wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase PGAM5, mitochondrial (Serine/threonine-protein phosphatase Pgam5, mitochondrial) (Q383P5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- FUN14 family
Sequence:
MTVLSRVLLGAAVGSVSAAFNIAWCDSSLQSGSVLSVNSLLPVDEIIRADGKNASLKSWGVPWVEDWDCLEAKDGAAGKSSGHKRQLILIRHGQYQNEKSSDDRQRTLTQLGEEQARLTGRYLWQAFQQKRLVKELGSEPALGVDNFMGGLLRFHEPKEIYVSDMTRAQQTVKLITEAFPYHIRARVKTDPILRERYPCDPQPPHKHRSAAHSDMLAVEEVFKKYFHRPLKDESSVEVIVGHANVIRYLVCRALQLPPEAWLRISLPHCSITSLVIGANGHVSLSSLGSAGHLPVDMVTTHNVP
Protein: FBD-associated F-box protein At4g10400 (Q9SV82)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At2g20380
- F-box/kelch-repeat protein At2g22030
- F-box protein At2g07140
- F-box/kelch-repeat protein At4g29370
- Putative F-box protein At3g22940
- Putative F-box/kelch-repeat protein At4g02310
- Putative F-box only protein 10
- F-box/kelch-repeat protein At2g43270
- F-box protein At3g08750
- F-box protein At1g31080
Sequence:
MDRISGLPDEVLVKILSFVPTKVAVSTSILSKRWEFLWMWLTKLKFGSKRYSESEFKRLQCFLDRNLPLHRAPVIESFRLVLSDSHFKPEDIRMWVVVAVSRYIRELKIYSSHYGEKQNILPSSLYTCKSLVILKLDGGVLLDVPRMVCLPSLKTLELKGVRYFKQGSLQRLLCNCPVLEDLVVNLSHHDNMGKLTVIVPSLQRLSLSTPSSREFVIDTPSLLSFQLVDRNDNSHTFLIENMPKLREAYINVPFADIKSLIGSITSVKRLAISSEVGYGEGFIFNHLEELTLWNKYSSNLLVWFLKNSPNLRELMLVSETDDHENLGMLSWNQPSIVPECMLSSLQKFTWFKYLGRPQDRDIAVYILKNACRLRTATIKSDTRLFTKLEMITELRLSSQASSTCELNFS
Protein: Notch-regulated ankyrin repeat-containing protein (Q91ZA8)
Organism: Mus musculus (Mouse)
Function: Downstream effector of Notch signaling. Involved in the regulation of liver cancer cells self-renewal (By similarity). Involved in the regulation of canonical Wnt signaling by stabilizing LEF1 (By similarity). Involved in angiogenesis acting downstream of Notch at branch points to regulate vascular density. Proposed to integrate endothelial Notch and Wnt signaling to control stalk cell proliferation and to stablilize new endothelial connections during angiogenesis. During somitogenesis involved in maintenance of proper somite segmentation and proper numbers of somites and vertebrae. Required for proper anterior-posterior somite patterning. Proposed to function in a negative feedback loop to destabilize Notch 1 intracellular domain (NICD) and down-regulate the Notch signal, preventing expansion of the Notch signal into the anterior somite domain.
Interaction partners:
- Recombining binding protein suppressor of hairless
- Neurogenic locus notch homolog protein 1
- Hairy/enhancer-of-split related with YRPW motif protein 1
- E3 ubiquitin-protein ligase DTX1
Sequence:
MSQAELSTCSAPQTQRIFQEAVRKGNTQELQSLLQNMTNCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLITKAKYAASGR
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Q9HEY7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00445}.
Interaction partners:
- Superoxide dismutase 1 copper chaperone
- Superoxide dismutase
- Superoxide dismutase
- Glutathione peroxidase
- Catalase B
- ThiJ/PfpI family protein
- DJ-1/PfpI domain-containing protein
- Thioredoxin
- Thioredoxin, putative
- Iron/copper transporter Atx1, putative
Sequence:
MVKAVAVLRGDSKVSGTVTFEQADENSNTTVSWNITGNDPNAERGFHIHQFGDNTNGCTSAGPHFNPFGKTHGAPEDEVRHVGDLGNFKTDAEGNSKGSKTDKLIKLIGAESVLGRTLVVHAGTDDLGRGDSEESKKTGNAGARPACGVIGIAA
Protein: Ras-related protein Rab-14 (EC 3.6.5.2) (Rab4-like GTPase) (P36410)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Regulates the fusion of phagosomes and lysosomes.
Subcellular location: Endosome {ECO:0000269|PubMed:12186956, ECO:0000269|PubMed:8898366}. Contractile vacuole {ECO:0000269|PubMed:12186956, ECO:0000269|PubMed:8898366}. Membrane {ECO:0000269|PubMed:12186956}; Lipid-anchor {ECO:0000305}. Note=Endosomal pathway and the contractile vacuole membrane system. {ECO:0000269|PubMed:12186956, ECO:0000269|PubMed:8898366}.
Interaction partners:
- Rab GDP dissociation inhibitor
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Rab escort protein 1
Sequence:
MSFPYEYIFKYIIIGDMGVGKSCLLHQFTENKFVPDSPHTIGVEFGTRIVDVNNKKIKLQIWDTAGQERFRAVTRSYYRGAAGALLVYDITRRITYNHLTTWLTDARNLTNPNTVIMLIGNKKDLEGQRDVTYEEASAFAKQNGLIFVESSAKTGENVEEAFLRTAKLIFQSVQEGNVDLIPDGGITKNPPQTITDKPQDASKCSC
Protein: FI16750p1 (Zyx102.6 isoform) (Zyxin, isoform G) (Q8I0G8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQVPSSRQVLCSREPLYSQPLIGVEKTMRGHMPFRKYLSSEFGVADTQINRKTTLDNPAILEQQLEALAYHKLQMEKKGLLGVQAKPTQPLNSFTKPLSKTLSKSLIYSNLGSVRKEIETLELLTDETKISASTYSNVNETAMDSSHSSTQKMLSVCTNFISDNEKDELPPPPSPESAVSSSYSELRHATLEFNKPIDYLQNNQTTNPLQIYANQYAMQHDATGKSSSTYDSIYEPINPRPCVADTLPRESYNLHNSYVNDNNPNISHEYNISNSIEANQTLYIHGNARTTFYDVNSIHRNDKEGLKNYISIPTEPVQELENYGRCVKCNSRVLGESSGCTAMDQIYHIFCFTCTDCQINLQGKPFYALDGKPYCEYDYLQTLEKCSVCMEPILERILRATGKPYHPQCFTCVVCGKSLDGLLFTVDATNQNYCITDFHKKFAPRCCVCKQPIMPDPGQEETIRVVALDRSFHLECYKCEDCGLLLSSEAEGRGCYPLDDHVLCKSCNAKRVQALTNRMTSEH
Protein: tRNA (34-2'-O)-methyltransferase regulator WDR6 (WD repeat-containing protein 6) (A0A087X295)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGSAARWEGSFSREFSSLLSRGCLSTSRIDMDALEDYVWPRATSELILLPVTGLECVGDRLLAGEGPDVLVYSLDFGGHLRMIKRVQNLLGHYLIHGFRVRPEPNGDLDLEAMVAVFGSKGLRVVKISWGQGHFWELWRSGLWNMSDWIWDARWLEGNIALALGHNSVVLYDPVVGCILQEVPCTDRCTLSSACLIGDAWKELTIVAGAVSNQLLVWYPATALADNKPVAPDRRISGHVGIIFSMSYLESKGLLATASEDRSVRIWKVGDLRVPGGRVQNIGHCFGHSARVWQVKLLENYLISAGEDCVCLVWSHEGEILQAFRGHQGRGIRAIAAHERQAWVITGGDDSGIRLWHLVGRGYRGLGVSALCFKSRSRPGTLKAVTLAGSWRLLAVTDTGALYLYDVEVKCWEQLLEDKHFQSYCLLEAAPGPEGFGLCAMANGEGRVKVVPINTPTAAVDQTLFPGKVHSLSWALRGYEELLLLASGPGGVVACLEISAAPSGKAIFVKERCRYLLPPSKQRWHTCSAFLPPGDFLVCGDRRGSVLLFPSRPGLLKDPGVGGKARAGAGAPVVGSGSSGGGNAFTGLGPVSTLPSLHGKQGVTSVTCHGGYVYTTGRDGAYYQLFVRDGQLQPVLRQKSCRGMNWLAGLRIVPDGSMVILGFHANEFVVWNPRSHEKLHIVNCGGGHRSWAFSDTEAAMAFAYLKDGDVMLYRALGGCTRPHVILREGLHGREITCVKRVGTITLGPEYGVPSFMQPDDLEPGSEGPDLTDIVITCSEDTTVCVLALPTTTGSAHALTAVCNHISSVRAVAVWGIGTPGGPQDPQPGLTAHVVSAGGRAEMHCFSIMVTPDPSTPSRLACHVMHLSSHRLDEYWDRQRNRHRMVKVDPETRYMSLAVCELDQPGLGPLVAAACSDGAVRLFLLQDSGRILQLLAETFHHKRCVLKVHSFTHEAPNQRRRLLLCSAATDGSLAFWDLTTMLDHDSTVLEPPVDPGLPYRLGTPSLTLQAHSCGINSLHTLPTREGHHLVASGSEDGSLHVFVLAVEMLQLEEAVGEAGLVPQLRVLEEYSVPCAHAAHVTGLKILSPSIMVSASIDQRLTFWRLGHGEPTFMNSTVFHVPDVADMDCWPVSPEFGHRCALGGQGLEVYNWYD
Protein: Taste receptor type 1 member 3 (Saccharin preference protein) (Sweet taste receptor T1R3) (Q925D8)
Organism: Mus musculus (Mouse)
Function: Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate) and also to most of the 20 standard L-amino acids, but not to their D-enantiomers or other compounds. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. TAS1R3 is essential for the recognition and response to the disaccharide trehalose. Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Taste receptor type 1 member 1
- Taste receptor type 1 member 2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Transient receptor potential cation channel subfamily M member 5
- Taste receptor type 2 member 4
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Taste receptor type 2 member 38
- Taste receptor type 2 member 7
Sequence:
MPALAIMGLSLAAFLELGMGASLCLSQQFKAQGDYILGGLFPLGSTEEATLNQRTQPNSIPCNRFSPLGLFLAMAMKMAVEEINNGSALLPGLRLGYDLFDTCSEPVVTMKSSLMFLAKVGSQSIAAYCNYTQYQPRVLAVIGPHSSELALITGKFFSFFLMPQVSYSASMDRLSDRETFPSFFRTVPSDRVQLQAVVTLLQNFSWNWVAALGSDDDYGREGLSIFSSLANARGICIAHEGLVPQHDTSGQQLGKVLDVLRQVNQSKVQVVVLFASARAVYSLFSYSIHHGLSPKVWVASESWLTSDLVMTLPNIARVGTVLGFLQRGALLPEFSHYVETHLALAADPAFCASLNAELDLEEHVMGQRCPRCDDIMLQNLSSGLLQNLSAGQLHHQIFATYAAVYSVAQALHNTLQCNVSHCHVSEHVLPWQLLENMYNMSFHARDLTLQFDAEGNVDMEYDLKMWVWQSPTPVLHTVGTFNGTLQLQQSKMYWPGNQVPVSQCSRQCKDGQVRRVKGFHSCCYDCVDCKAGSYRKHPDDFTCTPCNQDQWSPEKSTACLPRRPKFLAWGEPVVLSLLLLLCLVLGLALAALGLSVHHWDSPLVQASGGSQFCFGLICLGLFCLSVLLFPGRPSSASCLAQQPMAHLPLTGCLSTLFLQAAETFVESELPLSWANWLCSYLRGLWAWLVVLLATFVEAALCAWYLIAFPPEVVTDWSVLPTEVLEHCHVRSWVSLGLVHITNAMLAFLCFLGTFLVQSQPGRYNRARGLTFAMLAYFITWVSFVPLLANVQVAYQPAVQMGAILVCALGILVTFHLPKCYVLLWLPKLNTQEFFLGRNAKKAADENSGGGEAAQGHNE
Protein: Proteasome subunit alpha type-6 (Proteasome subunit alpha 1) (O17586)
Organism: Caenorhabditis elegans
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-1
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-1
- Proteasome subunit beta
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-4
- Proteasome subunit beta
Sequence:
MSRGSSAGFDRHITIFSPEGRVYQVEYAFKAINSTNLTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVSVGVKQLPATSFLEKKIKKKSELTSTEAIELAIEALQTSLGIDVRSKDLEVVVVTKDNSKFTKLTSDQVEHHLNQIANRD
Protein: NANOS3 (Nanos homolog 3) (Nanos2) (A7XBY3)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- DND microRNA-mediated repression inhibitor 1
- Piwi-like RNA-mediated silencing 1
- RRM domain-containing protein.
- CCR4-NOT transcription complex subunit 1
- Pumilio 2
- Pumilio homolog 1
Sequence:
MSDVESGLLHLIMEPSSSRFHLWKDYMGLSDTVKEILGRNPPTESYLECGGHRSSKYDLNRDMRSNAALQSAPAGTDLLRAPPLRSPRAPHLPGSFEVPPPEPPKSRSRDSKDTGRGRLDQPETPSSPDGPMVCSFCRHNGESEMVYRSHWLKNQKGDVLCPYLRQYVCPLCGATGAKAHTKRFCPKVDRTYSSVYVKSRR
Protein: V-type proton ATPase subunit C 1 (V-ATPase subunit C 1) (Vacuolar proton pump subunit C 1) (P21282)
Organism: Bos taurus (Bovine)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5FVI6}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit E 1
- Renin receptor
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase 116 kDa subunit a 1
- Ribonuclease kappa
Sequence:
MTEFWLISAPGEKTCQQTWEKLHAATTKNNNLAVSSKFNIPDLKVGTLDVLVGLSDELAKLDAFVEGVVKKVAQYMADVLEDSKDKVQENLLANGVDLVTYITRFQWDMAKYPIKQSLKNISEIIAKGVTQIDNDLKSRASAYNNLKGNLQNLERKNAGSLLTRSLAEIVKKDDFVLDSEYLVTLLVVVPKLNHNDWIKQYETLAEMVVPRSSNVLSEDQDSYLCNVTLFRKAVDDFRHKARENKFIVRDFQYNEEEMKADKEEMNRLSTDKKKQFGPLVRWLKVNFSEAFIAWIHVKALRVFVESVLRYGLPVNFQAMLLQPNKKTMKKLREVLYELYKHLDSSAAAIIDAPMDIPGLNLSQQEYYPYVYYKIDCNLLEFK
Protein: Type II NADH:quinone oxidoreductase (EC 1.6.5.9) (Cupric reductase) (EC 1.16.1.-) (NADH dehydrogenase-2) (NADH dh II) (NDH-2) (NADH-quinone reductase) (NQR) (NADH:ubiquinone oxidoreductase) (Respiratory NADH dehydrogenase) (P00393)
Organism: Escherichia coli (strain K12)
Function: Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones. Utilizes NADH exclusively, and electron flow from NADH to ubiquinone does not generate an electrochemical gradient.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:10664466, ECO:0000269|PubMed:2679883, ECO:0000269|PubMed:6362717, ECO:0000269|PubMed:6784762, ECO:0000269|PubMed:7009604, ECO:0000269|PubMed:7020757}; Peripheral membrane protein {ECO:0000269|PubMed:10664466, ECO:0000305|PubMed:12176061}; Cytoplasmic side {ECO:0000305|PubMed:12176061}. Note=Membrane-bound (PubMed:10664466). Interaction with the membrane is probably mediated by amphipathic helices and electrostatic interactions (PubMed:15581635). Copurifies with phospholipids (PubMed:6362717, PubMed:7020757). {ECO:0000269|PubMed:10664466, ECO:0000269|PubMed:15581635, ECO:0000269|PubMed:6362717, ECO:0000269|PubMed:7020757}.
Interaction partners:
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit C/D
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit K
Sequence:
MTTPLKKIVIVGGGAGGLEMATQLGHKLGRKKKAKITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVIDIDREAKTITIAELRDEKGELLVPERKIAYDTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANLGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYKGLTNEALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIEADLMVWAAGIKAPDFLKDIGGLETNRINQLVVEPTLQTTRDPDIYAIGDCASCPRPEGGFVPPRAQAAHQMATCAMNNILAQMNGKPLKNYQYKDHGSLVSLSNFSTVGSLMGNLTRGSMMIEGRIARFVYISLYRMHQIALHGYFKTGLMMLVGSINRVIRPRLKLH
Protein: DNA fragmentation factor subunit alpha (A0A8I6ANF5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
RLQWPTWVQRLTDPWRFYLHREAREGDGKLQIQAHWPDFEPNGVQRIRSTLAHKSACELLAIDKSLTPVTLVLAEDGTIVDDEDYFLCLPSNTKFVALACNEKWAYNDSDGGTAWLSQESFDTDQTDSGAGVKWKNVARQLKEDLSSIILLSEEELQALIDIPCAELAQELCQSCATVQGLQSTLQQVLDQREEARQSKQLLELYLQALEKEGSILSNQNESKAALGEELDAVDTGVGGEVASEVMLRSQILAALKEKPAPELSLSSQDLEVGKN
Protein: Aliphatic amidase expression-regulating protein (P27017)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Negatively regulates the expression of the aliphatic amidase operon. AmiC functions by inhibiting the action of AmiR at the protein level. It exhibits protein kinase activity.
Interaction partners:
- Aliphatic amidase regulator
- Aliphatic amidase
- ATP-dependent protease ATP-binding subunit-like protein AmiB
- High-affinity branched-chain amino acid transport system permease protein BraD
- Putative transporter protein AmiS
- Probable permease of ABC branched-chain amino acid transporter
- Probable permease of ABC transporter
- Amino acid binding protein
- Leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein
- High-affinity branched-chain amino acid transport system permease protein BraE
Sequence:
MGSHQERPLIGLLFSETGVTADIERSQRYGALLAVEQLNREGGVGGRPIETLSQDPGGDPDRYRLCAEDFIRNRGVRFLVGCYMSHTRKAVMPVVERADALLCYPTPYEGFEYSPNIVYGGPAPNQNSAPLAAYLIRHYGERVVFIGSDYIYPRESNHVMRHLYRQHGGTVLEEIYIPLYPSDDDVQRAVERIYQARADVVFSTVVGTGTAELYRAIARRYGDGRRPPIASLTTSEAEVAKMESDVAEGQVVVAPYFSSIDTAASRAFVQACHGFFPENATITAWAEAAYWQTLLLGRAAQAAGSWRVEDVQRHLYDICIDAPQGPVRVERQNNHSRLSSRIAEIDARGVFQVRWQSPEPIRPDPYVVVHNLDDWSASMGGGALP
Protein: Alpha-L-arabinofuranosidase 1 (AtASD1) (EC 3.2.1.55) (Beta-D-xylosidase) (EC 3.2.1.-) (Q9SG80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the coordinated dissolution of the cell wall matrix during abscission and in the secondary cell wall formation in xylem vessels. Prefers arabinoxylan, but may also use pectic arabinans as substrates.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- L-arabinokinase
- Mevalonate/galactokinase family protein
- Alpha-L-arabinofuranosidase 2
- Putative mannan endo-1,4-beta-mannosidase P
- Exopolygalacturonase clone GBGA483
- Beta-D-xylosidase 1
- Exopolygalacturonase clone GBGE184
- Probable glucuronokinase 2
- Glucuronokinase 1
- Aldo-keto reductase family 4 member C10
Sequence:
MDMESWKLLRSVCVLSFLLGSCFVYQSLRVVDAQEDPKPAVTLQVDASNGGGRPIPETLFGIFFEEINHAGAGGLWAELVSNRGFEAGGQNTPSNIWPWSIVGDHSSIYVATDRSSCFERNKIALRMDVLCDSKGCPSGGVGVYNPGYWGMNIEEGKKYKVALYVRSTGDIDLSVSLTSSNGSRTLASEKIIASASDVSKWIKKEVLLEAKATDPSARLQLTTTKKGSIWIDQVSAMPVDTHKGHGFRNDLFQMMADIKPRFIRFPGGCFVEGEWLSNAFRWKETVGPWEERPGHFGDVWKYWTDDGLGHFEFFQMAEDIGAAPIWVFNNGISHNDEVETASIMPFVQEALDGIEFARGDANSTWGSVRAKMGRQEPFELKYVAIGNEDCGKTYYRGNYIVFYDAIKKAYPDIKIISNCDGSSHPLDHPADYYDYHIYTSASNLFSMYHQFDRTSRKGPKAFVSEYAVTGKDAGTGSLLASLAEAAFLIGLEKNSDIVEMASYAPLFVNTNDRRWNPDAIVFNSSHLYGTPSYWVQRFFAESSGATLLTSTLKGNSTSLVASAISWKNNGKDYIRIKAVNFGANSENMQVLVTGLDPNVMRVSGSKKTVLTSTNVMDENSFSQPEKVVPHESLLELAEEDMTVVLPPHSFSSFDLLKESAKIRMPISDSSSHQKTTTV
Protein: Propionyl-CoA carboxylase, biotin carboxylase and biotin-carboxyl carrier subunit (PCC) (EC 6.4.1.3) [Includes: Biotin carboxylase (BC) (EC 6.3.4.14); Biotin-carboxyl carrier protein (BCCP)] (I3R7G3)
Organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Function: This is one of the subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), the enzyme catalyzing the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase is involved in propionate utilization and in the production of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate)(PHBV), which is a water-insoluble biopolymer used as intracellular energy reserve material when cells grow under conditions of nutrient limitation. Propionyl-CoA carboxylase is also able to catalyze the carboxylation of acetyl-CoA.
Interaction partners:
- Propionyl-CoA carboxylase, carboxyltransferase subunit
- Acyl-CoA carboxylase subunit beta
- Bifunctional biotin--[acetyl-CoA-carboxylase] synthetase/biotin operon repressor
- Propionyl-CoA carboxylase, protein PccX subunit
- Probable 2-isopropylmalate synthase
- 2-oxo acid dehydrogenase subunit E2)
- 3-ketoacyl-CoA thiolase
- acetyl-CoA C-acyltransferase
- Acetyl-CoA C-acyltransferase
- Acetate--CoA ligase
Sequence:
MFSKVLVANRGEIAVRVMRACEELGVRTVAVYSEADKHGGHVRYADEAYNIGPARAADSYLDHESVIEAARKADADAIHPGYGFLAENAEFARKVEDSEFTWVGPSADAMERLGEKTKARSLMQDADVPVVPGTTEPADSAEDVKAVADDYGYPVAIKAEGGGGGRGLKVVHSEDEVDGQFETAKREGEAYFDNASVYVEKYLEAPRHIEVQILADEHGNVRHLGERDCSLQRRHQKVIEEAPSPALSEDLRERIGEAARRGVRAAEYTNAGTVEFLVEDGEFYFMEVNTRIQVEHTVTEEVTGLDVVKWQLRVAAGEELDFSQDDVEIEGHSMEFRINAEAPEKEFAPATGTLSTYDPPGGIGIRMDDAVRQGDEIGGDYDSMIAKLIVTGSDREEVLVRAERALNEFDIEGLRTVIPFHRLMLTDEAFREGSHTTKYLDEVLDPERIEAAVERWSPEAVAGDEEEGEVTERTFTVEVNGKRFEVSLEERGAPAIPLGGASAAASASKPSGPRKRREESDEGGQQVIEGDGESVAAEMQGTILAVEVDEGDDVEPGDTVCILEAMKMENDVVAERGGTVSQVLVGEGDSVDMGDVLLVLE
Protein: TUBB protein (Q6P602)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA
Protein: Protein ARV1 (Q06541)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes. Regulates also the sphingolipid metabolism. Required for growth during anaerobiosis and sterol uptake.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12145310}; Multi-pass membrane protein {ECO:0000269|PubMed:12145310}. Golgi apparatus membrane {ECO:0000269|PubMed:12145310}; Multi-pass membrane protein {ECO:0000269|PubMed:12145310}.
Interaction partners:
- GPI ethanolamine phosphate transferase 2
Sequence:
MICITCMRPVDSLYTVYSNDHIQLTDCPYCQETVDKYVEIDNVLLFIDLLLLKAGAYRHLVFNALELHLSKYPKRKALNDCQCLRDYTQALLFNVKNWFCKYDRLNRLWLLLLSFEIYLTWVTEESKYIYYLNRNNNDGKLIMLSKKLPESFKWDSAIMRNTITSKVFTWSPPIQYLYFASYCILDVSLFHTFTQYFILKKLHWKHYSVSSKDVISYTILLSYGAKIFPILMLIWPYDTLISMSIIKWVANLYIIESLKIVTNLSYWNIIKIFISVSLLRYFMVKPILIVFVAKFNFSVIKNLIHQEFILLLQKSGTYLLL
Protein: F3N23.33 protein (Mucin) (Q9S781)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Rhomboid-like protein 18
- Rhomboid-like protein 20
- Autophagy-related protein 8f
Sequence:
MGPESKGRAWFSKIYNKLENLLVEVDSFTSQSTLCLKSSEPPRFEYVRGESKEVAEDHSSNVQGRHDRVASPRSESPSDPPSHQNFDIPGHVLVEKRVQGDILKENVVQRDSFEDNSSASSSSDGEIESTSPLHEEYCDAYMTSTTTLSDEEQLVSDEESQIFPDGERLSTSPLLEEYHDANLTSAASVGDEEPIVTDKESHITKSLSNSPSCNSPSDSPPCQNFDILGHVRVEERVQGDILVENIAHGENSSASSLDGEETLSTSPLLEELCDANLTSTSTLGGEEPIVTDDESQITNTLTPQKFSAENSSVFPGEESVQEVRVESSLSDEEILSKSPLLEEHCDANLTSTSTLGGEGPIVTDDESLITNTLTPQKFSEEEILSKSPLLEEHCDANLTSDTTLGDEKPIITDDESWISNSLTSQKSSAGNSWVFSGEDSVEEVKVKSCRDVVSTESQSTQSSMESFGTVVKCNDGPVLAALGCFRDNDSSLNPLVTKVPDENMRSSNADNPDDVINNCKSDVTPLDTKDIAFQKEPSYVNDTVRVRIMAELCGMESREDPLYVEDSELYAIHLRTKKLRSFKRKVLDVLTSKRRREKEYEQLPIWYGDAGMGSDLATKEESQQVEATDSKSSLLLESEDSQWELL
Protein: Proteasome-activating nucleotidase (PAN) (Proteasomal ATPase) (Proteasome regulatory ATPase) (Proteasome regulatory particle) (Q58576)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. In addition to ATP, is able to cleave other nucleotide triphosphates such as CTP, GTP and UTP, but hydrolysis of these other nucleotides is less effective in promoting proteolysis than ATP. Moreover, PAN by itself can function as a chaperone in vitro.
Subcellular location: Cytoplasm.
Interaction partners:
- Proteasome subunit alpha
- Proteasome subunit beta
- Large ribosomal subunit protein eL40
- Cell division cycle protein 48 homolog MJ1156
- DNA double-strand break repair Rad50 ATPase
- Uncharacterized protein MJ0585
- Probable ATP-dependent helicase MJ0942
- Leucine--tRNA ligase
- Alanine--tRNA ligase
Sequence:
MVFEEFISTELKKEKKAFTEEFKEEKEINDNSNLKNDLLKEELQEKARIAELESRILKLELEKKELERENLQLMKENEILRRELDRMRVPPLIVGTVVDKVGERKVVVKSSTGPSFLVNVSHFVNPDDLAPGKRVCLNQQTLTVVDVLPENKDYRAKAMEVDERPNVRYEDIGGLEKQMQEIREVVELPLKHPELFEKVGIEPPKGILLYGPPGTGKTLLAKAVATETNATFIRVVGSELVKKFIGEGASLVKDIFKLAKEKAPSIIFIDEIDAIAAKRTDALTGGDREVQRTLMQLLAEMDGFDARGDVKIIGATNRPDILDPAILRPGRFDRIIEVPAPDEKGRLEILKIHTRKMNLAEDVNLEEIAKMTEGCVGAELKAICTEAGMNAIRELRDYVTMDDFRKAVEKIMEKKKVKVKEPAHLDVLYR