wanglab/gogpt-training-data huggingface dataset:
Protein: Envelope glycoprotein D (gD) (Q69091)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Envelope glycoprotein that binds to the potential host cell entry receptors TNFRSF14/HVEM, NECTIN1 and 3-O-sulfated heparan sulfate (By similarity). May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL.
Subcellular location: Virion membrane {ECO:0000250|UniProtKB:Q05059}; Single-pass type I membrane protein {ECO:0000255}. Host Golgi apparatus {ECO:0000269|PubMed:31921110}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. {ECO:0000269|PubMed:31921110}.
Interaction partners:
Sequence:
MGGAAARLGAVILFVVIVGLHGVRSKYALVDASLKMADPNRFRGKDLPVLDQLTDPPGVRRVYHIQAGLPDPFQPPSLPITVYYAVLERACRSVLLNAPSEAPQIVRGASEDVRKQPYNLTIAWFRMGGNCAIPITVMEYTECSYNKSLGACPIRTQPRWNYYDSFSAVSEDNLGFLMHAPAFETAGTYLRLVKINDWTEITQFILEHRAKGSCKYALPLRIPPSACLSPQAYQQGVTVDSIGMLPRFIPENQRTVAVYSLKIAGWHGPKAPYTSTLLPPELSETPNATQPELAPEDPEDSALLEDPVGTVAPQIPPNWHIPSIQDAATPYHPPATPNNMGLIAGAVGGSLLAALVICGIVYWMRRHTQKAPKRIRLPHIREDDQPSSHQPLFY
Protein: NGFI-A-binding protein 1 (EGR-1-binding protein 1) (Q61122)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Early growth response protein 1
- E3 SUMO-protein ligase EGR2
- Early growth response protein 3
Sequence:
MATALPRTLGELQLYRILQKANLLSYFDAFIQQGGDDVQQLCEAGEEEFLEIMALVGMASKPLHVRRLQKALRDWVTNPGLFNQPLTSLPVSSIPIYKLPEGSPTWLGISCNSYERSSSSREPHLKIPKCAATTCVQSLGQGKSEVGSLALQSVSDSRLWQGHHATESEHSLSPADLGSPASPKESSEALDAAAALSVAECVERMAPTLPKSDLSEVKELLKNNKKLAKMIGHIFEMSDEDPHKEEEIRKYSAIYGRFDSKRKDGKHLTLHELTVNEAAAQLCVKDNALLTRRDELFALARQVSREVTYKYTYRTTRLKCGERDELSPKRIKIEDGFPDFQESVPTLFQQARAKSEELAGLGSQQAEKGMAKQMELLCAQAGYERLQQERRLTAGLYRQSSGEQSPDGGLPSDSSDGQGERPLNLRIPSVQNRQPHHFVVDGELSRLYSSEAKSHSSESLGILKDYPHSAFTLEKKVIKTEPEDSR
Protein: Junctophilin-3 (JP-3) (Junctophilin type 3) (Q9ET77)
Organism: Mus musculus (Mouse)
Function: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH3 is brain-specific and appears to have an active role in certain neurons involved in motor coordination and memory.
Subcellular location: Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Note=Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane.
Interaction partners:
- Ryanodine receptor 1
- Ryanodine receptor 3
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Triadin
- Calsequestrin-2
- Junctophilin-1
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Aspartyl/asparaginyl beta-hydroxylase
- Junctophilin-2
- Junctophilin-4
Sequence:
MSSGGRFNFDDGGSYCGGWEDGKAHGHGVCTGPKGQGEYTGSWSHGFEVLGVYTWPSGNTYQGTWAQGKRHGIGLESKGKWVYKGEWTHGFKGRYGVRECTGNGAKYEGTWSNGLQDGYGTETYSDGGTYQGQWVGGMRQGYGVRQSVPYGMAAVIRSPLRTSINSLRSEHTNGAALHPDASPAVAGSPAVSRGGFVLVAHSDSEILKSKKKGLFRRSLLSGLKLRKSESKSSLASQRSKQSSFRSEAGMSTVSSTASDIHSTISLGEAEAELAVIEDDIDATTTETYVGEWKNDKRSGFGVSQRSDGLKYEGEWVSNRRHGYGCMTFPDGTKEEGKYKQNVLVSGKRKNLIPLRASKIREKVDRAVEAAERAATIAKQKAEIAASRTSHSRAKAEAALTAAQKAQEEARIARITAKEFSPSFQHRENGLEYQRPKHQMSCDDIEVLSTGTPLQQESPELYRKGTTPSDLTPDDSPLQSFPASPTSTPPPAPASRTKMAHFSRQVSVDEERSGDIQMLLEGRGGDYARNSWGEEKAGASRGIRSGALRSGQPTEDFRTRGSGHKQPGNPKPRERRTESPTTFSWTSHHRAGNPCSGGPKLLEPDEEQLSNYKLEMKPLLRMDACPQDTHPQRRRHSRGAGGDRGFGLQRLRSKSQNKENLRPASSAEPTVQKLESLRLGDRPEPRLLRWDLTFSPPQKSLPVALESDEETGDELKSSTGSAPILVVMVILLNIGVAILFINFFI
Protein: SD05726p (Q95R58)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSMTPPPDQKLDDDQKAERVSVIMRVNSSGAVSSSSQDENSSSSTSCCSSSSNTNTSTSSVPPTVEDDYPEANVWRNLKFKMNRKRAAEVALPPVQTPETPVAKLVAPPAPAECIKEEEIKPILTPIYVSPVASSASQLILLSTVAAQQSPTPVPKTPTMSEEKLTTRITAAQAAATRSRIYECSFPDCGKNYFKSSHLKAHQRVHTGERPFICKWENCDKRFSRSDELSRHKRTHTGEKKFQCSVCQKKFMRSDHLSKHVKRHNKDKANGVNRHVSLANNNTSASVAASLCDASLHLRAIAPAGSSASSSPISSASLQVYSAQDLLRLQQQASSFTFGGTLLQVQR
Protein: Pappalysin (A0A096MJG5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Insulin-like growth factor-binding protein 5
- Bone marrow proteoglycan
- Insulin-like growth factor-binding protein 4
- Stanniocalcin-2
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Insulin-like growth factor-binding protein 1
- Proteoglycan 3, pro eosinophil major basic protein 2
Sequence:
MGIHTISDQGNRDPRYFFSLKTDRARKVTTIDAHRSYLPGQWVHLAATYDGRLMKLYMNGAQVATSAEQVGGIFSPLTQKCKVLMLGGSALNHNFRGHIEHFSLWKVARTQREILSDMETRGLHTPLPQLLLQENWDNVKRTWSPMKDGHSPQVEFSNAHGFLLDTNLEPPLCGQTLCDNTEVISSYNQLPSFRQSKVVRYRVVNIYDDHHENPTVSWQQIDFQHQQLAEAFQHYNISWELDVLDINSSSLRHRLILANCDISKIGDEKCDPECNHTLTGHDGGDCRQLRYPAFMKKQQNGACDMDCNYERFNFDGGECCDPDITDVTKTCFDPDSPHRPSIKEPAHVVEESWLPHGHQKAERRKRTRAYLDVNELKNILKLDGSTHLNIFFANSSEEELAGVATWPWDKEALMHLGGIVLNPSFYGIPGHTHTMIHEIGHSLGLYHIFRGISEIQSCSDPCMETEPSFETGDLCNDTNPAPKHKFCGDPGPGNDTCGFHGFFDTPYNNFMSYADDDCTDSFTPNQVSRMHCYLDLVYQSWQPSRKPAPVALAPQIVGHTTDSVMLEWFPPIDGHFFERELGSACDLCLEGRILVQYAFNASSPMPCGPSGHWSPREAEGHPDVEQPCKSSVRTWSPNSAVNPHTVPPACPEPQGCYLELEFRYPLVPESLTIWVTFVSSDWDSSGAVNDIKLLTVSGKNISLGPQNVFCDIPLTIRLRDVSEEVYGIQIYTLDEHLEIDAAMLTSAVDSPLCLQCKPLQYKVLRDPPLLDDVGSLLHLNRRFMDMDLKLGNVYQYRIITISGNEESEPSPAAIYTHGSGYCGDGVIQKDQGEECDDMNKVNGDGCSLFCKQEVSFNCIDEPSRCYFHDGDGMCEEFEQKTSIKDCGVYTPQGFLDQWASNASVSHQDQQCPGWVVIGQPAASQVCRTKVIDLSEGISQHAWYPCTINYPYYQLPQTTFWLQTYFSQPMVAAAVIIHLVTDGTYYGDQKQETISVQLLDTKDQSHDLGLHVLSCRNNPLIIPVVHDLSQPFYHSQAVHVSFSSPLVAISGVALRSFDNFDPVTLSSCQRGETYSPAEQSCVHFACEATDCPELTVENASLNCSSSHRYHGAQCTVSCQTGYVLQIQRDDELIKSQVGPSVTVTCTEGKWNKQVACEPVDCGIPDHHHVYAASFSCPEGTTFGRRCSFQCRHPAQLKGNNSFLTCMEDGLWSFPEALCELMCLAPPPVPNADLQTARCRENKHKVGSLCKYKCKPGYHVPGSSRKSKKRAFKTQCTQDGSWQEGTCVPVTCDPPPPKFHGLYQCTNGFQFNSECRIKCEDSDASQGRGSNTIHCRKDGTWSGSFHVCREMQGQCSAPNQLNSHLKLQCPDGYAIGSECATSCLDHNSESIILPVNLTVRDIPHWMNPTRVQRIVCTAGLQWYPHPARIHCVKGCEPFMGDNYCDAINNRAFCNYDGGDCCTSTVKTKKVTPFPMSCDLQDDCACRDPEAQEHSRKDLRGYSHG
Protein: Importin subunit alpha (O76521)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Importin subunit beta
- Nuclear pore complex protein Nup153
- Regulator of chromosome condensation
- D-Importin 7/RanBP7
- E3 SUMO-protein ligase RanBP2
- Exportin-2
- Wing blister, isoform B
- Nuclear pore complex protein Nup50
- Exportin-1
- Ran GTPase-activating protein
Sequence:
MSASHKQRYKNAALDSTEMRRRREEVGIQLRKNKREQQLFKRRNVVLEPATSSTSAGVESNTDNEQQAADMHMADSSTGGQNEEAAGSGAQPSVINEEMIQMLFSGRENEQLEATQKFRKLLSRDPNPPIEEVIQKGIVPQFVTFLRNSANATLQFEAAWTLTNIASGTSQQTKVVIEAGAVPIFIDLLSSPHDDVQEQAVWALGNIAGDSPMCRDHLLGSGILEPLLHVLSNSDRITMIRNAVWTLSNLCRGKSPPADFAKISHGLPILARLLKYTDADVLSDTCWAIGYLSDGPNDKIQAVIDAGVCRRLVELLLHPQQNVSTAALRAVGNIVTGDDQQTQVILGYNALTCISHLLHSTAETIKKESCWTISNIAAGNREQIQALINANIFPQLMVIMQTAEFKTRKEAAWAITNATSSGTHEQIHYLVQVGCVPPMCDFLTVVDSDIVQVALNALENILKAGEKFQTRPNPYAITIEECGGLDKIEYLQAHENRDIYHKSFYIIEQYFGNEEEDSRVAPVAGTQQFEFDPDNMPSTGFNF
Protein: Serine rich endogenous peptide 13 (AtSCOOP13) (Phytocytokine SCOOP13) (Precursor of serine rich endogenous peptide phytocytokine 13) (Secreted transmembrane peptide 1) (Q8LE06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation. Promotes the expression of immune-related marker genes (e.g. WRKY30, WRKY33 and CYP81F2) in a MIK2-dependent manner. Inhibits root growth and regulates root meristems. Prevents general growth and development. Exhibits antibacterial effects against Pseudomonas syringae pv. tomato DC3000, Ralstonia solanacearum, Bacillus subtilis and Agrobacterium tumefaciens, thus being an antimicrobial peptide (AMP).
Subcellular location: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Note=The precursor of SCOOP13, PROSCOOP13, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP13 in the apoplasm. {ECO:0000269|PubMed:31001913}.
Interaction partners:
Sequence:
MATKASNLVVFLLSLLLLFLLISFQVGVADATRNKRQGQEQRVDYDYPRPPTAPIYLPPSKSRKGKGP
Protein: Uncharacterized protein (Q383P0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGSMSGKGFVSTRLLQAVPAGGAVPAPRSIPSFKPVPFKREKFLSIKTRTAETFFGTRDRLFRRSTAIVEQMSDMRRKENLSSSVSGSGGNVLNGCEGIYIGAPLTPQMTDEINAWNRNLQGLEGMQGFVLTDELVYEAVSRNIRMGAFPHALNWLEKAAREKRLPVPTLVLKDLRMFFDFVLSVLPASNATFSTAVDMLLEETASTMLPEVSTDGSRGGENEDEVTCGEVCENSPIRLASTSPFALHIFRELFAPVWGCLLRLGLLPTVASAQKEWDRLQGNKVSDGVLSGLIERIDFDGCAPSNRESSGTNVGKVPAARQAYMELLLSLAQCAAEAKEVYVLLHLQSTFCALFAEPRDEGRSHPSVSSDDSRLQRWRLRRNVWCNSDDGREYFHRFANDFLSSVYYGRQLYQSEVSLNNCVRHLSSTVPGVQGTEELGDMRNDGRDVGGADDEQRQPNNPDADEDGKSRLFTVEEAVENVLWEVMSHEASLFPDALAYAGLLLRRTVTDTTLPTSATNPRFSRAELEWMQLHSDMCRRSHGGEDVTAELLNLIRPGSTVTRGLALNATCLEDKQCLLGLVVETVITIAGVSRLAGPQRGDLIIKATTQLLLCMREVECQGGQRLMLPQYSVGCVMVSLVPLLRTTLESAFKSLKQTECCEGHIKLSFSRRDVLRIVRGLMPSILEQRVVFGNVYSGVITVLTLAEMWDEVMQVLKHLDQPHVSDGEDGDHQGISSLLVDQRVWAWLFRRARDAGQVEICLFLRSRREKLFY
Protein: Engulfment and cell motility protein 3 (Q8BYZ7)
Organism: Mus musculus (Mouse)
Function: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Dedicator of cytokinesis protein 1
- Rho-related GTP-binding protein RhoG
- Dedicator of cytokinesis protein 2
- Engulfment and cell motility protein 1
- Engulfment and cell motility protein 2
- Dedicator of cytokinesis protein 4
- PTB domain-containing engulfment adapter protein 1
- Adapter molecule crk
- Dedicator of cytokinesis protein 3
- Dedicator of cytokinesis protein 5
Sequence:
MAPPRNVVKIAVQMSDAIPQLIQLDQAKPLATVLKEVCDAWSLTHPEHYALQFADGHRKYITENNRLEIKNGSILCLSTAPDLKAQQLLGRLQNTSREGCCEVLRNLVLLASDMTFAQEVISRDGLQKLSTIIENGDDLGEMLALGLRAFLELMEHGVVSWETLSISFVRKVISYVNMNLMDASVQPLALRLLESVTLSSPALGQLVKSEVPLDRLLVHLQVMNHQLQTKAMALLTALLQGASPTERKEMLDHLWKKNLRQFIYKNIIHSATPMGDEMAHHLYVLQALTLGLLEPRMRTPLDPYSQEQRDQLQALRQAAFEPEGESLGTGLSADRRRSLCVREFRKLGFSNSNPAQDLERVPPGLLALDNMLYFSRHAPSAYSRFVLENSSREDKHECPFARSSIQLTALLCELLRVGEPCSETAQDFSPMFFSQDHSFHELFCVAIQLLNKTWKEMRATQEDFDKVMQVVREQLARTLALKPTSLELFRTKVNALTYGEVLRLRQTERLHQEGTLAPPILELREKLKPELMGLIRQQRLLRLCEGMLFRKISSRRRQDKLWFCCLSPNHKVLQYGDVEEGAKPPTLESLPEQLPVADIRALLMGKDCPHVREKGSGKQNKDLYELAFSISYDHGEEEAYLNFIAPSKRDFYLWTDGLSALLGSTMGSELTRLDLEQLLTMETKLRLLELENVPIPEQPPPVPPPPTNFNFCYDYSITEP
Protein: GPCR-type G protein COLD1 (Protein CHILLING TOLERANCE DIVERGENCE 1) (Q7X7S8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in chilling tolerance. Interacts with the G-protein alpha subunit GPA1 to activate the calcium channel for sensing low temperature and to accelerate G-protein GTPase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25728666}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25728666}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein alpha-1 subunit
Sequence:
MGWGAVVYGGGVVGASLVGLGWAGLWFLNRRLYKEYEERRALVQILFGLVFAFSCNLFQLVLFEILPVLSKHARFLNWHLDLFCLILLLVFVLPYYHCYLLLRNSGVRRERALLVAALFLLVFLYGFWRMGIHFPMPSPEKGFFTMPQLVSRIGVIGVSVMAVLSGFGAVNLPYSYLSLFIREIDEKDIKTLERQLMQSMETCIAKKKKIVLSKMEMERIQGSEEKLKARSFLKRIVGTVVRSVQEDQTEQDIKSLDAEVQALEELSKQLFLEIYELRQAKIAAAFSRTWRGHAQNLLGYALSVYCVYKMLKSLQSVVFKEAGSVDPVTMTITIFLRHFDIGIDVTLLSQYISLIFIGMLVVISVRGFLANVMKFFFAVSRVGSGSTTNVVLFLSEIMGMYFISSILLIRKSLANEYRVIITDVLGGDIQFDFYHRWFDAIFVASAFLSLLLISAQYTSRQTDKHPID
Protein: Vacuolar protein sorting-associated protein 74 (O14205)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Mediates the cis and medial Golgi localization of mannosyltransferases through direct binding of their cytosolic domains. Involved in vacuolar protein sorting (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate-binding and oligomerization participate in the recruitment onto Golgi membranes. {ECO:0000250}.
Interaction partners:
- Uncharacterized protein C19F5.03
- Uncharacterized protein C3C7.01c
- Putative acyl carrier protein, mitochondrial
Sequence:
MSGGLSRRRVAAASSDEERPEMRSVSHSKSHLEGYDDDHKIAFDPKDLEQGAEREKQPRLTLMEEVLLLGLKDKQGYLSFWNDSISYSLRGCILMELAFRGKLRMQKDVNRKRFPLADRVVELVDEKLTGEVLLDEAIKMIHTSELMSVTSWIDLMSGETWNVMKIGYQLRQVRERLAKGLVDKGILRNEKKNFLLFDMPTHPIADTSIKDSIKKRVVSVLTSRVIEIDNSPSFPEYLSFRCLRTVALACSSYAANVLENALDNLNYEDREKAFSRVDELLCDFSQWPFDLHASSSVGANLPELISEELSSVKEEQLLFIEVVAAVLQVFTHLDSLL
Protein: Gigantea (F1DRI2)
Organism: Brachypodium distachyon (Purple false brome) (Trachynia distachya)
Interaction partners:
Sequence:
FWPPPHDAQQKQVQILAYVEYFGQFTSDSEQFPEDVAQLIQSCYPAKEKRLVDEVLANFVLHHPEHGHAVVHPILSRIIDGTLSYDRHGSPFNSFISLFTQTSEKEYSEQ
Protein: Probable ATP-dependent RNA helicase DDX6 (EC 3.6.4.13) (ATP-dependent RNA helicase p54) (DEAD box protein 6) (Oncogene RCK) (P26196)
Organism: Homo sapiens (Human)
Function: Essential for the formation of P-bodies, cytosolic membrane-less ribonucleoprotein granules involved in RNA metabolism through the coordinated storage of mRNAs encoding regulatory functions. Plays a role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation. In the process of mRNA degradation, plays a role in mRNA decapping. Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:25995375, ECO:0000269|PubMed:26184334, ECO:0000269|PubMed:31422817, ECO:0000269|PubMed:32354837}. Cytoplasm {ECO:0000269|PubMed:26184334, ECO:0000269|PubMed:28216671}. Nucleus {ECO:0000269|PubMed:26184334, ECO:0000269|PubMed:28216671}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:P54823}. Note=Imported in the nucleus via interaction with EIF4ENIF1/4E-T via a piggy-back mechanism (PubMed:28216671). Upon cellular stress, relocalizes to stress granules (PubMed:26184334). {ECO:0000269|PubMed:26184334, ECO:0000269|PubMed:28216671}.
Interaction partners:
- m7GpppN-mRNA hydrolase
- mRNA-decapping enzyme 1A
- Enhancer of mRNA-decapping protein 3
- Protein LSM14 homolog A
- Protein argonaute-2
- Enhancer of mRNA-decapping protein 4
- CCR4-NOT transcription complex subunit 1
- Protein PAT1 homolog 1
- Eukaryotic translation initiation factor 4E transporter
- Protein argonaute-1
Sequence:
MSTARTENPVIMGLSSQNGQLRGPVKPTGGPGGGGTQTQQQMNQLKNTNTINNGTQQQAQSMTTTIKPGDDWKKTLKLPPKDLRIKTSDVTSTKGNEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQVSQICIQVSKHMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTLKGVTQYYAYVTERQKVHCLNTLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPIPSNIDKSLYVAEYHSEPVEDEKP
Protein: C-1-tetrahydrofolate synthase, mitochondrial (C1-THF synthase) [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9); Formyltetrahydrofolate synthetase (EC 6.3.4.3)] (O43007)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Bifunctional purine biosynthesis protein ade10
- Phosphoribosylglycinamide formyltransferase
- Methylenetetrahydrofolate dehydrogenase [NAD
- Probable serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Probable 5-formyltetrahydrofolate cyclo-ligase
- Probable thymidylate synthase
- Putative methionyl-tRNA formyltransferase
- Dihydrofolate reductase
- Methylenetetrahydrofolate reductase 1
Sequence:
MNVMVSFNQLRNYFLESNSLRPSKWLFQSYGTSSSANILNGKLLARKLQRSVAEEVQALKAKDRNFKPALAIVQVGKREDSNVYVRMKEKAARLVGIDFKYCPFPETIQMPALLHELKKLNDDHTVHGVLVQLPLPKHLNERTVTESITPPKDVDGFGAFNIGLLAKNDATPIHYPCTPKGIMELLKDNKISVAGLNAVVLGRSDIVGNPISYLLRKDNATVTVCHSKTKDLIQHISNADLVIAALGKPEFVRGEWLKPGSVVVDVGINAVQRNGKRVLVGDVHFESASKVASSITPVPGGVGPMTVAMLMENIVNAAKIARTENIYRKIDLNPLELKKPVPSDIEIANSQEPKLISNLAKEMGIYDTELENYGNYKAKVNLAVYERLKHRKDGNYVVVSGITPTPFGEGKSTVVAGLVQAMGHLGKLGIACVRQPSQGPTFGVKGGAAGGGYAQFIPMDDFNLHMTGDIHAVTAANNLLVAALETRMFHENTQSDAALIKRLIPVKNGRRVIPRGLIGRWNRICASHNMDPEDVNNASPELLKEFVRLNVDPDTIECNRVLDVNDRFLRSIEVGKASTEKGHVRKTSFDISVASECMSILALSCDLNDMHSRLSRMVIANDKYGNAITAGDLGVSGALTVLLKDAIKPNLMQTLEGTPAFVHAGPFANISIGASSIIADKIALKLAGTESFDRPEDAGYVVTEAGFASDMGMEKFFNIKCRYSKLVPNTVVLVTTVKALKLHGGGPKLKPGAPIPEEYLVENLDLVKNGCSNMVKHIQNCHKFNIPVVVAINSYKTDSSKEHEIIREAALQAGAVDAVPSDHWAQGGKGAIELAKSVMTACDQSSNSKFRLLYDSETSIEDKVNVIAKEMYGANGVEFSSLAKERINTFIKQGFGNLPICMAKTQYSLSHNPEFRNVPKNFTVPIRDMRLNAGAGFIYPLAAEIQTIPGLPTAPAYLNIDICENGEIVGLS
Protein: Phosducin-like protein 2 (Viral IAP-associated factor 1 homolog) (Q12017)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for cell growth. Inhibits early G-protein signaling events following pheromone stimulation. Inhibits the folding activity of the chaperonin-containing T-complex (CCT) CCT2 which leads to inhibition of cytoskeletal actin folding. Plays a role in cell cycle progression in G1/S phase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Phosducin-like protein 1
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit zeta
- Mitochondrial chaperone TCM62
Sequence:
MQNEPMFQVQVDESEDSEWNDILRAKGVIPERAPSPTAKLEEALEEAIAKQHENRLEDKDLSDLEELEDDEDEDFLEAYKIKRLNEIRKLQERSKFGEVFHINKPEYNKEVTLASQGKKYEGAQTNDNGEEDDGGVYVFVHLSLQSKLQSRILSHLFQSAACKFREIKFVEIPANRAIENYPESNCPTLIVYYRGEVIKNMITLLELGGNNSKMEDFEDFMVKVGAVAEGDNRLIMNRDDEESREERKLHYGEKKSIRSGIRGKFNVGIGGNDDGNINDDDDGFFD
Protein: Double-stranded RNA-binding protein Staufen homolog 1 isoform X2 (Staufen double-stranded RNA-binding protein 1) (F1Q5V4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSQLQFQAPGNPAPSSAPLQLAPPQPGFSIPCGTAPLPSESASHPLRNSALPSASATPFCNPTVSNMANPKEKTPMCLVNELARYNKIQPEYKLLSEEGPAHSKIFSVRLTLGDQHWDAEGTSIKKAQHSAASSALAQTTLPKPSHRSPRHPDNVTHTVELNALCMKLGKKPIYKPIDAYQGMRPAFNYNIRAPSPYARSMQHYYYPFPPVGPVLYHMELSIGGQQFHGKGRTRQAAKHDAAAKAIKYLQKEPILQQITEMTDEPAQENLNKSEISQVFEIALKRNMPVDFEVLKEAGAPHMKSFVVRVVVGEFAGEGEGKSKKIAKKQAAIAVLEELRRLPQLPATDKIPLRIKKKSKSIIKLQTSPEYGQGMNPISRLAQIQQAKKEKEPEYTLVTERGLPRRREFVMQVSVAGQNAEGMGPSKKVAKRNAAEKMLELLGFKVPQPQPPKPALKTDEKPPAKKLGDGRKVTFFEPGSMEKAGLVVSKEEDFRLPFLSHQQLPAGILPMVPEVAQAVGANQGPHAKDYGRTAAPNPANATVTAMIANELLYAGTSPTAEGILKTNNSLAHRPQGPLTRPSEQLSYLANVQGLQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILKLLSELDQQSNERTANGPMSGCTKQDLEGDALLKPANSSTMGKTLDGTA
Protein: phosphorylase kinase (EC 2.7.11.19) (Q961E7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAKDEEDDLLPDKDAAKGFYAKYEPKEILGRGISSTVRRCIEKETGKEFAAKIIDLGATTESGETNPYHMLEATRQEISILRQVMGHPYIIDLQDVFESDAFVFLVFELCPKGELFDYLTSVVTLSEKKTRTIMRQIFEGVEYIHAKSIVHRDLKPENILLDENHNVKITDFGFAKQLQEGEKLTNLCGTPGYLAPETLKCNMFEGSPGYSQEVDIWACGVIMFTLLVGCPPFWHRKQMVMLRNIMEGKYSFTSPEWADISEDPKDLIRKCLVVDPSQRITVKEVLRHPFFNQMLFEQNIDGLKRSLSTKSRRMSRITEIALLRKQSRFNARKKFQFAILVIRAIIRIRRLRFTAEPLHVEEAIRDPYRVKVLRKVIDGCAFRVYGHWVKKGEGQNRAALFENTPRTELHALYINNLSR
Protein: ATP synthase F1 complex assembly factor (At2g34050/T14G11.17) (Expressed protein) (O22958)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- AT5g40660/MNF13_180
Sequence:
MRRIVGSISSLAKDKLSSSSYSSSRQIFTARSSSWQRDASSKLSEASLPGNHIKWASLGSVRNSRFASGFTPLQQKPLDSIMDLARAKTKSPEELTSIWDDYHLGRGHIGLTMKAQLYRLLEQRASECRYFVIPLWRGNGYITMFAQVEAPHMIFTGLEDYKARGTQAAPYLTTTFYTELSETKDLVFIRGDVVFTSKLTDEEAKWIMETAQSFYLNDSRYKLLERFNKHTHDFEFKDVLQALDMPLL
Protein: F-box only protein 3 (Q9DC63)
Organism: Mus musculus (Mouse)
Function: Substrate recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, SCF(FBXO3), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome (By similarity). In the presence of PML, HIPK2 ubiquitination still occurs, but degradation is prevented (By similarity). PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation (By similarity). The SCF(FBXO3) also acts as a regulator of inflammation by mediating ubiquitination and degradation of FBXL2: specifically recognizes FBXL2 phosphorylated at 'Thr-404' and promotes its ubiquitination.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UK99}. Note=Colocalizes with PML at the peripheries of nuclear bodies. {ECO:0000250|UniProtKB:Q9UK99}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- F-box/LRR-repeat protein 2
Sequence:
MAAVEAETGLLTLESLPTDPLLLILSFVDYRDLINCCYVSRRLSQLSTHDPLWRRHCKKYWLISEEEKAGKSQCWRSLFIETYSDVGRYIDHYAAIKKAWRDLKKYLEPRCPRMVLSLKEGAREEDLDAVEAQIGCKLPDDYRCSYRIHNGQKLVVPGLLGSMALSNHYRSEDLLDVDTAAGGFQQRQGLKYCLPLTFCIHTGLSQYIAVEAAEGRNKNEVFYQCPDQMARNPAAIDMFIIGATFTDWFTSYVNNVVSGGFPIIRDQIFRYIHDPECVATTGDITVSVSTSFLPELSSVHPPHYFFTYRIRIEMSRDALPEKACQLDSRYWRITNAKGDVEEVQGPGVVGEFPIISPGRIYEYTSCTTFSTTSGYMEGYYTFHFLYFKDKVFNVAIPRFHMACPTFRVSIARLEMGPDEYEEMEEEAEEEEEEENDDSADMDESDESDADENESDEGEGEARRRRVFDVPIRRRRCSRLF
Protein: Calcium-binding protein 5 (CaBP5) (Q9NP86)
Organism: Homo sapiens (Human)
Function: Inhibits calcium-dependent inactivation of L-type calcium channel and shifts voltage dependence of activation to more depolarized membrane potentials (By similarity). Involved in the transmission of light signals (By similarity). May positively regulate neurotransmitter vesicle endocytosis and exocytosis in a salt-dependent manner (By similarity). May play a role in the extension and network organization of neurites (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19338761}.
Interaction partners:
Sequence:
MQFPMGPACIFLRKGIAEKQRERPLGQDEIEELREAFLEFDKDRDGFISCKDLGNLMRTMGYMPTEMELIELGQQIRMNLGGRVDFDDFVELMTPKLLAETAGMIGVQEMRDAFKEFDTNGDGEITLVELQQAMQRLLGERLTPREISEVVREADVNGDGTVDFEEFVKMMSR
Protein: Acetyltransferase, GNAT family (Q50708)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTADTEPVTIGALTRADAQRCAELEAQLFVGDDPWPPAAFNRELASPHNHYVGARSGGTLVGYAGISRLGRTPPFEYEVHTIGVDPAYQGRGIGRRLLRELLDFARGGVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGADAYTMRRDSGDPS