wanglab/gogpt-training-data huggingface dataset:
Protein: Presenilin 1 (H0YM52)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}.
Interaction partners:
Sequence:
MTELPAPLSYFQNAQMSEDNHLSNTNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQL
Protein: E3 ubiquitin-protein ligase SH3RF1 (EC 2.3.2.27) (Plenty of SH3s) (Protein POSH) (RING-type E3 ubiquitin transferase SH3RF1) (SH3 domain-containing RING finger protein 1) (SH3 multiple domains protein 2) (Q71F54)
Organism: Rattus norvegicus (Rat)
Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis (By similarity). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16571722}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
Interaction partners:
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase kinase kinase 11
Sequence:
MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVDELPSNILLVRLLDGIKQRPWKPGPGGGGSTTCTNVLRAQGSTVVNCGSKDLQSPQCGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVNGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDTAECPSATAAQSSSASKHSDTKKNTRKRHSFTSLTMANKSSQASQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPTDVPYQAALGTMNPPLPPPPLLATTVLASTPSGATAAAVAAAAAAVAAGVGPRPAVGSTEQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWYKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQASRGVTMVSPSTAGGPAQKPQGNGVAGNPSVVPTAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAACIGPASVGLPHHSLASQPLPPMVGPAAHIAAVNINRTSVPLACAAGASSLASPNMTTAALETEPSGRTVTILPGLPTSPESAASACGNSSAVKPDKDSKKEKKGLLKLLSGASTKRKPRVSPPASPTLDVELGSGEVPLQGAVGPELPLGGVHGRVGSCPTDGDGPVAAGTAALAQDAFHRKTSSLDSAVPIAPPPRQACSSLGPVMNEARPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
Protein: Fibroblast growth factor 10 (FGF-10) (P70492)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Fibroblast growth factor-binding protein 1
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Platelet-derived growth factor receptor alpha
Sequence:
MWKWILTHCASAFPHLPGCCCCFLLLFLVSSVPVTCQALGQDMVSPEATNSSSSSSSSSSSSSFSSPSSAGRHVRSYNHLQGDVRWRKLFSFTKYFLKIEKNGKVSGTKKENCPYSILEITSVEIGVVAVKAINSNYYLAMNKKGKLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRRGQKTRRKNTSAHFLPMVVHS
Protein: Chaperone protein dnaJ C76, chloroplastic (atDjC76) (AtDjC17) (AtJ17) (Q9FMX6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function together with HSC70 chaperone to assist protein folding and prevent protein aggregation during salt stress in the chloroplast (Probable). Involved in root development. Required for the position-dependent cell fate determination during root hair development.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23894646}.
Interaction partners:
- Cell division cycle 5-like protein
- Chaperone DnaJ-domain superfamily protein
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- Transcriptional regulator ATRX
- Pre-mRNA-processing factor 19 homolog 1
- Protein pleiotropic regulatory locus 1
- AT4g21110/F7J7_50
- Protein pleiotropic regulator PRL2
- Pre-mRNA-processing factor 19 homolog 2
- At1g77930
Sequence:
MTPAIFSPTTLPPSTATWPCSTSQKLITVRSPLKFKCRATSSSSSITDFDLYDLLGIDRSSDKSQIKSAYRALQKRCHPDIAGDPGHDMAIILNEAYQLLSDPISRQAYDKEQAKLEELRGYTGKPIYSVWCGPETEQRAAFVDEVKCVGCLKCALCAEKTFAIETAYGRARVVAQWADPESKIKEAIEACPVDCISMVERSDLAPLEFLMSKQPRGNVRIGVGNTVGERVSNVFVDVKKFQERYAKAMSRTTKETSQREVQISAVEAIRSISNWLYWRSSPYTKPLSPESNMSLTFTKRKKAVDPDIRKLQDVVAAMKQADQSGRTKEKGSAYLLGEDYWSPSNAALPSSGNNNGSKASSNPQVTRKTFPSEEKPTSRRENRRQFRIKKFPIGTAIVAVFLVQYQASYRAASELNDHIGGSLALSIVNSPWQQILLAGVTWYFIGAMLLQLVEAVQHKLEDKET
Protein: Small ubiquitin-like protein (Q8N0B4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Sumo-conjugating enzyme ubc9
- UBC core domain-containing protein
- SUMO-activating enzyme subunit 2
- SUMO-activating enzyme subunit 1
- Ubiquitin-like protease family profile domain-containing protein
- Structural maintenance of chromosomes protein 5
- Proliferating cell nuclear antigen
- Ubiquitin-like protein NEDD8
- Ubiquitin-like protease family profile domain-containing protein
- Ubiquitin-like protease family profile domain-containing protein
Sequence:
MENTKEEPGVNGEAPVKDEHINLKVKNQGGGEVFFKIKRSTPLKKLMEAYCQRQGLNYASCRFLFDGVRVKEDATPNQLGMENEDVLDCALMQTGGSF
Protein: Olfactory receptor 51E1 (D-GPCR) (G-protein coupled receptor 164) (Olfactory receptor 52A3) (Prostate-overexpressed G protein-coupled receptor) (Prostate-specific G protein-coupled receptor 2) (Q8TCB6)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15313197}; Multi-pass membrane protein {ECO:0000269|PubMed:15313197}.
Interaction partners:
- Alpha-methylacyl-CoA racemase
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 3
- G protein-coupled receptor kinase 3
- Beta-arrestin-2
Sequence:
MMVDPNGNESSATYFILIGLPGLEEAQFWLAFPLCSLYLIAVLGNLTIIYIVRTEHSLHEPMYIFLCMLSGIDILISTSSMPKMLAIFWFNSTTIQFDACLLQMFAIHSLSGMESTVLLAMAFDRYVAICHPLRHATVLTLPRVTKIGVAAVVRGAALMAPLPVFIKQLPFCRSNILSHSYCLHQDVMKLACDDIRVNVVYGLIVIISAIGLDSLLISFSYLLILKTVLGLTREAQAKAFGTCVSHVCAVFIFYVPFIGLSMVHRFSKRRDSPLPVILANIYLLVPPVLNPIVYGVKTKEIRQRILRLFHVATHASEP
Protein: Probable cystathionine beta-synthase Rv1077 (EC 4.2.1.22) (Beta-thionase) (Serine sulfhydrase) (P9WP51)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Cystathionine gamma-synthase
- O-succinylhomoserine sulfhydrylase
- Serine acetyltransferase
- Serine hydroxymethyltransferase 2
- Phosphoserine phosphatase SerB2
- Serine hydroxymethyltransferase 1
- Adenosylhomocysteinase
- Methionine synthase
- Probable O-acetylhomoserine sulfhydrylase MetC
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Sequence:
MRIAQHISELIGGTPLVRLNSVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTAVPPHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVTTGPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEVSGGRVRIVGADPEGSVYSGGAGRPYLVEGVGEDFWPAAYDPSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMSKIFNDAWMSSYGFLRSRLDGSTEQSTVGDVLRRKSGALPALVHTHPSETVRDAIGILREYGVSQMPVVGAEPPVMAGEVAGSVSERELLSAVFEGRAKLADAVSAHMSPPLRMIGAGELVSAAGKALRDWDALMVVEEGKPVGVITRYDLLGFLSEGAGRR
Protein: Kinetochore protein NUF2 (P33895)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the essential kinetochore-associated NDC80 complex, which is involved in chromosome segregation and spindle checkpoint activity.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Interaction partners:
- Kinetochore protein SPC24
- Kinetochore protein NDC80
- Kinetochore protein SPC25
- Protein STU2
- Outer kinetochore KNL1 complex subunit SPC105
- Serine/threonine-protein kinase MPS1
- Kinetochore-associated protein DSN1
- Mitotic spindle checkpoint component MAD2
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Kinetochore-associated protein NNF1
Sequence:
MSRNQDVFPILDLQELVICLQSCDFALATQENISRPTSDYMVTLYKQIIENFMGISVESLLNSSNQETGDGHLQEENENIYLDTLNVLVLNKICFKFFENIGVQDFNMTDLYKPEAQRTQRLLSAVVNYARFREERMFDCNSFILQMESLLGQLRSKFDDYNLIQQQLKQYEDVDGDNIPDEQELQKLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIFKDLEALSFQIVELESNRDKLIKISNTDMEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQESNRTETELVGLKQNLINNKLKLMNVLETGIMYKLEILQEQLDLQLKNLEKLSQDTKEESRLNDTKLMDLQIKYENEIKPKIDKTDIFIQEELISGKINKLNDEIKQLQKDFEVEVKEIEIEYSLLSGHINKYMNEMLEYMQ
Protein: Vacuolar protein sorting-associated protein 26 (Q8I4T1)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Plays a role in vesicular protein sorting (By similarity). Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport (By similarity).
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- Phosphoinositide-binding protein, putative
- Sortilin
- GTPase-activating protein, putative
Sequence:
MLSTIFGSVCSIDLKIDADDNKKFAFLRKDKKGEKCPIFSDGEDINGTATISLKPGKKFEHYGIKLELIGQINILNDKANSYDFFSISKDLEPPGFLVESKQFKWKFSAVDKQHESYFGTNVQLRYFVRLNIIKGYSGNIQKEIDFIVQNLCIPPEINNTIKMEVGIEDCLHIEFEYDKSKYHLKDVVVGKVYFLLVRIKIKHMELDIIKMETSGVGKNYTTETVTLSKFEIMDGSPIKSECIPVRLYLSGFDLTPTYKNIQNKFSVKYYINLIIVDEEERRYFKKQEIFLWRKKMG
Protein: [PIN+] prion protein RNQ1 (Rich in asparagine and glutamine protein 1) (P25367)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Eukaryotic peptide chain release factor GTP-binding subunit
- Protein SIS1
- Heat shock protein 104
- Transcriptional regulator URE2
- Mitochondrial protein import protein MAS5
- SWI/SNF chromatin-remodeling complex subunit SWI1
- Heat shock protein SSA1
- [NU+] prion formation protein 1
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Transcriptional activator/repressor MOT3
Sequence:
MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY
Protein: Murinoglobulin-1 (MuG1) (P28665)
Organism: Mus musculus (Mouse)
Function: A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective.
Subcellular location: Secreted.
Interaction partners:
- UDP-glucuronosyltransferase
- Carboxylesterase 3B
- Cytochrome P450 2C50
- Serine protease inhibitor A3K
- Major urinary protein 3
- Cytochrome P450 2A12
- Carboxylesterase 3A
- Estradiol 17 beta-dehydrogenase 5
- Murinoglobulin-2
- Apolipoprotein A-V
Sequence:
MWKSRRAQLCLFSVLLAFLHSASLLNGDSKYMVLVPSQLYTETPEKICLHLYQLNETVTVTASLVSQSGRKNLFDELVLDKDLFQCVSFIIPRLSSSDEEDFLYVDIKGPTHEFSKRKAVLVKNKESVVFVQTDKPVYKPGQSVKFRVVSMDKMLRPLNELLPLAYIEDPKKNRIMQWRDIKTENGLKQMSFSLAAEPIQGPYKIVVHKESGEKEEHSFTVMEFVLPRFNVDLKVPNAMSVNDEVLSVTACGKYTYGKPVPGHVKINVCRETETGCREVNSQLDNNGCSTQEVNITELQSKKRNYEVQLFHVNATVTEEGTGLEFSRSGTTKIERITNKLIFLKADSHFRHGIPFFVKVRLVDIKGDPIPNEKVFIKAQELSYTSATTTDQHGLAEFSIDTTCISGSSLHIKVNHKEEDSCSYFYCMEERHASAKHVAYAVYSLSKSYIYLDTETSSILPCNQIHTVQAHFILKGDLGVLKELIFYYLVMAQGSIIQTGNHTHQVEPGEAPVKGKFALEIPVEFSMVPMAKMLIYTILPDGEVIADSVNFEIEKCLRNKVDLRFSTSQSLPASQTRLQVTASPQSLCGLRAVDQSVLLLKPESELSPSWIYNLPGMQQNKFVPSSRLSEDQEDCILYSSWLAEKHTNLVPHGTEKDVYRYVEDMGLTAFTNLMIKLPIICFDYGMVPISAPRVEFDLAFTPEISWSLRTTLSKRPEEPPRKDPSSNDPLTETIRKYFPETWVWDIVTVNSTGLAEVEMTVPDTITEWKAGALCLSNDTGLGLSSVVPLQAFKPFFVEVSLPYSVVRGEAFMLKATVMNYLPTSMQMSVQLEASPDFTAVPVGDDQDSYCLSANGRHTSSWLVTPKSLGNVNFSVSAEAQQSSEPCGSEVATVPETGRKDTVVKVLIVEPEGIKQEHTFSSLFCASDAEISEKMSLVLPPTVVKDSARAHFSVMGDILSSAIRNTQNLLHMPYGCGEQNMVLFAPNIYVLKYLNETQQLTQKIKTKALGFLRAGYQRELNYKHKDGSYSAFGDQNGEREGNTWLTAFVLKSFAQARAFIFIDESHITHAFTWLSQKQKDNGCFRSSGSLFNNAMKGGVDDEMTLSAYITMALLESSLPATHPVVSKALSCLESSWKTIEQERNASFVYTKALMAYAFALAGNQNKRDEILKSLDEEAIKENNSIHWKRPQKSRKSEHHLYKPQASSAEVEMNAYVVLARLTAQPAPSPEDLTLSMSTIMWLTKQQNSNGGFSSTQDTVVALDALSKYGAVTFSRSQKTTLVTIQSTGSFSQKFQVENSNRLLLQQVALPDIPGDYTISVSGEGCVYAQTMLRYNMHLEKQLSAFAIWVQTVPLTCNNPKGHNSFQISLEISYTGSRPASNMVIADVKMLSGFIPLKPTVKKLERLEHVSRTEVSNNNVLIYLDQVTNQTLAFSFIIQQDIPVRNLQPAIVKVYDYYETDEMAFAEYSSPCSTDKQNV
Protein: Malate dehydrogenase [NADP], chloroplastic (EC 1.1.1.82) (NADP-MDH) (Q8H1E2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells (Probable). Plays an essential role in the regulation of catalase activity and the accumulation of a hydrogen peroxide-dependent signal by transmitting the redox state of the chloroplast to other cell compartments.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Phosphoenolpyruvate carboxylase 3
- Phosphoenolpyruvate carboxylase 2
- Phosphoenolpyruvate carboxylase 1
- Phosphoenolpyruvate carboxylase 4
- Malate dehydrogenase, chloroplastic
- Malate dehydrogenase 2, peroxisomal
- Malate dehydrogenase 1, peroxisomal
- Fumarate hydratase 2
- Fumarate hydratase 1, mitochondrial
- Malate synthase
Sequence:
MAMAELSTPKTTSPFLNSSSRLRLSSKLHLSNHFRHLLLPPLHTTTPNSKISCSVSQNSQAPVAVQENGLVKTKKECYGVFCLTYDLKAEEETRSWKKLINIAVSGAAGMISNHLLFKLASGEVFGPDQPIALKLLGSERSIQALEGVAMELEDSLFPLLREVDIGTDPNEVFQDVEWAILIGAKPRGPGMERADLLDINGQIFAEQGKALNKAASPNVKVLVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNMTIWGNHSTTQVPDFLNARINGLPVKEVITDHKWLEEGFTESVQKRGGLLIQKWGRSSAASTAVSIVDAIKSLVTPTPEGDWFSTGVYTDGNPYGIEEGLVFSMPCRSKGDGDYELVKDVEIDDYLRQRIAKSEAELLAEKRCVAHLTGEGIAYCDLGPVDTMLPGEV
Protein: Retrotransposon hot spot (RHS) protein, putative (Q585H0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNQNGGSVGDTRNVLNGWLNGAYCPMKRQAGRQNENPSETGEGKSLEEKLYDSTYNAKWSYIIIDDGTQPLGMRMVDGMPNEGLMWKDEEVNVVPEIEETLEQKPERTKGVELLVLTSEMGWPYTDFARGSNSDIFIRREELRVWNFVRSGIELWRAQRVIPGCPYLPRSYVAIGNPGIGKSQNLGSFILYKLLHYDAEELPVVAYFRGVAAYIFEKSGGGGVGRVREYSKEAAITFMKVISSNTRGYVIYDFVKKGEQPPADVAPKWGSILISSPNLRNFDSWQKQRKGAFIVVNCWEMSEMRAFFSRMGPKLFPQATHVELREKWNMYENRVERVGPSLRYVFDEVMYGQELTAVDGELGSIVAGNKYGIYTKVLDNCGEWRDNDASHKLVKIVRIKAREGNSFDTYVCVAHSESIKKRILNVVFSGIAEEWALTTGMMRNASAIGLYFEENAIKYLCSPRVLTCFVNLITKLPANERARRMRTRKSILQHVRDGLLKVRRPKTVPGDINWAESEGAPVELYVPCVPNYPVADAFFIVDDEQAAQASGTTGKKTIVLLQFTVASRHDTKTDEFIHLLQSLLPSAEGGGHQNEATVEQLKEITEMFHWEIIYVQHFESTAMRSEQKCEITQGKAKHRSHQFVEGFWKNNVQQYHVQYEDNIVIKMLAVAAAGRR
Protein: Aldehyde dehydrogenase, mitochondrial (EC 1.2.1.3) (ALDH class 2) (ALDH-E2) (ALDHI) (P05091)
Organism: Homo sapiens (Human)
Function: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- All-trans-retinol dehydrogenase [NAD
- Alcohol dehydrogenase 1C
- Amine oxidase [flavin-containing] A
- All-trans-retinol dehydrogenase [NAD
- Amine oxidase [copper-containing] 3
- Alcohol dehydrogenase 1A
- Amine oxidase [flavin-containing] B
- All-trans-retinol dehydrogenase [NAD
- Amine oxidase [copper-containing] 2
- Alcohol dehydrogenase 6
Sequence:
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Protein: Nuclear factor of activated T-cells 2 (A0A8I6G9R9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQRSALRRPGPRQPLRTMGSADREEPIAHKAISSPSGLAYPDDVLDYGLKPCNPLASLSGEPPGRFGESDSIGFQNFLSPAKPAGASGPSPRIEITPSHELMQAGGALRGRDAGLSPEQPALALAGMAASPRFTLPVPGFEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNAGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVAPLPAASPQRSRSPSPQPSPHVAPQDDGIPAGYPPTAGSAVLMDALNSLATDSPCGIPSKIWKTSPDPTPVSTAPSKAGLARHIYPAVEFLGPCEQEERRNSAPESILLVPPTWPKQLVPAIPICSIPVTASLPPLEWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPEPSGRIVSLQAASNPIECSQRSAHELPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTGPAGTCETQPLPISLISADRLSPWLSRLQRNPPARSVFRCSVLLPAPGSSLVLLAL
Protein: Probable cytosolic iron-sulfur protein assembly protein CIAO1 (WD repeat-containing protein 39) (Q99KN2)
Organism: Mus musculus (Mouse)
Function: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins (By similarity). As a CIA complex component, interacts specifically with CIAO2A or CIAO2B and MMS19 to assist different branches of iron-sulfur protein assembly, depending of its interactors. The complex CIAO1:CIAO2B:MMS19 binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A specifically matures ACO1 and stabilizes IREB2 (By similarity). Seems to specifically modulate the transactivation activity of WT1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O76071}.
Interaction partners:
- Cytosolic iron-sulfur assembly component 2B
- MMS19 nucleotide excision repair protein homolog
- Cytosolic iron-sulfur assembly component 2A
- Cytosolic iron-sulfur assembly component 3
- ADP/ATP translocase 2
- General transcription and DNA repair factor IIH helicase subunit XPD
- Cytosolic Fe-S cluster assembly factor NUBP1
- Anamorsin
- Cysteine desulfurase
- Lipoyl synthase, mitochondrial
Sequence:
MKDSLVLQSRVPAHPDSRCWFLAWNPSGTLLASCGGDRKIRIWGTEGDSWICKSVLSEGHQRTVRKVAWSPCGNYLASASFDATTCIWKKNQDDFECVTTLEGHENEVKSVAWAPSGNLLATCSRDKSVWVWEVDEEDEYECVSVLSSHTQDVKHVVWHPSQELLASASYDDTVKLYQEEGDDWVCCATLEGHESTVWSIAFDPSGQRLASCSDDRTVRIWRQYLPGNEQGVACSGSDPSWKCICTLSGFHTRTIYDVAWCQLTGALATACGDDAIRVFEEDPGSDPQQPTFSLTAHLRQAHSQDVNCVAWNPKEPGLLASCSDDGEVAFWEYHQPAGL
Protein: Os05g0163900 protein (cDNA clone:002-168-H12, full insert sequence) (Q75IR0)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Transcription factor RF2a
- Defective in exine formation protein, putative, expressed
- Os03g0830300 protein
- Os10g0112100 protein
- Os03g0830400 protein
- Os03g0101800 protein
- Os03g0830500 protein
- Os01g0267400 protein
- Os04g0461600 protein
- Os06g0266266 protein
Sequence:
MAACQQQIWQEGKQQQHLHHGGYDDLSSVYRGTVVLPRRQGGLAPEPPPPRPSSSSGRSAAAQATAMTIHSEAERRRRERINAHLATLRRILPDAKQMDKATLLASVVNQVKHLKTRATEATTPSTAATIPPEANEVTVQCYAGGEHTAAARTYVRATVSCDDRPGLLADIAATFRRLRLRPLSADMSCLGGRTRHAFVLCREEEEEEDAAAEARPLKEAVRQALAKVALPETVYGGGGRSKRQRLMMESRYSTAVVHTHVDPQYCWYNSR
Protein: AP-3 complex subunit mu-2 (Adaptor-related protein complex 3 subunit mu-2) (Clathrin assembly protein assembly protein complex 3 mu-2 medium chain) (Clathrin coat assembly protein AP47 homolog 2) (Clathrin coat-associated protein AP47 homolog 2) (Golgi adaptor AP-1 47 kDa protein homolog 2) (HA1 47 kDa subunit homolog 2) (Mu3B-adaptin) (m3B) (P47B) (Q8R2R9)
Organism: Mus musculus (Mouse)
Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Ap47 is a subunit of the plasma membrane adaptor (By similarity). In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit delta-1
- AP-3 complex subunit beta-2
- AP-3 complex subunit beta-1
- AP-3 complex subunit sigma-2
- AP-3 complex subunit sigma-1
- AP-3 complex subunit mu-1
- AP-1 complex subunit gamma-like 2
- AP-1 complex subunit gamma-1
- AP-4 complex subunit epsilon-1
- AP-2 complex subunit alpha-1
Sequence:
MIHSLFLINSSGDIFLEKHWKSVVSRSVCDYFFEAQERATEAENVPPVIPTPHHYLLSVYRHKIFFVAVIQTEVPPLFVIEFLHRVVDTFQDYFGVCSEPVIKDNVVVVYEVLEEMLDNGFPLATESNILKELIKPPTILRTVVNTITGSTNVGDQLPTGQLSVVPWRRTGVKYTNNEAYFDVVEEIDAIIDKSGSTVTAEIQGVIDACVKLTGMPDLTLSFMNPRLLDDVSFHPCVRFKRWESERILSFIPPDGNFRLLAYHVSAQNLVAIPVYVKHSISFRDSSSLGRFEITVGPKQTMGKTIEGVIVTSQMPKGVLNMSLTPSQGTHTFDPVTKMLSWDVGKINPQKLPSLKGTMGLQVGASKPDENPTINLQFKIQQLAISGLKVNRLDMYGEKYKPFKGIKYMTKAGKFQVRT