wanglab/gogpt-training-data huggingface dataset:
Protein: Nardilysin (EC 3.4.24.61) (N-arginine dibasic convertase) (NRD convertase) (NRD-C) (Nardilysin convertase) (O43847)
Organism: Homo sapiens (Human)
Function: Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. Is a critical activator of BACE1- and ADAM17-mediated pro-neuregulin ectodomain shedding, involved in the positive regulation of axonal maturation and myelination. Required for proper functioning of 2-oxoglutarate dehydrogenase (OGDH) (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:28017472}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8BHG1}.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Probable helicase senataxin
- Arf-GAP with dual PH domain-containing protein 1
Sequence:
MLRRVTVAAVCATRRKLCEAGRELAALWGIETRGRCEDSAAARPFPILAMPGRNKAKSTCSCPDLQPNGQDLGENSRVARLGADESEEEGRRGSLSNAGDPEIVKSPSDPKQYRYIKLQNGLQALLISDLSNMEGKTGNTTDDEEEEEVEEEEEDDDEDSGAEIEDDDEEGFDDEDEFDDEHDDDLDTEDNELEELEERAEARKKTTEKQSAAALCVGVGSFADPDDLPGLAHFLEHMVFMGSLKYPDENGFDAFLKKHGGSDNASTDCERTVFQFDVQRKYFKEALDRWAQFFIHPLMIRDAIDREVEAVDSEYQLARPSDANRKEMLFGSLARPGHPMGKFFWGNAETLKHEPRKNNIDTHARLREFWMRYYSSHYMTLVVQSKETLDTLEKWVTEIFSQIPNNGLPRPNFGHLTDPFDTPAFNKLYRVVPIRKIHALTITWALPPQQQHYRVKPLHYISWLVGHEGKGSILSFLRKKCWALALFGGNGETGFEQNSTYSVFSISITLTDEGYEHFYEVAYTVFQYLKMLQKLGPEKRIFEEIRKIEDNEFHYQEQTDPVEYVENMCENMQLYPLQDILTGDQLLFEYKPEVIGEALNQLVPQKANLVLLSGANEGKCDLKEKWFGTQYSIEDIENSWAELWNSNFELNPDLHLPAENKYIATDFTLKAFDCPETEYPVKIVNTPQGCLWYKKDNKFKIPKAYIRFHLISPLIQKSAANVVLFDIFVNILTHNLAEPAYEADVAQLEYKLVAGEHGLIIRVKGFNHKLPLLFQLIIDYLAEFNSTPAVFTMITEQLKKTYFNILIKPETLAKDVRLLILEYARWSMIDKYQALMDGLSLESLLSFVKEFKSQLFVEGLVQGNVTSTESMDFLKYVVDKLNFKPLEQEMPVQFQVVELPSGHHLCKVKALNKGDANSEVTVYYQSGTRSLREYTLMELLVMHMEEPCFDFLRTKQTLGYHVYPTCRNTSGILGFSVTVGTQATKYNSEVVDKKIEEFLSSFEEKIENLTEEAFNTQVTALIKLKECEDTHLGEEVDRNWNEVVTQQYLFDRLAHEIEALKSFSKSDLVNWFKAHRGPGSKMLSVHVVGYGKYELEEDGTPSSEDSNSSCEVMQLTYLPTSPLLADCIIPITDIRAFTTTLNLLPYHKIVK
Protein: mRNA degradation protein pet127, mitochondrial (O74832)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the degradation of mRNA in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent RNA helicase suv3, mitochondrial
- Exoribonuclease II, mitochondrial
- ATP synthase subunit a
- Uncharacterized exonuclease C637.09
- Ribonuclease Z 1
- Pentatricopeptide repeat-containing protein 5
- Probable oligoribonuclease
Sequence:
MLIYKKKNFGRRSVYNLKKCLHKGFQINSCNIKAADNVLHSKASAFEKVNVVDKESIGNLQHHLDTVLPKKKFQFLRDPKTNDYKWDEYLSKILPVDKFNFGLLSKFRPPSEDEQLQKVANSIGAEFVGSTSSLTGLMSQLHFFISKWKFPNFSDLSKGFYISPNERNFTRLCRSASSVHISYQNGLYCIDKDKSLTKEPSVNIILMNVGKSLETFFTVDKDQFLLYKKPPSSNGVLKPLKDVFQYGRCSSLLVRSQLDCYDKKIPESGVFDLKTRAVFGVRMNQTQPELFKSYKLTHYYGNRISFEREYFDLIRSAFMKYSLQARLGYMQGVFVAYHNTSDIFGFQYIPLVAMDRAIHGSSEIGEAEFNLNLQLLEKILQYATSIFPKRSFRVMLSTTEDVPNPPLKVYLEVADDKENRGFDLLDGQKNLEAKTVSPSNFCALEVCALQFVNGVHKSVVKHLDEKETWSIKYHFRKPRDQDNLLRNYIRLRDDIKRRESKISNPPESLLHDYYACSEQYYKRN
Protein: Stevor (C0H5N4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MYYLKMLLFTFLINTLVLQHYENYLNNHYNVSLIQNNTKRTTIHSRLLAQTKNHNPHYHNDPELKEIIDKMNEEAIKKYQQTHDPYKQLKDVVEKNGTKYTGGNDVEPMSTLEKELLETYEETFGNKSDMLKLGKYKNDDDKSDDSSSCGCTNINNMKLAKTKGRDKYLKHLKGRCTRGIYISSLTTVILTTIALHTAKAAALAKFVESAKTCASYMTIFNMLNAGNLNTAIQAGGGICTSAYSDIVLPAANAALSAIYPCGIAALVLLILTVVLIILYIWLYRRRKRSWKHECKKHLCK
Protein: E3 ubiquitin-protein ligase RNF185 (EC 2.3.2.27) (RING finger protein 185) (Q96GF1)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination of BNIP1. Acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway. Also acts as a regulator of the innate antiviral response by catalyzing 'Lys-27'-linked polyubiquitination of CGAS at 'Lys-173' and 'Lys-384', thereby promoting CGAS cyclic GMP-AMP synthase activity. Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:21931693}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24019521, ECO:0000269|PubMed:27485036}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF5
- Erlin-1
- Erlin-2
- Membralin
- Transmembrane and ubiquitin-like domain-containing protein 2
- Transmembrane and ubiquitin-like domain-containing protein 1
- Derlin-1
- LIM domain kinase 2
- E3 ubiquitin-protein ligase AMFR
- Cystic fibrosis transmembrane conductance regulator
Sequence:
MASKGPSASASPENSSAGGPSGSSNGAGESGGQDSTFECNICLDTAKDAVISLCGHLFCWPCLHQWLETRPNRQVCPVCKAGISRDKVIPLYGRGSTGQQDPREKTPPRPQGQRPEPENRGGFQGFGFGDGGFQMSFGIGAFPFGIFATAFNINDGRPPPAVPGTPQYVDEQFLSRLFLFVALVIMFWLLIA
Protein: Small ribosomal subunit protein uS15c (30S ribosomal protein S15, chloroplastic) (P0C470)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Os03g0612600 protein
- Os01g0220300 protein
- Small ribosomal subunit protein eS19
- Os10g0411700 protein
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein uS14c
- Small ribosomal subunit protein bS16c
- Small ribosomal subunit protein uS9c
- Os07g0658200 protein
- 40S ribosomal protein S6
Sequence:
MKKKGGRKIFGFMVKEEKEENWGSVEFQVFSFTNKIRRLASHLELHKKDFSSERGLRRLLGKRQRLLAYLAKKNRVRYKKLISQLDIRER
Protein: Uncharacterized protein YfdR (P76514)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YfdS
- Uncharacterized protein YfdT
- Uncharacterized protein YfdQ
- Uncharacterized protein YfdP
- 5'-deoxynucleotidase YfbR
- Uncharacterized protein YmfL
- Uncharacterized protein YdfR
Sequence:
MSFIKTFSGKHFYYDKINKDDIVINDIAVSLSNICRFAGHLSHFYSVAQHAVLCSQLVPQEFAFEALMHDATEAYCQDIPAPLKRLLPDYKRMEEKIDAVIREKYGLPPVMSTPVKYADLIMLATERRDLGLDDGSFWPVLEGIPATEMFNVIPLAPGHAYGMFMERFNDLSELRKCA
Protein: Nucleoside triphosphate pyrophosphohydrolase (NTP-PPase) (EC 3.6.1.8) (P96379)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required to maintain the full capacity of the mycobacterium to respond to oxidative stress via the degradation of oxidation-induced damaged nucleotides. Hydrolyzes all canonical (d)NTPs, as well as mutagenic dUTP and 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP). Also involved in the transcriptional activation of RelA in response to oxidative stress.
Interaction partners:
- Transcription-repair-coupling factor
- Probable transcriptional regulatory protein
- Hypoxanthine-guanine phosphoribosyltransferase
- dITP/XTP pyrophosphatase
- Inosine-5'-monophosphate dehydrogenase
- GMP reductase
- GMP synthase
- Uncharacterized oxidoreductase Rv3410c
- Nucleoside diphosphate kinase
- Secreted protein
Sequence:
MIVVLVDPRRPTLVPVEAIEFLRGEVQYTEEMPVAVPWSLPAARSAHAGNDAPVLLSSDPNHPAVITRLAAGARLISAPDSQRGERLVDAVAMMDKLRTAGPWESEQTHDSLRRYLLEETYELLDAVRSGSVDQLREELGDLLLQVLFHARIAEDASQSPFTIDDVADTLMRKLGNRAPGVLAGESISLEDQLAQWEAAKASEKARKSVADDVHTGQPALALAQKVIQRAQKAGLPAHLIPDEITSVSVSADVDAENTLRTAVLDFIDRLRCAERAIAVARRGSNVAEQLDVTPLGVITEQEWLAHWPTAVNDSRGGSKKRKGMR
Protein: VRK serine/threonine kinase 3 (M0QYA8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISFCPDCGKSIQAAFKFCPYCGNSLPVEEHVGSQTFVNPHVSSFQGSKRGLNSSFETSPKKVKWSSTVTSPRLSLFSDGDSSESEDTLSSSERSKGSGSRPPTPKSSPQKTRKSPQVTRGSPQKTSCSPQKTRQSPQTLKRSRVTTSLEALPTGTVLTDKSGRQWKLKSFQTRDNQGILYEAAPTSTLTCDSGPQKQKFSLKLDAKDGRLFNEQNFFQRAAKPLQVNKWKKLYSTPLLAIPTCMGFGVHQDKYRFLVLPSLGRSLQSALDVSPKHVLSERSVLQVACRLLDALEFLHENEYVHGNVTAENIFVDPEDQSQVTLAGYGFAFRYCPSGKHVAYVEGSRSPHEGDLEFISMDLHKGCGPSRRSDLQSLGYCMLKWLYGFLPWTNCLPNTEDIMKQKQK
Protein: T-cell leukemia homeobox protein 3 (Homeobox protein Hox-11L2) (O43711)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- PHD finger protein 6
- Protein lyl-1
- Nuclear pore complex protein Nup214
- T-cell acute lymphocytic leukemia protein 1
- Rhombotin-1
- B-cell lymphoma/leukemia 11B
- Ran-binding protein 17
- Rhombotin-2
- Tyrosine-protein kinase ABL1
Sequence:
MEAPASAQTPHPHEPISFGIDQILNSPDQDSAPAPRGPDGASYLGGPPGGRPGATYPSLPASFAGLGAPFEDAGSYSVNLSLAPAGVIRVPAHRPLPGAVPPPLPSALPAMPSVPTVSSLGGLNFPWMESSRRFVKDRFTAAAALTPFTVTRRIGHPYQNRTPPKRKKPRTSFSRVQICELEKRFHRQKYLASAERAALAKSLKMTDAQVKTWFQNRRTKWRRQTAEEREAERQQASRLMLQLQHDAFQKSLNDSIQPDPLCLHNSSLFALQNLQPWEEDSSKVPAVTSLV
Protein: Sodium- and chloride-dependent betaine transporter (Betaine transporter SNF-3) (Na(+)/Cl(-) betaine/GABA transporter) (Sodium:neurotransmitter symporter family protein 3) (G5EBN9)
Organism: Caenorhabditis elegans
Function: Betaine transporter dependent on Na(+) and Cl(-) ions that functions primarily in the epidermis to clear betaine from the extracellular space. Elicits current in response to betaine but not in response to GABA, L-carnitine, sarcosine, glycine or dimethylglycine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24212673}; Multi-pass membrane protein {ECO:0000305|PubMed:24212673}.
Interaction partners:
- Hcy-binding domain-containing protein
- Betaine receptor acr-23
Sequence:
MGTSEHVPLPTDEAKAKELEQSQHSEEPDRGQWTGKFDFLMSMVAYAVGLGNVWRFPYLCYKNGGGSFLVVYMIFFCLAAVPIFLMEVTVGQYLQKGAMEMWLMCPLFRGVGIGNVVIAFMCIAYFCVIVAWAMFYMISSIAWVFPWETCNNYWNDATCVTGKENFTELARIKALVASAGGHTQTSVEQFWEKRVLHDTGDISEFGGIQWELFFIMAAAWLIVYFALWKGITQARKFVYFCALFPYVLIFILLIRGLTLEGAGTGIYFYLKPNATRLLDTAVWKDAGTQVFYSYGVGFGALIALGSHNKFNHNCFKDAITMCFINGCTSITAGFAVFSILGYMSHVAQKDISEIVKPGVGLAFLAYPEVASNLPMKQVFAVLFFLMITILGLDSQVCMMEGLFTALEDAFPILRKYKKQSLGIFCLFFFCIGIPMVTHSGSHWLTLFDAYGASGYALLFVVFFEVVGLAYGFGAHNIRKALHEMIGVTLPKGIEYVWKFCAPATSLVLFVFCVVYYHPVKYPDGKDFPFWANAFGWFLSSCSMVVIPGYAIYYLFFTNKHLTLKERVRKGLNLDGSFESPAKKNLVNNAEELKFIESSSQ
Protein: Potassium channel toxin alpha-KTx 8.8 (OSK3) (A0A1L2FZD4)
Organism: Orthochirus scrobiculosus (Central Asian scorpion)
Function: Selectively inhibits voltage-gated potassium channels rKv1.2/KCNA2 (IC(50)=331 nM) and hKv1.3/KCNA3 (IC(50)=503 nM). Partially inihibts rKv1.6/KCNA6 (IC(50)=9983 nM).
Subcellular location: Secreted {ECO:0000269|PubMed:28179135}.
Interaction partners:
Sequence:
MCRLYAIILIVLVMNVIMTIIPDSKVEVVSCEDCPEHCSTQKARAKCDNDKCVCEPI
Protein: Crumbs-like protein 1 (Protein crumbs homolog 1 precursor) (Q1A5L3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDMDLAVWGSVWLRLVACVLFVLLQWTESVTLLKTSTLCLDNPCQHQSECREALSDFLCQCQTTVPVFPSTRCDSSSTLCQLSICQGNATCQPTGAHPGELVCQCDSGLLGQDCLSSAQLCAQGHCGDSAHCLAVRDQSPGYACICQEGYTGRSCEKEVDHCSPNPCRNRAICRSRRNGPTCFCVPGFQGQLCEIEVNECVSRPCRNGATCVDKIGHYICLCRPGYMGSSCELEIDECQSQPCLHGASCHDHINGFTCTCLAGFQGESCEINIDECRDQPCQNGALCVDEINSYRCDCSQTANFTGVDCEIPPPPCWSQPCLNSALCEDQQENYTCNCWPGFEGRNCEVDVSECESSPCVNEGICMELSWKTLYGTEPLFTARYNPRLASGFICKCPPGFSGALCEQNTTACTTSPCHNGATCEDFLGSYKCICPSESEDGVLYGGRNCSEPLTGCEGHECQNGASCIPFLSEGVHGYSCICQPGYTGSYCQTLTVFSFETSRAFLHLQTPLLGAETYFNITLSFRTVLENTVLFQRGSGGVTLSLEIQETHLILDLKTDPQPNATSWTLMLPQVVSDGEWHTVEAVLGEGTLLLQLLEPCQGGQNCGTTAQVKIGALELESALLSTFVGGLDEGGSSRSFIGCMRDLLVDSQLMIPEDWLSSSAVNVVQGCSHHDRCLSGPCENHGECVNLWQGYQCKCLRPYVGQNCDEEYITTRFGQEDSTSYAVFTINDEPDSETLHLSMFLRTRKDSGLLVLLANSTSDYLQMWLEKGKLTVQVNNLKTVTGERVLNDGERHFVSVTIEDGMMTLQNSDHEFEATYVQPVSIQFGDTINVGGLFDVQALTAFGGHFKGCLQDLQLNEKKLEFFPIDTSAMSYKPDRVVEVTAGCTSDDTCSKNPCQNGGICFSSWDDFTCNCPPNTSGQHCEEVSWCDLNPCPPQAICKALNQGYECISNVTFQENTTLVYQGNGLISRHLTSIVFNIRTRKRNAIVLHAESGSEFVTVSLQDGFLVLELLSGPTTSSSLSPVTLHSPRVVADGEWHVIELLMATPGSNSSHWIMVPLDEKDEPTKSDSMTGNLDFLRESVYIMLGGLGPDSGSNLIGCLSNVEIGGIVLPYYGQTEVRFPRTQEEMFNKISEEPVQTGCFGEVVCEPNPCLHGGICDDHFNLFHCFCLPGWGGDHCELNTNTCASNPCRHGYCSVQDLTYNCTCEDGYTGTNCEMKVDACAGHRCANGATCLRGFNMYSCLCTDKFTGPLCNIQIEEVPWYVVVRNIPPKLPVSICGDEQQNYTCFNGGNCSDTNMPCDCHPGFSGHWCELELDECRSNPCKNGGYCQNMVNRFQCVCEMTFAGETCEVDLNAESVTSQLLLSISLVCVVLLLVVFGVTTALVIALNRRATRGTYSPSRQEKEGSRVEMWNIVQPPPMERLI
Protein: Uncharacterized protein, isoform D (A0A0B4KFS6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFAGIRKRLARKQNEKDCDEDDKEDVLDSMPPPPNYIQISQGRIQLVHQPRTPVESEAGTLSLERHGGSISGSGGCDKDVLEKRMIEVEGALLRLQEQFQKSQCGSPTFEKELREQIENMNRIMKSKERKQMQTCRDHKALQTRFARQESLLQSMQQENRSLLTRIRQYEHCLDDVMRKVVDAIVAEDNLREEVSMLKGRVRDLEAQNAALSASPVKGRDEGYCTMSSGQPQPSNGHLEDLPEEPEQWLLPAEPCSTEMEDWSMSQEELAVMTFDDERDPHHPHLQQQRRKRDHDWLWPSSDFINSTTVETDSVADGITQLLQQKIVYSEDEEVACTDFTNDFYKLVNIRSNSSRSLYSYLEGETDDEDEDDDDGEDSSISESQVGPAGRISPTPSEAGRAQLTSCSSSETDELSASQAKKDEEPDYAVIDECRRRVSDIEIEDVPMIVSSTPMKPLDEQQCIAQIIKSELRRPPHVLVKSKSVLEDQEPSCILRHNQRRELESTVVCSDSISCAMMNKLAKEVVPPAPGMVTKLKERMLLRQASTPPTASSWRRSNGWKRVTSPVHPPVAVSPKKAAKSTEPPKSCLPKAQPTRIPTSIHSSVSSSSSMSSSCSPSPSSPSPQSPQQRSPGQQTQQQQQQQQQRKSKIPPPVPVRRSYAS
Protein: Protein lin-7 homolog C (Lin-7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3) (Q9NUP9)
Organism: Homo sapiens (Human)
Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12967566, ECO:0000269|PubMed:21849460}; Peripheral membrane protein {ECO:0000269|PubMed:12967566}. Basolateral cell membrane {ECO:0000269|PubMed:12967566}; Peripheral membrane protein {ECO:0000269|PubMed:12967566}. Cell junction {ECO:0000250}. Postsynaptic density membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Mainly basolateral in renal epithelial cells. {ECO:0000250}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Amyloid-beta A4 precursor protein-binding family A member 1
- Disks large homolog 4
- MAGUK p55 subfamily member 7
- Protein PALS1
- Disks large homolog 1
- MAGUK p55 subfamily member 3
- MAGUK p55 subfamily member 2
- Protein PALS2
- Protein lin-7 homolog B
Sequence:
MAALGEPVRLERDICRAIELLEKLQRSGEVPPQKLQALQRVLQSEFCNAVREVYEHVYETVDISSSPEVRANATAKATVAAFAASEGHSHPRVVELPKTEEGLGFNIMGGKEQNSPIYISRIIPGGIADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGKVKLVVRYTPKVLEEMESRFEKMRSAKRRQQT
Protein: GH27120p (Q7K2L7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Protein transport protein Sec31A
- ALG-2 interacting protein X
- GEO09647p1
- 26S proteasome non-ATPase regulatory subunit 5
Sequence:
MSYGQGYNPYAQPGGGYAPPPGAFPPQNAQVSPQAQQWFSMVDRDRSGKINASELQAALVNGRGDHFSDNACKLMISMFDNDASGTIDIYEFEKLYNYINQWLQVFKTYDQDSSGHIEEQELTQAFTQMGFRFSPEFINFLVKKSDPQGHKEVSVDQFIVLCVQVQRFTEAFRQRDTQQNGTITIGFEDFLTVAIGCSY
Protein: Forkhead domain 3F, isoform C (Q9W4Q1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MIVNMPVNGTGSASSPTSNPSSNNNNNSSTTNQNDTNTNLPGDYNFLKRKFDDQEDLALGHDYEPIGANPWKKRHLDYDAGDLHFHLQLEQPPSNPPTNAAPAQSSTSFINDLFSYESSLLVPAVAYSHCPPSSAPLDDNGGWTGGELLELDHRYNSGLQAELGQLNATLPPPPPTSSSAQNASNHTQQSTQQNVSPGQNPHQNQHFLVPQKQRIQSAGRRTSSGSVSGANEATEADFEDKNLSWLLNFKFDEFPHLSPHNQIHGQAVNLPEGSAPPHPPSTAVPIATSPCSSSSPSSASAASASASAISTNQSLGSGLVDQRARSPKSCSSAAMPAALGGGGNGSAGASAAGGVAGVGSTKTGRKFEELVMEVTSELDGNDMIVAEHVVVEDTSSKAPKKPPFTYTELIEYALEDKGELTVSGIYQWISDRFPYYKSNDDRWKNSVRHNLSINPHFRKGVKAPQGAGHLWAISSGDSAENVLAWEHKKQRLDLFFKMESINRERIQQHQQQQQLQQHQQQHQQHSPQQKQHSAAQQQHMPQASSCMYDEAAVAVATLTQEMMQTNSGGGSTETSQQQQQQQQHHHHHSHQNHQNHNQHHQRLLPFNDLLSDDELRKTAGQILNGIHREVEVQSVNSIISTYHDVLLDNDYLNPIHKDVVVTESVLRQQHGTNLGGGNNNQNNQMGGNSHMGGGNSQYYITEIDPMELGIQMSHQVEPSEEEVLFSDEFNLNYFGYNPGSDIVA
Protein: Acyl-CoA wax alcohol acyltransferase 2 (EC 2.3.1.75) (11-cis-specific retinyl-ester synthase) (11-cis-RE-synthase) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diacylglycerol O-acyltransferase 2-like protein 4) (EC 2.3.1.20) (Long-chain-alcohol O-fatty-acyltransferase 2) (Wax synthase) (mWS) (Q6E1M8)
Organism: Mus musculus (Mouse)
Function: Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters. Shows a preference for medium chain acyl-CoAs from C12 to C16 in length and fatty alcohols shorter than C20, as the acyl donor and acceptor, respectively. Also possesses acyl-CoA retinol acyltransferase (ARAT) activity that catalyzes 11-cis-specific retinyl ester synthesis. Shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis-retinol, 13- cis-retinol and all-trans-retinol substrates (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15220349}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Retinol dehydrogenase 11
- Cytochrome P450 26A1
- Alcohol dehydrogenase 1
- Alcohol dehydrogenase class-3
- All-trans-retinol dehydrogenase [NAD
- All-trans-retinol dehydrogenase [NAD
- 17-beta-hydroxysteroid dehydrogenase type 6
- Epidermal retinol dehydrogenase 2
- Retinol dehydrogenase 5
Sequence:
MFWPTKKDLKTAMEVFALFQWALSALVIVTTVIIVNLYLVVFTSYWPVTVLMLTWLAFDWKTPERGGRRFTCVRKWRLWKHYSDYFPLKMVKTKDISPDRNYILVCHPHGLMAHSCFGHFATDTTGFSKTFPGITPYMLTLGAFFWVPFLRDYVMSTGSCSVSRSSMDFLLTQKGTGNMLVVVVGGLAECRYSTPGSTTLFLKKRQGFVRTALKHGVSLIPAYAFGETDLYDQHIFTPGGFVNRFQKWFQKMVHIYPCAFYGRGLTKNSWGLLPYSQPVTTVVGEPLPLPKIENPSEEIVAKYHTLYIDALRKLFDQHKTKFGISETQELVIV
Protein: Carnitine palmitoyltransferase 1Aa (liver) (Q1MTA9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAEAHQAVAFQFTVGPDGIDLQLSHEALRQVYLSGIHSWKKKFIRFKNGILNGVYPGSAPGFVLVLAGYLGRAQYLKVDPSLGLLFKLGNYVPISRYMSEQKQMLVGGVMVGTGLWIAIIFGMRTVLKGLLSWHGWMFASHGRMTWKIRLWLVFVKVFSGMQTPMLYSFQNSLPHLFVPSVKETTRRYLESVQPLLSDEEHQRMQRLALDFERNLGPKLQWYLKLKSWWATNYVSDWWEEYIYLRGRGPIMVNSNYYVMDFLYAFPTNIQAARAGNVIHAIMLYRRKLDRAQIKPLMLQNTIPMCSSQYERMFNTSRIPGIETDSVQHVSDSRHIVVYHRGRYFKVWMFYDGRLLLPREIEQQMERILADTSEPQPGEETLAALTAGDRVPWACARNAYLRHGTNKKSLDSVEKAAFFVTLDDTEQRFDQKNPVESLDRYAKSLLHGKCYDRWFDKSINLIIFKNGTMGLNAEHSWADAPIVGHLWEQVLSMDPVKLGYTEDGHCKGEPHANLPGPQRLQWNIPTECQTMITNSLSVAEALADDVDSHIIPFSDFGKGLIKKCRTSPDAFIQLALQLAHYRDKGKFCLTYEASMTRLFREGRTETVRSCTTESCAFVRAMNSNHTREQKLQLLKNAAEKHQQMYRLAMTGHGIDRHLFCLYVVLKYLGQDSPFLKEVLSEPWRLSTSQTPLQQGELFDLVKNPEYVTSGGGFGPVADDGYGVAYVIVGEKLINFHISSKRSSPETDSHRFGNNIRRAMIDMLDLFQLDKKDPK
Protein: Leucine aminopeptidase (EC 3.4.11.-) (Epoxide hydrolase) (EC 3.3.2.10) (Leukotriene A-4 hydrolase homolog) (LTA-4 hydrolase) (Q9FY49)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Leucine aminopeptidase 2, chloroplastic
- Transcription initiation factor TFIID subunit 2
- Threonine dehydratase biosynthetic, chloroplastic
- beta-galactosidase
- Leucine aminopeptidase 3, chloroplastic
Sequence:
MAPIDPHSFTDSSHPLTTHVALSLYLDFNTSIIHGSALLTLSSAFSGELSLDTRCISIAMVLDPLTLEPIPYSVSTTPDRIRGTEVVVVLSGQSSLLIVYSTSPSASALQWLSPLQTFSKLHPYVYTQCQAIHARSIFPCQDTPAARIRYDVVMNIPNSLSAVMSARHVRRRLAVPEEAKHLEAGSLGSSLWCGEDRVVEEFAMEQPIPPYLFAFAVGELGFREVGPRTRVYTESAAIEVLDAAALEFAGTEDMIKQGEKLFGDYEWERFDLLVLPPSFPYGGMENPRMVFLTPTVIKGDATGAQVVAHELAHSWTGNLITNINNEHFWLNEGFTTYAERRIVEVVQGADIATLNIGIGWRGLTDEMERFKDNLECTKLWNKQEGVDPDDVYSQVPYEKGFQFVLRIERQIGRTAFDEFLKKYIATFKFKSIDTNTFLEFLKANIPGIEKEINLQLWTEGVGIPEDAYEPVSTIYTKIISLAKEFKEGKMPSEDDVAEWNGQEWELYLENLPKSCEPSQVMALDKRYRLAESKDYEVKVSFLQLAVTSKCREYHGEVKKTLKEVGRMKYLRPLFTALAQSGGTEEKQLAKQVFAEARETYHPIAQGVVESILSKYI
Protein: 5'-AMP-activated protein kinase subunit beta-1 (Q8IGW5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGNASSSVHMQRERHKSTDLSTPSSPAHFRDSIGGGGAGQGGSAGAAALGAAAGAVGAAGGGGGGGGGQAFSFDKKHTAVLNEGSSQEDDDPYYAGTGTGSTRRGTAHDDATSAVTRDHSSMDNNEEEEEAAVGAEPATGSQLTGDEDDIRKTALPTVLRWDGGGKNVTISGTFSDWKPMAMVRSHQNFVTIIDLPEGDHQYKFCVDGEWKHDPKLKSVENAEGQRNNLVSVRESDFEVFQALAKDSENVTNYAEKEYSQEVPQVKPWEKVSGPPVLPPHLLQVILNKDTPLSCEPTLLPEPNHVMLNHLYALSIKDGVMVLSATHRYRKKYVTTLLYKPI
Protein: Histone deacetylase (EC 3.5.1.98) (A0A2R8QIW0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
Interaction partners:
Sequence:
MALSSQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDSTIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNDYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAVQEDSGDEEDDPDKRISIRAHDKRIACDEEFSDSEDEGQGGRRNAANYKKPKRVKTEEEKDGEEKKGEPTDVKEEEKASEEKMDTKGPKEELKTV
Protein: Hepcidin (A1Z0M0)
Organism: Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea)
Function: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9EQ21}.
Interaction partners:
Sequence:
MKTFSVAVAVAVVLAFICLQESSAVPANEEQELEQQIYFADPEMPVESCKMPYYMRENRQGSPARCRFCCRCCPRMRGCGICCRF
Protein: Diaminopimelate epimerase, chloroplastic (DAP epimerase) (EC 5.1.1.7) (Q9LFG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Racemase that operates by a 'two-base' mechanism, which involves one active-site cysteine acting as a base to abstract the alpha-proton of an amino acid, while a second cysteine thiol functions as an acid to reprotonate the resulting planar carbanionic intermediate from the opposite face.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Diaminopimelate decarboxylase 2, chloroplastic
- Diaminopimelate decarboxylase 1, chloroplastic
- LL-diaminopimelate aminotransferase, chloroplastic
- aspartate-semialdehyde dehydrogenase
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Aminotransferase ALD1, chloroplastic
- Aspartokinase 1, chloroplastic
- Aspartokinase 3, chloroplastic
- Aspartokinase 2, chloroplastic
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
Sequence:
MEIAAVSTVSVAPQSRRVSNAFSRNLGSVSSLSFGFFEKEYCFKSPSLRVSAAASMDAVTAEKFSPASFLDKKETGVLHFVKYHGLGNDFILVDNRDSSEPKITQEQAAKLCDRNFGVGADGVIFAMPGVNGTDYAMRIFNSDGSEPEMCGNGVRCFARFIAELENLQGKHSFTIHTGAGLIVPEIQDDGQVKVDMGTPILKAQDVPTKLSGNKGEAVVEAELVVDGVSWNVTCVSMGNPHCITFGKKGGPNLKVDDLNLPEIGPKFEHHEMFPARTNTEFVEVLSRSHLKMRVWERGAGATLACGTGACALVVAAVLEGRADRKCTVDLPGGPLEIEWKQEDNHIYMTGPAEAVFYGSALL
Protein: Protein OSCP1 (Q8BHW2)
Organism: Mus musculus (Mouse)
Function: May be involved in drug clearance in the placenta.
Subcellular location: Basal cell membrane {ECO:0000250}.
Interaction partners:
Sequence:
MSVRTLPLLFLNLGGEMLYVLDQRLRAQNIPGDKARKVLNDIISTMFNRKFMDELFKPQELYSKKALRTVYDRLAHASIMRLNQASMDKLYDLMTMAFKYQVLLCPRPKDVLLVTFNHLDAIKGFVQDSPTVIHQVDETFRQLSEVYGKLSEGEFQLIRQTLLNFFQDLHIRVSTFLKDKVQNSNGRFVLPVSGPVPWGTEVPGVIRVFSVKGKEVKKMKFRHGGDYVAAQKEGSFELYGDRVLKLGTNMYSASRPVETHMSATSKNAASRAQENIVPNPLAKEELNFLARLMGGMEIKKPSGPEPGFRLNLFTTDEEEEHAALSRPEELSYEVISIQATQDQQRNEELARIMGEFEITEQLEQNTSKGDDLLAMMDRL