wanglab/gogpt-training-data huggingface dataset:
Protein: Fimbrial adhesin PapGI (P13720)
Organism: Escherichia coli
Function: Tip adhesin component of type P pili that binds preferentially to host cell glycosphingolipids such as globotriaosylceramide.
Subcellular location: Secreted. Fimbrium. Note=At the tip of P pili. {ECO:0000269|PubMed:2886993}.
Interaction partners:
Sequence:
MKKWFPAFLFLSLSGGNDALAGWHNVMFYAFNDYLTTNAGNVKVIDQPQLYIPWNTGSATATYYSCSGPEFASGVYFQEYLAWMVVPKHVYTNEGFNIFLDVQSKYGWSMENENDKDFYFFVNGYEWDTWTNNGARICFYPGNMKQLNNKFNDLVFRVLLPVDLPKGHYNFPVRYIRGIQHHYYDLWQDHYKMPYDQIKQLPATNTLMLSFDNVGGCQPSTQVLNIDHGSIVIDRANGNIASQTLSIYCDVPVSVKISLLRNTPPIYNNNKFSVGLGNGWDSIISLDGVEQSEEILRWYTAGSKTVKIESRLYGEEGKRKPGELSGSMTMVLSFP
Protein: Tyrosine-protein kinase JAK3 (EC 2.7.10.2) (Janus kinase 3) (JAK-3) (Q62137)
Organism: Mus musculus (Mouse)
Function: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A and STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion.
Subcellular location: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Cytokine receptor common subunit gamma
- Interleukin-2
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription 3
- Interleukin-4
- Interleukin-2 receptor subunit beta
- Interleukin-4 receptor subunit alpha
- Tyrosine-protein kinase JAK1
- Interleukin-7
- Signal transducer and activator of transcription 5B
Sequence:
MAPPSEETPLIPQRSCSLSSSEAGALHVLLPPRGPGPPQRLSFSFGDYLAEDLCVRAAKACGILPVYHSLFALATEDFSCWFPPSHIFCIEDVDTQVLVYRLRFYFPDWFGLETCHRFGLRKDLTSAILDLHVLEHLFAQHRSDLVSGRLPVGLSMKEQGEFLSLAVLDLAQMAREQAQRPGELLKTVSYKACLPPSLRDVIQGQNFVTRRRIRRTVVLALRRVVACQADRYALMAKYILDLERLHPAATTETFRVGLPGAQEEPGLLRVAGDNGISWSSGDQELFQTFCDFPEIVDVSIKQAPRVGPAGEHRLVTVTRMDGHILEAEFPGLPEALSFVALVDGYFRLICDSRHYFCKEVAPPRLLEEEAELCHGPITLDFAIHKLKAAGSLPGTYILRRSPQDYDSFLLTACVQTPLGPDYKGCLIRQDPSGAFSLVGLSQPHRSLRELLAACWNSGLRVDGAALNLTSCCAPRPKEKSNLIVVRRGCTPAPAPGCSPSCCALTQLSFHTIPTDSLEWHENLGHGSFTKIFRGRRREVVDGETHDSEVLLKVMDSRHRNCMESFLEAASLMSQVSYPHLVLLHGVCMAGDSIMVQEFVYLGAIDMYLRKRGHLVSASWKLQVTKQLAYALNYLEDKGLPHGNVSARKVLLAREGGDGNPPFIKLSDPGVSPTVLSLEMLTDRIPWVAPECLQEAQTLCLEADKWGFGATTWEVFSGGPAHITSLEPAKKLKFYEDQGQLPALKWTELAGLITQCMAYDPGRRPSFRAILRDLNGLITSDYELLSDPTPGIPSPRDELCGGAQLYACQDPAIFEERHLKYISLLGKGNFGSVELCRYDPLGDNTGPLVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRQSLRLVMEYLPSGCLRDFLQRHRARLHTDRLLLFAWQICKGMEYLGARRCVHRDLAARNILVESEAHVKIADFGLAKLLPLGKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGPEREGPPLCRLLELLAEGRRLPPPPTCPTEVQELMQLCWAPSPHDRPAFGTLSPQLDALWRGRPG
Protein: Protein FMP25, mitochondrial (Found in mitochondrial proteome protein 25) (Q08023)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Altered inheritance of mitochondria protein 39
- GTP-binding protein YPT1
- Assembly factor CBP4
Sequence:
MSFRLFTRTSQRLPRLNWVSPIRRYAKQPQYDEAELFAENINHGAYKAKKRPSDEHFQWPEKSPDQITKESELQWERMAKLSAVGQGILILVVVGGLGTAYLRWPELKSWWLIKMNGGRINATQEQSGQDSLEKLIRQKAKNLLREIPQVPAFQLGIDHPGVYIWGRCHSKDSLFPVRVPNLDGRKFRDILLAPSDDFNTNFAIDEKGDLISWDDLGQTKTILPDQDLTSMKYSSHFLYALNKKGEILVIPIRTPDLIASQVSSRRSKLLPWKTKLRYDWKLQTNQIFNGKEGEKRVVQFDAGSHHLVLLSNLGKAYCCATGNDQKQAQVSKGQFGIPTFSQFDEFPPNNQLFEIELLNKFKHEGEDVVRKREIKKIACGSYHTLAIDKTGEIYAFGWNRFGQLALPISYNLEYVSFPRSVTHAFKPHFPGMTNWKCVDIHCDDETSFVTIRKPGSTSDHHYFAFGNGLFGELGNNTFKNSQCDPIKIKSDDKKLTNWSCGSHCVFTETEQENEVIAWGNNDHGQLGIGKKTMKCAKPMNIPEVLKPGQDTTDLDSIYNSKLHLKKEQRVVTNGNKSCLYWRV
Protein: Transcription factor TCP20 (Q9LSD5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds to the site II motif (3'-TGGGCC/T-5') in the promoter of PCNA-2 and to 3'-GCCCG/A-5' elements in the promoters of cyclin CYCB1-1 and ribosomal protein genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein NLP6
- Protein NLP7
- WD repeat-containing protein LWD1
- Nitrate regulatory gene2 protein
- Transcription factor TCP4
- Transcription factor TCP3
- Transcription factor TCP2
- Transcription factor TCP24
- Transcription factor TCP5
- Transcription factor TCP10
Sequence:
MDPKNLNRHQVPNFLNPPPPPRNQGLVDDDAASAVVSDENRKPTTEIKDFQIVVSASDKEPNKKSQNQNQLGPKRSSNKDRHTKVEGRGRRIRMPALCAARIFQLTRELGHKSDGETIQWLLQQAEPSIIAATGSGTIPASALASSAATSNHHQGGSLTAGLMISHDLDGGSSSSGRPLNWGIGGGEGVSRSSLPTGLWPNVAGFGSGVPTTGLMSEGAGYRIGFPGFDFPGVGHMSFASILGGNHNQMPGLELGLSQEGNVGVLNPQSFTQIYQQMGQAQAQAQGRVLHHMHHNHEEHQQESGEKDDSQGSGR
Protein: Choline/ethanolaminephosphotransferase 1 (hCEPT1) (EC 2.7.8.1) (EC 2.7.8.2) (1-alkenyl-2-acylglycerol choline phosphotransferase) (EC 2.7.8.22) (Q9Y6K0)
Organism: Homo sapiens (Human)
Function: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein {ECO:0000269|PubMed:12221122}. Nucleus membrane {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein {ECO:0000269|PubMed:12221122}.
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Choline-phosphate cytidylyltransferase A
- Choline-phosphate cytidylyltransferase B
- Phosphatidylethanolamine N-methyltransferase
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phosphatidylserine synthase 2
- Phosphatidylserine synthase 1
- Lysophosphatidylcholine acyltransferase 2
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Lysophospholipid acyltransferase 5
Sequence:
MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIPVLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH
Protein: Probable proline--tRNA ligase, mitochondrial (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) (Q8CFI5)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q7L3T8}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Isoleucine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Probable leucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, mitochondrial
- Asparaginyl-tRNA synthetase
- Tyrosine--tRNA ligase, mitochondrial
Sequence:
MEGLLTRCRTLSALAACSLRHCRYIIHKCYHRAPGRGQRLVLSRMFQPQNLREDQVLSLEGRASDLTCKSQRLMLQVGLILPASPGCYHLMPYTVRAVEKLVRVIDQEMQAIGGQKINMPSLSPAELWRATSRWDLMGRELLRLRDRHGKEYCLGPTHEEAVTALVASQKKLSYKQLPLLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSSEAAQETYGLVCDAYCRLFDRLGLQWMKARADVGSIGGTMSHEFQLPVDIGEDRLVVCPSCHFSANTEILDLSQKICPDCQGPLTETKGIEVGHTFYLSTKYSSIFNALFTNAHGESLLAEMGCYGLGVTRILAAAIEVLSTEDCIRWPRLLAPYQVCVIPPKKGSKETAATEIVEKLYDDIMEAVPQLRGEVLLDDRTHLTIGNRLKDANKLGYPFVIIAGKRALEDPAHFEVWSQNTGEVVFLTKEGVMELLTGVHVV
Protein: Mediator of RNA polymerase II transcription subunit 18 (Mediator complex subunit 18) (Q9CZ82)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 23
Sequence:
MEAPPVTMMPVTGGTINMMEYLLQGSVLDHSLESLIHRLRGLCDNMEPETFLDHEMVFLLKGQQASPFVLRARRSMDRAGAPWHLRYLGQPEMGDKNRHALVRNCVDIATSENLTDFLMEMGFRMDHEFVAKGHLFRKGIMKVVVYKIFRILVPGNTDSTEALSLSYLVELSVVAPAGQDMVSDDMRNFAEQLKPLVHLEKIDPKRLM
Protein: SWI/SNF Subunit INI1 DNA binding domain-containing protein (Q21831)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR038126}.
Interaction partners:
- SWI/SNF complex subunit SMARCC2
- Bromo domain-containing protein
- SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4
- HMG box domain-containing protein
- Actin-related protein 4
- SWI/SNF chromatin-remodeling accessory subunit 2
- ARID domain-containing protein
- SWI/SNF chromatin remodeling complex subunit swsn-7
- PHD finger protein 10
- SWI/SNF chromatin-remodeling accessory subunit 1
Sequence:
MSSSTKTLSQTYGPRPQSFSLDEAGERYYIGSEIGAYLRLHRGTLYKKYPLLWRKVATSDDKDKLKQIAMSNAFLHTNIMLLRAHEVDELLDGSEEKYRAAGAAPSTPRTEGASRTVAKTPATGWAGQQVTSGSHHLESVPCSCPIAHSRGRMKHRELVYSAEDLEMSKRVMKNAEEGEDLVPIRLDMELDGIKLRDTFTFNKNEKMITPEMIAEIMCEDLDLPLAVFQPAITAAINQQLEASTEAPPLDVNICDQRAVLKLNINVGNQSLVDQFEWDMSDPNNSPEEFSRNICKELGLGGEFMSGIAYSIRGQLQWNQRTYAFSESPLATVDCPFRTSSEVESWGPFLETLTDAEIEKKMRDQDRNTRRMRRLVGGGFNY
Protein: ODAD1 central coiled coil region domain-containing protein (Q381H7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tubulin alpha chain
- Cilia- and flagella-associated protein 45
- Uncharacterized protein
- CFA20 domain-containing protein
- Dynein heavy chain, putative
- Nucleoside diphosphate kinase-like domain-containing protein
- Uncharacterized protein
- Dynein axonemal intermediate chain 4
- Paraflagellar rod component
- Outer dynein arm docking complex
Sequence:
MPPSQLLKDMDERRCLMASNIVAAQDEIMRQQEAVQKLTSENERLKKEIAVASGEQYDYVKADKYAALKTEVDSLEQRYQFEKMHLNELTKQYQLARIDLMQGSKLKGGVNAEQENVRAVQRQLEILENRLDQALARFNDAVSYNKELRDHIDIIRGERRVFQRVHKKMEDDLRSKKKIMSERIEQSNHDLDERDGYLQQVEQLRTALSEQKEEYDTAVRNLDVCMIDINRMRDELHRRQIEFEARSYMPNPTVDHSGVGKNLPVANTHAPTPFTEDGEDASDGMSSAEVGSEIMDIPAQLSMFAPDGDLQKLAQTYQVVGESNFSLYKRINELTTSREEMERDIHTLKKVIAEEHEHDVQQRRLIKEYEDRLAETELMLDRLNRSAEVHKEVLARIRETTEGVFKRIGCSAEEARRLVGSDHCTESTQLKFLGLIEERATRILCTYQLYKRTEAMLQEQKAAEEGADGSKRTLPIGAGDDQTYLPGKEKETDGDRGGNAAAAGGAENTRGIVSAVKEEGGEGSSGSKVDVRLLQALVEGTADFSPVLNLPVRKDGTAAKFVRCSVLPSAQLYGDESVEGKDDHDGDPVVSHEELRQQMQQRLLSKRLREEKGQRRKRDLKDQFADAPPILRRK
Protein: rRNA maturation factor (Q581T7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- G domain-containing protein
Sequence:
MPRSLFRNVRVLGATPRFAAGVQGLTEAVLLAERAPQAVELSIHFVTPGRMHELNLEHRGVDKPTDVLTFPGSGSGTPYAKFLNETVLLARVEGDNACVADPSVLAERRALLQELGDIYFSVEYISMRCSCRPTHCLRFHDYLQAALTHALLHALGYDHATPEQWKRMTKRERFLRHRLSVWRRRWPGCLQELDGVEMLMSPVTR
Protein: tRNA (guanine(10)-N(2))-methyltransferase (EC 2.1.1.214) (tRNA [Gm10] methyltransferase) (tRNA guanosine-2'-O-methyltransferase TRM11) (tRNA methylase 11) (Q12463)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15899842}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- eRF1 methyltransferase catalytic subunit MTQ2
- Multisite-specific tRNA:
- 18S rRNA
- tRNA
Sequence:
MKKYLLYMVQVHLNFRRAELESLADLYNLSIDFSQYDANSPFFIVELENDQQAKDWIKRSILTRGIYEYWGQGTTLDELHKDIQRQSNFEQDLQLKFKHSTFKFEFECYKGNSKAKRVEQIETFRYLGFEGKIDMKHPQEVFTVIEEYTPISENVGGKTPTRIYFGRQVQMSNRSAMEKYDLKKRPYKGTTSFEAELSLVSANIAQVKPGTIMYDPFAGTGSFLVAGGHFGSLVIGSDIDGRMIRGKGAQVNISANFKKYGESSQFLDVLTMDFTNNALRNNLVIDTILCDPPYGIRESIKVLGAKDPERFLGKEDMEIDGEKAYLRRDYIPTKKPYALDSLLDDLLQYSSERLPIGGRLAFWMPTANDANIETIVPMHENLELKYNCVQEFNKWSRRLLVYINRGSTFNGSSNHGIKRSKDNFRERYFNNFN
Protein: Probable serine/threonine-protein kinase ndrA (EC 2.7.11.1) (Nuclear DBF2-related kinase A) (Q54Y26)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable serine/threonine-protein kinase DDB_G0290859
- cAMP-dependent protein kinase regulatory subunit
- WW domain-containing protein A
- Emp24/gp25L/p24 family protein
Sequence:
MINDHESVIDVGSDDERENFEDEEDTTTVYSSDPLSRPTMDRSLAAKMYIEQYYINAQQSVKERGQRRKDLELKLENMKLSSKESNDLRKELDKKESDYMRIKRLKLKRSDFEVIRIIGRGAFGEVSLVRHRESNDLYAMKRLKKSEMLKKEQAAHVRAERDVLASANTNWVVKLYYSFQDDNYLYLIMEYLPGGDMMSLLIKYDIFTENQARFYIAETILAIESVHTLGYIHRDIKPDNLLLDSKGHVKLCDLGLCTGFHRLHSSEFYQMLVGDAMTIKMKLIEATPLTQTERIASWKKARRALAYSAVGTPDYTAPEVFLQIGYNKEVDWWSLGVILYEMVVGHPPFLSDNTTETCLKILNCKETLQIPTDMGLSKEVIDLIKRLVCEKDRYKSADEIKLHPFFKGVNWDNIRNQSAPFVPELKSPTDTSNFDIYEEIPNDIDDDDNNNNNNSNNNINLNDNINSNCTYTTPTKKSNIMGKGNIKDKDLAFIGFTFKGFDAVNKSPTNRRNVESIFNTNNSTTTSTTK
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (Prt1 homolog) (hPrt1) (eIF-3-eta) (eIF3 p110) (eIF3 p116) (P55884)
Organism: Homo sapiens (Human)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17984221}. Note=Localizes to stress granules following cellular stress. {ECO:0000269|PubMed:17984221}.
Interaction partners:
- Eukaryotic translation initiation factor 5
- Small ribosomal subunit protein RACK1
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit H
Sequence:
MQDAENVAVPEAAEERAEPGQQQPAAEPPPAEGLLRPAGPGAPEAAGTEASSEEVGIAEAGPESEVRTEPAAEAEAASGPSESPSPPAAEELPGSHAEPPVPAQGEAPGEQARDERSDSRAQAVSEDAGGNEGRAAEAEPRALENGDADEPSFSDPEDFVDDVSEEELLGDVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKITNDFYPEEDGKTKGYIFLEYASPAHAVDAVKNADGYKLDKQHTFRVNLFTDFDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVSIEERARWTETYVRWSPKGTYLATFHQRGIALWGGEKFKQIQRFSHQGVQLIDFSPCERYLVTFSPLMDTQDDPQAIIIWDILTGHKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSIYETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAFAWEPNGSKFAVLHGEAPRISVSFYHVKNNGKIELIKMFDKQQANTIFWSPQGQFVVLAGLRSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQGRLLQKNNKDRFCQLLWRPRPPTLLSQEQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVERRRTMMEDFRKYRKMAQELYMEQKNERLELRGGVDTDELDSNVDDWEEETIEFFVTEEIIPLGNQE
Protein: Eukaryotic translation initiation factor isoform 4E (PeaeIF(iso)4E) (eIF(iso)-4E) (eIF-(iso)4F 25 kDa subunit) (eIF-(iso)4F p28 subunit) (mRNA cap-binding protein) (A0A445AGS0)
Organism: Arachis hypogaea (Peanut)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses such as peanut stripe virus (PStV).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus {ECO:0000269|PubMed:28344571}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus {ECO:0000269|PubMed:28344571}. Note=(Microbial infection) Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with viral helper component proteinase (HC-Pro) in the cytoplasm. {ECO:0000269|PubMed:28344571}.
Interaction partners:
- MI domain-containing protein
- MI domain-containing protein
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Polyadenylate-binding protein
- Polyadenylate-binding protein
Sequence:
MATETAGAVVESSSAATVPSPAPEAGSKHKLERKWTFWFDNQSKPKQGAAWGTSLREVYTFDTVEEFWCLYDQVFKPSKLPGNADFHLFKTGIEPKWEDPECAKGGKWTVTSNRKANLDNMWLETMMALIGEQFDDAEDICGVVASVRQRQDKLSLWTKTAANEAAQMGIGRKWKEIIDVTDKIIYNFHDDSRTRSSKSRYSV
Protein: CorA-like Mg2+ transporter family protein (RacA) (Rho GTPase protein rac1) (Q5DR84)
Organism: Aspergillus niger
Interaction partners:
Sequence:
MATGPATQSLKCVVTGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYTASVMVDGRPISLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSIVSPPSFDNVKAKWFPEIEHHAPNVPIILVGTKLDLRDDRGTIDALRQRKMEPVSYEQALAVAKEIRAHKYLECSALTQRNLKSVFDEAIRAVLNPRPAAKPKNKKCVIL
Protein: Paired box PAX-3 (Q9PSS2)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
GQGRVNQLGGVFINGRPLPNHIRHKIVQMAHHGIRPCVISRQLRVSHGCVSKILCRYQETGSIRPGAIGGSKPKQVTTPDVEKKIEEYKRENAGMFSWEIRDRLLKDGVCDRNTVPSVSSISLILRSKFQRRSRTTFTAEQLEELERAFERTHYPDIYTREELAQRAKLTEARVQVWFSNRRARWRKQAG
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (Q9VVL8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Tryptophan--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- histidine--tRNA ligase
- Methionine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, mitochondrial
- GH06388p
- serine--tRNA ligase
- leucine--tRNA ligase
Sequence:
MFRFGKLHRSLSKVAKKGQTAVYSQRRCIQARSFLPGLASRTAGTPSATAQVTGGNKQHVHPHGNSVNSGHEEHNTRWPRKVFSGIQPTGSLHLGNYLGAVRKWVQLQNARDDVTVCIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQSAVAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIYNGRYGETFPVCTAIIEDGDASRVLSLRDPSKKMSKSEANPKATINLCDSPDLITQKIKKAVTDFTSDITYNPGKRAGVSNLVNIHAQVTGQSIKTVVNEAATLDTAKYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKARQQARQTLNDVKQRLGLGTSANIPAAVHVAPLLPAPDISKTSASRRMSKDFDGNVHERHERMYGFGDQPSGGAGQSATGEVADMPQAVVPRVIRRAPIVPTQSMRVEKQLGSTRTRHVFQMDTCNAPHIGFKPPPGFSASMVTGALAKNKRATVKPVTGNLGFGQQSQGGSYKHSQNVNPSAVSTIAREVNAAKKQEFTCNPALYGSALESLSNSSRSSEKTNSTAGDSEFIIVASEEEEQAASSEEQREEAEEEESGEREREKGERNATEATKVEI
Protein: Anterior gradient protein 3 (AG-3) (AG3) (hAG-3) (Anterior gradient 3 homolog) (Breast cancer membrane protein 11) (Protein disulfide isomerase family A, member 18) (Q8TD06)
Organism: Homo sapiens (Human)
Function: Required for calcium-mediated regulation of ciliary beat frequency and mucociliary clearance in the airway. Might be involved in the regulation of intracellular calcium in tracheal epithelial cells.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:18086916, ECO:0000269|PubMed:25751668}. Note=Found in the cytoplasm, which could include the endoplasmic reticulum. {ECO:0000305|PubMed:26170690}.
Interaction partners:
- Ly6/PLAUR domain-containing protein 3
Sequence:
MMLHSALGLCLLLVTVSSNLAIAIKKEKRPPQTLSRGWGDDITWVQTYEEGLFYAQKSKKPLMVIHHLEDCQYSQALKKVFAQNEEIQEMAQNKFIMLNLMHETTDKNLSPDGQYVPRIMFVDPSLTVRADIAGRYSNRLYTYEPRDLPLLIENMKKALRLIQSEL
Protein: Grainyhead-like protein 1 homolog (Mammalian grainyhead) (NH32) (Transcription factor CP2-like 2) (Transcription factor LBP-32) (Q9NZI5)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3'. Important regulator of DSG1 in the context of hair anchorage and epidermal differentiation, participates in the maintenance of the skin barrier. There is no genetic interaction with GRHL3, no functional cooperativity due to diverse target gene selectivity during epithelia development (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18288204, ECO:0000269|PubMed:35013237}.
Interaction partners:
Sequence:
MTQEYDNKRPVLVLQNEALYPQRRSYTSEDEAWKSFLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRERRSSTAKPEVEHPEPDHSKRNSIPIVTEQPLISAGENRVQVLKNVPFNIVLPHGNQLGIDKRGHLTAPDTTVTVSIATMPTHSIKTETQPHGFAVGIPPAVYHPEPTERVVVFDRNLNTDQFSSGAQAPNAQRRTPDSTFSETFKEGVQEVFFPSDLSLRMPGMNSEDYVFDSVSGNNFEYTLEASKSLRQKPGDSTMTYLNKGQFYPITLKEVSSSEGIHHPISKVRSVIMVVFAEDKSREDQLRHWKYWHSRQHTAKQRCIDIADYKESFNTISNIEEIAYNAISFTWDINDEAKVFISVNCLSTDFSSQKGVKGLPLNIQVDTYSYNNRSNKPVHRAYCQIKVFCDKGAERKIRDEERKQSKRKVSDVKVPLLPSHKRMDITVFKPFIDLDTQPVLFIPDVHFANLQRGTHVLPIASEELEGEGSVLKRGPYGTEDDFAVPPSTKLARIEEPKRVLLYVRKESEEVFDALMLKTPSLKGLMEAISDKYDVPHDKIGKIFKKCKKGILVNMDDNIVKHYSNEDTFQLQIEEAGGSYKLTLTEI
Protein: Uncharacterized protein YOR389W (Q08912)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Putative uncharacterized protein YOR392W
- Fluoride export protein 1
- Uncharacterized membrane protein YOR365C
- Uncharacterized protein YPL277C
Sequence:
MRFHRQGTAATVGVLLIVLLGFCWKLSESYGIVSTALPHKQPATKITDTPSIRWDNYHEFVRDIDFDNSTAIFNSIRAALRQSPSDIHPVGVSYFPAVIPKGTLMYHAGSKVPTTFEWLAMDHEFSYSFGLRSPSYGRKSLERRHGRFGNGTHGDHPKGPPPPPPPDEKDRGSQKMLTYRAARDLNKFLYLDGASAAKTDSGEMDTQLMLSNVIKEKLNLTDDGENERMAERLYAARICKWGKPFGLDGIIRVEVGFEVVLCDFSADNVELVSMLEMVQPNQYLGLPAPTVISKEEGWPLDENGNLVEDQLTDDQKAILEREDGWEKTFSNFNAVKSFNQLRAGTAHDNGEHRIHIDYRYLVSGINRTYIAPDPNNRRLLDEGMTWEKQLDMVDDLEKALEVGFDATQSMDWQLAFDELVLKFAPLLKSVSNILNSNGDINESIAINATALTLNFCLRFEPASNNSDEFGSGKDFAVYQYVSPYQALKTDADFLIWSSAVSVVGEIVDAIYKVNDLLIPEVYSFMTDNTTSSDLIKNVETARSTIDGLIESLGWIELNYRCERQCNWDEVCYTPSWGPSPMGMTEPGSHNEGFGTHFDESRQRLVINSKLQCININDLMVNRNH