wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 3 subunit F (eIF3f) (Deubiquitinating enzyme eIF3f) (EC 3.4.19.12) (Eukaryotic translation initiation factor 3 subunit 5) (eIF-3-epsilon) (eIF3 p47) (O00303)
Organism: Homo sapiens (Human)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MATPAVPVSAPPATPTPVPAAAPASVPAPTPAPAAAPVPAAAPASSSDPAAAAAATAAPGQTPASAQAPAQTPAPALPGPALPGPFPGGRVVRLHPVILASIVDSYERRNEGAARVIGTLLGTVDKHSVEVTNCFSVPHNESEDEVAVDMEFAKNMYELHKKVSPNELILGWYATGHDITEHSVLIHEYYSREAPNPIHLTVDTSLQNGRMSIKAYVSTLMGVPGRTMGVMFTPLTVKYAYYDTERIGVDLIMKTCFSPNRVIGLSSDLQQVGGASARIQDALSTVLQYAEDVLSGKVSADNTVGRFLMSLVNQVPKIVPDDFETMLNSNINDLLMVTYLANLTQSQIALNEKLVNL
Protein: Tropomodulin (Q91006)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSYRKELEKYRDLDEDKILGALTEEELRKLENELEELDPDNALLPAGLRQRDQTQKPPTGPFKREELMAHLEQQAKDIKDREDLVPFTGEKRGKAWIPKQKPMDPVLESVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYEALGSSTIVNKEGLNSVIKPTKYKPVPDEEPNSTDVEETLKRIQNNDPDLEEVNLNNIMNIPVPTLKALAEALKTNTYVKKFSIVGTRSNDPVAFALAEMLKVNNTLKSLNVESNFISGSGILALVEALQSNTSLIELRIDNQSQPLGNNVEMEIANMLEKNTTLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLAELNGPIFPKCRTGV
Protein: Uncharacterized protein (Q57X23)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- CAP/Srv2p
Sequence:
METRKVTECTPSPEEEFRSGTSLKYPDEERTRQQLTLAFPSIDADVIEEMAFLVGRKRYTIDKVVYMLRLIEESMKLDNPANKGLVNSGESEGQEVQVLQEGTDDTSTGHSLPLQSSQPQEGLDQTTMKQQRDLPEGNRGGVEELQPFMLSYSNSHSANFVGVKLFFTSMTGDRRIRDHCRRAETLLYLKRITYEPVNVADSPTLQRNLREMYAACTGKRGAPPLPALFVGTSYVGNYEEMQEMEDDGTLMDTLEHLGYKHEIQSSVVTR
Protein: Dynein light intermediate chain (Eurofung) (C8VB15)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Cytoplasmic dynein intermediate chain
- Dynein heavy chain, cytoplasmic
- P150 dynactin NUDM
- Dynamitin homolog
- Dynein light chain, cytoplasmic
- F-actin-capping protein subunit beta
- Dynein light chain
- Dynactin subunit 4
- Arp11 homolog
- Ypt/Rab-type GTPase avaA
Sequence:
MSTSKRSSTVSSKDGLKKNIWSSMLDSAATGKRLPEKNLLILGGTPESQREFLEAYSADTLDSSLSNEKRKGKGKVPPVANQFALGYTYLDVLDADQEDTLARVSAYLLSEPSLSFAPLLKPLLTPQSIPETSVVILLDWSDPWTWVRRLREWVRLLRHVLVSLDDETKVVMEENMTQWRERKKGIDTSSTGSQATSSGSAIIGPGEWDEGLGVPLCVVCQGTDKMEKLERDHGWSEDEFDFIHQFMRTLLVKHGASLIYTKPFHANNLHSVLHSSLGIHSLLKKLSLKANFIERDKILIPTNWDSWAKIRVIREGSNLEGISTAWSIEIQDPPEPLSDRNDEAQDDGSSEEDDGTSAVKIYEQTIKDPKRNTSLSYPGSQQSGNKIEVETLDMQGFLTKQLEVLEQLKIEDEKDRAAKKTPQLEMSPLEDNSRVNEHIGPVQFNMGGIQVDADDMLQKLKDREASRSQRKDPVSSPGDEKANNQALANFFAGLVKKPGGSPRGA
Protein: V-type proton ATPase subunit H (V-ATPase subunit H) (Vacuolar proton pump subunit H) (Q8MML6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity).
Interaction partners:
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase subunit B
- V-type proton ATPase subunit d
- V-type proton ATPase subunit G
- Vacuolar proton translocating ATPase 100 kDa subunit
Sequence:
MNFRELDTSNGVKAAESSFRTKVVLAREIPWNGFASSNSITSEQYNLISKYDKHTDAEKKEKFAANSASYVNFFVNFINSTSNIEIIQYLLTLINEIIEIDPRAAGAFSKITKDDDKSYPYSVFFRLLNREDAYTNLHASIALAQIMCAGKPTQNDVESFFNWILKLLRKNNSSEVEVGLIALQSLLLKDDFRIFFNNIDGSALLLNILQALSTSSVNIQLLYETIYAIWLLTYNKDIAAAYSGTGLVANLVQLVKTVAKEKIVRLSLSTLRNLLNNGKSNEEMIDNGFVRMLNILNIKKWGDDDIPADIEVLINGLAKDIDNMSSFNKYKTEIISGELEWTPVHKSERFWKENISKFEENNYQVIKHLHQILKTSQSTPLQLSIACHDLCEFVRHHSRGKAIMTITNQTRYHGYDVKSNEEVKNQALFALQKMMLNNWEYLNAK
Protein: Protein ESC2 (Establishes silent chromatin protein 2) (Q06340)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ESC2). Involved in HMR and telomere silencing via the recruitment or stabilizing of the SIR (silent information regulators) complex.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- ATP-dependent DNA helicase SRS2
- Telomere length regulation protein ELG1
- ATP-dependent helicase SGS1
- E3 SUMO-protein ligase MMS21
- Crossover junction endonuclease MMS4
- Structure-specific endonuclease subunit SLX4
- Structural maintenance of chromosomes protein 5
- SUMO-conjugating enzyme UBC9
- Structure-specific endonuclease subunit SLX1
- Crossover junction endonuclease MUS81
Sequence:
MTGDSRSISEPSINLDPDNTSFSDENSDDFFMDNSYDIDEIDHSDESNRQSVIVDSKVTVPPSKHSTLTLSDSEDSDAKEQHQSLSRSSSKNVNIEDITEPKPDKPSGRTRGRSVMKESVVEINSSESDLDEDKNFPRSRSRSRSSIRSISPAGKYKRQKSSLLYTYDENDDFFKELAKEAKKSTTISKESTPDQRKRVYNIKFLSKLEGTINKAVQVKVLGKYEFSKILPAALDGLMKSYKIPKVMKDIYKVENVTLYWNNAKLLTFMTCNSLHIPQDFENEVSDIDVTIVSKEYEKNFEATLESKLKEEEAALLIKERQEMERKLEKKRNEQEESEYREFESELKNVEETQEIKENDTVMNTKLLQEGGSLSGNSSSMEEVMRIALMGQDNKKIYVHVRRSTPFSKIAEYYRIQKQLPQKTRVKLLFDHDELDMNECIADQDMEDEDMVDVIID
Protein: 1,3-beta-glucan synthase component FKS3 (EC 2.4.1.34) (1,3-beta-D-glucan-UDP glucosyltransferase) (FK506 sensitivity protein 3) (Q04952)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for spore wall assembly.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- 1,3-beta-glucan synthase component GSC2
- 1,3-beta-glucan synthase component FKS1
- GTP-binding protein RHO1
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Sporulation-specific glucan 1,3-beta-glucosidase
- UTP--glucose-1-phosphate uridylyltransferase
- Glucan 1,3-beta-glucosidase I/II
- Glucan 1,3-beta-glucosidase
- Glycogen [starch] synthase isoform 1
- Glycogen [starch] synthase isoform 2
Sequence:
MDFMSPKFSLTDVEYPAWCQDDEVPITMQEIREIFVELMDKFGFQKSSMENMYQHLMGQLDSRASRTGAQNALVSLHVSYIGGEHANYRKWYFAAQLDLDEEIGFQNMRLHGKARQRNVKMAKKRGVSIKEQIKQWNEKEQEFINNHPKITLTQEQLEDQTNLKSADYKWKLKMKKLTPENMIRQLALYLLCWGEANQVRFAPECLCFIFKCALDYDISTSSSEKTVKSPEYSYLNDVITPLYEFLRGQVYKKDAKGNWKRREKDHKNIIGYDDINQLFWYPEGFERIILNNGERLVDKPLEERYLYFKDVAWSKVFYKTYRETRSWKHCFTNFNRFWIIHFAPFWFFTTFNSPTLYTKNYIQLLNNQPTPQVRLSVIAFGGTIACLVQILATVFEWGFVPREWPGAQHLSSRMIGLLFCLAINLGPSVYVLGFFEWDVHSKSAYIVSIVQLIIAFLTTFFFAVRPLGGLFRPYLNKDKKHRRYISSQTFTASFPKLTGRSKWFSYGLWVFVYLAKYIESYFFLTLSLRDPIRVLSIMDLSRCQGEYLLGPILCKWQAKITLVLMLLSDLGLFFLDTYLWYIICNCIFSIVLSFSLGTSILTPWKNVYSRLPKRIYSKILATSEMDVKFKAKILISQVWNAIVISMYREHLLSIEHLQRLLFQQVDSLMGDTRTLKSPTFFVAQDDSTFKSMEFFPSNSEAKRRISFFAQSLATPISEPVPVDCMPTFTVLVPHYSEKILLGLKEIIREESPKSKITVLEYLKHLHPTEWECFVKDTKLLSMEKSFLKEAESSHDEDRLEIPDALYDPRSSPLSDHTESRKLPTEDDLIKEKINDLPFSYFGFNSSEPSYTLRTRIWASLRTQTLYRTLSGFMNYSKAIKLLYRIENPSLVSLYRGNNEALENDLENMASRKFRMVVAMQRYAKFNKDEVEATELLLRAYPNMFISYLLEELEQNESEKTYYSCLTNGYAEFDEESGLRKPIFKIRLSGNPILGDGKSDNQNHSIIFYRGEYIQVIDANQDNYLEECLKIRSVLSEFEELELNPTIPYIPGIEYEEEPPPIAIVGSREYIFSENIGVLGDIAAGKEQTFGTLFARTLAEIGGKLHYGHPDFLNGIFMTTRGGLSKAQRGLHLNEDIYAGMNAICRGGKIKHSDYYQCGKGRDLGFGSILNFTTKIGAGMGEQLLSREYYYLGTQLPMDRFLSFFYAHPGFHLNNLFISFSVQLFFVLLLNLGALNHEIIACFYDKDAPITNLETPVGCYNIQPALHWVSIFVLSIFIVFFIAFAPLLIQEVLEKGIWRAASRFLHHLLSMAPLFEVFVCQVYSNSLLMDLTFGGAKYISTGRGFAITRLDFFTLYSRFVNISIYSGFQVFFMLLFAIISMWQPALLWFWITVISMCFAPFIFNPHQFAFMDFFIDYKTFIHWLFSGNTKYQKESWANFVKSSRSRFTGYKSKTVDDISEDSGHDSKKARFWNVFFAELFLPFCVFLFNFTAFSFINAQTGVSDSTPTSAVFRLLLVTFLPIFLNSIVLFLLFWVSLFVVPGLSYCCKDAGAVIAFIAHTFSVLVYLLDFELMWFLQGWNFTRTLILLITCINMHLILFKVFTTIFLTREYKNNKAHLAWWNGKWYNTGMGWSIILQPIREYFVKIMESSYFAADFFLGHFLLFIQTPIILLPFIDYWHTMVLFWMNPRSIIAHKRILTRKQRALRSRIVSKYFSLYFVMLGVLLFMLIAPFFAGDFVSSPQELLEGTLFEGIFQPNNQNNNDTGPNAPSTILTTTPTLPTFRTVA
Protein: Klaroid, isoform D (Klaroid, isoform F) (A1Z6Q0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSENTYQIETRRRSRSKTPFLRSSCDHENCEHAGEEGHVHHLKRKSAAPNVQTIIEEHIVESSISKKTRAKAFAQLTSDYSSDDMTPDAKRKQNSITATVTSILTKRSGGATSTPRNRSQLETTQNTLNSAQEKLNQSNGNLSSGNVSDYLAYIEYRDAGEYWNKTPKTDYTYSELSPHRRQLAPGIVAMPNMSRKSLENHNDRVNYMVQQNPAQEEFIRRRYQSKYTQQVNYDSADELDATFGQQKQSWWLIRLIQLVVSSITTVWSRVTNLSATETTAYQNYHAKRQQSQQVGLWWKIVQTIGGGLASLLRYLYVFIGSVLSLDTWLLRSSDAENKSKKRFLIFLLILLPLLLLSGLFYYIHPNETFPPKSLSEYTFTLPELPKIDVKDYLNQEQFESLRSQAAEHAVRVRDWADDYVLYLRTIGQNVVNKGRQLFQGDDKVYYERV
Protein: SD01229p (Q8T9H1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSQTGSGSGGNNTSNSNNSSSGSGGSGSGSSTGNTASGSGNNNSTSAGGPPSSQGGNNGNGSGSSSSSSSGKSSAKMSIDHQATLDKGLKMKIKRTKPGTKSSEAKHEIVKATDQQQNGALGAGSNNSANEDGSSGSSSTNASSLGSTNSSSSASSGSSSSSGSSSSSSKKHLNNASSGSGSSSSGGGSQNNASGHASGGGSSGSSQSTPQGTKRGSSGHRREKTKDKNAHSNRMSVDKSAAAASAAGEKDTPEKCSGTGAGGSPCSCNGDVGAPCSHHACIRRAAHMSNSAGNTNSSAGTGQSGGSSSMSAVPPGVFTPSAGSPSTGSPSTVVPAAASLLAATGAASSSASQMASSSAGGVGGSGGGANAPGPPGKESAGSIKISSHIAAQLAAAAASNSYSGSGANTNQGQNSNAGGNGGSESKAAAAAQAKLMAPGMISATMHHTISVPAGTGTGDDDTKSPPAKRVKHEAGASGAGGGKEMVDICIGTSVGTITEPDCLGPCEPGTSVTLEGIVWHETEGGVLVVNVTWRGKTYVGTLLDCTRHDWAPPRFCDSPTEELDSRTPKGRGKRGRSAGLTPDLSNFTETRSSIYFSHAQVHSKLRNGATKGRGATRSASGNAAANSNSSSSGNGGGATPSTSPTAFLPPRPEKRKSKDEAPSPLNGDASDGASGGGIGGAGGVNMVNASGIPISASGGGLATQPQSLLNPVTGLNVQISTKKCKTASPCAISPVLLECPEQDCSKKYKHANGLRYHQSHAHGAGGGASSMDEDSMQAPEDPATPPSPGVASGTGSGASVASSAVPATAPSAGQGTVAVSPNTPLANSSNPVTNGNVAPSAPATGSATIAAPNTTPSVVETQAPLTGPPPVTPPAPTPICAVATPGAEQSVSSVLPLGNLPLTAGPNSATQQQQPPTQQQQPQLLVPGGSAASLQQQQQQQQPVAGGSITAGISGQALSQHQQQLMGGLPAMLSDQQQQALLQQGALKAGVLRFGPPDGNPLQQQPGQASVNPQTQQSPPRPPSHVQDQQTPSAYAQQAGLKTSPGFGSVGVGAASSKQKKNRKSPGPSDFEGRVSREDVQSPAYSDISDDSTPVAEQEMLDKSVGQAVTAKHIELMGKKPTEVGVGVPPAPAPNMYVPGMYQFYPAQQQSAPPPQQQQQQPQYMVQTEPGKPPGLPPALTQAQQQQQLQPGAPPPTSQPPSHLLGPPGQQSVAAHLADYSGKNKDPPLDLMTKPQPQPGQPPSQQQQSGQLSGQENNGKDVGPPTSQPGSQPPPVNLSAVAGPPPGSLPPGLGGLSALGAAGLGGPGPGKGMPHFYPFNFIPPAYPYNVDPNFGSVSIVASEEAAKLSGHPGLPPSSQAQQLSGISIKEERLKESPSPHDQPKHMPSQQQMIASKLIKQEPMTKQEIKQEPNSNPGQQHPPPQQQPAPQPQQQQPPPPQPQQPHALHPKDLQALGAYPAIYQRHSINLAVQQAREEELRRYYMFTGRQNSAAAAAAAAAQNAASGGLPPHPGMMHKDEPGMGSAQQQQQQQQQQMQIAQQQQQAIQQHHQHLQQQHQAQQQQQQQQHQQQQQQQQQQQQQQQQQQQQQQKLKQSQAASAGANNKATNLTKDSPKQKGGDDDQPLKVKQEGQKPTMETQGPPPPPTSQYFLHPSYISPTPFGFDPNHPMYRNVLVSAAGPYNTAPYHLPIPRPYHAPEDLSRNTGTKALDALHHAASQYYTTHKIHELSERALKSPTSGSGPVKVSVSSPSIGPPQPGGPTSSGPGSGPVSGVLGPGSGSNQQLGSAPGSAGGVPLNLQPPPGGMGPSPGSKPDLSGPKGHGGVTPGSSLDGHKQSMPGGPPPNGPSGNGAVGGVGGAAGNGAAGGGGAGAADSRSPPPQRHVHTHHHTHVGLGYPMYPAPYGAAVLASQQAAAVAVINPFPPGPSK
Protein: Nuclear mitotic apparatus protein 1 (F5H6Y5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTLHATRGAALLSWVNSLHVADPVEAVLQLQDCSIFIKIIDRIHGTEEGQQILKQPVSERLDFVCSFLQKNRKHPSSPECLVSAQKVLEGSELELAKMTMLLLYHSTMSSKSPRDWEQFEYKIQAELAVILKFVLDHEDGLNLNEDLENFLQKAPVPSTCSSTFPEELSPPSHQAKREIRFLELQKVASSSSGNNFLSGSPASPMGDILQTPQFQMRRLKKQLADERSNRDELELELAENRKLLTEKDAQIAMMQQRIDRLALLNEKQAASPLEPKELEELRDKNESLTMRLHETLKQCQDLKTEKSQMDRKINQLSEENGDLSFKLREFASHLQQLQDALNELTEEHSKATQEWLEKQAQLEKELSAALQDKKCLEEKNEILQGKLSQLEEHLSQLQDNPPQEKGEVLGDVLQLETLKQEAATLAANNTQLQARVEMLETERGQQEAKLLAERGHFEEEKQQLSSLITDLQSSISNLSQAKEELEQASQAHGARLTAQVASLTSELTTLNATIQQQDQELAGLKQQAKEKQAQLAQTLQQQEQASQGLRHQVEQLSSSLKQKEQQLKEVAEKQEATRQDHAQQLATAAEEREASLRERDAALKQLEALEKEKAAKLEILQQQLQVANEARDSAQTSVTQAQREKAELSRKVEELQACVETARQEQHEAQAQVAELELQLRSEQQKATEKE
Protein: Serine-aspartate repeat-containing protein E (Q932F7)
Organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)
Function: Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Contributes to the resistance to killing by innate immune components in blood and thus attenuates bacterial clearance by interacting with host complement factor H/CFAH and modulating its activity. Inhibits also bacterial opsonization and killing by interacting with host complement regulator C4BPA and thus inhibiting classical complement pathway activation (By similarity).
Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Note=Anchored to the cell wall by sortase A (By similarity). {ECO:0000250|UniProtKB:O86489}.
Interaction partners:
Sequence:
MINRDNKKAITKKGMISNRLNKFSIRKYTVGTASILVGTTLIFGLGNQEAKAAENTSTENAKQDDATTSDNKEVVSETENNSTTENDSTNPIKKETNTDSQPEAKEESTTSSTQQQQNNVTATTETKPQNIEKENVKPSTDKTATEDTSVILEEKKAPNYTNNDVTTKPSTSEIQTKPTTPQESTNIENSQPQPTPSKVDNQVTDATNPKEPVNVSKEELKNNPEKLKELVRNDNNTDRSTKPVATAPTSVAPKRLNAKMRFAVAQPAAVASNNVNDLITVTKQTIKVGDGKDNVAAAHDGKDIEYDTEFTIDNKVKKGDTMTINYDKNVIPSDLTDKNDPIDITDPSGEVIAKGTFDKATKQITYTFTDYVDKYEDIKARLTLYSYIDKQAVPNETSLNLTFATAGKETSQNVSVDYQDPMVHGDSNIQSIFTKLDENKQTIEQQIYVNPLKKTATNTKVDIAGSQVDDYGNIKLGNGSTIIDQNTEIKVYKVNPNQQLPQSNRIYDFSQYEDVTSQFDNKKSFSNNVATLDFGDINSAYIIKVVSKYTPTSDGELDIAQGTSMRTTDKYGYYNYAGYSNFIVTSNDTGGGDGTVKPEEKLYKIGDYVWEDVDKDGVQGTDSKEKPMANVLVTLTYPDGTTKSVRTDANGHYEFGGLKDGETYTVKFETPAGYLPTKVNGTTDGEKDSNGSSITVKINGKDDMSLDTGFYKEPKYNLGDYVWEDTNKDGIQDANEPGIKDVKVTLKDSTGKVIGTTTTDASGKYKFTDLDNGNYTVEFETPAGYTPTVKNTTAEDKDSNGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKDVKVTLLNEKGEVIGTTKTDENGKYRFDNLDSGKYKVIFEKPAGLTQTVTNTTEDDKDADGGEVDVTITDHDDFILDNGYFEEDTSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDAGKHTPVKPMSTTKDHHNKAKALPETGSENNGSNNATLFGGLFAALGSLLLFGRRKKQNK
Protein: Y-box-binding protein 1 (YB-1) (ZfY1) (Y-box transcription factor) (B5DE31)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing and transcription regulation. Binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and recruiting pabpc1a, thereby preventing mRNA decay. Plays a role in the maternal-to-zygotic transition in early embryo by binding to m5C-containing maternal mRNAs and preventing their degradation. Also promotes maternal-to-zygotic transition in oocytes and embryos by promoting translation repression; molecular mechanisms governing translation repression are unknown. Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs. Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs (By similarity). Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence-associated subset of cytokine mRNAs, possibly by binding to m5C-containing mRNAs (By similarity). Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection (By similarity). Also able to bind DNA and regulate transcription. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'). Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair. The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P67809}. Nucleus {ECO:0000250|UniProtKB:P67809}. Cytoplasmic granule {ECO:0000250|UniProtKB:P67809}. Secreted {ECO:0000250|UniProtKB:P67809}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P67809}. Cytoplasm, P-body {ECO:0000250|UniProtKB:P62960}.
Interaction partners:
- Polyadenylate-binding protein 1A
- tRNA
- Aly/REF export factor.
- Heterogeneous nuclear ribonucleoprotein U
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- Small nuclear ribonucleoprotein 48
- RNA helicase
- Small nuclear ribonucleoprotein 25
- Programmed cell death 7.
- RNA helicase
Sequence:
MSSEAETQQPPQPAADAESPSSPAAAATAGDKKVIATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPGGVPVQGSKYAADRNRYRRYPRRRAPPRDYQENYQSDPEAEPREKREGAESAPEGEMQQQQRRPTYPGRRRYPPYFVRRRYGRRPPYTNSQRGEMTEGGEGEENQGGPDQGNKPMRQNYYRGFRPSRGPSRPRPVRDGEEDKENQSESGQNQEPRQRRYRRNFNYRRRRPQTTKPQDGKDSKAADASADKSAAPEAEQGGAD
Protein: Molybdate import system permease protein MolB (Q57130)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Part of the ABC transporter complex MolBCA involved in molybdate import. Responsible for the translocation of the substrate across the membrane. Functions as a low-affinity molybdate transporter.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:17158291}; Multi-pass membrane protein {ECO:0000269|PubMed:17158291}.
Interaction partners:
- Molybdate import ATP-binding protein MolC
- Molybdate-binding protein MolA
- Uncharacterized ABC transporter ATP-binding protein HI_1272
- Uncharacterized protein HI_1269
- Uncharacterized protein HI_1469
Sequence:
MQPDSYPKILFGLTLLLVITAVISLGIGRYSLSVPQIGQILWAKATALEIDPVQQQVIFQVRLPRILTALCVGAGLALSGVVLQGIFRNPLVNPHIIGVTSGSAFGGTLAIFFGFSLYGLFTSTILFGFGTLALVFLFSFKFNQRSLLMLILIGMILSGLFSALVSLLQYISDTEEKLPSIVFWLMGSFATSNWEKLLFFFVPFLLCSSILLSLSWRLNLLSLDEKEAKALGVKMAPLRWLVIFLSGSLVACQVAISGSIGWVGLIIPHLSRMLVGANHQSLLPCTMLVGATYMLLVDNVARSLSDAEIPISILTALIGAPLFGVLVYKLKRGGMNE
Protein: Ferric uptake regulation protein (Q87WN7)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
- Alkyl hydroperoxide reductase C
Sequence:
MVENSELRKAGLKVTLPRVKILQMLDSAEQRHMSAEDVYKALMEASEDVGLATVYRVLTQFEAAGLVVRHNFDGGHAVFELADGGHHDHMVNVESGEVIEFFDEEIEKLQKAIVERHGFDLVDHNLVLYVRNKKA
Protein: Interleukin (C7AL05)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDRRYRISFLTLFLTGCLQGNPIPRLLAGIDYLEENITCPDSVFYTPTDVEDSCIVAALACSIKELDTVKVECLDKAVHLESMQHHISMTATALQKTIDKENSTTDTSECICEDKRLEKSFKDFIQNIRHLTQAHAAKRLSS
Protein: Rab proteins geranylgeranyltransferase component A (Rab escort protein homolog) (REP) (Q9V8W3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds unprenylated Rab proteins, presents it to the catalytic component B, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab to a protein acceptor (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10082978}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10082978}. Note=Coordinated with the cell cycle, located around nuclei during prophase and telophase. Located to spindle poles during metaphase.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- LD45906p
- Geranylgeranyl transferase type-2 subunit beta
- EG:80H7.4 protein
- Rab32, isoform B
- LD44762p
- Ras-related protein Rab-3
- LD39986p
- Ras-related protein Rab6
- Ras-related protein Rab5
Sequence:
MLDDLPEQFDLVVIGTGFTESCIAAAGSRIGKSVLHLDSNEYYGDVWSSFSMDALCARLDQEVEPHSALRNARYTWHSMEKESETDAQSWNRDSVLAKSRRFSLDLCPRILYAAGELVQLLIKSNICRYAEFRAVDHVCMRHNGEIVSVPCSRSDVFNTKTLTIVEKRLLMKFLTACNDYGEDKCNEDSLEFRGRTFLEYLQAQRVTEKISSCVMQAIAMCGPSTSFEEGMQRTQRFLGSLGRYGNTPFLFPMYGCGELPQCFCRLCAVYGGIYCLKRAVDDIALDSNSNEFLLSSAGKTLRAKNVVSAPGYTPVSKGIELKPHISRGLFISSSPLGNEELNKGGGGVNLLRLLDNEGGREAFLIQLSHYTGACPEGLYIFHLTTPALSEDPASDLAIFTSQLFDQSDAQIIFSSYFTIAAQSSKSPAAEHIYYTDPPTYELDYDAAIANARDIFGKMFPDADFLPRAPDPEEIVVDGEDPSALNEHTLPEDLRAQLHDMQQATQEMDIQE
Protein: Peptidylglycine alpha-amidating monooxygenase (PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase (PHM) (EC 1.14.17.3); Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC 4.3.2.5) (Peptidylamidoglycolate lyase) (PAL)] (P14925)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (By similarity). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate. The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate. Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P10731}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10731}. Note=Secretory granules. {ECO:0000250|UniProtKB:P10731}.
Interaction partners:
- Kalirin
- Ras association domain-containing protein 9
- Carboxypeptidase E
Sequence:
MAGRARSGLLLLLLGLLALQSSCLAFRSPLSVFKRFKETTRSFSNECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANIPIPVKPDMVMMHGHHKEAENKEKSALMQQPKQGEEEVLEQGDFYSLLSKLLGEREDVHVHKYNPTEKTESGSDLVAEIANVVQKKDLGRSDAREGAEHEEWGNAILVRDRIHRFHQLESTLRPAESRAFSFQQPGEGPWEPEPSGDFHVEEELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAEILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPSTGAVFVSDGYCNSRIVQFSPSGKFVTQWGEESSGSSPRPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVFAISYIPGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKMEHRSVKKAGIEVQEIKEAEAVVEPKVENKPTSSELQKMQEKQKLSTEPGSGVSVVLITTLLVIPVLVLLAIVMFIRWKKSRAFGDHDRKLESSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRVSTEGSDQEKDEDDGTESEEEYSAPLPKPAPSS