wanglab/gogpt-training-data huggingface dataset:
Protein: Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3 (EC 7.2.1.3) (Cytochrome b ascorbate-dependent protein 3) (Cytochrome b561 family member A3) (Lysosomal cytochrome b) (LCytb) (Q6P1H1)
Organism: Mus musculus (Mouse)
Function: Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce iron cations Fe(3+) into Fe(2+) in the lumen of the late endosome and lysosome. Reduced iron can then be extruded from the late endosome and lysosome to the cytoplasm by divalent metal-specific transporters (Probable). It is therefore most probably involved in endosomal and lysosomal cellular iron homeostasis (Probable).
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:16996694}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Lysosome membrane {ECO:0000269|PubMed:16996694}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}.
Interaction partners:
Sequence:
MASGWFYLSCMVLGSLGSMCILFTAYWMQYWRGGFAWDGTVLMFNWHPVLMVAGMVVLYGAASLVYRLPSSWVGPRLPWKVLHAALHLLAFTCTVVGLIAVFRFHNHSRIAHLYSLHSWLGITTVVLFACQWFLGFAVFLLPWASQWLRSLLKPLHVFFGACILSLSITSVISGINEKLFFVLKNATKPYSSLPGEAVFANSTGLLVVAFGLLVLYVLLASSWKRPDPGALTDRQPLLHDRE
Protein: PSEA-binding protein 45kD (RE52723p) (Q9VF25)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- snRNA-activating protein complex subunit 3
- LD18233p
- Transcription initiation factor IIB
- TATA-box-binding protein
- TBP-related factor
- Transcription initiation factor IIA subunit 1
- Transcription initiation factor IIA subunit 2
Sequence:
MELNIFDDCWELVQRFQRLVNDGENCEFEVFCRCWRELQLQHLFTAQTNHTEVIATTLAALHVAKRLSCSRRTTGDVFPASRAQRIGGFFLLYVIYYKQPTHNFIKIEVSPRTWQELTDYALDLRKDSPERKDTHQIAYMLWRLTQEQAFRFTALDYCQGLDNLVDYDRVETVAGAKEQRQSALMQKQQRANGVSLTYELEGLRALDQASQPLCELEAAYNAQKKQLAAGHEHALPPSQIFGHLREVFADIQSVLGARKSTPDENCTTTSTGNQLEVRQRVRNKAMYGVEEREPQNQADELEVQLEVNETYQRRMSSATVFQRELPADVQQEYEMIEFSDDEEMEVGESEEVTEEELKAILDT
Protein: Heat shock 70 kDa protein 10, mitochondrial (Chaperone protein HscA homolog 2) (AtHscA2) (Heat shock protein 70-10) (AtHsp70-10) (Mitochondrial heat shock protein 70-2) (mtHsc70-2) (Q9LDZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone involved in the maturation of iron-sulfur [Fe-S] cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HSCB and ISU1 (By similarity). In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable).
Subcellular location: Mitochondrion {ECO:0000305|PubMed:19865480, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Iron-sulfur cluster co-chaperone protein HscB homolog
- Chaperonin CPN60-like 2, mitochondrial
- Heat shock protein 90-1
- Chaperonin CPN60, mitochondrial
- Chaperonin CPN60-like 1, mitochondrial
- Heat shock 70 kDa protein 9, mitochondrial
- Iron-sulfur cluster assembly protein 1
- Heat shock protein 90-4
- Chaperonin 60 subunit beta 4, chloroplastic
- Chaperonin 60 subunit beta 2, chloroplastic
Sequence:
MATAALLRSIRRREVVSSPFSAYRCLSSSGKASLNSSYLGQNFRSFSRAFSSKPAGNDVIGIDLGTTNSCVAVMEGKNPKVIENAEGARTTPSVVAFNTKGELLVGTPAKRQAVTNPTNTVSGTKRLIGRKFDDPQTQKEMKMVPYKIVRAPNGDAWVEANGQQYSPSQIGAFILTKMKETAEAYLGKSVTKAVVTVPAYFNDAQRQATKDAGRIAGLDVERIINEPTAAALSYGMTNKEGLIAVFDLGGGTFDVSVLEISNGVFEVKATNGDTFLGGEDFDNALLDFLVNEFKTTEGIDLAKDRLALQRLREAAEKAKIELSSTSQTEINLPFITADASGAKHFNITLTRSRFETLVNHLIERTRDPCKNCLKDAGISAKEVDEVLLVGGMTRVPKVQSIVAEIFGKSPSKGVNPDEAVAMGAALQGGILRGDVKELLLLDVTPLSLGIETLGGVFTRLITRNTTIPTKKSQVFSTAADNQTQVGIRVLQGEREMATDNKLLGEFDLVGIPPSPRGVPQIEVTFDIDANGIVTVSAKDKTTGKVQQITIRSSGGLSEDDIQKMVREAELHAQKDKERKELIDTKNTADTTIYSIEKSLGEYREKIPSEIAKEIEDAVADLRSASSGDDLNEIKAKIEAANKAVSKIGEHMSGGSGGGSAPGGGSEGGSDQAPEAEYEEVKK
Protein: Polyubiquitin-C [Cleaved into: Ubiquitin; Ubiquitin-related] (Q63429)
Organism: Rattus norvegicus (Rat)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0CG48}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0CG48}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin-conjugating enzyme E2 N
- 26S proteasome non-ATPase regulatory subunit 14
- Vacuolar protein-sorting-associated protein 36
- NF-kappa-B essential modulator
- E3 ubiquitin-protein ligase parkin
- Ubiquitin-conjugating enzyme E2K
- Ubiquitin-like modifier-activating enzyme 1
- Proteasome subunit beta type-2
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSVNTKKVKQEDTRTFLTTVSRKSPSCACSWV
Protein: Large ribosomal subunit protein uL24m (54S ribosomal protein L40, mitochondrial) (O14178)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mitochondrial genome encoded proteins translation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MRDLRKLIPRLRGPGTNVLKMKKPLPLHMRTKIREHLNKSDPTVKDDKSAKPELPFGKPADRVPFWHIFKGDYVYVHQGPLKGKWGRVVETNKYTNGITIEGVNVRSVKVPIFLLRNKPEDNQDPVIDIAHEVHYANVRLLAHAKTDAGEPVLIPVKLKKHSSTNLRSIIRPNIEGVQIHTIHLPRPKTEDKPKDPEGKLDTKNPVVSKVTWSPSLSEPPLPPFAIGDLRANWSRRLDRIWGYKKNNDDFTEIAKDLVRAETAAEDLIKKPISPNTYSD
Protein: Small ubiquitin-related modifier 1-A (SUMO-1-A) (O57686)
Organism: Xenopus laevis (African clawed frog)
Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity).
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
Interaction partners:
Sequence:
MSDQEAKPSSEDLGDKKDGGDYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYRQRQGVPMNSLRFLFEGQRISDHQTPKELGMEEEDVIEVYQEQTGGHSTF
Protein: X-prolyl aminopeptidase 1 (Q5T6H2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETIP
Protein: Chromobox protein (CHCB1) (O93480)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGKKQNKKKVEEVLEEEEEEYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEFLQSQKTAHESEKSEGSKRKAESDTEDKGEESKPKKKKEESEKPRGFARGFEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANIKCPQVVISFYEERLTWHSYPSEDDDKKEDKN
Protein: KIAA0319 (A0A087X0U9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQEGDYTFQLKVTDSSRQQSTAVVTVIVQPENNRPPVAVAGPDKELIFPVESATLDGSSSSDDHGIVFYHWEHVRGPSAVEMENIDKAIATVTGLQVGTYHFRLTVKDQQGLSSTSTLTVAVKKENNSPPRARAGGRHVLVLPNNSITLDGSRSTDDQRIVSYLWIRDGQSPAAGDVIDGSDHSVALQLTNLVEGVYTFHLRVTDSQGASDTDTATVEVQPDPRKSGLVELTLQVGVGQLTEQRKDTLVRQLAVLLNVLDSDIKVQKIRAHSDLSTVIVFYVQSRPPFKVLKAAEVARNLHMRLSKEKADFLLFKVLRVDTAGCLLKCSGHGHCDPLTKRCICSHLWMENLIQRYIWDGESNCEWSIFYVTVLAFTLIVLTGGFTWLCICCCKRQKRTKIRKKTKYTILDNMDEQERMELRPKYGIKHRSTEHNSSLMVSESEFDSDQDTIFSREKMERGNPKVSMNGSIRNGASFSYCSKDR
Protein: Glutathione reductase (EC 1.8.1.7) (Q59NQ5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU365016}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta
- Glutathione synthetase
- Thioredoxin reductase
- Gst2p
- Thioredoxin peroxidase
- Endonuclease/exonuclease/phosphatase domain-containing protein
- glutathione transferase
- Thioredoxin
- Gst1p
- Acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MFTNSIISKSTTRLTQLSRQLSTTTMAPTSTKNSIKHFDYLVIGGGSGGVASARRAAKYGAKVLLIESNFKKFGGTCVNVGCVPKKVMWYTADLAHKKHDLYAYGLDKEPDSIKYGDFDWAKLKHKRDAYVTRLNGIYENNLKREKVDYAYGFAKFINSEGEVEVTLSGDQELPFLDEGKTYKKGEKLVFSADKTLIATGGTAIVPPSVPGAELGTTSDGFFALEKQPKKVAIVGAGYIGVELSGVFSSLGSETHFFIRGDTVLRSFDEVIQNTVTDYYIDNLGINIHKQSTITKIEGSKDGKKVVHLKDGTSVEVDELIWTVGRKSLIDIGLDKVDVKINDKQQIVADEYQVTNNPKIFSLGDVVGKVELTPVAIAAGRRLSNRLFGGPEFAKDKLDYNNIPSVIFSHPEAGSIGLSTKEAIEKYGEENLKIYQSKFTAMYYAMMDDQKDKSPTVYKIICAGPEEKVVGLHIVGDSSAEILQGFGVAIKMGATKKDFDNCVAIHPTSAEELVTMT
Protein: Phosphotransferase (EC 2.7.1.-) (Q4WCS2)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Phosphoglucomutase
- Mannitol-1-phosphate 5-dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
- Beta-fructofuranosidase, putative
- Exoinulinase InuD
- Fructose-1,6-bisphosphatase
- Phosphomannomutase
- Phosphoglucomutase, putative
Sequence:
MSSPLVTEATRIARQFDFSAEQIQSGVKEYIREMCEGLTKEHTTLSQIPTYVTSVPNGTEKGLYLAVDLGGTNFRVCSIDLHGDTTFNLTQSKIMIPRELMASGTSKDLFLFLARQIEAFLRIHHNEHFEAHLRRRREPNSEEELFDLGFTFSFPVRQLGINKGTLIRWTKGFNIPDAVGHDVCALLQNAIDELDLPVRVAALVNDTVGTLMARSYTSPGDTSTFIGAIFGTGTNGAYVEKLDRITKLQTIEHADYEKSTGEMIINAEWGSFDNHLSVLPNTKWDKELDEDSNNPGIQMFEKRVSGMFLGEILRRALLDMHKDEAFGLFKPNQSSKVVTPENSPLYRQWGIDTSFLSLVEADKTDRMEEVKAALKDHLKIENPSDAECQAVKVLVHAIGKRAARLSAVPLAAILISTGKLETDDMVDIGVDGSLVEFYPNFEGYIREALREVPEVGAAGEKKVRIGISKDGSGVGAALIALVASRNETGSGPK
Protein: Dynamin-like GTPase MGM1, mitochondrial (EC 3.6.5.5) (Mitochondrial division and morphology protein 17) (Mitochondrial genome maintenance protein 1) [Cleaved into: Dynamin-like GTPase MGM1, long form (l-MGM1); Dynamin-like GTPase MGM1, small form (s-MGM1)] (P32266)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.
Subcellular location: [Dynamin-like GTPase MGM1, long form]: Mitochondrion inner membrane {ECO:0000269|PubMed:15096522, ECO:0000269|PubMed:19752025}; Single-pass type II membrane protein {ECO:0000255}; Intermembrane side {ECO:0000305|PubMed:15096522}.; SUBCELLULAR LOCATION: [Dynamin-like GTPase MGM1, small form]: Mitochondrion intermembrane space {ECO:0000269|PubMed:19752025}.
Interaction partners:
- Mitofusin FZO1
- Mitochondrial fusion and transport protein UGO1
- Rhomboid protein 1, mitochondrial
- Mitochondrial fission 1 protein
- Mitochondrial metalloendopeptidase OMA1
- Dynamin-related protein DNM1
- Mitochondrial division protein 1
- CCR4-associated factor 4
- Protein UPS1, mitochondrial
- Mitochondrial distribution and morphology protein 30
Sequence:
MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL
Protein: Plasmodium RESA N-terminal domain-containing protein (Q8IBE9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKQSNKTNVDFCGFFGSILFILCMVSLICITLLNVWTSYEFLNCGTQLSNIRILSEVESLQSSNYSEVMKNVKDGNDSSSEELDNTNVPTSKPKKKLSAVFKENKTFFQYLINEDIYAEYELVPTNKKHTKYSNENDKALNYELESIKKSKKNRYEKMYQLWTRIVQNEENKYILSVRKMFEVFNFIVNYYSVHYSKEEEIMNELRTTFTDLYRNVTPNMNDLFIRWITDNDVLNHGEFALLVDGNRYVWRNLLKHLEIAFKEIITKHFRYQLRSFELERNLIVCEEKSNKSDNINLEKNKKSKKSIKKKILKDMNK
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 (C9JTA6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMMMALSKTFGQKPVKFQLEDDGEFYMIGSEVGNYLRMFRGSLYKRYPSLWRRLATVEERKKIVASSHGKKTKPNTKDHGYTTLATSVTLLKASEVEEILDGNDEKYKAVSISTEPPTYLREQKAKRNSQWVPTLPNSSHHLDAVPCSTTINRNRMGRDKKRTFPLWCGCIAALTLRADSALVLHFDDHDPAVIHENASQPEVLVPIRLDMEIDGQKLRDAFTWNMNEKLMTPEMFSEILCDDLDLNP
Protein: High mobility group B protein 7 (Nucleosome/chromatin assembly factor group D 07) (Nucleosome/chromatin assembly factor group D 7) (Protein NUCLEAR FUSION DEFECTIVE 7) (Q8LDF9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds preferentially double-stranded supercoiled DNA. Required for karyogamy during female gametophyte development, when the two polar nuclei fuse to form the diploid central cell nucleus.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:14756567}.
Interaction partners:
- Glycine-rich protein like
- Actin-related protein 9
- Glycine-rich RNA-binding protein 4, mitochondrial
- Mutator-like transposase
- Mutator-like transposase
- RuvB-like protein 1
Sequence:
MAGPSTTSNAPKQRKRVEAETSSNTSTTLRRAKDGSAFALCEGCNKSVAVALISMHNCSLDAKIRVNLEAQVVETQAEAKKKPAEKKKTTSDGPKPKRLKKTNDEKKSSSTSNKPKRPLTAFFIFMSDFRKTFKSEHNGSLAKDAAKIGGEKWKSLTEEEKKVYLDKAAELKAEYNKSLESNDADEEEEDEEKQSDDVDDAEEKQVDDDDEVEEKEVENTDDDKKEAEGKEEEEEEILDDY
Protein: Global transcriptional regulator CodY (Q18BE1)
Organism: Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00621}.
Interaction partners:
- RNA polymerase factor sigma-70
- Stage 0 sporulation protein A homolog
- Transcriptional regulator, LacI family
- DNA topoisomerase 1
Sequence:
MASEVLQKTRKINKTLQTSGGSSVSFDLLAGALGDVLSSNVYVVSAKGKVLGLHLNDVQDSSVIEDEYTKQKKFSDEYTQNVLKIDETLENLNGEKILEIFPEEHGRLQKYTTVVPILGSGQRLGTLVLSRYSNSFNDDDLVIAEYSATVVGLEILRAIGEELEEEMRKKAVVQMAIGTLSYSELEAVEHIFAELDGKEGLLVASKIADRVGITRSVIVNALRKFESAGVIESRSLGMKGTHIRILNDKLTDELKKLKNNQ
Protein: MGC83926 protein (Nucleoporin 37kDa L homeolog) (Q66IZ6)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
- WD_REPEATS_REGION domain-containing protein.
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein
- Uncharacterized protein.
- Nuclear pore complex protein Nup133
- Protein SEC13 homolog
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup155
- Nucleoporin NUP53
- Nucleoporin NUP188
Sequence:
MKQDSASNATYTVDCEDYVHVVEFNPFDSGEAGSLLAYGGISYVVIASCRFQEEDSTVEGIEFKTLKTFHHGERVVAIAWSPETRCDALLPLLRFATAAGDKKIRIFTSDFQDKNEYKVIEGHSGYINDLVFCSPEGTDIASVGDDHTCRIWDLDGKQIAMFILRSPGMSVAWHPEGAFKLMVAEKTGTIRFYDLTTHQAILSLESVQVPLMSADWCVRNTLRIGAVAGNDWIIWEMPRSSYPQDNKPAHADRARMFRWSKCNENVFATTGYPGKMKSQIAIHHLAHPQPILIGTAPVGSGLSWHRRLPLCVVGGYRKLFFWLTEM
Protein: Acetolactate synthase, chloroplastic (AtALS) (EC 2.2.1.6) (Acetohydroxy-acid synthase) (Protein CHLORSULFURON RESISTANT 1) (P17597)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Acetolactate synthase small subunit 2, chloroplastic
- Acetolactate synthase small subunit 1, chloroplastic
- Ketol-acid reductoisomerase, chloroplastic
- Dihydroxy-acid dehydratase, chloroplastic
- Threonine dehydratase biosynthetic, chloroplastic
- 3-isopropylmalate dehydrogenase 2, chloroplastic
- 3-isopropylmalate dehydrogenase 3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
- 2-isopropylmalate synthase 2, chloroplastic
- NADP-dependent malic enzyme 4, chloroplastic
Sequence:
MAAATTTTTTSSSISFSTKPSPSSSKSPLPISRFSLPFSLNPNKSSSSSRRRGIKSSSPSSISAVLNTTTNVTTTPSPTKPTKPETFISRFAPDQPRKGADILVEALERQGVETVFAYPGGASMEIHQALTRSSSIRNVLPRHEQGGVFAAEGYARSSGKPGICIATSGPGATNLVSGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRIIEEAFFLATSGRPGPVLVDVPKDIQQQLAIPNWEQAMRLPGYMSRMPKPPEDSHLEQIVRLISESKKPVLYVGGGCLNSSDELGRFVELTGIPVASTLMGLGSYPCDDELSLHMLGMHGTVYANYAVEHSDLLLAFGVRFDDRVTGKLEAFASRAKIVHIDIDSAEIGKNKTPHVSVCGDVKLALQGMNKVLENRAEELKLDFGVWRNELNVQKQKFPLSFKTFGEAIPPQYAIKVLDELTDGKAIISTGVGQHQMWAAQFYNYKKPRQWLSSGGLGAMGFGLPAAIGASVANPDAIVVDIDGDGSFIMNVQELATIRVENLPVKVLLLNNQHLGMVMQWEDRFYKANRAHTFLGDPAQEDEIFPNMLLFAAACGIPAARVTKKADLREAIQTMLDTPGPYLLDVICPHQEHVLPMIPSGGTFNDVITEGDGRIKY
Protein: L-ornithine N(5)-monooxygenase (EC 1.14.13.195) (L-ornithine N(5)-hydroxylase) (Ornithine hydroxylase) (L-ornithine N(5)-oxygenase) (Pyoverdin biosynthesis protein A) (Q51548)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as pyoverdin. Pyoverdin is a hydroxamate siderophore composed of a 6,7-dihydroxyquinoline-containing fluorescent chromophore joined to the N-terminus of a partly cyclic octapeptide (D-Ser-L-Arg-D-Ser-L-N(5)-OH-Orn-L-Lys-L-N(5)-OH-Orn-L-Thr-L-Thr in strain PAO1). Specific for NADPH, which plays a role in stabilization of the C4a-hydroperoxyflavin intermediate.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:18757814}; Peripheral membrane protein {ECO:0000269|PubMed:18757814}; Cytoplasmic side {ECO:0000269|PubMed:18757814}.
Interaction partners:
- PvdJ
- phosphoribosylglycinamide formyltransferase 1
- Acyl-homoserine lactone acylase PvdQ
- Pyoverdine synthetase D
- PvdL
- L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, PvdH
- Pyoverdine biosynthesis protein PvdE
- Ferripyoverdine receptor
- MbtH-like domain-containing protein
- PvdO
Sequence:
MTQATATAVVHDLIGVGFGPSNIALAIALQERAQAQGALEVLFLDKQGDYRWHGNTLVSQSELQISFLKDLVSLRNPTSPYSFVNYLHKHDRLVDFINLGTFYPCRMEFNDYLRWVASHFQEQSRYGEEVLRIEPMLSAGQVEALRVISRNADGEELVRTTRALVVSPGGTPRIPQVFRALKGDGRVFHHSQYLEHMAKQPCSSGKPMKIAIIGGGQSAAEAFIDLNDSYPSVQADMILRASALKPADDSPFVNEVFAPKFTDLIYSREHAERERLLREYHNTNYSVVDTDLIERIYGVFYRQKVSGIPRHAFRCMTTVERATATAQGIELALRDAGSGELSVETYDAVILATGYERQLHRQLLEPLAEYLGDHEIGRDYRLQTDERCKVAIYAQGFSQASHGLSDTLLSVLPVRAEEISGSLYQHLKPGTAARALHEHALAS
Protein: AE binding protein 2 (F5GZR7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDVDSTISSGRSTPAMMNGQGSTTSSSKNIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGVFVCLWKGCKVYNTPSTSQSWLQRHMLTHSGDKPFKCVVGGCNASF
Protein: Neurotrophin-4 (NT-4) (Neurotrophin-5) (NT-5) (Neutrophic factor 4) (P34130)
Organism: Homo sapiens (Human)
Function: Target-derived survival factor for peripheral sensory sympathetic neurons.
Subcellular location: Secreted {ECO:0000269|PubMed:1742028}.
Interaction partners:
- BDNF/NT-3 growth factors receptor
- High affinity nerve growth factor receptor
- NT-3 growth factor receptor
- Tumor necrosis factor receptor superfamily member 16
- Neurotrophic factor BDNF precursor form
- Beta-nerve growth factor
- Glial cell line-derived neurotrophic factor
- Sortilin
- WD repeat-containing protein 36
- Epidermal growth factor receptor
Sequence:
MLPLPSCSLPILLLFLLPSVPIESQPPPSTLPPFLAPEWDLLSPRVVLSRGAPAGPPLLFLLEAGAFRESAGAPANRSRRGVSETAPASRRGELAVCDAVSGWVTDRRTAVDLRGREVEVLGEVPAAGGSPLRQYFFETRCKADNAEEGGPGAGGGGCRGVDRRHWVSECKAKQSYVRALTADAQGRVGWRWIRIDTACVCTLLSRTGRA
Protein: DNA primase (EC 2.7.7.-) (Q57XP3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA polymerase
- DNA primase large subunit
- DNA polymerase alpha subunit B
- DNA polymerase epsilon catalytic subunit
- DNA polymerase
- DNA polymerase II subunit 2
- Proliferating cell nuclear antigen
- Replication factor C, subunit 2, putative
- DNA polymerase
- DNA replication licensing factor MCM5
Sequence:
MIDETSLREFYEFVYPVDLVVQWLSYNLQHADKIISSPPGSVANGNDPKVLPSTGEDVTEGGRGSTSSADGYLARREFCFTLLGDIFTRFRSYSSVTELRRELIRSFPEKIDVGAVYNIRPNQKQKVGTIVPVERELVFDIDMSDYDNSRSCCTGKSICRWCWTWMSCAAAVLRKVLEDDFGFRYLFPVFSGRRGIHLWVCDKRACKMHDDERSALVSYLTVVVPKASQHAVVADFVNGKPIHPTIQHVQATVLDPAFTSLFLNSTPENPNRVTHPKGARIVYKAIVSALKMGTRRDVEQRFLRNVPFEEGNILDWTYVLRTLGDAATNVIAAAQILLMYPRLDEHVSTRRDHLLKLPFCVHPATGSLCCPLEWDNVPTFDPVSDPPKLQDMLLHRHMDEKWLAPLQRMLQEMGRDPAEER