wanglab/gogpt-training-data huggingface dataset:
Protein: von Hippel-Lindau disease tumor suppressor (pVHL) (P40338)
Organism: Mus musculus (Mouse)
Function: Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Seems to act as a target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia-inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P40337}. Cell membrane {ECO:0000250|UniProtKB:P40337}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40337}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P40337}. Nucleus {ECO:0000250|UniProtKB:P40337}. Note=Found predominantly in the cytoplasm and with less amounts nuclear or membrane-associated. Colocalizes with ADRB2 at the cell membrane. {ECO:0000250|UniProtKB:P40337}.
Interaction partners:
- Elongin-C
- Cullin-2
- Hypoxia-inducible factor 1-alpha
- E3 ubiquitin-protein ligase RBX1
- Elongin-B
- Endothelial PAS domain-containing protein 1
- Egl nine homolog 1
- Hypoxia-inducible factor 3-alpha
- Ankyrin repeat and SOCS box protein 4
- Prolyl hydroxylase EGLN3
Sequence:
MPRKAASPEEAAGEPGPEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPLWLNFDGEPQPYPILPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDYPSVRKDIQRLSQEHLESQHLEEEP
Protein: Photosynthetic NDH subunit of lumenal location 3, chloroplastic (PsbQ-like protein 2) (Q9SGH4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (Probable). Required for both formation and activity of the chloroplast NAD(P)H dehydrogenase (NDH) complex.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20460499}; Peripheral membrane protein {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20460499}; Lumenal side {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20460499}. Note=Associated with the chloroplast NAD(P)H dehydrogenase/photosystem I (NDH/PSI) supercomplex.
Interaction partners:
- Photosynthetic NDH subunit of lumenal location 2, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 6, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
- Photosynthetic NDH subunit of lumenal location 1, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 5, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 5, chloroplastic
- Photosystem I iron-sulfur center
- Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
Sequence:
MAHFIDLNSLTNTLPSLPKLPESRKTGKSSGFACRRTEEFQEPDSVQITRRMTLGFAVSIGLTGILGENNVSLAQDNGFWIDGPLPIPPIYNNIVNEKTGTRTFIKKGVYVADIGTKGRMYRVKKNAFDLLAMEDLIGPDTLNYVKKYLRLKSTFLFYDFDNLISAAASEDKQPLTDLANRLFDNFEKLEDAAKTKNLAETESCYKDTKFLLQEVMTRMA
Protein: Negative regulator of flagellin synthesis (Anti-sigma-28 factor) (Q9HYP5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- RNA polymerase sigma factor FliA
- Flagellar secretion chaperone FliSB
- Flagellar protein FlgN
- B-type flagellar hook-associated protein 2
- Flagellar hook-associated protein 1
- B-type flagellin
- Flagellar basal body rod protein FlgB
- Probable chemotaxis protein
- Flagella basal body P-ring formation protein FlgA
- STAS domain-containing protein
Sequence:
MVIDFNRLNPGSTPATTGRTGSTAAGRPDATGADKAGQAATSAPKSGESVQISETAQNMQKVTDQLQTLPVVDNDKVARIKQAIADGTYQVDSERVASKLLDFESQR
Protein: C3 and PZP-like alpha-2-macroglobulin domain-containing protein 8 (Q8IZJ3)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305|PubMed:15177561}. Cell membrane {ECO:0000269|PubMed:15177561}; Peripheral membrane protein {ECO:0000269|PubMed:15177561}; Extracellular side {ECO:0000269|PubMed:15177561}.
Interaction partners:
Sequence:
MSGALLWPLLPLLLLLLSARDGVRAAQPQAPGYLIAAPSVFRAGVEEVISVTIFNSPREVTVQAQLVAQGEPVVQSQGAILDKGTIKLKVPTGLRGQALLKVWGRGWQAEEGPLFHNQTSVTVDGRGASVFIQTDKPVYRPQHRVLISIFTVSPNLRPVNEKLEAYILDPRGSRMIEWRHLKPFCCGITNMSFPLSDQPVLGEWFIFVEMQGHAYNKSFEVQKYVLPKFELLIDPPRYIQDLDACETGTVRARYTFGKPVAGALMINMTVNGVGYYSHEVGRPVLRTTKILGSRDFDICVRDMIPADVPEHFRGRVSIWAMVTSVDGSQQVAFDDSTPVQRQLVDIRYSKDTRKQFKPGLAYVGKVELSYPDGSPAEGVTVQIKAELTPKDNIYTSEVVSQRGLVGFEIPSIPTSAQHVWLETKVMALNGKPVGAQYLPSYLSLGSWYSPSQCYLQLQPPSHPLQVGEEAYFSVKSTCPCNFTLYYEVAARGNIVLSGQQPAHTTQQRSKRAAPALEKPIRLTHLSETEPPPAPEAEVDVCVTSLHLAVTPSMVPLGRLLVFYVRENGEGVADSLQFAVETFFENQVSVTYSANETQPGEVVDLRIRAARGSCVCVAAVDKSVYLLRSGFRLTPAQVFQELEDYDVSDSFGVSREDGPFWWAGLTAQRRRRSSVFPWPWGITKDSGFAFTETGLVVMTDRVSLNHRQDGGLYTDEAVPAFQPHTGSLVAVAPSRHPPRTEKRKRTFFPETWIWHCLNISDPSGEGTLSVKVPDSITSWVGEAVALSTSQGLGIAEPSLLKTFKPFFVDFMLPALIIRGEQVKIPLSVYNYMGTCAEVYMKLSVPKGIQFVGHPGKRHVTKKMCVAPGEAEPIWVVLSFSDLGLNNITAKALAYGDTNCCRDGRSSKHPEENHADRRVPIGVDHVRRSVMVEAEGVPRAYTYSAFFCPSERVHISTPNKYEFQYVQRPLRLTRFDVAVRAHNDARVALSSGPQDTAGMIEIVLGGHQNTRSWISTSKMGEPVASAHTAKILSWDEFRTFWISWRGGLIQVGHGPEPSNESVIVAWTLPRPPEVQFIGFSTGWGSMGEFRIWRKMEVDESYSEAFTLGVPHGAIPGSERATASIIGDVMGPTLNHLNNLLRLPFGCGEQNMIHFAPNVFVLKYLQKTQQLSPEVERETTDYLVQGYQRQLTYKRQDGSYSAFGERDASGSMWLTAFVLKSFAQARSFIFVDPRELAAAKSWIIQQQQADGSFLAVGRVLNKDIQGGIHGTVPLTAYVVVALLETGTASEEERGSTDKARHFLESAAPLAMDPYSCALTTYALTLLRSPAAPEALRKLRSLAIMRDGVTHWSLSNSWDVDKGTFLSFSDRVSQSVVSAEVEMTAYALLTYTLLGDVAAALPVVKWLSQQRNALGGFSSTQDTCVALQALAEYAILSYAGGINLTVSLASTNLDYQETFELHRTNQKVLQTAAIPSLPTGLFVSAKGDGCCLMQIDVTYNVPDPVAKPAFQLLVSLQEPEAQGRPPPMPASAAEGSRGDWPPADDDDPAADQHHQEYKVMLEVCTRWLHAGSSNMAVLEVPLLSGFRADIESLEQLLLDKHMGMKRYEVAGRRVLFYFDEIPSRCLTCVRFRALRECVVGRTSALPVSVYDYYEPAFEATRFYNVSTHSPLARELCAGPACNEVERAPARGPGWFPGESGPAVAPEEGAAIARCGCDHDCGAQGNPVCGSDGVVYASACRLREAACRQAAPLEPAPPSCCALEQRLPASSSSTYGDDLASVAPGPLQQDVKLNGAGLEVEDSDPEPEGEAEDRVTAGPRPPVSSGNLESSTQSASPFHRWGQTPAPQRHSGRVVGAHRPGLLSPVFVYSPAFQSGGEEGLWMSNTCTLR
Protein: Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Protein ST2) (Q01638)
Organism: Homo sapiens (Human)
Function: Receptor for interleukin-33 (IL-33); signaling requires association of the coreceptor IL1RAP. Its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function (Probable). Upon tissue injury, induces UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity).
Subcellular location: [Isoform C]: Cell membrane.; SUBCELLULAR LOCATION: [Isoform B]: Secreted.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11478810}; Single-pass type I membrane protein {ECO:0000269|PubMed:11478810}.
Interaction partners:
- Interleukin-1 receptor accessory protein
- Interleukin-33
- Myeloid differentiation primary response protein MyD88
- Interleukin-1 receptor type 1
- Interleukin-1 receptor-associated kinase 1
- Interleukin-1 beta
- Interleukin-13
- Transmembrane emp24 domain-containing protein 1
- Interleukin-1 receptor-associated kinase 4
- Interleukin-1 alpha
Sequence:
MGFWILAILTILMYSTAAKFSKQSWGLENEALIVRCPRQGKPSYTVDWYYSQTNKSIPTQERNRVFASGQLLKFLPAAVADSGIYTCIVRSPTFNRTGYANVTIYKKQSDCNVPDYLMYSTVSGSEKNSKIYCPTIDLYNWTAPLEWFKNCQALQGSRYRAHKSFLVIDNVMTEDAGDYTCKFIHNENGANYSVTATRSFTVKDEQGFSLFPVIGAPAQNEIKEVEIGKNANLTCSACFGKGTQFLAAVLWQLNGTKITDFGEPRIQQEEGQNQSFSNGLACLDMVLRIADVKEEDLLLQYDCLALNLHGLRRHTVRLSRKNPIDHHSIYCIIAVCSVFLMLINVLVIILKMFWIEATLLWRDIAKPYKTRNDGKLYDAYVVYPRNYKSSTDGASRVEHFVHQILPDVLENKCGYTLCIYGRDMLPGEDVVTAVETNIRKSRRHIFILTPQITHNKEFAYEQEVALHCALIQNDAKVILIEMEALSELDMLQAEALQDSLQHLMKVQGTIKWREDHIANKRSLNSKFWKHVRYQMPVPSKIPRKASSLTPLAAQKQ
Protein: Peptidyl-Asp metalloendopeptidase (EC 3.4.24.33) (Biofilm-associated metzincin protease) (Metalloendopeptidase Mep72) (Q9I060)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Metalloprotease with endopeptidase activity. Specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues (By similarity). Mep72 appears to be a secreted biofilm-specific regulator that affects the processing of a very specific subset of virulence factors exported by the type III secretion machinery as well as flagellar proteins. Binds directly to ExoS and PcrV and affects the processing of these proteins in the biofilm secretome, but contrary to expectation, Mep72 seems to protect these targets against proteolytic processing/degradation.
Subcellular location: Secreted {ECO:0000269|PubMed:24279383, ECO:0000269|PubMed:25488299}. Note=Is secreted through the type II general secretory pathway (Xcp system) and undergoes processing during export. {ECO:0000269|PubMed:25488299}.
Interaction partners:
- Biofilm-associated metzincin protease inhibitor
- Uncharacterized protein
- DUF2975 domain-containing protein
- DNA translocase FtsK
Sequence:
MKKSLLCSTLALAVASAAQAAPKTVDIMVLYTPAATQTANGRDIDARIASYIEFANTAYEKSGVNLRLRLVHKQRLDWADYPTVTGANLDRFMRDPQVQRLREQYGADLVSLVNRSQNSGNGYITCGIGYMGSGDKNSGRFHGNAKDIAYNLTGVDCGLNTFAHEAGHNMGLRHSYEQDLESSYYDPRYAHSGTYEWSRGYGVQGRFATVMAYPHAFGTNKQAPFFANPRLVNAECANQPCGREEHADAVRALNSMATQIADFRPTKVPGTVNPGSGGDTPTPPDLPWCTKAKLGGLLGDGEFASMEGWRAWSGNAQLSLVNVAKGCRDNALLVDVRGFDLLVRPIAPLRAGSGYRLSGKVMLKAANTRETVRMALLSERADGALAYNPAQSVELSVSGNEFSRLEKTFDYRPAADQRNLYVAVWSDSGASLLVDEMNLQEAQAAPPSVPPAPKRIAYDFESGIGGWSGVHASARATRVASAGRLALEAYQRRYAGTGASTSLLGNLEAGRTYAFSADVRVGDGRGSQAMTYAYLYLESQGRPGEYLPLGYKVVENGRWASLRGQVQLPKGPIKRAELMILSGNQQESMFIDNVQLLQK
Protein: Solute carrier organic anion transporter family member 1C1 (BBB-specific anion transporter type 1) (BAST1) (Blood-brain barrier-specific anion transporter 1) (Organic anion transporter 1C1) (OATP1C1) (Organic anion-transporting polypeptide 14) (OATP-14) (Solute carrier family 21 member 14) (Thyroxine transporter) (Q9EPZ7)
Organism: Rattus norvegicus (Rat)
Function: Mediates the Na(+)-independent high affinity transport of thyroid hormones at the plasma membrane of brain capillary endothelial cells. The transport activity of substrates L-thyroxine (T4) and 3,3',5'-triiodo-L-thyronine (reverse T3, rT3) is much greater than that of 3,3',5-triiodo-L-thyronine (T3). The prehormone, T4, is the major form in the circulating blood and is converted to the active form, T3, by the iodothyronine-deiodinase in peripheral organs. T3 plays an essential role in brain development via binding to specific nuclear receptors (thyroid hormone receptor). Also transports organic anions such as the conjugated steroid 17-beta-glucuronosyl estradiol (17beta-estradiol 17-O-(beta-D-glucuronate)). Transports T4 and estrone-3-sulfate in a pH-insensitive manner (By similarity). May serve as a drug efflux system at the blood brain barrier.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12923172, ECO:0000269|PubMed:18687783}; Multi-pass membrane protein {ECO:0000269|PubMed:18687783}. Note=Expressed in the plasma membranes of brain capillary endothelial cells. {ECO:0000269|PubMed:12923172}.
Interaction partners:
- Monocarboxylate transporter 8
- Monocarboxylate transporter 10
Sequence:
MDTSSKENAHLFHKNSAQPAGGPSFKAGYPSTEEARPCCGKLKVFLGALSFVYFAKALTEGYLKSTITQIERRFDIPSSLVGIIDGSFEIGNLLVITFVSYFGAKLHRPKIIGAGCLVMGFGTMLIAVPQFFMEKYSYEKYERYSPSSNLTPNISPCYLESSSPSPRSIVGKSQNKINDECEVDTSSSMWVYVFLGNLLRGLGETPIQPLGIAYLDDFASEDNAAFYIGCVQTVAIIGPIFGFLLGSLCAKLYVDIGFVNLDHITITPKDPQWVGAWWLGYLIAGFLSLLAAVPFWCLPKTLPRSQSREDSGSSSEKSKFITDDPVNYQMAPREESMKIMEMARDFLPSLKSLFRNPVYILYLCASTVQFNSLFGMVTYKPKYIEQQYGQSSSKANFVIGLINIPAVALGIFSGGIVMKKFRLGICEATKLYLGSSVFGYLLFLSLFALGCENSSVAGLTVSYQGTKPVSYHERALFSDCNSRCKCSDSKWEPMCGDNGITYASACLAGCQSSSRSGKNIIFSNCTCVGFAAPKSGNWSGMMGRCQKDNGCSQMFLYFLVISVITSYTLSLGGIPGYILLLRCIQPQLKSFALGIYTLAVRVLAGIPAPVYFGVLIDTSCLKWGFKKCGSRGSCRLYDSHAFRHIYLGLTTLLGTVSVFLSTAVLLVLKKKYVSKRSSFITAREKIVMSSSVKKETCAARDHGLQPKYWPGKETRL
Protein: Probable receptor-like protein kinase At4g10390 (EC 2.7.11.1) (Q9SV83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MACFLNCVRFDVSKTITDKPTSQGSGVTCYNSWDDVETLTSNFSRLIGSGGYSSIYMARFSGSDKAALKVHVSSHRLYQVFRLELDILLRLQHPNIVKLLGYFDDSEENGALLLEYLPQGNLQEKLQSNSKQVLQWRNRVAIALQLVQAIEHIHEKCSPQIVHGDIKSSNVLLDKNFDCKLCDFGSAKVGFSSMVQPPTMSPRSRQVKMVGSPGYTDPHYLRTGIASKKMDMYGFGVVVLELVSGKEAFSAERGEMLVHIAAPLMNEILDSSVDISEDKVRQFLDPRLLRDSLDIDEVKTMLSVAAVCISSKLSLRPSAAQVADTLIKEIPSLSFLGCGKGV
Protein: Elongation factor-like GTPase 1 (EC 3.6.5.-) (Elongation factor Tu GTP-binding domain-containing protein 1) (Elongation factor-like 1) (Protein FAM42A) (Q7Z2Z2)
Organism: Homo sapiens (Human)
Function: Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SBDS, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Has low intrinsic GTPase activity. GTPase activity is increased by contact with 60S ribosome subunits.
Interaction partners:
- Ribosome maturation protein SBDS
- Ubiquitin-like protein FUBI
- Ubiquitin-ribosomal protein eL40 fusion protein
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS13
Sequence:
MVLNSLDKMIQLQKNTANIRNICVLAHVDHGKTTLADCLISSNGIISSRLAGKLRYMDSREDEQIRGITMKSSAISLHYATGNEEYLINLIDSPGHVDFSSEVSTAVRICDGCIIVVDAVEGVCPQTQAVLRQAWLENIRPVLVINKIDRLIVELKFTPQEAYSHLKNILEQINALTGTLFTSKVLEERAERETESQVNPNSEQGEQVYDWSTGLEDTDDSHLYFSPEQGNVVFTSAIDGWGFGIEHFARIYSQKIGIKKEVLMKTLWGDYYINMKAKKIMKGDQAKGKKPLFVQLILENIWSLYDAVLKKDKDKIDKIVTSLGLKIGAREARHSDPKVQINAICSQWLPISHAVLAMVCQKLPSPLDITAERVERLMCTGSQTFDSFPPETQALKAAFMKCGSEDTAPVIIFVSKMFAVDAKALPQNKPRPLTQEEIAQRRERARQRHAEKLAAAQGQAPLEPTQDGSAIETCPKGEEPRGDEQQVESMTPKPVLQEENNQESFIAFARVFSGVARRGKKIFVLGPKYSPLEFLRRVPLGFSAPPDGLPQVPHMAYCALENLYLLMGRELEYLEEVPPGNVLGIGGLQDFVLKSATLCSLPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGEHVLVTAGEVHLQRCLDDLKERFAKIHISVSEPIIPFRETITKPPKVDMVNEEIGKQQKVAVIHQMKEDQSKIPEGIQVDSDGLITITTPNKLATLSVRAMPLPEEVTQILEENSDLIRSMEQLTSSLNEGENTHMIHQKTQEKIWEFKGKLEQHLTGRRWRNIVDQIWSFGPRKCGPNILVNKSEDFQNSVWTGPADKASKEASRYRDLGNSIVSGFQLATLSGPMCEEPLMGVCFVLEKWDLSKFEEQGASDLAKEGQEENETCSGGNENQELQDGCSEAFEKRTSQKGESPLTDCYGPFSGQLIATMKEACRYALQVKPQRLMAAMYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTDMFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEIIPSDPFWVPTTEEEYLHFGEKADSENQARKYMNAVRKRKGLYVEEKIVEHAEKQRTLSKNK
Protein: Semaphorin-3D (Collapsin-2) (COLL-2) (Q90663)
Organism: Gallus gallus (Chicken)
Function: Induces the collapse and paralysis of neuronal growth cones. Could potentially act as repulsive cues toward specific neuronal populations. Binds to neuropilin.
Subcellular location: Secreted.
Interaction partners:
- Neuropilin-1
- Plexin A1.
- Uncharacterized protein.
- Plexin-D1
- Transcription factor 21
- Plexin-A4
- Uncharacterized protein.
- Basic helix-loop-helix transcription factor scleraxis
Sequence:
MRASQVPNACSLLSLAMLFFPVTGTSKQNIPRLKLSYKDLLLSNSCIPFLGSTEGLDFRTLLLDEERGRLLVGAKDHIFLLNLVDLNKNVKKIYWPAAKEKMELCKLAGKDAHTDCANFIRVLQPYNRTHVYVCGTGAFHPLCGYIELGTHKEETIFRLDTQNLESGRLKCPFDPQQPFASVMADEYLYAGTASDFLGKDTALTRSLGPSHDHHYIRTDISEHYWLTGAKFIATFPIPDTYNPDDDKIYFFFREISQDSSTSDKTILSRVGRVCKNDMGGQRSLINKWTTFLKARLVCSIPGPEGADTHFDELQDIFLLSTRDERNPLVYGVFTTTSSVFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYEGRIPYPRPGTCPSKTYDPLIKSTRDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVDHVMAEDGQYDVIFLGTDIGTVLKAVSITKEKWTKEEVVLEELQIFKHPSFISTMEISQKQQQLYIGSRDGLVQLSLHRCHTYGKACADCCLARDPYCAWDGNSCSRYAPTSKRRARRQDVKYGDPVAQCWDVEDSISHETADEKVIFGIEFNSTFLECIPKSQQASIRWYIQRSGEEHREELKADERIIKTEHGLLIRSLQRRDAGAYFCKAQEHTFIHTIVKLNLNVIENGQMESTQKTEDEEGRVRDLLTESRLRYKDYIQLVSSPSFSLDEYCEQMWHREKRRQRNKGGAKWKHVQEMKKKRNRRHHEPARPPST
Protein: Glutamate dehydrogenase 1, mitochondrial (GDH 1) (EC 1.4.1.3) (P00367)
Organism: Homo sapiens (Human)
Function: Mitochondrial glutamate dehydrogenase that catalyzes the conversion of L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. Plays a role in insulin homeostasis. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19448744}. Endoplasmic reticulum {ECO:0000269|PubMed:19448744}. Note=Mostly translocates into the mitochondria, only a small amount of the protein localizes to the endoplasmic reticulum. {ECO:0000269|PubMed:19448744}.
Interaction partners:
- Glutamine synthetase
- Pyruvate carboxylase, mitochondrial
- Glutaminase kidney isoform, mitochondrial
- Glutamate dehydrogenase 2, mitochondrial
- Glutaminase liver isoform, mitochondrial
- Delta-1-pyrroline-5-carboxylate synthase
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Isocitrate dehydrogenase cytoplasmic
- Receptor-interacting serine/threonine-protein kinase 3
Sequence:
MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADREDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT
Protein: GH23463p (Q961H0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MTLQNGSLAQLVNLRVLHLENNKLTALEGTEFRSLGLLRELYLHNNMLTHISNATFEPLVSLEVLRLDNNRLSSLPHLQYRHSLQGLTLGRNAWSCRCQQLRELAQFVSDNAMVVRDAHDIYCLDAGIKRELELIGNLANGPDCSDLLDASASNISSSQDLAGGYRLPLLAAVLVLIFLVVVLIIVFVFRESVRMWLFAHYGVRVCEPRFEDAGKLYDAIILHSEKDYEFVCRNIAAELEHGRPPFRLCIQQRDLPPQASHLQLVEGARASRKIILVLTRNLLATEWNRIEFRNAFHESLRGLAQKLVIIEETSVSAEAEDVAELSPYLKSVPSNRLLTCDRYFWEKLRYAIPIELSPRGNNYTLDHHERFKQPVSPGMIFRQAPPPPAYYCTEEMEANYSSATTATPSPRPTRPGGAARIVDSMPMPMRPPSEHIYHSIESEYSAYDQHEALSMIPTGLMHQHQQQQLRLHQQQQQQQQQRLLQPQFRAMPQQAIPAPSAPVHLRSGSGLSQASTSTQSTAQASTSAAAAQQQQQQQQQQAAGSEAANKNGQAFLV
Protein: J domain-containing protein (Q20774)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock protein 110
- Heat shock protein hsp-1
- Heat shock protein 70
- Stress-induced-phosphoprotein 1
- DUF148 domain-containing protein
- DNaJ domain
- Heat shock protein 70
- Peptidyl-prolyl cis-trans isomerase 8
- Peptidyl-prolyl cis-trans isomerase 9
- Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein
Sequence:
MGKDYYKVLGISKGATDDEIKKAYRKMALKYHPDKNKEAGAENKFKEIAEAYDVLSDDKKKKIYDQFGEEGLKEGGPGAGGGGGGGMHYEFRGDPMNIFSSFFGGSDPFGAGGPGMFDLGGGAGGPNMFFMNQGGMDDGMFGGMHQGGRRGHARQDPAVLHDLSVSLEDVLKGTTKKMKITRKVMTDNAQRLEDKVLTVTIKPGWKSGTKITFPKEGDQHPNRTPADIVFVIKDKPHPKFKREGSDIKRVEKISLKSALTGLDIMIPTLDGADYRLQLNDVIKPGTTRRLTGKGLPNPKSPSHRGDLIIEFDVEFPSQLNPTQREVILRNF
Protein: Nucleoside diphosphate kinase B (NDK B) (NDP kinase B) (EC 2.7.4.6) (Histidine protein kinase NDKB) (EC 2.7.13.3) (P18) (nm23-M2) (Q01768)
Organism: Mus musculus (Mouse)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically. Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not. Exhibits histidine protein kinase activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P22392}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P22392}. Cell projection, ruffle {ECO:0000250|UniProtKB:P22392}. Nucleus {ECO:0000250|UniProtKB:P22392}. Note=Colocalizes with ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen but not on vitronectin or laminin substrates. {ECO:0000250|UniProtKB:P22392}.
Interaction partners:
- Nucleoside diphosphate kinase A
- Nucleoside diphosphate kinase 3
- Thymidylate kinase
- Nucleoside diphosphate kinase, mitochondrial
- CTP synthase 1
- UMP-CMP kinase
- Inosine triphosphate pyrophosphatase
- Nucleoside diphosphate kinase 6
- Adenylate kinase 9
- Ribonucleoside-diphosphate reductase large subunit
Sequence:
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIHLWFKPEELIDYKSCAHDWVYE
Protein: Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCH-L1) (EC 3.4.19.12) (Neuron cytoplasmic protein 9.5) (PGP 9.5) (PGP9.5) (Ubiquitin thioesterase L1) (Q9R0P9)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins (Probable). This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12913066, ECO:0000269|PubMed:33137160, ECO:0000269|PubMed:37215988}. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Localizes near and/or within mitochondria to potentially interact with mitochondrial proteins. {ECO:0000269|PubMed:33137160}.
Interaction partners:
- Lysosome-associated membrane glycoprotein 2
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
- Alpha-synuclein
- E3 ubiquitin-protein ligase parkin
- Ubiquitin-ribosomal protein eL40 fusion protein
- Heat shock cognate 71 kDa protein
- Adiponectin receptor protein 1
- Neural cell adhesion molecule 1
Sequence:
MQLKPMEINPEMLNKVLAKLGVAGQWRFADVLGLEEETLGSVPSPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLEFEDGSVLKQFLSETEKLSPEDRAKCFEKNEAIQAAHDSVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDSLLQDAAKVCREFTEREQGEVRFSAVALCKAA
Protein: TIR domain-containing protein (Q2YN91)
Organism: Brucella abortus (strain 2308)
Interaction partners:
Sequence:
MPCTFDLSRCVNQHEYTDQKIAEKFGKLDGAELAELTRLPTIFAYEAACKLDPKFGLIRDVTVRRGQVRIEYEFIPVQPFLTVADFDTLAFELDIGNWEMNRTHWAVKDVNLPKELHTAKGITLPSWTRQASRAVDITQHDFDVGLSFPGEARGLVEQVARELEARVGPNAYFYDNNYVSQLARPSLDTLLQDIYRNRCKLIVVFVGDDYQRKDWCGVEFRAIREIIMARAEQRIMFVRVDDGAVDGVFRTDGYVDARRFNPSEIAQFIAERVALIT