARAVPELKQEGTIGESYYLLGAAVVAVSLFMAWRMMN
Protein: Uncharacterized membrane protein YJR124C (P47159)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MAPEIFVKFKCASRDIKLLWASVFLRLLSYGLTNQVLTLFLNAINMTEDKIGLFMSLTLAGDVICSYILTWYADSWGRRRVLVYGCAMMLLSGLVFSFSENFTLLLVFAIFGVISPSSDEVGPFKSIEEAMIAHLSPHNARPEIYAIHALVGTIGSALGAIICGIFVDLLKRTGLAATDLQCYKLVFLLYAFFAFCKMVIMLLLSDATELDGHYEHTDCNEETAEPLDVNDETAPLMRQATHPEERSNKLSKETVSVLMKLLVIFMVDSLGSGFMTSGWMVYYYSKQFLMGSLALGTLFFITQLVMASSTIPSSIIARCFGPVRATLLVQIPSGIFSILIPMAKNYLPLSILFLNLHFATTAMDVTPRQILLTNIIKPRDLTKVMGVVNIGKTFARCVGPIFTGILANNNYLWLCYIISGSLVITADLILACMFLGVDAKIKKQMNRH
Protein: ESAT-6-like protein EsxJ (P9WNJ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Secreted {ECO:0000269|PubMed:12919853}. Note=Probably secreted via the ESX-5 / type VII secretion system (T7SS). {ECO:0000305|PubMed:19876390}.
Interaction partners:
- ESAT-6-like protein EsxI
- ESAT-6-like protein EsxL
- ESAT-6-like protein EsxO
- ESAT-6-like protein EsxN
- ESAT-6-like protein EsxB
- 6 kDa early secretory antigenic target
- ESAT-6-like protein EsxK
- ESAT-6-like protein EsxP
- ESAT-6-like protein EsxW
- ESAT-6-like protein EsxH
Sequence:
MASRFMTDPHAMRDMAGRFEVHAQTVEDEARRMWASAQNISGAGWSGMAEATSLDTMTQMNQAFRNIVNMLHGVRDGLVRDANNYEQQEQASQQILSS
Protein: Uncharacterized protein (Q381E2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDAFLESLKEAHEEVMNATGWGAFFSGEGQKWSMSPIGAFQQFRKEVAAFISAVNWWEPYFRYLALFHLTVAVTVVLTTWRASIDRIFVVTVLLLLVVWGSSYLNEWGSSHASQIFVEKGANYFDPSGLFIMVTLDMPLFLLVLWLQARAFLQLLRLMVVVKRNQIKREMEKFPCGRKGERPAASSKKKT
Protein: ATP synthase subunit b, chloroplastic (ATP synthase F(0) sector subunit b) (ATPase subunit I) (P0C2Y8)
Organism: Oryza sativa (Rice)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
Interaction partners:
Sequence:
MKNVTHSFVFLAHWPSAGSFGLNTDILATNLINLTVVVGVLIYFGKGVLKDLLDNRKQRILSTIRNSEELRRGTIEQLEKARIRLQKVELEADEYRMNGYSEIEREKANLINATSISLEQLEKSKNETLYFEKQRAMNQVRQRVFQQAVQGALGTLNSCLNTELHFRTIRANISILGAMEWKS
Protein: Flagellar motor switch protein FliG (Flagellar motor switch protein G) (O25119)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P0ABZ1}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0ABZ1}; Cytoplasmic side {ECO:0000250|UniProtKB:P0ABZ1}. Bacterial flagellum basal body {ECO:0000250|UniProtKB:P0ABZ1}.
Interaction partners:
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliN
- Flagellar M-ring protein
- Flagellar motor switch protein FliN
- Flagellar assembly protein FliH
- Flagellar biosynthesis protein FlhA
- Flagellum-specific ATP synthase
- Motility protein A
- Flagellar basal-body rod protein FlgC
- Flagellar biosynthetic protein FlhB
Sequence:
MATKLTPKQKAQLDELSMSEKIAILLIQVGEDTTGEILRHLDIDSITEISKQIVQLNGTDKQIGAAVLEEFFAIFQSNQYINTGGLEYARELLTRTLGSEEAKKVMDKLTKSLQTQKNFAYLGKIKPQQLADFIINEHPQTIALILAHMEAPNAAETLSYFPDEMKAEISIRMANLGEISPQVVKRVSTVLENKLESLTSYKIEVGGLRAVAEIFNRLGQKSAKTTLARIESVDNKLAGAIKEMMFTFEDIVKLDNFAIREILKVADKKDLSLALKTSTKDLTDKFLNNMSSRAAEQFVEEMQYLGAVKIKDVDVAQRKIIEIVQSLQEKGVIQTGEEEDVIE
Protein: Equilibrative nucleoside transporter 2, isoform A (Equilibrative nucleoside transporter 2, isoform B) (GH12067p) (Q9VMB6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- LD05244p
- Adenosine receptor, isoform A
- Adenosine kinase
- Sodium/nucleoside cotransporter
Sequence:
MAEAKSEKSPFIGKQQAPVTLNPSWESKLPPHDSNGKGSTSVLAKLGLPAPKDKFLIVFFIFLLHGVGTLMPWNMFITAKSYFEDFKFGPNNTVATEVSYRTHFMQNMGFASQIPNLVFNWLNIFVNFGGDLTTRIVYSIIFEMVILLVTIILAMLDSSQWPGVFFWTTMVCIVLLNVCNGIYQNTIYGIVASLPIKYTGAVVLGSNISGCFTTAMALICGEIFSSKRTSAIYYFVTAILVLLLCFDTYFALPLNKFFRHYETISRSSEKKSDSKAQLNVPYWQIFKKAAPQLFNIFLTFFVTLSVFPAIQSNVHRSDPNFVVGPDYFTLVTCFATFNVFAMLGSLTTSWVQWPGPRFLWVPVVLRLAFIPLFVMCNYVPPDSVRSLAVFIENDWVYWGIGIAMAYSSGYLSSLGMMYAPQTVHTKYQTTAGMYAAAMLITGIFSGVLFSYLGPFFVV
Protein: U10-myrmicitoxin-Mri1c (U10-MYRTX-Mri1c) (A0A6G9KHD6)
Organism: Manica rubida (European giant red ant)
Function: Induces paralysis 5 minutes after injection into blowflies (L.caesar). In most cases is not lethal 24 hours after injection, but paralysis is irreversible. May have antimicrobial properties, like most ant linear peptides (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:32182430}.
Interaction partners:
Sequence:
MRLSYVSLTLAIIFVMAIVHAPETEAKAYPEADAVGEASAVGEADAVGVADPGVGSLLAKAALKILKIVAPAAAEVIANKIG
Protein: Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic (ACCase subunit alpha) (Acetyl-CoA carboxylase carboxyltransferase subunit alpha) (EC 2.1.3.15) (Q9LD43)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity).
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:10759501, ECO:0000269|PubMed:18431481}; Peripheral membrane protein {ECO:0000269|PubMed:10759501, ECO:0000269|PubMed:18431481}; Stromal side {ECO:0000269|PubMed:10759501, ECO:0000269|PubMed:18431481}.
Interaction partners:
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic
- Biotin carboxylase, chloroplastic
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase 1, chloroplastic
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase 2, chloroplastic
- Beta-ketoacyl-[acyl-carrier-protein] synthase III, chloroplastic
- Acetyl-CoA carboxylase 2
- Acetyl-CoA carboxylase 1
- EMBRYO DEFECTIVE 3147
- 2-isopropylmalate synthase 1, chloroplastic
- 2-isopropylmalate synthase 2, chloroplastic
Sequence:
MASISHSSLALGGASSASASDYLRSSSNGVNGVPLKTLGRAVFTTIRRKDLAVTSRLKKGKKFEHPWPANPDPNVKGGVLSYLAEFKPLGDTQKPVTLDFEKPLVELEKKIVDVRKMANETGLDFTEQIITLENKYRQALKDLYTHLTPIQRVNIARHPNRPTFLDHIHNITDKFMELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPGAYADLKSEELGQGEAIANNLRTMFGLKVPILSIVIGEGGSGGALAIGCANKMLMLENAVFYVASPEACAAILWKTSKAAPEAAEKLRITSKELVKLNVADGIIPEPLGGAHADPSWTSQQIKIAINENMNEFGKMSGEELLKHRMAKYRKIGVFIEGEPIEPSRKINMKKREAVFSDSRKLQGEVDKLKEQILKAKETSTEAEPSSEVLNEMIEKLKSEIDDEYTEAAIAVGLEERLTAMREEFSKASSEEHLMHPVLIEKIEKLKEEFNTRLTDAPNYESLKSKLNMLRDFSRAKAASEATSLKKEINKRFQEAVDRPEIREKVEAIKAEVASSGASSFDELPDALKEKVLKTKGEVEAEMAGVLKSMGLELDAVKQNQKDTAEQIYAANENLQEKLEKLNQEITSKIEEVVRTPEIKSMVELLKVETAKASKTPGVTEAYQKIEALEQQIKQKIAEALNTSGLQEKQDELEKELAAARELAAEESDGSVKEDDDDDEDSSESGKSEMVNPSFA
Protein: Uncharacterized protein ycf72 (P0C308)
Organism: Oryza sativa (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MGAFPSPPPWGWSTGFITTPLTTGRLPSQHLDPALPKLFWFTPTLPTCPTVAKQFWDTKRTSPDGNLKVADLPSFAISFATAPAALANCPPLPRVISMLCMAVPKGISVEVDSSFLSKNPFPNCTSFFQSIRLSRCI
Protein: 16kDa heat-shock protein A (G0T621)
Organism: Buchnera aphidicola (Acyrthosiphon pisum)
Interaction partners:
Sequence:
MSYRSLSFIPNFNDHNVFSNRFNQIDKMFSTLTGEKPISDTPTYNLCQINEIEYQLTLSIPGYQEKELDISVHNNQLSIQGKKENSDTQECNKWLHKGIVFNNFSLNF
Protein: Glutathione S-transferase (EC 2.5.1.18) (A6NNT0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLGSLLAQLSFPGFPSIQLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDFEKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPNLKDFISRFEVMPPSSFLFDAPCSVTSFQMLSQSWSYIKNNLHLLSAGFMPGTLPSTLYLSCGI
Protein: Ribosomal protein L15 (Q6FY78)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS1
- 40S ribosomal protein S27
- Candida glabrata strain CBS138 chromosome G complete sequence
- Large ribosomal subunit protein eL39
- Candida glabrata strain CBS138 chromosome M complete sequence
- YL17
Sequence:
MGAYKYLEELQRKKQSDVLRFLQRVRVWEYRQKNVIHRASRPSRPDKARRMGYKAKQGFVIYRVRVRRGNRKRPVPKGATYGKPTNQGVNELKYQRSLRATAEERVGRRASNLRVLNSYWVNQDSTYKYFEVILVDPSHKAIRRDARYNWICNPVHKHREARGLTATGKKSRGINKGHRYTNTKAGRRKTWKRHNTLSLWRYRK
Protein: Bradykinin-related peptides [Cleaved into: Nattererimorphin; [Val1,Thr6]-bradykinyl-Ser,Pro,Ala; Bradykinin; Des-Arg9-bradykinin; [Hyp3]-bradykinyl-Val,Asp] (A0A088MIT0)
Organism: Physalaemus nattereri (Cuyaba dwarf frog) (Eupemphix nattereri)
Function: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB).
Subcellular location: Secreted {ECO:0000269|PubMed:26443407}.
Interaction partners:
Sequence:
MAFLKKSLFLVLFLGVVSLSFCEEEKREEHEEEKRDEEDAESLGKRYGGLSPLRISKRVPPGFTPFRSPARSISGLTPIRLSKRVPPGFTPFRSPARRISEADPGFTPSFVVIKGLSPLRGKRRPPGFSPFRVD
Protein: Inner membrane complex sub-compartment protein 3 (Q8IKM6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Glideosome associated protein with multiple membrane spans 1
Sequence:
MGNLCCSNNDIKNSKSNIDIFQDNEIYGDNENWTLENWINKYKSGNSIKVAFPDGNEIQCNFRIFFKEKYFELSLDNKVRVIKFNDINCILHRNSCETLLESEQNLLKSPKVIGIRLISTLKAIAFSMDSPGEARIFNDFLQKYCLNA
Protein: Membrane associated guanylate kinase, WW and PDZ domain containing 1 (H7C5T8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KQSTPKRTKSYNDMQNAGIVHAENEEEDDVPEMNSSFTADSGEQEEHTLQETALPPVNSSIIAAPITDPSQKFPQYLPLSAEDNLGPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRCLNKQQKPLEECEDDEGVHTEELDSELELPAGWEKIEDPVYGIYYVDHINRKTQYENPVLEAKRKKQLEQQQQQQQQQQQQQQQQQQQQTEEWTEDHSALVPPVIPNHPPSNPEPAREVPLQGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLPFDPDDPNTSLVTSVAILDKEPIIVNGQETYDSPASHSSKTGKVNGMKDARPSSPADVASNSSHGYPNDTVSLASSIATQPELITVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLVECPKGSEVTLLVQRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHSTQVLPEFPPAEAQAPDQTDSSGQKKPDPFKIWAQSRSMYENRLPDYQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTPVIGKSHQLVVQLMQQAAKQGHVNLTVRRKVVFAVPKTENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGSGVVSTVVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNATLLTNAEKIATITTTHTPSQQGTQETRNTTKPKQESQFEFKAPQATQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGETTKNMKHSRAIELIKNGGRRVRLFLKRGDGSVPEYGGSNYENIPSFPGMTP
Protein: Release factor glutamine methyltransferase (RF MTase) (EC 2.1.1.297) (N5-glutamine methyltransferase PrmC) (Protein-(glutamine-N5) MTase PrmC) (Protein-glutamine N-methyltransferase PrmC) (B0B9D1)
Organism: Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)
Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Interaction partners:
Sequence:
MKKLLREASEYLLSRGIRFPQREAEDILMDLLEISSRSALHQAKLSSEEQSLYWKRLRKRGDRCPTAYIHGKVHFLGVELQVTPQVLIPRQETEIFVEQIIGYLQMHKEKTTFYDVCCGSGCIGLAVRKHCPHVRVTLSDISPEALAIAESNARSNALAVDFLLGDLFDPFSFPADVLVCNPPYLSYKEFFESDPEVRCHEPWKALVGGVSGLEFYHRIATHIHKILVSGGVGWLEIGSTQGEDVKQIFHAKGIRGRVLKDYAQLDRFFFLENQANDAVSSGEVSGFSER
Protein: Protein MSN1 (Multicopy suppressor of SNF1 protein 1) (P22148)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May function as a transcriptional activator. Increased dosage of MSN1 restores invertase expression in yeast mutants defective in the SNF1 protein kinase, and msn1 disruption reduced derepression of invertase in the wild-type. May affect SUC2 expression. Expression of MSN1 enhances growth in iron-limiting conditions.
Subcellular location: Nucleus.
Interaction partners:
- Transcription activator MSS11
- Flocculation protein FLO1
- Putative transcription factor PHD1
- Uncharacterized protein YMR181C
- CRE-binding bZIP protein SKO1
Sequence:
MASNQHIGASNLNENEAILTNRVAELERRMSMFEGIFHALSNRLDLHFKKYDVVVNSQQQQINELTAFLSTLLNDQQRHAEILSEKLSGTLHGVSATSISLSQTLDPQGFTDGTTAPGAPRNYTSVPMNNDQTAHPQNEGAVSNETLFEDILNGNSQENDKSQQQTNSSNSISQENNSTNPSVDTRFNKPQNYNSNLVPSLEEYSANPPNNDGGQSQGLYISSNSSQSRQSPNLQKVSPNHENAVESNAQESVPTFEEEQYETKTGLKRKRIVCTRPFEFIKSPHSVMEVWKEYTEGVNGQPSIRKMEALYQTAWRRDPAVNKRYSRRKVLWKAIQTGLNRGYSLNYVVEILENSRYVNDKQKVKQPIGWLCHSSHIPETLK