wanglab/gogpt-training-data huggingface dataset:
Protein: Polyadenylate-binding protein RBP47B (Poly(A)-binding protein RBP47B) (RNA-binding protein 47B) (AtRBP47B) (Q0WW84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein binding the poly(A) tail of mRNA and probably involved in some steps of pre-mRNA maturation.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasmic granule {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 4E-1
- AT3g17750/MIG5_4
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 2
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 1, mitochondrial
- THO complex subunit 4B
- Ribonuclease TUDOR 2
- Ribonuclease TUDOR 1
- mRNA-decapping enzyme-like protein
- FCS-Like Zinc finger 13
Sequence:
MQTTNGSDSTLATSGATPPNQQTPPPPQQWQQQQQQQQQWMAAMQYPPAAAMMMMQQQQMLMYPHQYVPYNQGPYQQHHPQLHQYGSYQQHQHQQHKAIDRGSGDDVKTLWVGDLLHWMDETYLHSCFSHTGEVSSVKVIRNKLTSQSEGYGFVEFLSRAAAEEVLQNYSGSVMPNSDQPFRINWASFSTGEKRAVENGPDLSVFVGDLSPDVTDVLLHETFSDRYPSVKSAKVVIDSNTGRSKGYGFVRFGDENERSRALTEMNGAYCSNRQMRVGIATPKRAIANQQQHSSQAVILAGGHGSNGSMGYGSQSDGESTNATIFVGGIDPDVIDEDLRQPFSQFGEVVSVKIPVGKGCGFVQFADRKSAEDAIESLNGTVIGKNTVRLSWGRSPNKQWRGDSGQQWNGGYSRGHGYNNGGGYANHHDSNNYHGEN
Protein: Homeotic protein spalt-major (P39770)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the establishment of the posterior-most head and the anterior-most tail segments of the embryo. Probably function as a transcriptional regulator. Could repress the transcription of the tsh gene.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- FI23031p1
- Homeobox protein homothorax
- Chromatin assembly factor 1 p55 subunit
- Optomotor-blind protein
- Homeobox protein abdominal-A
Sequence:
MKNHLSNVLCAMRSDFKDNHQETINKMIQFGTVKYGIVKQLKDRARSADKDIGSDQEENGGCSPLTTATTTASPSRSPEPEEEQPEEQSTSEQSIPEQSTPDHQLENDIKSEAKSEIEPVEDNNNRVAMTKPSSEEREPNASGSMPSSPVAEASAEEAATERTPEKEKEKDVEVDVEKPDEAPSSAVPSTEVTLPGGAGAPVTLEAIQNMQMAIAQFAAKTIANGSNGADNEAAMKQLAFLQQTLFNLQQQQLFQIQLIQQLQSQLALNQAKQEEDTEEDADQEQDQEQETDTYEEEERIADMELRQKAEARMAEAKARQHLINAGVPLRESSGSPAESLKRRREHDHESQPNRRPSLDNTHKADTAQDALAKLKEMENTPLPFGSDLASSIITNHDDLPEPNSLDLLQKRAQEVLDSASQGILANSMADDFAFGEKSGEGKGRNEPFFKHRCRYCGKVFGSDSALQIHIRSHTGERPFKCNVCGSRFTTKGNLKVHFQRHAQKFPHVPMNATPIPEHMDKFHPPLLDQMSPTDSSPNHSPAPPPLGSAPASFPPAFPGLQNLYRPPMEILKSLGAAAPHQYFPQELPTDLRKPSPQLDEDEPQVKNEPVEEKDQREEHEQEMAECSEPEPEPLPLEVRIKEERVEEQEQVKQEDHRIEPRRTPSPSSEHRSPHHHRHSHMGYPPVVQPIQPAALMHPQSSPGSQSHLDHLPTPGQLPPREDFFAERFPLNFTTAKMLSPEHHSPVRSPAGGALPPGVPPPPHHHPHHMARSPFFNPIKHEMAALLPRPHSNDNSWENFIEVSNTCETMKLKELMKNKKISDPNQCVVCDRVLSCKSALQMHYRTHTGERPFKCRICGRAFTTKGNLKTHMAVHKIRPPMRNFHQCPVCHKKYSNALVLQQHIRLHTGEPTDLTPEQIQAAEIRDPPPSMMPGHFMNPFAAAAFHFGALPGGPGGPPGPNHGAHNGALGSESSQGDMDDNMDCGEDYDDDVSSEHLSNSNLEQEGDRSRSGDDFKSLLFEQKLRIDATGVVNTNPVRPRSSASSHGHSVGSTSAPTSPSVHASSQVIKRSSSPARSEASQGALDLTPRAAPTSSSSSRSPLPKEKPVSPPSLPRSPSGSSHASANILTSPLPPTVGIDCLPPGLQHHLQQQHQHLMQQQAAVAAAAAAQHHHHQQMAALHQHQEQLRREAAEAQQKAAAAAAAAAAAAAAQRQTPPQARDQRQEGGPGAGPPPNPLMGARPPFGMFPNLPLFPPATTQNMCNAMNQIAQSVMPAAPFNPLALSGVRGSTTCGICYKTFPCHSALEIHYRSHTKERPFKCSICDRGFTTKGNLKQHMLTHKIRDMEQETFRNRAVKYMSEWNEDRE
Protein: GATA-binding protein 2b (Gata2b protein) (Q6DG89)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDAPAEPRWMMHAHHSAMMSTSDSVSPHAGLGHHSSGYMEPGAPLLQPDEVDVFLSHLDSQGNPYYHTHGSRARMSYSQTHARLTGGSMCRPHLINTHGLPLLDNSKSTFSTAQHHGSWTVSHLGKAVLHSAGAESSNGLYAGTGAPASGPMPCLSMTQHCSAQLYCLPPTPPKDVSPDPACAAVRDAGKYHLHLVDGMKMECSSPIRSNPHLAQTTTPIPSYPDYSVAGAHEYPASVFHSRNLLGNMTTKCKSKNRAFSGRECVNCGATSTPLWRRDGTGHYLCNACGLYHKMNGQNRPLIRPKRRLSASRRAGTCCANCQTGTTTLWRRNANGEPVCNACGLYYKLHNVNRPLTMKKDGIQTRNRKMSGKSKKRRGEHIHQFDSCVHDKPSSFSHMANIHHPFNMTPQIQLHPAFSHSSLVTAIG
Protein: Protein argonaute 3 (Q9SHF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in RNA-mediated post-transcriptional gene silencing (PTGS). Main component of the RNA-induced silencing complex (RISC) that binds to a short guide RNA such as a microRNA (miRNA) or small interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide for slicer-directed cleavage of homologous mRNAs to repress gene expression (By similarity).
Interaction partners:
- Endoribonuclease Dicer homolog 3
- Endoribonuclease Dicer homolog 2
- Dicer-like protein 4
- Endoribonuclease Dicer homolog 1
- RNA-dependent RNA polymerase 6
- RNA-dependent RNA polymerase 2
- DNA-directed RNA polymerase IV subunit 1
- Protein DCL homolog, chloroplastic
- Probable RNA-dependent RNA polymerase 5
- Probable RNA-dependent RNA polymerase 3
Sequence:
MDRGGYRGGRGDGRGRGGGGDRGRGYSGRGDGRGRGGDGDRGYSGRGDGHGRGGGGDRGRGYSGRGDGRGRGGGGDRGRGYSGRGDGHGRGGGGDRGRGYSGRGRGFVQDRDGGWVNPGQSSGGHVRGRGTQLQQPPPQEVPPSSSQAQVSQGVAPGDVGQGGVGDVGRDGVGDVGRDGVGDVGQGGVGDVGQVGVGDVGQGGVGDVGQGGVGDVGRDGVGDVGRDGVGDVGRGGVGDRGQSQSGLSSGHFGRGTQLQQPQPQAVSQSSSQGQVSQSFATGGVGLGAWARKPQLFSDSTVLPSSSSSNVVASHTASGSQVMTPKPSSSDKKEPVKRPDKGGNIKVKGVINLSVNHFRVSFSTESVIRHYDVDIKGENSSKKISRFELAMVKEKLFKDNNDFPNAMTAYDGQKNIFSAVELPTGSFKVDFSETEEIMRGRSYTFIIKQVKELKLLDLQAYIDGRSTFIPRDVLQGMDVVMKEHPSKRMITVGKRFFSTRLEIDFGYGVGAAKGFHHTLKPTVQGLSLCLNSSLLAFRKAISVIEYLKLYFGWRNIRQFKNCRPDDVVQELIGLKVTVDHRKTKQKFIIMGLSKDDTKDIKFDFIDHAGNQPPRKISIVEYFKEKYGRDIDHKDIPCLNLGKKGRENFVPMEFCNLVEGQIFPKEKLYRDSAAWLKELSLVTPQQRLENINKMIKSSDGPRGGDIIGNFGLRVDPNMTTVEGRVLEAPTLKLTDRRGNPIHEKLMSESNQWNLTTKGVTKGSIIKHWAVLDFTASESLKKKMPGYFVNKLIERCKGLGMQMEAPIVCKTSSMETLYDGNALEELLRSVIDEASHNHGGACPTLVLCAMTGKHDGYKTLKWIAETKLGLVTQCFLTISAIKGETVSDQYLANLALKINAKVGGTNVELVDNIFSFFKKEDKVMFIGADVNHPAAHDNMSPSIVAVVGTLNWPEANRYAARVKAQSHRKEEIQGFGETCWELIEAHSQAPEKRPNKIVIFRDGVSDGQFDMVLNVELQNVKDVFAKVGYNPQITVIVAQKRHQTRFFPATTSKDGRAKGNVPSGTVVDTTIIHPFEYDFYLCSQHGAIGTSKPTHYYVLSDEIGFNSNQIQKLIFDLCFTFTRCTKPVALVPPVSYADKAASRGRVYYEASLMKKNSKQSRGASSSSASVASSSSSVTMEDKEIFKVHAGIENFMFFV
Protein: Hydroxyproline-rich glycoprotein family protein (Putative proline-rich protein) (Q8VYM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, cytoplasmic
- Methionine-tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Glutamyl-tRNA
- Proline--tRNA ligase, chloroplastic/mitochondrial
- Proline--tRNA ligase, cytoplasmic
- proline--tRNA ligase
- Pre-mRNA cleavage factor Im 25 kDa subunit 2
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MAGKQIGGDGGLPANLAGMTKSQLYDIMSQMKTLIDQNHQQAREILIRNPLLTKALFQAQIMLGMVQPPQVTPKVEPQAVQQPQQSHQSIPPKPNVQAHMSSFQGGGSVHEPANTMQPQAPIRKHPTPQPMPMPPPPPSVSANSAQSQPRFSHPQRQGHLNPAVTSMSHPQSSQVQNAPPPASHHPTSQQPPFHHLDIPASSTQLQQQPMHSGGGPHVAQQQSRPYHHQYGQAQTGPNTGFQHHGAPTQHLSQPMYHSGNRPPASGGPQFPQGQPHLPSQPTYQGGGQYRGDYNNNQLAGLMAQDRGPSWMAGQSESSNITHLPGLGPVPPPSQVGPGGGPPPRPAPISAEMEKALLQQVMSLTPEQINLLPPEQRNQVLQLQQILRQ
Protein: Protein lin-7 homolog B (Lin-7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2) (Q9Z252)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction {ECO:0000269|PubMed:15494546}. Postsynaptic density membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction, tight junction {ECO:0000269|PubMed:15494546}. Note=Mainly basolateral in renal epithelial cells (By similarity). {ECO:0000250}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Amyloid-beta A4 precursor protein-binding family A member 1
- Rhotekin
- Peripheral plasma membrane protein CASK
- PTPRF interacting protein alpha 2
- PRKCA-binding protein
- Guanine nucleotide-binding protein G
- Liprin-alpha-3
- Disks large homolog 1
- Peripheral-type benzodiazepine receptor-associated protein 1
Sequence:
MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDITGSAEVRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHHSYSSLESRG
Protein: Small membrane A-kinase anchor protein (Small membrane AKAP) (smAKAP) (Q9BSF0)
Organism: Homo sapiens (Human)
Function: Binds to type I regulatory subunits of protein kinase A (PKA-RI) and may anchor/target them to the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23115245}. Note=The GFP-tagged protein has been detected at the plasma membrane, enriched in filopodia and cell-cell junctions. {ECO:0000269|PubMed:23115245}.
Interaction partners:
- cAMP-dependent protein kinase type I-alpha regulatory subunit
Sequence:
MGCMKSKQTFPFPTIYEGEKQHESEEPFMPEERCLPRMASPVNVKEEVKEPPGTNTVILEYAHRLSQDILCDALQQWACNNIKYHDIPYIESEGP
Protein: Mitochondrial 2-methylisocitrate lyase ICL2 (Methylisocitrate lyase) (EC 4.1.3.30) (Q12031)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11092862, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Malate synthase 1
- Malate synthase 2
- Aconitate hydratase, mitochondrial
- Alanine--glyoxylate aminotransferase 1
- Citrate synthase 3, mitochondrial
- Glyoxylate reductase 1
- Isocitrate lyase
- Citrate synthase, mitochondrial
- Citrate synthase, peroxisomal
- Acetyl-coenzyme A synthetase 1
Sequence:
MITMINNKTFNRKTTGTLKKLVLSSDKSLRRSFNGASSTKDFVFSESSKVEEWWESARFKNISRPYSATDVVKHRGSLPANTSIYPSSYQARKLFNLLEENFKNGTPLHTLGVIDPVQMSQLARCRNIKVAYISGWACSSTLVGSTNEVSPDFGDYPYDTVPNQVERIFKAQQLHDRKAFLEASIKGSTPVDYLKPIIADADMGHGGPTTVMKVAKLFAEKGAAGIHLEDQMVGGKRCGHLSGAVLVPTATHLMRLISTRFQWDIMGTENLVIARTDSCNGKLLSSSSDPRDHEFIRGIIRDNVVPWSEKLIEMEDKKIPNSAIADMEKEWYHENELFTFEEALEKQFTASEFESYKEKKEDLMVNKLGRAYLSLREMKLLAQEVTPLKKIIFDWDAPRTKEGYYMFNGCIEAAIRRSLVFAPYSDMIWLETKTPDLEQARSFSRKIHKQLPATKLVYNLSPSFNWSAHGFDDKALKSFVWDLAKEGFTLQLVSLAGLHSDGVSFWELANSFQSDGMKAYVEKVQKREKETNCDIMTHQLWSGAEYVDSLMKVVQNGASSQTLSTSGESFTETQF
Protein: Regulating synaptic membrane exocytosis protein 1 (Rab-3-interacting molecule 1) (RIM 1) (Rab-3-interacting protein 2) (Q86UR5)
Organism: Homo sapiens (Human)
Function: Rab effector involved in exocytosis (By similarity). May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity (By similarity). Plays a role in dendrite formation by melanocytes.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Presynaptic cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-3A
- Protein unc-13 homolog B
- Protein unc-13 homolog A
- Peripheral-type benzodiazepine receptor-associated protein 1
- RIMS-binding protein 2
- ERC protein 2
- ELKS/Rab6-interacting/CAST family member 1
- Synaptosomal-associated protein 25
- Syntaxin-binding protein 1
- Syntaxin-1A
Sequence:
MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGSGPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASSQDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPEGKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELKAQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGKKRQMSVSSSEEEGVSTPEYTSCEDVELESESVSEKGDLDYYWLDPATWHSRETSPISSHPVTWQPSKEGDRLIGRVILNKRTTMPKDSGALLGLKVVGGKMTDLGRLGAFITKVKKGSLADVVGHLRAGDEVLEWNGKPLPGATNEEVYNIILESKSEPQVEIIVSRPIGDIPRIPESSHPPLESSSSSFESQKMERPSISVISPTSPGALKDAPQVLPGQLSVKLWYDKVGHQLIVNVLQATDLPARVDGRPRNPYVKMYFLPDRSDKSKRRTKTVKKILEPKWNQTFVYSHVHRRDFRERMLEITVWDQPRVQEEESEFLGEILIELETALLDDEPHWYKLQTHDESSLPLPQPSPFMPRRHIHGESSSKKLQRSQRISDSDISDYEVDDGIGVVPPVGYRSSARESKSTTLTVPEQQRTTHHRSRSVSPHRGNDQGKPRSRLPNVPLQRSLDEIHPTRRSRSPTRHHDASRSPVDHRTRDVDSQYLSEQDSELLMLPRAKRGRSAECLHTTRHLVRHYKTLPPKMPLLQSSSHWNIYSSILPAHTKTKSVTRQDISLHHECFNSTVLRFTDEILVSELQPFLDRARSASTNCLRPDTSLHSPERERGRWSPSLDRRRPPSPRIQIQHASPENDRHSRKSERSSIQKQTRKGTASDAERVLPTCLSRRGHAAPRATDQPVIRGKHPARSRSSEHSSIRTLCSMHHLVPGGSAPPSPLLTRMHRQRSPTQSPPADTSFSSRRGRQLPQVPVRSGSIEQASLVVEERTRQMKMKVHRFKQTTGSGSSQELDREQYSKYNIHKDQYRSCDNVSAKSSDSDVSDVSAISRTSSASRLSSTSFMSEQSERPRGRISSFTPKMQGRRMGTSGRSIMKSTSVSGEMYTLEHNDGSQSDTAVGTVGAGGKKRRSSLSAKVVAIVSRRSRSTSQLSQTESGHKKLKSTIQRSTETGMAAEMRKMVRQPSRESTDGSINSYSSEGNLIFPGVRLGADSQFSDFLDGLGPAQLVGRQTLATPAMGDIQIGMEDKKGQLEVEVIRARSLTQKPGSKSTPAPYVKVYLLENGACIAKKKTRIARKTLDPLYQQSLVFDESPQGKVLQVIVWGDYGRMDHKCFMGVAQILLEELDLSSMVIGWYKLFPPSSLVDPTLTPLTRRASQSSLESSTGPPCIRS
Protein: Glycogen accumulation regulator GarA (P9WJA9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in regulation of glutamate metabolism. Acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB.
Interaction partners:
- Multifunctional 2-oxoglutarate metabolism enzyme
- Serine/threonine-protein kinase PknB
- Serine/threonine-protein kinase PknG
- Serine/threonine-protein kinase PknA
- NAD-specific glutamate dehydrogenase
- Uncharacterized HTH-type transcriptional regulator Rv1828
- Serine/threonine-protein kinase PknF
- Serine/threonine-protein kinase PknE
- Serine/threonine-protein kinase PknD
- Serine/threonine-protein kinase PknH
Sequence:
MTDMNPDIEKDQTSDEVTVETTSVFRADFLSELDAPAQAGTESAVSGVEGLPPGSALLVVKRGPNAGSRFLLDQAITSAGRHPDSDIFLDDVTVSRRHAEFRLENNEFNVVDVGSLNGTYVNREPVDSAVLANGDEVQIGKFRLVFLTGPKQGEDDGSTGGP
Protein: Torsin 1A interacting protein 1 (H0YDU3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
EVRESAYYLRSRQRRQPRPQETEEMKTRRTTRLQQQHSEQPPLQPSPVMTRRGLRDSHSSEEDEASSQTDLSQTISKKTVRSIQEAPVSEDLVIRLRRPPLRYPRYGETEEDDQDSSHSSVTTVKARSRDSDESGDKTTRSSSQYIESFWQSSQSQNFTAHDKQPSVLSSGYQKTPQEWAPQTARIRTRMQND
Protein: Small ribosomal subunit protein RACK1 (D6R9Z1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPLHSSLGDRARLHLKKKKSYQDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCA
Protein: RNA cytidine acetyltransferase (EC 2.3.1.-) (18S rRNA cytosine acetyltransferase) (Q582B4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|HAMAP-Rule:MF_03211}.
Interaction partners:
- CCAAT-binding factor domain-containing protein
- Uncharacterized protein
- Periodic tryptophan protein 2, putative
- Nucleolar RNA binding protein, putative
- KRR1 small subunit processome component
- U3 small nuclear ribonucleoprotein
- Bms1-type G domain-containing protein
- BING4 C-terminal domain-containing protein
- Uncharacterized protein
- Nop14-like protein
Sequence:
MPPPTSVASTARSSSGATIKRKVDDRIRKVIENAVHKRHRALLLLVGDRGKDQIVNLHQMVSHANHNAKVNVLWCMKKEPDFGSTSLKQQEKKARLEVKGGMSTDATKEAFQTFLSQTIIRFCQYKETHKILGQTFGMAVLQDFEAMTPNTLARTIETVKGGGIIVIMFRAMKSLKQLYTIAMDVHSRYRTEALQDVVPRFNERFLLSLVDCDTSLCVDDDLNVLPITAKMCAVESARTTSYDETLVLQGRQKHEADLAALKERLRASNEVGPLISLCQTLDQGKTILSLMQTVVEKSLNTTCVVTAGRGRGKSAALGLATAGAVAQGYSNIFCTAPSPENLQTFFEFVVRGLQELGYKERTDFEAMQSTNVEFSKCIIRINVFREHRQTVQYISPNDASKFAQAELAIIDEAAALPLPIVKQMLGPYLVFLSSTISGYEGTGRSLSMKLVADMRKHSGSTNASVAGDDRRLLRELSMSDPIRYGPNDPVEFWLNKLLCLDATVRPIAVKSSPHPNSCELYYVNRDALFSYHPLAEQLLQAIVAMLVAAHYKNQPNDLQLMSDAPGHHLFILCPSTVDAKSGIPDVFCVIHACEEGHVSSEAIKSNLSRGLRPSGDLIPYTLSQYYLEEGFAKLAGLRIVRIATNPELQRAGYGSRALELLQQYYTGSVSLRPAASAAATENNTELKAVDDADEVSSTISHTIKPRKRIPSLLVPLIERPYEEIDYLGVSFGVTTPLFNFWKRGGFEPLYLRHAANELTGEHSCVMVRSFGFDLGLLRAEFRRRFIPLLAMPFRQLPTELALSILKDVDVNDPQKLAAATDLSHVAEHNVRVAGQPQCTWKELQEIFSISDLKRLKLNATTFVEGGHVLDLVPALAKLYFESRLFHLPDGAEGVVLSHAQAAVLLGVGLQCQTIEEVGQQAVFSGVPTQQLRAFLQKAISRIVDHFTRLQKLKLTGSKEEETVKRNGGNDDADENTHEIYDKEGRVVGLSVEKRVRSVINVDSTLLRDAKSATVGARNDAGGTTGLQRAFKRSKKTRRG
Protein: Exocyst complex component 7 (Exocyst complex component Exo70) (rExo70) (O54922)
Organism: Rattus norvegicus (Rat)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion (By similarity). It is required for neuron survival and plays an essential role in cortical development (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O35250}. Cell membrane {ECO:0000250|UniProtKB:O35250}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35250}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9UPT5}. Note=Translocates, as a preformed complex with SEC6 and SEC8, to the plasma membrane in response to insulin through the activation of ARHQ (By similarity). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:O35250, ECO:0000250|UniProtKB:Q9UPT5}.
Interaction partners:
- Exocyst complex component 4
- Exocyst complex component 3
- Exocyst complex component 6
- Exocyst complex component 8
- Exocyst complex component 2
- Rho-related GTP-binding protein RhoQ
- Exocyst complex component 5
- Exocyst complex component 1
- Exocyst complex component
- Exocyst complex component 1-like
Sequence:
MIPPQEASARRREIEDKLKQEEETLSFIRDSLEKSDQLTKNMVSILSSFESRLMKLENSIIPVHKQTENLQRLQENVEKTLSCLDHVISYYHVASDTEKIIREGPTGRLEEYLGSMAKIQKAVEYFQDNSPDSPELNKVKLLFERGKESLESEFRSLMTRHSKVISPVLVLDLISADDELEVQEDVVLEHLPESVLQDVIRISRWLVEYGRNQDFMNVYYQIRSSQLDRSIKGLKEHFRKSSSSSGVPYSPAIPNKRKDTPTKKPIKRPGRDDMLDVETDAYIHCVSAFVRLAQSEYQLLMGIIPEHHQKKTFDSLIQDALDGLMLEGENIVSAARKAIIRHDFSTVLTVFPILRHLKQTKPEFDQVLQGTAASTKNKLPGLITSMETIGAKALEDFADNIKNDPDKEYNMPKDGTVHELTSNAILFLQQLLDFQETAGAMLASQETSSSATSYNSEFSKRLLSTYICKVLGNLQLNLLSKSKVYEDPALSAIFLHNNYNYILKSLEKSELIQLVAVTQKTAERSYREHIEQQIQTYQRSWLKVTDYIAEKNLPVFQPGVKLRDKERQMIKERFKGFNDGLEELCKIQKAWAIPDTEQRDKIRQAQKSIVKETYGAFLHRYSSVPFTKNPEKYIKYRVEQVGDMIDRLFDTSA
Protein: Proteasome activator complex subunit 3 (Activator of multicatalytic protease subunit 3) (Proteasome activator 28 subunit gamma) (K9J957)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY
Protein: Heat shock 70 kDa protein BIP2 (Heat shock 70 kDa protein 12) (Heat shock protein 70-12) (AtHsp70-12) (Luminal-binding protein 2) (AtBP2) (BiP2) (Q39043)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable). Involved in polar nuclei fusion during female gametophyte development and is essential for the regulation of endosperm nuclei proliferation. Involved in sperm nuclear fusion with central cell polar nuclei at fertilization, which is critical for normal endosperm nuclear proliferation. Required for pollen development and pollen tube growth.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. Nucleus {ECO:0000305}.
Interaction partners:
- Heat shock 70 kDa protein 17
- Endoplasmin homolog
- Calnexin homolog 1
- DnaJ protein ERDJ2A
- Serine/threonine-protein kinase/endoribonuclease IRE1b
- Heat shock 70 kDa protein BIP1
- DnaJ protein ERDJ3B
- Calreticulin-2
- Serine/threonine-protein kinase/endoribonuclease IRE1a
- Protein disulfide isomerase-like 1-1
Sequence:
MARSFGANSTVVLAIIFFGCLFAFSTAKEEATKLGSVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDSERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQKDRKLVPYQIVNKDGKPYIQVKIKDGETKVFSPEEISAMILTKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVIAGLNVARIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSVLTIDNGVFEVLSTNGDTHLGGEDFDHRIMEYFIKLIKKKHQKDISKDNKALGKLRRECERAKRALSSQHQVRVEIESLFDGVDLSEPLTRARFEELNNDLFRKTMGPVKKAMDDAGLQKSQIDEIVLVGGSTRIPKVQQLLKDFFEGKEPNKGVNPDEAVAYGAAVQGGILSGEGGDETKDILLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVSIQVFEGERSLTKDCRLLGKFDLTGVPPAPRGTPQIEVTFEVDANGILNVKAEDKASGKSEKITITNEKGRLSQEEIDRMVKEAEEFAEEDKKVKEKIDARNALETYVYNMKNQVSDKDKLADKLEGDEKEKIEAATKEALEWLDENQNSEKEEYDEKLKEVEAVCNPIITAVYQRSGGAPGAGGESSTEEEDESHDEL
Protein: Transcription factor SOX-7 (Q9BT81)
Organism: Homo sapiens (Human)
Function: Binds to and activates the CDH5 promoter, hence plays a role in the transcriptional regulation of genes expressed in the hemogenic endothelium and blocks further differentiation into blood precursors (By similarity). May be required for the survival of both hematopoietic and endothelial precursors during specification (By similarity). Competes with GATA4 for binding and activation of the FGF3 promoter (By similarity). Represses Wnt/beta-catenin-stimulated transcription, probably by targeting CTNNB1 to proteasomal degradation. Binds the DNA sequence 5'-AACAAT-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. Cytoplasm {ECO:0000269|PubMed:18819930}.
Interaction partners:
- Mitochondrial peptide methionine sulfoxide reductase
- Retinitis pigmentosa 1-like 1 protein
- Transcription factor GATA-4
- Catenin beta-1
- Transcription factor GATA-6
- POU domain, class 5, transcription factor 1
Sequence:
MASLLGAYPWPEGLECPALDAELSDGQSPPAVPRPPGDKGSESRIRRPMNAFMVWAKDERKRLAVQNPDLHNAELSKMLGKSWKALTLSQKRPYVDEAERLRLQHMQDYPNYKYRPRRKKQAKRLCKRVDPGFLLSSLSRDQNALPEKRSGSRGALGEKEDRGEYSPGTALPSLRGCYHEGPAGGGGGGTPSSVDTYPYGLPTPPEMSPLDVLEPEQTFFSSPCQEEHGHPRRIPHLPGHPYSPEYAPSPLHCSHPLGSLALGQSPGVSMMSPVPGCPPSPAYYSPATYHPLHSNLQAHLGQLSPPPEHPGFDALDQLSQVELLGDMDRNEFDQYLNTPGHPDSATGAMALSGHVPVSQVTPTGPTETSLISVLADATATYYNSYSVS