wanglab/gogpt-training-data huggingface dataset:
Protein: Homoisocitrate dehydrogenase, mitochondrial (HIcDH) (EC 1.1.1.87) (P40495)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the NAD(+)-dependent conversion of homoisocitrate to alpha-ketoadipate.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Homoaconitase, mitochondrial
- Homocitrate synthase, mitochondrial
- Citrate synthase, mitochondrial
- Triosephosphate isomerase
- Saccharopine dehydrogenase [NADP
- Aromatic/aminoadipate aminotransferase 1
- Homocitrate synthase, cytosolic isozyme
- Isocitrate dehydrogenase subunit 1, mitochondrial
- 3-isopropylmalate dehydratase
- Homocitrate dehydratase, mitochondrial
Sequence:
MFRSVATRLSACRGLASNAARKSLTIGLIPGDGIGKEVIPAGKQVLENLNSKHGLSFNFIDLYAGFQTFQETGKALPDETVKVLKEQCQGALFGAVQSPTTKVEGYSSPIVALRREMGLFANVRPVKSVEGEKGKPIDMVIVRENTEDLYIKIEKTYIDKATGTRVADATKRISEIATRRIATIALDIALKRLQTRGQATLTVTHKSNVLSQSDGLFREICKEVYESNKDKYGQIKYNEQIVDSMVYRLFREPQCFDVIVAPNLYGDILSDGAAALVGSLGVVPSANVGPEIVIGEPCHGSAPDIAGKGIANPIATIRSTALMLEFLGHNEAAQDIYKAVDANLREGSIKTPDLGGKASTQQVVDDVLSRL
Protein: Tryparedoxin peroxidase (Q9GU47)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MLRRFSMLPLSGGIARRSFFRTAPLFNLDYQAYRTATVREAAPEFAGKAVVDGKIKDISMNDYKGKYIVLFFYPLDFTFVCPTEIVSFSDSHAEFEKLNTQVIAVSCDSHFSHLAWVETPRKKGGLGEMKIPLLSDFTKEISRDYGVLVEEQGLSLRALFVIDDKGILRHVTINDLPVGRNVDEVLRVVQAFQYADKTGDVIPCNWKPGKETMKVEAAKEYFEKNL
Protein: Protein twisted gastrulation (P54356)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in dorsal-ventral patterning. Required for specification of a narrow strip of dorsal midline cells that will give rise to the amnioserosa, but not for specification of dorsal ectoderm cells. Inhibits BMP signaling; enhances the binding of sog to dpp, thus enhancing the antagonistic activity of sog.
Subcellular location: Secreted.
Interaction partners:
- Dorsal-ventral patterning protein Sog
- Protein screw
- Crossveinless 2
- Dorsal-ventral patterning protein tolloid
- Protein decapentaplegic
Sequence:
MQLLCYFVILFVGIAPWSSLANDDGCNEVVCGSVVSKCLITQSCQCKLNDCHCCKDCLNCLGELYIECCGCLDMCPKHKDVLPSLTPRSEIGDIEGVPELFDTLTAEDDEGWSTIRFSMRAGFKQRVQGGASGDAGNGNGNGNAGSAGVTLCTVIYVNSCIRANKCRQQCESMGASSYRWFHDGCCECVGENCLNYGINESRCRGCPEDQDQLLTADTVPAEAEQDLERFFGNEEIEDEWGYGEEDEFS
Protein: Nuclear hormone receptor family member nhr-76 (Q65CM0)
Organism: Caenorhabditis elegans
Function: Ligand-activated transcription factor (By similarity). Involved in modulating serotonin-mediated induction of adipose triglyceride lipase atgl-1, thereby regulating body fat.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Protein kinase domain-containing protein
- SAND domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- Nuclear hormone receptor family member nhr-49
Sequence:
MEVLGKQKVLAMMKLNGAGQLTGYPFETPSSSTTTPSVPPSFPHSSNPNAYMKPSPPSAISSPPSTSSCSSASEKKECAVCKNPNSSGYHFGCIACAACSAFFRRTVVLSRRYYCRRDPVGNSLCPLDRRHRSNCRACRYVRCIDMGMNPSSVQNLRDSIKPRSPAEMIQEAEEEDKKEKLDDILFSAATPGSWISSTSTCNEPLPVAPKEIPGENYIETLAALYKNSVERRRMFYCNGSLREMLGGTGLKMRPTRFDERYYKEKMRFELVLYVEMMNSMSVFRQMDLDTKETLVKGCAVSLAMLEKYYISVKYDGLRTQKLIAPDGSYTDLSDHGAQFDDEFTQITESVMDKETCLKLLYDPLRSCLNELGSALEHSRMTDTEFCALFAILLFNTAADNLSDASRNAVVMARNRVMKDWFEFYAKQGIDPHEAGLLVGNTLLLLTAVRNAMAVHRENFHVIRVFNVMEYDKLIDDLAFT
Protein: DNA polymerase processivity factor component OPG148 (P20995)
Organism: Vaccinia virus (strain Copenhagen) (VACV)
Function: Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein OPG116. Serves as a bridge which links the DNA polymerase OPG071 and the uracil DNA glycosylase.
Interaction partners:
Sequence:
MTSSADLTNLKELLSLYKSLRFSDSAAIEKYNSLVEWGTSTYWKIGVQKVANVETSISDYYDEVKNKPFNIDPGYYIFLPVYFGSVFIYSKGKNMVELGSGNSFQIPDDMRSACNKVLDSDNGIDFLRFVLLNNRWIMEDAISKYQSPVNIFKLASEYGLNIPKYLEIEIEEDTLFDDELYSIIERSFDDKFPKISISYIKLGELRRQVVDFFKFSFMYIESIKVDRIGDNIFIPSVITKSGKKILVKDVDHLIRSKVREHTFVKVKKKNTFSILYDYDGNGTETRGEVIKRIIDTIGRDYYVNGKYFSKVGSAGLKQLTNKLDINECATVDELVDEINKSGTVKRKIKNQSAFDLSRECLGYPEADFITLVNNMRFKIENCKVVNFNIENTNCLNNPSIETIYRNFNQFVSIFNVVTDVKKRLFE
Protein: 40S ribosomal protein S12 (Q6FP23)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Large ribosomal subunit protein uL23
- RP41
- 40S ribosomal protein S8
- Small ribosomal subunit protein eS21
- L21
- 60S acidic ribosomal protein P0
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein uS5
- Candida glabrata strain CBS138 chromosome M complete sequence
- Small ribosomal subunit protein eS6
Sequence:
MSDVEEVVEVQEEVVEQTAEVSIEDALKVVLRTALVHDGLARGLRESTKALTRHEAQLVVLVSSVTEDNIIKLVEGLANDPNNKVPLIKVADAKQLGEWAGLGKIDRDGNARKVVGASVVVVKKWGAETDERNMILEHFSQQ
Protein: Putative sulfurtransferase DsrE (EC 2.8.1.-) (Intracellular sulfur oxidation protein DsrE) (O87896)
Organism: Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
Function: Not known. Could be involved in the oxidation of intracellular sulfur.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Intracellular sulfur oxidation protein DsrF
- DsrH
- Sulfur carrier protein TusA
- Sulfurtransferase
- Sulfur relay protein, TusE/DsrC/DsvC family
- Sulfur relay protein, TusE/DsrC/DsvC family
- DsrM
- DsrB
- DsrK
- Sulfite reductase, dissimilatory-type subunit alpha
Sequence:
MKFALQINEGPYQHQASDSAYQFAKAALEKGHEIFRVFFYHDGVNNSTRLTTPPQDDRHIVNRWAELAEQYELDMVVCVAAAQRRGIVDEGEASRNGKDATNIHPKFRISGLGQLVEAAIQADRLVVFGD
Protein: Dihydropyrimidinase-related protein 3 (DRP-3) (Collapsin response mediator protein 4) (CRMP-4) (Unc-33-like phosphoprotein 1) (ULIP-1) (Q14195)
Organism: Homo sapiens (Human)
Function: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Colocalizes with synaptic vesicle protein 2 in the central region of the growth cone. {ECO:0000250}.
Interaction partners:
- Dihydropyrimidinase-related protein 2
- Dihydropyrimidinase-related protein 1
- Dihydropyrimidinase-related protein 5
- Dihydropyrimidine dehydrogenase [NADP
- Semaphorin-3A
- Dihydropyrimidinase
- Plexin-A2
- Dihydropyrimidinase-related protein 4
- Plexin-A1
- Transforming protein RhoA
Sequence:
MSYQGKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIVSAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSDYVYKRIKARRKMADLHAVPRGMYDGPVFDLTTTPKGGTPAGSARGSPTRPNPPVRNLHQSGFSLSGTQVDEGVRSASKRIVAPPGGRSNITSLS
Protein: Semaphorin-3G (Semaphorin sem2) (Q9NS98)
Organism: Homo sapiens (Human)
Function: Has chemorepulsive activities for sympathetic axons. Ligand of NRP2 (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Neuropilin-1
- Plexin-A3
- Neuropilin-2
Sequence:
MAPSAWAICWLLGGLLLHGGSSGPSPGPSVPRLRLSYRDLLSANRSAIFLGPQGSLNLQAMYLDEYRDRLFLGGLDALYSLRLDQAWPDPREVLWPPQPGQREECVRKGRDPLTECANFVRVLQPHNRTHLLACGTGAFQPTCALITVGHRGEHVLHLEPGSVESGRGRCPHEPSRPFASTFIDGELYTGLTADFLGREAMIFRSGGPRPALRSDSDQSLLHDPRFVMAARIPENSDQDNDKVYFFFSETVPSPDGGSNHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKSLEVYALFSTVSAVFQGFAVCVYHMADIWEVFNGPFAHRDGPQHQWGPYGGKVPFPRPGVCPSKMTAQPGRPFGSTKDYPDEVLQFARAHPLMFWPVRPRHGRPVLVKTHLAQQLHQIVVDRVEAEDGTYDVIFLGTDSGSVLKVIALQAGGSAEPEEVVLEELQVFKVPTPITEMEISVKRQMLYVGSRLGVAQLRLHQCETYGTACAECCLARDPYCAWDGASCTHYRPSLGKRRFRRQDIRHGNPALQCLGQSQEEEAVGLVAATMVYGTEHNSTFLECLPKSPQAAVRWLLQRPGDEGPDQVKTDERVLHTERGLLFRRLSRFDAGTYTCTTLEHGFSQTVVRLALVVIVASQLDNLFPPEPKPEEPPARGGLASTPPKAWYKDILQLIGFANLPRVDEYCERVWCRGTTECSGCFRSRSRGKQARGKSWAGLELGKKMKSRVHAEHNRTPREVEAT
Protein: P-granule-associated novel protein 1 (Q9U3A0)
Organism: Caenorhabditis elegans
Function: Regulates diverse developmental processes including larval molting and gonad maturation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22342905, ECO:0000269|PubMed:23682709, ECO:0000269|PubMed:33950834}. Apical cell membrane {ECO:0000269|PubMed:22342905, ECO:0000269|PubMed:23682709, ECO:0000269|PubMed:33950834}; Single-pass type I membrane protein {ECO:0000269|PubMed:22342905, ECO:0000269|PubMed:23682709}. Note=Detected throughout the cytoplasm in germline and somatic blastomeres during embryogenesis and in germline and somatic tissue in adult hermaphrodites. Localizes to P-granules in L1 larval Z2 and Z3 germline precursor cells. Expression in P-granules is most pronounced during the meiotic stage of the germline; in mature oocytes and sperm expression switches to a cytoplasmic pattern. {ECO:0000269|PubMed:22342905, ECO:0000269|PubMed:23682709}.
Interaction partners:
- Apple domain-containing protein
- Latrophilin-like protein 1
- Inactive angiotensin-converting enzyme-related protein
- Uncharacterized protein
- Transthyretin-like family protein
Sequence:
MRSLLSFVLLALARIAISEETKSCIDIEKGFKEEFNAHKQPVCICADNGIFSTVKGFTIECESASIASVSENLASLNGTELGRLTIRDSTVNVLPQDLFENVFAKQVKLERCGLSTLQPNSFQSLGGSAELLSLRENRIKKLEKGLFTGLKSLKTLDLAMNKIQEIDVGAFEELKKVEELLLNENDIRVLKTGTFDGMKNLKKLTLQNCNLEIIQKGAFRGLNSLEQLILSNNNLENIDWTIFSALKNLRVLDLGSNKISNVEMKSFPKLEKLVLNNNTIDSMKSIKLKDLPSLVVALFDRNKIESIGDMDMFGLTRSDRIETLSLARNNLSQISPKAFQHTPNLITLLLQYNQIEELSSHSPSQVRTPFLASLKKLVTLQLSSNNLSVIRSDELPKSLSSLALDHNVISKIEARALEGMEIKRLYLHSNKLNYLYQGTFDSFSPKSVEAVDVSLNPWVCVCNDPKEWLPRWLEASEEADVAEGALGCLAIPNCGQKEGSTVMPEEEEVYRSGWITVAATILTIVTIVIMVIIAMLYFKDARYQFPLRGRRSDSDLHKLIENDPLNIASDSILVVPAMPKRNTGPKKTVRFQNF
Protein: Uncharacterized lipoprotein YjbH (P32689)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Uncharacterized lipoprotein YjbF
- Uncharacterized protein YjbG
- Uncharacterized protein YjbE
- Uncharacterized lipoprotein GfcB
- Uncharacterized protein GfcC
- Colanic acid biosynthesis protein WcaK
- UDP-glucose 6-dehydrogenase
- Inner membrane protein YcfT
- Putative colanic acid biosynthesis glycosyl transferase WcaC
Sequence:
MKKRHLLSLLALGISTACYGETYPAPIGPSQSDFGGVGLLQTPTARMAREGELSLNYRDNDQYRYYSASVQLFPWLETTLRYTDVRTRQYSSVEAFSGDQTYKDKAFDLKLRLWEESYWLPQVAVGARDIGGTGLFDAEYLVASKAWGPFDFTLGLGWGYLGTSGNVKNPLCSASDKYCYRDNSYKQAGSIDGSQMFHGPASLFGGVEYQTPWQPLRLKLEYEGNNYQQDFAGKLEQKSKFNVGAIYRVTDWADVNLSYERGNTFMFGVTLRTNFNDLRPSYNDNARPQYQPQPQDAILQHSVVANQLTLLKYNAGLADPQIQAKGDTLYVTGEQVKYRDSREGIIRANRIVMNDLPDGIKTIRITENRLNMPQVTTETDVASLKNHLAGEPLGHETTLAQKRVEPVVPQSTEQGWYIDKSRFDFHIDPVLNQSVGGPENFYMYQLGVMGTADLWLTDHLLTTGSLFANLANNYDKFNYTNPPQDSHLPRVRTHVREYVQNDVYVNNLQANYFQHLGNGFYGQVYGGYLETMFGGAGAEVLYRPLDSNWAFGLDANYVKQRDWRSAKDMMKFTDYSVKTGHLTAYWTPSFAQDVLVKASVGQYLAGDKGGTLEIAKRFDSGVVVGGYATITNVSKEEYGEGDFTKGVYVSVPLDLFSSGPTRSRAAIGWTPLTRDGGQQLGRKFQLYDMTSDRSVNFR
Protein: Polyribonucleotide nucleotidyltransferase 1, chloroplastic (AtcpPNPase) (EC 2.7.7.8) (Polynucleotide phosphorylase 1) (PNPase 1) (Protein PIGMENT DEFECTIVE 326) (Protein RESISTANT TO INHIBITION WITH FSM 10) (Q8GZQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the metabolism of all major classes of plastid RNAs. Required for efficient 3'-end processing of mRNAs and 3'-end maturation of rRNA transcripts, but is not sufficient to mediate their degradation. Mediates tRNA degradation. May function as a poly(A) mRNA 3'-5' degrading phosphorylase. May be required for plastid ribosome assembly and non-coding RNA biogenesis and accumulation. Seems not required for efficient translation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12486011, ECO:0000269|PubMed:18469163}.
Interaction partners:
- Ribonuclease II, chloroplastic/mitochondrial
- Polyribonucleotide nucleotidyltransferase 2, mitochondrial
- Ribonuclease E/G-like protein, chloroplastic
- Ribonuclease J
- Exosome complex exonuclease RRP44 homolog A
- Pentatricopeptide repeat-containing protein MRL1, chloroplastic
- 50S ribosomal protein L24
- At3g27906
- Probable eukaryotic translation initiation factor 5-1
- Inactive exonuclease DIS3L2
Sequence:
MLTSPSNALHSSTPQFWPLRRSKLCRSRNFPRFHSGERSSGGGGKLCSLSLLSGSGAGKFSVRALVRPDDTDDADSVGDGSLAFPNHVSVKIPFGNREILVETGLMGRQASSAVTVTDGETIVYTSVCLADVPSEPSDFLPLYVHYQERFSAVGRTSGGFFKREGRTKDHEVLICRLIDRPLRPTMPKGFYNETQILSWVLSYDGLHAPDALAVTSAGIAVALSEVPNAKAIAGVRVGLIGGEFIVNPTVKEMEESQLDLFLAGTDTAILTIEGYSNFLPEEMLLQAVKVGQDAVQATCIAIEVLAKKYGKPKMLDAIRLPPPELYKHVKELAGEELTKALQIKSKISRRKAISSLEEKVLTILTEKGYVIDEVAFGTIEAQPDLLEDEDEDEEVVPEGEVDQGDVHIRPIPRKPIPLLFSEVDVKLVFKEVSSKLLRRRIVEGGKRSDGRTLDEIRPINSRCGLLPRAHGSTLFTRGETQALAVVTLGDKQMAQRIDNLEGSDEYKRFYLQYTFPPSSVGEVGRIGAPSRREIGHGTLAERALETILPSDDDFPYTIRVESTVIESNGSSSMASVCGGCLALQDAGVPVKCSVAGIAMGMVWDTEEFGGDGSPLILSDITGAEDASGDMDFKVAGNEDGVTAFQMDIKVGGITLEIMEKALIQAKAGRRHILAEMAKCSPPPTLSLSKYAPLILIMKVHPSKVYSLIGSGGKKVKSIIEESGVEAIDMQDDGTVKIMAIDVASLERAKAIISGLTMVPSVGDIYRNCEIKSMAPYGAFVEIAPGREGLCHISELSAEWLAKPEDAYKVGDRIDVKLIEVNEKGQLRLSVRALLPESETDKDSQKQQPAGDSTKDKSSQRKYVNTSSKDRAAAGASKVSSGDELVLKKKDVRRATGGSSDKTMNSNSSTNEESLVNGEATIS
Protein: Exosome complex component SKI6 (Extracellular mutant protein 20) (Ribosomal RNA-processing protein 41) (Superkiller protein 6) (P46948)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. SKI6 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Exosome complex component CSL4
- Exosome complex exonuclease RRP6
- Exosome complex component RRP4
- Exosome complex exonuclease DIS3
- Exosome complex component RRP42
- Superkiller protein 7
- ATP-dependent RNA helicase DOB1
- Exosome complex component RRP46
- Exosome complex component RRP40
- Exosome complex component MTR3
Sequence:
MSRLEIYSPEGLRLDGRRWNELRRFESSINTHPHAADGSSYMEQGNNKIITLVKGPKEPRLKSQMDTSKALLNVSVNITKFSKFERSKSSHKNERRVLEIQTSLVRMFEKNVMLNIYPRTVIDIEIHVLEQDGGIMGSLINGITLALIDAGISMFDYISGISVGLYDTTPLLDTNSLEENAMSTVTLGVVGKSEKLSLLLVEDKIPLDRLENVLAIGIAGAHRVRDLMDEELRKHAQKRVSNASAR
Protein: Heat shock protein 15 (HSP15) (P0ACG8)
Organism: Escherichia coli (strain K12)
Function: Involved in the recycling of free 50S ribosomal subunits that still carry a nascent chain. Binds RNA more specifically than DNA. Binds with very high affinity to the free 50S ribosomal subunit. Does not bind it when it is part of the 70S ribosome.
Interaction partners:
- 33 kDa chaperonin
- GMP/IMP nucleotidase YrfG
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL28
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL34
- ATP-dependent protease subunit HslV
- Large ribosomal subunit protein uL13
Sequence:
MKEKPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAALLYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFKHGDSE
Protein: LysT endolysin (A0A088FLK9)
Organism: Thermus phage 2631
Interaction partners:
Sequence:
MRILEPWNRWYRQKRAYRVRLTPIHYVVLHHTAGPENQTPEAIKRYHEEARGWPHIGYHYLVYRDGRVYKTLPNNAVPICVREFNPVSICVAAVGDFSAGVWPDDAPGWRALWELKQALAKAYPKALFVLHKNLVPTECPGRLTWELIQRKGGGGQ
Protein: Mucin-5B (Ovomucin, alpha-subunit) (Q98UI9)
Organism: Gallus gallus (Chicken)
Function: Ovomucin, the glycoprotein responsible for the gel properties of egg white, is composed for 2 subunits, alpha-ovomucin/MUC5B and beta-ovomucin/MUC6.
Subcellular location: Secreted.
Interaction partners:
- Uncharacterized protein.
- Uncharacterized protein.
- Protein TENP
- Uncharacterized protein.
Sequence:
MEIKKERSFWIFCLIWSFCKGKEPVQIVQVSTVGRSECTTWGNFHFHTFDHVKFTFPGTCTYVFASHCNDSYQDFNIKIRRSDKNSHLIYFTVTTDGVILEVKETGITVNGNQIPLPFSLKSILIEDTCAYFQVTSKLGLTLKWNWADTLLLDLEETYKEKICGLCGNYDGNKKNDLILDGYKMHPRQFGNFHKVEDPSEKCPDVRPDDHTGRHPTEDDNRCSKYKKMCKKLLSRFGNCPKVVAFDDYVATCTEDMCNCVVNSSQSDLVSSCICSTLNQYSRDCVLSKGDPGEWRTKELCYQECPSNMEYMECGNSCADTCADPERSKICKAPCTDGCFCPPGTILDDLGGKKCVPRDSCPCMFQGKVYSSGGTYSTPCQNCTCKGGHWSCISLPCSGSCSIDGGFHIKTFDNKKFNFHGNCHYVLAKNTDDTFVVIGEIIQCGTSKTMTCLKNVLVTLGRTTIKICSCGSIYMNNFIVKLPVSKDGITIFRPSTFFIKILSSAGVQIRVQMKPVMQLSITVDHSYQNRTSGLCGNFNNIQTDDFRTATGAVEDSAAAFGNSWKTRASCFDVEDSFEDPCSNSVDKEKFAQHWCALLSNTSSTFAACHSVVDPSVYIKRCMYDTCNAEKSEVALCSVLSTYSRDCAAAGMTLKGWRQGICDPSEECPETMVYNYSVKYCNQSCRSLDEPDPLCKVQIAPMEGCGCPEGTYLNDEEECVTPDDCPCYYKGKIVQPGNSFQEDKLLCKCIQGRLDCIGETVLVKDCPAPMYYFNCSSAGPGAIGSECQKSCKTQDMHCYVTECVSGCMCPDGLVLDGSGGCIPKDQCPCVHGGHFYKPGETIRVDCNTCTCNKRQWNCTDNPCKGTCTVYGNGHYMSFDGEKFDFLGDCDYILAQDFCPNNMDAGTFRIVIQNNACGKSLSICSLKITLIFESSEIRLLEGRIQEIATDPGAEKNYKVDLRGGYIVIETTQGMSFMWDQKTTVVVHVTPSFQGKVCGLCGDFDGRSRNDFTTRGQSVEMSIQEFGNSWKITSTCSNINMTDLCADQPFKSALGQKHCSIIKSSVFEACHSKVNPIPYYESCVSDFCGCDSVGDCECFCTSVAAYARSCSTAGVCINWRTPAICPVFCDYYNPPDKHEWFYKPCGAPCLKTCRNPQGKCGNILYSLEGCYPECSPDKPYFDEERRECVSLPDCTSCNPEEKLCTEDSKDCLCCYNGKTYPLNETIYSQTEGTKCGNAFCGPNGMIIETFIPCSTLSVPAQEQLMQPVTSAPLLSTEATPCFCTDNGQLIQMGENVSLPMNISGHCAYSICNASCQIELIWAECKVVQTEALETCEPNSEACPPTAAPNATSLVPATALAPMSDCLGLIPPRKFNESWDFGNCQIATCLGEENNIKLSSITCPPQQLKLCVNGFPFMKHHDETGCCEVFECQCICSGWGNEHYVTFDGTYYHFKENCTYVLVELIQPSSEKFWIHIDNYYCGAADGAICSMSLLIFHSNSLVILTQAKEHGKGTNLVLFNDKKVVPDISKNGIRITSSGLYIIVEIPELEVYVSYSRLAFYIKLPFGKYYNNTMGLCGTCTNQKSDDARKRNGEVTDSFKEMALDWKAPVSTNRYCNPGISEPVKIENYQHCEPSELCKIIWNLTECHRVVPPQPYYEACVASRCSQQHPSTECQSMQTYAALCGLHGICVDWRGQTNGQCEATCARDQVYKPCGEAKRNTCFSREVIVDTLLSRNNTPVFVEGCYCPDGNILLNEHDGICVSVCGCTAQDGSVKKPREAWEHDCQYCTCDEETLNISCFPRPCAKSPPINCTKEGFVRKIKPRLDDPCCTETVCECDIKTCIINKTACDLGFQPVVAISEDGCCPIFSCIPKGVCVSEGVEFKPGAVVPKSSCEDCVCTDEQDAVTGTNRIQCVPVKCQTTCQQGFRYVEKEGQCCSQCQQVACVANFPFGSVTIEVGKSYKAPYDNCTQYTCTESGGQFSLTSTVKVCLPFEESNCVPGTVDVTSDGCCKTCIDLPHKCKRSMKEQYIVHKHCKSAAPVPVPFCEGTCSTYSVYSFENNEMEHKCICCHEKKSHVEKVELVCSEHKTLKFSYVHVDECGCVETKCPMRRT
Protein: Chromosome transmission fidelity protein 18 (Q9USQ1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Replication factor C (RFC) complex has an essential but redundant activity in sister chromatid cohesion establishment. Acts as a PCNA loader, loading PCNA onto primed templates. An RFC-like complex (ctf18-RFC) is formed where ctf18 replaces rfc1 in the RFC complex along with the association of dcc1 and ctf8. This complex is required for efficient establishment of chromosome cohesion during S-phase.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Sister chromatid cohesion protein dcc1
- Replication factor C subunit 5
- Replication factor C subunit 2
- Replication factor C subunit 3
- Replication factor C subunit 4
- Telomere length regulation protein elg1
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit B
- Structural maintenance of chromosomes protein 3
- DNA polymerase alpha catalytic subunit
Sequence:
MDSIPNEDDLEKLLVAEQNVPYGKNYESFEDEENYLLELRNANALENLEHRSIPNDLFHSSQPVGSPTRNGDDIPSTLDLYSSDNAAIDTDISEDETINQRHAPQTDYRYPNTSANPKMGLEESMDIDMPSIDLDISNAAAFPRDSNLLFRNYNSHTKTSEKGSPVNFEKENQDSNVLFSTGRTSVLHIDAEQSQTNNTVTPLKDDALSLFSFENDVNGAVNDNSLDQKLSASKNSQRVSLPFFSKIELDEGSSFSGPKISARTSSGKIIYFPKKKNRHSDGLLLQPKRLADEISQVNEIGKDFNQDLLNSVRIWSENFLIVSKEKSVALKTEKLDSLQITNCTTKPQSQKLWVDTYRPQLFRDLLGDERVHRAAMHWIKAWDPCVFGKSRLQPSKSMRFNPRFTNITSDSDRPDKRIMMLTGLAGAGKTTLAHVIAHQAGYKVLEINASDDRTAHTVHEKVSSAISNHSALSSQPTCVIVDEIDGGDPAFVRALLSLLESDEKATEYSQAGNSKKKKKFKKLCRPIICICNDLYTPALRPLRPYAQIIYFRPPPQASLVGRLRTICRNENIAVDSRSLTLLTDIYNSDIRSCINSLQLLSLNNKRIDSETIKLLQPKSNSFSTSSLIQSLFLQLDNKQIRAIEASQPTYSHLDALLARIDGANDSESVLMNCFHTYLDLPFTDSLLSKPALTSEWLYFFDQLHSQCYKGNYELWRYIPYSIIHFHYLYATPEKCRLPHPPRSDLEALKLYRTRKEILDSFISTLNAYENQMHGERSILLELIRTILITINPTLKQKEDSMPRSALPSKIEHAINILNHYNLRFQQLPVGDGNYVYRLEPPLDELVWDAPTSSYSVRQMLSQELLKKRLADIKKQTLTDNPTSSNSSRKRKDFNSGKAIKRDFFGRIISEPKSEAVTSNNAALNTGDHPVSIKHAINIKFHDGFSNAVRKPISLNEILNF
Protein: Plastid-encoded RNA polymerase subunit alpha (Q387X6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase subunit beta
- Nitroreductase, putative
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase III subunit RPC3
Sequence:
MVKVYNLQRRTETLPTVRRTAPNAEELEYQSHLSRPAGAGDGEPTRRVETITFDMDNVSPPVANMFRRLMLTEVPVFAFDRILIEHNDGVVPDELLAHRIGLVPLAGPVSSMQYITDSASVGFDNLDPERVLLFELDVTAKRDVPTTSVYSGHLKWQPIAKQEELAARSEDDRVFLVHPDIVLTRLGPGQRLKLRAIAIKGIGAVHAKWTPVAACFYEMKQAKAGAEDSDGRASGRGRSRSGRGRVDANEEESNATRPRSASGNHSHEPHRETVNEVIAKRDTSSVRFTVESIGQLYAVDVFRQALILFAERIRDLAVRIRSTEPRMTGAAATAFTE
Protein: Immunoglobulin heavy constant epsilon (Ig epsilon chain C region) (Ig epsilon chain C region ND) (P01854)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: [Isoform 1]: Secreted {ECO:0000269|PubMed:7995941}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:20458139, ECO:0000269|PubMed:7995941, ECO:0000269|PubMed:8976175}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:8976175}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
ASTQSPSVFPLTRCCKNIPSNATSVTLGCLATGYFPEPVMVTWDTGSLNGTTMTLPATTLTLSGHYATISLLTVSGAWAKQMFTCRVAHTPSSTDWVDNKTFSVCSRDFTPPTVKILQSSCDGGGHFPPTIQLLCLVSGYTPGTINITWLEDGQVMDVDLSTASTTQEGELASTQSELTLSQKHWLSDRTYTCQVTYQGHTFEDSTKKCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVNLTWSRASGKPVNHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNPGLAGGSAQSQRAPDRVLCHSGQQQGLPRAAGGSVPHPRCHCGAGRADWPGPPELDVCVEEAEGEAPWTWTGLCIFAALFLLSVSYSAAITLLMVQRFLSATRQGRPQTSLDYTNVLQPHA