wanglab/gogpt-training-data huggingface dataset:
Protein: Sarcosine dehydrogenase, mitochondrial (SarDH) (EC 1.5.8.3) (Q99LB7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the last step of the oxidative degradation of choline to glycine. Converts sarcosine into glycine.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q64380}.
Interaction partners:
- Glycine dehydrogenase
- Glycine N-methyltransferase
- Peroxisomal sarcosine oxidase
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Alanine--glyoxylate aminotransferase
- D-amino-acid oxidase
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
- Dimethylglycine dehydrogenase, mitochondrial
- 5-aminolevulinate synthase, non-specific, mitochondrial
Sequence:
MASLSRVLRVAATCPRGRAAWNLGLQPLATEARPTTEKSVPYQRTLKEEAQGASVVPQGPSQPLPSTANVVVIGGGSLGCQTLYHLAKLGVGGAVLLERERLTSGTTWHTAGLLWQLRPSDVEVELLAHTRQVVSRDLEEETGLHTGWIQNGGLFIASNQQRLNEYKRLMSLGKAYGIESHVLSPAETKSLYPLMNVDDLYGTLYVPQDGTMDPAGTCTTLTRAAVARGAQVIENCAVTGIRVRTDDFGVRRVAAVETEHGSIQTPCVVNCAGVWASKVGRMAGVKVPLVAMHHAYVVTERIEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWDVFTQHIEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGCGQELAHWIVHGRPEKDMYSYDIRRFHHSLTDHTRWIRERSHESYAKNYSVVFPHDEPLAGRNMRRDPLHEELLGQGCVFQERQGWERPGWFNPQETAQVLDYDYYGAYGNQAHKDYTYSRLLGDEYTFDFPPHHHMIQKECLACRGAAAVFNMSYFGKFYLLGVDARKAADWLFSADVNRPPGSTVYTCMLNQRGGTESDLTVSRLAPGTQASPLVPAFEGDCYYLAVGGAVAQHNWSHINTVLQDQEFRCQLMDSSEDLGMLSIQGPASRDILQDVLDADLSNEAFPFSTHQLVRAAGHLVRAIRLSFVGELGWELHVPRASCLPVYRAVMAAGARHGLVNAGYRAIDSLSIEKGYRHWHADLRPDDSPLEAGLAFTCKLKTSVPFLGREALEKQRATGLRRRLICLTVEEEVPMFGLEAIWRNGQVVGHVRRADFGFTVNKTIAYGYIRDPSGGPVSLDFVKNGEYALERMGVTYAAQVHLKSPFDPDNKRVKGIY
Protein: Mastermind-like protein 2 (Mam-2) (Q8IZL2)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Potentiates activation by NOTCH3 and NOTCH4 more efficiently than MAML1 or MAML3.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:12370315}. Note=Nuclear, in a punctate manner.
Interaction partners:
- Recombining binding protein suppressor of hairless
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 4
- Neurogenic locus notch homolog protein 2
- Recombining binding protein suppressor of hairless-like protein
- Histone acetyltransferase p300
- Mastermind-like protein 1
- Mastermind-like protein 3
- CREB-binding protein
Sequence:
MGDTAPPQAPAGGLGGASGAGLLGGGSVTPRVHSAIVERLRARIAVCRQHHLSCEGRYERGRAESSDRERESTLQLLSLVQHGQGARKAGKHTKATATAATTTAPPPPPAAPPAASQAAATAAPPPPPDYHHHHQQHLLNSSNNGGSGGINGEQQPPASTPGDQRNSALIALQGSLKRKQVVNLSPANSKRPNGFVDNSFLDIKRIRVGENLSAGQGGLQINNGQSQIMSGTLPMSQAPLRKTNTLPSHTHSPGNGLFNMGLKEVKKEPGETLSCSKHMDGQMTQENIFPNRYGDDPGEQLMDPELQELFNELTNISVPPMSDLELENMINATIKQDDPFNIDLGQQSQRSTPRPSLPMEKIVIKSEYSPGLTQGPSGSPQLRPPSAGPAFSMANSALSTSSPIPSVPQSQAQPQTGSGASRALPSWQEVSHAQQLKQIAANRQQHARMQQHQQQHQPTNWSALPSSAGPSPGPFGQEKIPSPSFGQQTFSPQSSPMPGVAGGSGQSKVMANYMYKAGPSAQGGHLDVLMQQKPQDLSRSFINNPHPAMEPRQGNTKPLFHFNSDQANQQMPSVLPSQNKPSLLHYTQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQSSISAQQQQQQQSSISAQQQQQQQQQQQQQQQQQQQQQQQQQQQPSSQPAQSLPSQPLLRSPLPLQQKLLLQQMQNQPIAGMGYQVSQQQRQDQHSVVGQNTGPSPSPNPCSNPNTGSGYMNSQQSLLNQQLMGKKQTLQRQIMEQKQQLLLQQQMLADAEKIAPQDQINRHLSRPPPDYKDQRRNVGNMQPTAQYSGGSSTISLNSNQALANPVSTHTILTPNSSLLSTSHGTRMPSLSTAVQNMGMYGNLPCNQPNTYSVTSGMNQLTQQRNPKQLLANQNNPMMPRPPTLGPSNNNNVATFGAGSVGNSQQLRPNLTHSMASMPPQRTSNVMITSNTTAPNWASQEGTSKQQEALTSAGVRFPTGTPAAYTPNQSLQQAVGSQQFSQRAVAPPNQLTPAVQMRPMNQMSQTLNGQTMGPLRGLNLRPNQLSTQILPNLNQSGTGLNQSRTGINQPPSLTPSNFPSPNQSSRAFQGTDHSSDLAFDFLSQQNDNMGPALNSDADFIDSLLKTEPGNDDWMKDINLDEILGNNS
Protein: Periplasmic acid trehalase ATH1 (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (P48016)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Periplasmic acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source. Growth on trehalose is strictly respiratory (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:17475771}; Single-pass type II membrane protein {ECO:0000269|PubMed:17475771}. Vacuole lumen {ECO:0000269|PubMed:17475771, ECO:0000269|PubMed:19703229}. Periplasm {ECO:0000250|UniProtKB:N1P212}. Note=May exist in the periplasm either as a membrane-bound or as a free protein (By similarity). Vacuolar localization is dependent on the multivesicular body (MVB) sorting pathway (PubMed:17475771). Vacuolar localization appears to be associated with its degradation (PubMed:19703229). {ECO:0000250|UniProtKB:N1P212, ECO:0000269|PubMed:17475771, ECO:0000269|PubMed:19703229}.
Interaction partners:
- Probable trehalase
- Cytosolic neutral trehalase
- Trehalose synthase complex regulatory subunit TPS3
- Trehalose-phosphatase
- Trehalose synthase complex regulatory subunit TSL1
- Protein ATC1/LIC4
- Alpha,alpha-trehalose-phosphate synthase 56 kDa subunit
- General alpha-glucoside permease
- Bifunctional protein GAL10
- Glycogen phosphorylase
Sequence:
MKRIRSLWFNAEASYSNLNNSPSLRNKNSTGNNSRSKNYRSFSRFDLINSILLLMMLFLLAIFVTALYLTKSSRLTYSHASRAALFNPLGVISPSLGNHTLNYDPEARESSKKLYELLSDFNTAYYDDENMILGSNLFSKNTYSRQPYVANGYIGSRIPNIGFGYALDTLNFYTDAPGALNNGWPLRNHRFAGAFVSDFYCLQPKLNSTNFPELDDVGYSTVISSIPQWTNLQFSLVNDSKWFNPQNVTLDDVTNYSQNLSMKDGIVTTELDWLNSQIHVKSEIWAHRHIHPLGVVSLEISLNTDHLPSDFDSLDVNIWDILDFNTSHRTVLHSTGTDEKNNAVFMIVQPDNVPSSNCAIYSTCTVKYENSTNPINSSESFEEKDVSSNIYNVILTEDQPKIIVHKYVGIMSTEFNKNKEQQDNTNIGLAKMIALNSKGNYEKLLSSHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRDYNVSSDRGLPVGVSGLSSDSYGGMVFWDADIWMEPALLPFFPNVAQNMNNYRNATHSQAKLNAEKYGYPGAIYPWTSGKYANCTSTGPCVDYEYHINVDVAMASFSIYLNGHEGIDDEYLRYTTWPIIKNAAQFFTAYVKYNSSLGLYETYNLTDPDEFANHINNGAFTNAGIKTLLKWATDIGNHLGEVVDPKWSEISKDIYIPRSSSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAAGLLNHGSSSQSYLYKSVLPYLRAPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGIRYSYEVDPDTKKINRLLRFNPIELPLLPGGIAIRNFKYMNQVLDIIIDDHNGTIVHKSGDVPIHIKIPNRSLIHDQDINFYNGSENERKPNLERRDVDRVGDPMRMDRYGTYYLLKPKQELTVQLFKPGLNARNNIAENKQITNLTAGVPGDVAFSALDGNNYTHWQPLDKIHRAKLLIDLGEYNEKEITKGMILWGQRPAKNISISILPHSEKVENLFANVTEIMQNSGNDQLLNETIGQLLDNAGIPVENVIDFDGIEQEDDESLDDVQALLHWKKEDLAKLIEQIPRLNFLKRKFVKILDNVPVSPSEPYYEASRNQSLIEILPSNRTTFTIDYDKLQVGDKGNTDWRKTRYIVVAVQGVYDDYDDDNKGATIKEIVLND
Protein: Transmembrane protein 188 (A5PEW7)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}.
Interaction partners:
Sequence:
MAIQARRMPEDPSTACEDLKFFEKRLTEVITYMGPTCTRWRIAIVIFAVLVGVIGSKYFANELQKIEIFQIPMIDMFLTTHLDFTLCFFVGLLLFAVFGVHRRIVAPTIVARRCRDALSPFSLSCDHNGKLIVKPAVRNSAP
Protein: Nuclear pore protein (Q9BKT9)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567, ECO:0000256|RuleBase:RU364035}.
Interaction partners:
- Nuclear Pore complex Protein
- Nucleoporin_N domain-containing protein
- Nsp1_C domain-containing protein
- Nucleoporin NUP35
- Nuclear pore complex protein 5
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein 14
- Protein SEC13 homolog
- Nucleoporin Nup54 alpha-helical domain-containing protein
- WD_REPEATS_REGION domain-containing protein
Sequence:
MLQFTEILGRVDHQGFAQLLANPIFQTNRVGQENSQQFTVRNGVEQELCGILGGSEGDWTRQTHSVQKQMMFGERGIELPSRQPKSHTAEDTLTDEGVVDVPEAVMDDIDEEELDEDISRVKVETDRAFFNHMLLSRPAAVPMNPAQAMERDNLPFGGGKFVNKNISDRRELIFGDKLHKFLKNQGKKSLVDLMKEAIDESGTDGALGDVWNDVTSVLNRKTSASRDDLTTTANLVEDACKYLQAVFTEHMQTVVERNLEVAERGGIPGTRGLVNAFLKVGTEESFQPEDDSIDGMPTWQVTYHCVRAGDMKSASETLNRLKSFPQCATLVAALNHVAKHGKLDSELKKKLKVEWRHNLAHTKDKYKRALYAALLGGLDSAALADTLENWIWFKLYPLHVDPQLTDVLFKEVQKAVSVDYGEQYFMSNGPSEFQYFFTALWLSGQFERAIYLLHECGQRVDSVHVAVLAHKLGYLRMSKKSTDEMLVVDQNDSTKCHLNLARLIVAYTKSFELVDVPRSLDYWFLLKGITTPTGSDVFEMAVSRSVYLTGQTDEILGKLTPDGRREKGLIDEYLDDPSEVICRVASDTEITGEWDQAVGLYLLASKPTNAAILLSSEISETLRTENKEKIADLVHVAEQFKKVQRGCQASEYATLSLLVDLAVLFDHCRNEEAEIAYGISTHLRLIPTEPDQVTVIVNEFHMVPQKVREVLPDMCLHLMKCLVDHCIRQSTTQANRGANSATTSMFSSSNRYVKQIKAIVLYSATVPYKFPTHVTSRLLQLQASLGI
Protein: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS) (P24224)
Organism: Escherichia coli (strain K12)
Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Acyl carrier protein
- Pyridoxine 5'-phosphate synthase
- Acyl carrier protein phosphodiesterase
- DNA repair protein RecO
- GTPase Era
- Dephospho-CoA kinase
- Ribonuclease 3
Sequence:
MAILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWKTHHQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDELGKPRLRLWGEALKLAEKLGVANMHVTLADERHYACATVIIES
Protein: Chromodomain helicase DNA binding protein 4 (F5H6N4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKERMLLCRQLGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTTKKKKK
Protein: ACP53C14B (Accessory gland protein 53C14b, isoform A) (Accessory gland protein 53C14b, isoform B) (FI06403p) (IP05657p) (Q6GUR9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Accessory gland-specific peptide 26Aa
- ACP53C14A
- Accessory gland protein Acp53Ea
- Accessory gland protein Acp29AB
- Accessory gland protein Acp76A
- IP20609p
- Serpin 28F
- Accessory gland-specific peptide 57Da
- Lectin-29Ca
- Accessory gland-specific peptide 70A
Sequence:
MSVIKSIFLLSILAVCLIPRETEAQATISESWGRLGKCTQVAIETLTSLADKIVPTVYELKQCSGYVTLEPANGKDRKITWYLKVSYEFFKKLVFDEPKCLHGLLNKLAATIKPFAEQISGLGCLDEEDYII
Protein: Peroxidase 36 (Atperox P36) (EC 1.11.1.7) (Q9SD46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- Pectinesterase inhibitor 6
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- Cellulose synthase A catalytic subunit 5
- Endo-1,4-beta-xylanase 4
- Berberine bridge enzyme-like 9
- rhamnogalacturonan endolyase
- Beta-galactosidase 6
- Berberine bridge enzyme-like 23
- Transmembrane E3 ubiquitin-protein ligase FLY1
- UDP-rhamnose/UDP-galactose transporter 2
Sequence:
MNTKTVKSMAGIVLSQISLVALFPLCICYQTHQSTSSVASLSPQFYENSCPNAQAIVQSYVANAYFNDPRMAASILRLHFHDCFVNGCDASVLLDSSGTMESEKRSNANRDSARGFEVIDEIKSALENECPETVSCADLLALVARDSIVICGGPSWEVYLGRRDAREASLIGSMENIPSPESTLQTILTMFNFQGLDLTDLVALLGSHTIGNSRCIGFRQRLYNHTGNNDPDQTLNQDYASMLQQGCPISGNDQNLFNLDYVTPTKFDNYYYKNLVNFRGLLSSDEILFTQSIETMEMVKYYAENEGAFFEQFAKSMVKMGNISPLTGTDGEIRRICRRVNHDV
Protein: Glutathione S transferase E6 (EC 2.5.1.18) (A1ZB71)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutathione S transferase E7
- Glutathione S transferase E5
- Bifunctional glutamate/proline--tRNA ligase
- Glutathione S transferase E8, isoform A
- FI01423p
- Glutathione S transferase E9
- Glutathione S transferase T1
- Glutathione S-transferase D1
- Glutathione S transferase T2
- Inactive glutathione S-transferase D3
Sequence:
MVKLTLYGLDPSPPVRAVKLTLAALNLTYEYVNVDIVARAQLSPEYLEKNPQHTVPTLEDDGHYIWDSHAIIAYLVSKYADSDALYPKDPLKRAVVDQRLHFESGVVFANGIRSISKSVLFQGQTKVPKERYDAIIEIYDFVETFLKGQDYIAGNQLTIADFSLVSSVASLEAFVALDTTKYPRIGAWIKKLEQLPYYEEANGKGVRQLVAIFKKTNFTFEA
Protein: Pectate lyase (EC 4.2.2.2) (E0SJQ8)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Pectinesterase A
- Pectate lyase C
- Pectate lyase B
- Pectate lyase L
- Exo-poly-alpha-D-galacturonosidase
- Pectin acetylesterase
- Pectate lyase
- Pectate lyase E
- Pectate lyase D
- Exo-poly-alpha-D-galacturonosidase
Sequence:
MEQAIMKHTLLFALLFSTSVLTVQAASTAAPDLKGFGTETVAGSGGKIIRVTTLDSGGAGSLREALATKGPRIIVFEVGGIIDLDEKDIRLAEPYVTIAGQTAPSPGITLVKGGMMITTHDVLVQHIRFRIGDNGHAKKSGFEKDVSLYGPNAYNVVVDHCSFAWGTDENLSVSGPRYDGPSGTAHNVTFSNNIIAEGLYDSSHSKGIHSMGTLVHDNVTDAAIIGNLYAHNNERNPWFKGATTGVVVNNLIYNPGIWGIRIGAIQSEWEGRSLPVNAKVAIAGNVMYHGANTKSGLSLVGSNTTGGDVWMSDNLAFDKAGKAVAQTSGTGINLLKSAPVWPTGLTAISSSSVANQVTQHAGARPKDRDAVDKRIVSDFQKRSGTFVNSQSEVGGYPTATATKRTLTVPSTNVDAWLQQMAKDLE
Protein: Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (POMGnT1) (EC 2.4.1.-) (UDP-GlcNAc:alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2) (GnT I.2) (Q8WZA1)
Organism: Homo sapiens (Human)
Function: Participates in O-mannosyl glycosylation by catalyzing the addition of N-acetylglucosamine to O-linked mannose on glycoproteins. Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins, providing the necessary basis for the addition of further carbohydrate moieties. Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17034757, ECO:0000303|PubMed:11709191}; Single-pass type II membrane protein {ECO:0000305|PubMed:11709191}.
Interaction partners:
- Protein O-mannosyl-transferase 1
- Protein O-mannosyl-transferase 2
- Dystroglycan 1
- Ribitol-5-phosphate transferase FKTN
- Ribitol 5-phosphate transferase FKRP
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 3
- Beta-1,4-galactosyltransferase 2
Sequence:
MDDWKPSPLIKPFGARKKRSWYLTWKYKLTNQRALRRFCQTGAVLFLLVTVIVNIKLILDTRRAISEANEDPEPEQDYDEALGRLEPPRRRGSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAEEAECHWADTELNRRRRRFCSKVEGYGSVCSCKDPTPIEFSPDPLPDNKVLNVPVAVIAGNRPNYLYRMLRSLLSAQGVSPQMITVFIDGYYEEPMDVVALFGLRGIQHTPISIKNARVSQHYKASLTATFNLFPEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAEDPALLYRVETMPGLGWVLRRSLYKEELEPKWPTPEKLWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMNGYFHEAYFKKHKFNTVPGVQLRNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAFIRMEKDDDFTTWTQLAKCLHIWDLDVRGNHRGLWRLFRKKNHFLMVGVPASPYSVKKPPSVTPIFLEPPPKEEGAPGAPEQT
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (B4DSK5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367045}.
Interaction partners:
Sequence:
MAGRSMQAARHPSVVPGSIAFSLPQRKWAGLSIGQEIEVSLYTFDKAKQCIGTMTIEIDFLQKKSIDSNPYDTDKMAAEFIQQFNNQAFSVGQQLVFSFNEKLFGLLVKDIEAMDPSILKGEPATGKRQKIEVGLVVGNSQVAFEKAENSSLNLIGKAKTKENRQSIINPDWNFEKMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGLVRAAQSTAMNRHIKASTKVEVDMEKAESLQVTRGDFLASLENDIKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEGASPLDFD
Protein: Ribosomal RNA large subunit methyltransferase F (EC 2.1.1.181) (23S rRNA mA1618 methyltransferase) (rRNA adenine N-6-methyltransferase) (P75782)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18021804}.
Interaction partners:
- Ribosomal RNA large subunit methyltransferase J
- Ribosomal RNA small subunit methyltransferase A
Sequence:
MSAQKPGLHPRNRHHSRYDLATLCQVNPELRQFLTLTPAGEQSVDFANPLAVKALNKALLAHFYAVANWDIPDGFLCPPVPGRADYIHHLADLLAEASGTIPANASILDIGVGANCIYPLIGVHEYGWRFTGSETSSQALSSAQAIISSNPGLNRAIRLRRQKESGAIFNGIIHKNEQYDATLCNPPFHDSAAAARAGSERKRRNLGLNKDDALNFGGQQQELWCEGGEVTFIKKMIEESKGFAKQVMWFTSLVSRGENLPPLYRALTDVGAVKVVKKEMAQGQKQSRFIAWTFMNDEQRRRFVNRQR
Protein: Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C (PP6-ARS-C) (Serine/threonine-protein phosphatase 6 regulatory subunit ARS-C) (Ankyrin repeat domain-containing protein 52) (Q8NB46)
Organism: Homo sapiens (Human)
Function: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates.
Interaction partners:
- Serine/threonine-protein phosphatase 6 catalytic subunit
- Serine/threonine-protein phosphatase 6 regulatory subunit 2
- Serine/threonine-protein phosphatase 6 regulatory subunit 1
- Serine/threonine-protein phosphatase 6 regulatory subunit 3
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A
Sequence:
MGILSITDQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSLSNEHVLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAEPHTPSSHDAEEDEPLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTIPVSPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPLHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAKIVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINATNSALQMPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACAPNKDVADCLALILSTMKPFPPKDAVSPFSFSLLKNCSIAAAKTVGGCGALPHGASCPYSQERPGAIGLDGCYSE
Protein: Uncharacterized J domain-containing protein C3E7.11c (O59731)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MVQRVVDRDYYDILNISVDADGDTIKKSYRRLAILYHPDKNRENPEAAREKFQKLAEAYQVLSDPKLREKYDKLGKVGAVPDAGFEDAFEFFKNLFGGDSFRDYVGELNLLKELCKMINEEPELKAIEDTEESKKQLQREESKEADRLLQERIDVLCKNLLDKLSIWTETDMSDRVTDAFKQKMQFEAELLKDESFGNEMLHAIGSTYVQRANILIQSQSFLGIRGVWGSLCAKGTLLKDTWNTVVSAVDVQSSAAALAKAEEGEEQWSKEKRDEAARELTGKVLSATWKGTRFEVQSVIRTVSDKILYDKAVPLEKRINRANALLMIGQVFLKVAPNEKSDANYFEDLMNDRGK
Protein: tRNA pseudouridine synthase-like 1 (EC 5.4.99.-) (tRNA pseudouridylate synthase-like 1) (tRNA-uridine isomerase-like 1) (Q8N0Z8)
Organism: Homo sapiens (Human)
Interaction partners:
- RNA pseudouridylate synthase domain-containing protein 1
- Pseudouridylate synthase TRUB2, mitochondrial
- Pseudouridylate synthase TRUB1
- Large ribosomal subunit protein bL17m
- Pseudouridylate synthase PUS7L
- Mitochondrial mRNA pseudouridine synthase RPUSD3
- Pseudouridylate synthase RPUSD4, mitochondrial
- Pseudouridylate synthase RPUSD2
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MSSAPASGSVRARYLVYFQYVGTDFNGVAAVRGTQRAVGVQNYLEEAAERLNSVEPVRFTISSRTDAGVHALSNAAHLDVQRRSGRPPFPPEVLAEALNTHLRHPAIRVLRAFRVPSDFHARHAATSRTYLYRLATGCHRRDELPVFERNLCWTLPADCLDMVAMQEAAQHLLGTHDFSAFQSAGSPVPSPVRTLRRVSVSPGQASPLVTPEESRKLRFWNLEFESQSFLYRQVRRMTAVLVAVGLGALAPAQVKTILESQDPLGKHQTRVAPAHGLFLKSVLYGNLGAASCTLQGPQFGSHG
Protein: Processing of GAS1 and ALP protein 2 (P53903)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the processing and trafficking of GAS1 and PHO8 glycosylated proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14690591}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:14690591}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSEVAETWVDTWMAKLVNYDYKHFIRLVIIVGGYLLLRNIASRELAKKQLAAQVEKDKRDKEEKRSKDLIDKPDDAATAETTSFGWGKKTRRRVKRQQELFENALEEAKRRNQGLDPDSDADIEELLEE
Protein: Kelch-like protein diablo (Q9VGE6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPSQLLQVEDQTFSAHRVVLAATIPYFYAMFTNNMAESRIKEITMKESAIEPSALESLINYVYSGQVRIDNQNVQNLMVGASFLQLSNVRDACASFLISRFHPHNVLGIRTFADSMICRQLIDAADKYIDQNFAKVSQSEEFLALDCEQLLELMRRDELNVRTEEVIFEACMKWVKYAEDKRSELFPQVLAAVRLPLLSPQFLADRVAREELIRSSHQCRDLLDEAKDFHLMPERRGLLQSFRTRQRSGEFFTGQIYAVGGLASTGESVSTVEIYDPLTKKWKMGEQMSMMRSRVGVAVLNGKLYAFGGFNGTERLSTVEVYDPRKNKWSQGCAMLCKRSAVGVAALDDCIYVCGGYDGVTSLNTVEVYYPKSNTWKTVAQMMKYRSAGGVTQLNGYVYALGGHDGLSIFDSVERYDQAEDVWVKMSPMLNRRCRLGVATLNGKIYVCGGYCGNSFLRSVECYDPQTDTWKLVTPMNCKRSRVALAANMGKLWAIGGYDGESNLSTVEVYDPETDKWTFMPPMCAHSGGVGAGVIRIE
Protein: Protein amalgam (P15364)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Neurotactin
- Dpp target protein
- BARBU
Sequence:
MARLRLLIGLIFCLAISLDSVLSAPVISQISKDVVASVGDSVEFNCTVEEVGQLSVSWAKRPSESDTNSVVLSMRNILSLPDQRYNVTVTEGPKTGSAIYTFRIQNIEVSDMGPYECQVLVSATEKVTKKLSLQIKTPPVIAENTPKSTLVTEGQNLELTCHANGFPKPTISWAREHNAVMPAGGHLLAEPTLRIRSVHRMDRGGYYCIAQNGEGQPDKRLIRVEVEFRPQIAVQRPKIAQMVSHSAELECSVQGYPAPTVVWHKNGVPLQSSRHHEVANTASSSGTTTSVLRIDSVGEEDFGDYYCNATNKLGHADARLHLFQTVIPVPSLS
Protein: Membrane-associated protein Hem (dHem-2) (P55162)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role during growth of the oocyte.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Abelson interacting protein, isoform D
- Cytoplasmic FMR1-interacting protein
- FI14118p
- Wiskott-Aldrich syndrome protein family member
- RE12101p
- Dreadlocks, isoform B
- Wiskott-Aldrich syndrome protein family member
- Insulin receptor substrate 53 kDa, isoform A
- Actin-related protein 2
- Tyrosine-protein kinase Abl
Sequence:
MARPIFPNQQKIAEKLIILNDRGLGILTRIYNIKKACGDTKSKPGFLSEKSLESSIKFIVKRFPNIDVKGLNAIVNIKAEIIKSLSLYYHTFVDLLDFKDNVCELLTTMDACQIHLDITLNFELTKYYLDLVVTYVSLMIVLSRVEDRKAVLGLYNAAYELQNNQADTGFPRLGQMILDYEVPLKKLAEEFIPHQRLLTSALRSLTSIYALRNLPADKWREMQKLSLVGNPAILLKAVRTDTMSCEYISLEAMDRWIIFGLLLNHQMLGQYPEVNKIWLSALESSWVVALFRDEVLQIHQYIQATFDGIKGYSKRIGEVKEAYNTAVQKAALMHRERRKFLRTALKELALIMTDQPGLLGPKAIFIFIGLCLARDEILWLLRHNDNPPLLKNKGKSNEDLVDRQLPELLFHMEELRALVRKYSQVMQRYYVQYLSGFDATDLNIRMQSLQMCPEDESIIFSSLYNTAAALTVKQVEDNELFYFRPFRLDWFRLQTYMSVGKAALRIAEHAELARLLDSMVFHTRVVDNLDEILVETSDLSIFCFYNKMFDDQFHMCLEFPAQNRYIIAFPLICSHFQNCTHEMCPEERHHIRERSLSVVNIFLEEMAKEAKNIITTICDEQCTMADALLPKHCAKILSVQSARKKKDKSKSKHFDDIRKPGDESYRKTREDLTTMDKLHMALTELCFAINYCPTVNVWEFAFAPREYLCQNLEHRFSRDLVGMVMFNQETMEIAKPSELLASVRAYMNVLQTVENYVHIDITRVFNNCLLQQTQALDSHGEKTIAALYNTWYSEVLLRRVSAGNIVFSINQKAFVPISPEGWVPFNPQEFSDLNELRALAELVGPYGIKTLNETLMWHIANQVQELKSLVSTNKEVLITLRTSFDKPEVMKEQFKRLQDVDRVLQRMTIIGVIICFRNLVHEALVDVLDKRIPFLLSSVKDFQEHLPGGDQIRVASEMASAAGLLCKVDPTLATTLKSKKPEFDEGEHLTACLLMVFVAVSIPKLARNENSFYRATIDGHSNNTHCMAAAINNIFGALFTICGQSDMEDRMKEFLALASSSLLRLGQESDKEATRNRESIYLLLDEIVKQSPFLTMDLLESCFPYVLIRNAYHGVYKQEQILGLAL
Protein: Keratin-associated protein 2-2 (High sulfur keratin-associated protein 2.2) (Keratin-associated protein 2.2) (Q9BYT5)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity).
Interaction partners:
Sequence:
MTGSCCGSTFSSLSYGGGCCQPCCCRDPCCCRPVTCQTTVCRPVTCVPRCTRPICEPCRRPVCCDPCSLQEGCCRPITCCPSSCTAVVCRPCCWATTCCQPVSVQSPCGQPTPCSTTCRTSSC