wanglab/gogpt-training-data huggingface dataset:
Protein: dextransucrase (EC 2.4.1.5) (A5VL73)
Organism: Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri)
Interaction partners:
Sequence:
MNLPTIPNTNVQTDNNWYLVDNGIAQSGVQQWAGSYYYFNPSTYLRVDNEYRQSQWGDWYMFGKDGRAVTGLYDYNGNTYYANPTTYLRETNKYISTSKGNMLLGNDGAALSGIQSVNGKYYYFDPVTHLQANKENYVQSQWGDWYLIGNDGQVLSGVQQWAGTYYYFDPTTYLRVDNDYRQSQWGLWYMFGHDGRIVTKVYPWAGTYYYFDPTTYLRVDNAYLQSQWGDWYLFGNDGRIQSGVQRWAGTYYYFDPTTYLRVDNDYVTSQWGSKYMFGPDGRIVTGLYKWSKNNQLYYFDPVTYLAVTNNYIKANNGNWYLFTADGTAASKVAPWAGSYYYFDPVTHLRVDNAYVQSQWGDWYMFGPDGRIVTGLKEWYGSYYYFDPTTYLKVTNKWIDNKYFGPDGRQAISSLENINNKFYCFDGNGQIIRNQFKKIDTHTYYFGSDGAALVGKQTIDGKNYHFASNGQLLGNLYGKIVDGKFNIYDSLSNKLIKTLDSGDWENMAYSQDSSSINNTDGYLSYSGWYRPYGTSQDGKTWYKTTASDWRPLLMYTWPSKDVEAKFIKYFVDNGYTNTDYGLTKDNVTNLSQDTDTQTLNKYARNLRFVIEKSIAANKSTGPLANDINKFMLTIPELSAKSELPVEYSNGYVPDVSGSIDNNQLIFINNNSDNQAKGNTSYADSNYRLMNRTINNQTNNDNSDQSPELLVGNDIDNSNPAVQAENFNWEYFLLNYGKLMKYNADGNFDGFRVDAADNIDADVLDQLGQLVNDMYHTKGNQENANNHLVYNEGYHSGAARMLNDKGNPELFMDAGYFYTLENVLGQAENKRDNVNNLITNSVVNRANDITENTATPNWSFVTNHDQRKNVINQIIIDNHPNIPDIMANSYKSTYAQKAWDEFYADQAKADKKYAQYNLPAQYALLLSNKDTVPQVYYGDLYKETDQYMKTKSMYYDAITTLMKARGEFVNGGQTMTKVNDNLITSVRYGKGVVDVSSNGTDPLSRTTGMAVIVGNNPSMSEQVVAINMGLAHANEQYRNLIDSTADGLTYNSNGSVNPSVLTTDSKGILRVTVKGYSNPYVSGYLSVWVPLINGTQNARTSAQEVRNVPGKVFTSNAALDSHMIYEDFSLFQPEPTTVNEHAYNVIKDNVALFNQLGITDFWMAPSYTPFNTSRYNEGYAMTDRYNLGTADNPTKYGNGEELSNAIAALHQAGLKVQEDLVMNQMIGFSTQEAVTVTRVDRDAKQLSVDGQTFADQIYFGYTRGGGQGQQDYGGKYLAELKQKYPDLFTTKAASTGVAPDPNTRITEWSAKYENGTSLQNVGIGLAVKMPNGYYAYLNDGNNKAFATTLPDAISSADYYANQENI
Protein: Uncharacterized glycosyltransferase YaiP (EC 2.4.-.-) (Q47536)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized outer membrane usher protein YhcD
Sequence:
MKTWIFICMSIAMLLWFLSTLRRKPSQKKGCIDAIIPAYNEGPCLAQSLDNLLRNPYFCRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQKNTGKGGALMNGLNYATCDQVFLSDADTYVPPDQDGMGYMLAEIERGADAVGGIPSTALKGAGLLPHIRATVKLPMIVMKRTLQQLLGGAPFIISGACGMFRTDVLRKFGFSDRTKVEDLDLTWTLVANGYRIRQANRCIVYPQECNSPREEWRRWRRWIVGYAVCMRLHKRLLFSRFGIFSIFPMLLVVLYGVGIYLTTWFNEFITTGPHGVVLAMFPLIWVGVVCVIGAFSAWFHRCWLLVPLAPLSVVYVLLAYAIWIIYGLIAFFTGREPQRDKPTRYSALVEASTAYSQPSVTGTEKLSEA
Protein: DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2 homolog) (Nuclear protein BM28) (P97310)
Organism: Mus musculus (Mouse)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division. Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P49736}. Chromosome {ECO:0000250|UniProtKB:P49736}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000250|UniProtKB:P55861}.
Interaction partners:
- Cell division control protein 45 homolog
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM3
- Origin recognition complex subunit 2
- Cell division cycle 7-related protein kinase
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM7
- DNA replication complex GINS protein PSF2
Sequence:
MAESSESLSASSPARQRRRISDPLTSSPGRSSRRADALTSSPGRDLPPFEDESEGLLGTEGPMEEEEDGEELIGDGMERDYRPIPELDVYEAEGLALDDEDVEELTASQREAAERTMRQRDREAGRGLGRMRRGLLYDSSEEDEERPARKRRHVERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLPQLSMVKYNCSKCNFVLGPFCQSQNQEVKPGSCPECQSAGPFEINMEETIYQNYQRIRIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTANGFPVFATIILANHVAKKDNKVAVGELTDEDVKMITGLSKDQQIGEKIFASIAPSIYGHEDIKRGLALALFGGEPKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYIEKVSSRAIFTTGQGASAVGLTAYVQRHPVSREWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSLTFSENVDLTEPIISRFDVLCVVRDTVDPVQDEMLARFVVGSHVRHHPSNKKDEGLTNGGTLEPAMPNTYGVEPLPQEVLKKYIIYAKERVRPKLNQMDQDKVARMYSDLRKESMATGSIPITVRHIESMIRMAEAHARMHLRDYVMEDDVNMAIRVMMESFIDTQKFSVMRSMRKTFARYLSFRRDNNDLLLFILKQLVAEQVTYQRNRFGAQQDTIEIPEKDLMDKARQINIHNLSAFYDSDLFKFNKFSRDLKRKLILQQF
Protein: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase 1) (Glutamine:fructose-6-phosphate amidotransferase 1) (GFAT 1) (GFAT1) (Hexosephosphate aminotransferase 1) (P82808)
Organism: Rattus norvegicus (Rat)
Function: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes BMAL1 and CRY1. Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and its effects on hyaluronan synthesis that occur during tissue remodeling (By similarity).
Interaction partners:
- Glucosamine 6-phosphate N-acetyltransferase.
- Glucose-6-phosphate isomerase
- N-acetylglucosamine-6-phosphate deacetylase
- Glutamine synthetase
- Hexokinase-3
- Hexokinase-2
- Glucosamine-6-phosphate isomerase.
- Glucosamine-6-phosphate isomerase
- Mannose-6-phosphate isomerase
- Amidophosphoribosyltransferase
Sequence:
MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGLDGGNDKDWEANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNWESQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTGKDKKGSCGLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE
Protein: Thyrotropin receptor (Q0MWV3)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Cell membrane {ECO:0000256|RuleBase:RU361222}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361222}.
Interaction partners:
Sequence:
MMMMKMKKIMKMLLCVLDCVCVSQAEVAMVNSGTTFTYLCMGNTITHMPTHIPKNTTNLEFKQTHIRVFPREAFTNLLQLTAIVLTENGMLESIGAFAFANLPRLTEITITKSKHLVVIHHQAFMGLPKLSHLTICNTGLRVLPNFSRIHSTALTFLLDLQDNVHIVIIPSNAFLGLTTNTIDELRLTKNGISEVESHAFNGTKIHKLFLMGNLQLSHMHNNSFKGAEGPGFLDISRTALSSLPESVLGEVEHLSAVSVFSLRALPPLSLFTKLRQANLTYPSHCCAFHKHQRNRTFRMNSACFKPGAQDNLHFFMDFCLNWTSVACSPAPDAFNPCEDIMGSAPLRVLIWIISVLALLGNTIVLLVLLGSRAKMTVPRFLMCHLSFADLCMGVYLVVIATVDVRTRGLYYNHAISWQTGAGCDIAGFFTVFASELSVFTLTAITLERCHTITHALRLDRKLRLRHACAVMATGWAFSCLAALLPTVGVSSYSKVSICLPMDVESLPSQVFVMFLLLLNVVAFLCVCVCYLSIYLSVRNSSSPPASAETRMAQRMAILIFTDFLCMAPISFFALSAALKLPLITVSDSKLLLVLFYPINSCANPFLYGLCTRTFRRDFFLLAARYGLFTTKAQIYRTESFSVQQAAWIQMSPKTSHGTLC
Protein: Y-box binding protein 1 (C9J5V9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSEAETQQPPAAPPAAPALSAADTKPGTTGSGAGSGGPGGLTSAAPAGGDKKVIATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQGAEAANVTGPGGVPVQGSKYAADRNHYRRYPRRRGPPRNYQQNYQNSESGEKNEGSESAPEGQAQQRRPYRRRRFPPYYMRRPYGRRPQYSNPPVQGEVMEGADNQGAGEQGRPVRQNMYRGYRPRFR
Protein: Mannan polymerase complex subunit MNN9 (P53697)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for the addition of the long alpha 1,6-mannose backbone of N-linked glycans on cell wall and periplasmic proteins.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:P39107}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P39107}.
Interaction partners:
- Alpha-1,6-mannosyltransferase
- Alpha-1,6-mannosyltransferase
- Alpha-1,6-mannosyltransferase
- Initiation-specific alpha-1,6-mannosyltransferase
- Van1p
- Anp1p
- Alpha-1,2-mannosyltransferase MNN24
- GDP-mannose transporter
- Mitochondrial thiamine pyrophosphate carrier 1
- Alpha-1,2-mannosyltransferase MNN21
Sequence:
MVHYRNRYLNYIRRKPLALLAPITLLVVIYFYFFSAHGFSSNKQKYNYNKKSRGWFYKNRDTVILKDLPKNHISHYDLNKLTASKDALNKREEVLILTPMSKFLPEYWENINKLTYDHSLISLGFIFPRTTQGDDALKELENALKKTKREKRLNFKKITILRQDSNSLQSQLEKDRHAFKVQKERRSMMALARNSLVFSTILPSTSWVLWLDADIVETPVTLIQDLTGHNKPVVSANVHQRFINQDTKQPDIRPYDFNNWVESEEGLKLAASLPDDEIIVEGYSEMVTHRALMAHFYDPKGDPSTEMTLDGVGGGAVMVKADVHRDGAMFPSFPFYHLIETEGFAKMAKRLGYEVYGLPNYLVFHYNE
Protein: Si:dkey-199l1.2 protein (A2RUY7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MVMLPRNNTYLFSYTRVFPAIEYAKKALREADAYAGLRFNVRFENSACGMDALYALVDRQKDERPDLVLGPVCEYAASSVTRVASHWNIPVISAGALATGFNSKTPEYSHLTRIAPTYLKMAETFQAIFGHFGWRTAYLIYDDDKDERNCYFTMEGVFTVLSEYHISTDFAVLNSNEERVDPDGIITSVYGSEVVIMCSKADIVRDLMLAAHRRKLTSDSHIFFNIELFNSSSYGDGSWRRRDKYDDEARAAYSFLNTVTLLRSTKPEFEDFSIEMKKSLQQSKIPICEDCSAVNMFMEGFHDALLLYAIALREVKSKGLTKKNGLEITHSMWNRTFEGIAGQVSLDANGDRNGDFSVVRMTDPESGKHETVMNYFGTNGSFQILPGFKREWFSLRTIPPPKPLDPSCGLGVSAVTGIIVGGILGTALLLAFYFFRKNYRITIERRTLREECDIGKHRQLREDSIRSNFSAA
Protein: Large ribosomal subunit protein uL30-like 1 (60S ribosomal protein L7-like 1) (Q9D8M4)
Organism: Mus musculus (Mouse)
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein eL33
Sequence:
MAEEGERKKIPLVPENLLKKRKAYQALKATQAKQALLAKRERKGKQFRFRRLESFVHDSWRQQRDKVRVQRLEVKPRALEVPDKHPLAFVIRMERIEGVSLLVKSTIMKLGLKKLFSGVFVKVTPQSVRMLRTVEPYVTWGFPNLKSVRELILKRGQAKINNKTVPLTDNTVIEEHLGRFGVICLEDLIHEIAFPGKHFQEVSSFLCPFLLSVARHATRNRVGFRKEMGSPGYRGDRINQLIRQLN
Protein: Large ribosomal subunit protein P1 (60S acidic ribosomal protein P1) (Q6P5K5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein eS25
Sequence:
MASVSELACIYSALILHDDEVTVTEDKLNALIKAAGVTIEPFWPGLFAKALASVDIGSLICNVGAGGGAAPAAAAGAAAPAGGDAPAKEEEKKEEKKEESEESDDDMGFGLFD
Protein: C3H1-type domain-containing protein (Q586A3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGFPSGSGLDKFSDLQSFIRASFPTHSGDFTTDTAIRVLAAYLSVSPWEVSRVVDMSRPIHNMENLEEYVSCVVSSLQKQGEVRTRAVTSTLTGRVGSSPAEVIHTEGNCMRSPTVKPHTFGKKKLCKQFCKTGLCAFGSRCLFHHEEPYRGDTWSVSSDTCITDRNFIEPKSTESSSTVPTGAGRELFTELASPSNNFSLPTERRRVTQPINKVTAQGQTDETGIGFAPPGTQLPGVYVMPLSVRSGELYVYTPVQFHVSFPICLPPPGASH
Protein: Suppressyn (Endogenous retrovirus group 48 member 1) (NDUFV3 antisense RNA 1) (endogenous retrovirus group Fb member 1) (M5A8F1)
Organism: Homo sapiens (Human)
Function: May play a role in trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development. May negatively regulate cell-cell fusion by interacting with SLC1A5, the probable receptor on the cell surface of the fusogenic syncytin-1/ERVW-1.
Subcellular location: Secreted {ECO:0000269|PubMed:23492904}. Note=Also found in cell lysates.
Interaction partners:
Sequence:
MACIYPTTFYTSLPTKSLNMGISLTTILILSVAVLLSTAAPPSCRECYQSLHYRGEMQQYFTYHTHIERSCYGNLIEECVESGKSYYKVKNLGVCGSRNGAICPRGKQWLCFTKIGQWGVNTQVLEDIKREQIIAKAKASKPTTPPENRPRHFHSFIQKL
Protein: Tyrosine-protein phosphatase non-receptor type 4 (EC 3.1.3.48) (Testis-enriched protein tyrosine phosphatase) (Q9WU22)
Organism: Mus musculus (Mouse)
Function: Phosphatase that plays a role in immunity, learning, synaptic plasticity or cell homeostasis. Regulates neuronal cell homeostasis by protecting neurons against apoptosis (By similarity). Negatively regulates TLR4-induced interferon beta production by dephosphorylating adapter TICAM2 and inhibiting subsequent TRAM-TRIF interaction. Dephosphorylates also the immunoreceptor tyrosine-based activation motifs/ITAMs of the TCR zeta subunit and thereby negatively regulates TCR-mediated signaling pathway. May act at junctions between the membrane and the cytoskeleton.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Glutamate receptor ionotropic, NMDA 2A
- TIR domain-containing adapter molecule 2
- Glutamate receptor ionotropic, delta-2
Sequence:
MTARFRLPAGRTYNVRASELARDRQHTEVVCNILLLDNTVQAFRVNKHDQGQVLLDIVFKHLDLTERDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPYNLNFRVKFFVSDPNKLQEEYTRYQYFLQIKQDILTGRLSCPCNTAALLASFAVQSELGDYNQSENLAGYLSDYSFIPNQPQDFEKEIAKLHQQHVGLSPAEAEFNYLNAARTLELYGVEFHYARDQSNNEILIGVMSGGILIYKNRVRMNTFLWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKTLWKACVEHHTFFRLDRPLPPQKNFFAHYFTLGSKFRYCGRTEVQSVQYGKEKANKDRVFARSPSKPLARKLMDWEVVSRNSLSDDRLETQSLPSRSPPGTPNHRNSSFTQEATRVRPSSVGHLVDHVVHMSPSEDFVSQRSPSSTQANSIVLESSPSQETPEDGQPPALPPKQSKKNSWNQIHFSNSQQDLVTHTNESFDVPSSPEKSTPNGGIPHDNLVLIKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCEKHSGELVLLVRPNAVYDVVEEKLESEPDFQYIPEKAPLDSVHQDDHSLRESMIQLAEGLITGTVLAQFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVLLKGNEDYINANYINMEIPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEEGFVKPLTTSSNK
Protein: Tyrosine ammonia-lyase (CmTAL) (EC 4.3.1.23) (Tyrosine 2,3-aminomutase) (EC 5.4.3.6) (Q1LRV9)
Organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
Function: Has ammonia-lyase and, to a lesser extent, aminomutase activity. Catalyzes the rearrangement of L-tyrosine to R-beta-tyrosine and S-beta-tyrosine. Does not accept L-histidine or L-phenylalanine as substrates.
Interaction partners:
- Urocanate hydratase
- Imidazolonepropionase
- Histidinol-phosphate aminotransferase
- Histidinol-phosphate aminotransferase
- Aminotransferase
- Phenylalanine-4-hydroxylase
- Formiminoglutamate deiminase
- N-Formylglutamate amidohydrolase
Sequence:
MPHAHPADIDGHHLTPDTVAAIARGQRAAIVPEPVLGKVADARARFEQVAAANVPIYGVSTGFGELVHNWVDIEHGRALQENLLRSHCAGVGPLFSRDEVRAMMVARANALARGYSAVRPAVIEQLLKYLEAGITPAVPQVGSLGASGDLAPLSHVAITLIGEGKVLTEDGGTAPTAEVLRERGITPLALAYKEGLALINGTSAMTGVSCLLLETLRAQVQQAEIIAALALEGLSASADAFMAHGHDIAKPHPGQIRSAANMRALLADSARLSGHGELSAEMKTRAGEAKNTGTGVFIQKAYTLRCIPQVLGAVRDTLDHCATVVERELNSSNDNPLFFEDGELFHGGNFHGQQVAFAMDFLAIAATQLGVVSERRLNRLLSPHLNNNLPAFLAAANEGLSCGFAGAQYPATALIAENRTICSPASIQSVPSNGDNQDVVSMGLIAARNARRILDNNQYILALELLASCQAAELAGAVEQLAPAGRAVFAFVRERVPFLSIDRYMTDDIEAMAALLRQGALVEVVRGAGIELA
Protein: Gag-pol polyprotein (O16893)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTSETAAQFGIVPNLAHQSAEERARDAPRLPFLMKLNLLVEARGITSFEDLLQAKTEVEKELEVGKQKDLAEDKENDVESEERLPEEPKAKKAKKSPKIKGFPNLVRRNARRGMGVLGGETWTEEIVMG
Protein: Pre-mycofactocin glycosyltransferase (EC 2.4.1.-) (P9WMX1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of the enzyme cofactor mycofactocin (MFT). Acts as a glycosyltransferase that catalyzes the oligoglycosylation of pre-mycofactocin (PMFT), adding up to nine beta-1,4-linked glucose residues.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mycofactocin precursor peptide peptidase
- Peptide chaperone MftB
- Mycofactocin maturase MftC
- Pre-mycofactocin synthase
- Probable dehydrogenase
- Mycofactocin precursor peptide
- Uncharacterized protein Rv1354c
- Putative mycofactocin biosynthesis transcriptional regulator MftR
- Sulfotransferase
- Tetratrico peptide repeat group 5 domain-containing protein
Sequence:
MTATRLPDGFAVQVDRRVRVLGDGSALLGGSPTRLLRLAPAARGLLCDGRLKVRDEVSAELARILLDATVAHPRPPSGPSHRDVTVVIPVRNNASGLRRLVTSLRGLRVIVVDDGSACPVESDDFVGAHCDIEVLHHPHSKGPAAARNTGLAACTTDFVAFLDSDVTPRRGWLESLLGHFCDPTVALVAPRIVSLVEGENPVARYEALHSSLDLGQREAPVLPHSTVSYVPSAAIVCRSSAIRDVGGFDETMHSGEDVDLCWRLIEAGARLRYEPIALVAHDHRTQLRDWIARKAFYGGSAAPLAVRHPDKTAPLVISGGALMAWILMSIGTGLGRLASLVIAVLTGRRIARAMRCAETSFLDVLAVATRGLWAAALQLASAICRHYWPLALLAAILSRRCRRVVLIAAVVDGVVDWLRRREGADDDAEPIGPLTYLVLKRVDDLAYGAGLWYGVVRERNIGALKPQIRT
Protein: Protein neuralized (P29503)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in neurogenesis. Interacts with other neurogenic proteins in the specification of the neuroblast versus epidermoblast cell fate.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Bearded
- E3 ubiquitin-protein ligase mind-bomb
- Neurogenic locus protein delta
- Protein serrate
- FI19443p1
- BARBU
Sequence:
MGLSDIPANYMQGSHPHLTLHPQQQHHQNQQHLQHLQQMQQLHNAMPTPAQQAAQVLAMESNELLMSTKDKLSSKKKMHLLKKIKKRFGLVRRSPSSCPGPNNLPPLQFHSVHGDNIRISRDGTLARRFESFCRAITFSARPVRINERICVKFAEISNNWNGGIRFGFTSNDPVTLEGTLPKYACPDLTNRPGFWAKALHEQYCEKDNILYYYVNGAGDVIYGINNEEKGVILTGIDTRSLLWTVIDIYGNCTGIEFLDSRIYMYQQQPAAIPMATVPAQQQQMPQPAANASSALNSHHPHQQSRRSLPGHTAAIEHDLERHVMPSLQSLHLAGNGGSVASVEQAAIAHDLANGLPPLRYNANGRLIPVPFHNTKGRNVRLSQDRFVASRTESDFCQGYVFTARPIRIGEKLIVQVLKTEQMYVGALALGLTSCNPAMLQPNDLPNDSDFLLDRPEYWVVSKDIAAAPQRGDEIAFFVAPNGEVSISKNNGPAVVVMHVDQSLQLWAFLDVYGSTQSLRMFRQQLPNMVAYPSQPQVNVNASSSSACNAASTSRMLPMTESMSSLNAGATAKLLHHPSQLSVAQSTSTLASAGGVNGSRMISMPSNGDILQIQPNGGGTVLVVNLPPASSSHDINGQLAARPTATVTSSGVLAGACSSGTLISTTSSQYIEQPIANSTNNAANKWKDSLSDQQSTDSSAECTICYENPIDSVLYMCGHMCMCYDCAIEQWRGVGGGQCPLCRAVIRDVIRTYTT
Protein: Beta-glucosidase 26, peroxisomal (AtBGLU26) (EC 3.2.1.21) (Protein PENETRATION 2) (O64883)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses beta-glucosidase activity toward 4-methyl-umbelliferyl-beta-D-glucoside in vitro. Possesses myrosinase activity toward indol-3-yl-methylglucosinolate (I3M) and 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) in vivo. Component of an inducible preinvasion resistance mechanism that prevents penetration of the nonhost fungal species B.graminis and E.pisi. Involved in indole glucosinolate (IGS) activation during pattern-triggered immunity (PTI). Functions as myrosinase for the breakdown of flg22-triggered IGS. Required for both callose deposition and glucosinolate activation during pathogen-triggered resistance. During fungal attack, required for IGS activation that mediates broad-spectrum antifungal defense.
Subcellular location: Peroxisome {ECO:0000269|PubMed:16293760}.
Interaction partners:
- Splicing factor YJU2
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- At5g38980
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Beta-glucosidase 7
- Pathogenesis-related thaumatin superfamily protein
- Beta-glucosidase 8
- Beta-glucosidase 45
Sequence:
MAHLQRTFPTEMSKGRASFPKGFLFGTASSSYQYEGAVNEGARGQSVWDHFSNRFPHRISDSSDGNVAVDFYHRYKEDIKRMKDINMDSFRLSIAWPRVLPYGKRDRGVSEEGIKFYNDVIDELLANEITPLVTIFHWDIPQDLEDEYGGFLSEQIIDDFRDYASLCFERFGDRVSLWCTMNEPWVYSVAGYDTGRKAPGRCSKYVNGASVAGMSGYEAYIVSHNMLLAHAEAVEVFRKCDHIKNGQIGIAHNPLWYEPYDPSDPDDVEGCNRAMDFMLGWHQHPTACGDYPETMKKSVGDRLPSFTPEQSKKLIGSCDYVGINYYSSLFVKSIKHVDPTQPTWRTDQGVDWMKTNIDGKQIAKQGGSEWSFTYPTGLRNILKYVKKTYGNPPILITENGYGEVAEQSQSLYMYNPSIDTERLEYIEGHIHAIHQAIHEDGVRVEGYYVWSLLDNFEWNSGYGVRYGLYYIDYKDGLRRYPKMSALWLKEFLRFDQEDDSSTSKKEEKKESYGKQLLHSVQDSQFVHSIKDSGALPAVLGSLFVVSATVGTSLFFKGANN
Protein: Uncharacterized protein (Q38DG2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPEVGTQVYWYDFEDAPPPWKNEEELAKMLELSSSIEGPISDARHMLVQPREVYISMRTKLRNRQQPCNRYWSIVLEPHFGPLLGMNMVMRELKVEMVTREEAEEAVNGVVEEFNAMSQLYSATDGANDGLGTALSGKSAQAMDVKVAPFLEVVRKLCEPRNLDVVEWNRDELRRRGRIAFTDLLYHKRVVMIVDTSKPHFLICLPVTHKKRLTDKREVYCMQLLAPTASPVPWRRLTKYALVSPRAREFVIITITKRDSVKNSNLSIDVIGAAPEAKSASQKDLEDGEDGDYDDEEAEDEYDNDDDDDEEDDGDEDENSNDGDNRPRKRARVADSVDNSETDSLNNNEDYPFLDEIDAYERMRTGSAPIFSAEDRVLDDPLFNTPVATYRRASRATREGRDWVYRFTHQNDRNKLFALTN
Protein: RNA polymerase sigma factor RpoH (Heat shock regulatory protein F33.4) (RNA polymerase sigma-32 factor) (P0AGB3)
Organism: Escherichia coli (strain K12)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quickly degraded, leading to a decrease in the rate of synthesis of heat shock proteins and shut-off of the heat shock response.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00961}.
Interaction partners:
- Chaperone protein DnaK
- Chaperone protein DnaJ
- Chaperonin GroEL
- Protein GrpE
- RNA polymerase sigma-54 factor
- DNA-directed RNA polymerase subunit alpha
- ATP-dependent zinc metalloprotease FtsH
- ECF RNA polymerase sigma-E factor
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit omega
Sequence:
MTDKMQSLALAPVGNLDSYIRAANAWPMLSADEERALAEKLHYHGDLEAAKTLILSHLRFVVHIARNYAGYGLPQADLIQEGNIGLMKAVRRFNPEVGVRLVSFAVHWIKAEIHEYVLRNWRIVKVATTKAQRKLFFNLRKTKQRLGWFNQDEVEMVARELGVTSKDVREMESRMAAQDMTFDLSSDDDSDSQPMAPVLYLQDKSSNFADGIEDDNWEEQAANRLTDAMQGLDERSQDIIRARWLDEDNKSTLQELADRYGVSAERVRQLEKNAMKKLRAAIEA
Protein: Protein kinase C-like 1B (PKC1B) (EC 2.7.11.13) (P34885)
Organism: Caenorhabditis elegans
Function: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. Involved in neuropeptide secretion in motor axons. Likely to act via the extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) pathway in the signaling response to various sensory neurons; temperature, odor, taste, and osmolality. Its role in regulation differs depending on the neuron in which it is acting; thermosensation in AFD neurons, osmolality in ASH neurons, olfactory perception in AWA and AWC neurons. Promotes dauer formation mediated by the insulin/IGF pathway. Required for resistance to antimitotic toxins.
Subcellular location: Membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. Note=Associated with membranes and the cytoskeleton.
Interaction partners:
- Ras-like GTP-binding protein rhoA
- Protein kinase C-like 1
- Guanine nucleotide-binding protein subunit alpha
- Neuroendocrine convertase 2
Sequence:
MLFTGTVRVRVLEARQLRPTEWSRRFRQDEAATAAIDSYVNVDWDEYHIGKTQVRPKTNEPRWNEEFTASGVHQGKAIGFSVFHSCVMPPDDFVANTRIAFDQLKIGSANDIWVDLEPHGQLHVVVEMHGTNVEDVHSHNKTRVFKERTNAFNDRQRRGAMRRKIHEVTGHKFMALFLRQPTFCAHCKEFIWGIGKQGYQCQICTVVVHKRCHEDVVWKCPGNKADAVEELGKEIQETGAGRFNINMPHRFSVHSYKRPTFCDHCGSMLYGLINQGLQCSTCKLNVHKRCQRNVANNCGINAKQMAAELAQLGLTGDKMSIRSKKKPSIMTDTSTDISGSSNSENSGYLQQISEDDSGTTSSRSASKVPGGTLSIHDFTFMKVLGKGSFGKVMLAERKGTDEVYAIKILKKDVIVQDDDVECTMCEKRILSLAAKHPFLTALHSSFQTSDRLFFVMEYVNGGDLMFQIQRARKFDESRARFYAAEVTCALQFLHRNDVIYRDLKLDNILLDAEGHCRLADFGMCKEGINKDNLTSTFCGTPDYIAPEILQEMEYGVSVDWWALGVLMYEMMAGQPPFEADNEDDLFEAILNDDVLYPVWLSKEAVNILKAFMTKNAGKRLGCVVSQGGEDAIRAHPFFREIDWDALESRQVKPPFKPKIKSKRDANNFDSDFTKEEPVLTPSDPAVVRAINQDEFRGFSFINPHFTY