wanglab/gogpt-training-data huggingface dataset:
Protein: Endoglucanase (EC 3.2.1.4) (A3DBF5)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Interaction partners:
- Cellulose 1,4-beta-cellobiosidase
- Type 3a cellulose-binding domain protein
- Cellulosomal-scaffolding protein A
Sequence:
MKKMGLGRFSNKFVLTVLLFFLTAVLLPSSSFESKVQAASSPRYGGAYYNYGEALQKAILFYKANRLGDLPDDYILPYRADAAMTDGQDVGLDLTGGWADAGDGIKFTHPMSYAAGQLGWAVYEYRQAFEKAGLLDDILDEIKWATDFFIKAHPEPNVLYYMCGYNDSDHSVWVPHELLDYVTDRKSFVLNPSTPGSDVAGQTAACLAIASIIFEPTDPEYAETCLTHAKQIFEFGDKYRGKNPLDVLYPSGGYLDDLAWGAVWLYIKTGDSTYLEKAKSFLPVTSLGGGHTHCWDDVSYGAALKIAQLTHDEGYAAMVEKNLDFWLPGGGITYTPGGLAWLSPWGSLRYASTAAFLAFVWADDPTVGTPSKKETYRAFAEKQINYILGDNPRKGSYVVGFGENSPKHPHHRTAHGSWVSMLEVPSFHRHILYGALVGGPSSDDSWEDDISDYTRNEVATDYNAGFVGALAKMYDMYGGEPLENWPQPEDFRAPEDDIVEYFCRGWIIYEGYGTLNLLLQVNNRSGWPPTMKDKLSVRYFMDLTEVFESGGTVDDVQISLGQNEGAKLIGLKHYRDNIYYFTVDFTGTMIMPAEWEMCEKDAHVTIKYRDGITGSNENDWSYQNLRKDPDYDATSFAGLTPYIPVYDNGVLLWGEEPPAGGDDPGSSPPPTPTEPVIVYGDLNGDGNINSTDFTMLKRAILGNPAPGTNLAAGDLNRDGNTNSTDLMILRRYLLKLIGSLPI
Protein: Lysosomal protective protein (U3KQ41)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVT
Protein: Acyl-coenzyme A synthetase ACSM3, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 3) (Butyrate--CoA ligase 3) (Butyryl-coenzyme A synthetase 3) (Middle-chain acyl-CoA synthetase 3) (Propionate--CoA ligase) (EC 6.2.1.17) (Protein SA homolog) (Q3UNX5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism. Capable of activating medium-chain fatty acids with a preference for isobutyrate among fatty acids with 2-6 carbon atoms.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15525578}. Mitochondrion matrix {ECO:0000269|PubMed:11470804}.
Interaction partners:
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Solute carrier family 7 member 13
- Peroxisomal acyl-coenzyme A oxidase 1
Sequence:
MVMLLRARCFQRLAIPDPMRVLYKDYRTATPQNFSNYESMKQDFKIEIPEYFNFAKDVLDQWTNMEKAGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLKKEIQEHVKKTTAPYKYPRKVEFIEELPKTVSGKVKRNELRKKEWVTT
Protein: Vimentin (P20152)
Organism: Mus musculus (Mouse)
Function: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19029034, ECO:0000269|PubMed:27559293}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}. Cell membrane {ECO:0000269|PubMed:19029034}.
Interaction partners:
- Desmin
- Caspase-7
- Caspase-3
- Zinc finger protein SNAI1
- Caspase-8
- Zinc finger E-box-binding homeobox 1
- Fibronectin
- Cadherin-1
- Zinc finger protein SNAI2
- Telethonin
Sequence:
MSTRSVSSSSYRRMFGGSGTSSRPSSNRSYVTTSTRTYSLGSALRPSTSRSLYSSSPGGAYVTRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPTFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
Protein: Serine/threonine-protein kinase (EC 2.7.11.13) (Q9VE91)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR000552}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MEGPEVTFLFQFGSVRDAVCVPANSLTLKTLKDLACDFINTKIPDSGLTYLSERILLFVHDYSTPNVLHIINSAAEVVDETLVEIVLTASPILYPTSEMPTLKPHSLNVHSYKGPTFCDFCGEMLFGLVRQGLKCDGCGQNYHKRCVVKIPNNCNRSNDATSRRSFTLQAPRSPSGSSQQSLVSTEDSTGRNDSSSSLNIPGRHQRTHSSGSRNGLMVLRIPHTFMVHTYGIPTVCQLCKKLLKGLFKQGLQCRDCQYNTHKKCMDKVPHDCTGEAQLSQLQIQAGAKERDNFFREEFDDSDGDDGSEYGKYKSAMSSGVNLVAGRPREAPKALTNAHNSPPELVNGGLVDDSSVSGGETSKSSSDGQSEQSQSSTSSSPSANIPLMRIVQSVKHTKKRGGQALKEGWLVHYTSLDKAVKRYYWRLDSKTITLFVSEQGSKYHKELPLAELLSIESHLGDPRPECNYCFELRLPNLSYFVGQDPQVGAKEEQAVRLPPPDSGIGSDIAKSWETSIRQAFMHVTNTQCCESEEQVQDMGQLYQIFPDEVLGSGQFGVVYGGVHKKTQREVAIKVIDKLRFPTKQEAQLKNEVAILQNISHCGVVNLERMFETPERIFVVMEKLKGDMLEMILSHARGRLSERVTKFLITQILIALKYLHSQNIVHCDLKPENVLLSSDAEFPQVKLCDFGYARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEEEDINDQIQNAAFMYPPNPWKEISSNAIDLINNLLQVKQRKRYTVDKSLLHYWLQDKQTYRDLRNLEAQVGAGRYLTHEADDLRWDCAGDM
Protein: Choline dehydrogenase, mitochondrial (CDH) (CHD) (EC 1.1.99.1) (Q8BJ64)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:20371614}.
Interaction partners:
- Alpha-aminoadipic semialdehyde dehydrogenase
- Phosphatidylethanolamine N-methyltransferase
- Choline/ethanolaminephosphotransferase 1
- Ethanolaminephosphotransferase 1
- Intraflagellar transport protein 52 homolog
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phospholipase D2
- Phospholipase A and acyltransferase 3
- Phospholipase D1
- Membrane-bound glycerophospholipid O-acyltransferase 1
Sequence:
MWQVLRGWRKGWQSPRGALAWAVQGQPCPPCSRAVASVGKDEYTFVVVGAGSAGCVLASRLTEDPNHRVLLLEAGPKDLLMGSKRLQWKIHMPAALVSNLCDDKYNWYYHTEPQPGMDSRVLYWPRGRVWGGSSSLNAMVYIRGHAEDYNRWHREGAEGWDYAHCLPYFRKAQRHELGANMYRGGDGPLHVSRGKTNHPLHQAFLQAARQAGYPFTEDMNGFQQEGFGWMDMTVHQGKRWSTACAYLHPVLSRPNLRAEVQTLVSRVLFEGTRAVGVEYIKDGQRHKAYVSREVILSGGAINSPQLLMLSGVGNADDLRKLDIPVVCHLPGVGQNLQDHLEVYVQQACTQPITLHSAQKPLRKVCIGLEWLWSYTGDGATAHLETGGFIRSRPGVPHPDIQFHFLPSQVIDHGRKPTQQEAYQVHVGTMRATSVGWLKLRSANPRDHPVIHPNYLSTETDVEDFRQCVRLSREIFAQEALAPFRGKELQPGSHVQSDKEIDAFVRAKADSAYHPSCTCKMGRSSDPTAVVDAQTKVIGVENLRVVDASIMPSVVSGNLNAPTVMIAEKAADIIKGHPALEDKNVPVYKPQTLDTQR
Protein: Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) (P04179)
Organism: Homo sapiens (Human)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Superoxide dismutase
- WD repeat-containing protein 5
- Histone acetyltransferase KAT2A
- Forkhead box protein O3
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Aconitate hydratase, mitochondrial
- Cytoplasmic aconitate hydratase
- Parkinson disease protein 7
- Catalase
- Glutathione peroxidase 7
Sequence:
MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
Protein: IP01552p (Sox21a, isoform A) (Q9VUD1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSISALLHRSHSHSNGYTSSGSSNHSHSSSLSPQLPGINLGLGMVGGLGMGMSVGVGSGSGNTTPPPMPPADLAVPPAAPTPVAPKMHQHTHHHGNSHHNAPTSHSNSNTGSHHNSHDHIKRPMNAFMVWSRGQRRKMAQDNPKMHNSEISKRLGAEWKLLTEGQKRPFIDEAKRLRALHMKEHPDYKYRPRRKPKTLNKSPVPGGGGGGGGGGANGGVNAGGAGNSGPSGPGSVGSPKDMQPQLSPLGQSLPHLHGHPHQSPYQSHPHHPHPHPHHVQLAAATLSAKYGFGSPLELSLPRLPNAFPGLAHYPLDPTLALDLQARLQAMYAGSIYHPWRYLPLISPETPPSPPSSSGTGISSYGCVKSEKSSPNAVVASAASPPNII
Protein: ribonuclease III (EC 3.1.26.3) (Q7KNF1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD23072p
- Protein argonaute-1
- LD06392p
- Protein Loquacious
- LD26789p
- Endoribonuclease Dcr-2
- Protein argonaute-2
- TAR DNA-binding protein 43
- Endoribonuclease Dcr-1
- Protein piwi
Sequence:
MYQPPLPPPPVQPAPPPPPPPPEEDLSPPGVGVPSHNYSSNESHSQSSKSLDYVYPETPAPYASSVPSYDPYQQPPAYGYEGYAYNEQAQKYGGQESHYQYQYPASGSSFLYESYKYPDRYPAYSSNYRPPSERQRYTSNSSSQGYHHYPGYSSGRRYEQRHDQEHRQIQDSRYAHEPRHGHYAHRQAKGSQHGYYGSAARNQVSDDYSPRGHHERERNETLEKTRAKPKVETERDRLLRQWCSNFCEKPEDYVKKMNALSEADAPVESWVRSSPAELYYERTKSENEVRGRARLQKLCTLFDEELLQRAKRVREKLPVYVPPPRKARRRVCKHKHKSEACSSSSSSDDDSDEDAFKIEQDCCMEELSRKVQHPQRVHADLWHNDAGEMNDGPLCRCSAKSRRIGIRHGIYPGETGYKLCDPNSNNAGKLFHYRISISPPTNFLTKTPTIIKHDEHEFLFEGFSLLSHVRLSDLPVCKVIRFNIEYTIEYEEEKMPENFTIHELDIFFKYLFHELLELVDFNLMPNLPSGNVEESCPAFHFFPRFVRDLPDNGKEVLAMVEVLRYLLDNSAQLVERQQLLHLNQISQSEWQNYVDFIKGMLVTKPGYKPCSLRVDQLDRNNSDLPECVDRETGISHPAIVHFGICHPQLSYAGNPEYQKAWREYVKYRHLMANMSKPSFKDKRKLEEKEQRLQEMRTQGRMKRNITVAISSEGFYRTGIMCDVVQHAMLIPVLTGHLRFHKSLDLLEESIGYRFKNRYLLQLALTHPSYKENYGTNPDHARNSLTNCGIRQPEYGDRKIHYMNTRKRGINTLVSIMSRFGKEHETVSNITHNERLEFLGDAVVEFLSSIHLFFMFPELEEGGLATYRAAIVQNQHLALLAKKLQLEEFMLYAHGSDLCHELELRHAMANCFEALMGALLLDGGIKVADEVFTDALFRQDEKLLSIWKNLPEHPLQEQEPLGDRSCIDSYRVLKELTKFEDSIGIKFKHIRLLARAFTDRSIGFTHLTLGSNQRLEFLGDTVLQLICSEYLYRHFPEHHEGHLSLLRSSLVNNRTQAVVCDDLGMPKYAVYANPKADLKTKDRADLLEAFLGALYVDKGLLYCEQFCHVCLFPRLQLFIMNQDWNDPKSKLQQCCLTLRTMDGGEPDIPYYKVVEASGPTNTRVYKVAVYFRSKRLATSSGSSIQQAEMNAAKQALENSRDLFPQLDHQKRVIAKSIKKQTGNELDNDSDRQHQEEKIKRPKYATPLQDESHLPKQYRMHENISSDELPEDEDFESTAPKSPTMPLRSNRSGSSSSSSSSDSDGSTSSPKCKRRLKKCSSVSSKSSLG
Protein: Ubiquitin carboxyl-terminal hydrolase MINDY-2 (EC 3.4.19.12) (Deubiquitinating enzyme MINDY-2) (Protein FAM63B) (Q8NBR6)
Organism: Homo sapiens (Human)
Function: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins. Binds to polyubiquitin chains of different linkage types, including 'Lys-6', 'Lys-11', 'Lys-29', 'Lys-33', 'Lys-48' and 'Lys-63'. May play a regulatory role at the level of protein turnover.
Interaction partners:
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MESSPESLQPLEHGVAAGPASGTGSSQEGLQETRLAAGDGPGVWAAETSGGNGLGAAAARRSLPDSASPAGSPEVPGPCSSSAGLDLKDSGLESPAAAEAPLRGQYKVTASPETAVAGVGHELGTAGDAGARPDLAGTCQAELTAAGSEEPSSAGGLSSSCSDPSPPGESPSLDSLESFSNLHSFPSSCEFNSEEGAENRVPEEEEGAAVLPGAVPLCKEEEGEETAQVLAASKERFPGQSVYHIKWIQWKEENTPIITQNENGPCPLLAILNVLLLAWKVKLPPMMEIITAEQLMEYLGDYMLDAKPKEISEIQRLNYEQNMSDAMAILHKLQTGLDVNVRFTGVRVFEYTPECIVFDLLDIPLYHGWLVDPQIDDIVKAVGNCSYNQLVEKIISCKQSDNSELVSEGFVAEQFLNNTATQLTYHGLCELTSTVQEGELCVFFRNNHFSTMTKYKGQLYLLVTDQGFLTEEKVVWESLHNVDGDGNFCDSEFHLRPPSDPETVYKGQQDQIDQDYLMALSLQQEQQSQEINWEQIPEGISDLELAKKLQEEEDRRASQYYQEQEQAAAAAAAASTQAQQGQPAQASPSSGRQSGNSERKRKEPREKDKEKEKEKNSCVIL
Protein: KAT8 regulatory NSL complex subunit 2 (NSL complex protein NSL2) (Non-specific lethal 2 homolog) (F8VX10)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAVLFPLSSCGWAAISLFLSAQSCYSASKQCQSQSPSCRLPGARISGDWSRRTKWRSHRLPRPGPVVRSEAGRDKGGVRGGGVAAAWGWCCRFPSCCSCASPEDTFSVVWFGVGPGMEGHAKGRQSHRCLWRLGEGGGDLRSVPYGDDFCMSFGNCPRDLCGAGIFGKGKGFLVFRLTPQVLVMNRIRIHVLPTNRGRITPVPRSQEPLSCAFTHRPCSHPRLEGQEFCIKHILEDKNAPFKQCSYISTKNGKRCPNAAPKPEKKDGVSFCAEHVRRNALALHAQMKKTNPGPVGETLLCQLSSYAKTELGSQTPESSRSEASRILDEDSWSDGEQEPITVDQTWRGDPDSEADSIDSDQEDPLKHAGVYTAEEVALIMREKLIRLQSLYIDQFKRLQHLLKEKKRRYLHNRKVEHEALGSSLLTGPEGLLAKERENLKRLKCLRRYRQRYGVEALLHRQLKERRMLATDGAAQQAHTTRSSQRCLAFVDDVRCSNQSLPMTRHCLTHICQDTNQVLFKCCQGSEEVPCNKPVPVSLSEDPCCPLHFQLPPQMYKPEQVLSVPDDLEAGPMDLYLSAAELQPTESLPLEFSDDLDVVGDGMQCPPSPLLFDPSLTLEDHLVKEIAEDPVDILGQMQMAGDGCRSQGSRNSEKASAPLSQSGLATANGKPEPTSIS
Protein: Putative histone H1.9 (H1.9 linker histone pseudogene) (Putative spermatid-specific linker histone H1-like protein) (P60008)
Organism: Homo sapiens (Human)
Function: DNA-binding protein that may be implicated in chromatin remodeling and/or transcriptional regulation during spermiogenesis, the process of spermatid maturation into spermatozoa.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
Interaction partners:
Sequence:
MLHASTIWHLRSTPPRRKQWGHCDPHRILVASEVTTEITSPTPAPRAQVCGGQPWVTVLDPLSGHTGREAERHFATVSISAVELKYCHGWRPAGQRVPSKTATGQRTCAKPCQKPSTSKVILRAVADKGTCKYVSLATLKKAVSTTGYDMARNAYHFKRVLKGLVDKGSAGSFTLGKKQASKSKLKVKRQRQQRWRSGQRPFGQHRSLLGSKQGHKRLIKGVRRVAKCHCN
Protein: Purine-rich binding protein-alpha, isoform B (Purine-rich binding protein-alpha, isoform F) (Q9V4D9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Fragile X messenger ribonucleoprotein 1 homolog
- LD24793p
- Heterogeneous nuclear ribonucleoprotein A1
- ATP-dependent RNA helicase me31b
- Eukaryotic translation initiation factor 4E1
- LD37574p
- Protein muscleblind
- Trailer hitch, isoform H
- TAR DNA-binding protein 43
- Translational regulator orb2
Sequence:
MSDLGSGDDGISGSKYNVANMEGSSSRNDFDSSAKGGSGVEQELATKMLQIQSKRFYLDVKQNRRGRFIKVAEIGADGRRSQIYLALSTAAEFRDHLSSFSDYYASLGPPNTDNLPEDGKLKSEMMIKDYRRYYLDLKENARGRFLRVSQTITRGGPRSQIALPAQGMIEFRDALTDLLEEFGANDGGRFKGDLPEERHMKVDNKNFYFDIGQNNRGVYMRISEVKNNFRTSITIPEKCWIRFRDIFNDYCEKMKKSSDSITAEINLPTSSNSLK
Protein: LIM domain-binding protein 2 (LDB-2) (Carboxyl-terminal LIM domain-binding protein 1) (CLIM-1) (LIM domain-binding factor CLIM1) (O43679)
Organism: Homo sapiens (Human)
Function: Transcription cofactor. Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:9853615}.
Interaction partners:
- Rhombotin-2
- Erythroid transcription factor
- T-cell acute lymphocytic leukemia protein 1
- Transcription factor E2-alpha
- Endothelial transcription factor GATA-2
- Protein CBFA2T3
- Protein lyl-1
- Insulin gene enhancer protein ISL-1
- Rhombotin-1
- LIM/homeobox protein Lhx2
Sequence:
MSSTPHDPFYSSPFGPFYRRHTPYMVQPEYRIYEMNKRLQSRTEDSDNLWWDAFATEFFEDDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESYHNSSITVDCDQCTMVTQHGKPMFTKVCTEGRLILEFTFDDLMRIKTWHFTIRQYRELVPRSILAMHAQDPQVLDQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAEPTRQPTTKRRKRKNSTSSTSNSSAGNNANSTGSKKKTTAANLSLSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQYDAANGMDDEEDFNNSPALGNNSPWNSKPPATQETKSENPPPQASQ
Protein: WRKY transcription factor WRKY71 (OsWRKY71) (Q6IEL0)
Organism: Oryza sativa subsp. indica (Rice)
Function: Transcription repressor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Represses specifically gibberellic acid (GA)-induced promoters in aleurone cells, probably by interfering with GAM1. Regulates, probably indirectly, the activation of defense-related genes such as GF14E during defense response (By similarity). Modulates plant innate immunity against X.oryzae pv. oryzae (Xoo) (By similarity). Confers resistance to the virulent bacterial pathogen X.oryzae pv. oryzae (Xoo) 13751, probably via the regulation of NPR1 and PR1b defense signaling pathways.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223, ECO:0000269|PubMed:15047897}. Note=Localized in nuclei of aleurone cells. {ECO:0000269|PubMed:15047897}.
Interaction partners:
Sequence:
MDPWISTQPSLSLDLRVGLPATAAVAMVKPKVLVEEDFFHQQPLKKDPEVAALEAELKRMGAENRQLSEMLAAVAAKYEALQSQFSDMVTASANNGGGGGNNQSSTSEGGSVSPSRKRKSESLDDSPPPPPPPHPHAAPHHMHVMPGAAAAGYADQTECTSGEPCKRIREECKPKISKLYVHADPSDLSLVVKDGYQWRKYGQKVTKDNPCPRAYFRCSFAPACPVKKKVQRSAEDNTILVATYEGEHNHGQPPPPLQSAAQNSDGSGKSAGKPPHAPAAAPPAPVVPHRQHEPVVVNGEQQAAAASEMIRRNLAEQMAMTLTRDPSFKAALVTALSGRILELSPTKD
Protein: Putative invertase inhibitor (Pollen allergen Pla a 1) (allergen Pla a 1.0101) (Q8GT41)
Organism: Platanus acerifolia (London plane tree)
Function: Invertase inhibitor (Probable).
Subcellular location: Secreted {ECO:0000269|Ref.4}. Secreted, cell wall {ECO:0000269|Ref.4}. Endoplasmic reticulum {ECO:0000269|Ref.4}. Note=After 5 minutes in germination medium, detected as a soluble protein and released from apertural and non-apertural regions of pollen grain wall. In mature, non-hydrated pollen grains, predominantly associated with the endoplasmic reticulum (ER) concentric cisternae, which are situated between the vegetative nucleus and the generative cell. After 5, 15 and 30 minutes as well as 2 hours of hydration, localization to this ER region is noticeably decreased. {ECO:0000269|Ref.4}.
Interaction partners:
Sequence:
MKLSFSLCIFFFNLLLLLQAVISADIVQGTCKKVAQRSPNVNYDFCVKSLGADPKSHTADLQGLGVISANLAIQHGSKIQTFIGRILKSKVDPALKKYLNDCVGLYADAKSSVQEAIADFKSKDYASANVKMSAALDDSVTCEDGFKEKKGIVSPVTKENKDYVQLTAISLAITKLLGA
Protein: Ribonuclease H1 (RNase H1) (EC 3.1.26.4) (Q7JY33)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ribonuclease H2 subunit A
- Single-stranded DNA-binding protein, mitochondrial
- Aquaporin
- Senataxin, isoform B
- DNA topoisomerase 1
- DNA topoisomerase 3-alpha
- ATP-dependent DNA helicase PIF1
- Flap endonuclease 1
- NIF3-like protein 1
- Mitochondrial tRNA-specific 2-thiouridylase 1
Sequence:
MLLPRYFCWNLQRCTMAFYAVASGRRSGVYGSWAECEEQVKGFKNAKYKKFKTRQEADQFVNGCKSYAPQDVAVPLGKEKASLASWKNSIEVNKNPKYTDEWPEEDHDLAEDDLNAAMNEVEGDPKPSNSSNLPDILNRKRKGTTSGDKRNKIPRHASQVSEATGLKQVGAFQFEIDAEGYVIVYTDGSCIGNGRAGACAGYGVYFGKNHQLNAAKPVEGRVTNNVGEIQAAIHAIKTALDLGIQKLCISTDSQFLINSITLWVAGWKKRDWKLKNNQPVKNVVDFKELDKLLQENNITVKWNYVEAHKGIEGNEMADKLARQGSALYKQKNG
Protein: Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) (Aspartate beta-hydroxylase) (ASP beta-hydroxylase) (Peptide-aspartate beta-dioxygenase) (Q8BSY0)
Organism: Mus musculus (Mouse)
Function: Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q28056}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28056}.; SUBCELLULAR LOCATION: [Isoform 2]: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:8530521}; Single-pass type II membrane protein {ECO:0000303|PubMed:8530521}.
Interaction partners:
- Triadin
- Calsequestrin-1
- Ryanodine receptor 2
- Calsequestrin-2
- Ryanodine receptor 1
- Ryanodine receptor 3
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Peptidyl-prolyl cis-trans isomerase FKBP1B
- Junctophilin-1
- Peptidyl-prolyl cis-trans isomerase FKBP1A
Sequence:
MAPRKNAKGGGGNSSSSGSGSGSGSGSPSTGSSGSSSSPGARREAKHGGHKNGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKERSPSERTFPPEEEAETHAELEEQAPEGADIQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEDLEPGTVHEEIEDTYHVEDTASQNHPNDMEEMTNEQENSDPSEAVTDAGVLLPHAEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQQDTPPVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADLPDAPTDLVKLSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPRETGYTELVKSLERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCALLEKFSETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
Protein: Transcription factor PU.1 (Q6BDS1)
Organism: Rattus norvegicus (Rat)
Function: Pioneer transcription factor, which controls hematopoietic cell fate by decompacting stem cell heterochromatin and allowing other transcription factors to enter otherwise inaccessible genomic sites. Once in open chromatin, can directly control gene expression by binding genetic regulatory elements and can also more broadly influence transcription by recruiting transcription factors, such as interferon regulatory factors (IRFs), to otherwise inaccessible genomic regions (By similarity). Transcriptionally activates genes important for myeloid and lymphoid lineages, such as CSF1R or FCER1A. Transcriptional activation from certain promoters, possibly containing low affinity binding sites, is achieved cooperatively with other transcription factors. FCER1A transactivation is achieved in cooperation with GATA1. May be particularly important for the pro- to pre-B cell transition. Binds (via the ETS domain) onto the purine-rich DNA core sequence 5'-GAGGAA-3', also known as the PU-box (By similarity). In vitro can bind RNA and interfere with pre-mRNA splicing (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
Interaction partners:
- Runt-related transcription factor 1
- Macrophage colony-stimulating factor 1 receptor
- Interferon regulatory factor 8.
- Retinoic acid receptor, alpha
- Receptor-type tyrosine-protein kinase FLT3
- CCAAT/enhancer-binding protein alpha
- Fc fragment of IgG receptor Ia.
- RUNX1 partner transcriptional co-repressor 1
- Interferon regulatory factor 1
- Erythroid transcription factor
Sequence:
MLQACKMEGFPLVAPPSDELVTYESELYQRQTHDYYSLIGGDGDSHSDHYWDFSTHHVHSEFESFPENHFTELQSVQPPQLQQLYRHMELEQMHVLDTPMAPPHASLSHQVSYMPRVCFPYPPLSPAHQQSSDEEEGERQSPPLEVSDGEADGLEPGPGLLHGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRLPPH
Protein: Purine-uracil permease NCS1 (Nucleobase cation symporter 1) (AtNCS1) (Plastidic nucleobase transporter) (Uracil/purine transport protein NCS1) (Q9LZD0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleobase-proton symporter that facilitates the uptake of nucleobases in the cells. Can transport adenine, guanine and uracil. Contributes to uracil import into plastids for plastidic uracil salvage which is essential for plant growth and development.
Subcellular location: Plastid, chloroplast envelope {ECO:0000269|PubMed:22474184}. Plastid, chloroplast membrane {ECO:0000269|PubMed:22474184}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytoplasmic tRNA 2-thiolation protein 2
- Putative nucleobase-ascorbate transporter 9
- Hydroxyethylthiazole kinase
- Nucleobase-ascorbate transporter 12
- Bifunctional TH2 protein, mitochondrial
- Nucleobase-ascorbate transporter 5
- Nucleobase-ascorbate transporter 1
- Nucleobase-ascorbate transporter 8
- Nucleobase-ascorbate transporter 3
- Nucleobase-ascorbate transporter 6
Sequence:
MVSNCLSLSLHLNLHPHKHNRHSLSSLRSRTKAKLYQHVSFTDSSHKSSYTSCVSTFDIQRKSSKHYELGKHSFSPILPGDNLVLSRSGVIRPRLSAMTGSEINDHGYDESQFDPSLTNDDLKPTTPSQRTFSWLDMSSLWIGLVVGVPTYYLAGSLVDLGMAWWQGIATVVTANLILLVPLVLTAQPGTLYGISFPVLARSSFGIRGAHIPTLLRALVGCGWYGIETWIGGEAIFLLLPGHIKKSALSHTLPWLGTSPLEFSCFIVFWLAQLCIVWRGMDGIRKLEKYSAPILISLTSCLLAWSYLKAGGFGHMLSLSSKLTSAQFWTLFFPSLTANISFWATLALNIPDFSRFAKSQTDQIIGQVGLPVFMGLFTFVGVAVTSSTSIIFGRVISNPIELLGQIGGLATTLLAIVGISLATLTTNIAANVVAPANALVNLNPKFFTFGRGAFLTAVLGIVFQPWRLLKSSESFVYTWLIGYSALLGPIGGIILVDYYLIKKMKLNIGDLYSLSPSGEYYFSKGYNVAAVVALVAGIIPVVPGFLHKISALSKISNGFVVVYDNALFFSFIIAGFVYWIIMSRLGRKQSSLSSSSHPLL
Protein: Uncharacterized protein YfgD (P76569)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Beta-barrel assembly-enhancing protease
- Dihydroorotate dehydrogenase
- UPF0370 protein YpfN
- Esterase YpfH
Sequence:
MTKQVKIYHNPRCSKSRETLNLLKENGVEPEVVLYLETPADAATLRDLLKILGMNSARELMRQKEDLYKELNLADSSLSEEALIQAMVDNPKLMERPIVVANGKARIGRPPEQVLEIVG