wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase subunit 8C, mitochondrial (Cytochrome c oxidase polypeptide 8 isoform 3) (Cytochrome c oxidase polypeptide VIII isoform 3) (COX VIII-3) (Cytochrome c oxidase subunit 8-3) (A6H666)
Organism: Mus musculus (Mouse)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P10175}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10175}.
Interaction partners:
- Cytochrome c oxidase subunit 8A, mitochondrial
- Cytochrome c oxidase subunit 8B, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 2, mitochondrial
- Cytochrome c oxidase subunit 7A2, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Heme A synthase COX15
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 7C, mitochondrial
Sequence:
MSRLLLLCSSLLRHRAVLFSKPGHPGRLSHSESPQKKILSPTESAVGIVVFFTTFYIPAAYVLSSLKYFKGE
Protein: Probable glycine betaine-binding protein (Q9HZ04)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
- Probable ATP-binding component of ABC transporter
- Probable permease of ABC transporter
- Probable permease of ABC transporter
- Quaternary amine transport ATP-binding protein
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- 4-vinyl reductase 4VR domain-containing protein
- Glycine betaine monooxygenase reductase subunit
- Glycine betaine monooxygenase oxygenase subunit
- (S)-ureidoglycine aminohydrolase cupin domain-containing protein
- Phosphorylcholine phosphatase
Sequence:
MRMMRRLLCWSAGLAMSAAVGMAAAADKPVITIGYVDGWSDSVATTHVAAEVIREKLGYEVKLMPVAAGIMWQGVARGKLDAMLSAWLPGTHGAYYEKMKDKVVNLAINYPDARIGLIVPEYVSANSIADLQAQKDAFGGRVVGIDAGAGVMIKTDEAIKQYGLDYKLVASSGSGMIAELTRAENEKKPVVVTGWIPHWMFAKWKLKFLDDPKKVYGDTEHVDTVANPALEAKAKPVWEFLKKFGWKDGNEVGQVMLAIQEGAKPEDAAKQWVAANPGRVKDWVQ
Protein: Ubiquitin-conjugating enzyme E2 L3 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme L3) (L-UBC) (UbcH7) (Ubiquitin carrier protein L3) (Ubiquitin-conjugating enzyme E2-F1) (Ubiquitin-protein ligase L3) (P68036)
Organism: Homo sapiens (Human)
Function: Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11278816, ECO:0000269|PubMed:17003263}. Cytoplasm {ECO:0000269|PubMed:11278816, ECO:0000269|PubMed:17003263}.
Interaction partners:
Sequence:
MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD
Protein: Myelin basic protein (MBP) (P02688)
Organism: Rattus norvegicus (Rat)
Function: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity).
Subcellular location: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
Interaction partners:
- Myelin-associated glycoprotein
- Myelin proteolipid protein
- Myelin-oligodendrocyte glycoprotein
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- Glial fibrillary acidic protein
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Oligodendrocyte transcription factor 2
- T-cell surface glycoprotein CD4
- Calmodulin-1
Sequence:
MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKVPWLKQSRSPLPSHARSRPGLCHMYKDSHTRTTHYGSLPQKSQRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR
Protein: leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (Q8MRF8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATTERKGTFKVEYLQKIEREVQQRWEAERVHESDAPTAPKKRQAEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMPIKACADKLTRELEQFGFPPQFPETEEVVPVAAEAASEVPKDKSKGKKSKAVAKTGAAKYQWQIMQSLGLKDEEIKDFANAEHWLNYFPPLAVQDLKRIGVHVDWRRTFITTDANPYFDSFVRWQFNHLKERGKIMYGKRYTIYSPKDGQPCMDHDRSSGEGVGPQEYTLIKMKVLEVPKALSSIKQPIFMVAATLRPETMYGQTNCWLHPDIKYIAWQTNKNNEVWVSTRRAARNMTYQGFTAVEGEIKVLAEVTGQDLLGVPLSAPLTKHKVVYSLPMLSIKEDKGTGVVTSVPSDSPDDYAALVDLQKKEAFRQKYGLKDEMVLPYEPIPIIEVPTLGKLSAVHAYETLKIQSQNDKDKLAEAKEMCYLKSFYDGVMLVGAFAGRKIQDVKKDLQKRLVDANEADVYYEPEKTIMSRSADECVVALCNQWYLNYGEPEWQAQATKILHGMETFHEEARNNFEACLNWLHEYACSRTYGLGTKLPWDDKWLIESLSDSTIYMAFYTVVHLLQGGTFRGEKPGPFGIKPSDMTGEIWDYIFFKETPLPKKTAIKQEHLAVLRREFEYWYPMDLRVSGKDLIQNHLTFCLYNHAAIWPNDENKWPKGMRVNGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCLADAGDSVEDANFVESTADAGILRLYTFIEWVKEMLENRSSLRKGTDKTFNDQVFLSELNLKTQQTDENYRKMLFKEALRSGFYELQLARDKYRELCGANGMHEDLVLEFIRRQALLVSPICPHMAEHVWGLLGNKESIVHARWPEVGAINEVDILCSEYLMESAHSFRLNLKNLLQIKGKAGKDKSVNVQAAKPNRGLVWVAKTYPPWQCCVLDTMKELFNKSQALPDNKVIAATLQQKAELKKFMKRVMPFAQMIREKVESGKGVAALAVTLEFDERQVLISNLEYLKNTLDLDVLEIKYTDDPSAPEKTREEVRPGSPFISFSVAPNVSVELTNPIERSSLFQVNTVISEGDTVQSLREKLSKIIGLKTDAATLKIWRYEDPVLGPRKIPNFEDYKAGKSVLGEGNFVLDVENKKVSLEQAGKLTEVGRNLIYVVD
Protein: MYND-type zinc finger protein samB (Suppressor of anucleate metulae protein B) (O42631)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in determination of the onset of polarized growth and morphogenesis. Plays a role in the regulation of branching in hyphae and spore formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9427754}.
Interaction partners:
- Anucleate primary sterigmata protein A
Sequence:
MREVNFSIPNVNKASVNITTTLYDRRALDCTSTLPLINSLNHLAYLTTSSARIRDILTVDGGIERLVCILKEGRSNNLMEMWKWSLAFQCVVNIGVRGSENVRTRVVEADMVPVIATILDNYIKVMDKVRARSDSEAQRHRHHQLHHKITPTASDSTSRSSFSDASSNEQRTSRRQPPPTHIEIPPFFHDTRAVESNAADVPSPPRAPMTSPPERSTFGQDTYAHRSHAPLRHRAIQPLATAIPSMDAADGSGLRPVRDTERLPSMLPAAFNELASQPDSPTTPSGAGHIRSNVHVPIGTHARPPLSQHQSTSGDSDDANGEDSIMADDTGSGQSRRPIIGLQSRMDIDDDADRQTVIDSVTDSSHDLTVTDTTSDGQESETFNITHRSAVDGSIITNDNAQAVNNANSPPIVPSPYSLYFRDRTNIATQNFLNTMPREEDVLMSLQLLAYVSKYCNLRSYFQNSHFVPKLKIDRELRMLDEGASPVELIEEEDEYLLPDDVNIFPLVEKFTARHHSKDMSYWACVVMRNLCRKDESRGGIRQCANYKCGKWEEFTRQFAKCRRCRRTKYCSKDCQKAAWLYHRHWCATP
Protein: Exocyst subunit Exo70 family protein (Q9SYG5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC5B
- Exocyst complex component SEC5A
- Exocyst complex component SEC10a
- Exocyst complex component EXO84C
- Exocyst complex component EXO84B
- Exocyst complex component SEC3A
- Exocyst complex component SEC3B
- Exocyst complex component EXO84A
Sequence:
MATPETRGVDSDLETAEKIILRWDSTTSEEAKENLIFQSGGDREEVDRYLKAVDEVQRHISSISISDEVKATIQIAMARLEDELRNILISQTSTFEPDSLLLDSSLSSSSFASSSRTELEDDTCDDGNEEEEQQQVDLVLPDGSGSDSGSRRLSRSRRSNSKSTSSIREIDLVTPEAVSDLRSIAQRMIGAGYSRECVQVYGNVRKSAMEMIFKQLGIVKLGIGDVQRLDWEAVEVKIRRWIRAAKVCVRVVFASEKRLCEQIFEGTMEETCFMEIVKTSALQLFNFPEAISISRRSPEKLFKILDLHDAITDLLPDMEEIFDSSSSESILVQATEIQSRLAEAARGILTEFENAVFREPSVVPVPGGTIHPLTRYVMNYLNLISDYRETLIDLVMTKPCRGLKCTNDRNDPDMDISELEGISPLALHMIWTMVMLQFNLEEKSLHYRDEPLSHIFVMNNVHYIVQKVKSSPELMELIGDKYLRKLTGIFRQAATKYQRATWVRVLNSLRDEGLHVSGSFSSGVSKSALRERFKAFNTMFEEVHRIQSTWSVPDTQLREELRISLSEHLIPAYRSFLGRFRGHIESGRHPENYLKYSVENLETAVLDFFEGYTTAPHLRRSQ
Protein: Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2) (O55137)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O88267}.
Interaction partners:
- Cytosolic acyl coenzyme A thioester hydrolase
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Acyl-coenzyme A thioesterase THEM5
- Fructose-1,6-bisphosphatase isozyme 2
- Acyl-coenzyme A thioesterase 3
- Acyl-coenzyme A thioesterase THEM4
- Fructose-1,6-bisphosphatase 1
- Peroxisomal succinyl-coenzyme A thioesterase
- ATP-dependent 6-phosphofructokinase, muscle type
- ATP-dependent 6-phosphofructokinase, liver type
Sequence:
MEATLNLEPSGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLVKRDVQTPFVVELEVLDGHEPDGGQRLAHAVHERHFLAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKNMETMHMEYFEEAVNYLRSHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTISYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVDKKSFIPVERSDTTFLFLVGQDDHNWKSEFYADEISKRLQAHGKEKPQIICYPAAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHAMAQLDAWQQLQTFFHKQLGSECLHVSPKI
Protein: trypsin (EC 3.4.21.4) (Q9VXC9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
- GH14734p
- Peptidase S1 domain-containing protein
- RH54371p
- RH26557p
- trypsin
Sequence:
MLPFWTSLLVLCAAGVLAQNDSVVEPRIVGGTKAREGQFPHQISLRRRGSHTCGGSIISKDYVVTAAHCVKQGNNVAPANELEIQAGSLLLSSGGVRVPVATVTVHPNYNSNGHDVAVLRLRNSLTFNSNIAAIKLATEDPPNDATVDISGWGAISQRGPISNSLLYVQVKALSRESCQKTYLRQLPETTMCLLHPKDKGACYGDSGGPATYQGKLVGLASFVIGGCGRAAPDGYERVSKLRNWIAEKASL
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (Q90ZN9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MATLWIYPSLLFFLFPSLTPSQALRNYPENEVTLLDTMSALGDLGWEAYPAEGWEEISVMDERNTPMRSYQVCNVMEASQNNWFRTRHIAREGAQRVYIEIKFTLRDCNSLPGVPGTCKETFNMYYYESNNPNLWFIKESQYIKIDTIAADESFTQTDVGDRVMRLNTEIRDINNLSKKGFYLAFQDVGACIALVSLRVFYKKCPLAVLNLAQFPDTVTGGDSALVEVRGSCVNDSEEFEAPRMYCSGDGGWLVPIGRCVCKPGFEENKDYCQACRPGTYKASSMDAYCSKCPPHSFSHQEKASECSCEKGFYRADMDPRSMACTRPPSAPENPISTLNDTSVTLEWSPPRDSGGRGDVTYSIHCRKCAGDGRICSPCSNNVHFVPRQFGLSIPKVLITDLLSNTNYTFSVEAVNGVSDLSPTPKQLVTVNITTSQTVNVILKERKSKDSITLAWQGPDRPNGVIVEYEVIYYEKNQRDQNYTVLKTKGHMMTVEGLKPGTTYVFRVRARTDGGYGNYGGEIELETSHEDMLAIGGPNQSTILAVSIAGGIVLLTFLVACFVVSGRHCGYIKAKQDPDEEKMQFQNGRVKLPGSRTYIHPHTYEDPNQAVRDFAKEIDASTIRIERVIGAGEFGEVCSGRLKLPSKREIYVAIKSLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTRCKPVMIITEYMENGSLDTFLKKHDGQFTVIQLVGMMRGIASGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVISYGERPYWEMSNQDVIKAIDEGYRLPAPMDCPVVLHQLMLDCWEKSRSERPKFGQIVNTLDKLIRNPNSLKELANSSVWEDPTTPEFSVSTVDEWLDAINMGQYKDNFANAGYVSLDSILYISMCELSKMDVTLVGHQKKILSAVQSLHAQGTHVQV
Protein: Zn(2)-C6 fungal-type domain-containing protein (G8BCU0)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Lanosterol 14-alpha demethylase
- Zn
- C-8 sterol isomerase
- Fatty acid hydroxylase domain-containing protein
- Pre-rRNA-processing protein IPI3
- Pescadillo homolog
- Pre-rRNA-processing protein
- C-8 sterol isomerase
- Squalene monooxygenase
- Ribosome biogenesis protein ERB1
Sequence:
MLSKDLEDALQGYQTRKEAPESTRRVSSTVIDDELCSLSNASASPPEAVKKNSKASTGKRKYHQKSRSGCSTCKKRRVKCDEQKPLCGNCVKLKLECGYLHMDPEESSPPPPPPKKAKKMKTETESKKAKAVSTGRSSIKSGSDDVIGNNNYSDETSTRNNSIDQRSLDGLNSSTTTQQATPSLTPTPNTSQPSLDSSVPPGNPMATMGQSMNNPLSALSSGLLSAGNLNNLNIAHLVNNLAGMGGVAGDAGNGLNNLMNLGNLANLSNLATLAQLPIDLSNLAGLFGGAGGVGGGLIEQLASAAINGNSGSPLDALLNAQSGQQQQQQQLRSQGRDQLNMGQSNRQQAQYRSTSSDDGQFENQKSAPLQQQQQQQPQPQSSQQPQNLDDSSIDANINLDSQGSASSPPFNIPPHTSSEPVPDSAGTLPNIAPNQTSSIPSSVPLNNKTMAQAMNSSTLNMLDLKLMFHYTSQVANTITGAGISETNIWIHDIPMLAFEHPFLMHSILAFSATHLSRTEKGLDQCVTCHRGDALRLLREAVLDINADNTDALVASALILIMDSLANASFPSSTSPKSLPASAWIFHVKGAATILTAVWPLTEASRFYKFISVDLGDLGDIINQKANLNTTNPSGSTSNGNGERFYADLECHDADIADLFPVEIDSPYLITLAYLNKLHKERYKSDFILRIFAFPALLDKQFMSLLMSGDVKSMRIMRSYYKLLRSFTMEMKDKVWFLEGVAQVLPSNVEEYAGGAGGMHMMMDFLGGGPDIVDDYGNEFDDSDGDEELDGDVAGGNCGVRNGSDANVTTTKRTKMNLTEMTNTNNLPSDITRELDIMQGDQGFINLK
Protein: DNA replication licensing factor MCM4 (EC 3.6.4.12) (A0A3B3ITP6)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSPASTPSRRGSRRGRATPAQTPRSEDARSSPSQRRRGEDSTSTGELQPMPTSPGVDLQSPAAQDVLFSSPPQMHSSAIPLDFDVSSPLTYGTPSSRVEGTPRSGVRGTPVRQRPDLGSAQKGLQVDLQSDGAAAEDIVASEQSLGQKLVIWGTDVNVAACKENFQRFLQRFIDPLAKEEENVGIDITEPLYMQRLGEINVIGEPFLNVNCEHIKSFDKNLYRQLISYPQEVIPTFDMAVNEIFFDRYPDSILEHQIQVRPFNALKTKNMRNLNPEDIDQLITISGMVIRTSQLIPEMQEAFFQCQVCAHTTRVEMDRGRIAEPSVCGRCHTTHSMALIHNRSLFSDKQMIKLQESPEDMPAGQTPHTVILFAHNDLVDKVQPGDRVNVTGIYRAVPIRVNPRVSNVKSVYKTHIDVIHYRKTDAKRLHGLDEEAEQKLFSEKRVELLKELSRKPDIYERLASALAPSIYEHEDIKKGILLQLFGGTRKDFSHTGRGKFRAEINILLCGDPGTSKSQLLQYVYNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMNESTRSVLHEVMEQQTLSIAKAGIICQLNARTSVLAAANPIESQWNPKKTTIENIQLPHTLLSRFDLIFLLLDPQDEAYDRRLAHHLVALYYQSEEQAEEELLDMAVLKDYIAYAHSTIMPRLSEEASQALIEAITKDMFEEALRALADDDFLTVTGKTVRLL
Protein: Packaging protein 2 (Packaging protein 22K) (L4-22K) (P0DJX1)
Organism: Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Function: Component of the packaging machinery which encapsidates the viral DNA into preformed capsids and transcriptional activator of the viral major late promoter (MLP). Binds, along with packaging proteins 1 and 3, to the specific packaging sequence on the left end of viral genomic DNA and plays an active role in packaging of the viral genome into preformed capsids. Specifically binds to the 5'-TTTG-3' nucleotides of the repeats making up the packaging sequence. Forms a transcription factor called DEF-A through cooperative binding with packaging protein 1 (Probable). DEF-A binds to downstream elements of the major late promoter (MLP) and stimulates transcription from the MLP after initiation of viral DNA replication. Simultaneously suppresses early gene expression and is thus likely to participate in the early-late switch in the expression pattern of the late viral proteins. May as well enhance transcription from IVa2 and pIX promoters.
Subcellular location: Host nucleus {ECO:0000269|PubMed:22944109}.
Interaction partners:
Sequence:
MAPKKKLQLPPPPPTDEEEYWDSQAEEVLDEEEEMMEDWDSLDEASEAEEVSDETPSPSVAFPSPAPQKLATVPSIATTSAPQAPPALPVRRPNRRWDTTGTRAGKSKQPPPLAQEQQQRQGYRSWRGHKNAIVACLQDCGGNISFARRFLLYHHGVAFPRNILHYYRHLYSPYCTGGSGSGSNSSGHTEAKATG
Protein: 26S proteasome regulatory subunit 4 homolog B (26S proteasome AAA-ATPase subunit RPT2b) (26S proteasome subunit 4 homolog B) (Regulatory particle triple-A ATPase subunit 2b) (Q9SL67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. Acts redundantly with RPT2A in the regulation of gametogenesis. With RPT2A plays a critical role in 26S proteasome assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22158466}. Nucleus {ECO:0000269|PubMed:22158466}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 7 homolog B
- 26S proteasome non-ATPase regulatory subunit 1 homolog A
- 26S proteasome regulatory subunit RPN13
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 1 homolog B
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
Sequence:
MGQGPSGGLNRQGDRKPDGGEKKEKKFEPAAPPARVGRKQRKQKGPEAAARLPTVTPSTKCKLRLLKLERIKDYLLMEEEFVANQERLKPQEEKAEEDRSKVDDLRGTPMSVGNLEELIDENHAIVSSSVGPEYYVGILSFVDKDQLEPGCSILMHNKVLSVVGILQDEVDPMVSVMKVEKAPLESYADIGGLEAQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGEPGTGKTLLAKAVANSTSATFLRVVGSELIQKYLGDGPKLVRELFRVADDLSPSIVFIDEIDAVGTKRYDANSGGEREIQRTMLELLNQLDGFDSRGDVKVILATNRIESLDPALLRPGRIDRKIEFPLPDIKTRRRIFQIHTSKMTLAEDVNLEEFVMTKDEFSGADIKAICTEAGLLALRERRMKVTHVDFKKAKEKVMFKKKEGVPEGLYM
Protein: PC-esterase domain-containing protein 1B (Protein FAM113B) (Q96HM7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MILLRASEVRQLLHNKFVVILGDSVHRAVYKDLVLLLQKDRLLTPGQLRARGELNFEQDELVDGGQRGHMHNGLNYREVREFRSDHHLVRFYFLTRVYSDYLQTILKELQSGEHAPDLVIMNSCLWDISRYGPNSWRSYLENLENLFQCLGQVLPESCLLVWNTAMPVGEEVTGGFLPPKLRRQKATFLKNEVVKANFHSATEARKHNFDVLDLHFHFRHARENLHWDGVHWNGRVHRCLSQLLLAHVADAWGVELPHRHPVGEWIKKKKPGPRVEGPPQANRNHPALPLSPPLPSPTYRPLLGFPPQRLPLLPLLSPQPPPPILHHQGMPRFPQGPPDACFSSDHTFQSDQFYCHSDVPSSAHAGFFVEDNFMVGPQLPMPFFPTPRYQRPAPVVHRGFGRYRPRGPYTPWGQRPRPSKRRAPANPEPRPQ
Protein: Neuropeptide FF receptor 1 (G-protein coupled receptor 147) (RFamide-related peptide receptor OT7T022) (Q9GZQ6)
Organism: Homo sapiens (Human)
Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11024015}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-FMRFamide-related neuropeptide FF
- Pro-FMRFamide-related neuropeptide VF
- Neuropeptide FF receptor 2
- Orexigenic neuropeptide QRFP
- Delta-type opioid receptor
- Galanin peptides
- Metastasis-suppressor KiSS-1
Sequence:
MEGEPSQPPNSSWPLSQNGTNTEATPATNLTFSSYYQHTSPVAAMFIVAYALIFLLCMVGNTLVCFIVLKNRHMHTVTNMFILNLAVSDLLVGIFCMPTTLVDNLITGWPFDNATCKMSGLVQGMSVSASVFTLVAIAVERFRCIVHPFREKLTLRKALVTIAVIWALALLIMCPSAVTLTVTREEHHFMVDARNRSYPLYSCWEAWPEKGMRRVYTTVLFSHIYLAPLALIVVMYARIARKLCQAPGPAPGGEEAADPRASRRRARVVHMLVMVALFFTLSWLPLWALLLLIDYGQLSAPQLHLVTVYAFPFAHWLAFFNSSANPIIYGYFNENFRRGFQAAFRARLCPRPSGSHKEAYSERPGGLLHRRVFVVVRPSDSGLPSESGPSSGAPRPGRLPLRNGRVAHHGLPREGPGCSHLPLTIPAWDI
Protein: Glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (GlnRS) (P13188)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative proline--tRNA ligase YHR020W
- Isoleucine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- tRNA-aminoacylation cofactor ARC1
- Arginine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
Sequence:
MSSVEELTQLFSQVGFEDKKVKEIVKNKKVSDSLYKLIKETPSDYQWNKSTRALVHNLASFVKGTDLPKSELIVNGIINGDLKTSLQVDAAFKYVKANGEASTKMGMNENSGVGIEITEDQVRNYVMQYIQENKERILTERYKLVPGIFADVKNLKELKWADPRSFKPIIDQEVLKLLGPKDERDLIKKKTKNNEKKKTNSAKKSSDNSASSGPKRTMFNEGFLGDLHKVGENPQAYPELMKEHLEVTGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKPWKITYSSDYFDELYRLAEVLIKNGKAYVCHCTAEEIKRGRGIKEDGTPGGERYACKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMKQDLNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLEDTTPRLMFVLDPVEVVVDNLSDDYEELATIPYRPGTPEFGERTVPFTNKFYIERSDFSENVDDKEFFRLTPNQPVGLIKVSHTVSFKSLEKDEAGKIIRIHVNYDNKVEEGSKPKKPKTYIQWVPISSKYNSPLRVTETRVYNQLFKSENPSSHPEGFLKDINPESEVVYKESVMEHNFGDVVKNSPWVVDSVKNSEFYVEEDKDSKEVCRFQAMRVGYFTLDKESTTSKVILNRIVSLKDATSK
Protein: Transmembrane protein 141 (Q96I45)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVNLGLSRVDDAVAAKHPGLGEYAACQSHAFMKGVFTFVTGTGMAFGLQMFIQRKFPYPLQWSLLVAVVAGSVVSYGVTRVESEKCNNLWLFLETGQLPKDRSTDQRS
Protein: Alpha-catenin-like protein hmp-1 (Protein humpback-1) (P90947)
Organism: Caenorhabditis elegans
Function: Required for cell migration during body enclosure and cell shape changes during body elongation. Required for proper localization of other junctional components, such as pac-1.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:9531567}. Cytoplasm {ECO:0000269|PubMed:25938815}.
Interaction partners:
- Beta-catenin-like protein hmp-2
- Juxtamembrane domain-associated catenin
- Cadherin-related hmr-1
- Beta-catenin/armadillo-related protein 1
- Vinculin
- FERM domain-containing protein
- Disks large homolog 1
- Actin
- Protein Scribble homolog let-413
- Adenomatous polyposis coli protein-related protein 1
Sequence:
MPANGNSHAYFNIDEVRSKNVLKQITQLINEVTNITETFPLKPGQTTEGLVATLDAAVANFLQTGSFAISKCPIANSDPRAIDLLHEALGAVQDTGQVMIQTGRDFVRDSTSTNKRAIATNSGRNLLTAVAKFLILADSIDVKVIVDKVDEVRETAHQMIEADTKIKVDDLYNLLISQIEELDITVRRRAIDLVKPNQRDDLLAARSALRQTAPLLYTSTRTFVRHPEHEEARRNRDYTADEMHSALNALESVLNGQQPKVTFSEYGRIGDLINEIDTFQNRIEIDPAHYRRGTDRPDLEGHCERIVSGSASIADAESTRENRKQKIVAECNNLRQALQELLTEYEKSTGRRDDNDDIPLGIAEVHKRTKDLRRHLRRAIVDHISDAFLDTRTPLILLIEAAKEGHEENTRYRSKMFQEHANEIVSVARLSCQLSSDVESVSVIQHTAAQLEKLAPQVAQAAILLCHQPTSKTAQENMETYKNAWFDKVRLLTTALDNITTLDDFLAVSEAHIVEDCERGIKGITANASTPDENAANCETVDCAAGSIRGRALRVCDVVDAEMDFLQNSEYTETVKQAVRILKTQRVDQFAERASALANRQEAHGLTWDPKTKEEEMNEFINACTLVHDAVKDIRHALLMNRSMNDVDSDVEYEADGVGAANADANRTISEQENQQNLMRRLPEEEKKKIQAQIDIFKVTQTRFEREVAKWDETGNDIISLANNMCKIMMSMTEFTRGCGPLKTTMDVIRAAQEISLNGSKLNALARQIGEESADSQTKKDLLAYLSQITLYCQQLNICSKVKADVTQVGNELVVSALDSAMSLIQTARNLLTAVVQTVKAAYIASTKFRRPNANSVRVEWRMAPPKKQPLIRPQKNNAIIRRASERRPLQPAKVLAEFTRNEIETGRDSDDEELDRRHQQRINGRL
Protein: C3HC-type domain-containing protein (Q386Q0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
Sequence:
MLITENLFASVSTWRRNVLARAFIGGDEETIFLLSAMNITPCGVEPITLDRGENNEAAGWGDEEGEVALQICTSCCSRSRLMLTSDWVRLLQFLRSRSCASTSVAKCMEGETVGANIQSVASAGAATCEVSENIIEKLMSELHSPSCWWRLGEVARHALSSPSLSWTNSSLIRHRCSAVSLKTLSTAASGSCDTSSTALSNSALGNLAGSDTSPNNLPQGNKLLLPRGTPPSFIRENMLQRVMKWLRSLITNQASALSSTTPEGLLCTLFGIKKKRSLEADSSGNNRSDENPETRNGNIDLVPHVSLLITLFGYTVTEVPSSDAASRCSGGSEGNEASKGVGEDVEESLLAALGVDIFCRFCGGRPPVVYSTLNGNESGKGVQNVDSMSCDNNEGESGRVRTQCTIRWSERAEHSGHHESCPWRELFLTSVLKDDAAKACSTDLIFTVGATNSTVVLLMCFKLHEVVNLMECWRVSVYTEFKLGETYAKNPFPVALRSALPPPAEPIVEDFLQKLQSSRRCGEGTHGSSEEGRTVTSSGCSGQHQVPLFGGNSFWNSYFRVSSFVNAAASGAGSDPAELQATGSTAAPRTCRATVGPASAVNGQRNKDWKAAYDAGRRYILASAEAEADSQSAVECTLEELQKFTDLYRQNFQRDAEAAPELLYPPAIGAAMDQLWQQFSAECSSNALLHRENVTPPQRASQLSAEDRARVHSLLDSLERSTQNAARQRAAQAPQSLQKVSAKESPQAPVAAVSQQQPRQTQEIQQSTQGVSVMQNQPKQPWHQPWKQRHTQKNETTTSMPTPRKPAVPSEGILPIPVGEGGGGAVLSHPAPAVLQLPQPQPPFPITQQGFPPFAARGRESVLTGDSGGVLDDNYSQRTPLMGQRRGGTSRYGIDRIGGGRGSDSRRGRRGTGRGAGRGGSGVVFK