wanglab/gogpt-training-data huggingface dataset:
Protein: Ribosome-associated inhibitor A (Protein Y) (pY) (Ribosome associated factor Y) (Spot Y) (P0AD49)
Organism: Escherichia coli (strain K12)
Function: During stationary phase prevents 70S dimer formation, probably in order to regulate translation efficiency during transition between the exponential and the stationary phases. During environmental stress such as cold shock or excessive cell density at stationary phase, stabilizes the 70S ribosome against dissociation, inhibits translation elongation and increases translation accuracy. When normal growth conditions are restored, is quickly released from the ribosome. Has been suggested to inhibit translation elongation by blocking the A-site (aminoacyl-tRNA site). Has also been suggested to inhibit translation initiation by blocking the A-site and P-site (peptidyl-tRNA site) of the ribosome. At 15 degrees Celsius binds 30S subunits and stimulates their association with 50S subunits into idle 70S ribosomes. Crystallization with T.thermophilus 70S ribosomes shows it binds in the channel between the head and body of the 30S subunit, where mRNA, tRNAs, initiation factors IF1 and IF3 and elongation factor G would bind; this protein's extended tail follows the mRNA channel and probably prevents RMF binding, which would prevent ribosome dimerization. This protein also stabilizes the 30S head relative to the rest of the ribosome, which may also prevent dimerization. Counteracts miscoding (translation errors) particularly efficiently at magnesium concentrations close to those observed in vivo but less efficiently at higher concentrations. Counteraction of miscoding was shown to be stronger than inhibition of translation, suggesting that the former activity could be the main function of this protein in vivo.
Interaction partners:
- Ribosome modulation factor
- Cold shock-like protein CspC
- Elongation factor Tu 1
- Nitrogen regulatory protein
- Elongation factor Tu 2
- Protein YobF
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein bS21
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS9
Sequence:
MTMNITSKQMEITPAIRQHVADRLAKLEKWQTHLINPHIILSKEPQGFVADATINTPNGVLVASGKHEDMYTAINELINKLERQLNKLQHKGEARRAATSVKDANFVEEVEEE
Protein: RNA polymerase sigma factor SigB (P9WGI5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. A non-essential principal sigma factor that responds to cell envelope stress and hypoxia. Controls a regulon of about 40 genes, with another 100 genes expression being altered during SDS stress and about 50 gene being altered during diamide (oxidative) stress.
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- RNA polymerase-binding protein RbpA
- Iron-dependent repressor IdeR
- ECF RNA polymerase sigma factor SigH
- Transcriptional regulator WhiB1
- ECF RNA polymerase sigma factor SigE
- Zinc uptake regulation protein
Sequence:
MADAPTRATTSRVDSDLDAQSPAADLVRVYLNGIGKTALLNAAGEVELAKRIEAGLYAEHLLETRKRLGENRKRDLAAVVRDGEAARRHLLEANLRLVVSLAKRYTGRGMPLLDLIQEGNLGLIRAMEKFDYTKGFKFSTYATWWIRQAITRGMADQSRTIRLPVHLVEQVNKLARIKREMHQHLGREATDEELAAESGIPIDKINDLLEHSRDPVSLDMPVGSEEEAPLGDFIEDAEAMSAENAVIAELLHTDIRSVLATLDEREHQVIRLRFGLDDGQPRTLDQIGKLFGLSRERVRQIERDVMSKLRHGERADRLRSYAS
Protein: E3 ubiquitin-protein ligase RSL1 (EC 2.3.2.31) (Protein RING FINGER OF SEED LONGEVITY 1) (RING-type E3 ubiquitin transferase RSL1) (F4ITM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. Negative regulator of the abscisic acid (ABA) signaling pathway which targets PYL4 and PYR1 ABA receptors in plasma membrane to promote their FREE1/FYVE1-dependent trafficking and degradation upon ubiquitynation; this process involves clathrin-mediated endocytosis and trafficking through the ESCRT pathway. Involved in the maintenance of seed longevity. May enhance gibberellins responses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25330042}; Single-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:27495812}; Single-pass membrane protein {ECO:0000255}. Note=Localized transiently in the vacuole when in complex with PYL4 and PYR1. {ECO:0000269|PubMed:27495812}.
Interaction partners:
- Nuclear transcription factor Y subunit B-9
Sequence:
MEEDDLNPAGKPLYRLYFKGLVTEEKEMLLAGFGVAICGDKDDLLFDLKVSIHDPTITLLEVELIALKSGLNQAVSLGINHISICCDHEYIFELVMGISTPKQESIALLLRDVQGIRKYLTSSIPVMLTQNQSNLAYDFAIEAISSEIIIDIPAQKETCNICLNDDINADQMFSVDKSGHMCCSECVKRHIEVRLLEGSLITCPHYRCNSLLTSVRCGNLLTPKLNKMWEQKTKDELIPVMDRVYCPNPRCSTLMSETELSGLNIGVRRCCVKCGEPFCVKCKVSWHNNLSCDEYKTLHPNPTENDGRLRDLANEKSWRQCSKCKHMIELSSGCISVVCRCGHTFCYQCGADAGDCFHGLGRDDLDLTQCCGSCCCFVFFLVIIAIVVTIILLVRRFS
Protein: Uncharacterized protein (Q38AA4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTFEQCSGSRCGSSDFFYVCKSEAENRLRDFLSQLVEGVRSEEALFRATCGPRVAWNPYRPARGEHIRQGVLNSEIYEWRSRVPEDSLALVGNPLVMKESFNHSLATGCQRTGGLERVTEICESLVCEPSETNVEARTKAHTSLTSFEDDGVTREFTISDSCPVIYNEDVLRRVVAGVFDVLWRTVAVPWINEQYDGQSSPFHEKAPVAQHTAPFTPVRARNEEHSKHILQGGQELQPQHPRRWQHRQITSDTTRKPPPPQQGLTIVPGVTPLRGLPALSVQRDVHSVSPGDYRRAVTHLEVHTGERHDQLGLAGKSDAYLAKDPGGTKQHRGSSCVLKLRREDSKGKIEMVHPASGNPVCPKQSPSSRQLSPQDIRYSFDDITSAQRLTSRLTQTLCGDRVGTGVRGDISSRLGRCHRLAPVLIGVKQPPQPNHFPSPRRLQRQP
Protein: External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial (EC 1.6.5.9) (External alternative NADH dehydrogenase NDB1) (NADH:ubiquinone reductase (non-electrogenic) NDB1) (Q9ST62)
Organism: Solanum tuberosum (Potato)
Function: Calcium-dependent NAD(P)H dehydrogenase. Binds calcium ions (By similarity). Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10571867}; Peripheral membrane protein {ECO:0000269|PubMed:10571867}; Intermembrane side {ECO:0000269|PubMed:10571867}. Peroxisome {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
Sequence:
MRGFTYLSKVLHSHSSYSKLLVLCSVSTGGLLVYAESNVESGKQVVEQNQPESKKKRVVVLGTGWGGTSFLKDVDISSYDVQVVSPRNYFAFTPLLPSVTCGTVEARSIVEPVRNIIKKRSGEIQFWEAECLKIDPVNRTVSCRSGINDNLAGHNDFSLQYDYLVVAVGAQVNTFNTPGVMEHCHFLKEVEDAQRIRRTVIDCFEKSVIPGLSEEERRTNLHFVIVGGGPTGVEFAAELHDYVYEDLVKIYPSVKDFVKITVIQSGDHILNTFDERISSFAEQKFQRDGIEVSTGCRVTSVSDHFINMKVKSTGKHVEVPYGMVVWSTGVGTRPFVKDFMEQVGQEKRRILATDEWLRVKGCSNVYALGDCASVDQHKVMEDISTIFEAADKDDSGTLSVEEFRDVLEDIIIRYPQVDLYLKNKHLLEAKDLFRDSEGNEREEVDIEGFKLALSHVDSQMKSLPATAQVAAQQGTYLARCLNRWDQCKSNPEGPRRFKSSGRHEFLPFEYRHLGQFAPLGGDQAAAELPGDWVSMGHSTQWLWYSVYASKQVSWRTRYLVVGDWVRRYIFGRDSSRI
Protein: Varv peptide E (P83835)
Organism: Viola arvensis (European field pansy) (Field violet)
Function: Probably participates in a plant defense mechanism. Has cytotoxic activity against human lymphoma U-937 GTB and human myeloma RPMI-8226/s cell lines.
Interaction partners:
Sequence:
GLPICGETCVGGTCNTPGCSCSWPVCTRN
Protein: ADAM metallopeptidase with thrombospondin type 1 motif, 13 (M0R609)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSQLCLWLPCQPFLAASIRGILTGAIFILGCWGLSDFQKSFLQDLEPKDLSSSFSRHTAPLTGHPSSHLQRLRQRRTSEDILHLELLVAVGPDVYQAHQEDTERYVLTNLNIGSELLRNPSLGAQLQVHLVKLIILSDSENTPNITTNITSSLMSVCEWSQTINPHDDRDPSHADLIIYITRFDLELPDGNQQVRGVTQQGGACSPSWSCLITEDTGFDLGVTIAHEIGHSFGLDHDGAPGSGSTCEARGHVMASDGAVPAGGALEWSTCSQRQLQHLLSTGQMHCLWDPPGLQSGLTWHQLVAQPGLFYSADDQCRVAFGAGAVACTFSREGLDVCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKARCRSLAELAPVAVVHGHWSSWGPHSPCSRSCGGGVITRRRWCNNPRPAFGGRACVGEDLQAKMCNTQACEKTQLEFMSEQCAQTDRHPLQLSQGSASFYHWDAAVQYSQGDTLCRHMCWAVGESFIVSRGDSFLDGTRCVPNGPREDGTVSLCLLGSCRTFGCDGKMDSQQVWDACQVCGGDNSTCTSQNGSFTAGRAREYVTFLIVTPNMTSAHVINHRPLFTHLAVRIQDHYIVSGKSSMSPNVTYPSLLEDYRVEYRVTLTEDQLPRLEEIHIRGPVRDDIEIQVYRRYGGEYGGLTHPDITFTYFQRKQQAAWVWAAKRGPCSVSCGAGLRWVTYSCQDQAQNKWVRNAQCQGSPQPPAWQEPCVSAPCPPHWVADDFGPCSVSCGGGLRERSLRCVEAHNGFLKTLPPAPCRAVAQQPAGEVENCNSQPCPTGWEVSDPSPCVSSACEPGLESGSGTCVPRVGDSEKPAMAGPCRPDDMSPVPEPCVRTTCSPGSGPVDTMSLGEEASSPVGSGKPSSQAEHVWTPLVGLCSISCGKGLKELYFLCMDSVLKMPVQEELCGLASKPPSRWEVCRARPCPARWETRVLAPCPVTCGGGRVPLAIHCVQLDHGRPVSVPHSKCWPAPRPGSFEDCSPEPCPAR
Protein: Protein DIA2 (Digs into agar protein 2) (Q08496)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: F-box protein component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity). The SCF(DIA2) complex is specifically involved in the pheromone induced degradation of phosphorylated TEC1. The SCF(DIA2) complex binds to DNA replication origins. Involved in DNA replication, genome stability, and the control of cell cycle, probably through its association to replication origins to facilitate the ubiquitination of another origin-binding protein. Required for invasive growth and growth under alkaline conditions.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Suppressor of kinetochore protein 1
- DNA polymerase alpha-binding protein
- Chromosome segregation in meiosis protein 3
- Mediator of replication checkpoint protein 1
- Topoisomerase 1-associated factor 1
- DNA replication licensing factor MCM7
- Cell division control protein 45
- Cell division control protein 53
- DNA replication complex GINS protein SLD5
- DNA replication licensing factor MCM2
Sequence:
MSSPGNSGVAIDSTVLKAIELGTRLFKSGEYLQAKRIFTNALRVCDSYSQEQIMRIRNAYQLDTARPDNKRLYHPRYIKILDNICACYEKLNDLKSCLDVSQRLLKLEPGNIKCYIRCTRTLIKLKDWKRAYKTCSRGLQLCNNDSNHLRQQKQFIKNNMVQKQDGKRSYIDPLEETKIAKKKKNNNVLESLPKKKIKGSTKKTDLVGNLPIEILPIIFQRFTTKELVTLSLVCNKWRDKILYHLDCFQEFNLAPINFKNFVKFMDFLQQNFTRTYRKYILSQVKVSSRITSEELRITQLLFSKMPKCINIERLILSMPTLTTTQIFKLMVRGGTDFFTRLLELSLMITYRPDKQHELEILQTCPLLKKIELIFVNSLVPIFDGNNSVGRDGSFNVMARHTNMQISTADNDEQGIVEEKVIYSELEKITLICDKKKIKNFPLCRALLRGQFPLLQKLTITGVTFPMNNQDIMNFQWLLNFPDLKELWIEDNDNCELSKFLQLLKFSNVWKNLEKLTFRENKLYPIVNLDEDQPVTNDDEVPSMLFYKENLQNLEKLDLMGTSISGSALTRLCEQEYLDGRKLRSLNIGNCPNIQFPNNHAHTARMILDVNAVLKRLSKLEEINLSHLSSLNDSTMKSFIINVPFLENLKRLDISHNFEITGISIYEFLKKFQMDHDNEAGGQPLAYLNIDGCSQVSHITVNMIRAQNLVTQVDCVYERDVWRKFGINSYSYS
Protein: Unconventional myosin-XVI (Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3) (Unconventional myosin-16) (Q5DU14)
Organism: Mus musculus (Mouse)
Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. May be involved in targeting of the catalytic subunit of protein phosphatase 1 during brain development (By similarity). Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9ERC1}. Note=Found in puncta in soma and processes of astrocytes and dissociated cerebellar cells with the morphology of migrating granule cells. {ECO:0000250|UniProtKB:Q9ERC1}.
Interaction partners:
Sequence:
MEIDQCLLESLPLGQRQRLVKRMRCEQIKAYYEREKVFQKQEGPLKRSKPGKRQKVRFGLADMIQDAVIHHHDKEVLQLLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLILAGANVFLQDVNGNIPLDYAVEGTESSAILLAYLDEKGVDLSSLRQIKLQRPLSMLTDVRHFLSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASESIEEMLLKAEIAWEEKMKESPSAPSLAQEELYEILHDLPDLSSKLSPLVLPIAKQDSLLEKDIMFKDTTKGLCKQESQDGPPETSMTSNCGKPEQVQVMPPAPSDDLATLSELNDSSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIILSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEHSLNKERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESSNTNAVYSPVKDGNGNVAFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSLISSYPSFKFGGHKSTLLSKRTASSMVGVNKNYLELSKLLKKKGTSTFLQRLERGEPATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGQAAEERCRLVLQRCKLQGWQIGVHKVFLKYWHVDQLSDLWLQLQRKIVTCQKVIRGFLARQHLLQRMSIKQQEVTSIKSFLQSTEDMALKTYDALVIQNASDIAREHDRLRKEVHTAYHRNRQEEGTKRAEDQGGCRHVHSNSVPVPMVVDSLAQALTGPSTRPPSLHSVFSMDDSTGLPSPRKQPPPKPKRDPNTRLSASYEAVSACLSAAKDAAGEALTRPRPHSDDYSTMKKIPPRKPKRSPHTKLSGSYEEIWGPPRPSGTMGQGGRHQAPGTLSVQWARPDSVPQCTPQLPLHLPLPQGDYDDDAEPVYIEMVGNAARAGGSETDSPDQGESVYEEMKYILPEEGCGLGMLTFLPASPPLFLETRKAIILEAAEGNCQPSKDTCDIPPPFPNLLPHRPPLLVFPPTPVTRSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKAQKGDNDQLASPGFPVFNGPSRISPPATPPPPPGPPPAPCGPPPAPCGPPPAPCGPPPAPCGPPPAPCGPPPAPCGAASASCGVAPAPCRPPTHFAFPPESVLVTAAKALTNSDLPRTQPKPSSAPVPGPCSSFVKAPYSPGKTARADLRKTSSTFSPPSPYSPPNSRPLSSPLDELASLFNSGRSVLRRSAVGRRIREAEGFETNMNLSSRDEPSSSEMASETQDRNANNHGTQLSSSLSSDVTAENGNPVTNGLAEDDGCSRLCLSGMGTSSFQRNRESHTTQVIHQLRLSENESVALQELLDWRRKLCEAREGWQEALQHPEPRAPPPPPCKKPTLLKKPEGGSCTRLPSQLWDSSM
Protein: Placenta growth factor (PlGF) (P49764)
Organism: Mus musculus (Mouse)
Function: Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Also promotes cell tumor growth (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Vascular endothelial growth factor receptor 1
- Vascular endothelial growth factor receptor 3
- Vascular endothelial growth factor receptor 2
- Neuropilin-1
- Neuropilin-2
- Angiopoietin-1 receptor
- Platelet-derived growth factor receptor beta
- Vascular endothelial growth factor A, long form
- Macrophage colony-stimulating factor 1 receptor
- Platelet-derived growth factor receptor alpha
Sequence:
MLVMKLFTCFLQVLAGLAVHSQGALSAGNNSTEVEVVPFNEVWGRSYCRPMEKLVYILDEYPDEVSHIFSPSCVLLSRCSGCCGDEGLHCVPIKTANITMQILKIPPNRDPHFYVEMTFSQDVLCECRPILETTKAERRKTKGKRKRSRNSQTEEPHP
Protein: Nuclear receptor corepressor 1 (E7EW50)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSSGYPPNQGAFSTEQSRYPPHSVQYTFPNTRHQQEFAVPDYRSSHLEVSQASQLLQQQQQQQLRRRPSLLSEFHPGSDRPQERRTSYEPFHPGPSPVDHDSLESKRPRLEQVSDSHFQRVSAAVLPLVHPLPEGLRASADAKKDPAFGGKHEAPSSPISGQPCGDDQNASPSKLSKEELIQSMDRVDREIAKVEQQILKLKKKQQQLEEEAAKPPEPEKPVSPPPVEQKHRSIVQIIYDENRKKAEEAHKIFEGLGPKVELPLYNQPSDTKVYHENIKTNQVMRKKLILFFKRRNHARKQREQKICQRYDQLMEAWEKKVDRIENNPRRKAKESKTREYYEKQFPEIRKQREQQERFQRVGQRGAGLSATIARSEHEISEIIDGLSEQENNEKQMRQLSVIPPMMFDAEQRRVKFINMNGLMEDPMKVYKDRQFMNVWTDHEKEIFKDKFIQHPKNFGLIASYLERKSVPDCVLYYYLTKKNENYKALVRRNYGKRRGRNQQQIARPSQEEKVEEKEEDKAEKTEKKEEEKKDEEEKDEKEDS
Protein: EMAP-like 1 (Echinoderm microtubule-associated protein-like 1) (E7EXY5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Coiled-coil domain-containing protein 85C-A
Sequence:
MEDGFSSYSSLYDTSSLLQFCNDDSASATSSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNKKGPTKARPMIAALPLRPTVNNGTVLPKKGGTLPSPSNCKKDNNSPATRSTVKRTSSSEHVGPNNRKDSGVDSKNNRTRAGSTGSNSSGKKTTETKQREPVFSADEGYVKMYLKGRPITMYMPKDLVDTYCLETKADLPPKKLKLDWVYGYRGRDCRSNLYLLPTGETVYFIASVVVLYNVDEQLQRHYTGHTDDIKCLAVHPDKITIATGQVAGTSSDGKQLAPHVRVWDSVSLNTLHILGNGFFDRALVCLSFSKSNGGSWLCVVDDSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPTDANIIVTCGKSHLCFWSLEKGSLVKKQGLFEKQEKPKFVLCVTFSENGDAITGDSSGNILVWGKGSNRISLAIQGAHEASVFALCMLRNGTLVSGGKDRKLISWDENFQKIQTVEVPELYGPVRTVAEGRGETVLIGTTKNYVLQGSLNGEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWDSDSHQPIWTKTLEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKDLVTVHTDGNEQLSVIRFSPDGNFLAIGSHDNYIYIYAVAENGKKYSRVGKCSGHSSFITHLDWSVDSQYLVSNSGDYEILYWIPSVCKQVVSVETTRDIEWATFTCTLGFHVFGLWPDGSDGTDINAVCSSYAKRLLVTGDDFGKVHLFSFPCSQSRAPSHIYSGHSSHVTNVNFLFDDSHLVSTGGKDMSIMQWRVV
Protein: Furin (EC 3.4.21.75) (Dibasic-processing enzyme) (Paired basic amino acid residue-cleaving enzyme) (PACE) (Prohormone convertase 3) (P23188)
Organism: Mus musculus (Mouse)
Function: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (By similarity). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-45) (By similarity). By mediating processing of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the acidification of dense-core secretory granules in islets of Langerhans cells.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000250|UniProtKB:Q28193}. Endosome membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Note=Shuttles between the trans-Golgi network and the cell surface. Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin. {ECO:0000250|UniProtKB:P09958}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Prothrombin
- Transmembrane protease serine 2
- Angiotensin-converting enzyme 2
- Stromelysin-3
- Fibrillin-1
- Matrix metalloproteinase-14
- Vitamin K-dependent protein C
- Collagen alpha-1
- Phosphofurin acidic cluster sorting protein 1
Sequence:
MELRSWLLWVVAAAGAVVLLAADAQGQKIFTNTWAVHIPGGPAVADRVAQKHGFHNLGQIFGDYYHFWHRAVTKRSLSPHRPRHSRLQREPQVKWLEQQVAKRRAKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKEAWAQGFTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNADDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIVEILVEPKDIGKRLEVRKAVTACLGEPNHITRLEHVQARLTLSYNRRGDLAIHLISPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPAGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLSTPPESSGCKTLTSSQACVVCEEGYSLHQKSCVQHCPPGFIPQVLDTHYSTENDVEIIRASVCTPCHASCATCQGPAPTDCLSCPSHASLDPVEQTCSRQSQSSRESRPQQQPPALRPEVEMEPRLQAGLASHLPEVLAGLSCLIIVLIFGIVFLFLHRCSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL
Protein: Tetra-peptide repeat homeobox-like protein (Q17RH7)
Organism: Homo sapiens (Human)
Function: Transcription factor required for zygotic genome activation (ZGA), a critical event in early embryonic development during which the developmental control passes from maternally provided mRNAs to the expression of the zygotic genome after fertilization. Protein produced from maternal transcripts that binds and activates expression of key ZGA marker genes, such as NANOGNB, ZSCAN4, DUXB, KLF5 and DPPA3. Binds to regulatory DNA sequences containing a 5'-TAATCC-3' sequence motif (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:36074823}.
Interaction partners:
Sequence:
MQDPRHPQGLPLSPGLPKRQRQDRTIYNWKQQEVLENHFKEEQYPDYDTRQELAEMLNLREYQVQVWFKNRRAKRSRERWFQKQLQQLQKHPQQQHPQQQHPQQQLQQQQPQQQPQQQQPQQQPQQQQPQQQQLHQQPQ
Protein: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha) (Q42523)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Biotin-attachment subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic
- Probable enoyl-CoA hydratase 2, mitochondrial
- Ribulose bisphosphate carboxylase large chain, catalytic domain-containing protein
- Ribulose bisphosphate carboxylase large chain
- Putative uncharacterized mitochondrial protein AtMg00280
- Probable enoyl-CoA hydratase 1, peroxisomal
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Probable acyl-CoA dehydrogenase IBR3
Sequence:
MSMMTVWALRRNVRRKNHSMLVRYISGSASMKPKEQCIEKILVANRGEIACRIMRTAKRLGIQTVAVYSDADRDSLHVKSADEAVRIGPPSARLSYLSGVTIMEAAARTGAQAIHPGYGFLSESSDFAQLCEDSGLTFIGPPASAIRDMGDKSASKRIMGAAGVPLVPGYHGHEQDIDHMKSEAEKIGYPIIIKPTHGGGGKGMRIVQSGKDFADSFLGAQREAAASFGVNTILLEKYITRPRHIEVQIFGDKHGNVLHLYERDCSVQRRHQKIIEEAPAPNISEKFRANLGQAAVSAARAVGYYNAGTVEFIVDTESDQFYFMEMNTRLQVEHPVTEMIVGQDLVEWQIRVANGEPLPLSQSEVPMSGHAFEARIYAENVPKGFLPATGVLNHYRPVAVSPSVRVETGVEQGDTVSMHYDPMIAKLVVWGGNRGEALVKLKDCLSNFQVAGVPTNINFLQKLASHKEFAVGNVETHFIEHHKSDLFADESNPAATEVAYKAVKHSAALVAACISTIEHSTWNESNHGKVPSIWYSNPPFRVHHEAKQTIELEWNNECEGTGSNLISLGVRYQPDGSYLIEEGNDSPSLELRVTRAGKCDFRVEAAGLSMNVSLAAYLKDGYKHIHIWHGSEHHQFKQKVGIEFSEDEEGVQHRTSSETSSHPPGTIVAPMAGLVVKVLVENEAKVDQGQPILVLEAMKMEHVVKAPSSGSIQDLKVKAGQQVSDGSALFRIKG
Protein: TBC1 domain family member 2B (C9JW56)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MITTTKELAPNRQLMTYWLQELQQKRWEYCNSLDMVKWDSRTSPTPGDFPKGLVARDNTDLIYPHPNASAEKARNVLAVETVPGELVGEQAANQPAPGHPNSINFYSLKQWGNELKNSMSSFRPGRGHNDSRRTVFYTNEEWELLDPTPKDLEESIVQEEKKKLTPEGNKGVTGSGFPFDFGRNPYKGKRPLKDIIGSYKNRHSSGDPSSEGTSGSGSVSIRKPASEMQLQVQSQQEELEQLKKDLSSQKELVRLLQQTVRSSQYDKYFTSSRLCEGVPKDTLELLHQKDD
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (MutY homolog) (mMYH) (Q99P21)
Organism: Mus musculus (Mouse)
Function: Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities.
Subcellular location: Nucleus {ECO:0000269|PubMed:14742662}. Mitochondrion {ECO:0000269|PubMed:14742662}.
Interaction partners:
- N-glycosylase/DNA lyase
- DNA mismatch repair protein Msh6
- Endonuclease III-like protein 1 lyase)
- DNA repair nuclease/redox regulator APEX1
- Endonuclease 8-like 3
- Uracil-DNA glycosylase
- DNA polymerase beta
- Cell cycle checkpoint control protein RAD9A
- G/T mismatch-specific thymine DNA glycosylase
- Oxidized purine nucleoside triphosphate hydrolase
Sequence:
MKKLQASVRSHKKQPANHKRRRTRALSSSQAKPSSLDGLAKQKREELLQASVSPYHLFSDVADVTAFRSNLLSWYDQEKRDLPWRNLAKEEANSDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYQRVQRGQLSALPGRPDIEECALNTRQCQLCLTSSSPWDPSMGVANFPRKASRRPPREEYSATCVVEQPGAIGGPLVLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHKALLQELQRWCGPLPAIRLQHLGEVIHIFSHIKLTYQVYSLALDQAPASTAPPGARWLTWEEFCNAAVSTAMKKVFRMYEDHRQGTRKGSKRSQVCPPSSRKKPSLGQQVLDTFFQRHIPTDKPNSTTQ
Protein: Protein TENP (O42273)
Organism: Gallus gallus (Chicken)
Function: May play a role in the developmental transition from cell proliferation to cell differentiation during neurogenesis.
Interaction partners:
- Mucin-5B
- Uncharacterized protein.
- Ovotransferrin
- Uncharacterized protein.
- Ovotransferrin
- Vitelline membrane outer layer protein 1
- Ovotransferrin
- Ovalbumin-related protein Y
- Ovoinhibitor
- Ovomucoid
Sequence:
MGALLALLDPVQPTRAPDCGGILTPLGLSYLAEVSKPHAEVVLRQDLMPKEPQTCSLAPWSPAGTELPAVKVADLWLSVIPEAGLRLGIEVELRIAPLHTVPMPVRISIRADLHVDMGPDGNLQLLTSACRPTVQAQSTREAESKSSRSILDKVVDVDKLCLDVSKLLLFPNEQLMSLTALFPVTPNCQLQYLALAAPVFSKQGIALSLQTTFQVAGAVVPVPVSPVPFSMPELASTSTSHLILALSEHFYTSLYFTLERAGAFNMTIPSMLTTATLAQKITQVGSLYHEDLPITLSAALRSSPRVVLEEGRAALKLFLTVHIGAGSPDFQSFLSVSADVTRAGLQLSVSDTRMMISTAVIEDAELSLAASNVGLVRAALLEELFLAPVCQQVPAWMDDVLREGVHLPHMSHFTYTDVNVVVHKDYVLVPCKLKLRSTMA