wanglab/gogpt-training-data huggingface dataset:
Protein: Diazepam-binding inhibitor-like 5 (Endozepine-like peptide) (ELP) (P56702)
Organism: Rattus norvegicus (Rat)
Function: May be involved in the energy metabolism of the mature sperm.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Acyl-CoA-binding protein
- Tetratricopeptide repeat domain 39D
Sequence:
MSQVEFEMACASLKQLKGPLSDQEKLLVYSFYKQATQGDCNIPVPPATDVKAKAKWEAWMVNKGMSKMDAMRIYIAKVEELKKNETC
Protein: Rad10p (Q5AA15)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SsDNA endodeoxyribonuclease
- SsDNA endodeoxyribonuclease
- Crossover junction endonuclease MUS81
- DNA repair protein RAD14
- Endonuclease
- DNA 5'-3' helicase
- Nuclear protein localization protein 4
- UV excision repair protein RAD23
- asparagine--tRNA ligase
- DNA 3'-5' helicase
Sequence:
MSNTKDNANDIDASSFASILAGVQKMREDAGSIPSQDPTLAEVNHDTQPNASSLNAIQPPAPVPAPPPQTHTNVTNEKYQKATLNESTAKPIPPKRNNNSVKPSTKRTQTSGPSDILVSRSQEGNPLLSTPIMQATPWSFDKSLLSDYYINPKFQIIFLTLKYHKLHPEHIWNRWKKLNQGSSTVHTRGDDALRVLLVVVDVDSHQDLLRKLSDFCIKHDLSLVLAWSYEEAANYIALCKQLDKAPLKGRKIIEGTKGSDYNSSVVKAFTGIKSVNKTDVSNLLANCKSVKEIVLQSCQNDNDDGIGLASIPGLGAKKLENLKKVFSEPFISNKDYDT
Protein: Nucleoside diphosphate kinase (NDK) (NDP kinase) (EC 2.7.4.6) (Nucleoside-2-P kinase) (P0A763)
Organism: Escherichia coli (strain K12)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000305}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS2
- Cytidylate kinase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Small ribosomal subunit protein bS16
- Uridylate kinase
- Adenylate kinase
Sequence:
MAIERTFSIIKPNAVAKNVIGNIFARFEAAGFKIVGTKMLHLTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLEGENAVQRHRDLLGATNPANALAGTLRADYADSLTENGTHGSDSVESAAREIAYFFGEGEVCPRTR
Protein: Folate receptor alpha (FR-alpha) (Folate receptor 1) (Folate-binding protein 1) (P35846)
Organism: Mus musculus (Mouse)
Function: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH (By similarity). Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release (By similarity). Required for normal embryonic development and normal cell proliferation. Required for renal folate reabsorption.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P15328}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15328}. Apical cell membrane {ECO:0000250|UniProtKB:P15328}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15328}. Basolateral cell membrane {ECO:0000250|UniProtKB:P15328}; Lipid-anchor, GPI-like-anchor {ECO:0000250|UniProtKB:P15328}. Secreted {ECO:0000250|UniProtKB:P15328}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P15328}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P15328}. Endosome {ECO:0000250|UniProtKB:P15328}. Note=Endocytosed into cytoplasmic vesicles and then recycled to the cell membrane. {ECO:0000250|UniProtKB:P15328}.
Interaction partners:
- Sperm-egg fusion protein Juno
- Folate receptor beta
- Reduced folate transporter
- Proton-coupled folate transporter
- Glutamate carboxypeptidase 2
Sequence:
MAHLMTVQLLLLVMWMAECAQSRATRARTELLNVCMDAKHHKEKPGPEDNLHDQCSPWKTNSCCSTNTSQEAHKDISYLYRFNWNHCGTMTSECKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERILDVPLCKEDCQQWWEDCQSSFTCKSNWHKGWNWSSGHNECPVGASCHPFTFYFPTSAALCEEIWSHSYKLSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAEAMSGAGFHGTWPLLCSLSLVLLWVIS
Protein: NADPH oxidase (Q2PEP0)
Organism: Epichloe festucae
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAGQYGYRELIRKQFTTQKLFFHVLFWIFHWGIFAYGWWKQASEPRLAGLNTLKFSVWISRGAGLVLSVDGMLILLPVCRTIMRWLRPKLRFLPMDENLWFHRQLAYALLVFAILHVGAHYVNFFNVEQTQIRPVSALQIHYAQAGGITGHVMLLCMLLMYTTAHSRIRQQSFETFWYTHHLFIPFFLALYTHTVGCFVRDSVDAFSPFAGEQYWNHCIGYLGWRWELWTGGLYLVERLYREIRARRETQITRVVRHPYDVVEVQFNKPSFKYKAGQWLFLQVPSISKYQWHPFTITSCPFDPYVSVHVRQVGDFTRALGDATGAGGAQAKLYDGVDPMGMYEVALQNGQQMPGLRIDGPYGAPAEDVFENEIAVLIGTGIGVTPWAAILKNIWHLRNSPNPPTRLRRVEFIWVCKDTGSFEWFQTLLSSLEEQSIEAARVPGSSGVEFLKIHTYLTQKLDMDTTQNIVLNSVGADMDPLTELKSRTHFGRPDFNRLFTTMRDGILDRTYLNGLEGSMRTTVGVYFCGPSVAARDIKSACKSATAREVNFRFWKEHF
Protein: Putative lipoprotein LppO (P9WK71)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Putative thiosulfate sulfurtransferase SseB
- Oxaloacetate decarboxylase
- Possible conserved lipoprotein LppH
- HNH nuclease domain-containing protein
- Probable conserved transmembrane protein
- Conserved protein
- Possible PhiRv2 prophage protein
- Putative lipoprotein LppK
Sequence:
MTDPRHTVRIAVGATALGVSALGATLPACSAHSGPGSPPSAPSAPAAATVMVEGHTHTISGVVECRTSPAVRTATPSESGTQTTRVNAHDDSASVTLSLSDSTPPDVNGFGISLKIGSVDYQMPYQPVQSPTQVEATRQGKSYTLTGTGHAVIPGQTGMRELPFGVHVTCP
Protein: Putative transferase CAF17, mitochondrial (EC 2.1.-.-) (57 kDa iron-sulfur cluster assembly factor for biotin synthase- and aconitase-like mitochondrial proteins) (CCR4-associated factor 17) (P47158)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for lysine and glutamate prototrophy and mitochondrial genome maintenance. Has a role in the maturation of mitochondrial aconitase-type and radical-SAM Fe/S proteins biotin synthase and lipoic acid synthase.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:18086897}.
Interaction partners:
- Iron-sulfur assembly protein 2
- Iron-sulfur assembly protein 1
- NifU-like protein
- Cysteine desulfurase, mitochondrial
- Protein ISD11
- Lipoyl synthase, mitochondrial
- Frataxin homolog, mitochondrial
- Iron sulfur cluster assembly protein 1, mitochondrial
- Adrenodoxin homolog, mitochondrial
- Monothiol glutaredoxin-5
Sequence:
MFISRRCRIKGFTLKNLLWFRSSSTRFVSTESPDASAITKPDGIFNYSLLENRTYIRIRGPDTVKFLNGLVTSKLLPHFIKKNLTTVEENEVPTEEGTTKVDPIIPVPEFDARLGNWGLYNEKGIQGPYISRFGLYSAFLNGKGKLITDTIIYPTPVTVSEQISNYPEYLLELHGNVVDKILHVLQTHKLANKIKFEKIDHSSLKTWDVEVQFPNLPKDIENPWFDNLLDPMALPKNSIDANNFAVNVLNSLFNSDPRILGIYVERRTESMSRHYSTFPQSFRVVTSEQVDDLSKLFNFNVFDFPFQVNKKASVQVREIRFQKGLIDSTEDYISETLLPLELNFDFFPNTISTNKGCYVGQELTARTYATGILRKRLVPVKLDNYQLLDTDPERKYAEFHIDNVVEKSLAENEPTLNPFTNKPPERTKRKQRPAGLLISNEGLYGVALLRTEHFSAAFSSDEPVEFYITTTKGENIKITPQKPFWFSDWKNNNGPHK
Protein: Uncharacterized protein (Q8CCC1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
DSFLVVLKAMTKNIGDDGGGDDNTFNFSWKVFCSWDYLIGNPETADNKFNSITMNFKEAIIEERAAQVEENIHLIRFLRFLANFFVFLTLGASGYLIFWAVKRSQEFAQQDPDTLGWWEKNEVRLCMRLTC
Protein: NAC domain-containing protein 71 (ONAC071) (OsNAC5) (Q53NF7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription activator that binds to the promoter of the stress response gene LEA19. Involved in tolerance to abiotic stresses.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:20632034}.
Interaction partners:
- Os04g0589400 protein
Sequence:
MECGGALQLPPGFRFHPTDDELVMYYLCRKCGGLPLAAPVIAEVDLYKFNPWDLPERAMGGEKEWYFFSPRDRKYPNGQRPNRAAGTGYWKATGADKPVGSPRAVAIKKALVFYAGKPPKGVKTNWIMHEYRLADVDRSAAARKLSKSSHNALRLDDWVLCRIYNKKGVIERYDTVDAGEDVKPAAAAAAAKGGRIGGGGGAAAMKVELSDYGFYDQEPESEMLCFDRSGSADRDSMPRLHTDSSGSEHVLSPSPSPDDFPGGGDHDYAESQPSGGCGGWPGVDWAAVGDDGFVIDSSLFELPSPAAFSRAAGDGAAFGDMFTYLQKPF
Protein: DNA-directed RNA polymerases II, IV and V subunit 6A (RNA polymerase Rpb6) (Q9FJ98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 12
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerase IV subunit 1
- DNA-directed RNA polymerase III subunit 2
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases IV and V subunit 2
- DNA-directed RNA polymerases II, IV and V subunit 9B
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerase subunit 10-like protein
Sequence:
MADEDYNDVDDLGYEDEPAEPEIEEGVEEDVEMKENDDVNGEPIEAEDKVETEPVQRPRKTSKFMTKYERARILGTRALQISMNAPVMVELEGETDPLEIAMKELRQRKIPFTIRRYLPDGSFEEWGVDELIVEDSWKRQVGGD
Protein: Dendritic cell-specific transmembrane protein (DC-STAMP) (mDC-STAMP) (Dendrocyte-expressed seven transmembrane protein) (Transmembrane 7 superfamily member 4) (Q7TNJ0)
Organism: Mus musculus (Mouse)
Function: Probable cell surface receptor that plays several roles in cellular fusion, cell differentiation, bone and immune homeostasis. Plays a role in TNFSF11-mediated osteoclastogenesis. Cooperates with OCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign body giant cells (FBGCs). Participates in osteoclast bone resorption. Involved in inducing the expression of tartrate-resistant acid phosphatase in osteoclast precursors. Plays a role in haematopoietic stem cell differentiation of bone marrow cells toward the myeloid lineage. Inhibits the development of neutrophilic granulocytes. Plays also a role in the regulation of dendritic cell (DC) antigen presentation activity by controlling phagocytic activity. Involved in the maintenance of immune self-tolerance and avoidance of autoimmune reactions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Endosome. Note=Localized to the cell surface in osteoclasts and undifferentiated monocytes. Intracellular internalized DCSTAMP is detected in a fraction of RANKL-induced osteoclast precursor. Colocalizes with OS9 in the endoplasmic reticulum (ER) of immature dendritic cell (DC). Translocates from the endoplasmic reticulum to the intermediate/Golgi compartment upon maturation of DC in a OS9-dependent manner. Colocalizes with LAMP1 in endosomes.
Interaction partners:
- Osteoclast stimulatory transmembrane protein
- Cathepsin K
- Nuclear factor of activated T-cells, cytoplasmic 1
- Tumor necrosis factor ligand superfamily member 11
- Osteoclast-associated immunoglobulin-like receptor
- V-type proton ATPase subunit d 2
- Matrix metalloproteinase-9
- Tartrate-resistant acid phosphatase type 5
- Calcitonin receptor
- Protein c-Fos
Sequence:
MRLWTLGTSIFLRLWGTYVFPRSPSWLDFIQHLGVCCFVAFLSVSLFSAAFYWILPPVALLSSVWMITCVFLCCSKRARCFILLAVLSCGLREGRNALIAAGTGVVIFGHVENIFYNFRGLLDSMTCNLRAKSFSVHFPLLKRYTEAIQWIYGLATPLNLFDDLVSWNQTLVVSLFSPSHALEAHMNDTRGEVLGVLHHMVVTTELLTSVGQKLLALAGLLLILVSTGLFLKRFLGPCGWKYENVYITKQFVRFDEKERHQQRPCVLPLNKKERKKYVIVPSLQLTPKEKKTLGLFFLPVLTYLYMWVLFAAVDYLLYRLISSMNKQFQSLPGLEVHLKLRGEKQGTQGVVHDSAFNISMFEPSCIPKPRLSVSETWVPLSIILLTLIILGLLSSMLMQLKILVSVSFYPKVERERIEYLHAKLLEKRSKQPLREADGKPSLYFKKIHFWFPVLKMIRKKQTIPANEDDL
Protein: Translation initiation factor eIF2B subunit alpha (eIF2B GDP-GTP exchange factor subunit alpha) (P34604)
Organism: Caenorhabditis elegans
Function: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9USP0}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Translation initiation factor eIF2B subunit epsilon
- protein-synthesizing GTPase
- Translation initiation factor eIF2B subunit beta
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 2-alpha kinase gcn-2
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic peptide chain release factor subunit 1
Sequence:
MVQESIISSFRGKLENDPSKSTSLATVETLLEVLDRSRATTVAEFQNELNQVVAALEKTDYSSTSIRSAADLFTRFTSLAPAALLDQEDFSQVLDLYRQRARSFIKNVRGSRAKISKCARLFFTHHMNILTHSYSKVVLETILDAHKSGYHLHVWVTESQPDASGKLVFEELKKNGVPTTLVLDSCVGYVMERIQAVLVGAEGVMETGGIINKIGTVNVCIIAKSRHVPVYVCAETIKFVREFPLNQADIPQEFKYRTSVIERNNLELEHPDVDYTAPEFLTLIITDVGAMKPEAVGEELIKMYI
Protein: Profilin (Protein chickadee) (P25843)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. This profilin is required for intercellular cytoplasm transport during Drosophila oogenesis.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Adenylyl cyclase-associated protein
- Formin 3, isoform B
- Cofilin/actin-depolymerizing factor homolog
- IP04855p
- Protein diaphanous
- Dishevelled associated activator of morphogenesis, isoform D
- Protein cappuccino
- RE12101p
- Actin-related protein 3
- Actin-related protein 2
Sequence:
MSWQDYVDNQLLASQCVTKACIAGHDGNIWAQSSGFEVTKEELSKLISGFDQQDGLTSNGVTLAGQRYIYLSGTDRVVRAKLGRSGVHCMKTTQAVIVSIYEDPVQPQQAASVVEKLGDYLITCGY
Protein: UPF0145 protein YbjQ (P0A8C1)
Organism: Escherichia coli (strain K12)
Interaction partners:
- N-acetylmuramoyl-L-alanine amidase AmiD
- UPF0235 protein YggU
- Inner membrane protein YbhN
Sequence:
MQFSTTPTLEGQTIVEYCGVVTGEAILGANIFRDFFAGIRDIVGGRSGAYEKELRKAREIAFEELGSQARALGADAVVGIDIDYETVGQNGSMLMVSVSGTAVKTRR
Protein: Folate transporter 1, chloroplastic (AtFOLT1) (Q7XA87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates folate import into chloroplast.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:16055441}; Multi-pass membrane protein {ECO:0000269|PubMed:16055441}.
Interaction partners:
- AT5g24690/MXC17_8)
- tRNA-specific adenosine deaminase TAD3
- Histidinol-phosphate aminotransferase 2, chloroplastic
- ADP,ATP carrier protein 2, chloroplastic
- N-
- Protein QUA-QUINE STARCH
Sequence:
MAASWQWENATAGAVAGFATVAAMHSLDVVRTRFQVNDGRGSSLPTYKNTAHAVFTIARLEGLRGLYAGFFPAVIGSTVSWGLYFFFYGRAKQRYARGRDDEKLSPALHLASAAEAGALVCLCTNPIWLVKTRLQLQTPLHQTQPYSGLLDAFRTIVKEEGPRALYKGIVPGLVLVSHGAIQFTAYEELRKIIVDLKERRRKSESTDNLLNSADYAALGGSSKVAAVLLTYPFQVIRARLQQRPSTNGIPRYIDSLHVIRETARYEGLRGFYRGLTANLLKNVPASSITFIVYENVLKLLKQHPTTKD
Protein: Trafficking protein particle complex subunit 4 (Hematopoietic stem/progenitor cell protein 172) (Synbindin) (TRS23 homolog) (Q9Y296)
Organism: Homo sapiens (Human)
Function: Core component of the TRAPP complexes which has a function of guanine nucleotide exchange factor activity for Rab1 GTPase (Probable). Plays a role in vesicular transport from endoplasmic reticulum to Golgi and autophagy. May play a role in dendrite postsynaptic membrane trafficking (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9ES56}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ES56}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9ES56}. Vesicle {ECO:0000250|UniProtKB:Q9ES56}. Note=Associated with postsynaptic membranes and in intracellular cisterns and vesicles (Golgi). {ECO:0000250|UniProtKB:Q9ES56}.
Interaction partners:
- Trafficking protein particle complex subunit 6A
- Trafficking protein particle complex subunit 3
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit 9
- Trafficking protein particle complex subunit 10
Sequence:
MAIFSVYVVNKAGGLIYQLDSYAPRAEAEKTFSYPLDLLLKLHDERVLVAFGQRDGIRVGHAVLAINGMDVNGRYTADGKEVLEYLGNPANYPVSIRFGRPRLTSNEKLMLASMFHSLFAIGSQLSPEQGSSGIEMLETDTFKLHCYQTLTGIKFVVLADPRQAGIDSLLRKIYEIYSDFALKNPFYSLEMPIRCELFDQNLKLALEVAEKAGTFGPGS
Protein: Exostosin-like glycosyltransferase 3 (A0A0G2K6F4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648}.
Interaction partners:
Sequence:
MTGYTMLRNGGVGNGGQTCMLRWSNRIRLTWLSFTLFIILVFFPLIAHYYLTTLDEADEAGKRIFGPRAGNELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKVTRGCRLHNCFDYSRCPLTSGFPVFVYDSDQFAFGSYLDPLVKQAFQATVRANVYVTENAAIACLYVVLVGEIQEPAVLQPADLEKQLHSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVAQSTFYAAQYRAGFDLVVSPLVHAMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEARSFEEEMEGDPPADYDDRIIATLKAVQDSKLDQVLVEFTCKNQPKPSLPTEWALCGEREDRLELLKLSTFALIITPGDPSLLISSGCATRLFEALEVGAVPVVLGEQVQLPYHDMLQWNEAALVVPKPRVTEVHFLLRSLSDSDLLAMRRQGRFLWETYFSTADSIFNTVLAMIRTRIQIPAAPIREEVAAEIPHRSGKAAGTDPNMADNGDLDLGPVETEPPYASPKYLRNFTLTVTDCYRSWNSAPGPFHLFPHTPFDPVLPSEAKFLGSGTGFRPIGGGAGGSGKEFQAALGGNVQREQFTVVMLTYEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRTEKNSLNNRFLPWNEIETEAILSIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDIPHQSWLYNSNYSCELSMVLTGAAFFHKVRKQGRVSAPSLVKVSFCGKEHCLHTSLSASVALLCQK
Protein: Ubiquitin-like modifier-activating enzyme ATG7 (Autophagy-related protein 7) (G5EBK4)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU366022}. Preautophagosomal structure {ECO:0000256|RuleBase:RU366022}.
Interaction partners:
- Ubiquitin-like-conjugating enzyme ATG3
- Protein lgg-1
- Ubiquitin-like protein atg-12
- Autophagy-related protein 5
- Ubiquitin-like-conjugating enzyme ATG10
- Protein lgg-2
- Autophagy-related protein 9
- Autophagy-related protein 18
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Beclin homolog
Sequence:
MATFVPFVTCLDTGFWNEVNKKKLNDWKLDETPKCISSQLSLHQTEGFKCHLSLSYDSLSSLESTTGLSMSGTLLLYNTIESFKMVDKSDLIRSEAEKIWESITTRKWLQNPRLLSQFFIIAFADLKKFKYYYWTCVPALVYPSEIKQEITPLSSLGADHKILFDFYRKNNFPIFLYSKQSSKMLELSELENNTNPDEICVVVADPSPVAYSAGWMVRNVLAAVAHLHPTWKHCHIISLRSADSIGIKYTWTLPSAECSADGAQNAVPKAVGWERNANDKLQPISVDLSKEFDPKILMERSVDLNLSLIKWRLHPDIQLERYSQLKVLILGAGTLGCNIARCLIGWGVRHISFLDNSTVSYNNPVRQSLSEFEDARLGRGKAETAQAAIQRIFPSIQATAHRLTVPMPGHSIDEKDVPELEKDIAKLEQLVKDHDVVFLALDSREARWLPTVLASRHKKIAISVAIGFDTYVIIRHGIGSRSESVSDVSSSDSVPYSQLSCYFCSDVTAPGNSTFDRTLDQQCTVARPGTSMIASGIAVELLSSVLQYPDPLKTPASHDDNTTVLGAAPHQIRGFLGRFQQILPSVKRFDQCVACGDAIAAQFQQNGWKFVRDVMNSPGRLEEVTGLDELQNSVNAIDIDFEDDEDF
Protein: Aminoglycoside N(6')-acetyltransferase type 1 (EC 2.3.1.82) (AAC(6')-Ig) (Aminoglycoside resistance protein) (Q44057)
Organism: Acinetobacter haemolyticus
Function: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin, kanamycin, tobramycin and netilmicin.
Interaction partners:
Sequence:
MNIKPASEASLKDWLELRNKLWSDSEASHLQEMHQLLAEKYALQLLAYSDHQAIAMLEASIRFEYVNGTETSPVGFLEGIYVLPAHRRSGVATMLIRQAEVWAKQFSCTEFASDAALDNVISHAMHRSLGFQETEKVVYFSKKID
Protein: FI15955p1 (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q9VAN8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Clathrin light chain
Sequence:
MCEKVTARCTWPQLSGNGLDQLVATRLSDEDVFVKPDLDDVIDENRAVLFSMQSADPPPPCELRFQIPNRFKIAALTLICSAPKVELFIGPLQEYCETIYGTCVDDEDPEVAVRPYRYDMEIDRSGINDINLKMLTSASEICVYGALLQVAPNPNGITTQLPRPMDAQRIQELLQRGGTSPLKKEEQAEKFEQFMSLMKGYSPQAKDQTQETAPPSTDVAILKEHIDMRFEKLTLLVSKRLDNFEAQQTEKLNKIIALLEKEK
Protein: Heterogeneous nuclear ribonucleoprotein A/B (hnRNP A/B) (CArG-binding factor-A) (CBF-A) (Q99020)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. Binds to CArG box motifs, single-stranded and double-stranded DNA, and RNA. It may be that repression by CBF-A is a result of competitive binding of CBF, a putative positive factor, and CBF-A to the same or overlapping motifs around the CArG boxes.
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}.
Interaction partners:
- Y-box-binding protein 1
- Heterogeneous nuclear ribonucleoprotein Q
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein U
- Polypyrimidine tract-binding protein 1
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Serine/arginine-rich splicing factor 2
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein H2
- Heterogeneous nuclear ribonucleoprotein L
Sequence:
MSDAAEEQPMETTGATENGHEAAPEGEAPVEPSAAAAAPAASAGSGGGTTTAPSGNQNGAEGDQINASKNEEDAGKMFVGGLSWDTSKKDLKDYFTKFGEVVDCTIKMDPNTGRSRGFGFILFKDSSSVEKVLDQKEHRLDGRVIDPKKAMAMKKDPVKKIFVGGLNPEATEEKIREYFGQFGEIEAIELPIDPKLNKRRGFVFITFKEEDPVKKVLEKKFHTVSGSKCEIKVAQPKEVYQQQQYGSGGRGNRNRGNRGSGGGQGSTNYGKSQRRGGHQNNYKPY
Protein: Down syndrome cell adhesion molecule 1, isoform BN (A0A0B4K7I3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVPQSYTVNVMDESILRGNSAILKCHIPSFVADFIVVDSWVEDEERVIYPQEDIAESDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPIGSKAPAVPTGVLAFQQNVPIHSIFAMLCQAQAFPVPIYRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVLPQITPFATGSQPTHLGQYITYQCTLTEGDLPLNIRWTFNNQPLFNDDDQDILIAKMGRRSSVLTIESVADRHAGNYSCHGENAAGRATYSTQLRVIVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV