wanglab/gogpt-training-data huggingface dataset:
Protein: FAD-containing monooxygenase EthA (EC 1.14.13.-) (Baeyer-Villiger monooxygenase) (BVMO) (Prodrug activator EtaA) (Q7TVI2)
Organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Function: Monooxygenase able to convert a wide range of ketones to the corresponding esters or lactones via a Baeyer-Villiger oxidation reaction. Can act on long-chain aliphatic ketones (2-hexanone to 2-dodecanone) and on aromatic ketones (phenylacetone and benzylacetone). Is also able to catalyze enantioselective sulfoxidation of methyl-p-tolylsulfide. In vivo, likely functions as a BVMO, but the exact nature of the physiological substrate(s) remains to be established.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P9WNF9}. Note=Is most likely membrane-associated. {ECO:0000250|UniProtKB:P9WNF9}.
Interaction partners:
Sequence:
MTEHLDVVIVGAGISGVSAAWHLQDRCPTKSYAILEKRESMGGTWDLFRYPGIRSDSDMYTLGFRFRPWTGRQAIADGKPILEYVKSTAAMYGIDRHIRFHHKVISADWSTAENRWTVHIQSHGTLSALTCEFLFLCSGYYNYDEGYSPRFAGSEDFVGPIIHPQHWPEDLDYDAKNIVVIGSGATAVTLVPALADSGAKHVTMLQRSPTYIVSQPDRDGIAEKLNRWLPETMAYTAVRWKNVLRQAAVYSACQKWPRRMRKMFLSLIQRQLPEGYDVRKHFGPHYNPWDQRLCLVPNGDLFRAIRHGKVEVVTDTIERFTATGIRLNSGRELPADIIITATGLNLQLFGGATATIDGQQVDITTTMAYKGMMLSGIPNMAYTVGYTNASWTLKADLVSEFVCRLLNYMDDNGFDTVVVERPGSDVEERPFMEFTPGYVLRSLDELPKQGSRTPWRLNQNYLRDIRLIRRGKIDDEGLRFAKRPAPVGV
Protein: Protamine (Q24405)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTNNVNECKSLWNGIISISAKDESPKGLTEMCNHPIRRAPQKCKPMKSCAKPRRKAACAKATRPKVKCAPRQKCSKQGPVTNNAYLNFVRSFRKKHCNLKPRELIAKAR
Protein: Ribulose bisphosphate carboxylase small subunit (RuBisCO small subunit) (P06514)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:24907906}. Note=This cyanobacterium makes beta-type carboxysomes (PubMed:24907906). In the carboxysome RuBisCO is organized into a paracrystalline array (By similarity). {ECO:0000250|UniProtKB:Q31NB2, ECO:0000269|PubMed:24907906}.
Interaction partners:
- Ribulose bisphosphate carboxylase large chain
- phosphoribulokinase
- Carboxysome assembly protein CcmM
- Phosphoribulokinase
- Ribulose bisphosphate carboxylase/oxygenase activase
- Phosphoglycerate kinase
- Phosphoglycolate phosphatase
- All0135 protein
- All2681 protein
- Alr2873 protein
Sequence:
MQTLPKERRYETLSYLPPLTDVQIEKQVQYILSQGYIPAVEFNEVSEPTELYWTLWKLPLFGAKTSREVLAEVQSCRSQYPGHYIRVVGFDNIKQCQILSFIVHKPSRY
Protein: Acidic phospholipase A2 DE-I (svPA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A2 Ook-E6) (Phospholipase A2 PLA2-01) (P00625)
Organism: Ovophis okinavensis (Ryukyu Island pit viper) (Trimeresurus okinavensis)
Function: Snake venom phospholipase A2 (PLA2) that inhibits the ADP- and collagen-induced human platelet aggregation (By similarity). Exhibits high hydrolytic activities and preferred the anionic micelles to the zwitterionic micelles. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MRTLWIMAVLLLGVEGHLMQFETLIMKIAGRSGVWWYGSYGCYCGAGGQGRPQDPSDRCCFVHDCCYGKVTGCNTKDEFYTYSEENGAITCGGENPCLKEVCECDLAAAICFRDNLDTYNSKKYWMFPAKNCLEESEPC
Protein: Methylenetetrahydrofolate reductase (NADH) 1 (AtMTHFR1) (EC 1.5.1.54) (Q9SE60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The probable reversibility of the MTHFR reaction in plants suggests that they can metabolize the methyl group of 5,10-methylenetetrahydrofolate to serine, sugars and starch.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Serine hydroxymethyltransferase 7
- Aminomethyltransferase, mitochondrial
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Serine hydroxymethyltransferase 1, mitochondrial
- Serine hydroxymethyltransferase 2, mitochondrial
- Serine hydroxymethyltransferase 4
- Serine hydroxymethyltransferase 5
- Serine hydroxymethyltransferase 3, chloroplastic
Sequence:
MKVVDKIKSVTEQGQTAFSFEFFPPKTEDGVENLFERMDRLVSYGPTFCDITWGAGGSTADLTLEIASRMQNVICVETMMHLTCTNMPIEKIDHALETIRSNGIQNVLALRGDPPHGQDKFVQVEGGFACALDLVNHIRSKYGDYFGITVAGYPEAHPDVIEADGLATPESYQSDLAYLKKKVDAGADLIVTQLFYDTDIFLKFVNDCRQIGINCPIVPGIMPISNYKGFLRMAGFCKTKIPAELTAALEPIKDNDEAVKAYGIHFATEMCKKILAHGITSLHLYTLNVDKSAIGILMNLGLIDESKISRSLPWRRPANVFRTKEDVRPIFWANRPKSYISRTKGWNDFPHGRWGDSHSAAYSTLSDYQFARPKGRDKKLQQEWVVPLKSIEDVQEKFKELCIGNLKSSPWSELDGLQPETKIINEQLGKINSNGFLTINSQPSVNAAKSDSPAIGWGGPGGYVYQKAYLEFFCSKDKLDTLVEKSKAFPSITYMAVNKSENWVSNTGESDVNAVTWGVFPAKEVIQPTIVDPASFKVWKDEAFEIWSRSWANLYPEDDPSRKLLEEVKNSYYLVSLVDNNYINGDIFSVFA
Protein: Prolyl endopeptidase (EC 3.4.21.-) (O76728)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MQTERGPIAAHRPHEVVFGKVEGEDRGANPMDPPRRRVDPLFWLRDDNRADPEVLAHLHLEKDYYEKRAVDIKDLAETIYQEHISHIEETDMSAPYVYDRFLYYTRDVKGLSYKLHCRVPAGKTPGEGEDEEIVLDENKLAEGKSFCVVGCVAPAPPEHALVAYSVDYCGDEVYSIRFVRDVVADKVEGTNGSVVWGPNAECFFYITKDASKRDNKVWRHIIGQPQSEDVCLYTDDDPLFSVGVGRSGDGKTLIICSMSSETSESHLLDLRKGVKHNTLEMVRPREKGVRYTVEMHGTDTLIVLTNKDKCVNGKVVLTKRSAPTDWGTVLIPHDDKVTIDDVAVFAKFAVLSGRRDGLTRVWTVRLGPDNLFSSATLKELHFDEPVFTAHVVCSQMKTYDASLLRLRYSSMTTPTVWYDEDVLSGERKVVKARKVGGGFESKNYVCRRELATAPDGTKVPISLVYDTSIDLKKPNPTMLYGYGSYGICIEPEFNSRFLPYVDRGMIYAIAHVRGGGEMGRTWYEVGGKYLTKRNTFMDFIACAEHLISSGLTTPAQLSCEGRSAGGLLVGAVLNMRPDLFHVALAGVPFVDVMTTMCDPSIPLTTGEWEEWGNPNEYKFFDYMNSYSPIDNVRAQDYPHLMIQAGLHDPRVAYWEPAKWASKLRELKTDSNEVLLKMDLESGHFSASDRYKYLRENAIQQAFVLKHLNVRQLLRK
Protein: Erythropoietin (Epoetin) (P01588)
Organism: Homo sapiens (Human)
Function: Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3.
Subcellular location: Secreted {ECO:0000269|PubMed:32989016}.
Interaction partners:
- Erythropoietin receptor
- Thrombopoietin
- Tyrosine-protein kinase JAK2
- Granulocyte colony-stimulating factor
- Hypoxia-inducible factor 1-alpha
- Somatotropin
- Chorionic somatomammotropin hormone 2
- Chorionic somatomammotropin hormone 1
- Chorionic somatomammotropin hormone 1
- Interleukin-3
Sequence:
MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR
Protein: Sodium/potassium-transporting ATPase subunit beta-1 (Sodium/potassium-dependent ATPase subunit beta-1) (P08251)
Organism: Gallus gallus (Chicken)
Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type II membrane protein.
Interaction partners:
- FXYD domain-containing ion transport regulator
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit beta-3
- Uncharacterized protein.
- Protein ATP1B4
- cAMP-dependent protein kinase
- FXYD domain-containing ion transport regulator
- Sodium/potassium-transporting ATPase subunit alpha
- Uncharacterized protein.
Sequence:
MARGKANDGDGNWKKFIWNSEKKELLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTVSEFEPKYQDRVAPPGLTQVPQVQKTEISFTVNDPKSYDPYVKNLEGFLNKYSAGEQTDNIVFQDCGDIPTDYKERGPYNDAQGQKKVCKFKREWLENCSGLQDNTFGYKDGKPCILVKLNRIIGFKPKAPENESLPSDLAGKYNPYLIPVHCVAKRDEDADKIGMVEYYGMGGYPGFALQYYPYYGRLLQPQYLQPLVAVQFTNLTYDVEVRVECKEYGQNIQYSDKDRFQGRFDIKFDIKSS
Protein: Chymopasin (Q9EQZ8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLLLSLTLSLVLLGSSWGCGVPAITPALSYNQRIVNGENAVPGSWPWQVSLQDNTGFHFCGGSLIAPNWVVTAAHCKVTPGRHFVILGEYDRSSNAEPIQVLSISKAITHPSWNPNTMNNDLTLLKLASPARYTAQVSPVCLASSNEALPAGLTCVTTGWGRISGVGNVTPARLQQVVLPLVTVNQCRQYWGSRITDSMICAGGAGASSCQGDSGGPLVCQKGNTWVLIGIVSWGTENCNVQAPAMYTRVSKFNTWINQVIAYN
Protein: TBC1 domain family member 13 (Q9NVG8)
Organism: Homo sapiens (Human)
Function: Acts as a GTPase-activating protein for RAB35. Together with RAB35 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q8R3D1}. Cytoplasm {ECO:0000250|UniProtKB:Q8R3D1}.
Interaction partners:
- 28S rRNA
- Kynurenine--oxoglutarate transaminase 1
- Endonuclease G, mitochondrial
- NCK-interacting protein with SH3 domain
- Ras-related protein Rab-35
Sequence:
MSSLHKSRIADFQDVLKEPSIALEKLRELSFSGIPCEGGLRCLCWKILLNYLPLERASWTSILAKQRELYAQFLREMIIQPGIAKANMGVSREDVTFEDHPLNPNPDSRWNTYFKDNEVLLQIDKDVRRLCPDISFFQRATDYPCLLILDPQNEFETLRKRVEQTTLKSQTVARNRSGVTNMSSPHKNSVPSSLNEYEVLPNGCEAHWEVVERILFIYAKLNPGIAYVQGMNEIVGPLYYTFATDPNSEWKEHAEADTFFCFTNLMAEIRDNFIKSLDDSQCGITYKMEKVYSTLKDKDVELYLKLQEQNIKPQFFAFRWLTLLLSQEFLLPDVIRIWDSLFADDNRFDFLLLVCCAMLMLIREQLLEGDFTVNMRLLQDYPITDVCQILQKAKELQDSK
Protein: 27 protein (Transmembrane glycoprotein) (O41944)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Interaction partners:
Sequence:
MPEEIELRSLGRNSSGEVVLNGPYHCSENSRCPDCEKFSYLAYSFLIFLTVLLFSVYLLFVCPFEIKHLYGTWQSGDSILAGEVGPILNRTVTSKSCWRGPRCEMFIPNIPIILPNDTIYPNFTNYNGSYADYRTTLQEIIHTILYDQCNVTVLLHTSFGKTYGMDDVFFKTVMYKLITSFLMEGSTMCDLKTAARDVYVLHSLSHLHDVGKGCKLRLDNIYDESSGSHYSRECVKQFDCMLCIYPKSISVSFN
Protein: 11S globulin seed storage protein Jug r 4 (allergen Jug r 4) [Cleaved into: 11S globulin seed storage protein Jug r 4 acidic chain; 11S globulin seed storage protein Jug r 4 basic chain] (Q2TPW5)
Organism: Juglans regia (English walnut)
Function: Seed storage protein.
Interaction partners:
- ATP-dependent DNA helicase
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B-like
- DNA repair protein XRCC3 homolog
- DNA repair protein XRCC2 homolog isoform X1
- DNA repair protein RAD51 homolog 3-like isoform X3.
- Meiotic recombination protein DMC1 homolog
- DNA repair protein RAD51 homolog 3-like isoform X1.
- Endoplasmic reticulum chaperone BiP
- DNA repair protein RAD50
- Tudor domain-containing protein 3
Sequence:
MAKPILLSIYLFLIVALFNGCLAQSGGRQQQQFGQCQLNRLDALEPTNRIEAEAGVIESWDPNNQQFQCAGVAVVRRTIEPNGLLLPQYSNAPQLVYIARGRGITGVLFPGCPETFEESQRQSQQGQSREFQQDRHQKIRHFREGDIIAFPAGVAHWSYNDGSNPVVAISLLDTNNNANQLDQNPRNFYLAGNPDDEFRPQGQQEYEQHRRQQQRQQRPGEHGQQQRGLGNNVFSGFDADFLADAFNVDTETARRLQSENDHRRSIVRVEGRQLQVIRPRWSREEQEREERKERERERESESERRQSRRGGRDDNGLEETICTLRLRENIGDPSRADIYTEEAGRISTVNSHTLPVLRWLQLSAERGALYSDALYVPHWNLNAHSVVYALRGRAEVQVVDNFGQTVFDDELREGQLLTIPQNFAVVKRARNEGFEWVSFKTNENAMVSPLAGRTSAIRALPEEVLATAFQIPREDARRLKFNRQESTLVRSRPSRSRSSRSERRAEV
Protein: Cathepsin Lb (Uncharacterized protein LOC564979 precursor) (Wu:fa26c03 protein) (A7MCR7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Metalloendopeptidase
- Hatching enzyme 1.2
- Adenylyl cyclase-associated protein
Sequence:
MMFALLVTLCISAVFAASSIDIQLDDHWNSWKSQHGKSYHEDVEVGRRMIWEENLRKIEQHNFEYSYGNHTFKMGMNQFGDMTNEEFRQAMNGYKHDPNRTSQGPLFMEPSFFAAPQQVDWRQRGFVTPVKDQKQCGSCWSFSSTGALEGQLFRKTGKLISMSEQNLVDCSRPQGNQGCNGGLMDQAFQYVKENKGLDSEQSYPYLARDDLPCRYDPRFNVAKITGFVDIPRGNELALMNAVAAVGPVSVAIDASHQSLQFYQSGIYYERACSSSRLDHAVLVVGYGYQGADVAGNRYWIVKNSWSDKWGDKGYIYMAKDKNNHCGVATSASYPLM
Protein: Probable cytochrome P450 9f2 (EC 1.14.-.-) (CYPIXF2) (Q9VG82)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- NADPH--cytochrome P450 reductase
- NADPH-dependent diflavin oxidoreductase 1
- Probable cytochrome P450 303a1
- Probable cytochrome P450 12a4, mitochondrial
Sequence:
MLWEFFALFAIAAALFYRWASANNDFFKDRGIAYEKPVLYFGNMAGMFLRKRAMFDIVCDLYTKGGSKKFFGIFEQRQPLLMVRDPDLIKQITIKDFDHFINHRNVFATSSDDDPHDMSNLFGSSLFSMRDARWKDMRSTLSPAFTGSKMRQMFQLMNQVAKEAVDCLKQDDSRVQENELDMKDYCTRFTNDVIASTAFGLQVNSFKDRENTFYQMGKKLTTFTFLQSMKFMLFFALKGLNKILKVELFDRKSTQYFVRLVLDAMKYRQEHNIVRPDMINMLMEARGIIQTEKTKASAVREWSDRDIVAQCFVFFFAGFETSAVLMCFTAHELMENQDVQQRLYEEVQQVDQDLEGKELTYEAIMGMKYLDQVVNEVLRKWPAAIAVDRECNKDITFDVDGQKVEVKKGDVIWLPTCGFHRDPKYFENPMKFDPERFSDENKESIQPFTYFPFGLGQRNCIGSRFALLEAKAVIYYLLKDYRFAPAKKSCIPLELITSGFQLSPKGGFWIKLVQRN
Protein: Multiple organellar RNA editing factor 2, chloroplastic (Protein DIFFERENTIATION AND GREENING-like 1) (Protein DAG-like 1) (RNA editing-interacting protein 2) (O22793)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plastid rRNA processing and consequently in translation and early chloroplast differentiation. Involved in organellar RNA editing. Required for the processing of multiple editing sites in plastids.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12678554, ECO:0000269|PubMed:25583991, ECO:0000269|PubMed:28213559}.
Interaction partners:
- Pentatricopeptide repeat-containing protein GUN1, chloroplastic
- Organelle RRM domain-containing protein 6
- Protoporphyrinogen oxidase 1, chloroplastic
- Pentatricopeptide repeat-containing protein DWY1, chloroplastic
- NAD
- Pentatricopeptide repeat-containing protein At2g29760, chloroplastic
- Zinc finger protein VAR3, chloroplastic
- Pentatricopeptide repeat-containing protein At3g57430, chloroplastic
- Pentatricopeptide repeat-containing protein At5g13270
- Pentatricopeptide repeat-containing protein At1g02150
Sequence:
MALPLSGTRHLTRALLSNVTLMAPPRIPSSVHYGGSRLGCSTRFFSIRCGANRSGSTYSPLNSGSNFSDRPPTEMAPLFPGCDYEHWLIVMDKPGGEGATKQQMIDCYIQTLAKVVGSEEEAKKRIYNVSCERYLGFGCEIDEETSTKLEGLPGVLFVLPDSYVDPENKDYGAELFVNGEIVQRSPERQRRVEPQPQRAQDRPRYNDRTRYSRRRENTR
Protein: Packaging protein 3 (L1-52/55 kDa protein) (Packaging protein 52K) (P04496)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Involved in viral genome packaging through its interaction with packaging proteins 1 and 2. After proteolytic cleavage by adenovirus protease, L1 52/55k protein is removed from the capsid during viral maturation.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04058}. Note=Nuclear protein present in empty capsids and assembly intermediates. {ECO:0000255|HAMAP-Rule:MF_04058}.
Interaction partners:
Sequence:
MHPVLRQMRPPPQQRQEQEQRQTCRAPSPPPTASGGATSAVDAAADGDYEPPRRRARHYLDLEEGEGLARLGAPSPERYPRVQLKRDTREAYVPRQNLFRDREGEEPEEMRDRKFHAGRELRHGLNRERLLREEDFEPDARTGISPARAHVAAADLVTAYEQTVNQEINFQKSFNNHVRTLVAREEVAIGLMHLWDFVSALEQNPNSKPLMAQLFLIVQHSRDNEAFRDALLNIVEPEGRWLLDLINILQSIVVQERSLSLADKVAAINYSMLSLGKFYARKIYHTPYVPIDKEVKIEGFYMRMALKVLTLSDDLGVYRNERIHKAVSVSRRRELSDRELMHSLQRALAGTGSGDREAESYFDAGADLRWAPSRRALEAAGAGPGLAVAPARAGNVGGVEEYDEDDEYEPEDGEY
Protein: MRGB1 G protein-coupled receptor (Mas-related G protein-coupled receptor g6) (Q7TN48)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSFCEVVSCAIILLSLIIALVGLVGNGTVFWLLGFQMRRNAFSVYILNLAGADFLFMCFQIVYCSHIMLDMYYIPIKFPLFSIVVLNIGYLCGMSILSAISIERCLSVMWPIWYRCQRPRHTSAVICTLLWVLALVWSLIEGKECGFLFDTNGPGWCETFDLIATAWLIVLIVVLLGSSLALVINIFCGLYRIPVTRLYVTIVFTVLVFLLCGLPYGIYWFLLEWTEKFNYNLPCGFHPVTVLLSCVNSCANPIIYFLVGSIRHHRFQRKTLKLLLQKAMQDTPEEEECGEMGS
Protein: BEACH domain-containing protein B (BEACH-domain homolog B) (F4I9T0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the suppression of BCHC1 activity.
Interaction partners:
- Cell division topological specificity factor homolog, chloroplastic
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Cell division protein FtsZ homolog 1, chloroplastic
- Dynamin-like protein ARC5
Sequence:
MESDSVAGSASSSDAAASHLPSVSVLLDALEQSASTPRIANGLSQRLLRSLQFSNENKLSFKALNGACRVLRLACIQAKESRKSGCVSPLVESSDCGVIVDSPHKKSDSSHTEDCWFECVESCVGIFTEFFSSTNDAKVYVLRSSVCVDCLFELFWEKAVRNNVMKLIIDLMKIRPLCEEDKSAKLQVCSKYLETFTQVKERENDSVDLSVDLLAGMRDLIKSDSRYYQALFREGECFLHIVSLLNGNLDEANGEKLVLNVLQTLTSLLANNDTSKFAFKALAGKGYQTLQSLLLDFFQWKPTQRLLDALLDMLVDGKFDDKGSALIKNEDVIILYLNVLQKSSESLQCYGLNLFQQLLRDSISNRASCVRAGMLHLLLDWFSLENDDSVILKITQLTQTIGGHSISGKDIRKIFALLRSERVGNQQRYRSLLLACLLSMLNEKGPTGFFDMNGVESGIVIRTPVQWPANKGFSFCCWLRVESFPGDGKMGIFSFMSKNGKGCFAALGKDGLSYVSLNLKRQCVNVHTNLVCKKWHFICVSHSIGRAFWGGSLLRCYVNGDLVSSERCSYPKVTDVLTSCLIGTRITLPHIQDNDGLESIRDVFPFFGQIGPVYLFNDSLSSEQVQAIYSLGPSYMYAFLENEMTCPFSDNPFPSGILDGKDGLASKVSFGLNAQASDGRRLFNVSRVSDHLQERLAFEADIMVGTQLCSRRLLQQIIYCVGGISVFFPLITQSDRCESETLNEETSAMPTKERMTAEVIELIASVLDENPANQQQMHLLAGFPILGFLLQSIQPKQLNLETLSSLKHLFNVISSSGFAEQLVEDAISSIFLNPHIWLHAAYNVQRELYMFLIQQLDNDPRLLGSLCRLPRVIDIVWNFYWESERYCKGSKPLMHPTRTIAERPSRDEIHKIRLLLLSLGEMSLRHNISSGDVKALTAFFETCQDVACIEDVLHMVIRAISQTSVLVSFLEQVNLIGGCHIFVDLLQRDYEPIRLLSLQFLGRLLYDVPSERKGPKFFNLAVGRTKSLSQGHKKIGARTQPIFLAMSDRLFQYPQTDNLRATLFDVLLGGASPKQVLQKHNQVDKHRSKPSNSHFFLPQIFVFIFEFLSGCKDGLARMKIISDILDLLDSNPMNVEALMEFGWSAWLTASMKLDVIKDYRSELLNHDDLALNEQHFVRGLFCVVLCHYILSVKGGWQQLEETVNFILLQSEHNDVPYRSFLRDLYEDLIQRLVELSSEDNIFLSHPCRDNVLYLLRLVDEMLVREFGSRLLFPAISTDFSEDLLQLGNREDPTLGLDESFQRFLTEEISRNTECQQSCTTVTELMTNERWWNLYDNLWKIICDINGRGPVKMSPKSLATGPSIGQRARGLVESLNVPAAEMAAVVVSGGIGSALSGKMNKNVDKAMLLRGEKCPRIVFRLVTLYLCMSSLEKATRCVQQVTSLLPSFLAADDEQSKSRLHLFIGCLLYVRSQYGKLDDGARFHVISHLIRETVSCGKSILATSGMNKDDSSDSGGIFKEMGSIQNLIHKDRVLAAVTDETTYMKTLISDRTRQVQALGERNNETLSIECNSKKAFDGELQNVLKTVVTWDENRRVSVQLSHEEQQQNVTEKWIHMLRSLMDERGPWSATPFPNNILNRWKLDRTEDSWRRRPKLRRNYHFDERLCHPPSTSTATENETSNVINESKSGVIHIPEQMKKFLLKGIRRITDEGGSDSCENDSSQAEQSFMDTSADIQFSELVRTSSGLKDVVQDKVDASSLEVGTSEVLTSVPCVLVTPKRKLAGWLAVMKNVLHFSGEFLVEGTGGSAVFKNFSTSKGSDVTKAENKQNLVKWSSPYDSETFLDLESGNKNKKPLKKVKRHRRWKIGKVKSVHWTRYLLQYTALEIFFQESVPPVFLNFASQKNAKEVGMLIVSTRNEFLFPKNVPRDRTAMISFVDRRIAMEMAETARDRWRRREITNFEYLMILNTLAGRSYNDLTQYPVFPWVVADYSSETLDFSKASTFRDLSKPVGALDTRRFEIFEDRYHSFSDPDIPSFYYGSHYSSMGSVLYYLLRLEPFTSLHRSLQGGKFDHADRLFQSVEGSFRNCLSNTSDVKELIPEFFYMPEFLVNSNSYHLGVKQDGEPLGEVCLPPWAKGSPEMFIARNREALESEYVSSHLHDWIDLIFGHKQRGKPAVEAANIFYYLTYEGAVDVENMEDQLQISAIEDQIANFGQTPIQIFRKKHPRRGPPIPIAHPLYFAPASINLSSILPATTHSPSAVLYVGVVDSNIVLVNQGLTLSVKIWLTTQLHSGGNFTFSSAQDPFFGVGSDVLSPRNIGSPLADNVELGSQCFAAMQMPLENFLVSCGNWENSFHVISLTDGRVVQSIRHHKDVVSCVAVTADSTILATGSYDTTVMVWDILRMRTPEKRVRNTHAEVLRKDIVIADAPSHILCGHDDIITCLYVSTDLDIVISGSKDGTCVFHTLREGRYIRSLKHPSGSAVSKLAASHHGRIVLYGDDDLSLHLYSINGKHLASSESNGRINCLELSKCGEFLVSAGDQGQIIVRSMNTLEVVKRYNGAGKIITSLTVTQEECFLAGTKDGALLVYSIENPQHRKPSPIWSIKS
Protein: Arginase-1 (EC 3.5.3.1) (Liver-type arginase) (Type I arginase) (Q61176)
Organism: Mus musculus (Mouse)
Function: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P05089}. Cytoplasmic granule {ECO:0000250|UniProtKB:P05089}.
Interaction partners:
- Ornithine aminotransferase, mitochondrial
- Nitric oxide synthase, inducible
- Ornithine transcarbamylase, mitochondrial
- Ornithine decarboxylase
- Gene model 853
- Antizyme inhibitor 2
- Argininosuccinate lyase
- Nitric oxide synthase 3
- Nitric oxide synthase 1
- Glycine amidinotransferase, mitochondrial
Sequence:
MSSKPKSLEIIGAPFSKGQPRGGVEKGPAALRKAGLLEKLKETEYDVRDHGDLAFVDVPNDSSFQIVKNPRSVGKANEELAGVVAEVQKNGRVSVVLGGDHSLAVGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVSFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPAFTPATGTPVLGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKTAEEVKSTVNTAVALTLACFGTQREGNHKPGTDYLKPPK
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Q4QDU3)
Organism: Leishmania major
Interaction partners:
- phosphoglucomutase
- UTP-monosaccharide-1-phosphate uridylyltransferase
- UDP-glucose 4-epimerase
- Phosphomannomutase-like protein
- Galactokinase-like protein
- Phosphoacetylglucosamine mutase
- mannose-1-phosphate guanylyltransferase
- Glycylpeptide N-tetradecanoyltransferase
Sequence:
MENDMKSLSAAAQACVKKMRDAKVNEACIRTFIAQHVMVSKGETGSIPDSAIMPVDSLDALDSLTIECDNAVLQSTVVLKLNGGLGTGMGLCDAKTLLEVKDGKTFLDFTALQVQYLRQHCSEHLRFMLMDSFNTSASTKSFLKARYPWLYQVFDSEVELMQNQVPKILQDTLEPAAWAENPAYEWAPPGHGDIYTALYGSGKLQELVEQGYRYMFVSNGDNLGATIDKRVLAYMEKEKIDFLMEVCRRTESDKKGGHLARQTVYVKGKDGQPDAEKRVLLLRESAQCPKADMESFQDINKYSFFNTNNLWIRLPVLLETMQEHGGTLPLPVIRNEKTVDSSNSASPKVYQLETAMGAAIAMFESASAIVVPRSRFAPVKTCADLLALRSDAYVVTDDFRLVLDDRCHGHPPVVDLDSAHYKMMNGFEKLVQHGVPSLVECKRVTVKGLVQFGAGNVLTGTVTIENTDSASAFVIPDGAKLNDTTASPQQSTNK
Protein: Alanyl-tRNA editing protein AlaX-M (AlaX-M) (Alanyl-tRNA deacylase AlaX-M) (Q46AR9)
Organism: Methanosarcina barkeri (strain Fusaro / DSM 804)
Function: Functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala) or Gly-tRNA(Ala). Has no activity on incorrectly charged Ser-tRNA(Thr), nor on correctly charged Ala-tRNA(Ala) or Ser-tRNA(Ser).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Isoleucine--tRNA ligase
- WD-domain containing protein
- Pyrrolo-quinoline quinone repeat domain-containing protein
- WD-40 repeat-containing protein
- TIR domain-containing protein
- PQQ enzyme repeat domain protein
- WD-40 repeat-containing protein
- O-GlcNAc transferase, p110 subunit
- glycine--tRNA ligase
- TPR-domain containing protein
Sequence:
MTEALYFLDCYMKEFEATVEKVTDDKFVVLDRTVFYPESGGQPSDTGKLVRESDGAEFNVLYVRKFNGDISHEIDGENVSNGLKAGDKVKGFIDWDRRYRHMRMHTATHVIANVIEKEAGAQITGNQLGLDQSRVDFSLEVFDRDKFAEYEKIANDLIAQKSPVNLYLVSRKEAEEKLSRLTTLAKGFSDEIKEVRIVEIEGVTIEACGGTHVKNTEEIKGVKIIKLQNKGKSNRRMYFTLVD
Protein: Keratin-associated protein 20-2 (Q3LI61)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 22-1
- Small cysteine and glycine repeat-containing protein 1
- Keratin-associated protein 15-1
- Keratin-associated protein 24-1
- Keratin-associated protein 6-1
- Keratin-associated protein 26-1
- Keratin-associated protein 13-3
- Keratin-associated protein 6-3
- Keratin-associated protein 6-2
- Keratin-associated protein 7-1
Sequence:
MCYYSNYYGGLRYGYGVLGGGYGCGCGYGHGYGGLGCGYGRGYGGYGYGCCRPSCYGRYWSCGFY