wanglab/gogpt-training-data huggingface dataset:
Protein: Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 6 (AtCand6) (Q9LZ39)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: G-protein coupled receptor. Plays a role in plants and microbes interactions (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 8
- AT3g59090/F17J16_140
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 2
- Metal ion-binding protein
- Heptahelical transmembrane protein 5
- Heptahelical transmembrane protein 2
- Heptahelical transmembrane protein 1
- LanC-like protein GCR2
- G-protein coupled receptor 1
Sequence:
MTILPFLAAVFVLQLLSTLTVAEIKSFTISNDSRPVILLEKFGIIEIGHVTVSVSSVSVLSPILDSSKLGFFVLSEESLPHVLLELQQNFSFCVLDSHYILHFFTFVDLSPPPRSQFSKSYPITSPNDYSLFFANCVPETRVSMKVHTEIYHDLYPNGSRDYLLAGSAQLPGLYLVFFLCYLSFLCFWLCFCWNHKQIVKRIHLLMTALLLVKSLTLICAAVYKHYVKVTGTAHGWNIVFYIFQFISVVLLFMVIVLIGNGWSFLKPKLHVKEKKLLVIVVPLQVLANIASIVIGETGPYTQDWVSWNQIFFLADITCCCAIVFAMVWSMCCLRETSKTDGKAVKNLAKLPVLRKFYVLVIGYLFFTRIVVVVMKMKADFTYQWVSNAAEEIATLSFYCLMFYMFRPIEKNEYCDVDDEEEIVELSLK
Protein: Transmembrane gamma-carboxyglutamic acid protein 1 (Proline-rich gamma-carboxyglutamic acid protein 1) (Proline-rich Gla protein 1) (O14668)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Vitamin K-dependent gamma-carboxylase
Sequence:
MGRVFLTGEKANSILKRYPRANGFFEEIRQGNIERECKEEFCTFEEAREAFENNEKTKEFWSTYTKAQQGESNRGSDWFQFYLTFPLIFGLFIILLVIFLIWRCFLRNKTRRQTVTEGHIPFPQHLNIITPPPPPDEVFDSSGLSPGFLGYVVGRSDSVSTRLSNCDPPPTYEEATGQVNLQRSETEPHLDPPPEYEDIVNSNSASAIPMVPVVTTIK
Protein: VPS9 domain-containing protein (Q582V6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRCNSESETEFDSLKSENPLLHSPSLKSWNIMKNTPVVPPFSSAMTMAMKEHCGASTATSAANERQYKELNVDFNDKYFGEVTRSGSIEVPHGNGRLFSGEGKHFYEGGFVNRCRDGYGVLNTERYALWCKWKMNRPDLTSQSRVDYRDGTRYNGFLSAHQNNSAAANIPSSLRCRLSKFSIWVHSLTLVRERWGEIVHSGGDRYFGQWDNDMPSGFGCYVTKYGDRYIGLFQRGRFHDTGTLFVHACRWGNRASKIPDGVGFLYQQEQVENQHVEAAEAAKQRIEDRFKNTFTESCGCSGADYEISGHKRQGPPRGWDGVIFDGVWEMGRFLGEGHVTLPCGSRITAEWKNLFSPTQGRVFMASSNDNKASGRQDMDTRGWFQCFHWESLLSGLTDESKEQKYAACASFRERLGLATTEEEEQVVLADFCSNEDAIRNALKVFQRCFYFLHGSCGSSSEIGSGWGSNPLGWCYVRNSYGGCIHNIKGRRITACDVDLALTDIISFVRSTERWVVEMLGDSSLSSPSSHLFVMRKLLDLTLRSVYNVLFNLYVHAYDVEDIALTQALERVREHTTLDDLGVSFARQQSSEELFDPYADAVNRIERLARGVWTYGSKLKILAQWSMEIDLSTRLARVTLDDGPLALLPKRNAQPASGSADDLIPIHQFVLMKAKVDHLYVHTKLLVDLSSEDVFMEFTSQENFFVITFQACTMILSKFHPLLRDESHVLAPPSLFEERLRSGVHSIRRLAETFIAQLLKSHGVFEGEESREFSAEEFGAVALGYIKAWLAEAVDMAATHGGTAVASGSDQILPVAELLQMEETRQLALLSEPNFPRVLALFCWLAVANVLSVLHIHLGVMAANGDDLLNVDTDPAKLLDDYVAWRNVCGGDVSSLVLLLGKGAPRPLFLRRAAAFIASIL
Protein: Fur protein (Q8Y5U9)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Interaction partners:
- Lmo1734 protein
- HTH-type transcriptional regulator MntR
- DNA-directed RNA polymerase subunit alpha
Sequence:
MEGRIGRIKAQLHDASYKLTPQREATVRVLLENEKDHLSAEEVFLRVKDIAPDTGLATVYRTLELLTELRVVDKINFGDGVSRYDLRQEGAKHFHHHLVCLECGSVEEIQEDLLEDVEKIVESKWNFLVKDHRLTFQGICANCRQKSKKE
Protein: 2'-5' oligoadenylate synthase (EC 2.7.7.84) (H0YIB8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLMRQRLREVRSLAQGHQLTSGGNGIQAQWTLKPVLMSLC
Protein: Uncharacterized protein (Q54JQ7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- AP-3 complex subunit mu
Sequence:
MSNDLFLSLFRNELINNKIFKEIKEINKQNKFTTYNFYDFPITSIIKTKNEIMLNQRLDLFIKYMDSNDIENDKSFNYYIDFNGDNYIQLLNWTNLSINTFRKYYQLFKNEILSIKFNSFFFEKNRNLIFKNSNIEILSFLKQQFIENKNYELNPTDENYAFGKYDTFIVYCEIFLLDRKTPCTSIEFQTFLKLFNGLKISKIQFTMWLEKIENKIPNKSLNLDYFFSSSLFFNSNKSIINIEEIQLLPPSLSSPSSPPPLDSIELVIDFFINSINRINKEIISLPIINKQVLEEIKNKPTLFFNLINKILESNDLILMKLFLNLFNINETSKVESNRPNLIIEIYGIKILDSTFIKLFSQVNCFLLFSVINMFELFLMVVKTKSNKFLNNLNNGAGGGGENLVSFKINCPKIARFLIENFKNNSIKNNNITKSCPLQFTDSTLAIKENEIFFIESKSILLLDSFKETLSNEILIKFFRNRWIVKPNLMTIDFFGGDLEMVKTYLENCEKRIIFSELIINSFKKRFYNVTDYLLTQALVPTLENPVNRFTILKFLKSQGNDHNDDDKVIEQSSNLIKKILNSFRIDDFISEPKINDNFDFPETKYQFIYDLVKALPNNPTQRNVFLTNLVGGINDETGSSSNFQYYIELIMNEFNSLIYNNLIDYKSFDKYKYLYGYVKSRFQILNLQFTGIFKLDLQQLIDTGNLDNIKLFSNYDILIILKISLKEHFFSIIGSIIKILEKRIFSFGKNNKFQLKKRIIYDCFKLKSYSIPSNKSIFISEKNNNIKSLLFLIEIGFLKSSCYTTSIIYNRNRNNNDSNNGKLSIFEKQSKRVIGDTFSLDLYYIIYKSIHTLNLKLLEIIILKNQSQYLNIHSKLFTDQNDNYYLKNVDKIINNELIRFDKKTIELMKPLLKILKNKIN
Protein: PGL/p-HBAD biosynthesis glycosyltransferase Rv2958c (EC 2.4.1.-) (P9WFR1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in glycosylation steps downstream of mono-O-methyl-glycosyl-p-hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl-rhamnosyl-phenolphthiocerol dimycocerosate (mycoside B) during the p-hydroxybenzoic acid derivatives (p-HBAD) and glycosylated phenolphthiocerol dimycocerosates (PGL) biosynthesis.
Interaction partners:
- Rhamnosyl O-methyltransferase
- PGL/p-HBAD biosynthesis glycosyltransferase Rv2957
- Chorismate pyruvate-lyase
- Conserved protein
- GDP-L-fucose synthase
- Uncharacterized MFS-type transporter Rv2994
- Conserved protein
Sequence:
MEETSVAGDPGPDAGTSTAPNAAPEPVARRQRILFVGEAATLAHVVRPFVLARSLDPSRYEVHFACDPRFNKLLGPLPFPHHPIHTVPSEEVLLKIAQGRLFYNTRTLRKYIAADRKILNEIAPDVVVGDNRLSLSVSARLAGIPYIAIANAYWSPQARRRFPLPDVPWTRFFGVRPVSILYRLYRPLIFALYCLPLNWLRRKHGLSSLGWDLCRIFTDGDYTLYADVPELVPTYNLPANHRYLGPVLWSPDVKPPTWWHSLPTDRPIIYATLGSSGGKNLLQVVLNALADLPVTVIAATAGRNHLKNVPANAFVADYLPGEAAAARSAVVLCNGGSPTTQQALAAGVPVIGLPSNMDQHLNMEALERAGAGVLLRTERLNTEGVAAAVKQVLSGAEFRQAARRLAEAFGPDFAGFPQHIESALRLVC
Protein: Osteopontin-D (F2YQ21)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN
Protein: Homeobox protein aristaless (Q06453)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the morphogenesis of proximal and distal pattern elements in a subset of appendages. Also has a role in early imaginal disk development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}.
Interaction partners:
- C15
Sequence:
MGISEEIKLEELPQEAKLAHPDAVVLVDRAPGSSAASAGAALTVSMSVSGGAPSGASGASGGTNSPVSDGNSDCEADEYAPKRKQRRYRTTFTSFQLEELEKAFSRTHYPDVFTREELAMKIGLTEARIQVWFQNRRAKWRKQEKVGPQSHPYNPYLPGGAATMQTVVGAALPPNPFTHLGFQLRKPFDAQHAANLAAFRYPHLSAAPMIPSGYFNQFQRAPPHMLPHGMAGMYSPSSSFQSLLANMTAVPRGTPLGKPPALLVGSPDLHSPNHMLASPPTSPASGHASQHQQHPTAHPPPPQAPPQMPVGVQPAQLSPQHLVGIALTQQASSLSPTQTSPVALTLSHSPQRQLPPPSHQAPPPPPRAATPPEDRRTSSIAALRLKAREHELKLELLRQNGHGNDVVS
Protein: ATP synthase F(1) complex subunit alpha, mitochondrial (ATP synthase F1 subunit alpha) (P15999)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17575325}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side {ECO:0000250|UniProtKB:P19483}. Cell membrane {ECO:0000250|UniProtKB:P25705}; Peripheral membrane protein {ECO:0000250|UniProtKB:P25705}; Extracellular side {ECO:0000250|UniProtKB:P25705}. Note=Colocalizes with HRG on the cell surface of T-cells. {ECO:0000250|UniProtKB:P25705}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MLSVRIAAAVARALPRRAGLVSKNALGSSFVGTRNLHASNTRLQKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP
Protein: Probable NADH-ubiquinone oxidoreductase C3A11.07, mitochondrial (EC 1.6.5.9) (O14121)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the oxidation of NADH.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 2
Sequence:
MLFSRSILRGMPKAGIPKSPLALSASRNLRLANSVRFASDAASSPKSTTSKWKILKRTTLGLFATAVVLYGANVYRFRHPDPHQPLPDPSKKTLVVLGAGWGATSILRTIDTSLFNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKSCYVKFYEAECTDVDADKKVIHIKKTTTDGVDLEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAQFKDLPAETRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKSWYPELADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTAENIHVEVKNPDGSKQEEVIPYGLLVWAGGNRARPLTKKLMEGSEEQNNRRGLVVDEYLKLKGYKDIFALGDCTHTAYAPTAQVASQQGAYLGQLFNKLGSLNFEKPSEDRHIALGDEMDSSTLISLANEKHASTKVFLPFKYSHQGSLAYVGHEKAIADIEVPWFGKQLHASGALAFYFWRSVYLSELYSLRNRTNVTLDWIRVKLFGRDISSL
Protein: Trans-3-hydroxy-L-proline dehydratase (T3LHyp dehydratase) (t3HypD) (EC 4.2.1.77) (Trans-L-3-hydroxyproline dehydratase) (Q8G2I3)
Organism: Brucella suis biovar 1 (strain 1330)
Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Displays neither proline racemase activity nor 4-hydroxyproline 2-epimerase activity.
Interaction partners:
Sequence:
MRSTKVIHIVGCHAEGEVGDVIVGGVAPPPGETVWEQSRFIANDETLRNFVLNEPRGGVFRHVNLLVPPKDPRAQMGFIIMEPADTPPMSGSNSICVSTVLLDSGIIAMQEPVTHMVLEAPGGIIEVEAECRNGKAERISVRNVPSFADRLDAPLDVTGLGTIMVDTAYGGDSFVIVDAAQIGMKIEPGQARELAEIGVKITKAANEQLGFRHPERDWRHISFCQITEPVTREGDVLTGVNTVAIRPAKLDRSPTGTGCSARMAVLHAKGQMKAGERFIGKSVLGTEFHCRLDKVLELGGKPAISPIISGRAWVTGTSQLMLDPSDPFPHGYRLSDTWPRDE
Protein: Proteasome regulatory non-ATP-ase subunit 12 (Q8WRT9)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MMTTTDVGGVVRRINVDYKKLKAAYDQNNDSLCLNLVNGLKKQLILLPTFLNPAAASATWLEEVTLTREVLEYAVLVSARLEDLASFELYFNQLSVYYTDIDPTKLKESPLYSLILGLNLVRLLVDDRIAQFHTELEKVPNHIYAPNAYVRFAVLLERYLMEGSYSKLLNSRDQAPSKEYIPIVGMLEKTVRQGVAECIPHSYAKLSFERAQKILMVDSTDAVREIGKQYEWELGKDGASFVFTRREDIAKREVPFQEMLGHHLNFAADLQRIV
Protein: Microfibrillar-associated protein 1 (Spliceosome B complex protein MFAP1) (Q9W062)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000305|PubMed:18765666}.
Interaction partners:
- Pre-mRNA-splicing factor 38
- RE11167p
- LD44732p
- Pre-mRNA-processing-splicing factor 8
- Splicing factor 3B subunit 1
- U4/U6 small nuclear ribonucleoprotein Prp31
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Splicing factor 3A subunit 1
- Pre-mRNA-processing factor 6
- SD09427p
Sequence:
MSAATAAAAASGIQSTAGAIPMRNEKGELSMQKVKVQRYISGKRPDYARADSSSEESDDDDFIDTRKRLERHKAERHKLELSRQGGSAEGEERAAGEGQEEDDAEVDDPRLRRLRQRPVDMEDMERERRERHRHIHEPEIMESDSEDEEEDEGAQGAIQRGTNKITLASESDTDAELSDTELENRRTKLRSRMLQQQREEEVLQKEDEKQSESSESESSEYEEETESEEDNEPRLKPLFVRKRDRATIQEKEREAQKQKQLEAEAKRAAKERRRATLRMVEESVKKDLEKTKPETNEACIEDVCTDDENDEVEYEAWKLRELKRMKRDREERDNVEREKLDIDRMRNMTEEERRQELRQNPKVVTNKATKGKYKFLQKYYHRGAFYLDEENDVLKRDFAQATLEDHFDKTILPKVMQVKNFGRCGRTKYTHLVDQDTTKFDSPWYAESSSNIKFHNEHAGGMRQQFDKPTGSKRKKME
Protein: Sensor histidine kinase CpxA (EC 2.7.13.3) (P0AE82)
Organism: Escherichia coli (strain K12)
Function: Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Activates CpxR by phosphorylation; has autokinase, phosphotransferase and (in the presence of Mg(2+) and/or ATP or ADP) phosphatase activity. The kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition. Involved in several diverse cellular processes, including the functioning of acetohydroxyacid synthetase I, the biosynthesis of isoleucine and valine, the TraJ protein activation activity for tra gene expression in F plasmid, and the synthesis, translocation, or stability of cell envelope proteins. Activates transcription of periplasmic protease degP, probably by phosphorylating the cognate response protein CpxR; overexpression of an outer membrane lipoprotein NlpE also leads to transcription of degP via CpxRA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:25207645, ECO:0000269|PubMed:3058985}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996, ECO:0000305|PubMed:3058985}.
Interaction partners:
- Transcriptional regulatory protein CpxR
- Periplasmic protein CpxP
- Lipoprotein NlpE
- DNA-binding dual transcriptional regulator OmpR
- Transcriptional regulatory protein BaeR
- Transcriptional regulatory protein PhoP
- Periplasmic serine endoprotease DegP
- Transcriptional regulatory protein RstA
- Outer membrane porin C
- Outer membrane porin F
Sequence:
MIGSLTARIFAIFWLTLALVLMLVLMLPKLDSRQMTELLDSEQRQGLMIEQHVEAELANDPPNDLMWWRRLFRAIDKWAPPGQRLLLVTTEGRVIGAERSEMQIIRNFIGQADNADHPQKKKYGRVELVGPFSVRDGEDNYQLYLIRPASSSQSDFINLLFDRPLLLLIVTMLVSTPLLLWLAWSLAKPARKLKNAADEVAQGNLRQHPELEAGPQEFLAAGASFNQMVTALERMMTSQQRLLSDISHELRTPLTRLQLGTALLRRRSGESKELERIETEAQRLDSMINDLLVMSRNQQKNALVSETIKANQLWSEVLDNAAFEAEQMGKSLTVNFPPGPWPLYGNPNALESALENIVRNALRYSHTKIEVGFAVDKDGITITVDDDGPGVSPEDREQIFRPFYRTDEARDRESGGTGLGLAIVETAIQQHRGWVKAEDSPLGGLRLVIWLPLYKRS
Protein: Fibroblast growth factor 5 (FGF-5) (Heparin-binding growth factor 5) (HBGF-5) (P15656)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Fibroblast growth factor receptor 3
- Vascular endothelial growth factor receptor 2
- Platelet-derived growth factor receptor alpha
- Beta-klotho
- Vascular endothelial growth factor receptor 3
Sequence:
MSLSLLFLIFCSHLIHSAWAHGEKRLTPEGQPAPPRNPGDSSGSRGRSSATFSSSSASSPVAASPGSQGSGSEHSSFQWSPSGRRTGSLYCRVGIGFHLQIYPDGKVNGSHEASVLSILEIFAVSQGIVGIRGVFSNKFLAMSKKGKLHASAKFTDDCKFRERFQENSYNTYASAIHRTEKTGREWYVALNKRGKAKRGCSPRVKPQHVSTHFLPRFKQSEQPELSFTVTVPEKKKPPVKPKVPLSQPRRSPSPVKYRLKFRFG
Protein: Protein ORF3 (pORF3) (O90299)
Organism: Hepatitis E virus genotype 1 (isolate Human/India/Hyderabad) (HEV-1)
Function: Small multifunctional phosphoprotein involved in virion morphogenesis, egress and counteracting host innate immunity. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. Acts also as a viroporin and forms ion conductive pores allowing viral particle release. Impairs the generation of type I interferon by down-regulating host TLR3 and TLR7 as well as their downstream signaling pathways. Down-regulates the phosphorylation of host IRF3 via the interaction with host SIRP-alpha, thereby inhibiting IFN-I expression. Interacts with host microtubules.
Subcellular location: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q81870}; Lipid-anchor {ECO:0000250|UniProtKB:Q81870}. Host cytoplasm, host cytoskeleton {ECO:0000269|PubMed:9371561}. Virion {ECO:0000250|UniProtKB:Q81870}. Host cell membrane {ECO:0000250|UniProtKB:Q81870}; Lipid-anchor {ECO:0000250|UniProtKB:Q81870}. Note=The N-terminal region seems to associate with the cytoskeleton probably via one of its hydrophobic regions (By similarity) (PubMed:9371561). Present on the surface of the membrane-wrapped virions (By similarity). {ECO:0000250|UniProtKB:Q81870, ECO:0000269|PubMed:9371561}.
Interaction partners:
Sequence:
MGSRPWALGLFCCCSSCFCLCCSRHRPVSRLAAVVGGAAAVPAVVSGVTGLILSPSQSPIFIQPTPSPRMSPLRPGLDLVFANPSDHSAPLGATRPSAPPLPHVVDLPQLGPRR
Protein: V-type proton ATPase subunit B, kidney isoform (V-ATPase subunit B 1) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 1) (Q91YH6)
Organism: Mus musculus (Mouse)
Function: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential for the proper assembly and activity of V-ATPase (By similarity). In renal intercalated cells, mediates secretion of protons (H+) into the urine thereby ensuring correct urinary acidification. Required for optimal olfactory function by mediating the acidification of the nasal olfactory epithelium.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:23028982, ECO:0000269|PubMed:29993276}. Basolateral cell membrane {ECO:0000269|PubMed:23028982}.
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit E 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit d 1
- V-type proton ATPase 116 kDa subunit a 1
Sequence:
MATTVDSRSSGFTGNSCDPGTAQEHVQAVTRNYITHPRVTYRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDSQKTTCEFTGDILRTPVSEDMLGRIFNGSGKPIDKGPAVMAEEFLDINGQPINPHDRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKAVLDYHEDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQVYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFITQGPYENRTVFESLDLGWKLLRIFPKEMLKRIPQSMTDEFYSRQGAQQDPASDTAL
Protein: Carnosic acid synthase (EC 1.14.14.61) (Cytochrome P450 76AK6) (SpCYP76AK6) (Miltiradien-20-al synthase) (EC 1.14.14.-) (Pisiferic acid synthase) (EC 1.14.14.-) (A0A0S1TPC7)
Organism: Salvia pomifera (Apple sage)
Function: Monooxygenase involved in the biosynthesis of carnosate, a potent antioxidant labdane-related diterpene natural product. Catalyzes the oxidation of 11-hydroxyferruginol to produce carnosate. Mediates the conversion of miltiradien into miltiradien-20-al (By similarity). Also involved in the production of pisiferic acid and derivative products from ferruginol (By similarity).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MQVLILLSLAFLASCVVAYSRRRPGGRGAGDLPPGPPRLPIIGNMLQLGQNPHKSLAHLAKTYGPLMSLKLGNQFVVVVSSPEMAREVLQRHGLVFSRPFTPIAVQILGHGEVSMNMLPATSPIWKKIRKIAREKLFSNQALHATRAVRRERLRKLADYVGRCSGAMNVGEATFTTMSNLMFATLFSVEITQYADSDSDSGVNKKFREHVNAITRYMGVPNIADFFPIFAPFDPQGLRRKLTYHLGSLLELVQSLIEQRLRARNAATYRKKDDFLEMLLDLSEGDEYDLSVNEIKHLCVDLIIAGSDTSAATTEWAMVELLLHPDKLAKLKAELKSVVGDKSIIEESDISKLPYLQATVKEVLRYHPAAPLLAPHLAEEETQLNGYIIPKNTKIFINDWTISRDPSIWKNPEMFEPERFLNNDIDFCGQHFELIPFGSGRRICPGLPLASRMLHCMVATLCHNFDWELEKGTESKQLQREDVFGLALQKKIPLRAIPIKV
Protein: Dynein regulatory complex subunit 4 (Growth arrest-specific protein 8 homolog) (Protein PF2) (Q7XJ96)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:12847082, ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337, ECO:0000269|PubMed:27472056}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:12847082, ECO:0000269|PubMed:23427265}.
Interaction partners:
Sequence:
MAPKKKGTKKESKKDAVATGDIEGASVEELNQKIGTLEKEKNKEEEYRNYMQLERDKINAFWEITKKDLEDRRAELRNKDREMEEMEERHQVEIKVYKQKVKHLLYEHQNNITTLKSDGELALKLQQDEYRKREGDLGKDKRNLKLELKEQELAHQDIIRQLKLEHAKEITKLRQEFEQQAKDLQSKYEKKMKMLRDDMELRRKQEIHEIEERKNTHINELMKKHERAFAEIKNYYNDITHNNLDLIKTLKEDVAEMKRREAANEKLMYEIAQDNKKLSEPLSRALKEVELLRQQLANYDKDKLSLAQTKARLLNAERQIKNLEWENEVLSQRFSKVQTERDELYGKFEASIYDVQQKTGLKSALLEKKVEALGEALEMKEAQLAEVLTAANLDPGTLAAINQRLEEVLDNKNQIIKALQYDVAKVSKAHNDLIRVYEAKLTEFGIPVDELGFRPLVTNTSTGPAGLVVGA
Protein: Odorant binding protein b (Odorant-binding protein 22a, isoform B) (Odorant-binding protein 22a, isoform C) (Q8MVX6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP02289p
- Odorant binding protein c
- IP02285p
- Uncharacterized protein
- Uncharacterized protein
- Accessory gland protein Acp29AB
- Odorant-binding protein 93a
- Lectin-29Ca
- Intrepid
- AT20289p
Sequence:
MRVLLAFVLLLGLSVLATKEPEEVKIVSECAKENNVHRKKALDLLMSYRLKKKTHNVMCFINCIFERTNILQKVKEKVVKENHNCDSIKDADKCAESFQKFQCLVKIEMKVRGIDRG
Protein: EPM2A-interacting protein 1 (Laforin-interacting protein) (Q8VEH5)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Laforin
Sequence:
MWMTPKRIRMEVDEALVFRPEWTQRYLVVEPAEGDGALCLVCRRLVASTRERDVRRHYEAEHEFYERFVGDEERAALVERLRQGDMSLAAVLTPEERATRAGLGLCRFLALKGRGWGEGDFVHQCMEVLLREVLPDHVGVLEGIDLSPEITRQRILSIDSNLRSQLFNRARDFKAYSLALDDQAFVAYENYLLVFIRGVGRDLEVQEDLLTIINLTHHFSVGALMSAILEALQTAGLSLQRMVGLTTTHTLRMIGENSGLVSYMREKAVSPNCWNVIHYSGFLHLELLSSYDVDINQIINTISEWVVMIKTRGVRRPEFQPLLTESESEHGERVNGRCLNNWLRRGKTLKLIFSLRKEIEAFLVSVGATTVHFSDKQWLCDFGFLVDIMDYLREISEELQISKVFAAAAFERICTFEGKLSSLQRHMEEVNLTDFPAFSIIVDELKQQFKEDQKIFDPDRYQMVISRLQKDFERHFKDLRFIKKDLELFSNPFSFKPEYAPISVRVELTKLQANTDLWNEYRVKDLGQFYAGLSGEAYPIIKGVAYKVASLFDSNQICDKAFAYLTRNQHTLSQPLTDEHLQALFRVATTEMDPRWDDLVRERNDS