wanglab/gogpt-training-data huggingface dataset:
Protein: Insulin-like growth factor-binding protein 2 (IBP-2) (IGF-binding protein 2) (IGFBP-2) (mIGFBP-2) (P47877)
Organism: Mus musculus (Mouse)
Function: Inhibits IGF-mediated growth and developmental rates (By similarity). IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P18065}.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Insulin-1
- Insulin-2
- Receptor-type tyrosine-protein phosphatase beta
- Receptor-type tyrosine-protein phosphatase zeta
- Insulin-like growth factor 1 receptor
Sequence:
MLPRLGGPALPLLLPSLLLLLLLGAGGCGPGVRAEVLFRCPPCTPERLAACGPPPDAPCAELVREPGCGCCSVCARQEGEACGVYIPRCAQTLRCYPNPGSELPLKALVTGAGTCEKRRVGTTPQQVADSDDDHSEGGLVENHVDGTMNMLGGGSSAGRKPLKSGMKELAVFREKVNEQHRQMGKGAKHLSLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDDRGPLEHLYSLHIPNCDKHGRYNLKQCKMSLNGQRGECWCVNPNTGKPIQGAPTIRGDPECHLFYNEQQETGGAHAQSVQ
Protein: Rhodopsin (P31356)
Organism: Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus)
Function: Photoreceptor required for image-forming vision at low light intensity (Probable). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Signaling mediates the activation of phospholipase C (Probable). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).
Subcellular location: Cell projection, rhabdomere membrane {ECO:0000269|PubMed:17554166, ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518}; Multi-pass membrane protein {ECO:0000269|PubMed:18463093, ECO:0000269|PubMed:18480818, ECO:0000269|PubMed:21906602, ECO:0000269|PubMed:26024518}.
Interaction partners:
Sequence:
MGRDLRDNETWWYNPSIVVHPHWREFDQVPDAVYYSLGIFIGICGIIGCGGNGIVIYLFTKTKSLQTPANMFIINLAFSDFTFSLVNGFPLMTISCFLKKWIFGFAACKVYGFIGGIFGFMSIMTMAMISIDRYNVIGRPMAASKKMSHRRAFIMIIFVWLWSVLWAIGPIFGWGAYTLEGVLCNCSFDYISRDSTTRSNILCMFILGFFGPILIIFFCYFNIVMSVSNHEKEMAAMAKRLNAKELRKAQAGANAEMRLAKISIVIVSQFLLSWSPYAVVALLAQFGPLEWVTPYAAQLPVMFAKASAIHNPMIYSVSHPKFREAISQTFPWVLTCCQFDDKETEDDKDAETEIPAGESSDAAPSADAAQMKEMMAMMQKMQQQQAAYPPQGYAPPPQGYPPQGYPPQGYPPQGYPPQGYPPPPQGAPPQGAPPAAPPQGVDNQAYQA
Protein: Calpain-1 catalytic subunit (EC 3.4.22.52) (Calcium-activated neutral proteinase 1) (CANP 1) (Calpain mu-type) (Calpain-1 large subunit) (Micromolar-calpain) (muCANP) (P97571)
Organism: Rattus norvegicus (Rat)
Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-364', 'Gly-377' and 'His-399'. Cleaves and activates caspase-7 (CASP7).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P07384}. Cell membrane {ECO:0000250|UniProtKB:P07384}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250|UniProtKB:P07384}.
Interaction partners:
- Calpastatin
- Calpain-2 catalytic subunit
- BCL2-antagonist/killer 1, isoform CRA_b.
- Calpain small subunit 1
- Cyclin-dependent kinase 5 activator 1
- BH3-interacting domain death agonist
- Interleukin-1 alpha
- Apoptosis regulator BAX
- Titin
- Talin 1
Sequence:
MAEELITPVYCTGVSAQVQKQRDKELGLGRHENAIKYLGQDYENLRARCLQNGVLFQDDAFPPVSHSLGFKELGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNETILHRVVPYGQSFQEGYAGIFHFQLWQFGEWVDVVVDDLLPTKDGKLVFVHSAQGNEFWSALLEKAYAKVNGSYEALSGGCTSEAFEDFTGGVTEWYDLQKAPSDLYQIILKALERGSLLGCSINISDIRDLEAITFKNLVRGHAYSVTDAKQVTYQGQRVNLIRMRNPWGEVEWKGPWSDNSYEWNKVDPYEREQLRVKMEDGEFWMSFRDFIREFTKLEICNLTPDALKSRTLRNWNTTFYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLEEVDDADDYDSRESGCSFLLALMQKHRRRERRFGRDMETIGFAVYQVPRELAGQPVHLKRDFFLANASRAQSEHFINLREVSNRIRLPPGEYIVVPSTFEPNKEGDFLLRFFSEKKAGTQELDDQIQANLPDEKVLSEEEIDDNFKTLFSKLAGDDMEISVKELQTILNRIISKHKDLRTNGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLTIFRKFDLDKSGSMSAYEMRMAIEAAGFKLNKKLHELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKILDTDLDGVVTFDLFKWLQLTMFA
Protein: Protein O-mannosyl-transferase 1 (EC 2.4.1.109) (Dolichyl-phosphate-mannose--protein mannosyltransferase 1) (Q8R2R1)
Organism: Mus musculus (Mouse)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Protein O-mannosyl-transferase 2
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Dystroglycan 1
- Ribitol 5-phosphate transferase FKRP
- Ribitol-5-phosphate transferase FKTN
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Protein O-mannose kinase
- Ribitol-5-phosphate xylosyltransferase 1
- Beta-1,4-glucuronyltransferase 1
Sequence:
MGSHSTGLEETLGVLPSWLFCKMLRFLKRPLVVTVDINLNLVALTGLGLLTRLWQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSGPPFGHMLLALGGWLGGFDGNFLWNRIGAEYSSNVPIWSLRLLPALAGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQTHSPFSVHWWLWLLLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLYRSGPHDQIMSSAFQASLEGGLARITQGQPLEVAFGSQVTLKSVSGKPLPCWLHSHKNTYPMIYENGRGSSHQQQVTCYPFKDINNWWIVKDPGRHQLVVNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWKLDIVNRESNRDTWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSPGYHESMVWNVEEHRYGKSHEQKERELELHSPTQLDISRNLSFMARFSELQWKMLTLKNEDLEHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRRRSICDLPEDAWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCRSQLQRNVFSALVVAWYSSACHVSNMLRPLTYGDTSLSPGELRALRWKDSWDILIRK
Protein: Extracellular serine/threonine protein kinase FAM20C (EC 2.7.11.1) (Dentin matrix protein 4) (DMP-4) (Golgi casein kinase) (Golgi-enriched fraction casein kinase) (GEF-CK) (Q8IXL6)
Organism: Homo sapiens (Human)
Function: Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs and plays a key role in biomineralization of bones and teeth. Constitutes the main protein kinase for extracellular proteins, generating the majority of the extracellular phosphoproteome. Mainly phosphorylates proteins within the Ser-x-Glu/pSer motif, but also displays a broader substrate specificity. Phosphorylates ERO1A, enhancing its activity which is required to maintain endoplasmic reticulum redox homeostasis and for oxidative protein folding. During endoplasmic reticulum stress, phosphorylates P4HB/PDIA1 which induces a functional switch, causing P4HB to change from an oxidoreductase to a molecular chaperone. This is critical to maintain ER proteostasis and reduce cell death under ER stress. Phosphorylation of P4HB also promotes its interaction with ERN1, leading to reduced activity of ERN1, a key sensor for the endoplasmic reticulum unfolded protein response. Required for osteoblast differentiation and mineralization. Phosphorylates casein as well as a number of proteins involved in biomineralization such as AMELX, AMTN, ENAM and SPP1/OPN. In addition to its role in biomineralization, also plays a role in lipid homeostasis, wound healing and cell migration and adhesion.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:32149426, ECO:0000269|PubMed:34349020}; Single-pass type II membrane protein {ECO:0000269|PubMed:34349020}. Secreted {ECO:0000269|PubMed:26091039}. Endoplasmic reticulum {ECO:0000269|PubMed:32149426}. Note=Resides in the Golgi apparatus membrane and is secreted following propeptide cleavage (PubMed:34349020). Retained in the endoplasmic reticulum (ER) in response to ER stress where it phosphorylates P4HB (PubMed:32149426). {ECO:0000269|PubMed:32149426, ECO:0000269|PubMed:34349020}.
Interaction partners:
- Pseudokinase FAM20A
- Osteopontin
- NADH-ubiquinone oxidoreductase chain 1
- Dentin matrix acidic phosphoprotein 1
- Ameloblastin
- Enamelin
- NADH-ubiquinone oxidoreductase chain 5
- Matrix extracellular phosphoglycoprotein
- NADH-ubiquinone oxidoreductase chain 4
- Proprotein convertase subtilisin/kexin type 9
Sequence:
MKMMLVRRFRVLILMVFLVACALHIALDLLPRLERRGARPSGEPGCSCAQPAAEVAAPGWAQVRGRPGEPPAASSAAGDAGWPNKHTLRILQDFSSDPSSNLSSHSLEKLPPAAEPAERALRGRDPGALRPHDPAHRPLLRDPGPRRSESPPGPGGDASLLARLFEHPLYRVAVPPLTEEDVLFNVNSDTRLSPKAAENPDWPHAGAEGAEFLSPGEAAVDSYPNWLKFHIGINRYELYSRHNPAIEALLHDLSSQRITSVAMKSGGTQLKLIMTFQNYGQALFKPMKQTREQETPPDFFYFSDYERHNAEIAAFHLDRILDFRRVPPVAGRMVNMTKEIRDVTRDKKLWRTFFISPANNICFYGECSYYCSTEHALCGKPDQIEGSLAAFLPDLSLAKRKTWRNPWRRSYHKRKKAEWEVDPDYCEEVKQTPPYDSSHRILDVMDMTIFDFLMGNMDRHHYETFEKFGNETFIIHLDNGRGFGKYSHDELSILVPLQQCCRIRKSTYLRLQLLAKEEYKLSLLMAESLRGDQVAPVLYQPHLEALDRRLRVVLKAVRDCVERNGLHSVVDDDLDTEHRAASAR
Protein: Desmoglein-1-gamma (Dsg1-gamma) (Desmoglein-6) (Q7TSF0)
Organism: Mus musculus (Mouse)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q7TSF1}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q7TSF1}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q7TSF1}. Cytoplasm {ECO:0000250|UniProtKB:Q02413}. Nucleus {ECO:0000250|UniProtKB:Q02413}.
Interaction partners:
- Corneodesmosin
- Desmocollin-1
- Junction plakoglobin
- Desmoglein-1-alpha
- Desmoglein-1-beta
- Desmoplakin
- Envoplakin
- Filaggrin
- Periplakin
Sequence:
MDWHSFRIAALLLTSLVVLEVNSEFQIQVRDHNAKNGTIKWHSIRRQKREWIKFAAACREGEDNSKRNPIAKIHSDCAANQPVTYRISGVGIDQPPYGIFIINQKTGEINITSIVDREVTPFFIIYCRALNAQGQDLENPLELRVRVMDINDNPPVFSMTTFLGQIEENSNANTLVMKLNATDADEPNNLNSMIAFKIIRQEPSDSPMFTINRKTGEIRTMNNFLDREQYSQYSLVVRGSDRDGGADGMSAESECSITILDVNDNIPYLEQSSYDITIEENTLHSQLLQIRVIDLDEEFSDNWKAIIFFISGNEGNWFEIEMNERTNVGTLKVVKPLDYEAVKNLQLCIGVRNVAEFHQSIISQYRLTVTLITVTVLNVVKGCVFQPGSKTFIVDSRMEANHTVGEFLATDCETGQATNKFKNVRYRYVMGNNPENLLVVDSGIITLRNRVTMEQYERLNKRYEGTVLSIHDSLQRTCTGTIIMVLCGFWTTTEHPTTSTEKPVTLSITPNVDNVHFGPAGIGLLIMGFLVLGLVPFLLISCDCGGAPGGGAGFEPVPECSDGAIHTWAVEGPQPGGITTICVPQMPPGNANVIEYIDNSGVYTNEYCGREMQDLGGGERTTGFELMDGVKTSAAPEICQEYSGTLRRNSMRECRDGGLNMNFMESYFCQKAYAYADEDEGRPSNDCLLIYDIEGVGSPAGSVGCCSFIEDLDESFLDTLGPKFKKLADISLGKEIDSYPDPDPSWPPQSTEPICPQHMEQLASGHPSISPHFGKTTVISENAYPSGPGVQHPMLIPDPLGYGNITVRESYTTSGTLKPSVHFHDNQQASNVVVTERVVGPISGADLHGMLEIPALRDGTNVIVTERVIAPGSSLPNSLTIPNPRETSNVVVTERVIQPTSGMIGNLSIPP
Protein: Olfactory receptor (A0A126GW15)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
Sequence:
MKNKSMEIEFILLGLTDDPQLQIVIFLFLFLNYTLSLMGNLIIIILTLLDPRLKTPMYFFLRNFSFLEVIFTTVCIPRFLITIVTRDKTISYNNCATQLFFILLPGVTEFYLLAAMSYDRYVAICKPLHYPIIMSSKVCYQLVLSSWVTGFLIIFPPLVMGLKLDFCASKTIDHFMCETSPILQISCTDTHVLELMSFTLAVVTLVVTLVLVILSYTCIIKTILKFSSAQQRNKAFSTCTSHMIVVSMTYGSCIFMYIKPSAKERVTVSKGVALLYTSIAPLLNPFIYTLRNQQVKEVFWDVLQKNLCFSKRPF
Protein: UDP-glycosyltransferase 79A6 (EC 2.4.1.159) (Flavonol 3-O-glucoside (1->6) rhamnosyltransferase) (GmF3G6''Rt-a) (I1LCI8)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Flavonol 3-O-glucoside (1->6) rhamnosyltransferase converting kaempferol 3-O-glucoside to kaempferol 3-O-rutinoside and utilizing 3-O-glucosylated/galactosylated flavonols and UDP-rhamnose as substrates. Prefers kaempferol to quercetin as an aglycon, and 3-O-galactosides to 3-O-glucosides as a glycosylation pattern.
Interaction partners:
- UDP-glycosyltransferase 79B30 glucosyltransferase)
- UGT79B131
- Glycosyltransferase
- Glycosyltransferase
- UGT79B130
- Glycosyltransferase
- Flavonol-3-O-glucoside/galactoside
- UGT79B128
- Glycosyltransferase
- Beta-conglycinin alpha subunit 2
Sequence:
MPSELAMNNDELHVVMFPFLAFGHISPFVQLSNKLFSHGVHVTFLSAASNIPRIRSTLNLNPAINVISLKFPNGITNTAELPPHLAGNLIHALDLTQDQVKSLLLELKPHYVFFDFAQHWLPKLASEVGIKSVHFSVYSAISDAYITVPSRFADVEGRNITFEDLKKPPPGYPQNSNISLKAFEAMDFMFLFTRFGEKNLTGYERVLQSLGECSFIVFKTCKEIEGPYLDYIETQFRKPVLLSGPLVPEPSTDVLEEKWSKWLDGFPAKSVILCSFGSETFLSDYQIKELASGLELTGLPFILVLNFPSNLSAKAELERALPKGYLERVKNRGVVHSGWFQQQLVLKHSSVGCYVCHGGFSSVIEAMVNECQLVLLPFKGDQFFNSKLIANDLKAGVEVNRSDEDGFFHKEDILEALKTVMLEDNKEQGKQIRENHMQWSKFLSNKEIQNKFITDLVAQLKSMA
Protein: FAM50 family protein C1020.12c (Q7LKZ5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Histone H2A.Z
Sequence:
MSGHTDADEIHEILRNSTTGLVHLKDYQRVKQNIVEKREKHALSTTSTKIKKRKDALSKKVKQGIKVNKGKLSFGEDEELENDDLPLKKVEKKMFMGKDPSADTSFLPDAEREIRENAKRAEYRKQWLKEQEQIREKEILIPFIYYDGTSTTYHVRTRLKDSVGHFLADMKQQIPFLKRILDMDKFLLVQSDLIIPHHHELYYFYINKVQGRDGLLFDFDKLSCSSPEMVATTQLPSQCIPHLVQKSYYLQNRHVFPCVHWEVFDSRKDYSLEKHATDPNAALFYRPS
Protein: Tubulin beta-1 chain (Q9H4B7)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18849486}.
Interaction partners:
- Tubulin alpha-1B chain
- Tubulin alpha-4A chain
- Tubulin alpha-1C chain
- Tubulin alpha-3C chain
- Tubulin alpha-3E chain
- Tubulin alpha-8 chain
- Tubulin alpha-1A chain
- Tubulin alpha chain-like 3
- Gap junction alpha-1 protein
- Microtubule-associated protein tau
Sequence:
MREIVHIQIGQCGNQIGAKFWEMIGEEHGIDLAGSDRGASALQLERISVYYNEAYGRKYVPRAVLVDLEPGTMDSIRSSKLGALFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVLEVVRHESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRIMNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENADACFCIDNEALYDICFRTLKLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNTMAACDLRRGRYLTVACIFRGKMSTKEVDQQLLSVQTRNSSCFVEWIPNNVKVAVCDIPPRGLSMAATFIGNNTAIQEIFNRVSEHFSAMFKRKAFVHWYTSEGMDINEFGEAENNIHDLVSEYQQFQDAKAVLEEDEEVTEEAEMEPEDKGH
Protein: Probable E3 ubiquitin-protein ligase plr-1 (EC 2.3.2.-) (Probable E3 ubiquitin-protein transferase plr-1) (Q9U2B7)
Organism: Caenorhabditis elegans
Function: Probable E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled (By similarity). Acts on both canonical and non-canonical Wnt signaling pathway (By similarity). Plays a role in the migration and axon guidance of different neuronal cell types including CAN, HSN, AVK and AVG. Promotes the differentiation and regulates the anteroposterior polarity of AVG unpaired interneurons by sequestering the Wnt signaling proteins cfz-2, mig-1 and mom-5 to endosomes which thereby reduces their cell surface expression and negatively regulates Wnt signaling. May also regulate AVG polarity and axon guidance through Wnt-independent mechanisms involving unc-53/Nav2, unc-73/Trio and cytosolic protein vab-8.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ULT6}; Single-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:24401370, ECO:0000269|PubMed:25448694}. Late endosome {ECO:0000269|PubMed:24401370}. Perikaryon {ECO:0000269|PubMed:25448694}. Cell projection, axon {ECO:0000269|PubMed:25448694}.
Interaction partners:
- Acyl_transf_3 domain-containing protein
- ubiquitinyl hydrolase 1
- BED-type domain-containing protein
Sequence:
MRLLLFILLNTTLLSTNYVHARPSVSHTTLASQFKFAEKADIFVTHTNINEDRTQDEKTIKLSGTFSPVGSNYETGGDIVQVSSFRACDARRKGLDNTVFEHVPVVFYDDVEKFLTGCVALDNQARFAEKSGAMALIVGPASRVERTTRPMMIGGSKIPVIVLDDEQTERLRSELRSASERGAVTKLRISFIDEKPTKVLKLQVFRPTVLNITLLGLLIILIVFVSLLVVVKIRCQPTMHRELWLRALARTALTKMEIRSFQKEKNVEAGQKKKTSSTFARLKQHRSSSSRHSSYLAVFGSLTSVAQSSSHSAQERCVICLEEYEEGTELRVLFCGHEFHPKCVDPWLLSKRRCPLCQFDVVYKHYPKVDSPEKLSGRSDDTTSLLPRTSPSEDLPSAPSSRSTRLTRPYRTTHHLIPSSTRPSSHQRPSLQPTAPRTRSCPRRRQLRSRNQIDFSIRIGGYSSDVSSSHAEQSRSFEIEPRTSQQL
Protein: Zinc finger FYVE domain-containing protein (Q7K9H6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR037289}. Early endosome membrane {ECO:0000256|PIRNR:PIRNR037289}.
Interaction partners:
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog
- Myopic
- Protein mothers against dpp
Sequence:
MDLVDIDQVLDNLELSIAADEQLSRNAAAAAAAGANPGRFLGDGASASISGVGAGAGVSGAAGVTPTPASGKSFVGVSQVFNSLDDYRENVKSLQVDAQLPSYDWQTEAEHEDDIHKFSEQASKNNGQTIVSSSESLTTSSCSTFSSGPSPVSNGSHSEELATPPEDEKTSEVQVEPKEQDQQPEQVKHEDQHQDQAVPPPTQSKQTVEELAVGLSSISITASGTESQSLLPEEVTASSVLGQVLEELSEESSPSREPETEMTNGIDVPLANLPASVAEVPVPKEMEQPVQTEEEDVELPQEQHPRRSQPLTFCSTMDEISDTELDSMLQEMDADDNQADDQQMPDDEKSCSASPVTEEESVRILSDEQETTSNDQMNVDNFSQASTVEFADLKQPESTPVTAMGEDVASSFSSTESDSLSGRKLDGEVEVDREHEDASLATDALETQEQRPQRPQTLNLNGCQAESSTPSQDENPEIQQETLQPTEVREGAAGVGVIPGEDDEESPIYEAVGYSDPHANLGKVPPIWVPDNMAGQCMQCQQKFTMIKRRHHCRACGKVLCSVCCSQRFRLEFATEPESRVCVQCYMILSERQANGLNSESAPGSALPPTPIRSPNPNNPMEYCSTIPPHRQVANSPGAPPPSVIVPVGVLKKTDGSSSNSSSSDGQKGQRKRKSVMFSDGIAPGSELASTMEQQWGESKHSRRGLSRSGSGAGQKPPTPATEEPPRSIDTSSTLGLVAQLFRGSIPPSAAAATLSATETSAGRSSSQSQAQTSPRRKAESSRNRKLPPNGDAQGCYLPPEENGLPPICISSKEGGEVDYKVVRNDGSLLDRLQNETLKFIIKNNFFVLVKIVNMSCCMNRWVLNFTTSGLHHMGSDELIILLEIKQPKQEEYVKGEVAIPKDLFQHLYEIYVEAEHARSGTHELAFTSPRNANFLGSREHGGFIFIRPTYQCLQGVIVPDNPYLVGVLIHRHEVPWAKVLPLRLILRLGAQYRYYPCPLISVRGRESVYGEIAQTIINFLVDFRNYSYSLPAIRGLYIHMEDRQTTVIIPKYRQQDVIKAINNASDHILAFAGNFSKVADGHLVCMQNINDDRSEMYSYSTQAINIQGQPRKITGASFFVLNEALKSSSGLSGKCSIVEDGLMVQIMPAKMEEVRQALRNQNDIDIVCGPIDATDDQSEIVSIKWVDNNRDINVGVKSPIDDQPMDGISNMRVLKWASFNYSNTNYAIRLSDIYIIKCEDWYATNGGNCEEITRIAEQLARSASMALLPLLDLLAAAGINKLGLRATLDQDNVGYEAGARGSKLPPLYMNALDNHLIATLHGESSGIQEPIILELIFYILNA
Protein: Thioester-containing protein 4, isoform B (M9PD73)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEPVKAEGKYTIVGPGTIHSHRDYNVAVAVHQTKEPVTLKVGITGPSYNKTETVELATAGEFKQITFKLPPLEAGEYNLTAEGVKGLEFKNSTKLNWENFKPYIKIQTDKGKYKPGDTINYRVIFLDENLRPDTAKDEVVVWFEDSKRNRIKQEKHIKTTGGVYTGKFELSEFATLGSWSLHVQNGDQHHDGGIYFGGRKQFGGFGHRWHRSDELVNFEVEKYVLPKYSVKMDATQQVSVRDGEFNVVLKANYTYGKPVNGKVLVNVHLDSTSSWENVDGKTVQTDYPGHSVVGTADMVGGKAKLTMDLKDFASYLPHKTSSSYAQITATVEEDFTGVKLNETGGVQLYPYRYEMSCTDYSSCFSFKPDKEHELNFKITYVDGSLITDTKSVVKAKFTEGIRRNYAFYAFGTDHQEPELPTIEKKTFVFESHLNASGVAPFKVVLPDLPDIANFTRYYSIELEFVDEKRDLYTTYPYREPKQIENPSSEEEKEWFRAEVQRPKDVWNLKIGQEYQVILNSSRPLKYFVYNIVGRGNILETKRVDLAEPQTTVNVTIKPTFLTTPYGRVYFYYVDETGEFRYTEETFSVEVELQNQIEIKAPAEVKPGADVALEIKTSPKSFVGLLAVDQSVLLLGSNNDLNKESFNWRLNGYDTSTPWQGGYSYYPGERTGVVTMTNAYFFYNRTAPDYNIQGFGGSSFAMRKTTVAHDSHVFHSGAGGPTQAVGFSAESASASAAPVVRKNFAETWIFADIESTEEEVFKWVKTIPDTITNWVVTGFSLHPQKGLGVTNDQTNIKTFQPFFVSVRLPYSVKRGEVINVPALVFNYLPKTLDVELTLDNEDQEYDFVDASNEVIGDQKRTQNIRVGANEAAGASFLIRPKVIGNILLKFKAISPLAGDAIHKPLKVVPEGITQYQNRAFFINLKDTGEFKNTFELEVPEDVVPDSERVEFGLVGDLLGPVVKNLENLLRLPSGCGEQTMSKLVPNYLVRDYLKSIKKLTPALDTRIKRNLQDGYQHMLHYRHDDGSFSSFGPTKWRQEDPVRNGSTWLTAYVLRSFSKIKDIIDLDEQILAKGYEFLLTRQAENGSFTEHGEYFYSSQRSLLTLTANSLLALLEEEKPNQAAIDKAVAYLSANTAESIELLPKSIAIYALQKAKAPEAAKQVASLKSLAKHEDDRTWWTEDLDKLRASKNCGRWWCWIWSQDVEITSYALLSLLDSDQETADSVLNTVRWLIAQRNGFGGFASSQDTVVGLTALIKFAEKSGYEAAKWEVTVSNKGKREKTEKLNTSEENDLLLQTVEFPQGTKSLEFEAKGTGAAMVQISYQYNLVEKEPKPSFKIQTTVLPESSPANLELSVCVDYVEEGESKESNMAILEVSLPSGYTADEDSFADIRNIERVRLVETKNGDSVVVIYFENLAKNEEKCIRIEAYRTHAVANQKPSSVVLYDYYDTNKKATEYYSIKSKLCDICEGDDCKSKC
Protein: Eukaryotic initiation factor 4A-3 (eIF-4A-3) (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A-3) (DEAD-box ATP-dependent RNA helicase 23) (Q9CAI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor isoform 4G-1
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor isoform 4G-2
- Protein mago nashi homolog
- Regulator of nonsense transcripts UPF2
- RNA-binding protein Y14
- Eukaryotic initiation factor 4A-2
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic initiation factor 4A-1
- Eukaryotic translation initiation factor 3 subunit B
Sequence:
MAGMASDGTQYDPRQFDTKMNAILGEEGEETFYTNYDEVCDSFDAMELQPDLLRGIYAYGFEKPSAIQQRGIIPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDISLVQCQALVLAPTRELAQQIEKVMRALGDYLGVKAQACVGGTSVREDQRVLQSGVHVVVGTPGRVFDLLRRQSLRADAIKMFVLDEADEMLSRGFKDQIYDIFQLLPSKVQVGVFSATMPPEALEITRKFMNKPVRILVKRDELTLEGIKQFYVNVDKEEWKLETLCDLYETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGRSGRFGRKGVAINFMTSEDERMMADIQRFYNVVVEELPSNVADLL
Protein: CRS2-associated factor 2, mitochondrial (Q9FFU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the splicing of group IIB introns in mitochondria.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
Sequence:
MLSIRRSLTLAKEPKDLFLFLCNLRARCVSTDDYDPPFSPLSKPTKPPKEKKKQKTKKQDQSSELVNDLKIPVISDLPFDFRYSYSETNPEIEPIGFREPKRFSPFGPGRLDRKWTGTTALASPEIDQSQWVEERARVLGETLTEDEVTELIERYRHSDCTRQINLGKGGVTHNMIDDIHNHWKKAEAVRIKCLGVPTLDMDNICFHLEEKSGGKIVYRNINILVLYRGRNYDPKSRPIIPLMLWKPHPPIYPRLVKNVADGLEFEETKEMRNRGLHSPALMKLTRNGVYVNVVGRVREEFETEEIVRLDCTHVGMSDCKRIGVKLKEMVPCVPILFKDEQIILWRGKRTGEEELVTL
Protein: Iron-sulfur cluster assembly SufBD family protein ABCI8, chloroplastic (ABC transporter I family member 8) (ABC transporter ABCI.8) (AtABCI8) (Non-intrinsic ABC protein 1) (Protein ABC1) (Plastid sufB-like protein) (Protein LONG AFTER FAR-RED 6) (Q9ZS97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in light signaling, probably by mediating the transport and correct distribution of protoporphyrin IX, a chlorophyll precursor, in response to far-red light.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:11156608}.
Interaction partners:
- ABC transporter I family member 6, chloroplastic
- Cysteine desulfurase 1, chloroplastic
- Protein ABC transporter 1, mitochondrial
- Iron-sulfur cluster assembly protein 1
- Iron-sulfur cluster assembly protein 3
- Iron-sulfur cluster assembly protein 2
- ABC transporter I family member 1
- Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic
- ABC transporter I family member 17
- ABC transporter I family member 10
Sequence:
MASLLANGISSFSPQPTSDSSKSPKGFHPKPESLKFPSPKSLNPTRPIFKLRADVGIDSRPIGASESSSSGTSTVSSTDKLQQYFQNLDYDKKYGFVEDIDSFTIPKGLSEETIRLISKLKEEPDWMLEFRFKAYAKFLKLEEPKWSDNRYPSINFQDMCYYSAPKKKPTLNSLDEVDPQLLEYFDKLGVPLTEQKRLANVAVDAVIDSVSIATTHRKTLEKSGVIFCSISEAIREYPDLIKKYLGRVVPSDDNYYAALNSAVFSDGSFCYIPKNTRCPMPISTYFRINAMETGQFERTLIVAEEGSFVEYLEGCTAPSYDTNQLHAAVVELYCGKGAEIKYSTVQNWYAGDEQGKGGIYNFVTKRGLCAGDRSKISWTQVETGSAITWKYPSVVLEGDDSVGEFYSVALTNNYQQADTGTKMIHKGKNTKSRIISKGISAGHSRNCYRGLVQVQSKAEGAKNTSTCDSMLIGDKAAANTYPYIQVKNPSAKVEHEASTSKIGEDQLFYFQQRGIDHERALAAMISGFCRDVFNKLPDEFGAEVNQLMSIKLEGSVG