wanglab/gogpt-training-data huggingface dataset:
Protein: Zcf8p (A0A1D8PJ72)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MESNLSNTESPSPSPSSPSSSATPTTTNISTNTTNNENPGIHTSATTNTTPSSADTTTKPKRQRRSYSCGPCKLLKIKCDLQIPCTACKKFNRVNRCLLQPPQPPSQQELSKIQERKKRTTIKKMKLSNEFVQAYNVNPNALPSMISTMETTSKNYEKKTQKHKMNQISLDKDSSPKENTSKTLKQLNNFNGNRKDTQLTKNSNSMSPHSLIEIQRHHLSFQQPQMNKQQLHPISYITSVSSPSSALTSTSLNFPQGSQQEDVIQYLLTMDSQKTIDLTMVDIKRIKRLLPNDFGLFKSMFDCYLNTVNPIAIDMQDFSEIFKQSNLVYNKLLSIDDENPKNLSINVSFTLIELRNLSLFFLILVNGLLFDFRGEKPPLDSTRQTHNNRYTNFLLERSIYKSKHDVIEDWIKISKFIKLKVLAYESLTDIIFLIDWYMILKNYYDYENMVVENYLEFNNLLNYLVLNNDFINTIEDPYNEVGRNSNEEEEEEDAATTSVDENEVVYPDTRQFKVLSKYWIQLRLIEIDYTFFQFKGSLLFANQLKGTVVPHKKILKTLYKDVELDPITTHLMKIWGLYYKRSKNTTSVREIIKDYLLLYCNMMGTLKDELNEFETNKPLELPNSRSINLKDIELLIKNQRLLHLFVRWLSFIRIESNYFPSLRYTTYFTTVMNLFNHFNYLDDKSNNNVLSMIFNNYSLSNIKLFYQCLVFQGIFLVLLKNALNGNNNYPNNNPSTSLPKFKINLEKIYQFSLHQYQTTLNKILNHEVCRELQENITLFKLIANLSIEFNQYLINPITNNNPKDKDLDLTELIYDLKSKISSSNWDLLLNYFFGSKDNFARYIEKIWDLFQYLKIDPTTTTTTSTVSTTDIPITSKIYLNDQLIDDVMGKFSGFKFDENVVNEYFKHCVEPNIFE
Protein: 2-aminobenzoylacetyl-CoA thioesterase (EC 3.1.2.32) (P20581)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)-quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. Catalyzes the hydrolysis of the intermediate 2-aminobenzoylacetyl-CoA (2-ABA-CoA) to form 2-aminobenzoylacetate (2-ABA), the precursor of HHQ. In vitro, can also hydrolyze other substrates such as S-ethyl-acetothioacetate and acetoacetyl-CoA, but is inactive against anthraniloyl-CoA, malonyl-CoA and octanoyl-CoA. Beyond its thioesterase function, is involved in the regulation of diverse genes coding for key virulence determinants and biofilm development.
Interaction partners:
- 2-heptyl-4
- 2-heptyl-4
- Anthraniloyl-CoA anthraniloyltransferase
- Anthranilate--CoA ligase
- Anthranilate synthase component 1, pyocyanine specific
- HTH-type quorum-sensing regulator RhlR
- Anthranilate synthase component 2, pyocyanine specific
- 2-heptyl-3-hydroxy-4
- Multiple virulence factor regulator MvfR
- ATP-dependent RNA helicase RhlB
Sequence:
MLRLSAPGQLDDDLCLLGDVQVPVFLLRLGEASWALVEGGISRDAELVWADLCRWVADPSQVHYWLITHKHYDHCGLLPYLCPRLPNVQVLASERTCQAWKSESAVRVVERLNRQLLRAEQRLPEACAWDALPVRAVADGEWLELGPRHRLQVIEAHGHSDDHVVFYDVRRRRLFCGDALGEFDEAEGVWRPLVFDDMEAYLESLERLQRLPTLLQLIPGHGGLLRGRLAADGAESAYTECLRLCRRLLWRQSMGESLDELSEELHRAWGGQSVDFLPGELHLGSMRRMLEILSRQALPLD
Protein: Echinus splice form 3 (Echinus, isoform C) (Q1W9P9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Xenotropic and polytropic retrovirus receptor 1
Sequence:
MIKFRYKRKEPTNVVGVAAPTAGAAALGSGASSTPGTSPTSPVSVPVPVQAHHPHPQLGHLISNNGGTLPRSSPRKLILDGADKSATLTRQQSKQKSVSALAKVASSVELAVMGYNSTGNGNSNGHINSAGNSERDRCINAVIELFQQLQTSSEPALCPEPLRRALASGPLAGRRFPLGCLGDAAECFELLLHRVHSHISPDDGDSCESSACIAHRRFAMRVIEQSVCKCGANSEQLPFTQMVHYVSASALTSQKSLALQSHQQLSFGQLLRAAGNMGDIRDCPNTCGAKIGICRALLNRPEVVSIGIVWDSERPAADQVHAVLKAVGTSLRLGDVFHQVSEPRWAQQTQHELVGIVSYYGKHYTTFFFHTKLKVWVYFDDANVKEVGPSWEGVVDKCSRGRYQPLLLLYAVPQQPTVGNGVGIGHVDVAMPASAPSIAGSVVRRAVTPSPEKPSLGNTRRAITPTPLRTPPNDYQNLSVIQKNIFPSNLAMGTDETDAYISRKTVEHVLSAQYQNLSVIQDKIGGGNGVGVGQQSVDKDGGFLSRKPIEAVLSAQLARRQHLQLQRSHSAESSSGHASSNGSSPPSDGLTMPEHLNQPRRRDSGNWSGDRNSASSASSTTLDNPYLYMVAKRGVAAVPQSPTRHGLPYDPGYDSFSLSSTDSYPPKHALNPQLAKIPEAAMGVVPNGGAMPHGHGNGQLALSGDCEKLCHEADQLLEKSRLVEESHDLETALVLCNAAAGRARAAMDAPYSNPHTMTFARMKHNTCVMRARSLHRRILVEKGAETEAMPELKHMREGSTSSVKHVRQNSKDRTLEKEQQQLQFQQIQQIQQIHQIQQQIPASIEIYATLPKRKSPLKALASASACDDNAIEYEQEKQLATSPGKPERESRSLFGRKDKEKEKRSRSEDRNKLTREFSLTETLLVNAKDTLKKHKEDKDEKKEKDKSGKKQHKIRRKLLMGGLIRRKNRSMPDLTEAVDDSTANAGITHHPHYPAQGVTTAGTLLGTSVDDSAVGLGKHGHGMSGYISEGHFDYSGSGSASNSGAGSNPNPNLERSKLMRKSFHGSGRQLTMVPKVAPPPPMRTSSTLTPQQQQQQQQQFHHEANLSNLSAMSSNTSISEDSCQTIITTCAQVHSEQSPLKDLQMLVAQDELPLPPPMELPPYPSPPHSSCHSRQASEDFPPPPPPELDLEPLNQQLSQLQALEAASKQQRQQLESLEGTTSILAQLQQRQHLLKLRKEQANHPGAATTDATWLKELQAKQANDLRAMQRKLEASSPSSVRDLTHRFEQTSIRSYASQELLSQPGQSQQLGQLRTQMNGLPNGNAKMDVDEVDAMPAVRNSLPAALSAHQLLPKPKYEMTQSQIAEEIREVELLNTMVQQTLNQNGAAALPKRVKKKSVSFCDQVILVATAGNEEDDDFIPNPILERVLRTAQHPNEKVTAQMIQQQQQNMMRLQTEAQPRQQQVQQLQQPSPMLGRPAGATADMQRYVQRMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHQELYRQQQLHRTSMSGIASQQHLQQLDAQYTTMPRPLHHSQLGSYSVTLQKHQQLQQQQQQQQQQQAPQQLSLGYFSNGSVATSEQVPLPSPYQRVPLPHGYQPAAAGPYYPLPNAQQHLQQQQLMAKPVQKKVSFEPGTKGEADCLPPPPPPPQKNGLPETGSAGSGHPGAAPGASGAGGTTSAGITAIPTRVYNNAIVKASAKAVECNLCRKRHVIAPAVYCTNCEYYLQMLNQRR
Protein: histidine kinase (EC 2.7.13.3) (Q9HYX0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- Probable chemotaxis protein
- Sensory/regulatory protein RpfC
- Oxygen sensor histidine kinase NreB
- Response regulatory domain-containing protein
- histidine kinase
Sequence:
MSLSIGLIAVVALVYMAILFAIAFYGDRRRTPLSPRLRAWVYSLSLAVYCTSWTFFGAVGQATDQLWSFLPIYLGPVLLMLFAPWVLQKMIMISKQENITSIADFIAARYGKSQALAVVVALICMVGVLPYIALQLKGIVLGVNLLIGSGADSTGTRAQDTALIVSLVLALFTIVFGTRSLDVTEHHRGMVLAIAFESLVKLTAFLAVGIFATFGLYDGFADLFSQARAAPQLADYWEETVHWPAMLLQTGVAMTAIMCLPRQFHVTVVENIEPRDLNLARWVFPIYLVLAALFVVPIALAGQLHLPAGVMPDSFVISLPLAEAHPALALLAFIGGASAATGMVIVASVALSTMVSNDMLLPWLLRRREKDTERPFEAFRHWLLTVRRVSIAVILLLAYVAYRLLGSSASLATIGQIAFAAIAQLGPAMIGALYWKQANRRGVFAGLAAGSLLWAYTLVLPVVAKGLGWPLERIPGLTWLASNPFGLPIEPLTQGVLISLVGNFALFGLVSVLSRTRVSEHWQASRFIGQEISQRQNSRFMLAVQVEDLLMLAARFVGEERARQSFIRFAYRQGKGFTPNQTANNEWIAHTERLLAGVLGASSARAVVKAAIEGREMQVEDVVRIADEASEVLQFNRALLQGAIENITQGISVVDQSLRLVAWNHRYLELFEYPDGLIYVGRPIADIIRYNADRGLCGPGDPDMHVAKRLYWMRQGTPHTSERLFPNGRVIELIGNPMPGGGFVMSFTDITAYREAEQGLKGANESLEQRVQERTQELSQLNQELSEAKSNAEAANQSKTRFLAAVSHDLMQPLNAARLFSAALAHQDALPGEVRDLVQHLDSSLRSAEDLITDLLDISRLESGRVSAERNPFPLNNLYDALGVEFKALAQEQGLHFRLRGSQLRVDSDIKLLRRILQNFLTNAFRYAKGHVLLGVRREDGYLRLEVWDQGPGIPPDKQKVIFEEFKRLDSHQTRAEKGLGLGLAIADRLCKVLGHPLEVRSWPGKGSVFSVRVPLARQAPPALANGHKAEPAQALNGAQVLCVDNEDSILAGMNSLLSRWGCQVWTARSREECATLLDSEMRPQLALIDYHLDDGETGTQLMAWLRTRLGEPVPGVVISADARPELVAEIHAAGLDYLSKPVKPAALRALLSRHLSLR
Protein: Phosphorylase b kinase gamma catalytic chain, liver/testis isoform (PHK-gamma-LT) (PHK-gamma-T) (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-2) (P31325)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM.
Interaction partners:
- Phosphorylase b kinase regulatory subunit
- Phosphorylase b kinase regulatory subunit
- Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
- Calmodulin-1
- Calmodulin-like protein 3
- Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
- Calmodulin-like protein 4
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Glycogen phosphorylase, liver form
Sequence:
MTLDVGPEDELPDWAAAKEFYQKYDPKDIIGRGVSSVVRRCVHRATGDEFAVKIMEVSAERLSLEQLEEVRDATRREMHILRQVAGHPHIITLIDSYESSSFMFLVFDLMRKGELFDYLTEKVALSEKETRSIMRSLLEAVNFLHVNNIVHRDLKPENILLDDNMQIRLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQILMLRMIMEGQYQFSSPEWDDRSNTVKDLIAKLLQVDPNARLTAEQALQHPFFERCKGSQPWNLTPRQRFRVAVWTILAAGRVALSSHRLRPLTKNALLRDPYALRPVRRLIDNCAFRLYGHWVKKGEQQNRAALFQHQPPRPFPIIATDLEGDSSAITEDEVTLVRS
Protein: Lysozyme g (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase) (C1BF55)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MAFLWAWLGDFMKVKSKYGDIMEVKTTGASKETADADGHARGYSGVTASERMAEYDKDDINNYIDIIREVGKEYEIAPALICGIISRETRGGRAIRKPSPPIVPKQGWGDYGRGFGLMQVDVDPNGGNHKRRGEWDSETHLEQATGILIDFINEIKDKFPDCTEEQQLKGGIAAYNQGIGAIHSLCKRVDENTTGKDYSNDVVARAQWYHNNLV
Protein: Large ribosomal subunit protein bL12cy (50S ribosomal protein L12-2, chloroplastic) (CL12-B) (P36211)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein bL9c
- 50S ribosomal protein L33
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein bL28c
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Large ribosomal subunit protein uL4c
- Large ribosomal subunit protein uL15c
- Large ribosomal subunit protein bL31c
- Large ribosomal subunit protein bL17c
- AT5g15220/F8M21_110
Sequence:
MAATTLSIATTIRSSSFSSGLASAHHFPSRPLSIEFPFSFGVSSSSTLSHRAIYLHPISAVKTPKKIKKIGSEISSLTLEESRILVDYVQDKFGVSILFSAPAAAALPPPLDNGGATASVERQTTFDVVINDVPRGNRIAVITAIRAMTSLSLSESKELIEGFPKKFKEGVTKDEAEEDKTQLEEAGAKVSIV
Protein: Telomere bouquet protein 2 (Meiotic chromosome segregation protein bqt2) (Meiotically up-regulated gene 18 protein) (Q9US52)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in chromosome segregation. During meiotic prophase, connects telomeres to the spindle pole body by forming a bridge between the telomere protein rap1 and the spindle pole body protein sad1.
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Chromosome, telomere. Note=Colocalizes with the telomere cluster during the 'horsetail' stage and then disappears before the first meiotic division.
Interaction partners:
- Telomere bouquet protein 1
- DNA-binding protein rap1
- Karyogamy meiotic segregation protein 1
- Spindle pole body-associated protein sad1
- Telomere length regulator taz1
- Bouquet formation protein 4
- Bouquet formation protein 3
- Twin horsetail protein 2
- Karyogamy meiotic segregation protein 2
- Dynein heavy chain, cytoplasmic
Sequence:
MFQGKCAFFDETVPSALIALWQLHNGEAKFLAEGYENFDYAFSMHLRKHVRLPNYKSVQCRSPWWIAEQVAVSRSKSYVSEPVIHLNVMEPLYVDHRIRSVYLQPLPSTLSFLNGELP
Protein: Docking protein 4 (Downstream of tyrosine kinase 4) (Insulin receptor substrate 5) (IRS-5) (IRS5) (Q8TEW6)
Organism: Homo sapiens (Human)
Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK4 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway (By similarity). Putative link with downstream effectors of RET in neuronal differentiation. May be involved in the regulation of the immune response induced by T-cells.
Interaction partners:
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Pleckstrin-2
Sequence:
MATNFSDIVKQGYVKMKSRKLGIYRRCWLVFRKSSSKGPQRLEKYPDEKSVCLRGCPKVTEISNVKCVTRLPKETKRQAVAIIFTDDSARTFTCDSELEAEEWYKTLSVECLGSRLNDISLGEPDLLAPGVQCEQTDRFNVFLLPCPNLDVYGECKLQITHENIYLWDIHNPRVKLVSWPLCSLRRYGRDATRFTFEAGRMCDAGEGLYTFQTQEGEQIYQRVHSATLAIAEQHKRVLLEMEKNVRLLNKGTEHYSYPCTPTTMLPRSAYWHHITGSQNIAEASSYAGEGYGAAQASSETDLLNRFILLKPKPSQGDSSEAKTPSQ
Protein: Carboxylesterase 1D (Carboxylesterase 3) (EC 3.1.1.1, EC 3.1.1.67) (Fatty acid ethyl ester synthase) (FAEE synthase) (Triacylglycerol hydrolase) (TGH) (Q8VCT4)
Organism: Mus musculus (Mouse)
Function: Major lipase in white adipose tissue. Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty acid moiety. Catalyzes the synthesis of fatty acid ethyl esters. Hydrolyzes retinyl esters (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15220344}. Cytoplasm, cytosol {ECO:0000269|PubMed:15220344}. Lipid droplet {ECO:0000269|PubMed:15220344}. Microsome {ECO:0000250|UniProtKB:P16303}.
Interaction partners:
- Cytochrome P450 2E1
- Myeloperoxidase
- Beta-glucuronidase
- Arylamine N-acetyltransferase 1
- Arylamine N-acetyltransferase 2
- Cytidine deaminase
- Arylamine N-acetyltransferase 3
- Carboxylic ester hydrolase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase 1A6
Sequence:
MGLYPLIWLSLAACTAWGYPSSPPVVNTVKGKVLGKYVNLEGFTQPVAVFLGVPFAKPPLGSLRFAPPQPAEPWSFVKNTTSYPPMCSQDAVGGQVLSELFTNRKENIPLQFSEDCLYLNIYTPADLTKNSRLPVMVWIHGGGLVVGGASTYDGLALSAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIANFGGNPGSVTIFGESAGGFSVSVLVLSPLAKNLFHRAISESGVSLTAALITTDVKPIAGLVATLSGCKTTTSAVMVHCLRQKTEDELLETSLKLNLFKLDLLGNPKESYPFLPTVIDGVVLPKAPEEILAEKSFSTVPYIVGINKQEFGWIIPTLMGYPLAEGKLDQKTANSLLWKSYPTLKISENMIPVVAEKYLGGTDDLTKKKDLFQDLMADVVFGVPSVIVSRSHRDAGASTYMYEFEYRPSFVSAMRPKAVIGDHGDEIFSVFGSPFLKDGASEEETNLSKMVMKFWANFARNGNPNGGGLPHWPEYDQKEGYLKIGASTQAAQRLKDKEVSFWAELRAKESAQRPSHREHVEL
Protein: DNA helicase MCM9 (EC 3.6.4.12) (Minichromosome maintenance 9) (I0IUP4)
Organism: Gallus gallus (Chicken)
Function: Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8-MCM9 complex probably acts as a hexameric helicase required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart.
Subcellular location: Nucleus {ECO:0000269|PubMed:22771115}. Note=Localizes to nuclear foci and colocalizes with RAD51.
Interaction partners:
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- DNA helicase MCM8
- Chromatin licensing and DNA replication factor 1.
- Cell division control protein
- Cell division cycle 45.
- WD repeat and HMG-box DNA-binding protein 1
- Origin recognition complex subunit 1
- Uncharacterized protein.
Sequence:
MALRADQVSLIGQVFESYLLQHHRDDILGILRQGDDEAHYPVLVDALTLFETNMEIGEYFNAFPSQVLPIFDGALRRAAMAVLQAATPSPELRMKPNLHARISGLPICPELTREHIPKTRDVGHFLSVTGTVIRTSLVKVLEFERSYICNKCKHVFVAKADFEQYYAFCRPSACLNEEGCNSTKFTCLSGTSSSPSSCRDYQEIKIQEQVQRLSVGSIPRCMVVVLEDDLVDSCKSGDDITVYGVVMQRWKPFHQDARCDLELVLKANYVKVNNEQLAGVTIDEEVRKEFEDFWEKHRNNPLAGRNEILASLCPQVFGLYLVKLAVAMVLAGGVQRIDATGTRIRGESHLLLVGDPGTGKSQFLKYAVKITPRSVLTAGIGSTSAGLTVTAVKDFGEWNLEAGALVLADGGLCCIDEFNSIKEHDRTSIHEAMEQQTISVAKAGLVCKLNTRTTILAATNPKGHYDPAESVSVNIALGSPLLSRFDLVLVLLDTKNEEWDRIISSFILQNKGCPSKSEKLWSMEKMKTYFCLIKRIQPKLSDESNLILVRYYQMQRQSDCRNAARTTIRLLESLIRLAEAHARLMFRDTVTLEDAVTVVSVMESSMQGGALLGAINALHTSFPENPMTQYRMQCELILERLELHDLLHKELQRLDRLQKETYCQLQPEETSFSTITGCLNKNTFESKQKSQSEPSDQQKINSYPQPSLPKSNCEGDKHPEALRNPTPGNNISTKRLSRLNKRSDDGSLGWFDRLEDRNTDAEETFWKTSPLPKTSPDNMALKTMSKSSCSEEGNSSVPRKEDGMRGSLRTVTLCAPLEQDKVSEISSKRTEERKCFSSEANIQDPTSASASVQESVITQRVSKSLQRLHTEKSHRFFTSTQNSEANALPSVLPVSGLLDLSSDTDSVVGDENNSASAAVKHAVISMRKRSKGQAEKEAKAVSSHEPEITDGESPPAAKLAKFSFRPRTKLDDSSEKKNAEFPLFPSENTVKPGEQPQGEQLQKDCCPPEKRKMTLTCLGRKGLEKQSIGSKGNEEQLSQALGKEMGGNALIHSDVTLDVVSPPPTEKRREGEEKLGGPSTVRVCSSTLENLSKFCFASRPDSKSEAPPTIKTDTNNKESHSPLLKVHVSNPNKRKSFALGNASKDSVVTRKSLFSIAELDDATLDFDWD
Protein: Dihydrouridine synthase 2 (E7EUN9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MILNSLSLCYHNKLILAPMVRVGTLPMRLLALDYGADIVYCEELIDLKMIQCKRVVNEVLSTVDFVAPDDRVVFRTCEREQNRVVFQMGGMGAALLSDPDKIEKILSTLVKGTRRPVTCKIRILPSLEDTLSLVKRIERTGIAAIAVHGRKREERPQHPVSCEVIKAIADTLSIPVIANGGSHDHIQQYSDIEDFRQATAASSVMVARAAMWNPSIFLKEGLRPLEEVMQKYIRYAVQYDNHYTNTKYCLCQMLREQLESPQGRLLHAAQSSREICEAFGLGAFYEETTQELDAQQARLSAKTSEQTGEPAEDTSGVIKMAVKFDRRAYPAQITPKMCLLEWCRREKLAQPVYETVQRPLDRLFSSIVTVAEQKYQSTLWDKSKKLAEQAAAIVCLRSQGLPEGRLGEESPSLHKRKREAPDQDPGGPRAQELAQPGDLCKKPFVALGSGEESPLEGW
Protein: Synaptotagmin-1 (Synaptotagmin I) (SytI) (p65) (P21707)
Organism: Rattus norvegicus (Rat)
Function: Calcium sensor that participates in triggering neurotransmitter release at the synapse. May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:11823420}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17190793, ECO:0000269|PubMed:9867811}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000269|PubMed:1985919}; Single-pass membrane protein. Cytoplasm.
Interaction partners:
- Multifunctional fusion protein
- Vesicle-associated membrane protein 2
- S100 calcium-binding protein A13
- Syntaxin-1A
- Ras-related protein Rab-3A
- Complexin-1
- DnaJ homolog subfamily C member 5
- Vesicular glutamate transporter 1
- Vesicle-associated membrane protein 3
- Synapsin-2
Sequence:
MVSASHPEALAAPVTTVATLVPHNATEPASPGEGKEDAFSKLKQKFMNELHKIPLPPWALIAIAIVAVLLVVTCCFCVCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK
Protein: E3 ubiquitin-protein ligase RNF103 (EC 2.3.2.27) (KF-1) (hKF-1) (RING finger protein 103) (RING-type E3 ubiquitin transferase RNF103) (Zinc finger protein 103 homolog) (Zfp-103) (O00237)
Organism: Homo sapiens (Human)
Function: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18675248}; Multi-pass membrane protein {ECO:0000269|PubMed:18675248}.
Interaction partners:
- 43 kDa receptor-associated protein of the synapse
- Ubiquitin-conjugating enzyme E2 N
- Zinc finger protein ZPR1
Sequence:
MWLKLFFLLLYFLVLFVLARFFEAIVWYETGIFATQLVDPVALSFKKLKTILECRGLGYSGLPEKKDVRELVEKSGDLMEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQVIANDRSPLVGKIHWEKMVKKVSRFGIRTGTFNCSSDPRYCRRRGWVRSTLIMSVPQTSTSKGKVMLKEYSGRKIEVEHIFKWITAHAASRIKTIYNAEHLKEEWNKSDQYWLKIYLFANLDQPPAFFSALSIKFTGRVEFIFVNVENWDNKSYMTDIGIYNMPSYILRTPEGIYRYGNHTGEFISLQAMDSFLRSLQPEVNDLFVLSLVLVNLMAWMDLFITQGATIKRFVVLISTLGTYNSLLIISWLPVLGFLQLPYLDSFYEYSLKLLRYSNTTTLASWVRADWMFYSSHPALFLSTYLGHGLLIDYFEKKRRRNNNNDEVNANNLEWLSSLWDWYTSYLFHPIASFQNFPVESDWDEDPDLFLERLAFPDLWLHPLIPTDYIKNLPMWRFKCLGVQSEEEMSEGSQDTENDSESENTDTLSSEKEVFEDKQSVLHNSPGTASHCDAEACSCANKYCQTSPCERKGRSYGSYNTNEDMEPDWLTWPADMLHCTECVVCLENFENGCLLMGLPCGHVFHQNCIVMWLAGGRHCCPVCRWPSYKKKQPYAQHQPLSNDVPS
Protein: Geranylgeranyl transferase type-2 subunit beta (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta) (GGTase-II-beta) (Type II protein geranyl-geranyltransferase subunit beta) (PGGT) (YPT1/SEC4 proteins geranylgeranyltransferase subunit beta) (P20133)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- Rab proteins geranylgeranyltransferase component A
- GTP-binding protein YPT1
- Ras-related protein SEC4
- Synaptobrevin homolog YKT6
- Ypt/Rab-type GTPase YPT7
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Rab GDP-dissociation inhibitor
- GTP-binding protein YPT31/YPT8
- Vacuolar protein sorting-associated protein 21
Sequence:
MSGSLTLLKEKHIRYIESLDTKKHNFEYWLTEHLRLNGIYWGLTALCVLDSPETFVKEEVISFVLSCWDDKYGAFAPFPRHDAHLLTTLSAVQILATYDALDVLGKDRKVRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVLKCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLEEIGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSLAIIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSLMGYDNLVPIDPIYCMPKSVTSKFKKYPYK
Protein: Sarcoplasmic/endoplasmic reticulum calcium ATPase regulator DWORF (SERCA regulator DWORF) (Dwarf open reading frame) (DWORF) (Small transmembrane regulator of ion transport 1) (P0DN84)
Organism: Homo sapiens (Human)
Function: Enhances the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by displacing ATP2A1/SERCA1 inhibitors, thereby acting as a key regulator of skeletal muscle activity. Does not directly stimulate SERCA pump activity. Enhances sarcoplasmic reticulum Ca(2+) uptake and myocyte contractility by displacing the SERCA inhibitory peptides sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN).
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0DN83}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Myoregulin
- Sarcolipin
- Endoregulin
Sequence:
MAEKAGSTFSHLLVPILLLIGWIVGCIIMIYVVFS
Protein: Rac GTPase activating protein 1 (F8VS54)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEEQKSALAFLN
Protein: Small ribosomal subunit protein eS1B (40S ribosomal protein S1-B) (RP10B) (P23248)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS17B
- Small ribosomal subunit protein eS28B
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS2B
- Small ribosomal subunit protein eS6A
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL8A
- Small ribosomal subunit protein eS28A
- Small ribosomal subunit protein eS8A
Sequence:
MAVGKNKRLSRGKKGLKKKVVDPFTRKEWFDIKAPSTFENRNVGKTLVNKSTGLKNASDALKGRVVEVCLADLQGSEDHSFRKVKLRVDEVQGKNLLTNFHGMDFTTDKLRSMVRKWQTLIEANVTVKTSDDYVLRIFAIAFTRKQANQVKRHSYAQSSHIRAIRKVISEILTREVQNSTLAQLTSKLIPEVINKEIENATKDIFPLQNIHVRKVKLLKQPKFDVGALMALHGEGSGEEKGKKVSGFKDEVLETV