wanglab/gogpt-training-data huggingface dataset:
Protein: Rolling pebbles isoform 6 (Q8WTD1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
Interaction partners:
Sequence:
MFPLTNRSSSGNRTNNNPSNNNNNQTTSFIIGGTTNINNNNNQLGGTNSAKDKGNFENNWSCNKTTGRRSGSGNSCSFLDLQSIRRLLEHDASGSVCPSCRISFDKGKRRKLIDTCGHERCYSCMFRNDQCPMCMNSSLKDVDGANAQGYDTGIGGSTSTIVSPLGSPQPQLRSHAQRNAALARYMQQHRQESQSPDYHHRYASNGKLPRAAALSTNGNGFTTGTTQTVTVDVHHQLGGGGGGAAAAAKQLMANGISGHSRSTSLSHNIHAAAYSELSAAPPAFATPPTRRRFFNHKNLRSALTGGSGGGSGVGGGVGGAGGVGGGHRRTASNGGCPIDTASILSGGSDAIDHHSSFLNEKLQKDQLHARLGLLLNDPGSNGNSSSSGSGCEPISAHSTTSTTSSSGVGAASTTTSGSSQNVSPEQTLASGAGMLSGSQLSVATSHGVKEDALSLCGKFKAGCSMLHVYEALPSKSRKGNVRRSTRGQQGSSSSASAASAVGSRVTASSLAAVQLALKPLFFEVPLQEPDPPYVGRQWLVQQLSNILLGTETRVVLINGQPGTGKTAFCLQLVEYSCFGRRQMQDDPDGIYSQLQLGAHCERMRGLASHMVGYHFCQADANLTCQVPDFVHSLAAQLCQAPQLTAYRDYLLSEPHLQDILSVRECIADAERVMKLAILEPLAHLHRAGKIPAKVAVIVVDALCEAEYHRPDHGHTIASFLAQLTPHFPAWLKLVATVRTQMLELVKAPSYTQLTLDSWASSQALQQDMLDYIGARLADSPEIRMNIGGGGGQNSQSGSQPQTKFVSHLQSLSRGSMLYAKLILDLIARGQLVIKSSSYKVLPVSLAQIFLLHFNLRFPTARSFEQAAPILNICLAALYPLTLDEIYYSMEALSHGREALSWPDFMQRFKLLDGFLIKRLDNTYMFFHSSLREWLMRRDEGESNKFLCDARLGHAGIAFRLSRLQAPLSPQLTLELGHHMLKAHLYGGTSLTLLSPRDLQSYWLAGAADNISSSLGALRNVYSPNLKVSRLVLLAGASPNHRTDYMGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACDWSPRPHSQDVTRSVALQQALIGAAAQAHCKILEDLLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKLGPTTWSMAMGKPEILVILLNKLLEDGNVLYRKNRFQEAAHRYQYALRKISGLEQLLERNAIFAQLRTNLLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQSGVLCEVVEVLKRIQTELLTRISISSEDQTGRMSNIGGGASVAYESHHEITDL
Protein: histidine kinase (EC 2.7.13.3) (A4D9V5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Phosphotransmitter protein Ypd1, putative
- Uncharacterized protein
Sequence:
MRIPIAVQLGLLVLVTALVGLAVLSIATWVNNYNFVVDVQSDGLELVAKIKARQIASNLQLLESTCKTIVTRLLIQGALGRFYNGNSSDSNWTSSVTDVQSALGSNNYMDLYQVIIFSRNGQGDRHGLLNVTAKDIAEIALPYTHPDGTAVMLGEEGLGYPPALYPNLTYVAASDGSSTTDVYAFSDYKLGLDTALLLGPLPINSSFSLISVTVPIINNTSATDILGYMTVVASAANLQATINSRDGLGQTAQILLLGPSRLDNQFARDAYAATATSAPDVERLSHAEVHYVFEPTPLPGQSSRHGGNLSMSSFALSRYPLAWKLMSKPWAESNDSISDLSTRNEHGYQVAVGAIRPKTSMAQWILLVEQTQAEAFAPINKLRKIILACVFGTIGFIILIVPPLTHLAVAPIRRLSEATRKSIEPPSQPPHDCPPSSGPYIVGTAEAETEPRAFGDHMDEKGLVAWVKHFRRRDRPHSTHSNGSRNHAGAFQIPGRVKERKHLITDELTELTSTFNEMSDELSIHYHRLEERVAERTRELEAAKLAAETANESKTLFIANISHELKTPLNGILGMCTVCMGEDDLPRIKKSLQVVYKSGDLLLHLLNDLLTFSKNQIDQAIRLEEREFRLSDIRSQLAVIFQNQVQEKHIDFNVNFVSNDTLPPQADGFQEKTSLPAAPALGPPGTGRLRDMVLWGDQHRILQVLINLVSNSLKFTPEHGKVEVRIKCVREAETPGSPRTSLQDSRRNSRLRSQPPSHDSSQPRDPVDGLVQEEYHTPVLSQLRTLIFQFEVEDNGPGVAPHLQKRVFEPFVQGDLGLNRKYGGTGLGLSICAQLSRLMNGKITLESEPGKGALFTVEIPLKFVKEAAPSTPSSSAAGSRTPSVFSLDDLPGLARPPSNNGSVRSDPLTNFEKQDLQPRLVGLSQPFFTPTPSSPAPSTPRATPADGAKPEVKDNTSGKVRVLVAEDNVVNQEVVLRMLRLEEVYDVTVVKDGQEAYDTVKANMEEGKVFDVIFMDIQMPNLDGLESTRLIRGMGYSAPIVALSAFSEESNIKDCMDSGMDMFISKPIRRPALKQVLNRSRKSRRMRKIHSPGRSQ
Protein: NADH-cytochrome b5 reductase 3 (B5R) (Cytochrome b5 reductase) (EC 1.6.2.2) (Diaphorase-1) (P20070)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor.
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8978818}; Lipid-anchor {ECO:0000269|PubMed:8978818}; Cytoplasmic side {ECO:0000305|PubMed:8978818}. Mitochondrion outer membrane {ECO:0000269|PubMed:8978818}; Lipid-anchor {ECO:0000269|PubMed:8978818}; Cytoplasmic side {ECO:0000305|PubMed:8978818}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:1577871}.
Interaction partners:
- Cytochrome b5
- Cytochrome b5 type B
- Sulfite oxidase, mitochondrial
- Dihydroorotate dehydrogenase
- Cytidine monophospho-N-acetylneuraminic acid hydroxylase, pseudogene
- Dihydropyrimidine dehydrogenase [NADP
- Uridine monophosphate synthetase, isoform CRA_a.
- Mitochondrial amidoxime reducing component 2
- Mitochondrial amidoxime reducing component 1.
- NADPH:adrenodoxin oxidoreductase, mitochondrial
Sequence:
MGAQLSTLSRVVLSPVWFVYSLFMKLFQRSSPAITLENPDIKYPLRLIDKEIISHDTRRFRFALPSPQHILGLPIGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYFKDTHPKFPAGGKMSQYLENMNIGDTIEFRGPNGLLVYQGKGKFAIRADKKSNPVVRTVKSVGMIAGGTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEHSSRFKLWYTVDKAPDAWDYSQGFVNEEMIRDHLPPPGEETLILMCGPPPMIQFACLPNLERVGHPKERCFTF
Protein: Cell division control protein 7 (EC 2.7.11.1) (P06243)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine-protein kinase. Needed for the initiation of DNA synthesis during mitosis as well as for synaptonemal complex formation and commitment to recombination during meiosis. Required for HTA1-HTB1 locus transcription repression.
Interaction partners:
- Serine/threonine-protein kinase RAD53
- Minichromosome maintenance protein 5
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM2
- DDK kinase regulatory subunit DBF4
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM6
- Serine/threonine-protein kinase MEC1
- Cell division control protein 45
Sequence:
MTSKTKNIDDIPPEIKEEMIQLYHDLPGIENEYKLIDKIGEGTFSSVYKAKDITGKITKKFASHFWNYGSNYVALKKIYVTSSPQRIYNELNLLYIMTGSSRVAPLCDAKRVRDQVIAVLPYYPHEEFRTFYRDLPIKGIKKYIWELLRALKFVHSKGIIHRDIKPTNFLFNLELGRGVLVDFGLAEAQMDYKSMISSQNDYDNYANTNHDGGYSMRNHEQFCPCIMRNQYSPNSHNQTPPMVTIQNGKVVHLNNVNGVDLTKGYPKNETRRIKRANRAGTRGFRAPEVLMKCGAQSTKIDIWSVGVILLSLLGRRFPMFQSLDDADSLLELCTIFGWKELRKCAALHGLGFEASGLIWDKPNGYSNGLKEFVYDLLNKECTIGTFPEYSVAFETFGFLQQELHDRMSIEPQLPDPKTNMDAVDAYELKKYQEEIWSDHYWCFQVLEQCFEMDPQKRSSAEDLLKTPFFNELNENTYLLDGESTDEDDVVSSSEADLLDKDVLLISE
Protein: Uncharacterized protein YGR111W (P53265)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YOR012W
- Putative nitrilase-like protein YIL165C
- Homeostatic regulator of DAG
- Uncharacterized protein YGR127W
- Uncharacterized protein YMR085W
Sequence:
MTASSNDDDLIFECYSDPELKRWTHLANAKAWKGILTVQQYADREQLLGSSEISQKNKSNEMMTKYPKSYQWLGQKYFVLKDRSLPDNGKFSQVVSSCETLNRIGYCIHPGSNGKIEPALIVCIGGVFTFENHRGKGYAKKMIIKLNEFYDKIRDDANTVLELKNLVINLYSEVGEYYSALGYESMHVPLHRISKLDELTERYCGEDDDHDGKYLGFDDYRGLVGLHETQFKESLLSLHKENPEKFVFTVAPDFDIFTWFQYRDLFIMNKSGRKAQQNLFFGYALSDNSHIIWHHNWNGDSLIIVKIHIPEETFQRKELKLKKLLRKAIEETKLHGLQELEFWDEEIPIKKYPQLFQLLTELENESKVFSENGSISAVRPPKGYTAEQVIWDNNTKFCWF
Protein: Cilia- and flagella-associated protein 251 (F1Q8Y1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Cilia and flagella-associated protein 43.
- Rho guanine nucleotide exchange factor 3
- Ectonucleoside triphosphate diphosphohydrolase 6
- Dynein axonemal intermediate chain 4
- Dynein, axonemal, heavy chain 6.
- Cilia- and flagella-associated protein 91
- Phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit gamma
- Cilia and flagella-associated protein 52.
- Cilia and flagella-associated protein 58
- Zinc finger, MIZ-type-containing 2.
Sequence:
MSTENGKSSEAEDTGEPKSTENNQIKKESQGGDEATGEVEKRSDLPSQQEDTADSQIYTATSLPAIPKETNKTHPLVLEWAYGINSTLPVFSLQDEDRLVIIYACAHVAVIYDHTSKSQYLLQGHCSPITCLCTSEDRRWIVTADMGQESLVIIWDAYTGIPVKTLFDCHPEGGVAALALSKDSKYLVTVGAGLVQRVCIRNWTDESEEPACQVDLSPKYGCQKQILFNPSDSTQLVSNSSSQVLFYNWERGHLEYSAPEITDKTFNAVIGSLSQSVFHYDGVQAFTATSDGNIILWDKQTESVSRQPIVRNAIKLVSMQKEAITVLTLIDSFIVTGDVNGHIKFYDGNLKLINLYNEFNVDPIRSISFSKERPSNNSLEYPKDCTLDAKPFVMRNFVLSTTHATVVHVNTQTNVPKSLLREHAEPLEAVACHPKQPLVAMGSHSGTIKVWDYQHKEAVCSRVFLSHKQIQCIAYDPQGFYLAVGFASGALQIVDACTLHNDGKECLQFTQDSITHLTFSQDSHYLAAADTGKAVTLLCLCKEGTQEIWKYQGRHHSHYKPIQDLLFGVDLDSNQPRLLSLGMDRRLVEYDLQSSGENELLILSCDRIEQSAVPTCMAWYPHLTPENFLLTASNLYKMKLFNATSKMCRKTLSAPSYGSPVKKMLILPASKDGDSNSRYMAYITEDKVGIQILPLDGNPHKSFVMICHSTGVSTLACSYDGRYVFTAGGQDCTVFSWELNLLSLEASAALGGKGMKPFYDLLEGGRDGLLFKEMEEYFYYFQLLDQNLDSMETRLVSTRIPLADVPFLMRALGFYPTEQELEDMQNEVKFSRYAETRNYVTDIDLEEFIRLYVNHRPASGISRQELYNAFQVLGKPDEEGRYNIDRDELLELLQARGEHMTEDDLAECFTTLLGVTPDGGNYTGSLLESVLPAEITMDAFASDILGFSVATQELHQEHHGQES
Protein: Troponin T, fast skeletal muscle (TnTf) (Beta-TnTF) (Fast skeletal muscle troponin T) (fTnT) (P45378)
Organism: Homo sapiens (Human)
Function: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin I, fast skeletal muscle
- Troponin C, skeletal muscle
- Troponin I, slow skeletal muscle
- Troponin I, cardiac muscle
- Troponin C, slow skeletal and cardiac muscles
- Myosin light chain 1/3, skeletal muscle isoform
- Tropomyosin beta chain
- Myosin-3
- Myosin regulatory light chain 11
- Tropomyosin alpha-3 chain
Sequence:
MSDEEVEQVEEQYEEEEEAQEEAAEVHEEVHEPEEVQEDTAEEDAEEEKPRPKLTAPKIPEGEKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEDDLKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLGEDKLRDKAKELWETLHQLEIDKFEFGEKLKRQKYDITTLRSRIDQAQKHSKKAGTPAKGKVGGRWK
Protein: Phospholipase A2 (Lmr-PLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (B3EWP6)
Organism: Lachesis muta rhombeata (Bushmaster)
Function: Snake venom phospholipase A2 (PLA2) that displays mild but significant inhibition of mouse platelet aggregation induced by ADP and collagen. Induces edema in the foot pads and gastrocnemius muscles of mice but shows no myonecrotic or myotoxic activity. PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:26145564}.
Interaction partners:
Sequence:
HLLQFGDLINKIARRNGILYYSFYGCYCGLGGRGRPQDATDRCCFVHDCCYGKVTGCDPK
Protein: Apoptotic protease-activating factor 1 (APAF-1) (Q9EPV5)
Organism: Rattus norvegicus (Rat)
Function: Regulates programmed cell death; necessary for normal brain development. Participates with pro-caspase-9 (Apaf-3) in the cytochrome c-dependent activation of caspase-3, leading to apoptosis. This activation requires ATP (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Cytochrome c, somatic
- Caspase-9
- Caspase-3
- Heat shock 70 kDa protein 4
- Diablo IAP-binding mitochondrial protein
- Bcl-2-like protein 1
- Apoptosis regulator Bcl-2
- Caspase-8
- E3 ubiquitin-protein ligase XIAP
- Caspase 7, isoform CRA_c
Sequence:
MDAKARNCLLQHKEALEKDIKTSYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLHEGYKDLAGLLHSGLPLVSSSSGKDTDGGNTSFVRTVLCEGGVPQRPVIFVTRKKLVSAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAEAVRDHALLEGCFSGGVHWVSIGKQDKSGLLMKLQNLCTRLGQEESFSQRLPLNIEEAKDRLRVLMLRKHPRSLLILDDVWDPWVLKAFDNQCQILLTTRDKSVTDSVMGPKYVIPVESGLGKEKGLEILSLFVNMKKEDLPVEAHSIIKECKGSPLVVSLVGALLRDFPNRWAYYLRQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCVLWDLETEEVEDILQEFVNKSLLFCNRNGKSFCYYLHDLQVDFLTEKNRSQLQDLHRKMVTQFQRYHQPHTLSPGQEDCMYWYNFLAYHMASAGMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDTGRLYLEWINKKTIKNLSRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSGTGKLVHTYEEHSEQVNCCHFTNKSNHLLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWDVRSANEKKSINVKRFFLSSEDPPEDVEVIVKCCSWSADGDRIIVAAKNKVLLLDIHTSGLLTEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETRKVCKNSAIVLKQEIDVVFQENEMMVLAVDNIRGLQLIAGKTGQIDYLPEAQVSCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYVFLQAHQETVKDFRLLRDSRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPSPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHLCAPISIEEGTATHGGWVTDVCFSPDRKMLVSAGGYLKWWNVVTGESSQTFYTNGTNLKKIHVSPDFRTYVTVDNLGILYILQVLE
Protein: Portal protein (F5HBR4)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Forms a portal in the viral capsid through which viral DNA is translocated during DNA packaging. Assembles as a dodecamer at a single fivefold axe of the T=16 icosahedric capsid. Binds to the molecular motor that translocates the viral DNA, termed terminase.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04012}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04012}.
Interaction partners:
Sequence:
MERNHWNEKSSGAKRSRERDLTLSTIRSILAADERLRIKASSYLGVGRGVDDEAVIDIFPTGQTMSFLRLLHGFLGTCRGQSMHQVLRDPCVLRKQLLYGVCKTLFDTITVRRVAEEWKLHAALFPYRALDEEDLEQYLLVWSASLRQSVQTGVLGALRDILYQYADNDDYGLYVDWCVTVGLVPLLDVKTKPSEAAERAQFVRAAVQRATETHPLAQDLLQANLALLLQVAERLGAVRIANAPEVRVFKKVRSERLEAQLRGKHIRLYVAAEPLAYERDKLLFTTPVAHLHEEILRYDGLCRHQKICQLLNTFPVKVVTASRHELNCKKLVEMMEQHDRGSDAKKSIMKFLLNVSDSKSRIGIEDSVESFLQDLTPSLVDQNRLLPARGPGGPGVVGPGGAVVGGPAGHVGLLPPPPGPAAPERDIRDLFKKQVIKCLEEQIQSQVDEIQDLRTLNQTWENRVRELRDLLTRYASRREDSMSLGARDAELYHLPVLEAVRKARDAAPFRPLAVEDNRLVANSFFSQFVPGTESLERFLTQLWENEYFRTFRLRRLVTHQGAEEAIVYSNYTVERVTLPYLCHILALGTLDPVPEAYLQLSFGEIVAAAYDDSKFCRYVELICSREKARRRQMSREAAGGVPERGTASSGGPGTLERSAPRRLITADEERRGPERVGRFRNGGPDDPRRAGGPYGFH
Protein: Branched-chain alpha-ketoacid dehydrogenase kinase (BCKDH kinase) (BCKDHKIN) (BDK) (EC 2.7.11.1) ([3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial) (EC 2.7.11.4) (O14874)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q00972, ECO:0000305|PubMed:24449431}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000250|UniProtKB:Q00972}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Protein phosphatase Mn
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- 26S proteasome regulatory subunit 7
Sequence:
MILASVLRSGPGGGLPLRPLLGPALALRARSTSATDTHHVEMARERSKTVTSFYNQSAIDAAAEKPSVRLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGAQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
Protein: Flavodoxin 2 (P0ABY4)
Organism: Escherichia coli (strain K12)
Function: Low-potential electron donor to a number of redox enzymes.
Interaction partners:
Sequence:
MNMGLFYGSSTCYTEMAAEKIRDIIGPELVTLHNLKDDSPKLMEQYDVLILGIPTWDFGEIQEDWEAVWDQLDDLNLEGKIVALYGLGDQLGYGEWFLDALGMLHDKLSTKGVKFVGYWPTEGYEFTSPKPVIADGQLFVGLALDETNQYDLSDERIQSWCEQILNEMAEHYA
Protein: DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5) (Q9BTE7)
Organism: Homo sapiens (Human)
Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:18445686, ECO:0000269|PubMed:23098533, ECO:0000269|PubMed:26906416}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686}. Note=Subcellular localization is independent of the interaction with cullins. {ECO:0000269|PubMed:26906416}.
Interaction partners:
- NEDD8-conjugating enzyme Ubc12
- Cullin-2
- Cullin-3
- NEDD8-conjugating enzyme UBE2F
- Cullin-associated NEDD8-dissociated protein 1
- E3 ubiquitin-protein ligase RBX1
- Cullin-1
- Cullin-4A
- NEDD8-activating enzyme E1 catalytic subunit
- Cullin-4B
Sequence:
MPVKKKRKSPGVAAAVAEDGGLKKCKISSYCRSQPPARLISGEEHFSSKKCLAWFYEYAGPDEVVGPEGMEKFCEDIGVEPENIIMLVLAWKLEAESMGFFTKEEWLKGMTSLQCDCTEKLQNKFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTWPLFSVFYQYLEQSKYRVMNKDQWYNVLEFSRTVHADLSNYDEDGAWPVLLDEFVEWQKVRQTS
Protein: HTH APSES-type domain-containing protein (G8BK85)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- HTH APSES-type domain-containing protein
- BCR1
- Transcriptional repressor Tup1 N-terminal domain-containing protein
- TEA domain-containing protein
- Transcription factor CPH1
- GATA-type domain-containing protein
- C2H2-type domain-containing protein
- Ras-like protein 1
Sequence:
MSTYSLPLRSQMNGNYNSASAPQSGAAVPPAPNTPQYAQQTTGAEAASGTPQQHQQQQQQPTSQQSQQPYASYYMYNQQQNPQQSEYSYSRYQYPGNTQSYYPPAQSVQQQQQPYGGNRSYTSAPQGPTSTASSVSQPQHATPSHHPMQRPMPQQDTLNHASTSTVGQYQPPGIRPRVTTTMWEDEKTLCYQVDANNVSVVRRADNNMINGTKLLNVAQMTRGRRDGILKSEKVRHVVKIGSMHLKGVWIPFERALSMAQRENIVDLLYPLFVRDIKRVIQTGVTPSSSGGNAGNAGANTGAATSTSSNTSPSVSKASAGTSGGATNASQSGSGGSYYQGYGGASGYPQQYTYQQQAQQGQQTPQGQDQYQAQQQQPYGYQQGGYYSNASGGGNQNTTGAGSSSSSYPYQYQQPPPQQSQGSYNNYATTSGYPAQTSTSGATSNAGAAANSEPGSTGAVGAQQHTPQQPSASVGGVHVSPHQHTQHSPKVGK
Protein: FI11703p (Rad21 mitotic cohesin) (Verthandi, isoform A) (O96689)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nipped-B protein
- Structural maintenance of chromosomes protein
- Precocious dissociation of sisters 5, isoform A
- Structural maintenance of chromosomes protein
- LD34181p
- Protein wings apart-like
- CTCF
- Serine/threonine-protein kinase polo
- Stromalin-2
- separase
Sequence:
MFYEHIILAKKGPLARIWLAAHWDKKITKAHVFETNIEKSVEGILQPKVKLALRTSGHLLLGVVRIYSRKAKYLLADCNEAFVKIKMAFRPGMVDLPEGHREANVNAITLPEVFHDFDTALPELNDIDIEAQFSINQSRADEITMREDYGSLSLSLQDDGFGDIGFEAETPEIIRCSIPSNINDKIFDNDVLENIESLDPHSLDAHADMPGSRLDGDGFGDSFGQPALFEDDLFGDPSQPVEQITKESTTVLNADDSDEDAIDNIHNVPSPATSLVNSIEDEKEENNLNGHASVSENVPMNEITLVQNEDEGFALAPLDVSMYKGVTKAKRKRKLIIDEIKNISGEEMKAQLADTSDILTTLDLAPPTKRLMYWKETGGVEKLFSLPSRSIPARALFGNYNRQLFSHSTFFEDFSSVVPMEILALEFYTKENENALIIFNKKGRKRKNDNMSNLFLDHVPDSVVQSLEAPEVLRANHKSLGVSTVSVEIVSKEQESISCQNELTFFDNMRSPDLLSLNEMEQFSSINELPLTPRNMNHEMGDDFNQGDSTPAGLDHGHATPQHGNIGEMDHDSVIPTKKTAVILNESVGTSVLSDNGVSKRTNNILKGWDNYEIPSFVGQNHGDEQMENETDEQFEERVLNKRAAHLFIDVRAHFIAKDSLELSQLTSGNSRKQAAQKFYSLLVLKKFKVLHIDQSAPYADITITRGPTFENPKI
Protein: Leucine-rich repeat protein (LRRP) (Q385R4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKVDSLLSPRSAFSTENDPCGSVESVANDVASASDVVVAYPQPGKRWSRIIAGPELVGMSLKENQIKDGKALCIYGHCFDDGIIDYITNEVLPEARVLTKVEIAETKFSSAGMKILLRALWTNSPCEQMEELLLHDVHLHFEETLQLKEVIMKNRKCLRRLVLQRCHMDDSAAEPIVQAISHCEQLREVNFLDNNIVHALAIPTEREDIFPPTLQIFDISGNRIEPKHFTGLGNALRRCMANLHEVYLARCCVTESGLKTLLCGGLYNSQVLSVLNVSAGRLLHTAGKVLSSVISECPNLQRVYMQDNLLDVEGAAQIALVIPYAKKLTVLGMGRCHLGGRGARYIAEAVKQSASLRELDLSGNGVTDEDVHRICACNDDASFRLSYLDLSDNPLTEDCRCSLETLLEHQKDNSCIVVVRGTGLAVVSSYMEYHNKPTPG
Protein: UDP-glucose:glycoprotein glucosyltransferase 2 (UGT2) (hUGT2) (EC 2.4.1.-) (UDP--Glc:glycoprotein glucosyltransferase 2) (UDP-glucose ceramide glucosyltransferase-like 1) (Q9NYU1)
Organism: Homo sapiens (Human)
Function: Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12913004}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12913004}.
Interaction partners:
- Selenoprotein F
- UDP-glucose:glycoprotein glucosyltransferase 1
- Calnexin
- Protein OS-9
- Mannosyl-oligosaccharide glucosidase
- UDP-galactose translocator
- Calreticulin
- Neutral alpha-glucosidase AB
Sequence:
MAPAKATNVVRLLLGSTALWLSQLGSGTVAASKSVTAHLAAKWPETPLLLEASEFMAEESNEKFWQFLETVQELAIYKQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQQIAADEPPPDGCNAFVVIHKKHTCKINEIKKLLKKAASRTRPYLFKGDHKFPTNKENLPVVILYAEMGTRTFSAFHKVLSEKAQNEEILYVLRHYIQKPSSRKMYLSGYGVELAIKSTEYKALDDTQVKTVTNTTVEDETETNEVQGFLFGKLKEIYSDLRDNLTAFQKYLIESNKQMMPLKVWELQDLSFQAASQIMSAPVYDSIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLQVRFKIQPGDARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFLKLNSHIWEYTYVLDIRHSSIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQEYTLDFIKLADVFYSHEVPLRIGFVFILNTDDEVDGANDAGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIWDILGIHSKYDEERKAGASFYKMTGLGPLPQALYNGEPFKHEEMNIKELKMAVLQRMMDASVYLQREVFLGTLNDRTNAIDFLMDRNNVVPRINTLILRTNQQYLNLISTSVTADVEDFSTFFFLDSQDKSAVIAKNMYYLTQDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKINEENTAISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGDKIKTFLIEGMDKNAFEKKYNTVGVNIFRTHQLFCQDVLKLRPGEMGIVSNGRFLGPLDEDFYAEDFYLLEKITFSNLGEKIKGIVENMGINANNMSDFIMKVDALMSSVPKRASRYDVTFLRENHSVIKTNPQENDMFFNVIAIVDPLTREAQKMAQLLVVLGKIINMKIKLFMNCRGRLSEAPLESFYRFVLEPELMSGANDVSSLGPVAKFLDIPESPLLILNMITPEGWLVETVHSNCDLDNIHLKDTEKTVTAEYELEYLLLEGQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTDSQADLEDIIVVLNSFKSKILKVKVKKETDKIKEDILTDEDEKTKGLWDSIKSFTVSLHKENKKEKDVLNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIWGYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISALYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNPKTKESKLKAAARIVPEWVEYDAEIRQLLDHLENKKQDTILTHDEL
Protein: Ferroxidase (A0A1D8PPD8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- High-affinity iron permease
- Fth1p
- Ftr2p
- Fth2p
- Ferric/cupric reductase transmembrane component 1
- Cu
- Acyl-CoA desaturase
- Protein CFT1
- Copper metallochaperone
Sequence:
MRTFLSSFIILTTFLASLIAAETHTWYFKTGWVDANPDGVYPRKMIGFNDSWPLPTLRVKKGDRVQLYLINGFDNLNTTLHFHGLFVRGANQMDGPEMVTQCPIPPGETYLYNFTVTDQVGTYWYHSHTGGQYGDGMRGVFIIEDDDFPYHYDEEVVLTLSDHYHKYSGDIMPAFLTRFNPTGAEPIPQNFLFNETRNATWKVEPGKTYFVRILNIGGFVSQYLWMEDHEFTIVEIDGVYVEKNTTDLIYITVAQRYGVLITTKNSTDKNYAFMNGVDTTMLDSVPADLQVNGTNYIVYNESSALPDAYDIDSYDDALDDFYLKPLSKQKLMDDADYTITVDVQMNVLNDGINYAFFNNISYKAPKVPTLLTVLSAGEAATNELIYGTNTNSFVLQGGDIVDIVLNNFDTGKHPFHLHGHVFQLIERHEAVGSKESAVTFNVSDHAEWPEYPMIRDTVYVKPHSYMVLRFKADNPGVWFFHCHVDWHLEQGLAIVLIEDPQAIQKNEKITENHKRICEKVGVPWEGNAAANSNDYLDLKGENVQVKRLPTGFTTKGIVALVFSCVAAFLGLFTISFYGMNDIAHVEDKVARDLDIDLEAENEDEEEAVVLNQNSSSSDSNSKPH