wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein bS1 (30S ribosomal protein S1) (Bacteriophage Q beta RNA-directed RNA polymerase subunit I) (P0AG67)
Organism: Escherichia coli (strain K12)
Function: Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine-Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:342903}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS7
Sequence:
MTESFAQLFEESLKEIETRPGSIVRGVVVAIDKDVVLVDAGLKSESAIPAEQFKNAQGELEIQVGDEVDVALDAVEDGFGETLLSREKAKRHEAWITLEKAYEDAETVTGVINGKVKGGFTVELNGIRAFLPGSLVDVRPVRDTLHLEGKELEFKVIKLDQKRNNVVVSRRAVIESENSAERDQLLENLQEGMEVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRVKHPSEIVNVGDEITVKVLKFDRERTRVSLGLKQLGEDPWVAIAKRYPEGTKLTGRVTNLTDYGCFVEIEEGVEGLVHVSEMDWTNKNIHPSKVVNVGDVVEVMVLDIDEERRRISLGLKQCKANPWQQFAETHNKGDRVEGKIKSITDFGIFIGLDGGIDGLVHLSDISWNVAGEEAVREYKKGDEIAAVVLQVDAERERISLGVKQLAEDPFNNWVALNKKGAIVTGKVTAVDAKGATVELADGVEGYLRASEASRDRVEDATLVLSVGDEVEAKFTGVDRKNRAISLSVRAKDEADEKDAIATVNKQEDANFSNNAMAEAFKAAKGE
Protein: Endochitinase A1 (EC 3.2.1.14) (Chitinase A1) (Q4WEP7)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Endochitinase B1
Sequence:
MVSSKLSFVATAVAALAPLASAFDASSRSNLAIYWGQGPNQLRLSHFCQETSLDIINIGFINYFPDMSPGHWPGSNFGNQCDGSVYVTNDGVVTKLLSGCHQIMEDIPICQAAGKKVLLSIGGAYPPDQSILSEDSAVAFATFLWGAFGPVAEGWEGPRPFGDVVVDGFDFDIEHNGGFGYATMANTFRQYFNQVPERKFYLSAAPQCIIPDAQLSDAIFNAAFDFIWIQYYNTAACSAKSFIDTSLGTFNFDAWVTVLKASASKDAKLYVGLPASETAANQGYYLTPDEVESLVSTYMDRYPDTFGGIMLWEATASENNQIDGAPYADHMKDILLHCDPSPPVTSSSAIPSSTPVTTPSPSSSAVPSSTPAVSETPSPSSSAVPSSTPVASSTPVVPGTSASSSPVSSSSAVASSTPVVPGTSASSSPVSSSSAVASSTPVVPGTSTSPSTPVIPGTSASSSPVSSSSAVASSTPVVPGTSASSSPVSSSSAVASSTPVVPGTSASSSPVSSSSAVASSTPVVPGTSVPSSTPAIPGGSSSSSEAVASSTPLVTLTLTVSPTPAPSSSESSSTDLSSSTQTDVGTAPSQPAGPSTTATATTSSSSSSTDESSTTVGSGNGNGSGSTTTTAATDSITAAPTATSSATATGATSEPVTITTIIVTSYIDICPTGFTTVTTTYTTTYCPGTNTATATATVTNPPSGPGGAGSQTTAPTVPEGWTTTVTICTQCAAKPTTVTLTLPVTETGSTSTDAVPAPPAATGEGSNPTQPSGASPTGGNGSFSEEPVPPPAVTQVSTSTEIVTLVRPTSSRPLILGTGTVHPSSTLAVKPSAKPSGQNSGSSSHVPIPPSYTQEAVSPLSTGAASRVTGLGHGLVLTVLTLSAFFVL
Protein: Gamma-aminobutyric acid receptor subunit pi (GABA(A) receptor subunit pi) (GABAAR subunit pi) (O00591)
Organism: Homo sapiens (Human)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. In the uterus, the function of the receptor appears to be related to tissue contractility. The binding of this pI subunit with other GABA(A) receptor subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O09028}; Multi-pass membrane protein {ECO:0000255}. Note=Located on the apical plasma membrane of alveolar epithelial type II cells. {ECO:0000250|UniProtKB:O09028}.
Interaction partners:
- Inactive phospholipase C-like protein 1
- Huntingtin-associated protein 1
- Trafficking kinesin-binding protein 2
- Vesicle-fusing ATPase
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit alpha-6
- Gamma-aminobutyric acid receptor subunit epsilon
Sequence:
MNYSLHLAFVCLSLFTERMCIQGSQFNVEVGRSDKLSLPGFENLTAGYNKFLRPNFGGEPVQIALTLDIASISSISESNMDYTATIYLRQRWMDQRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVACNMDLSKYPMDTQTCKLQLESWGYDGNDVEFTWLRGNDSVRGLEHLRLAQYTIERYFTLVTRSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLDSVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGALLEYAVAHYSSLQQMAAKDRGTTKEVEEVSITNIINSSISSFKRKISFASIEISSDNVDYSDLTMKTSDKFKFVFREKMGRIVDYFTIQNPSNVDHYSKLLFPLIFMLANVFYWAYYMYF
Protein: Nickel ABC transporter, periplasmic nickel-binding protein, putative (Q880R4)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Interaction partners:
- Nickel ABC transporter, permease protein
- Nickel ABC transporter, permease protein, putative
- ABC-type dipeptide transporter
- Peptide ABC transporter, permease protein
- Dipeptide ABC transporter, permease protein DppC, putative
- Peptide ABC transporter, permease protein
- Peptide ABC transporter, permease protein
- Dipeptide ABC transporter, permease protein
- Dipeptide ABC transporter, permease protein DppB, putative
- Peptide ABC transporter, permease protein
Sequence:
MSGRPLLTRLLFAAITVTLLGCSPPSQDSQAGKTLKVTFFRDNTTLVSLDPFQVYWLEHRVVLRNVAESLTDQDPQTGNIIPWLAERWDVSDNALEYTFHLRKDVTFSNGTRFDAQAVKTAYDTNKAFADQLPATFGATYLKGYDHAQVLDDFTVKLVLAKPNAGFLQATSTTNLAILAPQSYALSVKERSLGAIIGTGPFVLERYTPESGLRLTKRKGYAWPSANAQNKGEAHLDAVDVSYVPEESVRNGQFVQGQVDILWPRTPFSEVDLNLFKSRGATIQSRSLPGPALNMYPNTRGNRILADRNVRLALQKAIDRKTYAATVYNPQFPVVSGIYDVTTPFYKNQADKLAYDPKGAERLLDEAGWAKNADGYRYKDGKRLKLAYNLSPAETAGDVLIQDQLRKVGIELKLNVVTTAEWAANNAAGNYDLTYNYMTRADPIILQTIIDPRSANSSTLATNLYAPQTLPKALELFDAGLTATRSEQRAKAYGDLQDLLIDEGSAFPVYERVWQAATAKNVRNFHWTAEGFALFNDIEIAAP
Protein: Receptor-like protein 48 (AtRLP48) (F4JTU7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in root hair development.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 12
- F-box/WD-40 repeat-containing protein At5g21040
- Ubiquitin carboxyl-terminal hydrolase 14
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 2
- Protein PHR1-LIKE 1
Sequence:
MHSCSERRMMTVIWSLCLIFCLSNSILAIAKDLCLPDQRDALLEFKNEFYVQEFDPHMKCEKATETWRNKTDCCSWNRVSCDPKTGKVVELDLMSSCLNGPLRSNSSLFRLQHLQSLELSSNNISGILPDSIGNLKYLRSLSFRTCHLFGKIPSSLGSLSYLTHLDLSYNDFTSEGPDSGGNLNRLTDLQLVLLNLSSVTWIDLGSNQLKGMLPSNMSSLSKLVSFDISENSFSGSIPSSLFMIPSLNFSGPLEIGNISSHSELGYLYMGENNFNGPIPGSLSKLVGLRDLSLSFWNTGRGIVDFSIFLHLKSLCSLDLSYLNTRSMVDLSFFSHLMSLDELDLSGINLKISSTLSFPSATGTLILASCNIVEFPKFLENQTSLFYLDISANHIEGQVPEWLWRLPTLSFVNIAQNSFSGELPMLPNSIYSFIASDNQFSGEIPRTVCELVSLNTLVLSNNKFSGSIPRCFENFKTISILHLRNNSLSGVFPKEIISETLTSLDVGHNWLSGQLPKSLIKCTDLEFLNVEDNRINDKFPFWLRSLSNLQILVLRSNEFYGPIFSLEDSLSFPKLRIFDISENHFTGVLPSDYFAGWSAMSSVVDIFDTTPQVHILGVFQGYYHNSVVLTNKGLNMELVGSGFTIYKTIDVSGNRLEGDIPESIGILKELIVLNMSNNAFTGHIPPSLSNLSNLQSLDLSQNRLSGSIPPELGKLTFLEWMNFSYNRLEGPIPQATQIQSQNSSSFAENPGLCGAPFLNKCGGEEEEEEEATKQEEDEDEEKEEKNQVFSWIAAAIGYVPGVFCGLTIAHILTS
Protein: Phosphatidylinositol 4-phosphate 5-kinase 2 (AtPIP5K2) (EC 2.7.1.68) (1-phosphatidylinositol 4-phosphate kinase 2) (Diphosphoinositide kinase 2) (PtdIns(4)P-5-kinase 2) (Q8L796)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses phosphatidylinositol (PtdIns) phosphate kinase activity (Probable). Phosphorylates PtdIns(4)P and PtdIns(3)P in vitro. Doesn't phosphorylate PtdIns(5)P nor PtdIns(3,4)P2 in vitro. Does not exhibit phosphatidylinositol kinase activity in vitro.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19903693}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta 1
- Phosphatidylinositol 4-kinase beta 2
- Phosphatidylinositol 4-kinase alpha 1
- Ras-related protein RABE1d
- Phosphatidylinositol 4-kinase alpha 2
- Phosphoinositide phospholipase C 2
- Peptidyl-prolyl cis-trans isomerase Pin1
- Phosphoinositide phospholipase C 1
- Phosphoinositide phospholipase C 3
- Type IV inositol polyphosphate 5-phosphatase 7
Sequence:
MMREPLVSEEEEEEATEVLLVEKTKLCKRRGDEEKTEERRDDLLLLALTPMVRSKSQGTTRRVTPTPPPVDVEKPLPNGDLYMGTFSGGFPNGSGKYLWKDGCMYEGEWKRGKASGKGKFSWPSGATYEGEFKSGRMEGSGTFVGVDGDTYRGSWVADRKQGHGQKRYANGDYYEGTWRRNLQDGRGRYVWMNGNQYTGEWRNGVICGKGVLAWPNGNRYEGQWENGVPKGSGVFTWADGSSWIGSWNESSNLMRNFFDGIEKNELIVATRKRSSVDSGAGSLTGEKIFPRICIWESDGEAGDITCDIVDNVEASVIYRDRISIDKDGFRQFRKNPCCFSGEAKKPGETISKGHKKYDLMLNLQHGIRYSVGKHASVVRDLKQSDFDPSEKFWTRFPPEGSKTTPPHLSVDFRWKDYCPLVFRRLRELFTVDPADYMLAICGNDALRELSSPGKSGSFFYLTQDDRFMIKTVKKSEVKVLLRMLPSYYKHVCQYENTLVTRFYGVHCIKPVGGQKTRFIVMGNLFCSEYRIQRRFDLKGSSHGRYTSKPEGEIDETTTLKDLDLNFAFRLQRNWYQELMTQIKRDCEFLEAERIMDYSLLVGVHFRDDNTGDKMGLSPFVLRSGKIESYQSEKFMRGCRFLEAELQDMDRILAGRKPLIRLGANMPARAERMARRSDYDQYSSGGTNYQSHGEVYEVVLYFGIIDILQDYDISKKIEHAYKSLQADPASISAVDPKLYSRRFRDFISRIFIEDG
Protein: Collectrin (Transmembrane protein 27) (Q9ESG3)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in amino acid transport by acting as binding partner of amino acid transporters SLC6A18 and SLC6A19, regulating their trafficking on the cell surface and their activity (By similarity). May also play a role in trafficking of amino acid transporters SLC3A1 and SLC7A9 to the renal cortical cell membrane (By similarity). Regulator of SNARE complex function. Stimulator of beta cell replication (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ESG4}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to the brush border membranes of cells in the proximal tubules of kidney. Colocalized with SLC6A19 in the early proximal S1 tubule. {ECO:0000250|UniProtKB:Q9ESG4}.
Interaction partners:
- Sodium-dependent neutral amino acid transporter B
- Sodium-dependent neutral amino acid transporter B
- Sodium- and chloride-dependent transporter XTRP3
- Neutral amino acid transporter B
- Amino acid transporter
- Angiotensinogen
Sequence:
MLWALFFLVTTIHAELCRPDAENAFKVRLSIKAALGDKAYVWDTDEEYLFRAMVAFSMRKVPNREGTEISHVLLCNVTQRVSFWFVVTDPLKNHTLPAAEVQSAIRMNRNRINSAFFLDDHTLEFLKIPSTLAPPMDPSVPVWIIVFGVIFCIVTVAIALLVLSGIRQRRRNKKGPPGVEDAEDKCENIITIENGIPCDPLDMKGGHINDGFLTEDERLTPL
Protein: LD21546p (Transportin-Serine/Arginine rich, isoform A) (Transportin-Serine/Arginine rich, isoform B) (Q9VQG0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD40489p
- D-Importin 7/RanBP7
- Serine-arginine protein 55
- Transportin-1
- Bifunctional glutamate/proline--tRNA ligase
- Nuclear pore complex protein Nup153
- Importin subunit alpha
- RNA helicase
- Importin subunit alpha
- Exportin-1
Sequence:
MDTYSVDVVYQAISALFQGNNPKEQEKANKWLQDFQKSIYSWTIADELLHQKRDLHANYFAAQTMRNKIQNSFSELPPHTHESLRDSLITHIGQIDEQTDNVIVTQLSLAVADLALLMASWREPINDLLVTLAPHQCAIWPLLEVLKVLPEEIDSRYLRLGANRREEVHKQLDASAECVLKFLCMCLQREDLDQQRVWNAALRTYSAWLVIHAFPVSHVYNNALTQLAFRLLSLPETSGKLHDNATECVCALLSCINTRQDGASDPESSFEAQLFGAVCMLETPYHLSVAHEDTDKTINYCRIFTSLCDAFFYDLLADAQKPHYSLKGLDLVLLCVGHFDYEVAEITFHLWYKLSEDLFQRNEDKLTVLFRPHIERLISALFRHSQMESDHDGLIEENNNFFDFRRKVSDLIKDVAFIVGSGACFKQMFHILQAPETTWESTEAALFIMQNVAKNILPDENEVIPKVVEAILNMSEQTHIAVRYTAILLIGELCDWIENHPESLEAVLNFLLYALQQKNGLAPAAAIALTSICSACRQKMVCHISGLVEIARSLDSFQINNDVAIGLLKGISLILTRLPREQLQPALREIVGFQLQPLAQLVDSTGSTPQKGERTDPVYWIDRACAIIRHTNPDVPDNVEHPTVAILNDAWQLISRVMDKYQSDLRIMERTCRLIRYGIRMVRKQAMMLVEPLIKQMVVLYSVQHHSCFLYVGSILVDEFAKSSECIGGLLEMLQAFIEPTFGLLQMENGLKNNPDTVDDFFRLASRYLDCCPHQLLQSSLITPIFQCALIACSLDHREANSSVMKFFINLLVWGRSNNHSRNTECRPLVVELASQHGGALVMNLIQASVFQLHSYMLVDVAEVLHELKQVVGNERMQPFLAQALEALPKKNSGGYVTATQQQLDEFSSTVLRADTTKAISQALKTFTRLFR
Protein: Neuroendocrine convertase 2 (NEC 2) (EC 3.4.21.94) (Egg-laying defective protein 3) (Kex2-like prohormone convertase 2) (CELPC2) (Prohormone convertase 2) (PC2) (Proprotein convertase 2) (G5ECN9)
Organism: Caenorhabditis elegans
Function: Serine endoprotease which cleaves preproteins at paired basic amino acids. Processes FMRFamide-like (flp) and neuropeptide-like protein (nlp) neuropeptides. Probably by processing flp-1 and flp-18, modulates the neuronal excitation-inhibition balance and thus the level of activity of the locomotor circuit. Regulates sensitivity to mechanosensory stimuli. By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions. Probably by processing flp neuropeptides, regulates the turning step of male mating behavior. Cleaves pro-insulin-like proteins ins-3, ins-4 and ins-6 into their mature active forms. Together with convertase kpc-1, cleaves pro-insulin-like protein ins-18. By controlling ins-4 and ins-6 processing and thus the activation of the daf-2/InsR pathway, negatively modulates synapse development and synaptic transmission at neuromuscular junctions. Similarly, by controlling ins-4 and ins-6 processing, negatively regulates dauer formation under optimal environmental conditions. Under adverse environmental conditions, may promote dauer formation by processing ins-18, a daf-2/InsR antagonist. May cleave dense-core vesicle membrane protein ida-1. Involved in egg-laying, fat storage and locomotion.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000303|PubMed:11717360}. Secreted {ECO:0000303|PubMed:24671950}.
Interaction partners:
- Carboxypeptidase E
- Neuroendocrine protein 7B2
- Receptor-type tyrosine-protein phosphatase-like ida-1
- Calcium-dependent secretion activator
- FMRFamide-like neuropeptides 3
- Neuropeptide-Like Protein
- Phorbol ester/diacylglycerol-binding protein unc-13
- FMRFamide-like neuropeptides 1
- Probable vesicular glutamate transporter eat-4
- Tyrosine decarboxylase
Sequence:
MKNTHVDLICVFLSIFIGIGEAVDVYTNHFHVHLKEGGGLEDAHRIAKRHGFINRGQVAASDNEYHFVQPALVHARTRRSAGHHAKLHNDDEVLHVEQLKGYTRTKRGYRPLEQRLESQFDFSAVMSPSDPLYGYQWYLKNTGQAGGKARLDLNVERAWAMGFTGKNITTAIMDDGVDYMHPDIKNNFNAEASYDFSSNDPFPYPRYTDDWFNSHGTRCAGEIVAARDNGVCGVGVAYDGKVAGIRMLDQPYMTDLIEANSMGHEPSKIHIYSASWGPTDDGKTVDGPRNATMRAIVRGVNEGRNGLGSIFVWASGDGGEDDDCNCDGYAASMWTISINSAINNGENAHYDESCSSTLASTFSNGGRNPETGVATTDLYGRCTRSHSGTSAAAPEAAGVFALALEANPSLTWRDLQHLTVLTSSRNSLFDGRCRDFPSLGINDNHRDSHGNCSHFEWQMNGVGLEYNHLFGFGVLDAAEMVMLAMAWKTSPPRYHCTAGLIDTPHEIPADGNLILEINTDGCAGSQFEVRYLEHVQAVVSFNSTRRGDTTLYLISPMGTRTMILSRRPKDDDSKDGFTNWPFMTTHTWGENPTGKWRLVARFQGPGAHAGTLKKFELMLHGTREAPYNLIEPIVGQTNKKLDTVQKAHKRSH
Protein: Syntaxin-21 (AtSYP21) (PEP12 homolog) (AtPEP12) (aPEP12) (Q39233)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function in the docking or fusion of transport vesicles with the prevacuolar membrane.
Subcellular location: Prevacuolar compartment membrane {ECO:0000269|PubMed:9144962}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9144962}.
Interaction partners:
- Vesicle transport v-SNARE 11
- VAMP-like protein YKT61
- Syntaxin-51
- VAMP-like protein YKT62
- Syntaxin-61
- Syntaxin-52
- Vesicle transport v-SNARE 12
- Vesicle transport v-SNARE 13
- Golgi SNAP receptor complex member 1-2
- Membrin-11
Sequence:
MSFQDLEAGTRSPAPNRFTGGRQQRPSSRGDPSQEVAAGIFRISTAVNSFFRLVNSIGTPKDTLELRDKLQKTRLQISELVKNTSAKLKEASEADLHGSASQIKKIADAKLAKDFQSVLKEFQKAQRLAAEREITYTPVVTKEIPTSYNAPELDTESLRISQQQALLLQSRRQEVVFLDNEITFNEAIIEEREQGIREIEDQIRDVNGMFKDLALMVNHQGNIVDDISSNLDNSHAATTQATVQLRKAAKTQRSNSSLTCLLILIFGIVLLIVIIVVLV
Protein: Structural maintenance of chromosomes protein 5 (Q7YU66)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGDRALSSKQLAGRIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRVYGRTPNTTETFRRIINSNGLSTFSVNDKDTSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFSKMNPQELLLNTMSSVCDEDLINSFNSLKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQKLQVYSAKKLWVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLPSQEQIEKEKESLRKALLEKTRLLENAVAEKAAIDGKMDSLKQGIYQKKYELEQNIKKSRRTATECDNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEMIPEITAYKLKIERLRNVKMQKIDEIRAKNPNLVVAMNWLAQNKQRYKLNVYDPMILELTVQNHEDAKFLENVVAQRDLFAFACEDKGDMSDLINELCVKQKLGVNVIYCAPSDRLVYSPKTPIDDLRSFGFRSYLVDLVTGPIPLINKLCASYSIHNIPIGTEAVGNYTSSIPKAIRVYFGGSKKFVVTASRYRSDTILTESSIRAKNQLITVDSQQLALVMKQCSEAVKESDSIKNAITQTDNEFERLQAVAKDEQEKRRKLDQKIAHFNSLKTEIETLQKKLEALRNSDSLDCLETNFCNSLHKDLKKIFDADAELCSCLKAIDRLIIEKNMAQTKVSIYMLQHETQIEALKESEEQSKAATRDFQQLLQCLENQISDVNKRKSAIQGLCHGEIPTSSKFPFKKEFRELENIDLPELREAIHDFQARLECMKSVNSEAISSYQGLQNEVKQLEEGIQESVNQAKSIESGMSNLYDKWEPKLNSLVETISTKFSEFMESIEYVGEVVLSKTDKYDFDSYGIQIMVQFRRGLQLQPLDKFIQSGGERAVSIAIYSLSLQHVTHVPFRCVDEINQGMDATNERHIFDLLLKEATKHGSAQYLFVTPKLLRDLNYNEHLCVSIVHNSKTVCHGMQFPMA
Protein: ATR-interacting protein mus304 (Mutagen-sensitive protein 304) (Q9VVN4)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA damage checkpoint protein required for chromosome break repair and for genomic stability during development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10733527}.
Interaction partners:
- Serine/threonine-protein kinase ATR
- Serine/threonine-protein kinase grp
- Serine/threonine-protein kinase ATM
Sequence:
MAKRFSAMKDFARCKKPRLDVSVTRGSARPSPPRNNFDGILWDDDDDVILMATQLAEAEIEAEERKKKGGTEVDIGNSEVTFSEFAPTFQGSTSTQQMFPPPPPPQKKPTSLDMDAIFADDDDFDFLAVTLMDSEPQKMPEPKTSTSRITTSSISVQQKTTTTTTINATQSRQQEHQLKFLMDRIEALKRENAQLEKNLGDSKERNEIKSGEVSLLRDELKHLRQQLQASKMEKLALADETNRDCNKKVAEAAKQIAAKDIELKIKNAEFSKLKTQQKAHERSMNSSMSILQAAPDPLEKRLSLRLNRLNIHRSVPGLKTDNGSVFEYSENEDQTKKRRNHFELELKQLLLHYARLQAKPESVDNLLPRILSSVGKVFTEFASYAQSLDFPHNCMLYPYNPHNLEEEVHRISLTHQSCLYDNEKAVPLRRFIATLALICRREERISRGLTEWKENDLGLLDMAIEAITKLGFSYEVGQHFGLLEALTSLLNSLLQENALLQHNEELLFDLLKQLVFTRPSPWVFAELSSCFLSCLRHPQLMDKMCVNSPKDCFVSDRVRSVYRFGPDSCLLQVYAGLLELCFFSETPLRQDYFQLLLKIGGNHVRFAFECFKNPPDFILEMLPYFADDGDEDSSDGTLMKTGTSLSFNSTGAVQGSVSNGSTSASVSNPNQNSNSSTTQRGKGCECYVKLCLSAVTIVFQVMHQWMLHSRKAGTEEVGEISRIAVHLLSLVFHEYYLTCLFRDSEETTKHYLSLICNWWSEHANLLGFQSIHLRLLNQLVKAHFMLKPLHLEAKPNNPVNDLSEWKRIVKNADDQRAVKSAVTVDPSKLLNTDFFSALKREENTFE
Protein: Myb domain protein 4r1 (Putative transcription factor) (Q9LV31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Gb|AAC33480.1
Sequence:
MNRNSLYEADDDDDDDEEDDIGEDLEDLRRACMVSDVNSDQFASKTGSIEPEGVGGGEIPSDSENEDDFEMLRTIKSQLASSKDAGRSSGPPMGLSLLSDSESEDDFEMIRSIKSQLSLSMDVSLPPIGLSDDEEDDAFETLRAIRRRFSAYKNFDSEGKFMNDSHGKKKQVHNSDNEPSSEILSRSNTCESFPDHGKSVVTVPDSEDVQDGHMPAASSSFPEAARAFVDAIRRNRAYQKFLRGKLAEIEATIEQNEKHKKNVRIVKDFQASCKRITKLALCQRKDPRVELISTRKSGPCDSSEVIGPCDSFEGNDKKISPLTLGPAENPCVENYRMALEKYPISVKRRKWSTEENKNLAKGLKQEVQKILLSEAIERSSDLEGATYDIDTINESIGNLEITPEMIRQFLPKINWDSLDIKDRSAAECEARWMSSEDPLINHGPWTAAEDKNLLRTIEQTSLTDWVDIAVSLGTNRTPFQCLARYQRSLNPSILKKEWTAEEDDQLRTAVELFGEKDWQSVANVLKGRTGTQCSNRWKKSLRPTRKGTWSLEEDKRVKVAVTLFGSQNWHKISQFVPGRTQTQCRERWLNCLDPKVNRGKWTEEEDEKLREAIAEHGYSWSKVATNLSCRTDNQCLRRWKRLYPHQVALLQEARRLQKEASVGNFVDRESERPALVTSPILALPDISLEPEPDSVALKKKRKAKQKKSDAERQPKRRRKGLKNCSGDVCRQENETVCENEPNNGGEERMLALECHDEIQDNAKEKPKQRRKSVAETVCENEPNNGGEERMLALECDNEIQDNAKEKRKRRRKSVAETSNNTTGLKKLTPRRRKISAVVPIKNQDAPN
Protein: GTPase grn1 (GTPase in ribosomal export from the nucleolus protein 1) (Nuclear GTP-binding protein grn1) (O74791)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for optimal growth. Required for normal processing of ribosomal pre-rRNA. Required for nuclear export of ribosomal protein rpl2501.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16251348, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pescadillo homolog
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome biogenesis protein erb1
- Probable nucleolar GTP-binding protein 1
- Ribosome assembly factor mrt4
- 25S rRNA
- Nucleolar GTP-binding protein 2
- Probable rRNA-processing protein ebp2
- ATP-dependent RNA helicase has1
- Ribosome biogenesis protein nsa2
Sequence:
MVSLKKKSKRRTTRLRSRIEKKAAESKRKQKRADKKNPQWKSRIPKDPGIPNSFPYKDKILAEIEEQKRIREEEKLARRASGQVDAAMEEEDAVDENGSLMISKIAEAAQASNPDDEEEFVMEEDNLGEAPLLVDSESYEASVKADTSRKAYDKEFKKVVEASDVILYVLDARDPEGTRSKDVERQVLASSAEEKRLIFVINKIDLVPSEVLNKWVTYLRNFFPTIPMRSASGSGNSNLKHQSASASSTISNLLKSLKSYSAKKKLKSSLTVGVIGYPNVGKSSVINALVNRSANGRSAPCPAGNVAGMTTSLREVKLDNKLRLVDSPGIVFPSSDSKDDLYRLVMLNAVSSTKVDDPVAVASYILQFLSRVPGQLERMFQRYELPPLLNTSDIDTATDFLVNIARKRGRLGRGGIPNLNAAANIVINDWHAGRIEWWAEPEVINEKNSSEVQDTQIVTEWAKEFDLNDF
Protein: 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase (EC 3.6.1.62) (A0A8I6APY3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MELLSRAEQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVVEEEARRAQQAARDKQSPSQANGCSDQRPIDILEMLSRAKDEYERSAPSGHKHLTVEELFGTSLPKEQPAPMGLESEDTDKLLGDAPQKEPSSFLPFPFEQSGGAPQAENLGVHSVTHHTVQPEVSAPVLITPASIAQSGDKHPPSYTLPLSPVLSPTLPAEAPTTQVPHLPRNSTMMQAVRTTPRQKSPLLNQPVPELSHSSLIASQSPFRAPVSLANTAGTAIPSSDLLQKLRLTPQHDQIQAQPLGKGAMAPNFSSAAGQLATPESFIEPSSKTAAARAAVAASLSNMVLAPTLQSMQQNQDPEVFAQPKVLPSAIPIAGPPLVTATTTAVSSVLLSPSVFQQTVPRSADLERKASCPSPLTIGAENQRKPSIILSRSQLQDTLIHLIKNDSGFLSTLHEVYLQVLTKSKDNHSL
Protein: Peptidoglycan-recognition protein SB1 (EC 3.5.1.28) (Q70PY2)
Organism: Drosophila melanogaster (Fruit fly)
Function: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN), preferentially DAP-type PGNs. Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments.
Subcellular location: Secreted {ECO:0000269|PubMed:11106397}.
Interaction partners:
- Attacin-C
- Diptericin B
- Metchnikowin
- Diptericin A
- Attacin-A
- Peptidoglycan-recognition protein SD
- Drosocin antimicrobial peptides
- Cecropin-C
- Elevated during infection
- Cecropin-B
Sequence:
MNTSTAISFVAALVLCCLALSANALQIEPRSSWGAVSARSPSRISGAVDYVIIHHSDNPNGCSTSEQCKRMIKNIQSDHKGRRNFSDIGYNFIVAGDGKVYEGRGFGLQGSHSPNYNRKSIGIVFIGNFERSAPSAQMLQNAKDLIELAKQRGYLKDNYTLFGHRQTKATSCPGDALYNEIKTWPHWRQN