wanglab/gogpt-training-data huggingface dataset:
Protein: Beclin 1-associated autophagy-related key regulator (Barkor) (Autophagy-related protein 14-like protein) (Atg14L) (Q8CDJ3)
Organism: Mus musculus (Mouse)
Function: Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 (By similarity). Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes (By similarity). Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1 (By similarity). Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation of PIK3C3 by AMPK. Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion (By similarity). Modulates the hepatic lipid metabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20639694}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20639694}; Peripheral membrane protein {ECO:0000305}. Preautophagosomal structure membrane {ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:20639694, ECO:0000269|PubMed:22863730}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein {ECO:0000305}. Note=Cytosolic under nutrient-rich conditions (PubMed:20639694). Following autophagy stimuli, such as starvation or rapamycin induction, predominantly detected in cytoplasmic foci, identified as isolation membranes and autophagosomes (PubMed:20639694). Accumulates on highly curved PtdIns(3)P enriched autophagic membrane via its BATS domain to sense and maintain membrane curvature (PubMed:21518905). Also localizes to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (PubMed:24089209). {ECO:0000269|PubMed:20639694, ECO:0000269|PubMed:21518905, ECO:0000269|PubMed:24089209}.
Interaction partners:
- Phosphoinositide 3-kinase regulatory subunit 4
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- UV radiation resistance-associated protein
- Syntaxin-17
- Beclin-1
- Nuclear receptor-binding factor 2
- RB1-inducible coiled-coil protein 1
- Activating molecule in BECN1-regulated autophagy protein 1
- Serine/threonine-protein kinase ULK1
- Synaptosomal-associated protein 29
Sequence:
MASPSGKGSWTPEAPGFGPRALARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLKSHYERLARLRRSHILELTSIIFPIDEVKTSGRDPADVSSETDSAMTSSMVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYNWVEEKKTTQGPDMEHNNPAYTISAALGYATQLVNIVSHILDINLPKKLCNSEFCGENLSKQKLTRAVRKLNANILYLCSSQHVNLDQLQPLHTLRNLMHLVSPRSEHLGRSGPFEVRADLEESMEFVDPGVAGESDASGDERVSDEETDLGTDWENLPSPRFCDIPSQPVEVSQSQSTQVSPPIASSSAGGMISSAAASVTSWFKAYTGHR
Protein: Uncharacterized fimbrial-like protein YfcQ (P76500)
Organism: Escherichia coli (strain K12)
Function: Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes.
Interaction partners:
- Uncharacterized protein YfcO
- Uncharacterized fimbrial-like protein YfcP
- Uncharacterized fimbrial-like protein YfcR
- Probable fimbrial chaperone YfcS
- Uncharacterized fimbrial-like protein YadN
Sequence:
MRKTFLTLLCVSSAIAHAADEDITFHGTLLSPPTCSISGGKTIEVEFRDLIIDDINGNYGRKEVPYELTCDSTTRHPDWEMTLTWTGTQTSFNDAAIETDVPGFGIELQHDGQRFKLNTPLAINATDFTQKPKLEAVPVKASDAVLSDTNFSAYATLRVDYQ
Protein: Tetraspanin-31 (Tspan-31) (Sarcoma-amplified sequence) (Q12999)
Organism: Homo sapiens (Human)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Leukocyte surface antigen CD53
Sequence:
MVCGGFACSKNALCALNVVYMLVSLLLIGVAAWGKGLGLVSSIHIIGGVIAVGVFLLLIAVAGLVGAVNHHQVLLFFYMIILGLVFIFQFVISCSCLAINRSKQTDVINASWWVMSNKTRDELERSFDCCGLFNLTTLYQQDYDFCTAICKSQSPTCQMCGEKFLKHSDEALKILGGVGLFFSFTEILGVWLAMRFRNQKDPRANPSAFL
Protein: Protein transport protein SEC9 (P40357)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of a SNARE complex that may be the effector of SEC4 function in exocytosis.
Interaction partners:
- Lethal
- Protein SSO1
- Exocyst complex component SEC6
- Synaptobrevin homolog 1
- Synaptobrevin homolog 2
- Protein SSO2
- Protein transport protein SEC22
- Protein MSO1
- Protein transport protein SEC1
- Alpha-soluble NSF attachment protein
Sequence:
MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR
Protein: DNA repair protein XRS2 (P33301)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: During meiosis is involved in homologous recombination and during vegetative growth it is necessary for DNA repair. It probably regulates the 5'-3' exonuclease degradation of double strand breaks either at the initiation stage or a later stage.
Subcellular location: Nucleus {ECO:0000269|PubMed:9845372}. Chromosome {ECO:0000250|UniProtKB:O43070}. Chromosome, telomere {ECO:0000250|UniProtKB:O43070}. Note=Localizes to DNA double-strand breaks (DSBs); recruited to DNA damage sites. {ECO:0000250|UniProtKB:O43070}.
Interaction partners:
- Double-strand break repair protein MRE11
- DNA repair protein RAD50
- DNA endonuclease SAE2
- Serine/threonine-protein kinase TEL1
- ATP-dependent DNA helicase SRS2
- Serine/threonine-protein kinase MEC1
- Non-homologous end-joining factor LIF1
- Telomere length regulation protein ELG1
- Guanine nucleotide-binding protein subunit beta
- Flap endonuclease 1
Sequence:
MWVVRYQNTLEDGSISFISCCLQAFKTYSIGRSSKNPLIIKNDKSISRQHITFKWEINNSSDLKHSSLCLVNKGKLTSLNKKFMKVGETFTINASDVLKSTIIELGTTPIRIEFEWINEVWNIPPHLTQFRTMLSEYGISTEISINDIPANLMISDYPKSEDNSIRELYALVSTIPMKKSRFLMELCNTLLPTSKTNLKFDEMWNDMISNPEYNVFDFDPNILLSKFMRLNNIRVLTTIKSEPRLSSLLRTFNINLFAFDNIDSLYKYVDSLEASTEYLILTTTDKKENGKILCTIKTMLTSIIDGTLSAVINMKGASSRTLDNGKFDQISEGMSTILKTSRAPEVEASPVVSKKRKLNRRRVLPLDSLDFFAGGLSTKTLSENRSLTDAKRLNCGAESKTVISSPNIAEADEKHAPFLQNALKPTEDIGKKSGHSSPGAIIVSSPNLGTVNTSEDSLDKSLQSHKLPQPSLPEVAGIGSQTISSNSADYETAAVNSMDDAEVTKNFRVNHHQNIEQPSKNIRKLSNYSREISSPLQENCKSPVKELSIKEKSGTPHAFVEAIQETKNREVKRVKSTIVELKDEELSEEAINQLKNLAIVEPSNNLLRKSFDSEGNKTSRTTEKWENSLMEPEWHKRKNFKTFVKVRPKSKAHKEEGKNNTQSSDFIRNAAFLITRNYVPLKKYSKKDTTTKWGTEENEDMFALTEMERFGSNTFMSDNINSNTIQKRSQALNRFTNEDSSNEGEEDSFSFSRCSGTAASVQPLKNKIFITDEDDLGDIDDKSDRLNHRENNRNLFVVKEMNLRPNLSEECSKQSRHSRSATSRSRGSFGASNNGDGDDDDDDGPKFTFKRRKG
Protein: Protein EMBRYO SAC DEVELOPMENT ARREST 30 (EC 2.4.1.-) (O-fucosyltransferase 22) (O-FucT-22) (O-fucosyltransferase family protein) (Protein TUBE GROWTH DEFECTIVE 1) (F4J2C8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVFKSRIKWIALFVLILSMGSLVVHLSMTKSSGVQLAYSARDNLWQDFDSLLGAQDFRNKHLWRPVKSLETLQPYANPRNSYPAPSSKNNGFIYAKIFGGFDKIRSSICDLVTISRLLNATLVIPELQESLRSKGISNKFKSFSYLYDEEQFIAFLKNDVIVMKTLPESLKAARKRNEFPLFKPKNSASPKFYLEDVLPKLKKANVIGLIVSDGGCLQSALPASMPELQRLRCRVAFHALQLRPEIQVLAKEMVDRLRKSGQPFLAYHPGLVREKLAYHGCAELFQDIHSELIQYRRAQMIKQRFILEELIVDSRLRRDNGLCPLMPEEVGILLKALGYSQKAIIYLAGSEIFGGQRVLIPLRAMFPNLVDRTSLCSTEELSELVGPETPLPENTYKMPPRKSDKQLKEEWNKAGPRPRPLPPPPDRPIYQHEKEGWYGWLTENDTEPSPSPMDLRNQAHRLLWDALDFAVSVEADVFFPGFNNDGSGWPDFSSLVMGQRLYERPSSRTYRLDRKVIQELFNITREDMYHPNRNWTLRVRKHLNSSLGESGLIRQSMLSKPRSFLSHPLPECSCRTSALEDSRQIQSDDGRFLYGGEDECPKWIKSAGVEKSKTDDGDQPDYDHDLLAEQSETEEEFAKSKVASAFDQDEEWDPND
Protein: Tenascin-X (Q62308)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
EFDSFLVQYKNRGGQVQVVPAAADQREVTISSLEPNRKYRFLLFGLIGLKRLGPVSVEGTTAPVEKTPQPRLGELSVTEETSDSMHLSWSVAQGPFDSFLVQYKDRDGQLQTVSLAADQREVTIEGLQPGRKYKFLLYGLTGGKRLGGISALGVTASEVDISAPDHTEPPHAPGLGTLAVTEATPDSLRLSWAVARGPFDSFVVQYQDTENETQALLVDGDQDKVLISGLEPKTSYKFFLYGLREGTRHGPVSVEGTTDPVPAGQGPGDPGPRLSQLSVSDVTTSSLRLNWEAPLGDFDSFQLRFGVPLLSTLEQNPRTLQQRELMVPGVRPSAMLRDLRPGTLYSLTLYGLRGPHKADSIQGTARTLSPVLESPRDLQFSDIGETSAKVKWVPPTSRVDSFKISYQLADGGEPQSVQVDGRTQTQILQGLIPDTRYEVTVVSVRGFEESEPLTGFLTTVPDGPTQLRALNLTDGSALLHWKPPHKPVDKYDVEVESPGAPPLQASAPGSAVDYPLTDLALDTNYTATVRGLRGPNFTSPASITFTTGLKPPQDLEAKEVTPRTALLTWTEPEVPPTGYLLSFDTPGGQIQEILLPAGTTSHRLLRLFPSTFYSAQLRAIWGESLTPPVLTSFTTGGQRIPFPRDCGEELKNGPSASKTTTIFLNGNRERPLDVFCDMETDGGGWLVFQRRMDGQTDFWRDWEEYAHGFGNISGEFWLGNEALHSLTQAGDYSLRVDLRAGKEAVFAQYDFFRVDSAKENYRLHLEGYHGTAGDSMSYHSGSVFSARDRDPNNLLISCAVSYRGAWWYRNCHYANLNGLYGSTVDHQGVSWYHWKGFEFSVPFTEMKLRPRNFQVPTRGT
Protein: Endoplasmic reticulum membrane sensor NFE2L1 (Nuclear factor erythroid 2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) (B4DYE1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004643}; Single-pass type III membrane protein {ECO:0000256|ARBA:ARBA00004643}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGWESHLTAASADIDLIDILWRQDIDLGAGREVFDYSHRQKEQDVEKELRDGGEQDTWAGEGAEALARNLLVDGETGESFPAQFPADISSITEAVPSESEPPALQNNLLSPLLTGTESPFDLEQQWQDLMSIMEMQAMEVNTSASEILYSAPPGDPLSTNYSLAPNTPINQNVSLHQASLGGCSQDFLLFSPEVESLPVASSSTLLPLAPSNSTSLNSTFGSTNLTGLFFPPQLNGTANDTAGPELPDPLGGLLDEAMLDEISLMDLAIEEGFNPVQASQLEEEFDSDSGLSLDSSHSPSSLSSSEGSSSSSSSSSSSSSSASSSASSSFSEEGAVGYSSDSETLDLEEAEGAVGYQPEYSKFCRMSYQDPAQLSCLPYLEHVGHNHTYNMAPSALDSADLPPPSALKKGSKEKQADFLDKQMSRDEHRARAMKIPFTNDKIINLPVEEFNELLSKYQLSEAQLSLIRDIRRRGKNKMAAQNCRKRKLDTILNLERDVEDLQRDKARLLREKVEFLRSLRQMKQKVQSLYQEVFGRLRDENGRPYSPSQYALQYAGDGSVLLIPRTMADQQARRQERKPKDRRK
Protein: Heparanase (EC 3.2.1.166) (Endo-glucoronidase) [Cleaved into: Heparanase 8 kDa subunit; Heparanase 50 kDa subunit] (Q71RP1)
Organism: Rattus norvegicus (Rat)
Function: Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000250}. Nucleus {ECO:0000250}. Note=Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium. Associates with lipid rafts (By similarity). {ECO:0000250}.
Interaction partners:
- Syndecan-1
- Uncharacterized protein.
Sequence:
MLRPLLLLWLWGRLGALTQGTPAGTAPTKDVVDLEFYTKRLFQSVSPSFLSITIDASLATDPRFLTFLGSPRLRALARGLSPAYLRFGGTKTDFLIFDPNKEPTSEERSYWQSQDNNDICGSERVSADVLRKLQMEWPFQELLLLREQYQREFKNSTYSRSSVDMLYSFAKCSRLDLIFGLNALLRTPDLRWNSSNAQLLLNYCSSKGYNISWELGNEPNSFWKKAHISIDGLQLGEDFVELHKLLQKSAFQNAKLYGPDIGQPRGKTVKLLRSFLKAGGEVIDSLTWHHYYLNGRVATKEDFLSSDVLDTFILSVQKILKVTKEMTPGKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLGLSAQLGIEVVMRQVFFGAGNYHLVDENFEPLPDYWLSLLFKKLVGPKVLMSRVKGPDRSKLRVYLHCTNVYHPRYREGDLTLYVLNLHNVTKHLKLPPPMFSRPVDKYLLKPFGSDGLLSKSVQLNGQTLKMVDEQTLPALTEKPLPAGSSLSVPAFSYGFFVIRNAKIAACI
Protein: M-phase inducer phosphatase cdc-25.1 (EC 3.1.3.48) (Cell division cycle-related protein 25.1) (O44552)
Organism: Caenorhabditis elegans
Interaction partners:
- G1/S-specific cyclin-E
- Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase wee-1.3
- Cyclin-dependent kinase 1
- G2/mitotic-specific cyclin-B1
- G2/mitotic-specific cyclin-B
- F-box/WD repeat-containing protein lin-23
- Cyclin N-terminal domain-containing protein
- Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase wee-1.1
- Cyclin-dependent kinase 2
- Serine/threonine-protein kinase chk-1
Sequence:
MATTGEKAIYEDQNNVNIIENVVDVANGINESPKTLFEEDGSSRDSGVSMTSCSDKSDASPEEDVDFSKLESGRVALTDCSNFVSILQRNSSVSSSRSSSFYNYDTPTGRKMKTVFDLDSLDHSEYEKRVMSERPTDNHRKRTSSSMSPSVTLLDRKRSRNLSLVAPQSDKSCRYNGLNNPRDDPFGDEDDEVFEQSNVRNSQVQNTSIFAQPAPRTATSLWDLAPPMFFERKTSDTSGNGSFQERPKQILRAMSVGEIDSELPPTLEVKYTLPGVDNPQRESQAFRSISPTTLLLEFQRLGDDFDKKYIIVDCRFPFEYKGGHVKGAINLFRHDKIKPIFFPENGEASSFQNRVPIFYCEYSQKRGPTMAHAVRSIDRVLNELRYPHVEYPEMYLLDYGYKSLWSTAECRQICEPCSYIPMTHSSFSMEFKSARLERHHSMASLKPNGETSHREEKKKRCTRSVIRRNNSSLNMLSRSSSALTSTGSKTSSMENILYGLDDERRPKWVSAFDIQSTESENDLDAALIYQRNISSNASNASSIVNLAEERIVQLGLQVITPDFPDRPSESSSTTPAGEHLPLGEGGHQIPCGILDFSSISDDAE
Protein: Uncharacterized protein (Q3V133)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMLLGEAGAAEKTPGGADGTRTRADGVAKEGAGGAGPDGAPEARAKPTVRVRLEDRFNSMPAEPPAPRGAEPAESGVALNNLVTLIRHPSELMNVPLHQQQNKCTTLVKNKTAAATTALQFTYPLFTSACSTGGNASLAQTQSSSNSCSILEAAKHQDIGLPRAFSFCYQQEIESTKQTGGSRNKALPEQVWIKVGEEALCKQAINKRNRSRIRQLDTSVERRALGEIQNVGEGSSTSQGTWQSSESSQSNLGEQTQSGPQGGRSQRRERHNRMERDRR
Protein: V-type proton ATPase subunit G (A0A8I6B3N3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MASQSQGIQQLLQAEKRAAEKVSEARKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETQEKMTILQNYFEQNRDEVLDNLLAFVCDIRPEIHENYRING
Protein: Fused isobutyryl-CoA mutase [Includes: Isobutyryl-CoA mutase (ICM) (EC 5.4.99.13); P-loop GTPase (EC 3.6.5.-) (G-protein chaperone)] (Q5KUG0)
Organism: Geobacillus kaustophilus (strain HTA426)
Function: Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, and to a lesser extent, of pivalyl-CoA and isovaleryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly. Also displays ATPase activity. Is not able to convert 3-hydroxybutyryl-CoA to 2-hydroxyisobutyryl-CoA. Does not exhibit methylmalonyl-CoA mutase (MCM) activity.
Interaction partners:
- methylmalonyl-CoA mutase
- methylmalonyl-CoA mutase
- Hypothetical conserved protein
- Transcriptional regulator
- Lactoylglutathione lyase
Sequence:
MAHIYRPKHHVRFVTASSLFDGHDASINIMRRILQASGAEVIHLGHNRSVEEIVNAAIQEDVQGIAVSSYQGGHMEFFKYMYDLLQERGASHIRIYGGGGGVIIPREIKELHEYGIARIFSPEDGRRLGLQGMINVMLEECDFPTVTVVTDELERLPSGDVQAIARLITLCEYRAEGENKEAAAAAEAAIEQVKALEKRVPVLGITGTGGAGKSSLTDELVRRFLNEIPDIKIAILSVDPTKQKTGGALLGDRIRMNSINSPRVYMRSLATRHSRTELSPAIRDAISVVKAAGFDLVIIETSGIGQGDAAITEVCDVSMYVMTSEFGAPTQLEKIDMIDYADLIVINKFERKGSEDAKRQVQKQYQRSHQLFDRDVSEMPVYGTIASQFNDPGTNTLFVALVDTINKKAGTNWKTSLKTVANVEKHNVIIPNERRYYLREIAETVRSYHRRAEQQVEVARRLFQIEGAIEAAKERGEAEDVIRALETLKADYEAKLTPESKRILATWEETKAKYAAKQFVTKVRDKEIVTELTTKTLSGLDIPKVVLPKFKDYGEILRWVYKENVPGSFPYTAGVFPFKRQGEDPKRQFAGEGTPERTNRRFHYLCKEDKAKRLSTAFDSVTLYGEDPDYRPDIFGKVGESGVSVCTLDDMKKLYKGFDLCDPLTSVSMTINGPAPILLAMFMNTAIDQQVEKKEAELGRPLTPEEYEQVKEWTLQTVRGTVQADILKEDQGQNTCIFSTDFALKMMGDIQEYFIKHRVRNYYSVSISGYHIAEAGANPITQLAFTLANGFTYVEYYLSRGMHIDDFAPNLSFFFSNGLDPEYSVIGRVARRIWAIVMREKYGANERSQKLKYHIQTSGRSLHAQEIDFNDIRTTLQALLAIYDNCNSLHTNAYDEAITTPTEESVRRAMAIQLIITKEFGLTKNENPLQGSFIIEELTDLVEEAVLQEFERLNDRGGVLGAMEMQYQRGKIQDESLYYETKKHTGELPIIGVNTFLNPNPPSEDELNNIQLARATYEEKETQIRNLREFQERNKDKAGPALERLKQVATSGGNIFEELMETVKVASLGQITRALYEVGGQYRRNM
Protein: Methionine adenosyltransferase 2 subunit beta (Methionine adenosyltransferase II beta) (MAT II beta) (Q99LB6)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine. Can bind NADP (in vitro).
Interaction partners:
- S-adenosylmethionine synthase isoform type-2
- S-adenosylmethionine synthase isoform type-1
- Betaine--homocysteine S-methyltransferase 1
- Methionine synthase
- DNA
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- DNA
- S-adenosylmethionine decarboxylase proenzyme 1
- S-adenosylmethionine decarboxylase proenzyme 2
- DNA
Sequence:
MVGREKELSIHFVPGCCQLVEEEVNIPSRRVLITGATGLLGRAVYKEFQQSNWHTVGCGFRRARPKFEQVNLLDSEAVHHLIHDFQPHVIVHCAAERRPDVVESQPDAASQLNVGASGNLAKEAAAIGAFLIYISSDYVFDGTNPPYTEEDIPSPLNLYGKTKLDGEKAVLENNLGAAVLRIPVLYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVASVCRQLAEKRMLDPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVIGAQRPKNAQLDCSKLETLGIGQRTPFRTGIKESLWPFLIDKRWRQTVFH
Protein: Uncharacterized protein (Q57WG1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- KOW domain-containing protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- LIM zinc-binding domain-containing protein
- EngB-type G domain-containing protein
- 39S ribosomal protein L28
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
Sequence:
MLFRSVSCKNYQRGGWSPGSKHQKHMTLNPTLYLYRFPGPHGPGPYTMKYWWTLGCFPTGMEVPFRLHEFLSTYQQEHVPVEVEEWLRCYIKDPLSELVNASNDFFKAVEVYPEVESARGYKTLQPSIAPLLVPMKKFEEQLGVKISPVGLRSVLSNPVLKDRFLDDLFDYKSYVEKGGSTPHRRLARSRFEGSLSVLGECEKCLPEQHQVEISESLGTFIGATVSPAETTADDERSLILLLTTISEGCINAGNYSDAASVLADALMFCHDPDSQATTHANISFASLLNADFKGAEYNGREAALLQPQVKPTSTACARGYVGWAAAAAYQDDFEKAEAIVKDGLTLYVGNEHLEKLANKLQALREEQPSVYKQVPRSLRESRSHLPSQQSRGLLSGSGKGFSNEFDWVEFKNKLYPSKMDPRNNEMGSVFRRVGDLGSFISTSRSMERL
Protein: 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase (EC 2.3.1.317) (3-dehydrocarnitine cleavage enzyme) (Q9HTH7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- L-carnitine dehydrogenase
- Betainyl-CoA thioesterase
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- Probable lipolytic enzyme
- HTH-type transcriptional regulator CdhR
- HTH-type transcriptional regulator BetI
- NAD/NADP-dependent betaine aldehyde dehydrogenase
Sequence:
MNHEVIVTCAVTGAGDTVGRHPAIPVTPKQIAEAAIEAARAGATVAHCHVRDPATGKPSRDVALYREVVERIRESDTDVIINLTAGMGGDLEIGKGEQPLEFGAGTDLVGPLERLRHVEELLPEICTLDCGTLNFGDGDYIYVSTPAQLRAGARRITELGVKAELEIFDTGHLWFAKQMLKEGLLEDPLFQICLGIPWGAPADTTTMKAMADNLPPGATWAGFGIGRTQMPMVAQAMLLGGNVRVGLEDNIWLDKGVPASNGSLVERAIEIIERLGGRALSPAEGRRRMNLKPR
Protein: (thale cress) hypothetical protein (A0A178V0I5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLAIFHEAFAHPPEELNSPASEKCSKQPKLPEETLNDFLLRYPLNTFSMSFGQAAVLAYVRPSASFSIHQRLFCGFDDIYCLFFGSLNNLCQLNKQYGLTKTTNEAMFVIEAYRTLRDRGPYPADQVVKDLDGSFSFVVYDSKAGSVFTALGSDGGVKLYWGIAADGSVVISDDLDVIKEGCAKSFAPFPTGCMFHSEGGLMSFEHPMNKIKAMPRVDSEGVLCGANFKVDVYNRVNSIPRRGSEANWSL
Protein: Leucine aminopeptidase 1 (EC 3.4.11.1) (Leucyl aminopeptidase 1) (AtLAP1) (Proline aminopeptidase 1) (EC 3.4.11.5) (Prolyl aminopeptidase 1) (P30184)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (Probable). Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Possesses Cys-Gly dipeptidase activity. In addition, can cleave Cys-Leu and Leu-Cys dipeptides.
Subcellular location: Cytoplasm.
Interaction partners:
- Gamma-glutamylcyclotransferase 2-2
- Gamma-glutamylcyclotransferase 2-3
- Puromycin-sensitive aminopeptidase
- Gamma-glutamylcyclotransferase 2-1
- Glutathione hydrolase 2
- Glutathione hydrolase 3
- Glutathione hydrolase 1
- Putative inactive glutathione hydrolase 4
- Glutathione synthetase, chloroplastic
- Glutamate--cysteine ligase, chloroplastic
Sequence:
MAHTLGLTQPNSTEPHKISFTAKEIDVIEWKGDILVVGVTEKDLAKDGNSKFENPILSKVDAHLSGLLAQVSSEEDFTGKPGQSTVLRLPGLGSKRIALIGLGQSVSSPVAFHSLGEAVATVSKASQSTSAAIVLASSVSDESKLSSVSALASGIVLGLFEDGRYKSESKKPSLKAVDIIGFGTGAEVEKKLKYAEDVSYGVIFGRELINSPANVLTPAVLAEEAAKVASTYSDVFTANILNEEQCKELKMGSYLAVAAASANPPHFIHLVYKPPNGSVKTKLALVGKGLTFDSGGYNIKTGPGCSIELMKFDMGGSAAVLGAAKAIGEIKPPGVEVHFIVAACENMISGTGMRPGDVITASNGKTIEVNNTDAEGRLTLADALVYACNQGVDKIVDLATLTGACVIALGTSMAGIYTPSDELAKEVIAASERSGEKLWRMPLEESYWEMMKSGVADMVNTGGRAGGSITAALFLKQFVSEKVQWMHIDMAGPVWNEKKKSGTGFGVATLVEWVQKNSSS
Protein: ATP-dependent RNA helicase DDX25 (EC 3.6.4.13) (DEAD box protein 25) (Gonadotropin-regulated testicular RNA helicase) (Q9UHL0)
Organism: Homo sapiens (Human)
Function: ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10608860}. Nucleus {ECO:0000250|UniProtKB:Q9QY15}. Note=Detected in both cytoplasm and nucleus of testicular cells. Also detected in chromatoid bodies of round spermatids (By similarity). {ECO:0000250|UniProtKB:Q9QY15}.
Interaction partners:
- Centriolar and ciliogenesis-associated protein HYLS1
- Homeobox protein PKNOX2
- mRNA export factor GLE1
- Nuclear pore complex protein Nup214
- ATP-dependent RNA helicase DDX19A
- Tudor domain-containing protein 6
Sequence:
MASLLWGGDAGAAESERLNSHFSNLSQPRKNLWGIKSTAVRNIDGSINNINEDDEEDVVDLAANSLLNKLIHQSLVESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVEQMGKFCVDVQVMYAIRGNRIPRGTDITKQIIIGTPGTVLDWCFKLKLIDLTKIRVFVLDEADVMIDTQGFSDHSIRIQRALPSECQMLLFSATFEDSVWHFAERIIPDPNVIKLRKEELTLNNIRQYYVLCEHRKDKYQALCNIYGSITIGQAIIFCQTRRNAKWLTVEMIQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVKQGEEPDYETYLHRIGRTGRFGKKGLAFNMIEVDELPSLMKIQDHFNSSIKQLNAEDMDEIEKIDY