wanglab/gogpt-training-data huggingface dataset:
Protein: CDC42 effector protein 3 (C9JEZ4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
Sequence:
MPAKTPIYLKAANNKKGKKFKLRDILSPDMISPPLGDFRHTIHIGKEGQHDVFGDISFLQGNYELLPGNQEKAHLGQFPGHNEFFRANSTSDSVFTETPSPVLKNAISLPTIGGSQALMLPLLSPVTFNSKQESFGPAKLPRLSCEPVMEEKAQEKSSLLENGTVHQGDTSWGSSGSASQSSQGRDSHSSSLSEQYPDWPAEDMFDHPTPCELIK
Protein: Tetratricopeptide repeat protein 28 (Q19955)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- PIPK domain-containing protein
- Guanine nucleotide-binding protein G
- Disks large homolog 1
- Protein inscuteable homologue C-terminal domain-containing protein
- Guanine nucleotide-binding protein alpha-16 subunit
- MAGUK p55 subfamily member 5
- PDZ domain-containing protein
- Probable delta-1-pyrroline-5-carboxylate synthase
- G-protein alpha subunit activating protein gbas-1
- G-protein regulator 1
Sequence:
MQDRSCYKLTQEGERLFRMQKYEKGIDLLKKALEVGTDDFSLLSAIYCQLGNAHTMLKDYEQALKFHTYDILVERLLGNKEGEAKSCANLGNIFKMKGAYNDALTFTFKQLDFAEELGDRVLKSRAYYNIATIYVERGRCTKLEAAEEKNDAKNAEATSDFENAAKYFMLNLEMSEKSEDALTMGRCYGSLGNTYYCLGDYDQSIHFHKLRLELSQQYGDRASMRRAHANIANCHALKSNMPLAIQHYKLAYNLAIEIGNKTEEAQMAYSLANALYIGKEVQKAITYFQRHLKIARSLEDISGQLRSYYSLALSFNNLCERRKALYFLVLAKRSSLQVNDTSALTDIDNLLNEILEAGQEDVLVDDIELIIDESADPAPADIEHRELRLTYFQKRNIHDKPVNTPEDPLAEDRYEKEEFFDMLAKLQSKRMNDQRVDASVLSSNLDFRVRQVDTEPDNSSTDGSEVLIDLLLNAQGRRMDDQRAPFLPGLNPNGQIILRRLNTDPGNEELDEHLVEWLMRVQGERLDEQRSELPPIKPEGQEEVDKKKEEDVTAIVMRMQAGRLEDQRAHLPNIPTSKN
Protein: GPI inositol-deacylase (EC 3.1.-.-) (Post-GPI attachment to proteins factor 1) (hPGAP1) (Q75T13)
Organism: Homo sapiens (Human)
Function: Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI-anchor transamidase
- GPI-anchor transamidase component PIGT
- GPI-anchor transamidase component GPAA1
- GPI-anchor transamidase component PIGS
- GPI-anchor transamidase component PIGU
- Transmembrane emp24 domain-containing protein 10
- Complement decay-accelerating factor
- GPI-specific phospholipase A2-like PGAP3
- Urokinase plasminogen activator surface receptor
- Acyltransferase PGAP2
Sequence:
MFLHSVNLWNLAFYVFMVFLATLGLWDVFFGFEENKCSMSYMFEYPEYQKIELPKKLAKRYPAYELYLYGEGSYAEEHKILPLTGIPVLFLPGNAGSYKQVRSIGSIALRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKTILKLYKGQEFAPKSVAIIGHSMGGLVARALLTLKNFKHDLINLLITQATPHVAPVMPLDRFITDFYTTVNNYWILNARHINLTTLSVAGGFRDYQVRSGLTFLPKLSHHTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTVRAFFDLIDADTKQITQNSKKKLSVLYHHFIRHPSKHFEENPAIISDLTGTSMWVLVKVSKWTYVAYNESEKIYFTFPLENHRKIYTHVYCQSTMLDTNSWIFACINSTSMCLQGVDLSWKAELLPTIKYLTLRLQDYPSLSHLVVYVPSVRGSKFVVDCEFFKKEKRYIQLPVTHLFSFGLSSRKVVLNTNGLYYNLELLNFGQIYQAFKINVVSKCSAVKEEITSIYRLHIPWSYEDSLTIAQAPSSTEISLKLHIAQPENNTHVALFKMYTSSDCRYEVTVKTSFSQILGQVVRFHGGALPAYVVSNILLAYRGQLYSLFSTGCCLEYATMLDKEAKPYKVDPFVIIIKFLLGYKWFKELWDVLLLPELDAVILTCQSMCFPLISLILFLFGTCTAYWSGLLSSASVRLLSSLWLALKRPSELPKDIKMISPDLPFLTIVLIIVSWTTCGALAILLSYLYYVFKVVHLQASLTTFKNSQPVNPKHSRRSEKKSNHHKDSSIHHLRLSANDAEDSLRMHSTVINLLTWIVLLSMPSLIYWLKNLRYYFKLNPDPCKPLAFILIPTMAILGNTYTVSIKSSKLLKTTSQFPLPLAVGVIAFGSAHLYRLPCFVFIPLLLHALCNFM
Protein: Small acidic protein (Q383T2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSLKSVARELREFAAGLADSRGVQSEELTSRQDALLLLALSALKELETSGSPADLAQAAKSARRLLRVFLPHPVVEKGQSLEYEQQDSERPSRKRERESKDDTGKAEKEESDNVSVDLGQYAKAHVFDDNAKKRDKFARLMGGRRNEGSHHNTFAPDKTTIKRINGELEEQFNNALVRSGRKGLGA
Protein: Uncharacterized protein YbfB (P0AAU5)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- L-rhamnose mutarotase
- Uncharacterized protein YjaH
- Hydroxycarboxylate dehydrogenase B
- Protein RhsC
- Uncharacterized protein YbfA
- Uncharacterized protein YbfC
- Protein YdeP
Sequence:
MKYIIFLFRAIWLALSLLILFFSMHRLSLLDSTRDVSELISLMSYGMMVICFPTGIVFFIALIFIGTVSDIIGVRIDSKYIMAIIIWLYFLSGGYIQWFVLSKRIINK
Protein: At4g25580/M7J2_50 (CAP160 protein) (Q8RY15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT1G27990 protein
- non-specific serine/threonine protein kinase
- Casein kinase 1-like protein 10
- non-specific serine/threonine protein kinase
- Cytochrome P450, family 702, subfamily A, polypeptide 8
- Calcineurin-like metallo-phosphoesterase superfamily protein
- Protein kinase superfamily protein
- Phosphoglycolate phosphatase
- Transmembrane protein
- Uncharacterized protein
Sequence:
MDSQAQLQRTHGHHQAQEPIRIHHPEEEGHHEKGPSKVLKKVKEKAKKIKNVLTKHGHGHEHDRGEHIPDDHDLDQEDDEDDYNDNQLHGGAPARGKAHIPVKEEIVPPGSKAFPVVSSSHTKPSEPVRGVGHEAMSRPIKHSGVPEKEERRGAPTLTPHNTPVSLLSATEDVTRTFVPDEHKSRNQSKVNIDRPKGLDQDPAAPGSHGGLSNYQSKVTDPIGKSTGEIGAASTVSAIGRLGLGTDLQKKSHGLDTKPTAQGSHGGMSSYQSKVTDPTGKGAGEQPSVAAFGRRNETGEDDHMGLGRDLREKSHGFDTKSRPEMGKHIPAGDYGSRLGKESPERSDEFDLGKDLPTRTQGIQNPQGFDSRGQRRGEEMHQPNQSSYTDKISLATSVVADKAVAAKNAVASKLGYSGEGGHENRVEGAENPSSAGGYGSTVASMVTPVYEKVKETGASVMTKLPFTGTGTEQGQDRGVSAKEFLTEKLSPGEEDKALSEVVTEKLHLGGGGGETAPPKRGIVTQSEEVEKRLGGFKDPSSEAATKQGEAYAEKGEGGIAEKLRGAVTSWIAGTTEEVTQKSTESVQDSTQSLGSTIGNKMGITGSGGGEAGQQGSMPLQKRFQESGN
Protein: Kinesin light chain (Q8CD76)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367020}.
Interaction partners:
Sequence:
MYDNMSTMVYIKEEKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSSMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDSDSSKEPLDDLFPNDEDEPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALGIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGSAFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPESMEKRRSRESLNMDVVKYESGPDGGEEVSMSVEWNGDGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRDSEPRNPGASPAEPLCVENDSSSLEDASTN
Protein: At2g20330/F11A3.12 (Putative WD-40 repeat protein) (Transducin/WD40 repeat-like superfamily protein) (Q9SK69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transducin/WD40 repeat-like superfamily protein
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-processing factor 19 homolog 2
- Pre-mRNA-processing factor 17
- Initiation factor eIF-4 gamma, MA3
- At1g80930/F23A5_23
- Peptidyl-prolyl cis-trans isomerase CYP65
- At3g05070
Sequence:
MEDELEGLRAHFPVSFGKTSKVSASTEAIHSATRRTDVANDAGVSSDITTKKPDSDKSGFPSLSSSSQTWLRSVRGPNRNPNSSGDVAMGPPPPPSSKRTQEEEEEDEEVMMGPPPPPKGLGNINDSDDEGDMIGPPPPPPAARDSDEDSDDDDDNDNEENRYQIPLSNEIQLKGHTKIVSSLAVDSAGARVLSGSYDYTVRMYDFQGMNSRLQSFRQIEPSEGHQVRSVSWSPTSGQFLCVTGSAQAKIFDRDGLTLGEFMKGDMYIRDLKNTKGHICGLTCGEWHPRTKETVLTSSEDGSLRIWDVNNFLSQTQVIKPKLARPGRVPVTTCAWDRDGKRIAGGVGDGSIQIWSLKPGWGSRPDIYVGKAHTDDITSVKFSSDGRILLSRSFDGSLKVWDLRQMKEALKVFEGLPNYYPQTNVAFSPDEQIILTGTSVEKDSTTGGLLCFYDRTKLEIVQKVGISPTSSVVQCAWHPRLNQIFATSGDKSQGGTHILYDPSQSERGACVCVARAPRKKSVDDYQPEPVIHNPHALPLFRDAPSRKREREKALKDPMKSHKPEIPMTGPGHGGRVGTTGSGLLTQYLLKQGGMIKETWMEEDPREAILKYAEVAVKDPKFIAPAYSQTQPKTIFAKSDDEEEEGDTKK
Protein: Calcineurin-like metallo-phosphoesterase superfamily protein (F4JPS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVSERHSARLYNSLPMESFRTILTHTYPYPHEHSRHAIIAVLFGCLFFISSDNMQTLIEKFSVKWWSMYACLLGFFYFFSSPFIQKTIRPNYSNFSRWYIAWILVAALYHLPNFQSMGLDLRMNLSLFLTIYISSILFLVVFHIIFLGLWYVGLVSRVAGRRPEILTILQNCAVLSMACCIFYSHCGNRAVLRQKPLGRQYTSWFSFWKREHRHNTWLAKFIRMNELKDQVCSSWFAPVGSASDYPLLSKWFIYGEIACNGSCPDSADEISPIYSLWATFIGLYIANYVVERSTGWALTHPLSVDKYEKLKNQQLKPDFLDMVPWYSGTSADLFKTVFDLLVSVTVFLGRFDMRMLQAAMTKSGDASGRKELLYDHLAEKQDFWFDFMADTGDGGNSSYSVAKLLAQPSLRVPVANNFISLPRGNVLLIGGDLAYPNPSSFTYEKRLFCPFEYALQPPRWYKNDSIAVDKPELPNGVSDLKSYEGPQCFLIPGNHDWFDGLNTFMRYICHKSWLGGWLMPQKKSYFALQLPKGWWVFGLDLALHGDIDVDQFKFFSELVKDKVGESDAVIIITHEPNWLLDWYWSGDTGQNVRHLICDVLKYRCKLRMAGDLHHYMRHSCNQSDGPAHVQHLLVNGCGGAFLHPTHVFSKFSKFYGASYGSKVAYPSFDDSSKIALGNILKFRKKNWQFDFIGGIIYFILVFSLFPQCKLAHVLRGDSFSGHLESFLGTVWSAFAYVMEQSYVSFTGVLMLLITAITFVPSKVSLKKRVVIGVLHVAAHLMAALILMLMLELGIEICIQHNLLANSGYHTLYEWYKSVENEHFPDPTGLRARIEQWTFGLYPACIKYLMSAFDVPEVMAVTRTNICKHGMESLSRSGAVIYYASVFLYFWVFSTPVVSMVFGSYLYICINWFHIHFDEAFSSLRIANYKSFTRFHILEDGDIEVFTLAVDKVPKDWKLDKDWDSEPKQSFKMSYEREFPSKWGASTSQQDPVNTVKIVDRFVIHRSQKENGEC
Protein: Pre-histone-like nucleoprotein (Pre-core protein VII) (pVII) [Cleaved into: Histone-like nucleoprotein (NP) (Core protein VII)] (P68951)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Plays a role in the inhibition of host immune response within the nucleus. Interacts with cellular nucleosomes and immobilizes the host immune danger signal HMGB1 on chromatin. In turn, prevents HMGB1 release out of the cell and thus decreases inflammation. Also plays a role in the wrapping and condensation of the viral DNA. May also promote viral genome import into the nucleus.
Subcellular location: [Histone-like nucleoprotein]: Virion {ECO:0000255|HAMAP-Rule:MF_04056}. Note=Located inside the capsid in association with the viral DNA (core). Present in about 1070 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04056}.; SUBCELLULAR LOCATION: [Pre-histone-like nucleoprotein]: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04056}.
Interaction partners:
Sequence:
MSILISPSNNTGWGLRFPSKMFGGAKKRSDQHPVRVRGHYRAPWGAHKRGRTGRTTVDDAIDAVVEEARNYTPTPPPVSTVDAAIQTVVRGARRYAKMKRRRRRVARRHRRRPGTAAQRAAAALLNRARRTGRRAAMRAARRLAAGIVTVPPRSRRRAAAAAAAAISAMTQGRRGNVYWVRDSVSGLRVPVRTRPPRN
Protein: NF-kappa-B essential modulator (C9JH59)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEG
Protein: LEK1 (Q9QZ84)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
SQETMLRDLQEKLNQQENSLTLEKLRLALADLERQRNCSQDLLKKREHHIDQLNNKLNKIEKEFETLLSALELKKKECEELKEEKNQISFWKIDSEKLINQIESEKEILLGKINHLETSLKTQQVSPDSNERIRTLEMERENFTVEIKNLQSMLDSKMVEIKTQKQAYLELQQKSESSDQKHQKEIENMCLKANKLTGQVESLECKLQLLSSEVVTKDQQYQDLRMEYETLRDLLKSRGSSLVTNEDNQRSSEDNPRSSEDNQRGSLAFEQQPAVSDSFANVMGRKGSINSERSDCSVDGGRSPEHIAILQNRVTSLESSLESQNQMNSDLQMRCEELLQIKGEVEENLSKAEQIHQNFVAETNQCISKLQEDAAVHQNIVAETLATLESKEKELQLLKEKLEAQQTEVQKLNKNNCLLEGTLKELQLLSDTLSSEKKEMNSIISLSKKNIEELTQANEALKEVNEALEQEKMNLLQKHEKITSCIAEQERSIAELSDQYKQERLQLLQRCEETEAVLEDLRGNYKTAQENNAKLECMLSECTALCENRKNELEQLKETFAKEQQEFLTKLAFAEEQNRKLMLELEIEQQTVRSEITNTNKHSMSATDGLRQECLTLNEEQNEQQNEVSNLTHENEQLMELTQTKHDSYLAVEPVENSVKATEDEIGKSSSQYQMDIDTKDISLDSYKAQLVHLEALVRILEVQLDQSEEENKKLHLELQTIREELETKSSQDPQSQARTGLKDCDTAEEKYVSMLQELSASQNENAHLQCSLQTAVNKLNELGKMCDVLRVEKLQLESELNDSRTECITATSQMTAEVEKLVSEMKMLNHESALSQNELMKDTSGGEFHDKANHSSVFLTPLDSSNFCEQMTLSSKEVRVHFAELQEKFSCLQSEHKILHDQHCEVSSKMSALRSYVDTLKAENSALSMSLRTLQGDLVKEGEPAAEGGHGLPLSFCGADSPSLTNFGETSFYKDVLEQTGDTCHLSLEGNASANSCDLDEEFSSSLEEETLTEKESPPAPGRTVEGLEVLCQVYLQSLKNLEEKTESQRIMKKKEIEELEQLLSSERKELSCLRKQYLSEKEQWQQKLTSVTLEMESKLAEEKQQTKNLSLELEVARLQLQELDLSSRSLLGTDLESVVRCQNDNYDIKESEVYISETTEKTPKQDTDQTCDKDIQQDLGLETSVTESETTRLTGEGCEEQPPKTNCEAPAEDKTQDCSECISELCSSSNVLVPMDVLEDQGSIQNLQLQKDTLNENLRFLPEVEDWDKKVESLLNEIMEADSKLSLQEVQLKMKIATCIQLEKIVKDLRKEKADLSEKLESLPCNQEVCLRVERSEEDLGFNLDMGANELLSKSTKDNATNTEDNYKEKFLDMERELTRIKSEKANIEHHILSVETNLEVVQAEKLCLERDTESKQKVIIDLKEELFTVISERNRLREELDNVSKESKALDQMSKKMKEKIEELESHQRESLRHIGAVESEVKDKADLIQTLSFNVGELTKDKAHLQEQLQNLQNDSQELSLAIGELEIQIGQLNKEKESLVKESQNFQIKLTESECEKQTISKALEVALKEKGEFAVQLSSAQEEVHQLRRGIEKLSVRIEADEKKHLSAVAKLKESQRESDSLKDTVETLERELERSEENQELAILDSENLKAEVETLKAQKDEMTKSLRIFELDLVTVRTERENLAKQLQEKQSRVSELDERCSSLRRLLEEKEQARVQMEEDSKSAMLMLQMQLKELREEVAALCNDQETLKAQEQSLDQPGEEVHHLKSSIRKLKVHIDADEKKHQNILEQLKESKHHADLLKDRVENLEQELILSEKNMIFQAEKSKAEIQTLKSEIQRMAQNLQDLQLELISTRSENENLIKELKKEQERVSDLETINPSIENLLKDKEQEKVQMKEEAKITVEMLQTQLKELNETVVSLCNDQEVSKTKEQNLGSQVQTLELEKAQLLQDLGEAKNKYIIFQSSVNALTQEVEAGKQKLEKGEKEIRTLKEQLKSQEQLVCKLAQVEGEQELWQKQKLELRNVTMALEQKVQVLQSENNTLQSTYEALQNSHKSLESELGLIKLEKVALVERVSTISGKEAELQRELRDMLQKTTQLSEDYNKEKNRLTEEVEVLREELQNTKAAHLKSVNQLEKELQRAQGKIKLMLKSCRQLEGEKEMLQKELSQLEAAQQQRAGSLVDSNVDEVMTENKALKETLEEKVKEADKYLDKYCSLLISHEELEKAKEILEIEVARLKSRQSRQDLQSSPLLNSSIPGPSPNTSVSEMKSASGQNKASGKRQRSSGVWEHGKRAAPSTAETFSKKSRKSDSKSTRPAEHEQETEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSPRFATQKLVGSSPSLGKENVVESSKPTAGGSRSQKVKVVQESSADSHTAFQELPAKSLTASNIPGRNSTESPREGLRAKRAYPASSPAAGPDPTNNENCRVQ
Protein: Solute carrier family 15 member 5 (A6NIM6)
Organism: Homo sapiens (Human)
Function: Proton oligopeptide cotransporter.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Na
- Na
- Solute carrier family 13 member 2
Sequence:
MSVTGFTITDEKVHLYHSIEKEKTVRHIGDLCSSHSVKKIQVGICLLLVELCERFTFFEVVCNMIPFCTIKLGYHNCQAAILNLCFIGTSILTPVFVRWLTDVYLGRNKLVYICLFLHFLGTALLSVVAFPLEDFYLGTYHAVNNIPKTEQHRLFYVALLTICLGIGGVRAIVCPLGAFGLQEYGSQKTMSFFNWFYWLMNLNATIVFLGISYIQHSQAWALVLLIPFMSMLMAVITLHMIYYNLIYQSEKRCSLLTGVGVLVSALKTCHPQYCHLGRDVTSQLDHAKEKNGGCYSELHVEDTTFFLTLLPLFIFQLLYRMCIMQIPSGYYLQTMNSNLNLDGFLLPIAVMNAISSLPLLILAPFLEYFSTCLFPSKRVGSFLSTCIIAGNLFAALSVMIAGFFEIHRKHFPAVEQPLSGKVLTVSSMPCFYLILQYVLLGVAETLVNPALSVISYRFVPSNVRGTSMNFLTLFNGFGCFTGALLVKLVYLISDGNWFPNTLNKGNLESFFFFLASLTLLNVLGFCSVSQRYCNLNHFNAQNIRGSNLEETLLLHEKSLKFYGSIQEFSSSIDLWETAL
Protein: Riboflavin transporter (Q8SYL6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368035}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368035}.
Interaction partners:
Sequence:
MSRYHRGRGAGSPTNPAGPVYGVISTLDDATPSPADFARCSSLEAKKSELSLFLNWGGPQKNMEISSKLRNRSWLVDVLAIFFGIGTWLGVNGTFIQLPLLVDEAPEGWGLPSYLSVMVQIGNLGPLLYTAIQKYSPKKLNDGWTIHGVLLVRAISCLLTAFFYNQTASVAGTDHSLALFLLTCFTALNACTSSVLFMPYMGRFKEQYMVTYFIGEGLSGLLPSVTALIQGIGESGDCVLVNVTESGEEVYALRKTPPRFDTRVFFLILFALMVLAYVGYALLNSLPLARREYAQVTVSEGNKYVYGEADNQPKAEKLSKGQYTYLLLLIGAISLFSNGMFGSIQSYSSAPYGSQAYHLAATLSVIANPVACFMAMFLHLPPCGLSRCSLSLRVC
Protein: DnaK suppressor, putative (O51190)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase, omega subunit
- Translation initiation factor IF-1
- Haloacid dehalogenase-like hydrolase
- IPT/TIG domain protein
- Haloacid dehalogenase-like hydrolase
- RNA polymerase sigma factor RpoD
- RNA polymerase sigma factor
- DNA-directed RNA polymerase subunit alpha
- Transcription elongation factor GreA
Sequence:
MQKAVSEHEFIEEIKKFLSAEKREILDSIKSVENSKKEIINNDMYPKDVVDIAFDNMDGNNLEALGFVEKRKLNLINQALYRISQNSYGKCLACEREIARERLLAIPYAFLCISCQTKKEKKNKR
Protein: Chromosome-anchoring protein RacA (P45870)
Organism: Bacillus subtilis (strain 168)
Function: Required for the formation of axial filaments and for anchoring the origin regions at the cell poles in sporulating cells, thus ensuring proper chromosome segregation in the prespore. Binds in a dispersed manner throughout the chromosome but preferentially to sites clustered in the origin portion of the chromosome, causing condensation of the chromosome and its remodeling into an elongated, anchored structure.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12493822}. Note=Localizes to cell poles and nucleoid, in a DivIVA-dependent manner.
Interaction partners:
- Septum site-determining protein DivIVA
- Stage 0 sporulation protein J
- Cell division topological determinant MinJ
- Stage II sporulation protein E
- Sporulation initiation inhibitor protein Soj
- Post-transcriptional regulator ComN
- Serine/threonine-protein kinase YabT
- Septum site-determining protein MinC
- DNA translocase SpoIIIE
Sequence:
MNTNMVASELGVSAKTVQRWVKQLNLPAERNELGHYSFTAEDVKVLKSVQKQISEGTAIQDIHLPKSAKKRTGFLVQKTSSDTERRIEQLEQKLDTLLQQRQDESELMARMSELERQLKQKADEGVSYQLLQHRREIDDILADLQSLTSQMKEFTAHSIPETAAASEKTKTRKKPLLSLFKFQT
Protein: Wee1-like protein kinase (EC 2.7.10.2) (Q6DRI0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR037281}.
Interaction partners:
Sequence:
MSFGAGRHGKSPNLKPVRQKLQFSTSDGEEDSIEDANNSTGAESGFTELDSPVPLRRSLEKRPEDLGNSSPLSRNRDDDESWDEEGFGSPSRVKPAFYMKSSPSPRKSPPAYDSSPERSYIHDDMEGCSSPIPDCPDTPPHKTFRKLRLFDTPHTPKSLLSRARTMGSTSRRVALFTNVDSTSKACLDGKRNQTPRVNINPFTPDSILVQSSTLQRNNRKRSHWNDSCGEDMDASDAEIEDELIPPSKRITMMENNMMSRYASEFHELEKNGSGQFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYYSAWAEDDHMLIQNEYCNGGTLSDVIAENNRRMHFLSELELKDLLLQVSRGLKYIHSTALVHMDIKPSNIFISRKPAASVEEFEDEEDGPTTNVVYKIGDLGHVTTVTNPQVEEGDSRFLANEVLQEDYSNLKKADIFALALTVVSASGAEPLPTNGDKWHKIRQGILPHIPQVLSQEFLSLLKLMIHPDPTRRPSTSELVRHPVLLTASRMSADQLRVELNAEKFKNALLQKELKKAQMAKAAAEERVLTTDRVLTRSTIQSSSRASRLIGKKMNRSVSLTIY
Protein: Protein LAZY 4 (AtLAZY4) (Protein DEEPER ROOTING 1) (AtDRO1) (Protein LAZY1-LIKE 3) (Protein NEGATIVE GRAVITROPIC RESPONSE OF ROOTS 2) (AtNGR2) (Q5XVG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of root gravitropism. Functions redundantly with LAZY2 and LAZY3 in the control of root gravitropism. Involved in the development of the root system architecture by influencing lateral root angles and primary root length. Functions redundantly with LAZY1, LAZY2 and LAZY3 to control plant architecture by coupling gravity sensing to the formation of auxin gradients. Involved in the establishement of auxin gradient in primary and lateral roots upon gravitropic stimulation. Involved redundantly with LAZY1 and LAZY2 in the regulation of both shoot and root gravitropism. Mediates gravity signaling in statocytes downstream of amyloplast displacement, leading to the generation of asymmetric auxin distribution in gravity-responding organs. Regulates the direction of polar auxin transport in response to gravity through the control of asymmetric PIN3 expression in the root cap columella. Regulation of auxin flow by the three proteins LAZY1, LAZY2 and LAZY4 in statocytes influences plant architecture by controlling the growth angle of lateral shoots and lateral roots.
Subcellular location: Nucleus {ECO:0000269|PubMed:32130643}. Note=Localizes in the nuclei of cortical and endodermal tissues near root tips in both primary and lateral roots. {ECO:0000269|PubMed:32130643}.
Interaction partners:
Sequence:
MKFFGWMQNKLHGKQEITHRPSISSASSHHPREEFNDWPHGLLAIGTFGNKKQTPQTLDQEVIQEETVSNLHVEGRQAQDTDQELSSSDDLEEDFTPEEVGKLQKELTKLLTRRSKKRKSDVNRELANLPLDRFLNCPSSLEVDRRISNALCDEKEEDIERTISVILGRCKAISTESKNKTKKNKRDLSKTSVSHLLKKMFVCTEGFSPVPRPILRDTFQETRMEKLLRMMLHKKVNTQASSKQTSTKKYLQDKQQLSLKNEEEEGRSSNDGGKWVKTDSDFIVLEI
Protein: 1-deoxy-11-beta-hydroxypentalenate dehydrogenase (EC 1.1.1.340) (Neopentalenolactone biosynthesis protein F) (Q82IY9)
Organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Function: Catalyzes the oxidation of 1-deoxy-11-beta-hydroxypentalenic acid to 1-deoxy-11-oxopentalenic acid in the biosynthesis of neopentalenolactone antibiotic.
Interaction partners:
Sequence:
MHLQPSTAVVTGAASGIGFALSARLAQAGARVVMTDIAGDGLAGAVEELAAHGADVTAVVADLTDPAAVQELADTAFGRLGDIDVVCNNAGVVGPVGMPLWSVPLDEMHAVFDVNYWAHVHVARAFVPRLLDSGRPSHLVQTASMSAFVVGAGTASYAASKHADLAAARSLRADLDGTPVRVSVLCPGRVDTPMTRGLVAPRNATGNTTISADEAADAVWNALGSDRFYIFTNADAQTRLGDQFNDVWRHLAREKYWTESSSPSVNSSRP
Protein: Diglucosylglycerate octanoyltransferase (DGG octanoyltransferase) (EC 2.3.1.273) (K5BJH8)
Organism: Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum)
Function: Sugar octanoyltransferase likely involved in the biosynthesis of mycobacterial methylglucose lipopolysaccharide (MGLP). Catalyzes the transfer of an octanoyl group from octanoyl-CoA to the C6 OH of the second glucose in diglucosylglycerate (DGG). Can also use hexanoyl-CoA as acyl donor in vitro. DGG is the preferred acceptor, but to a lesser extent, GG (glucosylglycerate) can be used as substrate. DGG and GG are the two earliest intermediates in MGLP biosynthesis.
Interaction partners:
- EDD, DegV family domain protein
- Histidine phosphatase super family protein
- Oligomerisation domain protein
- Probable nicotinate-nucleotide adenylyltransferase
- Bacterial transferase hexapeptide family protein
- Glycosyl hydrolase 57 family protein
- UbiE/COQ5 methyltransferase family protein
- Alpha/beta hydrolase family protein
- Uncharacterized protein
- Glycosyl transferases group 1 family protein
Sequence:
MSGRRPTLLVFCDSLSYYGPRGGLPADDPRIWPNIVASQLDWDVELIGRVGWTSRDVWWAATQDPRAWAALPRAGAVIFATGGMDSLPSPLPTALRELIRYIRPPWLRRRVRDLYGWLQPRLSPVSRNALPPHLTAEYLEMTRGAIDFNRPGIPVVAALPSVHIADSYGRAHHGREATARAITEWARQHGVVLVDLKAAVADQVLNGRGNPDGIHWNFEAHQAVAELMLKALAEAGVPCR
Protein: Flavin-dependent halogenase gsfI (EC 1.14.14.-) (Griseofulvin synthesis protein I) (D7PI14)
Organism: Penicillium aethiopicum
Function: Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of griseofulvin, an important antifungal drug that has been in use for a long time for treating dermatophyte infections. The first step of the pathway is the formation of the heptaketide backbone by gsfA which is initiated by priming with acetyl-CoA, followed by sequential condensations of 6 malonyl-CoA units. The resulting benzophenone can undergo a spontaneous dehydration to form norlichexanthone. However, the true precursor for the griseofulvin biosynthesis is not norlichexanthone, but the heptaketide benzophenone that is O-methylated at 3-OH by gsfB to produce griseophenone D which is further methylated at 9-OH by gsfC to yield griseophenone C. Griseophenone C is then substrate of halogenase gsfI which is responsible for the regio-specific chlorination at the C13 position to form griseophenone B. The cytochrome P450 gsfF catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A which is further methylated at 5-OH by gsfD to yield dehydrogriseofulvin. Finally, gsfE performs stereospecific reduction of enone 18 of dehydrogriseofulvin to afford the final product griseofulvin.
Interaction partners:
Sequence:
MAIPQSCTVLVAGGGPGGSYTAAALAREGVDVVLLEADCHPRYHIGESLLPSMRYLLRFIDLEDTFEQHGFQKKLGAFFKLNAKSAGYTDFIRANGPNGYSWNVVRSESDEILFRHATKSGAKTFENVSLKSVNFEPYENDKFTSQDKLTNPGRPVSAEWKTKDGCSGTISFDYLVDATGRVGILSTKYLKNRKFNESFRNIAMWGYFKGNIPPSPGTDRENQPISEGMRDGSGWVWMLPLHNGTVSIGAVVRKDIFQAKKKALPEGTTEAQTLASLVALCPTISSYLEPAELASGIRQAADYSYSANAYAGPNFRIVGDAGCFIDPFFSSGHHLALSSALAAATSINACIRGDCNEFDASRWFAKKVDEGYTLFLVVVMAALKQIRMQEQPILSDLDEEGFDRAFTILRPVIQGAADKETAPKAKGESITETIDLCLTALNDLHDTELQRKLTSIVEAKGTPEQEQLLGKLSPDETAALHRMRAMHSILPMGELEDFENSNIDGFKARLEKGSLGLRRERALCRDHAGDLQM
Protein: LHFPL tetraspan subfamily member 4 protein (Lipoma HMGIC fusion partner-like 4 protein) (Q7TSY2)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the regulation of inhibitory synapse formation and function by being involved in maintening gamma-aminobutyric acid receptors (GABAARs) clustering and their associated scaffold proteins at inhibitory synaptic sites. Acts in concert with NLGN2 to recruit or stabilize GABAARs.
Subcellular location: Cell projection, dendrite {ECO:0000269|PubMed:28978485}. Postsynaptic cell membrane {ECO:0000269|PubMed:28978485, ECO:0000269|PubMed:29742426}; Multi-pass membrane protein {ECO:0000255}. Note=Specifically localizes to inhibitory postsynaptic sites (PubMed:29742426). Colocalizes with GPHN, GABRG2 and NLGN2 at inhibitory postsynaptic sites (PubMed:28978485, PubMed:29742426). {ECO:0000269|PubMed:28978485, ECO:0000269|PubMed:29742426}.
Interaction partners:
- Neuroligin-2
- Gephyrin
Sequence:
MLPSQEASKLYHEHYMRNSRAIGVLWAIFTICFAIINVVVFIQPYWVGDSVSTPKPGYFGLFHYCVGSGLAGRELTCRGSFTDFSTIPSSAFKAAAFFVLLSMVLILGCITCFALFFFCNTATVYKICAWMQLLAALCLVLGCMIFPDGWDAETIRDMCGAKTGKYSLGDCSVRWAYILAIIGILNALILSFLAFVLGNRQTDLLQEELKQENKDFVGTTVSSVLRPGGDVSGWGVLPCPVAHTQGP