wanglab/gogpt-training-data huggingface dataset:
Protein: Orange carotenoid-binding protein (OCP) [Cleaved into: Red carotenoid-binding protein (RCP)] (P74102)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Acts as a blue-light photoreceptor and photo-protectant. Essential for inhibiting damaged induced by excess blue-green light via a process known as non-photochemical quenching (NPQ). In the dark or dim light the stable inactive form (OCP-O) is orange, upon illumination with blue-green light it converts to a metastable active red form (OCP-R), inducing energy dissipation, quenching cellular fluorescence via NPQ. One OCP-R molecule is sufficient to quench 1 phycobilisome. More OCP-R accumulates under high-light and low temperature; in the dark OCP-R spontaneously reverts to OCP-O. Reversion of OCP-O is accelerated by FRP. A kinetic study suggests conversion of OCP-O to OCP-R is limited by cis-trans proline isomerization of either Gln224-Pro225 or Pro225-Pro226.
Subcellular location: Cellular thylakoid membrane {ECO:0000269|PubMed:16531492}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:16531492}. Note=Associated with the phycobilisome on the cytoplasmic side of the thylakoid membrane (PubMed:16531492). {ECO:0000269|PubMed:16531492}.
Interaction partners:
- Fluorescence recovery protein
- Phycobiliprotein ApcE
- Allophycocyanin alpha chain
- Allophycocyanin subunit alpha-B
- Phycobilisome 7.8 kDa linker polypeptide, allophycocyanin-associated, core
- Allophycocyanin beta chain
- Allophycocyanin subunit beta-18
- Phycobilisome rod-core linker polypeptide CpcG
- Sll1873 protein
- LPS glycosyltransferase IcsA
Sequence:
MPFTIDSARGIFPNTLAADVVPATIARFSQLNAEDQLALIWFAYLEMGKTLTIAAPGAASMQLAENALKEIQAMGPLQQTQAMCDLANRADTPLCRTYASWSPNIKLGFWYRLGELMEQGFVAPIPAGYQLSANANAVLATIQGLESGQQITVLRNAVVDMGFTAGKDGKRIAEPVVPPQDTASRTKVSIEGVTNATVLNYMDNLNANDFDTLIELFTSDGALQPPFQRPIVGKENVLRFFREECQNLKLIPERGVTEPAEDGFTQIKVTGKVQTPWFGGNVGMNIAWRFLLNPEGKIFFVAIDLLASPKELLNFAR
Protein: Peroxiredoxin-5, mitochondrial (EC 1.11.1.24) (Antioxidant enzyme B166) (AOEB166) (Liver tissue 2D-page spot 2D-0014IV) (PLP) (Peroxiredoxin V) (Prx-V) (Peroxisomal antioxidant enzyme) (Thioredoxin peroxidase PMP20) (Thioredoxin-dependent peroxiredoxin 5) (P99029)
Organism: Mus musculus (Mouse)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:P30044}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm {ECO:0000250|UniProtKB:P30044}. Peroxisome matrix {ECO:0000250|UniProtKB:P30044}.
Interaction partners:
- Thioredoxin-dependent peroxide reductase, mitochondrial
- Thioredoxin
- Thioredoxin, mitochondrial
- Peroxiredoxin-1
- Peroxiredoxin-2
- Thioredoxin domain-containing protein 3
- Superoxide dismutase, mitochondrial
- Peroxiredoxin-4
- Peroxiredoxin-6
- Superoxide dismutase
Sequence:
MLQLGLRVLGCKASSVLRASTCLAGRAGRKEAGWECGGARSFSSSAVTMAPIKVGDAIPSVEVFEGEPGKKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDVFVIEEWGRAHQAEGKVRLLADPTGAFGKATDLLLDDSLVSLFGNRRLKRFSMVIDNGIVKALNVEPDGTGLTCSLAPNILSQL
Protein: NADPH-dependent thioredoxin reductase 3 (NTR3) (EC 1.8.1.9) (NADPH-dependent thioredoxin reductase C) (ANTR-C) (AtNTRC) (O22229)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for plastidial 2-Cys peroxiredoxins and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark. Required for chlorophyll biosynthesis and biogenesis of the photosynthetic apparatus. Activates aerobic cyclase which converts Mg-protoporhyrin monomethyl ester into protochlorophyllide. Involved in a light-dependent regulation of starch biosynthesis by redox activation of the ADP-glucose pyrophosphorylase (AGPase), a central enzyme of starch synthesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16884685}.
Interaction partners:
- 2-Cys peroxiredoxin BAS1, chloroplastic
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- 1-Cys peroxiredoxin PER1
- Peroxiredoxin Q, chloroplastic
- Glutathione reductase, chloroplastic
- Methionine gamma-lyase
- Thioredoxin reductase 1, mitochondrial
- Thioredoxin reductase 2
- Thioredoxin F1, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
Sequence:
MAASPKIGIGIASVSSPHRVSAASSALSPPPHLFFLTTTTTTRHGGSYLLRQPTRTRSSDSLRLRVSATANSPSSSSSGGEIIENVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGGVPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPEDVESLSVTTAPFTVQTSERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGASPLFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNTKGQMSGILLRRLDTGEETELEAKGLFYGIGHSPNSQLLEGQVELDSSGYVLVREGTSNTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYLTSNNLLVEFHQPQTEEAKKEFTQRDVQEKFDITLTKHKGQYALRKLYHESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYREFIEANK
Protein: Meiotic recombination protein SPO11-2 (AtSPO11-2) (EC 5.6.2.2) (Q9M4A1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with MTOPVIB, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles.
Subcellular location: Nucleus {ECO:0000269|PubMed:17018031, ECO:0000269|PubMed:17965269}.
Interaction partners:
- DNA topoisomerase 6 subunit B
- Type 2 DNA topoisomerase 6 subunit B-like
- Meiotic recombination protein DMC1 homolog
- DNA mismatch repair protein MSH4
- DNA repair protein RAD51 homolog 1
- Protein MULTIPOLAR SPINDLE 1
- DNA mismatch repair protein MSH5
- Protein PUTATIVE RECOMBINATION INITIATION DEFECT 1
- Meiosis-specific protein ASY1
- Meiotic recombination protein SPO11-1
Sequence:
MEESSGLSSMKFFSDQHLSYADILLPHEARARIEVSVLNLLRILNSPDPAISDLSLINRKRSNSCINKGILTDVSYIFLSTSFTKSSLTNAKTAKAFVRVWKVMEICFQILLQEKRVTQRELFYKLLCDSPDYFSSQIEVNRSVQDVVALLRCSRYSLGIMASSRGLVAGRLFLQEPGKEAVDCSACGSSGFAITGDLNLLDNTIMRTDARYIIIVEKHAIFHRLVEDRVFNHIPCVFITAKGYPDIATRFFLHRMSTTFPDLPILVLVDWNPAGLAILCTFKFGSIGMGLEAYRYACNVKWIGLRGDDLNLIPEESLVPLKPKDSQIAKSLLSSKILQENYIEELSLMVQTGKRAEIEALYCHGYNYLGKYIATKIVQGKYI
Protein: GH01690p (Q8SWY1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAMGVIQSAIGLFGNVPCPIIYGAVVDSACLIWKSVCGKHGACSLYDADTFRQYFLGITAGIMFLAFLMDLVVWRKAHRIDIAPEDPQEGGPASNGRTLEVSESKQPITPAPDTTV
Protein: Stretchin-MLCK (Q9NBB9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
PHNFGTDRIFVTVTVNPRARSATPTQPRWGLPLDSYSDTSYFRDPPGCISTEPLVVDSGPTHISLSWGKPVSANSAPVMAYKVEAWVVGHEGGAYWRELGLTPINSFDAFNLKPNVEYHFRVTPKNRYGWGPTVQTSSPLQVGGVECLPEFVKILPGQAKALLGSSFTLQCNMRGAPRPQVTWFKDGIQLSSSSERVKIRQIGSTCALTIATVSELDSGRYTCEATNSKGR
Protein: Transmembrane protein 256 (Q8N2U0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAGPAAAFRRLGALSGAAALGFASYGAHGAQFPDAYGKELFDKANKHHFLHSLALLGVPHCRKPLWAGLLLASGTTLFCTSFYYQALSGDPSIQTLAPAGGTLLLLGWLALAL
Protein: KLF transcription factor 3 (D4A4V3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- C-terminal-binding protein 1
- C-terminal-binding protein 2
Sequence:
MLMFDPVPVKQEAMDPVTVSYPSNYIESMKPNKYGVIYSTPLPDKFFQTPEGLAHGIQMEPVDLTVNKRGSPPSAAGSPSSLKFPSHRRASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPVMAAALTRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDNSNSGMPVPVIESYEKPILQKKIKIEPGIEPQRTDYYPEEMSPPLMNSVSPPQALLQENHPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV
Protein: SNAP25 homologous protein SNAP33 (AtSNAP33) (Snap25a) (Synaptosomal-associated protein SNAP25-like 1) (SNAP-25-like protein 1) (Q9S7P9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: t-SNARE involved in diverse vesicle trafficking and membrane fusion processes, including cell plate formation. May function in the secretory pathway.
Subcellular location: Membrane. Note=Plasma membrane, some endomembrane compartment and cell plate in dividing cells.
Interaction partners:
- Syntaxin-121
- Vesicle-associated membrane protein 721
- Vesicle-associated membrane protein 722
- Arabidiol synthase
- Syntaxin-related protein KNOLLE
- Putative syntaxin-24
- Syntaxin-122
- Syntaxin-132
- Exocyst complex component EXO70B2
- Syntaxin-21
Sequence:
MFGLRKSPANLPKHNSVDLKSSKPNPFDSDDESDNKHTLNPSKRTTSEPSLADMTNPFGGERVQKGDSSSSKQSLFSNSKYQYKNNFRDSGGIENQSVQELEGYAVYKAEETTKSVQGCLKVAEDIRSDATRTLVMLHDQGEQITRTHHKAVEIDHDLSRGEKLLGSLGGMFSKTWKPKKTRPINGPVVTRDDSPTRRVNHLEKREKLGLNSAPRGQSRTREPLPESADAYQRVEMEKAKQDDGLSDLSDILGELKNMAVDMGSEIEKQNKGLDHLHDDVDELNFRVQQSNQRGRRLLGK
Protein: Peroxisomal biogenesis factor 2 (EC 2.3.2.36) (E3 ubiquitin-protein ligase PEX2) (Peroxin-2) (Peroxisomal protein PER6) (Q01964)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 or PEX20 receptors from peroxisomes to the cytosol, thereby promoting PEX5 and PEX20 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 and PEX20 through the peroxisomal membrane (By similarity). PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase (By similarity). PEX2 ubiquitinates PEX5 or PEX20 during their passage through the retrotranslocation channel: catalyzes monoubiquitination of PEX5 and/or PEX20 at 'Cys-6' and 'Cys-8', respectively, a modification that acts as a signal for PEX5 or PEX20 extraction into the cytosol (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:8628321}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPNRLIPLANPANRVLQLDAKLLDNEISDMLYRQLSGAFNSNRLPSWLGRIHSNYASELKLLLELLIFKVTVWNKHSSYGLTLQNLVMYDGGVHNKKFRSKQQSELRVTKKILLLSSVLLGYFVKKIQSYVYSFEDYDLETDGEDLSTLERIRLKTIKLLKSQISTLEKAHSVLSLVNFVTFLVSGSFPDLTTRILNIRFKPLVTTQVAFASNPETISYEFQNRQLVWNTLTEFIVFILPALSVPKFTKSLVSSITGTSPKSSQVTDEDLKVFSSLPERVCAICFQNSQNSDSGAQNDISLNDTLVTNPYETTCGHIYCYVCILSKLQIFKEEGKNLPKSDPNKYWHCLRCNEPASWCRVYTGDVEDALRQKAVEEVTEDEDASSEDEEKRDQDSEGAKTVSQSFHHVNGSDYQTASFIEQAELNENEYTDGSEVEIYDAEDEYTDEEVDDDSPGFFVGAL
Protein: Copper transport protein (Q9VA22)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU367022}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367022}.
Interaction partners:
- P-type Cu
- Serine/threonine-protein phosphatase
- Copper transport protein ATOX1
- Protein Malvolio
- Glutamate transporter polyphemus
- Uncharacterized protein
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase b
Sequence:
MDHHGVDASEGHVHHHASHGSPEPVPPSSGHEGHHSPEMNHHGNHGEHTKHGHHEGGAHDMSMAMFFHTGDSETILFKFWRTESAMALTLSCLLIFMVAVLYEALKFFREWLFSWDRKRLAGGRDQYNRPRRYREANYNYNQPTYPPRTNQQSGTQVYAYRPRSPSMPPLQPPGRSSPQAQSSLILTQHTHHHVQENTPPAGRTTKLKVFCSGMHILQTFLHVLQVLISFLLMLVFMTFNVWLCVAVLLGAGVGYYIFCAFRTNVQEHCN
Protein: Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3) (Q9H4L5)
Organism: Homo sapiens (Human)
Function: Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes. Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With VAPA, may regulate ER morphology. Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion. Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3. Also binds 25-hydroxycholesterol and cholesterol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16143324}; Peripheral membrane protein {ECO:0000269|PubMed:16143324}. Cytoplasm, cytosol {ECO:0000269|PubMed:16143324}. Cell membrane {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}; Peripheral membrane protein {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}. Cell projection, filopodium tip {ECO:0000269|PubMed:18270267}. Nucleus membrane {ECO:0000269|PubMed:16143324}; Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with OSBPL6 at contact sites between the plasma membrane and the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9DBS9}.
Interaction partners:
- Ras-related protein R-Ras
- Vesicle-associated membrane protein-associated protein A
- Vesicle-associated membrane protein-associated protein B/C
- Pleckstrin-2
- Pleckstrin
Sequence:
MMSDEKNLGVSQKLVSPSRSTSSCSSKQGSRQDSWEVVEGLRGEMNYTQEPPVQKGFLLKKRKWPLKGWHKRFFYLDKGILKYAKSQTDIEREKLHGCIDVGLSVMSVKKSSKCIDLDTEEHIYHLKVKSEEVFDEWVSKLRHHRMYRQNEIAMFPHEVNHFFSGSTITDSSSGVFDSISSRKRSSISKQNLFQTGSNVSFSCGGETRVPLWLQSSEDMEKCSKDLAHCHAYLVEMSQLLQSMDVLHRTYSAPAINAIQGGSFESPKKEKRSHRRWRSRAIGKDAKGTLQVPKPFSGPVRLHSSNPNLSTLDFGEEKNYSDGSETSSEFSKMQEDLCHIAHKVYFTLRSAFNIMSAEREKLKQLMEQDASSSPSAQVIGLKNALSSALAQNTDLKERLRRIHAESLLLDSPAVAKSGDNLAEENSRDENRALVHQLSNESRLSITDSLSEFFDAQEVLLSPSSSENEISDDDSYVSDISDNLSLDNLSNDLDNERQTLGPVLDSGREAKSRRRTCLPAPCPSSSNISLWNILRNNIGKDLSKVAMPVELNEPLNTLQRLCEELEYSELLDKAAQIPSPLERMVYVAAFAISAYASSYYRAGSKPFNPVLGETYECIREDKGFQFFSEQVSHHPPISACHAESRNFVFWQDVRWKNKFWGKSMEIVPIGTTHVTLPVFGDHFEWNKVTSCIHNILSGQRWIEHYGEIVIKNLHDDSCYCKVNFIKAKYWSTNAHEIEGTVFDRSGKAVHRLFGKWHESIYCGGGSSSACVWRANPMPKGYEQYYSFTQFALELNEMDPSSKSLLPPTDTRFRPDQRFLEEGNLEEAEIQKQRIEQLQRERRRVLEENHVEHQPRFFRKSDDDSWVSNGTYLELRKDLGFSKLDHPVLW
Protein: Solute carrier family 12 member 7 (Electroneutral potassium-chloride cotransporter 4) (K-Cl cotransporter 4) (Q9Y666)
Organism: Homo sapiens (Human)
Function: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May mediate K(+) uptake into Deiters' cells in the cochlea and contribute to K(+) recycling in the inner ear. Important for the survival of cochlear outer and inner hair cells and the maintenance of the organ of Corti. May be required for basolateral Cl(-) extrusion in the kidney and contribute to renal acidification (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10913127}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPTNFTVVPVEAHADGGGDETAERTEAPGTPEGPEPERPSPGDGNPRENSPFLNNVEVEQESFFEGKNMALFEEEMDSNPMVSSLLNKLANYTNLSQGVVEHEEDEESRRREAKAPRMGTFIGVYLPCLQNILGVILFLRLTWIVGVAGVLESFLIVAMCCTCTMLTAISMSAIATNGVVPAGGSYYMISRSLGPEFGGAVGLCFYLGTTFAGAMYILGTIEIFLTYISPGAAIFQAEAAGGEAAAMLHNMRVYGTCTLVLMALVVFVGVKYVNKLALVFLACVVLSILAIYAGVIKSAFDPPDIPVCLLGNRTLSRRSFDACVKAYGIHNNSATSALWGLFCNGSQPSAACDEYFIQNNVTEIQGIPGAASGVFLENLWSTYAHAGAFVEKKGVPSVPVAEESRASALPYVLTDIAASFTLLVGIYFPSVTGIMAGSNRSGDLKDAQKSIPTGTILAIVTTSFIYLSCIVLFGACIEGVVLRDKFGEALQGNLVIGMLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIARDGIVPFLQVFGHGKANGEPTWALLLTVLICETGILIASLDSVAPILSMFFLMCYLFVNLACAVQTLLRTPNWRPRFKFYHWTLSFLGMSLCLALMFICSWYYALSAMLIAGCIYKYIEYRGAEKEWGDGIRGLSLNAARYALLRVEHGPPHTKNWRPQVLVMLNLDAEQAVKHPRLLSFTSQLKAGKGLTIVGSVLEGTYLDKHMEAQRAEENIRSLMSTEKTKGFCQLVVSSSLRDGMSHLIQSAGLGGLKHNTVLMAWPASWKQEDNPFSWKNFVDTVRDTTAAHQALLVAKNVDSFPQNQERFGGGHIDVWWIVHDGGMLMLLPFLLRQHKVWRKCRMRIFTVAQVDDNSIQMKKDLQMFLYHLRISAEVEVVEMVENDISAFTYERTLMMEQRSQMLKQMQLSKNEQEREAQLIHDRNTASHTAAAARTQAPPTPDKVQMTWTREKLIAEKYRSRDTSLSGFKDLFSMKPDQSNVRRMHTAVKLNGVVLNKSQDAQLVLLNMPGPPKNRQGDENYMEFLEVLTEGLNRVLLVRGGGREVITIYS
Protein: Adenine phosphoribosyltransferase (APRT) (EC 2.4.2.7) (O42842)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- GMP synthase
- Probable guanine deaminase
- Guanylate kinase
- AMP deaminase
- Adenosine kinase
- Putative purine nucleoside phosphorylase
- Adenylate kinase
- S-methyl-5'-thioadenosine phosphorylase
- Inosine triphosphate pyrophosphatase
- Adenylosuccinate lyase
Sequence:
MSDDRINYLKNKLVQYPDFPKKGILFEDIMPIFQDPRAFGILIDLLLEAVETEFNNIDVIVGLEARGFLFGPTLALRANCAFVPVRKPNKLPGDLVVVSYNKEYSTDSFAIQKGTIKPGQRVLIVDDILATGGTALAADELVTRLGGELVGHLFLLELTFLQGRKRLMAPTYTLLTGQDEAPDGSEFA
Protein: Prohibitin (A8DYI6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|RuleBase:RU366048}.
Interaction partners:
- Prohibitin 1
- CG6459 protein
- Mitochondrial-processing peptidase subunit beta
- Paraplegin, isoform A
- Serine/threonine-protein kinase Pink1, mitochondrial
- AFG3 like matrix AAA peptidase subunit 2, isoform A
- ATP-dependent zinc metalloprotease YME1L
- IP15825p
- Uncharacterized protein, isoform C
- Elongation factor Tu
Sequence:
MAQSKLNDLAGKLGKGGPPGLGIGLKVLAAVGAAAYGVSQSLYTVEGGHRAIIFSRLGGIQSDIYSEGLHVRIPWFQYPIIYDIRSRPRKISSPTGSKDLQMINISLRVLSRPDSLNLPYLHKQLGVDYDEKVLPSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEAKQVAQQEAQRAVFFVERAKQEKQQKIVQAEGEAEAAKMLGLAVKQNPAYLKLRKLRAAQSIARTIASSQNKVYLSADSLMLNIQDSGFDDMTEKVYKIGTGLPKDWLDARKMASKVAQPAEKEKNVGNVASSMAERMM
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC 2.3.1.294) (Beta-ketoacyl-ACP synthase 2) (KAS 2) (Beta-ketoacyl-acyl carrier protein synthase KasB) (Meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II) (P9WQD7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the elongation of long chain acyl-ACP substrates by the addition of two carbons from malonyl-ACP to an acyl acceptor. Involved in extension of the mycolate chains to full lengths and produces longer chain multiunsaturated hydrocarbons averaging 54 carbons in length. Essential for resistance to macrophage antimicrobial activity.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- Meromycolate extension acyl carrier protein
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta6 subunit
- Mycobacterial beta-ketoacyl-[acyl-carrier-protein] synthase III
- Probable biotin-dependent acyl-coenzyme A carboxylase beta3 subunit
- Enoyl-[acyl-carrier-protein] reductase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- Mycocerosic acid synthase-like polyketide synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
Sequence:
MTELVTGKAFPYVVVTGIAMTTALATDAETTWKLLLDRQSGIRTLDDPFVEEFDLPVRIGGHLLEEFDHQLTRIELRRMGYLQRMSTVLSRRLWENAGSPEVDTNRLMVSIGTGLGSAEELVFSYDDMRARGMKAVSPLTVQKYMPNGAAAAVGLERHAKAGVMTPVSACASGAEAIARAWQQIVLGEADAAICGGVETRIEAVPIAGFAQMRIVMSTNNDDPAGACRPFDRDRDGFVFGEGGALLLIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAITRAIQLAGLAPGDIDHVNAHATGTQVGDLAEGRAINNALGGNRPAVYAPKSALGHSVGAVGAVESILTVLALRDQVIPPTLNLVNLDPEIDLDVVAGEPRPGNYRYAINNSFGFGGHNVAIAFGRY
Protein: RUN and FYVE domain-containing protein 1 (Rab4-interacting protein) (Q8BIJ7)
Organism: Mus musculus (Mouse)
Function: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:11172003, ECO:0000269|PubMed:11509568, ECO:0000269|PubMed:16522682}; Peripheral membrane protein {ECO:0000269|PubMed:11172003, ECO:0000269|PubMed:11509568, ECO:0000269|PubMed:16522682}. Note=In oocytes, localizes in non-membrane-bound compartments called endo-lysosomal vesicular assemblies (ELVAs). {ECO:0000269|PubMed:38382525}.
Interaction partners:
- Ras-related protein Rab-4A
- Cytoplasmic tyrosine-protein kinase BMX
- Ras-related protein Rab-4B
- Podocalyxin
Sequence:
MAARGECRRAGQDSEPEPEREPESEPGPEPEPQAGLESGEAFEIVDRSQLPSPGELRSASRPRVADSWSAPILTLARRATGNLSASCGSALRAAAGLGDGGGGGERAASKGQMMEERANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLCLKGEDLDSQVGVIDFSLCLKDAQDLDSGREHERITDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALKGHTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCSSTAS
Protein: Desmin (O73665)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000256|ARBA:ARBA00004216}.
Interaction partners:
Sequence:
RVSSYRRTFGGGTSPVFPRASFGSRGSGSSVTSRVYQVSRTSAVPTLSTFRTTRVTPLRTYQSAYQGAGELLDFSLADAMNQEFLQTRTNEKVELQELNDRFANYIEKVRFLEQQNALMVAEVNRLRGKEPTRVAEMYEEELRELRRQVDALTGQRARVEVERDNLLDDLQKLKQRLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLQEEIAFLKKVHEEEIRELQAQLQEQHIQVEMDISKPDLTAALRDIRAQYESIAAKNIAEAEEWYKSKVSDLTQAANKNNDALRQAKQEMLEYRHQIQSYTCEIDALKGTNDSLMRQMREMEERFAGEAGGYQDTIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEENRISIPMHQTFASALNFRETSPDQRGSEVHTKKTVMIKTIETRDGEVVSEAT
Protein: Centrosomal protein of 76 kDa (Cep76) (Q8TAP6)
Organism: Homo sapiens (Human)
Function: Centrosomal protein involved in regulation of centriole duplication. Required to limit centriole duplication to once per cell cycle by preventing centriole reduplication.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Does not localize along the ciliary axoneme.
Interaction partners:
- Centriolar coiled-coil protein of 110 kDa
- Centrosomal protein of 290 kDa
- Serine/threonine-protein kinase PLK1
- Centrosomal protein of 97 kDa
Sequence:
MSLPPEKASELKQLIHQQLSKMDVHGRIREILAETIREELAPDQQHLSTEDLIKALRRRGIIDDVMKELNFVTDSVEQELPSSPKQPICFDRQSTLKKTNIDPTRRYLYLQVLGGKAFLEHLQEPEPLPGQVCSTFTLCLHYRNQRFRSKPVPCACEPDFHDGFLLEVHRESLGDGTRMADSTTMLSISDPIHMVLIKTDIFGETTLVASYFLEWRSVLGSENGVTSLTVELMGVGTESKVSVGILNIKLEMYPPLNQTLSQEVVNTQLALERQKTAEKERLFLVYAKQWWREYLQIRPSHNSRLVKIFAQDENGINRPVCSYVKPLRAGRLLDTPRQAARFVNVLGYERAPVIGGGGKQEQWCTLLAFLCRNKGDCEDHANLLCSLLLGYGLEAFVCVGTKAKGVPHAWVMTCGTDGAITFWESLTGHRYIHKPTNPDEPPVAEQPKPLYPYRTIGCVFNHQMFLGNCQPSDAVETCVFDLNDESKWKPMSEEAIKSVCAPGATTSLPPFPPLCASTIDASVTSNEIEMQLRLLVSEHRKDLGLTTVWEDQLSYLLSPALASYEFERTTSISAGNEEFQDAIRRAVPDGHTFKGFPIHFVYRNARRAFATCLRSPFCEEIICCRGDQVRLAVRVRVFTYPESACAVWIMFACKYRSVL
Protein: Probable acetate kinase EutP (EC 2.7.2.1) (Ethanolamine utilization protein EutP) (P0A208)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: A putative bidirectional acetate kinase that may drive flux through the ethanolamine (EA) degradation pathway under anoxic conditions found when this bacteria infects host intestine. It may generate ATP that can be used by other enzymes (EutA and EutT) in the eut pathway. Can use GTP instead of ATP with reduced efficiency. Overexpression in E.coli yields elongated protein sheets; prevents artificial BMC formation by eutS alone or by eutK, eutL, eutM, eutN, eutS in E.coli.
Subcellular location: Bacterial microcompartment {ECO:0000305|PubMed:26448059}.
Interaction partners:
- Acetate kinase EutQ
- Corrinoid adenosyltransferase EutT
- Bacterial microcompartment shell protein EutS
- Phosphate acetyltransferase EutD
- Ethanolamine utilization protein EutJ
- Ethanolamine ammonia-lyase reactivase EutA
- Bacterial microcompartment shell protein EutL
- Probable ethanolamine permease EutH
- Probable alcohol dehydrogenase EutG
- Acetaldehyde dehydrogenase
Sequence:
MKRIAFVGAVGAGKTTLFNALRGNYSLARKTQAVEFNDHGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDKESRLPAGLLDVGTRKRHIAVISKTDMPDADVAATRQLLCEIGFREPIFELNGHDPQSVRQLVDYLAALSEQEEEAGEKTYHS