wanglab/gogpt-training-data huggingface dataset:
Protein: Major histocompatibility complex, class II, DM alpha (H0Y732)
Organism: Homo sapiens (Human)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004530}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004352}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004352}.
Interaction partners:
Sequence:
VSCWLSDSCQELQRRGIILCSYGVTSPIAVFGRPGRLRNRRHFERRLVPMKWLKKCLDTAPTPMWPDDLQNHTFLHTVYCQDGSPSVGLSEAYDEDQLFFFDFSQNTRVPRLPEFADWAQEQGDAPAILFDKEFCEWMIQQIGPKLDGKIPVSRGFPIAEVFTLKPLEFGKPNTLVCFVSNLFPPMLTVNWQHHSVPVEGFGPTFVSAVDGLSFQAFSYLNFTPEPSDIFSCIVTHEIDRYTAIAYWVPRNALPSDLLENVLCGVAFGLGVLGIIVGIVLIIYFRKPCSG
Protein: Meiosis inducing protein mei3 (P08090)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This protein, expressed under control of the mating-type locus, induces meiosis and sporulation in fission yeast. It down regulates the ran1/pat1 gene product.
Interaction partners:
- Negative regulator of sexual conjugation and meiosis
- Meiosis protein mei2
- Mating-type M-specific polypeptide Mi
- Transcription factor ste11
- Meiosis-specific transcription factor mei4
Sequence:
MSSQNTSNSRHPASSASALPNRTNTARRSTSPRTSTGSSSTNTNTKTVDHAGTTFISSTSKRGRSTKAGSVHSVPMKRTKRVRRTPAQRIEHENKENIQTEKVYRIKPVQRVLSPSDLTNELTILDLFHVPRPNETFDITDRVNNTSR
Protein: CCA tRNA nucleotidyltransferase, mitochondrial (EC 2.7.7.72) (CCA-adding enzyme) (tRNA CCA-pyrophosphorylase) (tRNA adenylyltransferase) (tRNA nucleotidyltransferase) (Q9P4S5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: This enzyme carries out synthesis of the tRNA CCA terminus without the direction of a template using the multiple accepting and donating subsites within its active site.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P21269}. Cytoplasm {ECO:0000250|UniProtKB:P21269}. Nucleus {ECO:0000250|UniProtKB:P21269}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- 25S rRNA adenine-N
Sequence:
MFKAIRRVFTMIPRIQLTEKETRICNLLKDYTAHYNSLHYGQEPLTLRITGGWVRDKLLGQGSHDLDIAINIMSGEEFATGLNGYLLEHFDKYGVKPHSIHKIDKNPEKSKHLETATTKLFDVEVDFVNLRSEEYTEDSRIPTTQFGTPEEDALRRDATLNALFYNIQQDAVEDFTKRGWQDLQDGVLRTPLPARQTFLDDPLRVLRLIRFASRFNFNIEAGVLKEMHDPEINEAFNNKISRERIGVEMEKILVGPNPILGLKLIQRTHLENVIFLWHGDQSVIEYNRKNWPQTKDVEDIYKKGIFNHHLKNFIHHYKDFLSRYLKLRQAIETKDKSFQQNFLLASILIPMADLKIIALPKKKLNNTLPVSESIVREGLKFNKASSIVVARCVENIAAYNSMVEKYLQSGDLKRSEVGTFLRELRGDWEIVHYVSLMDQYLKYISRKDNVVNIIDKYDRFWNYIQEQNLQDSDKMVPIIDGKRMVKILETKPGPWLGKINDEVILWQFDHPQGTEQELISFIKSILPNYLQ
Protein: Transcriptional activator HAC1 (P41546)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional activator involved in the unfolded protein response (UPR) pathway. Recognizes and binds to the UPR element (UPRE) in the promoter of UPR-regulated genes such as KAR2, PDI1, EUG1 and FKB2. Increases the synthesis of endoplasmic reticulum-resident proteins required for protein folding as well as components of the secretory pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Serine/threonine-protein kinase/endoribonuclease IRE1
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase
- General control transcription factor GCN4
- Endoplasmic oxidoreductin-1
- tRNA ligase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- Protein INO2
- Heat shock protein 70 homolog LHS1
Sequence:
MEMTDFELTSNSQSNLAIPTNFKSTLPPRKRAKTKEEKEQRRIERILRNRRAAHQSREKKRLHLQYLERKCSLLENLLNSVNLEKLADHEDALTCSHDAFVASLDEYRDFQSTRGASLDTRASSHSSSDTFTPSPLNCTMEPATLSPKSMRDSASDQETSWELQMFKTENVPESTTLPAVDNNNLFDAVASPLADPLCDDIAGNSLPFDNSIDLDNWRNPEAQSGLNSFELNDFFITS
Protein: Translocon-associated protein subunit alpha (TRAP-alpha) (PGP35) (Signal sequence receptor subunit alpha) (SSR-alpha) (P16967)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- Translocon-associated protein subunit beta
- Signal sequence receptor subunit 3.
- Signal sequence receptor subunit 4.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Uncharacterized protein.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Protein transport protein Sec61 subunit beta
- Calnexin
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Sequence:
MRVLPRLLLLLLLAFPAAVLLRGGPGGSLVAAQDLTEDEETVEDSIIEDEDDEAEVEEDEPTDLAEDKEEEDVSGEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTIIEREDGLDGETIFMYMFLAGLGLLVVVGLHQLLESRKRKRPIQKVEMGTSSQNDVDMSWIPQETLNQINKASPRRLPRKRAQKRSVGSDE
Protein: cAMP-dependent protein kinase catalytic subunit (EC 2.7.11.11) (Q7K6A0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- cGMP-dependent protein kinase
- Calcium-dependent protein kinase 1
- Potassium channel K1
- Aquaporin, putative
- Merozoite surface protein 9
- Ornithine aminotransferase
- non-specific serine/threonine protein kinase
Sequence:
MQFIKNLQLNKKKDSDSSEQVLTNKKNKMKYEDFNFIRTLGTGSFGRVILATYKNGNYPPVAIKRFEKCKIIRQKQVDHVFSERKILNYINHPFCVNLHGSFKDDSYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKIVETRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFSNIDWVNLLNKNVEVPYKPKYKNIFDSSNFERVQEDLTIADKITNENDPFYDW
Protein: (thale cress) hypothetical protein (A0A384LCJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDTVNDSFSPGSSRPSPATLSREDCWSEEATFTLIQAWGNRYVDLSRGNLRQKHWQEVANAVNDRHYNTGRNVSAAKSQPYRTDVQCKNRIDTLKKKYKVEKARVSESNPGAYISPWPFFSALDDLLRESFPTSSNPDSTDNIPHQRLSLPMSINPVPVAPRSAIPRRPATSPAIIPHAGDDLLGFRGNLNAFAAAAAAAACPASEDDSEGSRSRSSGRSGSNKKRERKIEKKQGYKEVADAIERLGQIYERVEEKKRKEMVELEKQRMRFAKELECHRMQLFTEMQVRLHKLRRTSGSKGPTSSASAALDYGMMDFPSYF
Protein: Syndecan (Q5I5K4)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000649}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000649}.
Interaction partners:
Sequence:
MPLLRAAFLLGLLLAAAAAESVRETETMDAQWLNYPGSGDLPDDEDIGEFTPHLTSDKFDIDDVSGSGDYSDSDDAMYLTTVDTPAISDNFIPGDTERKIEGEKKNTMLDNEIIPDKASPVEENLSNKISMASTANSSIFERTEVLTALIAGGAVGLLFAVFLILLLVYRMKKKDEGSYDLGKKPIYKKAPTNEFYA
Protein: Casein kinase I isoform delta (CKI-delta) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26) (Q06486)
Organism: Rattus norvegicus (Rat)
Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). {ECO:0000250}.
Interaction partners:
- Cryptochrome-1
- Period circadian protein homolog 2
- Period circadian protein homolog 3
- Basic helix-loop-helix ARNT-like protein 1
- Period circadian protein homolog 1
- Neuronal PAS domain protein 2
- Protein LTV1 homolog
- Cryptochrome-2
- non-specific serine/threonine protein kinase
- Glycogen synthase kinase-3 beta
Sequence:
MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNVSSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR
Protein: LIM/homeobox protein lim-7 (G5EC36)
Organism: Caenorhabditis elegans
Function: Probable DNA-binding transcriptional activator.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682}.
Interaction partners:
- LIM/homeobox protein ceh-14
- LIM interaction domain-containing protein
- Paired box protein 6 homolog
Sequence:
MNICMRNGYEQFSLTSPGTSDLEIGGSFWKDEPDTKYLCLDSPVEQRQHQPPMAVCAGCRLEISDRYFLRVNPNLEFHAQCLKCVQCSRPLDENQTAFVKNGQTYCRDDYRRLFTTRCSRCHGDFDKTDLVMRAGPQNVFHLNCFACVACEKRLQTGEEFQIKNNSLYCRSDCRGLDNPDTSASVPDYSKLNNNNNNDNNNSSSNFDEDEWDEERSTLTSLDNNTSSPLGSPKSDGVRTPLFGHHNSGSGGSTSSCGKKKKDKQATRVRTVLNENQLKILRDCYSINSRPDATLKERLVEMTGLSARVIRVWFQNKRCKDKKRQIQITENRLNSEREEVLNRVRVNGIGPLMVQPATPHIDNTLGGPIDIQHFAQWNGTPPPPPPQYGNPMMFNSPSTFDVSVILAPVAPNVTSPSEALGPLGASVFPHFSPQHAPFTATSHDISSPAPCGE
Protein: 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta (OFOR1) (EC 1.2.7.11) (Q96Y68)
Organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
Function: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-oxobutyrate to form their CoA derivatives.
Interaction partners:
- 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha
- 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha
- 2-oxoacid oxidoreductase
- pyruvate synthase
- pyruvate synthase
- 2-oxoacid oxidoreductase
- Succinyl-CoA synthetase beta subunit
- Pyruvate kinase
- Succinate--CoA ligase subunit alpha
- Indolepyruvate--ferredoxin oxidoreductase beta subunit
Sequence:
MAAFKPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD
Protein: ATP-dependent zinc metallopeptidase, putative (Q387Q0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Prohibitin
- Prohibitin
Sequence:
MDPLSRDARASNLPSYYRGFYDAQQRRPTKNVEPSVTQAFGGAFLAAVPLAALYFFLRRRSAAAVKVAAPNAKPSGFFADVMKAMQKQMNPLGDKNFRVDVTDTKFKDVIGIPEAVEEIQQYVKFLQTPERFTRLGARLPKGCLLTGQPGTGKTLLAKAVAGEAGVPFFSCSGADFIEVYAGSGPKRVRELFAEAKKVAPSVVFLDEIDAVGTRGGEQDAGGVTSEENRTVNQLLAELDGLGASEAVVVFAATNFMDNIDKALLREGRFDRKIEVPMPDRQAREDLFRHYLKRIVASDVEVKAQRLAGLTPGVSPAAISTIVNEAALAAAVRGDGEVTEQTLLPAVDDVLLGKKHRSYMTDAALRRVALHESGHALVAWLLPQQPDVVKLSVTPRGCAAGFTQQLGREALDMHTDLSLFTDLCVLLAGRLAEATRYDGLTTGAQDDYQRATQAAIQQFLSFGMSQSVGLLAYEPQRLNEGRIYQRHSEKAQAMAEVEAARLVEVAQRFTQTLIAANANTLHRVADALVVKRELLSDELAALMGKRGTVRLTKEAKEALAEFLRKAEEHRPSFSDVTA
Protein: Positive regulator for alginate biosynthesis MucC (G3XCY1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Sigma factor AlgU regulatory protein MucB
- Sigma factor AlgU negative regulatory protein
- Probable periplasmic serine endoprotease DegP-like
- RNA polymerase sigma-H factor
- AlgW protein
- GDP-mannose 6-dehydrogenase
- Alginate biosynthesis transcriptional regulatory protein AlgB
- Ion-translocating oxidoreductase complex subunit G
- Ion-translocating oxidoreductase complex subunit C
Sequence:
MIEEQGRVVATEPGAVWVETVRRSTCSSCSANAGCGQGLMQRLGVGAGRARVRALSDLSLRVGDAVVLGIHEDLLLRASVLFYLFPLLGFFVAALLATRAGLVEPLIIVSGLAGLLAAWLLVRRHARRHADDPASQPVVLRALISGPSDSA
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (Transducin beta chain 1) (P62874)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity).
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Adhesion G protein-coupled receptor L3
Sequence:
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Protein: Bifunctional D-cysteine desulfhydrase/1-aminocyclopropane-1-carboxylate deaminase, mitochondrial (EC 3.5.99.7) (EC 4.4.1.15) (1-aminocyclopropane-1-carboxylic acid deaminase 1) (AtACD1) (AtD-CDes1) (D-CDes1) (D-CDES) (F4HYF3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the production of hydrogen sulfide (H2S) from cysteine. Is mainly responsible for the degradation of cysteine to generate H2S, a regulator of stomatal movement and closure. Has high affinity for D-cysteine.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15720402}.
Interaction partners:
- L-cysteine desulfhydrase
- Probable L-cysteine desulfhydrase, chloroplastic
- D-cysteine desulfhydrase 2, mitochondrial
- Cystathionine beta-lyase, chloroplastic
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 2
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial
- Bifunctional cystathionine gamma-lyase/cysteine synthase
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase C1, mitochondrial
- Protein DETOXIFICATION 34
- Assimilatory sulfite reductase
Sequence:
MRGRSLTLSRVKLELARRSMSATSVPSMADFLTKKPYSPPSWASHLRPLPSHTFSLAHLPTPIHRWNLPGLPNGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYLNLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYSSIGSEALTNALKEKLEKEGKKPYVIPVGGSNSLGTWGYIEAAREIEEQLNYRPDDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLDGLHAGVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDPKCWEGRKILFIHTGGLLGLYDKVDQMASLMGNWSRMDVSESVPRKDGVGKMF
Protein: Methylated RNA-binding protein 1 (PHOsphate metabolism protein 92) (YTH domain-containing protein PHO92) (Q06390)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein that acts as a post-transcriptional regulator of phosphate metabolism by binding to the 3'-UTR region of PHO4 mRNA, decreasing its stability. Acts by recognizing and binding N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs.
Interaction partners:
- Poly
- N
Sequence:
MNQIWSTGPPNFYFNSEWKENKRNDRTIEDSLRELDGLIHSLERTHIEVQTNPKLKNDVTALNDINKKENKEEITHENYTHQINSIPLTSSNLNRHFSFSRDYNQSDNSNNNYYREYLSKPRYLQQSTKEQTFNEINKRKSAAIIPPWLNIPENSRFFVIKSSSLKHVKRSFYNGIWSSTHFGNKRLSEAYKKLNSGAKVFLFFSINTSGRFCGVAEMVSDLKMDLDTSIWEDEQKYGKAFKVRWVIVRDINNRSLKRFLIPSNEMKPITHSRDTQEIPYSIGISIINLFKTQDSDIFSFLDETYE
Protein: Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) (Q728S0)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}.
Interaction partners:
- Phenylalanine--tRNA ligase alpha subunit
- Isoleucine--tRNA ligase
- Small ribosomal subunit protein uS2
- Leucine--tRNA ligase
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL15
- DNA-directed RNA polymerase subunit beta
- GMP synthase
- Tyrosine--tRNA ligase
- Small ribosomal subunit protein uS19
Sequence:
MLLSLKWLREFVPFEGTAAELGDRLTMLGLELEEIIRPFDAIEPIVVGHVVSRERHPEADKLSVCKVDVGQGEPLDIVCGAPNVAAGQRVPVALVGTTMPGGMVIKKAKLRGQPSHGMICSERELGLGEDHDGIMVLPESFRIGARLVDELDLDREVCDIAITPNRADCLSVLGLAREVALAFGLPLTMPALDLKEEGADASNALRIDIPDASLCPLFHGRVLEGAAVRKSPAWMRYRLIAVGVRPISNIVDVTNYILMELGQPLHAYDLDLLAGGRIEVSAAREGERLTTLDGVERVLTSNDLLIRDGEKPVGLAGVMGGAETEISDKSSRVFLEAAVFRPGTIRKTARRLGLSSEASYRFERGVDQVVCTYAMNRAAQLIAGLSGATLRPGICHNEPLPWQAPVLRFRRARGEALLGISLDETFCRETLERLGCKVDAADAADWKVTAPSHRRDFEREADLIEEVARVRGMDTIEPVLPKVMRPLDRAGAPESKYSFWLRLKHWAAGLGLNEAINYSFVGQKDLDHLNLAVDGRIPIMNPLTADQNVLRTELAPGLLQNLRHNIAQGNAGLRLFEVAHIFEADATSDTTARERARLDILVYGSRYDSQWPHVEADADYADIKGIVEHCLAFLHLEGATFTLAASHPFLMPCVDVAVQGRQVGVIGRVRPEIADAYHARKDAWLADLDLDVLRELHDAARIAFRSLPVYPPVRRDITVAAPGSLQVGAVLDHILGLRLPLLCGVELIDVFEPEGKDERNLTFRMTFRHASRTLKDAEVDKERDKVAHSLVEKLPVRI
Protein: Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1) (Q4KM74)
Organism: Rattus norvegicus (Rat)
Function: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14742712}; Single-pass type IV membrane protein {ECO:0000269|PubMed:14742712}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:14742712}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:14742712}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:14742712}. Melanosome {ECO:0000250|UniProtKB:O75396}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus. {ECO:0000269|PubMed:14742712}.
Interaction partners:
- BET1 homolog
- Golgi SNAP receptor complex member 2
- Syntaxin-5
- Syntaxin-4
- Syntaxin-18
- BET1-like protein
- Synaptobrevin homolog YKT6
- Golgi SNAP receptor complex member 1
- Alpha-soluble NSF attachment protein
- Vesicle transport protein USE1
Sequence:
MVLLTMIARVADGLPLAASMQEDEQSGRDLQQYQSQAKQLFRKLNEQSPTRCTLEAGAMTFHYIIEQGVCYLVLCEAAFPKKLAFAYLEDLHSEFDEQHGKKVPTVSRPYSFIEFDTFIQKTKKLYIDSRARRNLGSINTELQDVQRIMVANIEEVLQRGEALSALDSKANNLSSLSKKYRQDAKYLNMRSTYAKLAAVAVFFIMLIVYVRFWWL
Protein: Supernumerary limbs, isoform B (A0A0B4KHK1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cullin homolog 1
- Cullin 6
- Axin
- GEO01111p1
- RING-box protein 1A
- S-phase kinase-associated protein 2
- RT03845p
- GEO01805p1
- Armadillo segment polarity protein
- Transcriptional activator cubitus interruptus
Sequence:
MMKMETDKIMDETNSNAQAFTTTMLYDPVRKKDSSPTYQTERELCFQYFTQWSESGQVDFVEHLLSRMCHYQHGQINAYLKPMLQRDFITLLPIKGLDHIAENILSYLDAESLKSSELVCKEWLRVISEGMLWKKLIERKVRTDSLWRGLAERRNWMQYLFKPRPGQTQRPHSFHRELFPKIMNDIDSIENNWRTGRHMLRRINCRSENSKGVYCLQYDDGKIVSGLRDNTIKIWDRTDLQCVKTLMGHTGSVLCLQYDDKVIISGSSDSTVRVWDVNTGEMVNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMTSPSEITLRRVLVGHRAAVNVVDFDEKYIVSASGDRTIKVWSTSSCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNSIRLWDIECGACLRVLEGHEELVRCIRFDTKRIVSGAYDGKIKVWDLVAALDPRAASNTLCLNTLVEHTGRVFRLQFDEFQIVSSSHDDTILIWDFLNFTPNENKTGRTPSPALMEHXHFVQRQLRELHLQSSSEGEEDDDADEDDEDDFEEEDSRNDAGAFMGGYVRHRDAGGSGSVTGSGSDPESDDLDFDIDVENINDYDE
Protein: Putative disease resistance protein At3g15700 (Q9LW09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential disease resistance protein.
Interaction partners:
- Extensin-like protein
- Uncharacterized protein
- Endoglucanase 5
- Peroxidase 60
- Peroxidase 7
- Peroxidase 35
- DUF241 domain protein, putative
- Calcium-transporting ATPase 12, plasma membrane-type
- Calcium-transporting ATPase 1
- Peroxidase 73
Sequence:
MGKDFKSMVTRCIYVGKENDNVKKLKTATEELKDLRNIVMKRVKMYEDQQKLKRLEKVQVWLRQADVAIKEAEEMLITLMSSSSSNGSSMMSFHKLDKKLCKKLKEVQEIKSRGTFDVVVENSGIGSGSMMISNVDRDDQTVGLEAVSGLVWRCMTVDNTGIIGLYGVEGVGKTTVLTQVNNRLLQHKLNGFDFVIWVFVSKNVNLEKIQDTIREKIGFLDRSWMSKTEEEKAGKIFEILSKRRFALFLDDVWEKVDLVKAGVPPPDGLNRSKIVFTTCSDEVCQEMGAQTKIKMEKLPWERAWDLFKMNAGEEIVKSHPDITKVAQEVAAKCDGLPLALVTIGRAMASKKTPQEWRDALYILSTSPPNFSGPIL
Protein: phospholipase A2 (EC 3.1.1.4) (A0A590UK51)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLVNPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRQLQDLMHISRARKPAFILGSMRDEKRTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKAAETVRLSDTSQSNSPIACGWGAWDPEWEASPKIIQQIGSRACSEANKRGSGRAQRLTPVIPALWEAEGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLLLSP
Protein: Glucose-fructose oxidoreductase domain-containing protein 1 (Gfo/Idh/MocA-like oxidoreductase domain-containing protein 1) (Q9NXC2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- NF-kappa-B inhibitor-interacting Ras-like protein 2
- Glucose-fructose oxidoreductase domain-containing protein 2
- Ral GTPase-activating protein subunit alpha-2
- Putative keratin-associated protein 20-4
- dTDP-D-glucose 4,6-dehydratase
Sequence:
MLPGVGVFGTSLTARVIIPLLKDEGFAVKALWGRTQEEAEELAKEMSVPFYTSRIDEVLLHQDVDLVCINLPPPLTRQIAVKTLGIGKNVICDRTATPLDAFRMTSAAHYYPKLMSIMGNVLRFLPAFVRMKQLIEEGYVGEPLVCEVQVHGGSLLGKKYNWSCDDLMGGGGLHSVGTYIIDLLTFLTGQKAVKVHGLLKTFVKQTDHIKGIRQITSDDFCTFQMVLEGGVCCTVTLNFNVPGEFKQDVTVVGSAGRLLAVGTDLYGQRNSAPEQELLVQDATPVSNSLLPEKAFSDIPSPYLRGTIKMMQAVRQAFQDQDDRRTWDGRPLTMAATFDDCLYALCVVDTIKRSSQTGEWQNIAIMTEEPELSPAYLISEAMRRSRMSLYC