wanglab/gogpt-training-data huggingface dataset:
Protein: 2-hydroxyethylphosphonate dioxygenase (EC 1.13.11.72) (Hydroxyethylphosphonate dioxygenase) (Phosphinothricin tripeptide biosynthesis protein D) (Q5IW40)
Organism: Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
Function: Non-heme-dependent dioxygenase that catalyzes the conversion of 2-hydroxyethylphosphonate (HEP) to hydroxymethylphosphonate (HMP) in the biosynthesis of phosphinothricin tripeptide (PTT). PTT contains the unusual amino acid phosphinothricin attached to 2 alanine residues. Synthetic phosphinothricin (glufosinate) is a key component of commercial herbicides.
Interaction partners:
- Phosphonoacetaldehyde reductase
- PhpE
Sequence:
MRIDPFKLAHWMNARKYTAAQTADLAGLPLDDLRRLLGDEANEPDPAAATALAEALSVEPSQLAADAHRNLTVVHKSAEEMHASRRPIQRDGIHFYNYYTLAAPEGRVAPVVLDILCPSDRLPALNNGHLEPAITVNLGPGDINGRWGEEITPQTWRVLHANHGGDRWITGDSYVEPSYCPHSYSLAGDAPARIVSYTAQSNISPLMTEANNWSTGAFEEALKALSGKVSAGSVLDLFLARRAHTRTSAAEAAGVPPADLEAALRSPASETGLTVLRTLGRALGFDYRVLLPADDQHDGVGKTWTTIEDSRRSRRTFGTYEAASMASAAHLPDLVGSFLRVDADGRGADLIDHAENHYVVTEGRLTLEWDGPDGPASVELEPDGSAWTGPFVRHRWHGTGTVLKFGSGAHLGYQDWLELTNTFEPAATLRRGRRDLAGWGYDN
Protein: Coiled-coil domain-containing protein 185 (Q8N715)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGFSHFSQPPYRDLWEPPRPGGERESTQRLGGQRSGADSTACSRAGTPGAESEAGACWLHPHCSFTPRPRRRGCSDSLRGSRSLSDVARRPLERSRKHRPRSRRLEDAWGETGTKPRPAWQPQTQLPPQRPQPCPHYPLAQGDSPPPCPGGAGTPLSGTFRVEKAQGGDQWAVPLGRHLGRWSPSSVPSERSSVPSQKFKRHSACVCAQKRDSSDQVESLASRDSQPLASSKEMRSPHTQVLKSKLEEVVVSSQDQQIVALVLTRLKKAQRIRELQQQAAKAWEELKRSDQKVQMTLERERRLLLRQSQEQWQEKEQRKTLQSPEQRGLRRDSQRKNVPPGESRWKEQPEDQESPRQEKLEKARAQAEHRKQCQVRRLREQEKMLRNLREQHSLQLQRRLVEACRKRHLHAVEGQKKVQDTNLSSLINYQARKVLMDCQAKAEELLRQLSLEQSFQRSQEIHQGLRKERQRELREKAQKEEEQLQQARWRAGESEEQRKMRKRILVELADEKIRQARSHVHKTTRDKVQHLRELNHLREKNHHILKLKAEKEEKCHIEGIKEAIKKKEQRVQHISQGKDPNFQEFQKLPQASRREERAPPNSSLDQMVLEAQLRACQQNRGY
Protein: Histone H2B.1 (Q6FWM8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H3
- Histone H2A.2
- Histone H4
- Histone H2A.1
- Histone H2A
- Histone H3-like centromeric protein CSE4
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome B complete sequence
- RuvB-like helicase 1
- Chromatin-remodeling ATPase INO80
Sequence:
MSAEKKPASKAPAEKKPAAKKTAPSADGKKRTKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIASEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA
Protein: U11-myrmicitoxin-Tb1a (U11-MYRTX-Tb1a) (A0A6M3Z554)
Organism: Tetramorium bicarinatum (Tramp ant)
Function: May have antimicrobial properties, like most ant linear peptides.
Subcellular location: Secreted {ECO:0000269|PubMed:30149710}.
Interaction partners:
Sequence:
LAMAMGDAVADAQARAMAAAYAIAGKEKEKLKQCFKDMTLAAIDYAKHKVEKHLFKCI
Protein: Hydroxysteroid 11-beta-dehydrogenase 1-like protein (EC 1.1.1.-) (11-beta-hydroxysteroid dehydrogenase type 3) (11-DH3) (11-beta-HSD3) (Short chain dehydrogenase/reductase family 26C member 2) (Short-chain dehydrogenase/reductase 10) (Q7Z5J1)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cytochrome P450 11B2, mitochondrial
- Aldo-keto reductase family 1 member D1
- 11-beta-hydroxysteroid dehydrogenase type 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Cytochrome P450 11B1, mitochondrial
- Cytochrome P450 3A4)
- Cytochrome P450 1A1
- Steroid 21-hydroxylase
- Cytochrome P450 2A13
- Cytochrome P450 2E1
Sequence:
MKVLLLTGLGALFFAYYWDDNFDPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFGSLRRELDVQDVNVAITMCVLGLRDRASAAEAVRSSTSRPRQPEHRGVPLQSQTAMFLPPTVPGARTLTETPLRGWPQPKMKSSRQKSKTEKNDGHLEPVTAWEVQVPRVRRLCRGLARPHLFGHD
Protein: Protein Turandot Z (Q8IN42)
Organism: Drosophila melanogaster (Fruit fly)
Function: A humoral factor that may play a role in stress tolerance.
Subcellular location: Secreted {ECO:0000269|PubMed:11409894, ECO:0000305}.
Interaction partners:
- LD23158p
Sequence:
MYFAIRLSFVLAVLICLTGNGSARMLDADRNRLQQLQIRSQQSADANTQVDIAYEVIGIYDKYKGQGGSNVLREAQLNSQVNDFKRKTMVIDGVPAQGGVWGILGAIKKAADAVPDNVKKDAENLVKSSTKVLVRGIYDYLMGKMKH
Protein: Ganglioside GM2 activator (A0A0G2K1K3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRRVPLLLVLGLLFVLGLLFAGPVAPSRLISKRPSQLGGFSWDNCDEGKDPAVIKSLTLQPDPIVVPGDVIVSAEGKTSIPLTSPQKLTVEKEVAGFWVKIPCVEQLGSCTYENVCDLIDQYIPPGETCPEPLHTYGLPCHCPFKEGTYSLPSSNFTVPDLELPSWLSTGNYRIQSILSSGGKRLACIKIAASLKGK
Protein: D-gluconate dehydratase (EC 4.2.1.39) (Q704D2)
Organism: Thermoproteus tenax
Function: Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the dehydration of gluconate to produce 2-keto-3-deoxygluconate (KDG). It is not able to use D-galactonate as substrate.
Interaction partners:
Sequence:
MASAMASSALREATCTMTRLAADVAASVSSIFSCKDSAGPRPVVPATKTTSTPLDVMFFTWFAKSSGSSLPPLKVVMTGATISIDSTRGALKKLARKGIKGWLNQYMATIKEIEPIVLYEQETDARWASYSILVRVVTSDGRVSYGEAVPTLRILPVVSAVRQTARAFLGRDPHEISAAFYEWYRQDFFLSRSFESATALSAIDMALWDLKARELGAPLYELLGGKLRDRVKVYANGWYGGCRDPQCFAEKAKEVVARGYDALKFDPFGPSFNSITSEELRRAEEAVAAVRDAVGDDVDILIEHHGRFNANAAVEIAKRFEPYRPYFMEEPLHHEDIEGYRKYRSLTSARIAMGERLISAKEALQYLVEGLVDVIQPDACNIGGVTGSMKVAALAEAFSVEVSYHNAYGPVQFALEVQLSAVTPTLYRLESFYDYWPQWKRDLIGDPFRLSQSSVEVPRGPGIGVAVNERVLEKYRAEPSEIPVGEEPVWVVRGTWR
Protein: Disintegrin and metalloproteinase domain-containing protein 12 (ADAM 12) (EC 3.4.24.-) (Meltrin-alpha) (O43184)
Organism: Homo sapiens (Human)
Function: Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors (By similarity).
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
Interaction partners:
- SH3 and PX domain-containing protein 2A
- TGF-beta receptor type-2
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Syndecan-1
- Growth factor receptor-bound protein 2
- Integrin alpha-7
- Pappalysin-1
Sequence:
MAARPLPVSPARALLLALAGALLAPCEARGVSLWNQGRADEVVSASVGSGDLWIPVKSFDSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTVILGHCYYHGHVRGYSDSAVSLSTCSGLRGLIVFENESYVLEPMKSATNRYKLFPAKKLKSVRGSCGSHHNTPNLAAKNVFPPPSQTWARRHKRETLKATKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQMAVEKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLPEVRESFGGQKCGNRFVEEGEECDCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVYLHDGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSKSSFAKCEMRDAKCGKIQCQGGASRPVIGTNAVSIETNIPLQQGGRILCRGTHVYLGDDMPDPGLVLAGTKCADGKICLNRQCQNISVFGVHECAMQCHGRGVCNNRKNCHCEAHWAPPFCDKFGFGGSTDSGPIRQADNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLLFTNKKTTIEKLRCVRPSRPPRGFQPCQAHLGHLGKGLMRKPPDSYPPKDNPRRLLQCQNVDISRPLNGLNVPQPQSTQRVLPPLHRAPRAPSVPARPLPAKPALRQAQGTCKPNPPQKPLPADPLARTTRLTHALARTPGQWETGLRLAPLRPAPQYPHQVPRSTHTAYIK
Protein: Protein phosphatase 1, regulatory subunit 9A (H3BJD0)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MLKAESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKSDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPSENAAIIAKTRGKGRPSSPQRRMKPKEFVEKTDGSVVKLESSVSERISRFDTMHDGPSYAKFTETRKMFERSVHESGQNHRYSPKKEKGGGTEPQDEWGGSKSNRGSSDSLDSLSPRTEAVSPTVSQLSAVFENSEPPGALTSGKAESADYSVTGHYPLNLPSVTVTNLDTFGRLKDSNSKPPSNKQDTDTEDAQKSDAVPVPEVAQKGTSLASLPSEESQLSTEAEDVTTAQPEALDSTDKDSPEEPSAENQAMPKSHILSPRNEPLEDAEANVVGSERAQHQKKDLTGGDLTSPDASASSCGREVPEDSNSFESSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEEEDSDENNYYQPDMEYSEIVGLPEEEEIPANRKIKFSCAPIKVFNTYSNEDYDRRNDDVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTDGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLERHYAQYDADDDENTVAELQGVSGNCNNNNNRFLKTGEYATDEEEDEGGPILPSGDVAIEVFELPENEDMFSPSDLDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKNQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIKRQEVERKKREEVEKAHLLEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPTRTRLYDSVSSTDGEDSLERKPSDTITTHMLPNRFCPRLGEFLLQNRSVVSHSSPP
Protein: Beta-synuclein (Phosphoneuroprotein 14) (PNP 14) (Q63754)
Organism: Rattus norvegicus (Rat)
Function: May be involved in neuronal plasticity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTKEGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKKEEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDSPQEEYQEYEPEAKGP
Protein: Protein stoned-B (Stn-B) (StonedB) (Q24212)
Organism: Drosophila melanogaster (Fruit fly)
Function: Adapter protein involved in endocytic recycling of synaptic vesicles membranes. May act by mediating the retrieval of synaptotagmin protein Syt from the plasma membrane, thereby facilitating the internalization of multiple synaptic vesicles from the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10407025, ECO:0000269|PubMed:11160392}. Synapse {ECO:0000269|PubMed:10407025, ECO:0000269|PubMed:11160392}. Note=Colocalizes with synaptic vesicle pools. Colocalizes with the endocytic network within synaptic boutons. {ECO:0000269|PubMed:10407025, ECO:0000269|PubMed:11160392}.
Interaction partners:
- Protein stoned-A
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- Synaptotagmin 1
- Dynamin associated protein 160, isoform D
- AP-2 complex subunit alpha
- Adaptor protein complex 2, mu subunit, isoform A
- Ubiquitin-like protein NEDD8
- FI18813p1
- Phosphatidylinositol-binding clathrin assembly protein LAP
- AT02057p
Sequence:
MANPFLMDEDLDGCDAAANPFLMQSEPEPSSDNPFMAATVASNPFAFGADDLELGAEPEAEATHDNDLDPAMSFFGTTIEAEDDTLSLKSGAEEEDEGKKPPQSQPQLQSHAHPHPPPPRPLVPPQSTQDLISTVSSQLDETSSELLGRIPATRSPSPVSMRDLHSPSPTPDSGLADLLDVSVDSGSSAHTQGIEADLISGVAGGVRLDNPFAVPTAVPNIQAAVPLPATPIKQPPRPPPPRPAPPRPAPPGQAAPQRPPPPLAAVNPPPAAPEADDLLDMFGTTACKPAKPPPPKSKEDILSLFEQPHVPLSQPASKPDLLHDDLDETIGEGEPPEQEEPDTEQSNEISSRDEPVFTSLLIRPDESTHDITSQPQAATGLERQVNNMAAPSGTASTQRATTPDIEITTVEDLPRSDDEDEPEAMQEPETETKPQIEPDTEPEIVSEHSPPTERLVTQAALVDGELIAAEPEPEEMDTGLDFPLASSGQLSANPFASPDEEEPNFAPMPAAVANIFAVNDPDSQMETPKAPSHTANIFASDPDEFDAFSAKFDSVKKDNISIMDGFGGSGAITPTGGDAWGGSAFGSTTISANACGDTNSADDGFGNDDDDFYAMQAPARADSVESVDKDFSVVIRPMAEETSGVAPQLAPPPPPARGVNQAQTTSLPGLTVNPFEDVSGFPAPGLPPTDGTAIKRTDSQDTPQTPLYDEDVSQPLEEFPRLHYIGPGWEMQLRQPNKKKITGQRFWKKIVVRLVVQNDVPVVQLLNQAGDKQPFQELPLQPSYSVSEIGAQQYDQFGKIFTMKLQYIFYKERPGVRPGQVTKAERITNKLTKFAQYAIAGDYEGVKEFGSDLKKLGLPVEHAPQSSQLFKIGSMNYEDMKQFSVCIEEALFKIPALRERALTYKMEEVQVTAVDEITVEQDFEGKILKQIARVRLFFLAFLTGMPTIELGVNDMWRQGKEVVGRHDIIPVATEEWIRLEAVEFHSVVNQKEYERTRTIKFQPPDANYIELLRFRVRPPKNRELPLQLKATWCVSGNKVELRADILVPGFTSRKLGQIPCEDVSVRFPIPECWIYLFRVEKHFRYGSVKSAHRRTGKIKGIERILGAVDTLQESLIEVTSGQAKYEHHHRAIVWRCPRLPKEGQGAYTTHQLVCRMALTSYDQIPSELAPYAFVEFTMPATQVSHTTVRSVSVQDSDGDEPPEKYVRYLARHEYKVGIETTHGESTNAYLAATRPIREEPPTTATKPTASPVAPSDSDTDSN
Protein: Nuclear pore membrane glycoprotein 210 (Nuclear pore protein gp210) (Nuclear envelope pore membrane protein POM 210) (POM210) (Nucleoporin Nup210) (Pore membrane protein of 210 kDa) (P11654)
Organism: Rattus norvegicus (Rat)
Function: Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity.
Subcellular location: Nucleus, nuclear pore complex. Nucleus membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- Nucleoporin NUP35
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup155
- Nucleoporin NUP188
- Nucleoporin 205
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup107
- LOC683983 protein
- Nuclear pore complex protein Nup88
Sequence:
MARASLIQPGLWALLLLQAVGPAVAAKLNIPKVLLPFTRATRVNFTLEASEGCYRWSSTRPEVASIEPLGSSEQQCSQKAVVQARLTQPARLTSIIFAEDITTGQVLRCDAIVDLIHGIQIVSTTRELYLEDSPLELKIQALDSEGNTFSTLAGLVFDWTIVKDTEANGFSDSHNALRILTFLESTYIPPSYISEMEKAAKQGDTILVSGMKTGSSKLKARIQEAVYKNVRPAEVRLLILENILLNPAYDVYLLVGTSIHYKVQKIRQGKITELSMPSDQYELQLQNSIPDPQGDPARPVAVLTQDTSRVTAMQMGQSNLVLGHRSIRMQGASRLPNSTIYVVEAGYLGFTVHPGDRWVLETGHLYAVTIEVFDRSSNKVYPSDNIRIEAVFPAEFFEVLSSSQNGSYHHVRAIQSGQTTISASLTSVVDQDGGVHVLQVPVWNQQEVDIHIPITLYPSILTFPWQPKTGAYQYTIKAHGGSGNFTWSSSSYMVATVTVKGVMTTGGDTGLSVIRAHDVQNPLHFGEMKVYVIEPSSMEFAPCQVEARVGHTLELPLTISGLMPGGSSEVVTLSDCSHFDLVVEVENQGVFQPLPGRLPPGPEHCSGVKVRADAQGSTTLLVSYTHGHVHLGAKITLAAYLPLKAVDPSSVAVVTLGSSKEMLFEGGPRPWVLEPSKFFRNVTSEDTGSISLSLLGPPASRNYQQHRVLVTCQALGEQVIALSVGNRPSLSNPFPAVEPTVVKSVCAPPSRLTLMPVYALPQLDLSCPLLQQNKQVVPVSSHRNPLLDLGAYDQQGRRFDNFSSLSIQWESFRPLLASIEVDQPMQLVSQDDGNGQKKLHGLQTVSVHEASGTTAISATATGYQQSHLSAAGVKQLRDPLVPVSASIELILVEDVRVSPEEVTIYNHPGVQVELHITEGSGYFFLNTSTQDIINVAYQDTRGVAMVHPLFPGSSTVMVHDLCLTFPAPAKATIHVSDIQELYVRVVDKVEIGKAVKAYVRVLDFYKKPFLAKYFTFMDLKLRAASQIITLVTLDEALDNYTATFLVHGVAIGQTSLSASVTDKSGQRVSSTAQQIEVFPPFRLIPRKVTLIIGAMIQITSEGGPQPQSNILFSINNESVAAVSSAGLVRGLMVGNGSVLGVVQAVDAETGKVIIVSQDHVEVEVLQLQAVRIRAPITRMRTGTQMPVYVTGITSNQSPFSFGNAVPGLTFHWSVTKRDVLDLRGRHHEVSIRLSPQYNFAMNVHGRVKGRTGLRVVVKALDPTAGQLHGLGKELSDEIQIQVFEKLRLLNPEVEAEQILMSPNSFIKLQTNRDGAAILSYRVLDGPEKAPIVHIDEKGFLVSGSGIGVSTLEVIAQEPFGTNQTVLVAVKVSPISYLRISMSPVLHTQHKEVLTALPLGMTVTFTVHFHDSSGDIFHAHNSDLNFATNRDDFVQIGKGATNNTCIIRTVSVGLTLLHVWDVEHLGLSDFVPLPVLQAITPELSGAVVVGDILCLASVLISLGGVSGTWSSSAGNVLYVDPKTGVAIARDAGPVTVYYEIAGHLKTFKEIVVVTPQKIVARRLHATQTSIQEATASKVTVSVGDRSSNLLGECSSAQREAIEALHPESLISCQLQFKQDVFDFPARDIFSVEPGFDTALGQYLCSVTMHRLTDKQLKHLNMKKTSLAVTASMPSSRTSVEKVGAEVPFSPGLYANQAEILLSNHYPSSEVKIFGAVEILENLEVRSGSPAVLASVKEKSFGLPSFITYTVGVLDPTAGSQGPLSTALTFSSPATNQAITIPVTVAFVLDRRGPGPYGASLLSHFLDSYQVMFFTFFALLAGTAVTIIAYHTVCAPRELASPLALTPHASPQHSPHYLASSPTAFNTLPSDRKASPPSGLWSPAYASH
Protein: F-box protein UCC1 (Ubiquitination of citrate synthase in the glyoxylate cycle protein 1) (Q05947)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate recognition component of the SKP1-CUL1-F-box protein E3 ubiquitin-protein ligase complex SCF(UCC1) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The SCF(UCC1) complex acts as a metabolic switch for the glyoxylate cycle and regulates the level of CIT2 protein to maintain citrate homeostasis.
Interaction partners:
- F-box protein YDR306C
- F-box protein HRT3
- Suppressor of kinetochore protein 1
- Citrate synthase, peroxisomal
Sequence:
MNQSDSSLMDLPLEIHLSLLEYVPNELRAVNKYFYVLHNHSYKEKSLAWIAEDNYIWAVVKHSLCLYVKSLDPLRQHAREIIQETKEPGFNVPLCMTKYIADSWYIVYNALQYPGKIINMGWDKYTKSQDSNGSDSTSNFNSRPKERTLMQSLTALPVNFWSRRKDEPTPVNVWFYVKNAHVARYIPKIITEIGICNYGPKQIVASAGYINELITSEGIYCVNLGHLPRLYDEQIFEGTGTTHLPLELKAIDRTDSDVCINGDLVLLGYDFIPYQISKPWLLFRIEPVNSIEAIFNYSECSFSYQFAWSLACLQSEEKISFPRDTIIGHGLPYKPSKLIRIFVYKHPEQKQDLGQEIALPNWNTPYLRR
Protein: Cellular tumor antigen p53 (Tumor suppressor p53) (E9PCY9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYS
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC2 (RNA polymerases I, II, and III subunit ABC2) (DNA-directed RNA polymerases I, II, and III 15 kDa polypeptide) (RPC16) (P36595)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit rpb4
- DNA-directed RNA polymerase I subunit rpa1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerase I subunit rpa43
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MSDYEEDEAFGMDGAVMEEEVDELEMIDENGQSQQGVSHPGEPSTTVITEDVASSKTAQSGKAVAKEDRTTTPYMTKYERARILGTRALQISMNAPVLVDLEGETDPLQIAMKELAQKKIPLLVRRYLPDGSYEDWSVAELI
Protein: Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase) (Q9I016)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Peptide methionine sulfoxide reductase MsrA
- DUF1315 family protein
- Glutathione peroxidase
- Thiol:disulfide interchange protein DsbD 2
Sequence:
MSKIDKPLDSWREELTEEQFHICRLGGTERAFSGEYHATKTPGIYHCTCCGTALFDSDAKYDSGSGWPSYFQPVDAEAVRELDDFSHGMHRIEVRCGRCDAHLGHVFPDGPRPTGLRYCINSASLKLVPRES
Protein: Nonhistone chromosomal protein H6 (C1BFL7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPKRKSATKGDEPARRSARLSSRPAPKPAAKPKKAAAPKKPVKGKKAAENGDAKAEAKVEAAGDAK
Protein: RNA helicase (EC 3.6.4.13) (A0A8J8Y6U2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MATDSWALAVDEQEAAVKSMNSLQIKEEKVKADTNGVIKTSTTAEKTEEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPADRHPQCLCLSPTYELALQTGKVIEQMGKFHPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
Protein: NADH-quinone oxidoreductase subunit G (EC 7.1.1.-) (NADH dehydrogenase I subunit G) (NDH-1 subunit G) (NUO7) (P33602)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}.
Interaction partners:
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit C/D
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit F
Sequence:
MATIHVDGKEYEVNGADNLLEACLSLGLDIPYFCWHPALGSVGACRQCAVKQYQNAEDTRGRLVMSCMTPASDGTFISIDDEEAKQFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSFRRYRFTKRTHRNQDLGPFISHEMNRCIACYRCVRYYKDYADGTDLGVYGAHDNVYFGRPEDGTLESEFSGNLVEICPTGVFTDKTHSERYNRKWDMQFAPSICQQCSIGCNISPGERYGELRRIENRYNGTVNHYFLCDRGRFGYGYVNLKDRPRQPVQRRGDDFITLNAEQAMQGAADILRQSKKVIGIGSPRASVESNFALRELVGEENFYTGIAHGEQERLQLALKVLREGGIYTPALREIESYDAVLVLGEDVTQTGARVALAVRQAVKGKAREMAAAQKVADWQIAAILNIGQRAKHPLFVTNVDDTRLDDIAAWTYRAPVEDQARLGFAIAHALDNSAPAVDGIEPELQSKIDVIVQALAGAKKPLIISGTNAGSLEVIQAAANVAKALKGRGADVGITMIARSVNSMGLGIMGGGSLEEALTELETGRADAVVVLENDLHRHASAIRVNAALAKAPLVMVVDHQRTAIMENAHLVLSAASFAESDGTVINNEGRAQRFFQVYDPAYYDSKTVMLESWRWLHSLHSTLLSREVDWTQLDHVIDAVVAKIPELAGIKDAAPDATFRIRGQKLAREPHRYSGRTAMRANISVHEPRQPQDIDTMFTFSMEGNNQPTAHRSQVPFAWAPGWNSPQAWNKFQDEVGGKLRFGDPGVRLFETSENGLDYFTSVPARFQPQDGKWRIAPYYHLFGSDELSQRAPVFQSRMPQPYIKLNPADAAKLGVNAGTRVSFSYDGNTVTLPVEIAEGLTAGQVGLPMGMSGIAPVLAGAHLEDLKEAQQ
Protein: Glyoxylate/hydroxypyruvate reductase A (EC 1.1.1.79) (EC 1.1.1.81) (2-ketoacid reductase) (P75913)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:11237876}.
Interaction partners:
- Isocitrate lyase
- Malate synthase A
- Lactaldehyde dehydrogenase
- Malate synthase G
- Glyoxylate/hydroxypyruvate reductase B
- Glyoxylate carboligase
- Glycolate oxidase subunit GlcD
- Hydroxypyruvate isomerase
- 2-hydroxy-3-oxopropionate reductase
- Phosphoglycolate phosphatase
Sequence:
MDIIFYHPTFDTQWWIEALRKAIPQARVRAWKSGDNDSADYALVWHPPVEMLAGRDLKAVFALGAGVDSILSKLQAHPEMLNPSVPLFRLEDTGMGEQMQEYAVSQVLHWFRRFDDYRIQQNSSHWQPLPEYHREDFTIGILGAGVLGSKVAQSLQTWRFPLRCWSRTRKSWPGVQSFAGREELSAFLSQCRVLINLLPNTPETVGIINQQLLEKLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFNREPLPPESPLWQHPRVTITPHVAAITRPAEAVEYISRTIAQLEKGERVCGQVDRARGY
Protein: Microsomal glutathione S-transferase 3 (A0A8I6AAX9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLRPYPRRPQHWVCFPLCCAFFHRAKMAVLSKEYGFVLLTGAASFVMVLHLAINVGKARKKYKVEYPVMYSTDPENGHMFNCIQRAHQNTLEVYPPFLFFLTVGGVYHPRIASGLGVAWIIGRVLYAYGYYTGDPSKRYRGAVSSLALFALMGTTVCSAFQHLGWIKPGLGSGSRSCH
Protein: 26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27) (O00233)
Organism: Homo sapiens (Human)
Function: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process.
Interaction partners:
- 26S proteasome regulatory subunit 10B
- 26S proteasome regulatory subunit 6A
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 14
Sequence:
MSDEEARQSGGSSQAGVVTVSDVQELMRRKEEIEAQIKANYDVLESQKGIGMNEPLVDCEGYPRSDVDLYQVRTARHNIICLQNDHKAVMKQVEEALHQLHARDKEKQARDMAEAHKEAMSRKLGQSESQGPPRAFAKVNSISPGSPASIAGLQVDDEIVEFGSVNTQNFQSLHNIGSVVQHSEGKPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR