wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-directed DNA methylation 4 (Protein DEFECTIVE IN MERISTEM SILENCING 4) (Q8GYP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable regulatory factor for several RNA polymerases. Effector involved in facilitation of Pol V transcription as RNA scaffold and recruitment of silencing complex to target genomic sites.
Interaction partners:
- Protein RDM1
- Protein DEFECTIVE IN MERISTEM SILENCING 3
- Protein RNA-directed DNA methylation 3
- Protein CHROMATIN REMODELING 35
- DNA-directed RNA polymerase IV subunit 1
- DNA-directed RNA polymerases IV and V subunit 4
- DNA-directed RNA polymerase V subunit 1
- RNA-dependent RNA polymerase 2
- Protein INVOLVED IN DE NOVO 2
- SNF2 domain-containing protein CLASSY 1
Sequence:
MDGVGESSTQNEVEEKPVIVRVKRKVGQSLLDAFWLEINERPLKRPTLDFSKLSISDSGERGPSVAEDVKPKKVLVRHLETVTDSETTADIIHSFFESDHNEKSCSKGKFEERKIAFKKDNRKEQRLTKSVQKQQIASENARFEQIWRSRKGNKEGIHEKCHFFDVIRVDTEERRDNAQEFTSLEDQKMLASFLPLLRECIPTAAEEIEADIQSSHTEEYVYDYYAVNEEMDISEDSSKNQFPLVIVEDEEEFCDGSDESDYDSEDSNAEDHPKTDYPEEEEEEEEEDDDDDDDDESEEEKSEASDESDDEETSKRHVRSVLGDDEFDDYAEDVYGYSESDEEFES
Protein: CD44 antigen (CDw44) (Epican) (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44) (P16070)
Organism: Homo sapiens (Human)
Function: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22726066, ECO:0000269|PubMed:23589287}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000250|UniProtKB:P15379}. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli. Localizes to cholesterol-rich membrane-bound lipid raft domains. {ECO:0000250|UniProtKB:P15379, ECO:0000269|PubMed:23589287}.
Interaction partners:
- Radixin
- Receptor tyrosine-protein kinase erbB-2
- HLA class II histocompatibility antigen gamma chain
- Fibronectin
- Osteopontin
- Matrix metalloproteinase-9
- Epidermal growth factor receptor
- L-selectin
- E-selectin
- Versican core protein
Sequence:
MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSSGSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSETPDQFMTADETRNLQNVDMKIGV
Protein: Dual specificity protein phosphatase 9 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 4) (MAP kinase phosphatase 4) (MKP-4) (Q99956)
Organism: Homo sapiens (Human)
Function: Inactivates MAP kinases. Has a specificity for the ERK family.
Subcellular location: Cytoplasm.
Interaction partners:
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 9
- Dual specificity protein phosphatase 7
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
Sequence:
MEGLGRSCLWLRRELSPPRPRLLLLDCRSRELYESARIGGALSVALPALLLRRLRRGSLSVRALLPGPPLQPPPPAPVLLYDQGGGRRRRGEAEAEAEEWEAESVLGTLLQKLREEGYLAYYLQGGFSRFQAECPHLCETSLAGRAGSSMAPVPGPVPVVGLGSLCLGSDCSDAESEADRDSMSCGLDSEGATPPPVGLRASFPVQILPNLYLGSARDSANLESLAKLGIRYILNVTPNLPNFFEKNGDFHYKQIPISDHWSQNLSRFFPEAIEFIDEALSQNCGVLVHCLAGVSRSVTVTVAYLMQKLHLSLNDAYDLVKRKKSNISPNFNFMGQLLDFERSLRLEERHSQEQGSGGQASAASNPPSFFTTPTSDGAFELAPT
Protein: Centrosomal protein 290 (A0A5F9ZHU6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MPPNINWKEIMKVDPDDLPRQEELADNLLISLSKVEVNELKSEKQENVIHLFRITQSLMKMKAQEVELALEEVEKAGEEQAKFENQLKTKVMKLENELEMAQQSAGGRDTRFLRNEICQLEKQLEQKDRELEDMEKELEKEKKVNEQLALRNEEAENENSKLRRENKRLKKKNEQLCQDIIDYQKQIDSQKETLLSRRGEDSDYRSQLSKKNYELIQYLDEIQTLTEANEKIEVQNQEMRKNLEESVQEMEKMTDEYNRMKAIVHQTDNVIDQLKKENDHYQLQVQELTDLLKSKNEEDDPIMVAVNAKVEEWKLILSSKDDEIIEYQQMLHNLREKLKNAQLDADKSNVMALQQGIQERDSQIKMLTEQVEQYTKEMEKNTCIIEDLKNELQRNKGASTLSQQTHMKIQSTLDILKEKTKEAERTAELAEADAREKDKELVEALKRLKDYESGVYGLEDAVVEIKNCKNQIKIRDREIEILTKEINKLELKISDFLDENEALRERVGLEPKTMIDLTEFRNSKHLKQQQYRAENQILLKEIESLEEERLDLKKKIRQMAQERGKRSATSGLTTEDLNLTENISQGDRISERKLDLLSLKNMSEAQSKNEFLSRELIEKERDLERSRTVIAKFQNKLKELVEENKQLEEGMKEILQAIKEMQKDPDVKGGETSLIIPSLERLVNAIESKNAEGIFDASLHLKAQVDQLTGRNEELRQELRESRKEAINYSQQLAKANLKIDHLEKETSLLRQSEGSNVVFKGIDLPDGIAPSSASIINSQNEYLIHLLQELENKEKKLKNLEDSLEDYNRKFAVIRHQQSLLYKEYLSEKETWKTESKTIKEEKRKLEDQVQQDAIKVKEYNNLLNALQMDSDEMKKILAENSRKITVLQVNEKSLIRQYTTLVELERQLRKENEKQKNELLSMEAEVCEKIGCLQRFKEMAIFKIAALQKVVDNSVSLSELELANKQYNELTAKYRDILQKDNMLVQRTSNLEHLECENISLKEQVESINKELEITKEKLHTIEQAWEQETKLGNESSMDKAKKSITNSDIVSISKKITMLEMKELNERQRAEHCQKMYEHLRTSLKQMEERNFELETKFAELTKINLDAQKVEQMLRDELADSVSKAVSDADRQRILELEKNEMELKVEVSKLREISDIARRQVEILNAQQQSRDKEVESLRMQLLDYQAQSDEKSLIAKLHQHNVSLQLSEATALGKLESITSKLQKMEAYNLRLEQKLDEKEQALYYARLEGRNRAKHLRQTIQSLRRQFSGALPLAQQEKFSKTMIQLQNDKLKIMQEMKNSQQEHRNMENKTLEMELKLKGLEELISTLKDTKGAQKVINWHMKIEELRLQELKLNRELVKDKEEIKYLNNIISEYERTISSLEEEIVQQNKFHEERQMAWDQREVDLERQLDIFDRQQNEILNAAQKFEEATGSIPDPSLPLPNQLEIALRKIKENIRIILETRATCKSLEEKLKEKESALRLAEQNILSRDKVINELRLRLPATAEREKLIAELGRKEMEPKSHHTLKIAHQTIANMQARLNQKEEVLKKYQRLLEKAREEQREIVKKHEEDLHILHHRLELQADSSLNKFKQTAWDLMKQSPTPVPTNKHFIRLAEMEQTVAEQDDSLSSLLVKLKKVSQDLERQREITELKVKEFENIKLQLQENHEDEVKKVKAEVEDLKYLLDQSQKESQCLKSELQAQKEANSRAPTTTMRNLVERLKSQLALKEKQQKALSRALLELRAEMTAAAEERIISATSQKEAHLNVQQIVDRHTRELKTQVEDLNENLLKLKEALKTSKNRENSLTDNLNDLNNELQKKQKAYNKILREKEEIDQENDELKRQIKRLTSGLQGKPLTDNKQSLIEELQRKVKKLENQLEGKVEEVDLKPMKEKNAKEELIRWEEGKKWQAKIEGIRNKLKEKEGEVFTLTKQLNTLKDLFAKADKEKLTLQRKLKTTGMTVDQVLGIRALESEKELEELKKRNLDLENDILYMRAHQALPRDSVVEDLHLQNRYLQEKLHALEKQFSKDTYSKPSISGIESDDHCQREQELQKENLKLSSENIELKFQLEQANKDLPRLKNQVRDLKEMCEFLKKEKAEVQRKLGHVRGSGRSGKTIPELEKTIGLMKKVVEKVQRENEQLKKASGILTSEKMANIEQENEKLKETDAAEKLRIAKNNLEILNEKMTVQLEETGKRLQFAESRGPQLEGADSKSWKSIVVTRMYETKLKELETDIAKKNQSITDLKQLVKEATEREQKVNKYNEDLEQQIKILKHVPEGAETEQGLKRELQVLRLANHQLDKEKAELIHQIEANKDQSGAESTIPDADQLKEKIKDLETQLKMSDLEKQHLKEEIKKLKKELENFDPSFFEEIEDLKYNYKEEVKKNILLEEKVKKLSEQLGVELTSPVAASEEFEDEEESPVNFPIY
Protein: Synaptosomal-associated protein 23 (SNAP-23) (Vesicle-membrane fusion protein SNAP-23) (O70377)
Organism: Rattus norvegicus (Rat)
Function: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Mainly localized to the plasma membrane. {ECO:0000250}.
Interaction partners:
- Syntaxin-4
- Vesicle-associated membrane protein 3
- Vesicle-associated membrane protein 2
- Vesicle-associated membrane protein 8
- Syntaxin-3
- Alpha-soluble NSF attachment protein
- Syntaxin-1A
- Vesicle-associated membrane protein 7
- Syntaxin-7
- Syntaxin-8
Sequence:
MDDLSPEEIQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCVCPCNRTKNFESGKNYKATWGDGGDSSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS
Protein: SH3 domain-binding protein 1 (D3ZFJ3)
Organism: Rattus norvegicus (Rat)
Function: GTPase activating protein/GAP which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form. By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for proper cell migration. Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions. Through its GAP activity toward RAC1 and/or CDC42 plays a specific role in phagocytosis of large particles. Specifically recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large particles engagement, inactivates RAC1 and/or CDC42 allowing the reorganization of the underlying actin cytoskeleton required for engulfment. It also plays a role in angiogenesis and the process of repulsive guidance as part of a semaphorin-plexin signaling pathway. Following the binding of PLXND1 to extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the intracellular reorganization of the actin cytoskeleton and the collapse of cells (By similarity).
Subcellular location: Cell projection {ECO:0000269|PubMed:21658605}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9Y3L3}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9Y3L3}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q9Y3L3}. Nucleus {ECO:0000250|UniProtKB:Q9Y3L3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3L3}. Note=Localizes at the leading edge of migrating cells (PubMed:21658605). Accumulation at forming phagocytic cups is PI3 kinase/bPI3K-dependent and is specific for sites of large particles engagement and their phosphatidylinositol 3,4,5-triphosphate membrane content (By similarity). {ECO:0000250|UniProtKB:Q9Y3L3, ECO:0000269|PubMed:21658605}.
Interaction partners:
Sequence:
MMKRQLHRMRQLAHTGSSGRTPETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKSLQKLVSDWNTLKSRLSQAAKNSGSSQSLGGGSSSHTHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYANYFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPLTTAAPFSRVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVSSIQVVGVVEVLIQNADTLFPGDINFSVSGIFSGLAPQEKPNSQQVSEELAPVAVPATAATPTPTPAPTPAPASMTVKERTESELPKPASPKVSRSPTDTTALAEDMTRKTKRPAPARPTMPPPQPSSSRSSPPALSLPAGSVSPGTPQALPRRLVGTSLRAPTVPPPLPPAPPQPARRQSRRLPVSPCPASPVISNMPAQVDQGAATEDRGGPEAVGGHPPTPVLPPQPRPRGLISETD
Protein: Dehydration-responsive element-binding protein 1A (Protein DREB1A) (C-repeat/dehydration-responsive element-binding factor 3) (C-repeat-binding factor 3) (CRT/DRE-binding factor 3) (Cold resistance-related AP2 transcription factor) (Q9M0L0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates cold-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- ABSCISIC ACID-INSENSITIVE 5-like protein 5
- ABSCISIC ACID-INSENSITIVE 5-like protein 7
- Low-temperature-induced 78 kDa protein
- Protein COLD-REGULATED 15A, chloroplastic
- Transcription factor ICE1
- ABSCISIC ACID-INSENSITIVE 5-like protein 6
- Dehydrin COR47
- Floral homeotic protein APETALA 2
- Protein COLD-REGULATED 15B, chloroplastic
- Low-temperature-induced 65 kDa protein
Sequence:
MNSFSAFSEMFGSDYESSVSSGGDYIPTLASSCPKKPAGRKKFRETRHPIYRGVRRRNSGKWVCEVREPNKKTRIWLGTFQTAEMAARAHDVAALALRGRSACLNFADSAWRLRIPESTCAKDIQKAAAEAALAFQDEMCDATTDHGFDMEETLVEAIYTAEQSENAFYMHDEAMFEMPSLLANMAEGMLLPLPSVQWNHNHEVDGDDDDVSLWSY
Protein: Double-Strand Break factor (Q19220)
Organism: Caenorhabditis elegans
Interaction partners:
- Double-Strand Break factor
- Meiotic recombination protein spo-11
- DNA repair protein RAD51 homolog
- High Incidence of Males
- Cyclin N-terminal domain-containing protein
- Sun domain-containing protein 1
- X chromosome NonDisjunction factor
- Serine/threonine-protein kinase chk-2
- HORMA domain-containing protein
- HORMA domain-containing protein
Sequence:
MFPELQTLQWPIIKYKQLRGSGNRQEGKDIRVVMEVNSRKLTVIHGVEPIETVYCNMEVSRYPSLKMKNTNLFVIVNNQAQGFRLTLRGEDRENFLSTVRKFAYISETPVKDHLNRSSTNTDVWYNSVEKRKGGSSSQPTSFSQPCDIDIGGSVKKSAARNLSHTYSTNIGESSRMPALTANEFFSQPVYNPYNRPASSASTVSSSIGSAYSVLHDDSPFSGFSPNSNHSLQFPCPSPSHSSSFSGFSQSSSHSSQLSSSPANAPSFPDFHSPPSANDIQIDQLNPVTVAPQIKQTADKCVQTDKQYVDERFDDPAFLRRYIKRVMSDSKMARLVGMMRSEIRKLPNDEFDAFYKKVKDHQRTAPSSSSKIGPPAIVQQTSDMEF
Protein: Ent-kaurenoic acid oxidase 1 (AtKAO1) (EC 1.14.14.107) (Cytochrome P450 88A3) (O23051)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes three successive oxidations of ent-kaurenoic acid giving gibberellin 12 (GA12), a key step in gibberellins (GAs) biosynthesis. GAs, which are involved many processes, including stem elongation, play a central role in plant development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11722763}; Single-pass membrane protein {ECO:0000269|PubMed:11722763}.
Interaction partners:
- Gibberellin 20 oxidase 1
- Gibberellin 20 oxidase 2
- Gibberellin 20 oxidase 3
- Gibberellin 20 oxidase 4
- Ent-kaurene oxidase, chloroplastic
- Ent-kaurenoic acid oxidase 2
- Ent-copalyl diphosphate synthase, chloroplastic
- Gibberellin 3-beta-dioxygenase 1
- Ent-kaur-16-ene synthase, chloroplastic
- Gibberellin 2-beta-dioxygenase 1
Sequence:
MAETTSWIPVWFPLMVLGCFGLNWLVRKVNVWLYESSLGENRHYLPPGDLGWPFIGNMLSFLRAFKTSDPDSFTRTLIKRYGPKGIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVMYLPHTRPTDNCLARISYQ
Protein: Uncharacterized protein (G1NS52)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
Sequence:
MADEEIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEAIFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: HIVEP zinc finger 1 (Immunodeficiency virus type I enhancer binding protein 1, isoform CRA_a) (C9JLG1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLSWVPWRRVTGLHGVALPHGLDKIEEAQKELNGAEVSKKEILQAGVKGTSESLKGNLTKHMKSKAHSKKCVDLGVSVGLIDEQDTEESDEKQRFSYERSGYDLEESDGPDEDDNENEDDDEDSQAESVLSATPSVTASPQHLPSRSSLQDPVSTDEDVRITDCFSGVHTDPMDVLPRALLTRMTVLSTAQSDYNRKTLSPGKARQRAARDENDTIPSVDTSRSPCHQMSVDYPESEEILRSSMAGKAVAITQSPSSVRLPPAAAEHSPQTAAGMPSVASPHPDPQEQKQQITLQPTPGLPSPHTHLFSHLPLHSQQQSRTPYNMVPVGGIHVVPAGLTYSTFVPLQAGPVQLTIPAVSVVHRTLGTHRNTVTEVSGTTNPAGVAELSSVVPCIPIGQIRVPGLQNLSTPGLQSLPSLSMETVNIVGLANTNMAPQVHPPGLALNAVGLQVLTANPSSQSSPAPQAHIPGLQILNIALPTLIPSVSQVAVDAQGAPEMPASQSKACETQPKQTSVASANQVSRTESPQGLPTVQRENAKKVLNPPAPAGDHARLDGLSKMDTEKAASANHVKPKPELTSIQGQPASTSQPLLKAHSEVFTKPSGQQTLSPDRQVPRPTALPRRQPTVHFSDVSSDDDEDRLVIAT
Protein: Attachment protein G3P (Gene 3 protein) (G3P) (Minor coat protein) (P03661)
Organism: Enterobacteria phage fd (Bacteriophage fd)
Function: Plays essential roles both in the penetration of the viral genome into the bacterial host via pilus retraction and in the extrusion process. During the initial step of infection, G3P mediates adsorption of the phage to its primary receptor, the tip of host F-pilus. Subsequent interaction with the host entry receptor tolA induces penetration of the viral DNA into the host cytoplasm. In the extrusion process, G3P mediates the release of the membrane-anchored virion from the cell via its C-terminal domain.
Subcellular location: Virion {ECO:0000305}. Host membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Prior to assembly, G3P is found associated with the bacterial host inner membrane. There are about five copies of this protein per mature phage that are located on the head side of the filamentous virion.
Interaction partners:
Sequence:
MKKLLFAIPLVVPFYSHSAETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENEGGGSEGGGSEGGGSEGGGTKPPEYGDTPIPGYTYINPLDGTYPPGTEQNPANPNPSLEESQPLNTFMFQNNRFRNRQGALTVYTGTVTQGTDPVKTYYQYTPVSSKAMYDAYWNGKFRDCAFHSGFNEDPFVCEYQGQSSDLPQPPVNAGGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSGDFDYEKMANANKGAMTENADENALQSDAKGKLDSVATDYGAAIDGFIGDVSGLANGNGATGDFAGSNSQMAQVGDGDNSPLMNNFRQYLPSLPQSVECRPYVFGAGKPYEFSIDCDKINLFRGVFAFLLYVATFMYVFSTFANILRNKES
Protein: Ankyrin repeat and SAM domain-containing protein 6 (Ankyrin repeat domain-containing protein 14) (SamCystin) (Sterile alpha motif domain-containing protein 6) (SAM domain-containing protein 6) (Q5XJ13)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for renal function.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q6GQX6}.
Interaction partners:
Sequence:
MGASVLAMAARGGHTHTVKLLLENGAFVDDCEHACVSEGNTNTHCSAGSVQEARALLEVRALLAAAQHGQGAAVALLLDWGSDARVCHTGTGWSALMLAAAGGSLSVCQQLVERGADPDHTNVLGNTALEVALQLRRRDVQKYLDNITSVRPRPDDEKKRPDVFHALKLGNAQLVKEIVEQDAAQVDVCNADGASPLMMAAVSGQLEVVQLLVEKRADVDRQDSVHGWTALMQATYHGNKEVVKFLLSQGADVQLRAKNGYTAFDLVMLLNDPDTELVRLLASVCMLVDKDKSKQRGKSALRRRASAGTPSPPEDKTGLKSWWNRMSNRFRRLKLTHTLRHGLSTNRLAPFPDAADVPLDATMRAEEGGAEVASPTAPPAGAQSTACSRTEDCGLNGTGSGKEDFLITTMLRNGAPLARLPSEQLKAVIPPFLPPSCFEPWSSERCGSLRDARSTHTHSQRPGRSSAGSDTASISRVVNRSIKFPSITKGPSPSNSGSYNSAHSSGGSNGVGGVNRHSDTHNRSGGSAADSVLSQIAAQRKRAAGLMDSRSPAVETPSPAHTPLPDSRPKLELQKRPQSGNSSRSKSTSPTLTPSPSPTPAHTPAPAHTPAHRPTGASADSQGSASTQQRSRSSGGSSSGTITDEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIRTDGPRQQILAAISELNAGKGRERQILQETIINFQSSFGSSASTPRAATHTH
Protein: Putative choline-phosphate cytidylyltransferase (EC 2.7.7.15) (CTP:phosphocholine cytidylyltransferase) (CCT) (CT) (Phosphorylcholine transferase) (P49583)
Organism: Caenorhabditis elegans
Interaction partners:
- Phosphoethanolamine N-methyltransferase 2
- Choline kinase B1
- diacylglycerol cholinephosphotransferase
- Choline kinase B2
- Choline kinase A2
- Putative choline kinase B3
- Methyltransf_11 domain-containing protein.
- diacylglycerol cholinephosphotransferase
- Probable S-adenosylmethionine synthase 1
- choline-phosphate cytidylyltransferase
Sequence:
MFIHKQEKMPQRKRTMDSPQEEDVEVKKKATEVEYVVRSLASDEPAPFSDEALAITTREAVDYSKKITLAMAEANEAGRPVRIYADGIYDLFHHGHANQLRQVKKMFPNVYLIVGVCGDRDTHKYKGRTVTSEEERYDGVRHCRYVDEVYREAPWFCTVEFLKNLKVDFIAHDAIPYVAPGEEDLYEKFRREGMFLETERTEGVSTSDVVCRIIRDYDKYVRRNLQRGYSPKELNVGFLAASKYQIQNKVDSLKSKGIELLSTWKSKSDDIIRDFIDTFHKDGGLNAFGGRLKGIMSMSRSPSPSPHEGSPTGIEHHLETQDEEEEEEALEEEKVVEQKIVEKKEVVKKRSSRNKAKTPLEY
Protein: EF-hand domain-containing protein (Q57VP9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA editing associated helicase 2
Sequence:
MSTLTGSVGPNSAHGSTVGVSLDFEVNAAASHGDDEAETKSCFAEFSSPAADTKLAEEGESISRAPASPSGSHAVRNRSVSVPFVSFTDADEQPKDGLWSSKSLVPPLKRRPKQSRITRKSFRSLGAYRNPSTLSVLDLATTDLDKLKLSFVAHAAILNHGDLNDMQKLVNHVEREMRYGEQHLDRSHRGRQGSKAPSYQASVRSEDDGANADGGTDRAWQSLDDQSSSDVSVEESVKSMMDVPSQTKAMLCTWIYDRYVQQRIFELRAKRKARPNDTFTAVVSRQFPDAGTKELMVNLRNAPKPRNMRDLDLHDGIGSCLNEAGEKVGHTHLVTDADNLVLPLPVFVYVLSRALFRLHYLDRFPAEAFSVKSQQTNQGASCAGGSTPRTEVSLSVVMGDSGSNSLHNVSPLVSPRYEALHSLLQEAVSLLEECRRVAMQGFDIFDTEQKGVISWSVFTDALTECMEEKLRGLCDQDCGEDSERSGVAVFDDCVVEPFPSMLRRLGYVRAVTKVRHNPAAVLVEGTNDFAVCDSSYHGLIQRKLLVRSSEMLLMHCHGATDAWDPERWDIHAGTGENNKEQEKFTKGYVLYEDGRLQDGGGKQSLLFTLQRKQKKEQGLSEEEEDERKKEEKRTDQNNYRNKPTIECCMEVKDVGPNLPKTIITLTNDLIIRFYNMDQHIWVVPESLTMNVKETICAMDWCAAAADENLPLKGFLFVGTRSGKVIKLDLQAILRRMISAQTSTSDIMTTGIVAASTVRDRFERRVVQEQKIHSEVVTSVCLTASDMLLTSSLDGAIVLSRASTMTLVRSFRLETGGGVRLAYITPTGNAIVTLSSSNRVSLWGTTHQSSRVDFYDPISPHYFQIASFIVDESLEQLTTVDTSGHIKVWSLRTALVKFSFYAVSEECMNSLGFLSEENMGPNNGFRLFDVDDAGNKRLRVAGDTGSRALAAILQTSFAKLEDDQKRRSLHPIRTVAYDAYTRRLFVSGAKNNLVCVFISGSVAMKTHSSPPLYVGMCERNRWLVSVSPTDCRVWDCQSSKLVVGFKVNNPEFLMARLALTFASRSNLPTDAQLANAAADLERYKLDECKQPLPTINDVIRVATERADLARRENSRAMVAQKHEASTARDAGGGSRPSPESNHQTARGLPTPRFAAAAAAGADNSGEDDVSSKQMATHRVICAHVDAQERFVFYALGSGDVRMHRIKSGQLVKTLLTMSPSTELIYAAVLQCRHMYTYTRNPGENRHNQDCDDVKSPDGYVGAHVGVHDVAFVLQRLLREGHKLPLERSKTSSVHREVVGMMTPRNSHELCVVYVDGVIRFFPLLGSSVHAHRIIIPEFLVSKALSYLRMENTLMRKEAANRSGRTTRCTESEAAEAYRNVMVEADAVSFITVSHALNLVCLVQVNGRVSLMGMGSAVGMALQVFYVASEVSTISFLGGYPCLVVGEVQGTVGFYLLKGASFLDLFDNFYKALLLYRRQQQASLHEPSVELFNVDKLTESSVESTNQHGLNSTPCVWWFRVPGAPTTLHFDPHCCSLYVGTQQGFVTSYLVRNLIVAANLHPASLSGRSPSLMSRGRMSVQGQSGSAEVELCNVLLVFFNLTPDRVMRTINRQRNDLAFLNRRRRSLVSGSAATVQPTATDDSTDEGNAPSVPKPVSSSRSTSLGTLRLPKGSSNPEVDGQSERPQTAVPLQSWRPSLLWIYDSCRSLFHPHPTSTSTFRGPSEPTFSLLDLATVTLSDLLLGAAILHYVLQLMQTQRSGQPSSTDYGAMDGDQTTKCAAMINSQDLRHIRQCILEELHHRKSMFEEINSSHPTSTNRVSNCHIEEFVETIAASGELEEGPAPITGDWVELLFRRHAVNTVSSSPLTLLSMEAIIERARRERRERVRILMKYVDERRLLAREGTDHREGGASSRWQHKSISVNWNAFLEGAPPDCITEALRRCHEGASRDEEVFFSEDNNAVQCITTRRNGVLYVGSADGSVSVWTPYACARLQEFSPCNPLDAGIRRIGEFVKTQFTKQWKSAENLRQRKAYASGTNKQKLHEAMMRNITLKYRVALLKQGAKRGGGSGVYNSPGGGNSSGADGRKQASPRRAMSHVGFQSLGSMPTTLHNEMQNLIKKPKELLMAALPIDESEMDSKGIIMEDLYFLPMQMSVLSELEDLDGKAYAAAVDLSVARLLRDVCCSDGQGLDPFPSARYSGVLDRVKLNADESQTFAGAGPPLSATDVKRGGEAESAVDTSISFFISSHEKHMTSFYVEAKRKLDDGEYTSQHGNSLSRTGHSVTFISLHSKLQRPPFSFSRTQDAKESLPSTPDGETAVTASLPQFAQAGVVGRPGVIVVALSERREGQLNPQFEFDLPQLAANSQWIALEEALKLYINSSDGALTMDSFQCVSISPSPYLGRGQRVGDVSRGSVQVPPIAGILPSILTKETPLRCGDMGKGVTTLADPLLVMSPSNVEEDLGLLQSEGEPQHLDRTRLRRGSSQYLNANANENTATGKRCSFFFTETHDLRSPTKTPSAISTTAIGGKWSETHLKPFQEVESRRPRPHLDDVAESGRGSMHPTMNIRWTLESKQQNQRAKLSRTGRTVLTPPRSTRDSRPRNYQQPLRANGTTTLGNEWGVSPQGFQKEGNSNAVDGRAGVTSPNPRIPQPCRP
Protein: Regulator of G-protein signaling 13 (RGS13) (O14921)
Organism: Homo sapiens (Human)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to both G(i)-alpha and G(q)-alpha (By similarity).
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein G
- Rho guanine nucleotide exchange factor 1
- Regulator of G-protein signaling protein-like
- Rho guanine nucleotide exchange factor 11
- Beta-adrenergic receptor kinase 1
Sequence:
MSRRNCWICKMCRDESKRPPSNLTLEEVLQWAQSFENLMATKYGPVVYAAYLKMEHSDENIQFWMACETYKKIASRWSRISRAKKLYKIYIQPQSPREINIDSSTRETIIRNIQEPTETCFEEAQKIVYMHMERDSYPRFLKSEMYQKLLKTMQSNNSF