wanglab/gogpt-training-data huggingface dataset:
Protein: Hydrogenase expression/formation protein HypC (Q5JII0)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Interaction partners:
- hydrogenase expression/formation protein HypD
- Hydrogenase expression/formation protein HypE
- Hydrogenase maturation factor HypA
- Carbamoyltransferase
- Cytosolic NiFe-hydrogenase, alpha subunit
Sequence:
MCLAVPGKVIEVNGPVAVVDFGGVKREVRLDLMPDTKPGDWVIVHTGFAIEKLDEKKAMEILEAWAEVEKAMEGF
Protein: N-lysine methyltransferase SMYD2 (EC 2.1.1.-) (Histone methyltransferase SMYD2) (EC 2.1.1.354) (SET and MYND domain-containing protein 2) (Q8R5A0)
Organism: Mus musculus (Mouse)
Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Subcellular location: Cytoplasm, cytosol. Nucleus.
Interaction partners:
- Cellular tumor antigen p53
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Histone-lysine N-methyltransferase SETD7
- Histone H3.2
- Histone H3.1
- Calmodulin-lysine N-methyltransferase
- Actin-histidine N-methyltransferase
Sequence:
MRAEARGGLERFCSAGKGRGLRALRPFHVGDLLFSCPAYACVLTVGERGHHCECCFARKEGLSKCGRCKQAFYCDVECQKEDWPLHKLECSSMVVLGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVREFESHLDKLDNEKKDLIQSDIAALHQFYSKYLEFPDHSSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIHPGDEVFTSYIDLLYPTEDRNDRLRDSYFFTCECRECTTKDKDKAKVEVRKLSSPPQAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALKYGQKIIKPYSKHYPVYSLNVASMWLKLGRLYMGLENKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
Protein: Aspartokinase 2, chloroplastic (EC 2.7.2.4) (Aspartate kinase 2) (O23653)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- aspartate-semialdehyde dehydrogenase
- Homoserine dehydrogenase
- Homoserine kinase
- Diaminopimelate epimerase, chloroplastic
- Asparagine synthetase 1
- Argininosuccinate synthase, chloroplastic
- Cystathionine gamma-synthase 1, chloroplastic
- Probable cystathionine gamma-synthase 2
- 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic
- Asparagine synthetase 2
Sequence:
MASLQLYGVKTPGLALSSKRLEFASKGACFSVTLPSSSAVFRDVEHSCRNIGLRVSCEALRVDLLQRKEPETCDSSGTGKELTCVMKFGGSSVESAERMKEVANLILSFPDERPVIVLSAMGKTTNKLLKAGEKAVTCGVTNVESIEELSFIKELHLRTAHELGVETTVIEKHLEGLHQLLKGISMMKELTLRTRDYLVSFGECMSTRLFSAYLNKIGHKARQYDAFEIGFITTDDFTNADILEATYPAVSKTLVGDWSKENAVPVVTGYLGKGWRSCAITTLGRGGSDLTATTIGKALGLREIQVWKDVDGVLTCDPNIYPGAQSVPYLTFDEAAELAYFGAQVLHPLSMRPARDGDIPVRVKNSYNPTAPGTVITRSRDMSKAVLTSIVLKRNVTMLDIASTRMLGQYGFLAKVFTTFEDLGISVDVVATSEVSISLTLDPAKLWGRELIQRVNELDNLVEELEKIAVVKLLQRRSIISLIGNVQKSSLILEKVFQVFRSNGVNVQMISQGASKVNISLIVNDEEAEQCVRALHSAFFETDP
Protein: Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (PEPCK-C) (EC 4.1.1.32) (Serine-protein kinase PCK1) (EC 2.7.11.-) (Q9Z2V4)
Organism: Mus musculus (Mouse)
Function: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis. Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle. At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate. Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis. The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis. In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (By similarity). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35558}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35558}. Note=Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P35558}.
Interaction partners:
- Pyruvate carboxylase, mitochondrial
- Pyruvate kinase PKLR
- ATP-citrate synthase
- Citrate synthase
- Citrate synthase, mitochondrial
- Pyruvate kinase PKM
- Malate dehydrogenase, cytoplasmic
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Malate dehydrogenase, mitochondrial
- Alpha-enolase
Sequence:
MPPQLHNGLDFSAKVIQGSLDSLPQAVRKFVEGNAQLCQPEYIHICDGSEEEYGQLLAHMQEEGVIRKLKKYDNCWLALTDPRDVARIESKTVIITQEQRDTVPIPKTGLSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIELTDSPYVVASMRIMTRMGISVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPSLPGWKVECVGDDIAWMKFDAQGNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDAEPCAHPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPEGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPFAMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKDGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYIPKENALNLKGLGGVNVEELFGISKEFWEKEVEEIDRYLEDQVNTDLPYEIERELRALKQRISQM
Protein: Conserved protein (O05312)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable DNA-3-methyladenine glycosylase I TagA
- DUF4177 domain-containing protein
- Conserved protein
Sequence:
MLGADQARAGGPARIWREHSMAAMKPRTGDGPLEATKEGRGIVMRVPLEGGGRLVVELTPDEAAALGDELKGVTS
Protein: Dystrophin, isoform D (Protein detached) (Q0KI50)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the maintenance of appropriate synaptic retrograde communication and the stabilization of muscle cell architecture or physiology. May play a role in anchoring the cytoskeleton to the plasma membrane.
Subcellular location: Cell membrane, sarcolemma {ECO:0000269|PubMed:16399704}; Peripheral membrane protein {ECO:0000269|PubMed:16399704}; Cytoplasmic side {ECO:0000269|PubMed:16399704}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16399704}.
Interaction partners:
Sequence:
MTTTITAKIAQRQQQHQQHQQQQLQHQQQQQQQQQHQPTSSMNGFRITGYPAAATPPARSNPIYAKPNAHELDLHISESLLYPGSTTQQQQALQSSPGPPPQLTSMLPSSGLPGAAQPIALKGNNPFLNSPSPTEAAPGVPTGLSSAQPATSASSGNYEMPEYAEPSRLRGLKQRPHSIAVGGSPAQSSFVDYNAQQQQRLLQLSRQQQQLRNAVTAAASTANGGDKETLYAALFQQYRQSPTNGQPAPPVPLHRKPAAAPVVPRRSQSTPRPPLQQQQQQQQAGINGQINGNGNQRPRSLDRFNGGLQSEAPPIPLRRFPNGNGNNNNGTLSRQKSPKKSSSADNMLMSPAGSQVNTMRHSISFHGGQETENGSKAEQTRPMSYAAPAPDQAYLEHQLRAYSEQLRTITESVRKYSEQAKLLSELKRQQQLAKQSQTNLNLLTPTTCNNSTGSNGNNNFQPNMISPEIVSKSLASLSTSQANEAQTPSNQLRLFLDNIRSSMRQEYQQHMPDDVLKPTSTLKRNGTDSLVTSNTAAKPEVEATPTPSDQLRQFLDAIRANKIPESVDKPKMTSSQTLDSFISKPLQMPDVTSGTPGGGVVGGQAASGGVAVNGQTNGIPTRRRPKSSIIPSSSNGKLEQREHSLVTSESFHQISDNLRLMSEDLQALSPSKAIPSSASSNSLKSLAANGGSSLTTELRVITSSPYSTSPKLQQMVMSKSNSSLGSVTTPSSATTTPSTAPMITDFNEILDSFQAMADKYKSKGSYDYLRKCSEALRQHSLQLKLQQQHQAHQQQQLPAHQQQQHQQQQQQQIQNGFASDDNSSSCSTTPGSIREAVQNLLLQPRNGFQILDDRMRLFIDIIDSQDRLSQDLQSEIETHRVVYDRLDGTGRKLLGSLTSQEDAVMLQRRLDEMNQRWNNLKSKSIAIRNRLESNSEHWNALLLSLRELTEWVIRKDTELSTLGLGPVRGDAVSLQKQLDDHKAFRRQLEDKRPIVESNLTSGRQYIANEAAVSDTSDTEANHDSDSRYMSAEEQSRELTRSIRREVGKLSEQWNNLIDRSDNWKHRLDEYMTKMRQFQKILEDLSSRVALAEQTKTSWLPPSSVGEANEQMQQLQRLRDKMTTASALLDDCNEQQSFFTANQVLVPTPCLSKLEDLNTRMKLLQIAMDERQKVLCQAGAQQTHENGDDGRTTSNSGTIGPLPNLGQSVKPPWERATTAANVPYYIDHERETTHWDHPEMIELMKGLADLNEIRFSAYRTAMKLRSVQKRLALDRISMSTACESFDRHGLRAQNDKLIDIPDMTTVLHSLYVTIDKIDLTLMLDLAINWILNVYDSQRTGQIRVLSFKVGLVLLCKGHLEEKYRYLFRLVADTDRRADQRRLGLLLHDCIQVPRQLGEVAAFGGSNIEPSVRSCLEQAGISQEAIDGNQDISIELQHFLGWLQHEPQSLVWLPVLHRLAAAEAAKHQAKCNICKEYPIVGFRYRCLKCFNFDMCQKCFFFGRNAKNHKLTHPMHEYCTTTTSTEDVRDFTRALKNKFKSRKYFKKHPRVGYLPVQSVLEGDALESPAPSPQHTTHQLQNDMHSRLEMYASRLAQVEYGGTGSNSTPDSDDEHQLIAQYCQALPGTSNGSAPKSPVQVMAAMDAEQREELEAIIRDLEEENANLQAEYQQLCSKEQSGMPEDSNGMQHSSSSMTGLSGQGEQGQDMMAEAKLLRQHKGRLEARMQILEDHNRQLEAQLQRLRQLLDEPNGGGSSATSSGLPSAPGSALNSKPNTLQTRSVTASQLNTDSPAKMNQQNGHYEHNSKNSSGLVTVITEQELESINDDLEDSSSSNTTNTTTTTTTTATTEKTCVELQK
Protein: L-dopachrome tautomerase (DCT) (DT) (EC 5.3.3.12) (L-dopachrome Delta-isomerase) (Tyrosinase-related protein 2) (TRP-2) (TRP2) (P40126)
Organism: Homo sapiens (Human)
Function: Plays a role in melanin biosynthesis. Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA).
Subcellular location: Melanosome membrane {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}; Single-pass type I membrane protein {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000250|UniProtKB:P29812}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000250|UniProtKB:P29812}.
Interaction partners:
- Tyrosinase
- Microphthalmia-associated transcription factor
- Melanoma antigen recognized by T-cells 1
- Melanocyte protein PMEL
- Transcription factor SOX-10
- Membrane-associated transporter protein
- Paired box protein Pax-3
- Heat shock 70 kDa protein 4
- Melanocyte-stimulating hormone receptor
- Pro-opiomelanocortin
Sequence:
MSPLWWGFLLSCLGCKILPGAQGQFPRVCMTVDSLVNKECCPRLGAESANVCGSQQGRGQCTEVRADTRPWSGPYILRNQDDRELWPRKFFHRTCKCTGNFAGYNCGDCKFGWTGPNCERKKPPVIRQNIHSLSPQEREQFLGALDLAKKRVHPDYVITTQHWLGLLGPNGTQPQFANCSVYDFFVWLHYYSVRDTLLGPGRPYRAIDFSHQGPAFVTWHRYHLLCLERDLQRLIGNESFALPYWNFATGRNECDVCTDQLFGAARPDDPTLISRNSRFSSWETVCDSLDDYNHLVTLCNGTYEGLLRRNQMGRNSMKLPTLKDIRDCLSLQKFDNPPFFQNSTFSFRNALEGFDKADGTLDSQVMSLHNLVHSFLNGTNALPHSAANDPIFVVLHSFTDAIFDEWMKRFNPPADAWPQELAPIGHNRMYNMVPFFPPVTNEELFLTSDQLGYSYAIDLPVSVEETPGWPTTLLVVMGTLVALVGLFVLLAFLQYRRLRKGYTPLMETHLSSKRYTEEA
Protein: Plexus, isoform D (A0A0B4KFF4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMEWLPRGLPSIHAPIPICVPPKAGQKRPATSPAPHIPVPHHLQTPPGGGAGGLPGSSVANSPIPSSAGGNALMNHALPNNHIGTPSPQQQHQHQQHQQQQQQQQHQAQQQAQQQAVAAAVQQQLAAGVGLPPGAIGAASASSRGSFAAALRTLAKQADIKEEDVGGDRSVPTSGAGGPPPSSSGPGSLNSVAGRVGSERPGEDRVSSNKKRSPPSPQPPEKIARLSHTPQTASLQPELLARSGFQPYRSDERLMHPAGAFPLEAYSHFAGLQGIPPAFLNPAGLPYTEQLYLEHRYQLFRAAGAHPSHPHAAALYPQMASPYSHLYSMMPGAALGISPAMHDRMKLEEEHRARLAREEEREREIQREKERELREQREKEQREKEQREKEQREREQREKEQREKEARERKLRDEERERERERQQLLTASHHYSNQLYSPLNRNLLGSMIPHLNMSLRGPPGALHGLPGMSHYHAAAANAQRQSPHGAMGLNLGMAGLPGVPPLGGHGPNLQHHLQQAAMGLAHPGAAGLTHPGFSAAALGLGAHPHSLNLSHPHMSPHHPASLAHQLPPHTSSAGGGGLSNSIPVTASSSLSASSPHTSLNLTSSVKLSADQVPTSTPSGGVSGSGMPPTTSSSHIPNMGHYYHHGHLAAMHAAAAAASGMTPTAAHQQQPLSLPSSPKITPPITPSSSANGGRAGGSPHAMRHHIAAAVAAAAQQSAMIDKAATPVTHEPTTLDLTGSNSNSSNQAPSNASSGQPTNHEVNGAESNGASQTESKEHLAIKEDGHKSSPPPVALEKKPATPNAAADKPIHPDSSPENSSRRSASPQSDANNSLPAVSVTAAASGKCKEETPKILDSDTTATTKTDIEEEKQRARLSVSPTPTAPKIMVASPDTVSTSGGVTSTTSGTTPPPVVSSSTSSAGKAPALTSDEVSTSAATSAAEPTR
Protein: tRNA 2'-phosphotransferase (EC 2.7.1.160) (Q12272)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Interaction partners:
- tRNA ligase
- tRNA-splicing endonuclease subunit SEN34
- tRNA-splicing endonuclease subunit SEN54
- tRNA-splicing endonuclease subunit SEN2
- tRNA-splicing endonuclease subunit SEN15
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
Sequence:
MRQVLQKDKRDVQLSKALSYLLRHTAVKEKLTIDSNGYTPLKELLSHNRLKTHKCTVDDIHRIVKENDKQRFHIKTLGADEEWICATQGHSIKSIQPSDEVLVPITEASQLPQELIHGTNLQSVIKIIESGAISPMSRNHVHLSPGMLHAKGVISGMRSSSNVYIFIDCHSPLFFQTLKMFRSLNNVYLSSSIPVELIQKVVVKGNLKDEEKLDTLRRILHERNIPLEKI
Protein: Phage shock protein C (Q9F4H2)
Organism: Yersinia enterocolitica
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MGDMFKNNSFKNDSFKNYSFKNNVLSKKKLYRVPEEGMIKGVCAGLAHYFDIPVRLIRVMVVLSLFFGLFVFTIAAYIVLTFVLEPAPASSFSEHREATPRQLLDQLEYELGAGEQRLRQVERYVTSETFGVQSRFRQL
Protein: Mitogen-activated protein kinase kinase kinase 2 (EC 2.7.11.25) (MAPK/ERK kinase kinase 2) (MEK kinase 2) (MEKK 2) (Q9Y2U5)
Organism: Homo sapiens (Human)
Function: Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15075238}. Nucleus {ECO:0000269|PubMed:15075238}. Note=Upon EGF stimulation, translocates into the nucleus.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 5
- Histone-lysine N-methyltransferase SMYD3
- Mitogen-activated protein kinase kinase kinase 3
- Dual specificity mitogen-activated protein kinase kinase 3
- Dual specificity mitogen-activated protein kinase kinase 6
- Serine/threonine-protein kinase PAK 2
- Serine/threonine-protein kinase PAK 1
- Proto-oncogene tyrosine-protein kinase Src
- Mitogen-activated protein kinase 7
- E3 ubiquitin-protein ligase XIAP
Sequence:
MDDQQALNSIMQDLAVLHKASRPALSLQETRKAKSSSPKKQNDVRVKFEHRGEKRILQFPRPVKLEDLRSKAKIAFGQSMDLHYTNNELVIPLTTQDDLDKAVELLDRSIHMKSLKILLVINGSTQATNLEPLPSLEDLDNTVFGAERKKRLSIIGPTSRDRSSPPPGYIPDELHQVARNGSFTSINSEGEFIPESMDQMLDPLSLSSPENSGSGSCPSLDSPLDGESYPKSRMPRAQSYPDNHQEFSDYDNPIFEKFGKGGTYPRRYHVSYHHQEYNDGRKTFPRARRTQGTSLRSPVSFSPTDHSLSTSSGSSIFTPEYDDSRIRRRGSDIDNPTLTVMDISPPSRSPRAPTNWRLGKLLGQGAFGRVYLCYDVDTGRELAVKQVQFDPDSPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQEKTLSIFMEYMPGGSIKDQLKAYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSTGNVKLGDFGASKRLQTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVACTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPKLPPHVSDYTRDFLKRIFVEAKLRPSADELLRHMFVHYH
Protein: Lon protease homolog, mitochondrial (EC 3.4.21.53) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15) (Q924S5)
Organism: Rattus norvegicus (Rat)
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.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12752449, ECO:0000269|PubMed:15560797, ECO:0000269|PubMed:7961901}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent clpX-like chaperone, mitochondrial
- Mitochondrial disaggregase
- 10 kDa heat shock protein, mitochondrial
- 60 kDa heat shock protein, mitochondrial
- ATP-dependent zinc metalloprotease YME1L1
- Stress-70 protein, mitochondrial
- GrpE protein homolog
- AFG3 like matrix AAA peptidase subunit 2
- Mitochondrial inner membrane m-AAA protease component paraplegin
Sequence:
MAASTGYVRLWAAARCWVLRRPLLAVTGGRVPSASGSWLRRGCRVCDTSTPWGGRVPMGGGQWRGLWDAGSRGGSDETSEGGVEDGATASSGEGPVVTALAPMTVPDVFPHLPLIAISRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVTGHRRIHISRQLEVEPEGLEPEAENKQKSRRKLKRGKKEVGDELGAKPQLEMVTEATSDTSKEVLMVEVENVAHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTLCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVSGEAQTVHVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQPSGSKEDKDGSLEVTGQLGDVMKESARIAYTFARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAFPLREHQEALAVER
Protein: G-protein coupled receptors family 1 profile domain-containing protein (P91487)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha
- Neuropeptide-Like Protein
Sequence:
MPKECSVIISPYTIMISSIFLLCLILSLLGNAIVILTILGKSHRSRSITNFYLLNLAFADLLRSIICIPSTLLGELTQCWLLGAAMCKIVAFLQPVGVCASAYTLAVIAIERYYAICRPLESRKWQTKKRALITISLVWCFSFSANLTSLFLYDANPGKFTCDSTKGPLVDFIYQLYLTFTLLFVPLALMVGLYGNVIITLNTAINSDHPTVEQQMIEKTLPSRASFSDWFVSAVQRVPSMKVVSKTFQFKEKNSLSIPQTSGLSVRPSRSSFSSFFSTPRGSFDVTMLLRSTNQEKILIAKKKVTRMLITLVIVFAFCWVPSYLYWLLLRMAELAATDLWNPGLNSSLTIMTYISSLANPITYCFMNKSFRSSVLAYCRPKPKRPLTRCSALPTRKSPSSPTHAIPMIKIDLVLDSSVHI
Protein: Riboflavin synthase (RS) (EC 2.5.1.9) (Q9Y7P0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Interaction partners:
- 6,7-dimethyl-8-ribityllumazine synthase
- Probable GTP cyclohydrolase-2
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- 2,5-diamino-6-ribosylamino-4
- Riboflavin kinase
- Low molecular weight phosphotyrosine protein phosphatase
- Probable acid phosphatase SPBC4.06
- Thiamine-repressible acid phosphatase pho4
- Acid phosphatase
- Thiamine-repressible acid phosphatase SPBC21H7.03c
Sequence:
MFTGLVEAIGVVKDVQGTIDNGFAMKIEAPQILDDCHTGDSIAVNGTCLTVTDFDRYHFTVGIAPESLRLTNLGQCKAGDPVNLERAVLSSTRMGGHFVQGHVDTVAEIVEKKQDGEAIDFTFRPRDPFVLKYIVYKGYIALDGTSLTITHVDDSTFSIMMISYTQSKVIMAKKNVGDLVNVEVDQIGKYTEKLVEAHIADWIKKTQA
Protein: Serine/threonine-protein phosphatase 6 regulatory subunit (B2D6K9)
Organism: Caenorhabditis elegans
Function: Regulatory subunit of protein phosphatase 6 (PP6) (Probable). In complex with pph-6, promotes actomyosin contractility during cytokinesis by regulating the organization of cortical non-muscle myosin II nmy-2 and thus contributing to correct spindle positioning. Also required for the proper generation of pulling forces on spindle poles during anaphase by regulating the cortical localization of gpr-1, gpr-2 and lin-5. Negatively regulates kinase air-1 localization at the cell cortex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20040490}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20040490}. Note=In embryos, localizes mainly to the cytoplasm and to a lesser extent with microtubule asters. {ECO:0000269|PubMed:20040490}.
Interaction partners:
- Serine/threonine-protein phosphatase 6 catalytic subunit
- TPX2 domain-containing protein
- Protein Phosphatase Four Regulatory subunit
Sequence:
MFWAKEEEENSLMRLLKTDNFTLEDVLLNEFVVQESRYGKAELVQYITSRENMKALLELSLNPKINTDLPMKQQYRLSFIASEILTIRGTDVFQKQIVTTEETRKCLVDFLNDKTPLNHLVAGFFAKIMECLLSRHFDLFQTFSLLQETKFFDKCLRNINLGAIECLLENLVRIPTTSEGTRIVKEWMISENLFEKIVDRMRESETDDEKECLAEVYCEILRELRDKLYIMESKVDELHAKSMDETLIAKIADNLIVEEGCPAEELVKKSALISASAKILEAFIKTNFVSNAPAQQLEEIERNLIEERHYSYGLMRPCMDNDPYEHSYQPDPERIVEGILANRLPNILQTVLRDIEANGSVWQPLLRLIIELCNTNCMSTHEKIAVAFRSLPFINLIKAAKMLPRASVLHCLLVKVVILLLHSSFPCDELSPAAEYLLTEGGLIQNIYDTATSPNPGSSVACSGLRSFNQNLGDAINRAKKAGIPNQKLLAILSADNTWTELEDIIHLYNLKHRPQMQHDFNDSSVVSSIRNDSHGFNDSEEWTDASTKFAEMDATSSAKQAFSGFSSPFEPNMQRFSDFEGQFDDTPDEDEFRKLCSERANSSSCAGISFETSPIKWPGEAEKTSEKASEPPSVVASTYPQQTNGNQAFLEQEEGDGEWVWPTVPPLGETEVVTQTGHRPENNWVDETAPDFSHLDMAPPKEDDMWADFSSFPTISPTAAANSASSSSSDAWPGSDIHLQGEASDWPLNNSHESKASDPVMVGLAASISHPGDSSEA
Protein: Sesquiterpene synthase 14 (SlTPS14) (Terpene synthase 14) ((E)-gamma-bisabolene synthase TPS14) (EC 4.2.3.59) ((Z)-gamma-bisabolene synthase TPS14) (EC 4.2.3.40) (Alpha-bisabolene synthase TPS14) (EC 4.2.3.-) (Beta-bisabolene synthase TPS14) (EC 4.2.3.-) (G5CV54)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds. Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into beta-bisabolene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into alpha-bisabolene, but also smaller amounts of (Z)-gamma-bisabolene, (E)-gamma-bisabolene and nerolidol.
Interaction partners:
Sequence:
MATNLTLETDKEIKNMNQLSMIDTTITRPLANYHSSVWKNYFLSYTPQLTEISSQEKLELEELKEKVRQMLVETSDKSTQKLVLIDTIQRLGVAYHFDNEIKISIQNIFDEFEQNKNEDDNDLYIVALRFRLVRGQRHYMSSDVFKKFTNDDGKFKETLTKDVQGLLNLYEATHLRVHGEQILEEALSFTVTHLKSMSPKLDSSLKAQVSEALIQPIYTNVPRVVAPKYIRIYENIESHDDLLLKFVKLDFHILQKMHQRELSELTRWWKDLDHSNKYPYARDKLVECYFWATGVYFGPQYKRARRMITKLIVIITITDDLYDAYATYDELVPYTNAVERCEISAMDSISPYMRPLYQVFLDYFDEMEEELTKDGKAHYVYYAKVEMNKLIKSYLKEAEWLKNDIIPKCEEYKRNATITVANQMILITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFVECYVKEYRASKQEAYVEARRQIANAWKDINTDYLHATQVPTFVLQPALNLSRLVDILQEDDFTDSQNFLKDTIKLLFVDSVNSTSCG
Protein: Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13) (Fructose-1,6-bisphosphatase) (FBPase) (F9VMT6)
Organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
Function: Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).
Interaction partners:
- Triosephosphate isomerase
- D-glucosamine-6-phosphate 4-epimerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-1,6-bisphosphate aldolase
- Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
- 2-oxoacid oxidoreductase
- Enolase
- 2-oxoacid oxidoreductase
- 6-phospho-3-hexuloisomerase
- Phosphoglucosamine/phosphogalactosamine mutase
Sequence:
MKTTISVIKADIGSLAGHHIVHPDTMAAANKVLASAKEQGIILDYYITHVGDDLQLIMTHTRGELDTKVHETAWNAFKEAAKVAKDLGLYAAGQDLLSDSFSGNVRGLGPGVAEMEIEERASEPIAIFMADKTEPGAYNLPLYKMFADPFNTPGLVIDPTMHGGFKFEVLDVYQGEAVMLSAPQEIYDLLALIGTPARYVIRRVYRNEDNLLAAVVSIERLNLIAGKYVGKDDPVMIVRLQHGLPALGEALEAFAFPHLVPGWMRGSHYGPLMPVSQRDAKATRFDGPPRLLGLGFNVKNGRLVGPTDLFDDPAFDETRRLANIVADYMRRHGPFMPHRLEPTEMEYTTLPLILEKLKDRFKKESDVYKAKESIYAKEESQGHD
Protein: Quinolinate phosphoribosyltransferase [decarboxylating] 2, mitochondrial (NgQPT2) (EC 2.4.2.19) (B2RFS9)
Organism: Nicotiana glauca (Glaucous tobacco) (Tree tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (Probable). Involved in the catabolism of quinolinic acid (QA) (Probable).
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
Sequence:
MFRAIPFTATVHPYAITAPRLVVKMSAIATKNTRVESLEVKPPAHPTYDLKEVMQLALSEDAGNLGDVTCKATIPLDMESDAHFLAKEDGIVAGIALAEMIFAEVDPSLKVEWYVNDGDKVHKGLKFGKVQGNAYNIVIAERVVLNFMQRMSGIATLTKEMADAAHPAYILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHISAAGGVGKALKSVDQYLEQNKLQIGVEVETRTIEEVREVLEYASQTKTSLTRIMLDNMVVPLSNGDIDVSMLKEAVELINGRFDTEASGNVTLETVHKIGQTGVTYISSGALTHSVKALDISLKIDTELALEVGRRTKRA