wanglab/gogpt-training-data huggingface dataset:
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (EC 7.1.1.2) (Complex I-30kD) (CI-30kD) (NADH-ubiquinone oxidoreductase 30 kDa subunit) (P23709)
Organism: Bos taurus (Bovine)
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 (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Peripheral membrane protein {ECO:0000305|PubMed:25209663}; Matrix side {ECO:0000305|PubMed:25209663}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH-ubiquinone oxidoreductase chain 2
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
Sequence:
MAAAVAAAARGCWQRLVGSAAPARVAGRPSVLLLPVRRESSAADTRPTVRPRNDVAHKQLSAFGEYVAEILPKYVQQVQVSCFNELEICIHPDGVIPVLTFLRDHSNAQFKSLADLTAVDIPTRQNRFEIVYNLLSLRFNSRIRVKTYTDELTPIESSVPVYKAANWYEREIWDMFGVFFANHPDLRRILTDYGFEGHPFRKDFPLSGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWEAFPAYRQPPESLKLEAGDTKPEAK
Protein: Non-selective voltage-gated ion channel VDAC2 (Outer mitochondrial membrane protein porin 2) (H0UZA0)
Organism: Cavia porcellus (Guinea pig)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MSCCETMCIPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNSTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSINAGGHKLGLALELEA
Protein: Protein mono-ADP-ribosyltransferase PARP6 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 17) (ARTD17) (Poly [ADP-ribose] polymerase 6) (PARP-6) (Q2NL67)
Organism: Homo sapiens (Human)
Function: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins.
Interaction partners:
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL18
Sequence:
MDIKGQFWNDDDSEGDNESEEFLYGVQGSCAADLYRHPQLDADIEAVKEIYSENSVSIREYGTIDDVDIDLHINISFLDEEVSTAWKVLRTEPIVLRLRFSLSQYLDGPEPSIEVFQPSNKEGFGLGLQLKKILGMFTSQQWKHLSNDFLKTQQEKRHSWFKASGTIKKFRAGLSIFSPIPKSPSFPIIQDSMLKGKLGVPELRVGRLMNRSISCTMKNPKVEVFGYPPSPQAGLLCPQHVGLPPPARTSPLVSGHCKNIPTLEYGFLVQIMKYAEQRIPTLNEYCVVCDEQHVFQNGSMLKPAVCTRELCVFSFYTLGVMSGAAEEVATGAEVVDLLVAMCRAALESPRKSIIFEPYPSVVDPTDPKTLAFNPKKKNYERLQKALDSVMSIREMTQGSYLEIKKQMDKLDPLAHPLLQWIISSNRSHIVKLPLSRLKFMHTSHQFLLLSSPPAKEARFRTAKKLYGSTFAFHGSHIENWHSILRNGLVNASYTKLQLHGAAYGKGIYLSPISSISFGYSGMGKGQHRMPSKDELVQRYNRMNTIPQTRSIQSRFLQSRNLNCIALCEVITSKDLQKHGNIWVCPVSDHVCTRFFFVYEDGQVGDANINTQDPKIQKEIMRVIGTQVYTN
Protein: Histone H4 (Q587H6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone H3 variant
- Histone H3, putative
- Histone H2A
- Histone H2A
- Histone H2B
- Histone H2B
- Histone H2B
- SET domain-containing protein
- Histone H2B
- Protein arginine N-methyltransferase 7
Sequence:
MAKGKRVGESKGAQKRQKKVLRDNVRGITRGSIRRLARRAGVKRISGVIYDEVRGVLKTFVESIVRDAGAYTEYSRKKTVTAAHVVFALRKRGKVLYGYD
Protein: choline-phosphate cytidylyltransferase (EC 2.7.7.15) (Q8IEE9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Choline kinase
- Phosphoethanolamine N-methyltransferase
- Choline/ethanolaminephosphotransferase, putative
Sequence:
MIIKVNSVQTQKSQDGNKVHNSQDDMDNEEKSIRIYADGVYDLLHLGHMKQLEQAKHVDKNVTLIVGVTGDNETRKFKGQIVQTLEERTETLKHIRWVDEIISPCPWVITPEFMEEHKIDYVAHDDIPYANNQKKKKKKKSKGKSFSFDEENEDIYAWLKRAGKFKATQRTEGVSTTDLIVRILKNYEDYIERSLQRGIHPNELNIGVTKAQSIKMKKNLIRWGEKVTDELTKVTLTDKPLGTDFDQGIDIIRDKVHDLFKLWRYHSKKLLKDFAKSFDPMFIIIRKRYRKDNLSAMYLSDSNYFSSSMKDELKKKKSLSSTFNNIDEYYYSADEEDTRDNSFYRVINKIANHTYYSEKENYETCFELEHSLRDKKKSLIFKDKNMKLSPDDLLHFTNPMNSKYDHNYYYYNNTYDKLSNVTFNLNGIKKKSYDNESSYIKTAYHDIIDEDKNLLNKEKSFNKDEKKKKKSILETDQYKNCEDQQFDNKYNHIIIGKKKSDSTYDNSLDKESSNEKKLSIDKGQYSNMDSSNYFHDCKTMLSEHNESIESSNNDINGKQKEHIKKGNSENQDVDPDTNPDAVPDDDDDDDNSNDESEYESSQMDSEKNKGSIKNSKNVVIYADGVYDMLHLGHMKQLEQAKKLFENTTLIVGVTSDNETKLFKGQVVQTLEERTETLKHIRWVDEIISPCPWVVTPEFLEKYKIDYVAHDDIPYANNQKKKKKKKSKGKSFSFDEENEDIYAWLKRAGKFKATQRTEGVSTTDLIVRILKNYEDYIERSLQRGIHPNELNIGVTKAQSIKMKKNLIRWGEKVTDELTKVTLTDKPLGTDFDQGVENLQVKFKELFKIWKNASNKLITDFTRKLEATSYLTSIQNIIDYEIENDDYASSNFDDETSS
Protein: Desmin (F1R8W4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000256|ARBA:ARBA00004216}.
Interaction partners:
Sequence:
MSTKYSASAESASSYRRTFGSGLGSSIFAGHGSSGSSGSSRLTSRVYEVTKSSASPHFSSHRASGSFGGGSVVRSYAGLGEKLDFNLADAINQDFLNTRTNEKAELQHLNDRFASYIEKVRFLEQQNSALTVEIERLRGREPTRIAELYEEEMRELRRQVEALTNQRSRVEIERDNLVDDLQKLKLRLQEEIHQKEEAENNLSAFRADVDAATLARLDLERRIEGLHEEIAFLRKIHEEEIRELQNQMQESQVQIQMDMSKPDLTAALRDIRLQYEAIAAKNISEAEDWYKSKVSDLNQAVNKNNEALREAKQETMQFRHQLQSYTCEIDSLKGTNESLRRQMSEMEERLGREAGGYQDTIARLEAEIAKMKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRISLPVQSFSSLSFRESSPEQHHHQQQQPQRSSEVHSKKTVLIKTIETRDGEVVSESTQHQQDVM
Protein: Metallothionein-1G (MT-1G) (Metallothionein-1K) (MT-1K) (Metallothionein-IG) (MT-IG) (P13640)
Organism: Homo sapiens (Human)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Interaction partners:
- Metallothionein-1H
- Metallothionein-1F
- Metallothionein-1M
- Metallothionein
- Metallothionein-1X
- Metallothionein-2
Sequence:
MDPNCSCAAAGVSCTCASSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASEKCSCCA
Protein: ATP-dependent RNA helicase bel (EC 3.6.4.13) (Protein belle) (Q9VHP0)
Organism: Drosophila melanogaster (Fruit fly)
Function: ATP-dependent RNA helicase that is essential and required for cellular function, larval growth, and for male and female fertility. Also required for RNA interference (RNAi), double-stranded RNA induces potent and specific gene silencing, by acting downstream of dsRNA internalization. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15572142}. Note=In nurse cells, follicle cells, and within the oocyte. Vas and bel colocalize in the perinuclear region of nurse cells.
Interaction partners:
- LD07162p
- Protein argonaute-2
- Protein argonaute-1
- Fragile X messenger ribonucleoprotein 1 homolog
- Endoribonuclease Dcr-2
- ATP synthase subunit alpha, mitochondrial
- 116 kDa U5 small nuclear ribonucleoprotein component
- ATP synthase subunit gamma, mitochondrial
- Protein Gawky
- LD06392p
Sequence:
MSNAINQNGTGLEQQVAGLDLNGGSADYSGPITSKTSTNSVTGGVYVPPHLRGGGGNNNAADAESQGQGQGQGQGFDSRSGNPRQETRDPQQSRGGGGEYRRGGGGGGRGFNRQSGDYGYGSGGGGRRGGGGRFEDNYNGGEFDSRRGGDWNRSGGGGGGGRGFGRGPSYRGGGGGSGSNLNEQTAEDGQAQQQQQPRNDRWQEPERPAGFDGSEGGQSAGGNRSYNNRGERGGGGYNSRWKEGGGSNVDYTKLGARDERLEVELFGVGNTGINFDKYEDIPVEATGQNVPPNITSFDDVQLTEIIRNNVALARYDKPTPVQKHAIPIIINGRDLMACAQTGSGKTAAFLVPILNQMYELGHVPPPQSTRQYSRRKQYPLGLVLAPTRELATQIFEEAKKFAYRSRMRPAVLYGGNNTSEQMRELDRGCHLIVATPGRLEDMITRGKVGLENIRFLVLDEADRMLDMGFEPQIRRIVEQLNMPPTGQRQTLMFSATFPKQIQELASDFLSNYIFLAVGRVGSTSENITQTILWVYEPDKRSYLLDLLSSIRDGPEYTKDSLTLIFVETKKGADSLEEFLYQCNHPVTSIHGDRTQKEREEALRCFRSGDCPILVATAVAARGLDIPHVKHVINFDLPSDVEEYVHRIGRTGRMGNLGVATSFFNEKNRNICSDLLELLIETKQEIPSFMEDMSSDRGHGGAKRAGRGGGGRYGGGFGSRDYRQSSGGGGGGRSGPPPRSGGSGSGGGGGSYRSNGNSYGGNSGGGGYYGGGAGGGSYGGSYGGGSASHSSNAPDWWAQ
Protein: Cell death peptidase (Bacteriophage T4 late gene expression-blocking protein) (GpLit) (P11072)
Organism: Escherichia coli (strain K12)
Function: Interacts with a short DNA sequence about one-quarter of the way into the major capsid protein gene 23 of T4; general translation inhibition occurs when this late gene of the virus is expressed.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YmfI
- Uncharacterized protein YmfD
- Uncharacterized protein YmfE
- Type IV methyl-directed restriction enzyme EcoKMcrA
Sequence:
MRSPICHLFSAINSSPFKIAPEKEQDLKTIVDDKKIIISVVSEPGFNIRVRKNESNNSHEIVLTVASLEYIWAFSNFFWVFTQEYSKSQKNNDEHFDLTGKNRLKKSDELLKWARKNLQTTGCESWPKKCPKPEAYLQGSEDSQVASEIFLCAIAWILHHEISHVVLQHPLVTTAFSTQEEREADSHATKWILGNLYESAPELKKRALGIATAVLCIQSLEVENYFCLQNTHPAAYERIYSNISCYPVGNEELIEALCTVMLQYLFHGKNINVNLDGESFSSILGDLLCDISRLTSN
Protein: Signal transducer and activator of transcription 2 (Q9WVL2)
Organism: Mus musculus (Mouse)
Function: Signal transducer and activator of transcription that mediates signaling by type I interferons (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In addition, has also a negative feedback regulatory role in the type I interferon signaling by recruiting USP18 to the type I IFN receptor subunit IFNAR2 thereby mitigating the response to type I IFNs. Acts as a regulator of mitochondrial fission by modulating the phosphorylation of DNM1L at 'Ser-616' and 'Ser-637' which activate and inactivate the GTPase activity of DNM1L respectively.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P52630}. Nucleus {ECO:0000250|UniProtKB:P52630}. Note=Translocated into the nucleus upon activation by IFN-alpha/beta. {ECO:0000250|UniProtKB:P52630}.
Interaction partners:
- Interferon regulatory factor 9
- Signal transducer and activator of transcription 1
- Histone lysine acetyltransferase CREBBP
- Interferon alpha/beta receptor 1
- Non-receptor tyrosine-protein kinase TYK2
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase JAK1
- Tyrosine-protein kinase JAK3
- Interferon alpha/beta receptor 2
- Signal transducer and transcription activator 6
Sequence:
MAQWEMLQNLDSPFLDQLHQVYSQSFLPMDFRQHLASWIEDQNWREAALESDDAKANMLYFSILDQLNQWDHYSSDPKSLLLQHNLRKFSRDIQPFPNGPSQLAEMIFNLLLEEQRILIQAQRAQEVQPPPAPEAVVESQQLEIENRIQGLHVDIEFLVRSIRQLKDEQDVFSFRYTVFSLKKTSSSDPHQSQQAHVVQATANKVDRMRKEVLDISKGLVGRLTTLVDLLLPKLDEWKVQQQKSCIGAPPPVKSAAEQLEQWLTAGAKFLFHLRQLLKQLKEMSCLRYQGDMFAKGVDLRNAQVMELLQRLLQRSFVVETQPCMPQTLHRPLILKTGNKFTVRTRLLVRLQEGSESLKAEVSVDRNSDLPGFRKFNILTSNQKTLTPEKGQRQGLIWDFGFLTLVEQRAVGAGKGNNKGPLAVTEELHVISFVVEYTYQGLKMKLQTDTLPVVIISNMNQLSFAWASILWFNMLSPNPKNQQFFCQAPKAPWSLLGPVLSWQFSSYVARGLDSEQLGMLRTKLFGKSCKMEDALLSWVDFCKRESPPGKIPFWTWLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVEHQDDHKVEIYSVQPYTKEVLQSLPLTEIIRHYQVLAEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLEEQEEYLKHKLIVISNRQVDELQQPLELKQDSESLEVNAELLLAHDQELPLMMQTGLVLGTELKVDPILSTAPQVLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELAPQVLLEPAPQVLLELAPQVQLEPAHLLQQPSESDLPEDLQQISVEDLKKLSNPSTEYITTNENPMLAGESSGDETSIPYHSHFDADGLLGWTLDTF
Protein: Alhambra, isoform H (E1JJ76)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMMMDTMDTSQSQPMDVAPAVAVAATSGAALVDFTAAMVSMAATAEAESAESNNNHIDMAEYKEHRKNKKKKREKREREGKEHRHHKHRDREHREHRRHRDRDRDKERDREGHHHHPTHHHPNNSQHSTSASSSPSSASTTPSATIEYVGGSASASPSYLGGGATGTGAAVGATTTYPHNLKIRFLLSGQRTELSPPTHQTSATAEVNAPLASSTSASIAVTASATAASAPPATGTTTLGSSISGNAGSTSSGNSSGVSATGGAQSAVGSGGYPKTESSKSSGTASAGSGSGSSSNTSSTKHGSNIKDISSSSNQQASTASSSSAPSLYVSVPLSTANVPGINLPTSSTSSSTTSESHSASSRSSGAQSQHQQQLSNALVGPPMGGSAGAFHGGTTSAGSSSVIQQQSGKSSPALGTLVSGNSGGSIISASGFPLPSGNLTATTTESGNLKISYEKQTTRVQQLQEQEAPPARRSRTLDLSTASASSSSPSAVPATTSPLVVLSNQLPLNSVAASSSTGGLKFTYESQTQMDVPMMPVSAIKDSPPSSPGSEIGSAMHSATTAPGSLTGASTAATAQPGNVRKRGRKAKDATIAAAAAAAAAAAALSNSQQDLKDVRILQNGASNTPGNPAGSTPTPPATPASSNAVSSASSIITHTAAHMLGNQINPNSSVAQKLSEQLHMEVQDHSIYTPDSMNSQYAGVPFPGKQRNSTAVPSNATPAQNPLQSMFSGGGMNGNMPIPQSLEQLLERQWEQGSQFLMEQAQHFDIASLLNCLHQLQSENLRLEEHVTSLIARRDHLLAVNARLQIPLSTIASNTKAEAHAAISTTAAPTTTTTTSTTTATSTCTTSVISTIASSGNSSTSTIGLGSSTSALNAATTIAAAVSLATTAINTTIPTMANSRPTVAAASSSGVLDYRGPGATSNSSNSNSSNNTISNSVSNSSSNPTSSSSASVPPASSMSISGMSISNATNLGMRHVSAAHGSNNAGNSNSSVWSLTASSTVNSNSLHHQHSSQQQQQHQAQHQSHPLQQQQQQQQQVQHHLHQSHHTSAAVAAAHMLGVGMSLGAGGGAAGGIGRGGSATAMAATAATTTTTFTTTAGTGMGQQHHHPHPHQHPSIQIQVGGGGVGVDGLSSTSSSYAVHHAALYSTHHQSQLRRDDNLAKTS
Protein: Importin-alpha re-exporter (Cellular apoptosis susceptibility protein homolog) (O13671)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Export receptor for importin alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates have been released into the nucleoplasm (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- GTP-binding nuclear protein spi1
- Importin subunit beta-1
- Importin subunit alpha-1
- Importin subunit alpha-2
- Importin subunit beta-2
- Exportin-1
- Importin subunit beta-5
Sequence:
MDDIPTLLARTLNPTTSKSAEEALKVWELQDSSFALKLLNIVAEDTVDINIKLAASLYFKNYIKKHWDSEEGASIRISDEVAELIKREIINLMLKSTTIIQVQLGEVIGYIANFDFPDRWDTLLPDLISKLSAVDMNTNIAVLSTAHAIFKRWRPLFRSDALFLEIKYVLDRFCEPFLALFVQTNNLLRNGPQDAESLNSLFQVILLECKLFYDLNCQDIPEFFEDHMSEFMTAFLNYFTYTNPSLEGDEGETNVLIKVKASICEIVELYTLRYEEVFTMLYDFVNVTWTLLTTLTPDEKYDGLVGKAMAFLTSVIRIRKHAEFFQQDQVLQQFIELVVLPNICLRESDEELFEDDPLEYVRRDLEGSNSDSRARSAIVLVRGLLDHFDQKITSVVSTHINANLQQFSTNPSLEWNKKYVALQLFSAIAIKGQSTRLGVTSINLMVDVVAFFENNIKPDLLQPAGVIHPMVLAEDIKYVFTFRNQLNSQQLIDIFPTILRFLEMPSFVVYTYAAIALDQLLTVRHNHVHIFTSLLIAPHILPALNQLFLIVESASTPQKLAENDYLMKAVMRIIIMSQEAILPAASLLLQHLTKITEEVSKNPSNPKFNHYLFESIGALIRSLSKSGPQTVSQLENALLPVFQNVLIEDVTEFIPYVLQLLSQLVEASGNEPLPDFVVNLIQPCLSPALWDSKGNIPALVRLLRAMIFRGPQIFISNKFVEPVLGIFQKLISSKVNDHFGFDLLDRVFTVFNANILAPYINHIFFLLLSRLKNSRTERFVLRCTIFFFFVASEQTGTCGPDNLIQGVDAVQSGVFGQLMTSIILPQAQKLALPLDRKISALGLLRLLTCDLVLAPDAIYENLIIPLLTCILKLFEMPIEQAQTDADEELFMDEIDADSMSFQASFSRLATTGGKRVDPFPQITDLKQYCATEMNLANRNMGGRLSQIISTHLPGDGQSVLQSYGYVI
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (A1A5Z2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIRGVKRERDFDEDEEEEVRVKVGRGYVEDRRSRHCPYLDTINRSVLDFDFEKLCSISLSHINVYACLICGKYFQGRGQKSHAYIHSVQVAHHVFLNLHTLKFYCLPDNYEIIDSSLEDITYVLKPTFTKQHISGLDKQGKLYRAYDGTTYLPGIVGLNNIKANDYANVVLQALSNVPPLRNYFLEEENYRGIRRPPGDIMFLLVQRFGELMRKLWNPRNFKAHVSPHEMLQAVVLCSKKTFQITKQGDAVDFLSWFLNALHGALGGTKKKSSIITKAFQGSMRIFSKKLPHPDLPPEEKEALLLKEEYQEEMSESTFLYLTLDLPTAPLYKDEKEQLIIPQVPLFNILGKFNGNTEKEYKTYKENFLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYLTEEAQVTEKNTTYDLVANVVHDGKPTEGSYRIHVLHHGTGKWYELQDLQVIDILPQMITLSEAYIQIWKRQDKQDGAKSHTGA
Protein: Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (P19414)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Can also provide minor contributions to the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. Also plays an essential role in mtDNA maintenance. May directly protect mtDNA from accumulation of point mutations and ssDNA breaks as a component of mitochondrial nucleoids, or by preventing accumulation of iron citrate thereby alleviating its detrimental effects in mitochondria.
Subcellular location: Mitochondrion. Cytoplasm. Note=Mainly mitochondrial, small amounts are also detected in the cytosol with a ratio of 94:6.
Interaction partners:
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Citrate synthase, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Citrate synthase, peroxisomal
- Isocitrate dehydrogenase cytoplasmic
- Citrate synthase 3, mitochondrial
- Isocitrate dehydrogenase
- Isocitrate lyase
- Mitochondrial 2-methylisocitrate lyase ICL2
Sequence:
MLSARSAIKRPIVRGLATVSNLTRDSKVNQNLLEDHSFINYKQNVETLDIVRKRLNRPFTYAEKILYGHLDDPHGQDIQRGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPVTVHCDHLIQAQVGGEKDLKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGKIADFAKLYHKDLLSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVANNWPLDVRVGLIGSCTNSSYEDMSRSASIVKDAAAHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQWDRRDIKKGDKNTIVSSYNRNFTSRNDGNPQTHAFVASPELVTAFAIAGDLRFNPLTDKLKDKDGNEFMLKPPHGDGLPQRGYDAGENTYQAPPADRSTVEVKVSPTSDRLQLLKPFKPWDGKDAKDMPILIKAVGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNVYTGEYKGVPDTARDYRDQGIKWVVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDRIDILGLAELAPGKPVTMRVHPKNGKPWDAVLTHTFNDEQIEWFKYGSALNKIKADEKK
Protein: Portal protein (Gene product 8) (Gp8) (Head-to-tail connector) (P03728)
Organism: Escherichia phage T7 (Bacteriophage T7)
Function: Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04120, ECO:0000269|PubMed:23884409}.
Interaction partners:
Sequence:
MAEKRTGLAEDGAKSVYERLKNDRAPYETRAQNCAQYTIPSLFPKDSDNASTDYQTPWQAVGARGLNNLASKLMLALFPMQTWMRLTISEYEAKQLLSDPDGLAKVDEGLSMVERIIMNYIESNSYRVTLFEALKQLVVAGNVLLYLPEPEGSNYNPMKLYRLSSYVVQRDAFGNVLQMVTRDQIAFGALPEDIRKAVEGQGGEKKADETIDVYTHIYLDEDSGEYLRYEEVEGMEVQGSDGTYPKEACPYIPIRMVRLDGESYGRSYIEEYLGDLRSLENLQEAIVKMSMISSKVIGLVNPAGITQPRRLTKAQTGDFVTGRPEDISFLQLEKQADFTVAKAVSDAIEARLSFAFMLNSAVQRTGERVTAEEIRYVASELEDTLGGVYSILSQELQLPLVRVLLKQLQATQQIPELPKEAVEPTISTGLEAIGRGQDLDKLERCVTAWAALAPMRDDPDINLAMIKLRIANAIGIDTSGILLTEEQKQQKMAQQSMQMGMDNGAAALAQGMAAQATASPEAMAAAADSVGLQPGI
Protein: Bifunctional epoxide hydrolase 2 [Includes: Cytosolic epoxide hydrolase 2 (CEH) (EC 3.3.2.10) (Epoxide hydratase) (Soluble epoxide hydrolase) (SEH); Lipid-phosphate phosphatase (EC 3.1.3.76)] (P80299)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators (By similarity). The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid (By similarity).
Subcellular location: Cytoplasm. Peroxisome.
Interaction partners:
- Cytochrome P450, family 2, subfamily j, polypeptide 4
- Cytochrome P450 2C11
- Purine nucleoside phosphorylase
- S-methyl-5'-thioadenosine phosphorylase
- Cytochrome P450 2C23
- Protein kinase AMP-activated non-catalytic subunit gamma 2
- Protein kinase AMP-activated non-catalytic subunit gamma 3
- NAD-capped RNA hydrolase NUDT12
- Cytochrome P450 2C7
- NAD
Sequence:
MALRVAAFDLDGVLALPSIAGVLRHTEEALALPRDFLLGAFQMKFPEGPTEQLMKGKITFSQWVPLMDESCRKSSKACGASLPENFSISEIFSQAMAARSINRPMLQAAAALKKKGFTTCIVTNNWLDDSDKRDILAQMMCELSQHFDFLIESCQVGMIKPEPQIYKFVLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVRDTASALRELEKVTGTQFPEAPLPVPCSPNDVSHGYVTVKPGIRLHFVEMGSGPAICLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCEEMVTFLNKLGIPQAVFIGHDWAGVLVWNMALFHPERVRAVASLNTPLMPPNPEVSPMEVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRTSDDMGLLTVNKATEMGGILVGTPEDPKVSKITTEEEIEYYIQQFKKSGFRGPLNWYRNTERNWKWSCKALGRKILVPALMVTAEKDIVLRPEMSKNMENWIPFLKRGHIEDCGHWTQIEKPAEVNQILIKWLKTEIQNPSVTSKI
Protein: Carboxysome shell protein CcmK3 (Carbon dioxide-concentrating mechanism protein CcmK3) (Q31RK3)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: A non-essential, minor shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Hexamers form sheets that form the facets of the polyhedral carboxysome. In PCC 7942 there are several CcmK paralogs with presumably functional differences. This subunit probably only makes heterohexamers with CcmK4. The CcmK3-CcmK4 heterohexmers have been suggested to cap other hexamers, perhaps to alter metabolite flux (Probable).
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000269|PubMed:30389783, ECO:0000269|PubMed:31048338, ECO:0000305|PubMed:25117559}. Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000269|PubMed:25117559}.
Interaction partners:
- Carboxysome shell vertex protein CcmL
- Carboxysome shell protein CcmP
Sequence:
MPIAVGTIQTLGFPPIIAAADAMVKAARVTITQYGLAESAQFFVSVRGPVSEVETAVEAGLKAVAETEGAELINYIVIPNPQENVETVMPIDFTAESEPFRS
Protein: Cullin-1 (OsCUL1) (OsCUL1-1) (Q5ZC88)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- SKP1-like protein
- SKP1-like protein 1
- COP9 signalosome complex subunit 5
- Coronatine-insensitive protein homolog 1a
- Os01g0185400 protein
- Os01g0106800 protein
- Os02g0708300 protein
- Defective in cullin neddylation protein
- COP9 signalosome complex subunit 1, putative, expressed
- Os02g0169800 protein
Sequence:
MATHERKTIDLEQGWEFMQKGITKLKNILEGKPEPQFSSEDYMMLYTTIYNMCTQKPPHDYSQQLYEKYRESFEEYITSMVLPSLREKHDEFMLRELVKRWSNHKVMVRWLSRFFHYLDRYFISRRSLPQLSEVGLSCFRDLVYQEIKGKVKSAVISLIDQEREGEQIDRALLKNVLDIFVEIGLTSMDYYENDFEDFLLKDTADYYSIKAQTWILEDSCPDYMLKAEECLKREKERVAHYLHSSSEQKLLEKVQHELLTQYASQLLEKEHSGCHALLRDDKVDDLSRMYRLFSRITRGLEPVSQIFKQHVTNEGTALVKQAEDAASNKKPEKKEIVGLQEQVFVRKIIELHDKYVAYVTDCFQGHTLFHKALKEAFEVFCNKGVSGSSSAELLATFCDNILKKGGSEKLSDEAIEDTLEKVVRLLAYISDKDLFAEFYRKKLARRLLFDKSANDEHERSILTKLKQQCGGQFTSKMEGMVTDLTVARDHQAKFEEFISTHSELNPGIALAVTVLTTGFWPSYKSFDINLPAEMVKCVEVFKEFYQTRTKHRKLTWIYSLGTCNINAKFEAKTIELIVTTYQAALLLLFNGVDRLSYSEIVTQLNLSDDDVVRLLHSLSCAKYKILSKEPNNRSISPNDVFEFNSKFTDKLRRLKIPLPPVDEKKKVVEDVDKDRRYAIDASIVRIMKSRKVLGHQQLVMECVEQLGRMFKPDFKAIKKRIEDLITRDYLERDKDNPNVYRYLA
Protein: Valerianol synthase TPS1E (EC 4.2.3.204) (Terpene synthase 1e) (ChTps1e) (A0A348AUV9)
Organism: Camellia hiemalis (Camellia)
Function: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol, which is a volatile compound of floral scent.
Interaction partners:
Sequence:
MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNGEFKETMSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVGGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHFVGRAVLTKIMLLLSVTDDTYDAYGTYDELKLYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRDYGVHHSKEAFKEIVRSYEIEAEWFKEGYVASFEAYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVAASGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQHGVSKQEAIVELYKMIENAWRDINEEILKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIIKDHVISLFEDPIPM