wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane protein 106B (Q6AYA5)
Organism: Rattus norvegicus (Rat)
Function: Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking. May act as a molecular brake for retrograde transport of late endosomes/lysosomes, possibly via its interaction with MAP6. In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress (By similarity). Required for proper lysosomal acidification (By similarity).
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:24357581}; Single-pass type II membrane protein {ECO:0000269|PubMed:24357581}. Lysosome membrane {ECO:0000269|PubMed:24357581}; Single-pass type II membrane protein {ECO:0000269|PubMed:24357581}. Cell membrane {ECO:0000250|UniProtKB:Q9NUM4}; Single-pass type II membrane protein {ECO:0000255}. Note=Colocalizes with LAMP1 (PubMed:24357581). A small fraction resides on the cell surface (By similarity). {ECO:0000250|UniProtKB:Q9NUM4, ECO:0000269|PubMed:24357581}.
Interaction partners:
- Microtubule-associated protein 6
- Progranulin
- Charged multivesicular body protein 2B
- RCG31562, isoform CRA_c.
Sequence:
MGKSLSHLPLHSNKEDGYDGVTSTDNMRNGLVSSEVRNEDGRSGDVSQFPYVEFTGRDSVTCPTCQGTGRIPRGQENQLVALIPYSDQRLRPRRTKLYVMASVFVCLLLSGLAVFFLFPRSIDVKYIGVKSAYVSYDSQKRMIYLNITNTLNITNNNYYSVEVENITAQVQFSKTVIGKARLSNITNIGPLDMKQIDYTVPTVIAEEMSYMYDFCTLPSIKVHNIVLMMQVTVTTAYFGHSEQISQERYQYVDCGRNTTYQLAQSEYLNVLQPQQ
Protein: Pullulanase A (EC 3.2.1.41) (Alpha-dextrin endo-1,6-alpha-glucosidase) (Pullulan 6-glucanohydrolase) (A0A0H2UNG0)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Virulence factor (By similarity). Involved in the degradation of glycogen of the mammalian host cells. Hydrolyzes the alpha-1,6-branchpoints of glycogen. Hydrolyzes pullulan. Does not hydrolyze dextran. Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-binding protein, which binds to amylose (pure alpha-(1,4)-linked glucose), amylopectin (alpha-(1,4)-linked glucose with alpha-(1,6) branch points), pullulan (linear polymer of mixed alpha-(1,4)- and alpha-(1,6)-linked glucose) and glycogen (similar to amylopectin with more frequent alpha-(1,6) branch points) in vitro. Does not bind to dextran (a linear polymer of alpha-(1,6)-linked glucose).
Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000250|UniProtKB:Q9F930}. Note=Localizes to cytoplasm in the lung alveolar type II cells of the mouse and human hosts. {ECO:0000269|PubMed:17187076, ECO:0000269|PubMed:21565699}.
Interaction partners:
Sequence:
MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAAGSGKNESDISSPGNANASLEKTEEKPAASPADPAPQTGQDRSSEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIRKENYKFTDLKNHSQIFLKDDDESIYTNPYYVHDIRMTGAQHVGTSSIESSFSTLVGAKKEDILKHSNITNHLGNKVTITDVAIDEAGKKVTYSGDFSDTKHPYTVSYNSDQFTTKTSWRLKDETYSYDGKLGADLKEEGKQVDLTLWSPSADKVSVVVYDKNDPDKVVGTVALEKGERGTWKQTLDSTNKLGITDFTGYYYQYQIERQGKTVLALDPYAKSLAAWNSDDSKIDDAHKVAKAAFVDPAKLGPQDLTYGKIHNFKTREDAVIYEAHVRDFTSDPAIAKDLTKPFGTFEAFIEKLDYLKDLGVTHIQLLPVLSYYFVNELKNHERLSDYASSNSNYNWGYDPQNYFSLTGMYSSDPKNPEKRIAEFKNLINEIHKRGMGAILDVVYNHTAKVDLFEDLEPNYYHFMDADGTPRTSFGGGRLGTTHHMTKRLLIDSIKYLVDTYKVDGFRFDMMGDHDAASIEEAYKAARALNPNLIMLGEGWRTYAGDENMPTKAADQDWMKHTDTVAVFSDDIRNNLKSGYPNEGQPAFITGGKRDVNTIFKNLIAQPTNFEADSPGDVIQYIAAHDNLTLFDIIAQSIKKDPSKAENYAEIHRRLRLGNLMVLTAQGTPFIHSGQEYGRTKQFRDPAYKTPVAEDKVPNKSHLLRDKDGNPFDYPYFIHDSYDSSDAVNKFDWTKATDGKAYPENVKSRDYMKGLIALRQSTDAFRLKSLQDIKDRVHLITVPGQNGVEKEDVVIGYQITAPNGDIYAVFVNADEKAREFNLGTAFAHLRNAEVLADENQAGPVGIANPKGLEWTEKGLKLNALTATVLRVSQNGTSHESTAEEKPDSTPSKPEHQNEASHPAHQDPAPEARPDSTKPDAKVADAENKPSQATADSQAEQPAQEAQASSVKEAVRNESVENSSKENIPATPDKQAELPNTGIKNENKLLFAGISLLALLGLGFLLKNKKEN
Protein: Upstream stimulatory factor 1 (E9PME6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKGQQKTAETEEGTVQIQEGAVATGEDPTSVAIASIQSAATFPDPNVKYVFRTENGGQVMYRVIQVSEGQLDGQTEGTGAISGYPATQSMTQAVIQGQFFVMMSPQEVLQGGSQRSIAPRTHPYSPKSEAPRTTRDEKRRAQHNEVERRRRDKINNWIVQLSKIIPDCSMESTKSGQSKGGILSKACDYIQELRQSNHRLSEELQGLDQLQLDNDVL
Protein: Heavy metal-associated isoprenylated plant protein 33 (AtHIP33) (F4JZL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heavy-metal-binding protein.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 43
- Disease resistance-like protein DSC2
- MD-2-related lipid-recognition protein ROSY1
- Heavy metal-associated isoprenylated plant protein 14
- Protein RESTRICTED TEV MOVEMENT 3
- Obg-like ATPase 1
- Eukaryotic initiation factor 4A-3
- Kunitz trypsin inhibitor 1
- Eukaryotic initiation factor 4A-III homolog
- Temperature-induced lipocalin-1
Sequence:
MSKEEFMKIQTCVLKVNIHCDGCKQKVKKILQKIEGVFTTKIDAELGKVTVSGNVDPSVLIKKLLKSGKHAEIWGAPKGGSNNNQNQPNLANQFKAMQIDHGGKGGGGGGGGPANNNKGQKIGGGGGGGGGGGGGGGGGPPKMVIPQLTPQQMQQLNPQQLQQLQQLQQMKGFQDLKLPPQLKGGPGPGPGSVPMNKNPQMPNNPNQKAVKFNVPDDDDEEDFSDEFDDEFDEDDDEFDDDLEDDEFDDHPPPPNKMKPMMGGGNMIMPNNMMPNMMMPNAQQMLNAHKNGGGPGPAGGKIEGKGMPFPVQMGGGGGGPGGKKGGPGGGGGNMGNQNQGGGGKNGGKGGGGHPLDGKMGGGGGGPNGNKGGGGVQMNGGPNGGKKGGGGGGGGGGGPMSGGLPPGFRPMGGGGGGGGGPQSMSMPMGGAMGGPMGSLPQMGGGPGPMSNNMQAVQGLPAMGPGGGGGGGPSAEAPPGYFQGQVSGNGGGGQDSMPGNPYLQQQQQQQQQQYLAAVMNQQRSMGNERFQPMMYARPPPAVNYMPPQPQPHQQHPYPYPYPYPPQYPPHNGDQYSDYFNDENTSSCNIM
Protein: Guanine nucleotide-binding protein subunit alpha-13 (G alpha-13) (G-protein subunit alpha-13) (P27601)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG). GNA13-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1). Promotes tumor cell invasion and metastasis by activating Rho/ROCK signaling pathway (By similarity). Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:18703424}; Lipid-anchor {ECO:0000269|PubMed:18703424}. Melanosome {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:18703424}. Nucleus {ECO:0000269|PubMed:18703424}. Note=Cytoplasmic in adult somatic cells, but mainly nuclear in spermatids in the testes. Translocates from the cytoplasm to the nucleus during spermatogenesis, hence predominantly observed in the cytoplasm of round spermatids but localized in the nuclei of elongating or elongated spermatids and testicular spermatozoa.
Interaction partners:
- Sphingosine 1-phosphate receptor 2
- Rho guanine nucleotide exchange factor 11
- Rho guanine nucleotide exchange factor 1
- Rho guanine nucleotide exchange factor 12
- Integrin beta-3
- Sphingosine 1-phosphate receptor 3
- Estrogen receptor
- Transforming protein RhoA
- Guanine nucleotide-binding protein subunit alpha-12
- Lysophosphatidic acid receptor 1
Sequence:
MADFLPSRSVLSVCFPGCVLTNGEAEQQRKSKEIDKCLSREKTYVKRLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKGMRVLVDAREKLHIPWGDNKNQLHGDKLMAFDTRAPMAAQGMVETRVFLQYLPAIRALWEDSGIQNAYDRRREFQLGESVKYFLDNLDKLGVPDYIPSQQDILLARRPTKGIHEYDFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEFDQVLMEDRQTNRLTESLNIFETIVNNRVFSNVSIILFLNKTDLLEEKVQVVSIKDYFLEFEGDPHCLRDVQKFLVECFRGKRRDQQQRPLYHHFTTAINTENIRLVFRDVKDTILHDNLKQLMLQ
Protein: Fanconi anemia group C protein homolog (Protein FACC) (P50652)
Organism: Mus musculus (Mouse)
Function: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Upon IFNG induction, may facilitate STAT1 activation by recruiting STAT1 to IFNGR1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=The major form is nuclear. The minor form is cytoplasmic.
Interaction partners:
- Fanconi anemia group B protein homolog
- Fanconi anemia core complex-associated protein 100
- E3 ubiquitin-protein ligase FANCL
- Fanconi anemia group A protein homolog
- Fanconi anemia group M protein homolog
- Fanconi anemia group F protein
- Fanconi anemia, complementation group E
- Fanconi anemia group G protein homolog
- Fanconi anemia group D2 protein homolog
- Fanconi anemia group I protein homolog
Sequence:
MAQESADLASDCQSWLQKLSAWEQASSEETQKDTCLHLSGFQEFLRQMYEILKEMDSDAILERFPTIGQLLAKACWNPLILAYDESQKIVIWCLCCLMNKEPRTSAESGLNSWIRGLLSHVLSAFRFDMKEVCLFTKSLGYESIDYYPSLLKNMVLSLVSELRESHLNGLSTQSRMAPERMMSLSEVCVPLVTLPDMEPLVEALLTYHGHEPQEVLAPEFFEAVNEAFLSEKIVLPTSSVVSLWFRHLPSLEKATLHLFEKLFSSKIICLRRMECCIRESFLPQAACQPAIFRIVDEMFRFVLLETDGAPEVLAALQVFTSCLVEALKKENKQLTFALRTYFPYGAPCLAAALSQHPEAIPQGHRLQPLLHISQLLREAVEDCTRGSPRNPFESWFLFVHFGGWVDLAVAELLLREEAEPPAGLLWLLVFYYSPQDGSQQREQSMVELKVLINRLLMLLRSGPLSATDLQEAAESPSGDPRPPVCGQLVRRLLLSLLLWTPEGHAIVWEAVTHGPTFEITGPGCCPRIWRSTRPQHRPRAHLCCTEMAHTDAVIHEIIGFLDQTLYRSQHLCVEASRKLARDLLKELQAQV
Protein: DnaJ homolog subfamily C member 2 (Q94216)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Heat shock protein hsp-1
- Heat shock protein 110
- DUF148 domain-containing protein
- Heat shock protein 70
- DNaJ domain
- Heat shock protein 70
- Zinc finger CCCH domain-containing protein 15 homolog
- Zinc finger CCCH-type with G patch domain-containing protein
- Large ribosomal subunit protein eL31
- Heat shock protein hsp-6
Sequence:
MTTGNLQVAIYGFTARSRAFEPAGICYETRLIRDKLTLGHCTLPIYKNSPVAKPVTEQQRKKSSEEPAELRKDLFDADNEKYEKYLMKLDPNDCKNQDHYKVLGLSKLRWQATSDEIRFCYRQKVLKHHPDKKKHRGIVMEKEEYFTCITKAYEQVGMSDVKRQAFDSVDHKFNDIIPNEKSINHNNFYNELAPVFQLNSRWSNIKPVPELGKSDATREDVENFYDFWFNFQSWREFSYLDEEDKERGEDRYERREMEKQNKAERERRRKEEAKRIRKLVDIAYAKDPRIIKFKKEQQAKKDKAKEDKQRAIREKQEAIDREKREKEEAEAKQKEEADRKAKEEREREKKERDIAKKAMSQQRKRLKKLADEAGHWTENPRDKLTEMERIERICIGFTVDQLRELCEKVESLSIASEIQTALTDAEILKKEAAGAKVTITEDKNKENEKQADKETWTSEEIQLLVKASNTFPPGTVERWVQIADYINEHRKDSTGLPPKTEKQVIKQCKAVQTMNVKLPSTTQNQLGTALPDEDVWSATEQKTLEDAIKKHKSSDPERWEKISTEVGTKSKKACIRRFKYLVQMVKNKK
Protein: Exocyst complex component 3 (Exocyst complex component Sec6) (Q19262)
Organism: Caenorhabditis elegans
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Interaction partners:
- Exocyst complex component 5
- Exocyst complex component 1
- Exocyst component Exo84 C-terminal domain-containing protein
- Exocyst complex component 6
- Exocyst complex component 2
- Exocyst complex component 4
- Exocyst complex component 7
- Rab8
- Vacuolar protein sorting-associated protein 53 homolog
- RNA polymerase II-associated protein 3
Sequence:
MDVDVEEAALEQVAALLQRPDQLEKLPELKKRADRKKLAVEAMLRTGVQGQLEGIRTAIAHLQTASDDITAISQGVHDIRERLGPFPQLKEKLRELRDANARHGQYAAAMENLKHIFNLQTTLQEIRDALDDEKSGGNLLLAHKHIMDLERARDELLAEVHKMSGTNTEKEQMLLVNFFKGVDSVVAELSKNMWFILGRTLEMVKGNEQGGGPQQVVTCLRIVEREERIDKFYMEARSKNSSAFVPPGRPRNWKEKALRSLEKTVSNRVDGNQLEDRSLNKAWLARYLEVCKNVIMDDLQLAKVAIPCFPPDWQIYDRYVHMYHTSVCRRLREVASEHLEKSELVQLMSWIKFYASEDMLGHPKLRINAQAILQDSPVLSRSTLNQLCDQFVEMSRDDLKLWLKNTVSHETHDWYKNLRPSEDNHGYFYTDLPNTVFGMLKDTVTLAKEVSVEVIPSIINLTIQEFNELAGKYRDAFTAYKTDYFAERSKYQEFTSNIIAIANNLHTCIESTEKYKQQIRLSMEGEQNAAAAMTTPLASGRRTAVRQQQLIENMDALNTKWSNAASVAVNYLREEVITDIAPSLVEIFSKKWLTGSAALETVCMTISDYYHDHKHLRPVTRSTLLMDLQFRIVSEYLKAIETKRVSLNSYEERALAGKRMKADVVRLDNLYAEFATSSDMADQLPLLTSIVAAAGDVISLKDKSLLSLEATSFARKFPNCPAELLSAVIATRDDISGSEARSLASEVLQHVQFHPKDQIFDQLFALRQQENSERLPNLGMANMFKADFMSMLKRDA
Protein: TBC1 domain family member 3G (Q6DHY5)
Organism: Homo sapiens (Human)
Function: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associated with lipid rafts. {ECO:0000250}.
Interaction partners:
Sequence:
MDVVEVAGSWWAQEREDIIMKYEKGHRAGLPEDKGPKPFRSYNNNVDHLGIVHETELPPLTAREAKQIRREISRKSKWVDMLGDWEKYKSSRKLIDRAYKGMPMNIRGPMWSVLLNIEEMKLKNPGRYQIMKEKGKRSSEHIQRIDRDISGTLRKHMFFRDRYGTKQRELLHILLAYEEYNPEVGYCRDLSHIAALFLLYLPEEDAFWALVQLLASERHSLQGFHSPNGGTVQGLQDQQEHVVATSQPKTMGHQDKKDLCGQCSPLGCLIRILIDGISLGLTLRLWDVYLVEGEQALMPITRIAFKVQQKRLTKTSRCGPWARFCNRFVDTWARDEDTVLKHLRASMKKLTRKQGDLPPPAKPEQGSSASRPVPASRGGKTLCKGDRQAPPGPPARFPRPIWSASPPRAPRSSTPCPGGAVREDTYPVGTQGVPSPALAQGGPQGSWRFLQWNSMPRLPTDLDVEGPWFRHYDFRQSCWVRAISQEDQLAPCWQAEHPAERVRSAFAAPSTDSDQGTPFRARDEQQCAPTSGPCLCGLHLESSQFPPGF
Protein: Hydroxyacyl-CoA dehydrogenase (E9PF18)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MGRAGLEAPPPPCGVTGTPGARGLQGRVGPRPQSLAFRGCPPRASSLPGSPRCRRRCHTMAFVTRQFMRSVSSSSTASASAKKIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENLKAGDEFVEKTLSTIATSTDAASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERDFQTCGDSNSGLGFSLKGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKYK
Protein: Nuclear pore complex protein NUP43 (Nucleoporin 43) (Q24JJ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP133
- Protein SEH1
- Nuclear pore complex protein NUP85
- Protein transport protein SEC13 homolog B
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP96
- Nuclear pore complex protein NUP62
- Nuclear pore complex protein NUP214
- Protein RAE1
Sequence:
MEMMQDSFQVHRIPQSKYVDGVRWLPQASALNRFFATASYDADCDSSSIEIQSLDPNPRGNHNTNPLIESLSSWTSPSRVSSLEVAGNGGGGGSFKPMVSAATSSGSLHVLMIDLVEGAAIEEFYAAEGERFHVGRVEGVDWREGGECVTVGEDGRVNVVKIVNGEGLRYRKVFDGNGLVAYRAVKWASPTEFVTGGYGFGLQLWDQRKSGEAVSQLKGNWFQGKTSAIVHSIDIHPSRKHTCIAGGSSGTVFAWDLRWPQQPIVLSGVGASENINNPLSESEVWEVQYDSYTKSNVSSSRILPVMTCSEDGILGIIEQGEEPIELLAEPCAINSFDIDRQNPQDVICSLEWESIAVFSRP
Protein: Photosystem II D2 protein (PSII D2 protein) (EC 1.10.3.9) (Photosystem Q(A) protein) (P56761)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383}.
Interaction partners:
- Expressed protein
- Photosystem II reaction center protein Z
- Photosystem II reaction center protein K
- Photosystem II reaction center protein L
- Photosystem II reaction center protein I
- Photosystem II reaction center protein J
- Photosystem II reaction center protein H
- Photosystem II CP47 reaction center protein
- Cytochrome b559 subunit beta
- Photosystem II protein D1
Sequence:
MTIALGKFTKDEKDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWAFVALHGAFALIGFMLRQFELARSVQLRPYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL
Protein: Isoflavone reductase homolog A622 (NgA622) (EC 1.3.1.-) (B7UEU8)
Organism: Nicotiana glauca (Glaucous tobacco) (Tree tobacco)
Function: NADPH-binding protein. Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Reductase involved in a late step of tobacco alkaloid biosynthesis. Triggers either the formation of a nicotinic acid-derived precursor or the final condensation reaction of tobacco alkaloids.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P52580}.
Interaction partners:
Sequence:
MVASEKSKILIIGGTGYIGKYLVETSAKSGHPTFVLIRESTLKNPQKSKLIDTFKSYGVTLLFGDISNQESLLKAIKQVDVVISTVGGQQFADQVNIINAIKEAGNIKRFLPSEFGFDVDHAHAIEPAASLFALKVKIRRMIEAEGIPYTYVICNWFADFFLPNLGHLDAKTPPRDKVVIFGDGNPKAIYVKEEDIATYTIEAVDDPRTLNKTLHMRPPANILSFNEVVSLWEEKIGKTLEKIYLSEEDILEIVKEGPLPLRTNLAICHSVFVNGDSANFEVQPPTGVEATELYPKVKYTTVDEFYNKFV
Protein: Uncharacterized protein (Q381P0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSFKDAQLIENTSDIEGSRRTIEARIGNSLRDAQYKLTSSAAHDLPEAMADIYMALTSLTAYLSLPNGSPKAAATANRIAKLWRTIIYYYKRREGLAPESTAGSSAPSETDAMDHTLSPHTMQQGFTTYKDTDVNLEHLREEFHKTKCERDSTVKELESVRQKLQNYEENSQLTAILQNEHERIQQENSALKAALHEHERKLQRSTTQLQQSQLTLQEKEIEMTKTKEEYERRLREIKIKENNIDKEEQAALRENIKILHQTLRDMIQNTEAAEVKQGTLTLADIQTSHQEQIIAMKLTLAAQCEREQELSNIIKAKEQQHHKHIENLNTKKQNEQKKYKEKLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVVQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVAQENHEGMEKLHREQLLALEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVVQENHEGMEKLHREQLLTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEKVVQENHEGMEKLHREQLSTLEIAMEEQRVRYTHEVESLRTELQNERERVQASEMCVTRLVDIGKEQYCCEVDVDVVDMSRRLFVDDMKISFCSDEEQLVNTVFSQFSCSDRGVFSLVGCPAVSSFRRGSVAKQLRVGVRNVLDKLRSFEFDVSDAVVLSQQRMLFIQNVTKKLGIVPGAKLSVDDKFYSPVTSKSKCSAPELPFSFGPLKALCDVVGVGLQRAISFTAVWDEESRRLVEVVEALRHNILVVASLCSWYSQRFDAWGKLTGFTVAKLTVALQKLQYCLLRSLPLNVCDAPIFEACFLLVNDSRKTLCGIGQKLTATADTPLSSSCSVDGGAGIASSVLLSKYRKQQEVRPPVTLDAATLPQLPFLLSSRDGEDVSTPIKSRDNATVNGRSDEKFDGYTNPFGVTPSGCGAKFGPVEEGTTVEAAAEGRQGPFKKKQRRELRLKFIG
Protein: Ubiquitin carboxyl-terminal hydrolase 2 (EC 3.4.19.12) (41 kDa ubiquitin-specific protease) (Deubiquitinating enzyme 2) (Ubiquitin thioesterase 2) (Ubiquitin-specific-processing protease 2) (O75604)
Organism: Homo sapiens (Human)
Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (By similarity). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (By similarity). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and BMAL1 (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O88623}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:0000250|UniProtKB:Q5U349}. Membrane {ECO:0000250|UniProtKB:O88623}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O88623}. Note=Predominantly expressed at membranes. {ECO:0000250|UniProtKB:O88623}.
Interaction partners:
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- E3 ubiquitin-protein ligase Mdm2
- Protein Mdm4
- Zinc finger-containing ubiquitin peptidase 1
- Ubiquitin carboxyl-terminal hydrolase 28
- Ubiquitin carboxyl-terminal hydrolase 14
- Receptor-interacting serine/threonine-protein kinase 1
Sequence:
MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAASLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPLLRPDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLSYLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPRNLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRKGSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETGKGQAPGPSRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
Protein: Asator, isoform K (EC 2.7.11.1) (Asator, isoform L) (L0MLN1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSEDLLQPGHVVKERWKVVRKIGGGGFGEIYEGQDLITREQVALKVESARQPKQVLKMEVAVLKKLQGKEHVCRFIGCGRNDRFNYVVMQLQGKNLAELRRAQPRGAFSLSTTLRLGLQILKAIESIHSVGFLHRDIKPSNFSVGRLPYNCRRVYMLDFGLARQYTTGTGEVRCPRAAAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVNGQLPWRKIKDKEQVGLTKEKYDHRILLKHLPSDLKQFLEHIQSLTYGDRPDYAMLIGLFERCMKRRGVKESDPYDWEKVDSTAIGNISATGNPSIPIKSDYMHGNITQMTVAASNASGTEYIRKRAEIETAHITATDPLNIKEKVDKNCNATSLAQPAKGSGEPMVQHGNAANNQNITSKGLQQQSTLTNSQVAIANIQSAPSMIEREDVQYTKLEEGAPTKFITMKPNGECDNVDIAAKCIFEQKHVEANDDIVGRASLSGVEQHYKSQIKKHNSPEIANKQIQRTGTVTNDKTSEVNRSTEEQKSTFGRLRVLTAPPMSVHDLPSGGGHSHQVSDLSGKQDPYAATSNAAPIGINSSSTKFGSQHGQIFGLAAMPPINRRSATSTNLRPSSSASQRINSGSTIGGAVGNGSNTARSSVAGDHSVTQFALIDDENVSALQQVTKGGALTLASQWKSQFDDSEDTTDNEWNREHQLQPNLEQLIKLDISLPLNEAKPFPQHGVAGTGKLINPPGEAKGRPKRYTLNITGIENYEALRISIPNCWSEPAMGNVLRKGLEPPAVQQAAFDDTVYRMDIARNVCVRETYSEITHLARPSTSSVLRNRLPSPFKKDSALQLNSTNDSLDKSRHRNSLPNVSVNDIFDDLQMKLNLDLGSAIQENNCCISGRLEIRVIPKDTSHPDDSVYYDAMGAVKNTPTANEGHDHSDQAVNNCDEMEATSAVIAFPNKSISKIMSPPGRDATEERTGASLCSLYSAGVNKLKLNGNTAPRTQFKKGSTDGFGENESEFDFPLLNPSKIPVRQSKCASWAGADFISASKPLESAEVPQEIPYHPQSDTTYSVIDSIPVRKTTYSIALECPPNISDLTPGLSYFYCNIVVPLRLFSILLTES
Protein: Sodium-hydrogen exchanger NHE2 (Q9NGU8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
YMLPPIILDAGYFMPNRLFFDNLGTILLMAVVGTIFNIATIGGSLYACGKMGIYGESETPGLMDVFLFASL
Protein: Chitinase domain-containing protein 1 (Q9VLS0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD44003p
- BcDNA.GH08312
Sequence:
MRAPDALLLRVALLLLLLTTVRGTLAPDSHKSKSKTKESALRGGPQDQDVFDLGLVSPEPLAKDIVSNHRGYFKETGLRRFNGTTLGYVTPWNSHGYDVAKIFAKKFDIISPVWLQIVKQGDRYAVAGTHDIDAGWLTDVRRKGKQVHNQRTVKVFPRFIFDHFTDRDIKLLLSDAQERTKVNDVLIKCCKDNGFDGLVLEVWSQLAGRIDDKILYTLVLQMAKELQKQQLRLILVIPPFRKETGHLFGEKHMDKLFKHIYAFSLMTYDFSSVQRPGANAPLYFVRKAVETIAPEGCADMTAKRAKILLGLNMYGNDYTPDGGGPITFSQYLDLVRHVKKHLTYDERDVENFFEIKNDDGRHIVFYPTLYSINERIKLAQELGTGISIWELGQGLNYFYDLF