wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin-associated protein 4-5 (Keratin-associated protein 4.5) (Ultrahigh sulfur keratin-associated protein 4.5) (Q9BYR2)
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.
Interaction partners:
- Keratin-associated protein 4-3
- Keratin-associated protein 4-8
- Keratin-associated protein 17-1
- Keratin-associated protein 4-1
- Keratin-associated protein 3-1
- Keratin-associated protein 9-3
- Keratin-associated protein 9-8
- Keratin-associated protein 9-4
- Keratin-associated protein 11-1
- Keratin-associated protein 2-1
Sequence:
MVSSCCGSVSSEQSCGLENCCRPSCCQTTCCRTTCCRPSCCKPQCCQSVCYQPTCCHPSCCISSCCRPYCCESSCCRPCCCQTTCCRTTCCRTTCCCPSCCVSSCCRPQCCQSVCCQPTCCRPSCCISSCCHPSCCESSCCRPCCCVRPVCGRVSCHTTCYRPTCVISTCPRPLCCASSCC
Protein: Olfactory receptor 2H2 (Hs6M1-12) (Olfactory receptor 2H3) (Olfactory receptor-like protein FAT11) (O95918)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MVNQSSTPGFLLLGFSEHPGLERTLFVVVLTSYLLTLVGNTLIILLSALDPKLHSPMYFFLSNLSFLDLCFTTSCVPQMLVNLWGPKKTISFLDCSVQIFIFLSLGTTECILLTVMAFDRYVAVCQPLHYATIIHPRLCWQLASVAWVIGLVESVVQTPSTLHLPFCPDRQVDDFVCEVPALIRLSCEDTSYNEIQVAVASVFILVVPLSLILVSYGAITWAVLRINSAKGRRKAFGTCSSHLTVVTLFYSSVIAVYLQPKNPYAQERGKFFGLFYAVGTPSLNPLIYTLRNKEVTRAFRRLLGKEMGLTQS
Protein: Hypoxia-inducible factor 3-alpha (HIF-3-alpha) (HIF3-alpha) (Basic-helix-loop-helix-PAS protein MOP7) (HIF3-alpha-1) (Inhibitory PAS domain protein) (IPAS) (Member of PAS protein 7) (Neonatal and embryonic PAS protein) (Q0VBL6)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression. Plays a role in the development of the cardiorespiratory system.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y2N7}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y2N7}. Note=In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes. Localized in the cytoplasm and nuclei under normoxia, but increased in the nucleus under hypoxic conditions. Colocalized with HIF1A in kidney tumors. {ECO:0000250|UniProtKB:Q9JHS2, ECO:0000250|UniProtKB:Q9Y2N7}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:24092767}. Cytoplasm {ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:24092767}. Nucleus speckle {ECO:0000269|PubMed:21546903}. Mitochondrion {ECO:0000269|PubMed:21546903}. Note=Colocalizes with BAD in the cytoplasm (PubMed:21546903). Colocalizes with EPAS1 and HIF1A in the nucleus and speckles (PubMed:21546903). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (PubMed:24092767). {ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:24092767}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator
- Endothelial PAS domain-containing protein 1
- Hypoxia-inducible factor 1-alpha
- Aryl hydrocarbon receptor nuclear translocator 2
- Prolyl hydroxylase EGLN2
- Prolyl hydroxylase EGLN3
- von Hippel-Lindau disease tumor suppressor
- Egl nine homolog 1
- Histone lysine acetyltransferase CREBBP
- Elongin-C
Sequence:
MDWDQDRSNTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVEKGGEPLDACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALTPRPNLSKKKLEAPTERHFSLRMKSTLTSRGRTLNLKAATWKVLHCSGHMRAYKPPAQTSPAGSPRSEPPLQCLVLICEAIPHPASLEPPLGRGAFLSRHSLDMKFTYCDERIAEVAGYSPDDLIGCSAYEYIHALDSDAVSRSIHTLLSKGQAVTGQYRFLARTGGYLWTQTQATVVSGGRGPQSESIICVHFLISRVEETGVVLSLEQTEQHTRRPPRLSASSQKGIPGNSVDSPAPRILAFLHPPALSEASLAADPRRFCSPDLRRLMAPILDGPPPAATPSTPQATRRPQSPLPADLPDKLTVGLENAHRLSTAQKNKTVETDLDIAQDPDTLDLEMLAPYISMDDDFQLNSSEQLPKVHRRPPRVARRPRARSFHGLSPPIPEPSLLPRWGSDPRLNCSSPSRGDRPTASLMPGTRKRALAQSSEDKGLELLETKPPKRSPRLEPGSFLLPPLSLSFLLQGRQLPGNQQDPRAPLVHSHEPLGLAPSLLSLCQHEETVQPRNRFPPAAGLGQTH
Protein: alpha-1,2-Mannosidase (EC 3.2.1.-) (A2RBC3)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Cytoplasmic vesicle lumen {ECO:0000256|ARBA:ARBA00004321}.
Interaction partners:
Sequence:
MYKDKPYFAPRRTGPRARRRKIIYSGLCLFVLLALWYYSGSGKPEWKTPDAEKGAELWKWVQSFEESEPPYDGSAATEKIDWEARREKVRDVFIVSWDGYAANAWGYDEYHPIAKNGRHMIEGGMGWIIVDALDTLMIMNLTSRVQHARSWIHNSLQYNQDHDVNTFETTIRMLGGLLSAHYLSTNYPELAPLTDDDTGAPGEDLYIEKATDLADRLLGAFESGTGIPYASINLNKSEGLPSYADNGASSTAEATTLQLEFKYLAKLTGEAEYWQAVEKVMEVVDDQKMEDGLLPIYVYPETGEFKGDNIRLGSRGDSYYEYLIKQYLQTQETEPIYKDMWDESLVGVRKHLITYTQNAKLTVLGERPAGLHGVLSPKMDHLVCFYPGTIALAATGGRPLSEARQSPDWGQRQEEEILLARELTKTCWATYLITKTGLAPEITYFNVDDPRVMETDIDYSTKWRDDLNIHKQDRHNLQRPETVESLFYMYRITGDDIYRHWGWEMFKSFVKHTAVKITGFTSLSNADDNPPVKRDNMESFWMAETLKYFYLLFSDRDFISLEDHVFNTEAHPLPRFKPTGELKTGWMRKSRTIPTSSEVEESV
Protein: F-box/SPRY domain-containing protein 1 (F-box only protein 45) (hFbxo45) (P0C2W1)
Organism: Homo sapiens (Human)
Function: Component of E3 ubiquitin ligase complexes. Required for normal neuromuscular synaptogenesis, axon pathfinding and neuronal migration (By similarity). Plays a role in the regulation of neurotransmission at mature neurons (By similarity). May control synaptic activity by controlling UNC13A via ubiquitin dependent pathway (By similarity). Specifically recognizes TP73, promoting its ubiquitination and degradation.
Subcellular location: Secreted {ECO:0000269|PubMed:32341084}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P0CH38}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P0CH38}. Nucleus {ECO:0000269|PubMed:26068074}. Note=Secreted by a non-classical mechanism. {ECO:0000269|PubMed:32341084}.
Interaction partners:
- E3 ubiquitin-protein ligase MYCBP2
- S-phase kinase-associated protein 1
- Cullin-1
- Protein unc-13 homolog A
- SPRY domain-containing protein 3
- E3 ubiquitin-protein ligase SIAH1
- F-box/WD repeat-containing protein 7
- WD repeat-containing protein 53
- MAGUK p55 subfamily member 3
- Disks large homolog 3
Sequence:
MAAPAPGAGAASGGAGCSGGGAGAGAGSGSGAAGAGGRLPSRVLELVFSYLELSELRSCALVCKHWYRCLHGDENSEVWRSLCARSLAEEALRTDILCNLPSYKAKIRAFQHAFSTNDCSRNVYIKKNGFTLHRNPIAQSTDGARTKIGFSEGRHAWEVWWEGPLGTVAVIGIATKRAPMQCQGYVALLGSDDQSWGWNLVDNNLLHNGEVNGSFPQCNNAPKYQIGERIRVILDMEDKTLAFERGYEFLGVAFRGLPKVCLYPAVSAVYGNTEVTLVYLGKPLDG
Protein: Opsin 4 like, isoform a (G5EI88)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MDLPPRAPTKMTVKDVRGAFPTVDVPDHAHYTIGTVILIVGITGTLGNFLVIYAFCRSRTLQKPANIFIINLAVSDFLMSITQSPVFFTNSLHKRWIFGEKGCELYAFCGALFGITSMITLMVIALDRYFVITKPLASVRVMSKKKALIILVGVWLYSLAWSLPPFFGWSAYVPEGLLTSCSWDYMTFTPSVRAYTMLLFCFVFFIPLIAIIYSYVFIFEAIKKANKSVQTFGCKHGNRELQKQYHRMRNEWKLAKIALIVILLYVISWSPYSVVALVAFAGYSHVLTPFMNSVPAVIAKASAIHNPIIYAITHPKYRTAIATYVPCLGFLLRVSPKESRSFSSYPSSRRTTITSQSSETSGLQKGKRRLSSISDSESGCTDTETDITSMISRPASSQVSYEMGEDTTQTSDLGGKPKVKSHDSGIFRKTVVDADEIPMVEINDTEHSATSTCKTSEKCNVEEIQRSESLSGIGLREGESRHRTSASQIPSIIITYSNVQGVELPSGYSAGFLHPKNKSHKQNKSSNS
Protein: Epididymal-specific lipocalin-12 (B3EY83)
Organism: Rattus norvegicus (Rat)
Function: Binds all-trans retinoic acid and may act as a retinoid carrier protein within the epididymis. May play a role in male fertility.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Lipocalin 9
- von Ebner gland protein 1
- Lipocalin 8
Sequence:
MGPWWALWLILTLPQILGGQSPTMPQGFSQMTSFQSNKFQGEWFVLGLADNTYKREHRPLLHSFITLFKLRDNSEFQVTNSMTRGKHCSTWSYTLIPTNKPGQFTRDNRGSGPGADKENIQVIETDYVKFALVLSLRQASNQNITRVSLLGRDWKITHKTIDRFICLTKTQNLTKNNLLFPDLTDWLLDPKVC
Protein: Somatoliberin (Growth hormone-releasing factor) (GRF) (Growth hormone-releasing hormone) (GHRH) (P09916)
Organism: Rattus norvegicus (Rat)
Function: GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone.
Subcellular location: Secreted.
Interaction partners:
- Growth hormone-releasing hormone receptor
- Somatotropin
- Somatostatin
- Growth hormone secretagogue receptor type 1
- Appetite-regulating hormone
- Pro-neuropeptide Y
- Corticoliberin
- Pro-glucagon
- Amelogenin, X isoform
- Insulin-like growth factor 1
Sequence:
MPLWVFFVLLTLTSGSHCSLPPSPPFRVRRHADAIFTSSYRRILGQLYARKLLHEIMNRQQGERNQEQRSRFNRHLDRVWAEDKQMALESILQGFPRMKLSAEA
Protein: Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas (Adenylate cyclase-stimulating G alpha protein) (Extra large alphas protein) (XLalphas) (G-alpha-8) (Q63803)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP. GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. XLas isoforms interact with the same set of receptors as Gnas isoforms.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10931823}; Peripheral membrane protein {ECO:0000269|PubMed:10931823}. Apical cell membrane {ECO:0000250|UniProtKB:Q5JWF2}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Glucagon-like peptide 1 receptor
- Beta-2 adrenergic receptor
- Adhesion G-protein coupled receptor G2
- Guanine nucleotide-binding protein G
- Prostaglandin E2 receptor EP4 subtype
- Prostaglandin E2 receptor EP2 subtype
- Guanine nucleotide-binding protein subunit beta-4
- D
- Glucose-dependent insulinotropic receptor
Sequence:
MGMLNCLHGNNMSGQHDIPPEVGDQPEQEPLEAQGAAAPGAGVGPAEEMETEPSNNEPIPDETDSEVCGPPEDSKSDIQSPSQAFEEVQVGGDYSPPPEEAMPFEIQQPSLGDFWPTLEQPGPSGTPSGIKAFNPAILEPGTPTGAHPGLGAYSPPPEEAMPFEFNEPAQEDRCQPPLQVPDLAPGGPEAWVSRALPAEPGNLGFENTGFREDYSPPPEESVPFQLDGEEFGGDSPPPGLPRVTPQIGIGGEFPTVAVPSTLCLAPAANAPPLWVQGAIGRPFREAVRSPNFAYDISPMEITRPLLEIGRASTGVDDDTAVNMDSPPIASDGPPIEVSGAPVKSEHAKRPPLERQAAETGNSPISSTTAEEAKVPSLERGEGSPTQPETVHIKPAPVAESGTDSSKADPDSATHAVLQIGPEEVGGVPTMPTDLPPASEDAGPDVRAEPDGGTAPATPAESEDNREPAAAAAAEPAAEPAAEPAAEPAAEPAAEPAAEAVPDTEAESASGAVPDTQEEPAAAAASATPAEPAARAAPVTPTEPATRAVPSARAHPAAGAVPGASAMSAAARAAAARAAYAGPLVWGARSLSATPAARASLPARAAAAARAASAARAVAAGRSASAAPSRAHLRPPSPEIQVADPPTPRPAPRPSAWPDKYERGRSCCRYEAASGICEIESSSDESEEGATGCFQWLLRRNRRPGQPRSHTVGSNPVRNFFARAFGSCFGLSECTRSRSLSPGKAKDPMEERRKQMRKEAMEMREQKRADKKRSKLIDKQLEEEKMDYMCTHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPNFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLPRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
Protein: Phospholipid-transporting ATPase C4F10.16c (EC 7.6.2.1) (O36028)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the hydrolysis of ATP coupled with the transport of phospholipids.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P32660}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phospholipid-transporting ATPase accessory subunit mug89
- Phospholipid-transporting ATPase accessory subunit ivn1
- Phospholipid-transporting ATPase dnf2
Sequence:
MPSLINFDAISSLKSSLHGLSICAFNHLHHVPQHNGSLAHEGPTNQTDYSSRHHESQFSQEAHAEQRSRDDEEANSFEGSCNNSDQSWTSRVTSKKNEAGTESGDASVRRIYVTSIPEEHRHLPSQWFPSNKIRTTKYTPVSFIPKNLWNQFKNIANAFFLFVTLLQCIPLFCPEHLGLSFIPLSVILLTTAIKDGIEDYRRCVLDKKFNNTLTWKLVGFNNANALGEHIGLWRKLKKFISHTVADMSYCLKNSGISSGLATLTVDNISHRHSLESDSAFTLSSVSQDSLEIHEIGNSGPSNSFSVIQEQSTGSSNAKFERVCRKSLLVGDIVKVLADEAIPADLLILSTENSNGVCYVETKNLDGETNLKDKYALCSTKCCKSEYRCSAASFWVECEQPHADLYSLNGVVKAPGAVQSPSESTNGRKIHEEPFSISNVLLCGCTLRNSKWVIGLVLYTGSETRIQKNRGLTPSKRSRITRDLNWTIILNFLLLFAMCLFSGVLRSIYSAQNNSARVFELSKNSNTAPAHGIISIFTSLILFQNLVPISLYITMDIVRSIQSYFIFSDREMYDEKLDCPCSPKSWNISDDLGQIEYIFSDKTGTLTQNIMSFKKCSINGIRYGKSHNEDTCIKKRRNLNYNENLSCKVDLDKKKMLETLSLSDSPNPESITFISSKFVDHLQSNENYIQTEACFEFFKALALCHSVVTDVQDETLIYNAQSPDEEALVKVARDFGFTLLNTKNRRYTIRIRGENKNFRVLDIIPFTSTRKRMSVIIRDEDGIIHLICKGADTVIFPRLSSGQNNIIEKTKKHLASFSSEGFRTLCIARRTIDKQDYLEWKVNFNEANSAIHERNEKVSKVSEMIEQELELLGGTAIEDKLQENVPETIALLAIAGIKLWVLTGDKVETAINIGYSCNLLDPNMTIFRIDANSFGALEEVEAFIRNTLCFNFGYMGTDEEFRFLLKDHSPPSPKHAIVIDGDALNFVLSEQVSFLFLMLCKQCKTVLCCRVSPSQKAAVVALVKKSLNVVTLAIGDGANDVSMIQEADVGVGIKGVEGQAASMSADYAIGQFSFLGRLLLVHGRWDYKRMSQMISFFFYKNVIWTFILFWYQFYNEFDGNYIFDYTYVMLFNLLFTSLPVIIAGCFDQDVDASVSMKNPSLYQRGILGLEWNGKRFWSYMLDGIYQSLVCFGVALFVFKFGDFVSWTGRNIECIEDIGLFISSPTIFVINIFILMNQERLNLISLITWMFSIGVFWIWTFIYSEVGPSYAFHKSASRTCQTFGFWCVTVLTIALCLLPRFSYICLQKLFYPRDIDLLRRRLCAKSDDETSSSSSFATDIEMCEQCNDPLSSKKNSGIVTSVSFDDSNK
Protein: Tetratricopeptide repeat domain 8 (Tetratricopeptide repeat domain 8, isoform CRA_c) (A0A0C4DGX9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSEMEPLLLAWSYFRRRKFQLCADLCTQMLEKSPYDQAAWILKARALTEMVYIDEIDVDQEGIAEMMLDENAIAQVPRPGTSLKLPGTNQTGGPSQAVRPITQAGRPITGFLRPSTQSGRPGTMEQAIRTPRTAYTARPITSSSGRFVRLGTASMLTSPDGPFINLSRLNLTKYSQKPKLAKALFEYIFHHENDVKTIHLEDVVLHLGIYPFLLRNKNHIEKNALDLAALSTEHSQYKDWWWKVQIGKCYYRLGMYREAEKQFKSALKQQEMVDTFLYLAKVYVSLDQPVTALNLFKQGLDKFPGEVTLLCGIARIYEEMNNMSSAAEYYKEVLKQDNTHVEAIACIGSNHFYSDQPEIALRFYRRLLQMGIYNGQLFNNLGLCCFYAQQYDMTLTSFERALSLAENEEEAADVWYNLGHVAVGIGDTNLAHQCFRLALVNNNNHAEAYNNLAVLEMRKGHVEQARALLQTASSLAPHMYEPHFNFATISDKIGDLQRSYVAAQKSEAAFPDHVDTQHLIKQLRQHFAML
Protein: Coiled-coil domain-containing protein 154 (Golgin-160-like protein) (Q6RUT8)
Organism: Mus musculus (Mouse)
Subcellular location: Early endosome {ECO:0000269|PubMed:22895184}.
Interaction partners:
Sequence:
MSEPADGPSLRLSPSHLSTVTLEDLELLLTEGLVSAETSERDECSGRASGSLVPEQDTSKLWKQLEQWVAELQAEVVRLRGHKERCEHATLGLLRELLQVRARVQMQASELRQLRQVVQQAAWSPEKEELELSGPQSQNQMQTLDKRLVEVREALTHIRRKQALQDSERKHSEQEINLRLTNLTGMLSQEEQGREAACSALQKNQEDTSQKVDLGLAKMQAQMTKLNEEMSLRFLKREAKLCSFLQKSFLALEQRMKSSESTRQIAESSLREELESRWQKLHELTEERLRALRAQREEEEGHLLEQCRGLDKAVVYLTKFVRQNQVSLNRVLMAEQKAREAKVSLEETQAGELASYVHENLEAVQMAGKLAQQETQDALELLQEKSQVLEGSVAGLDQQLKDLSDHCLALSWRLDLQEQTLGLKLSQKQAAWEGMERESLKDLVQWLKEVTAHLEEVQEKVNSLPQQIESISNKCVIHKSEVDVKISAEGKAREFEVETVRQELAALLMSVQLLKEENPGRKIAEIQGQLATFQKQMIKLENSLQANKTIQNLKFNNETKLRTEEIATLRESMLRLWSEEGPWPLTLGSKRVFMSLVRQRFFIKDVALDAMVSVNSWGVYQAVRWLRWKRFLLNLVAQKRPGVTSAMTQWKPAYEVTSLTVFQK
Protein: Packaging protein 2 (Packaging protein 22K) (L4-22K) (Q2KS03)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
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:
MAPKKKLQLPPPPTDEEEYWDSQAEEVLDEEEEDMMEDWESLDEEASEVEEVSDETPSPSVAFPSPAPQKSATGSSMATTSAPQAPPALPVRRPNRRWDTTGTRAGKSKQPPPLAQEQQQRQGYRSWRGHKNAIVACLQDCGGNISFARRFLLYHHGVAFPRNILHYYRHLYSPYCTGGSGSGSNSSGHTEAKATG
Protein: Pyruvate kinase (PK) (EC 2.7.1.40) (O62619)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Enolase
- Glucose-6-phosphate isomerase
- Phosphoglycerate kinase
- L-lactate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- ATP-dependent 6-phosphofructokinase
- Uncharacterized protein, isoform A
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Pyruvate carboxylase
Sequence:
MVNVTIYDEAPQLKPNEVPQNMAAGADTQLEHMCRLQFDSPVPHVRLSGIVCTIGPASSSVEMLEKMMATGMNIARMNFSHGSHEYHAATVANVRQAVKNYSAKLGYEHPVAIALDTKGPEIRTGLIGGSGTAEIELKKGEKIKLTTNKEFLEKGSLEIVYVDYENIVNVVKPGNRVFVDDGLISLIVREVGKDSLTCEVENGGSLGSRKGVNLPGVPVDLPAVSEKDKSDLLFGVEQEVDMIFASFIRNAAALTEIRKVLGEKGKNIKIISKIENQQGMHNLDEIIEAGDGIMVARGDLGIEIPAEKVFLAQKAMIARCNKAGKPVICATQMLESMVKKPRPTRAEISDVANAVLDGADCVMLSGETAKGEYPLECVLTMAKTCKEAEAALWHQNLFNDLVRGAGTIDASHAAAIAAVEAATKAKASAIVVITTSGKSAFQVSKYRPRCPIIAVTRFAQTARQAHLYRGLVPLIYKEPGLGDWLKDVDVRVQFGLQVGKKNGFIKTGDSVVVVTGWKQGSGFTNTIRIVTVE
Protein: Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha) (P51128)
Organism: Xenopus laevis (African clawed frog)
Function: Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (rars) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription. The high affinity ligand for rxrs is 9-cis retinoic acid. In the absence of ligand, the rar/rxr heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
Sequence:
MSSAAMDTKHFLPLGGRTCADTLRCTTSWTAGYDFSSQVNSSSLSSSGLRGSMTAPLLHPSLGNSGLNNSLGSPTQLPSPLSSPINGMGPPFSVISPPLGPSMAIPSTPGLGYGTGSPQIHSPMNSVSSTEDIKPPPGINGILKVPMHPSGAMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDSKDCMIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKERNENEVESSNSANEDMPVEKILEAEHAVEPKTETYTEANMGLAPNSPSDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPLEVEALREKVYASLEAYCKQKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
Protein: Pyruvate kinase I (EC 2.7.1.40) (PK-1) (P0AD61)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of pyruvate in the last step of glycolysis, it is irreversible under physiological conditions. The reaction is critical for the control of metabolic flux in the second part of glycolysis.
Interaction partners:
- Enolase
- Glucose-6-phosphate isomerase
- Phosphoenolpyruvate synthase
- NADP-dependent malic enzyme
- Phosphoenolpyruvate carboxylase
- Phosphoenolpyruvate carboxykinase
- Transketolase 1
- ATP-dependent 6-phosphofructokinase isozyme 1
- NAD-dependent malic enzyme
- D-lactate dehydrogenase
Sequence:
MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNLRNVMSKTGKTAAILLDTKGPEIRTMKLEGGNDVSLKAGQTFTFTTDKSVIGNSEMVAVTYEGFTTDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNGDLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDVIEIREHLKAHGGENIHIISKIENQEGLNNFDEILEASDGIMVARGDLGVEIPVEEVIFAQKMMIEKCIRARKVVITATQMLDSMIKNPRPTRAEAGDVANAILDGTDAVMLSGESAKGKYPLEAVSIMATICERTDRVMNSRLEFNNDNRKLRITEAVCRGAVETAEKLDAPLIVVATQGGKSARAVRKYFPDATILALTTNEKTAHQLVLSKGVVPQLVKEITSTDDFYRLGKELALQSGLAHKGDVVVMVSGALVPSGTTNTASVHVL
Protein: Small ribosomal subunit protein uS12m (28S ribosomal protein S12, mitochondrial) (MRP-S12) (S12mt) (MT-RPS12) (O15235)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS11m
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein bS16m
Sequence:
MSWSGLLHGLNTSLTCGPALVPRLWATCSMATLNQMHRLGPPKRPPRKLGPTEGRPQLKGVVLCTFTRKPKKPNSANRKCCRVRLSTGREAVCFIPGEGHTLQEHQIVLVEGGRTQDLPGVKLTVVRGKYDCGHVQKK
Protein: Carbonic anhydrase (EC 4.2.1.1) (Carbonate dehydratase) (Q92051)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Reversible hydration of carbon dioxide.
Interaction partners:
- Ammonium transporter Rh type C-like 2
- Anion exchange protein
- Ubiquinol-cytochrome c reductase core protein 2a
Sequence:
MAHAWGYGPADGPESWAESFPIANGPRQSPIDIVPTQAQHDPSLKHLKLKYDPATTKSILNNGHSFQVDFVDDDNSSTLAGGPITGIYRLRQFHFHWGSSDDKGSEHTIAGTKFPCELHLVHWNTKYPNFGEAASKPDGLAVVGVFLKIGAANPRLQKVLDALDDIKSKGRQTTFANFDPKTLLPASLDYWTYEGSLTTPPLLESVTWIVLKEPISVSPAQMAKFRSLLFSSEGETPCCMVDNYRPPQPLKGRKVRASFK
Protein: High mobility group nucleosome-binding domain-containing protein 3 (Thyroid receptor-interacting protein 7) (TR-interacting protein 7) (TRIP-7) (Q15651)
Organism: Homo sapiens (Human)
Function: Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Sodium- and chloride-dependent glycine transporter 1
- Cyclin-T2
- Thyroid hormone receptor beta
Sequence:
MPKRKSPENTEGKDGSKVTKQEPTRRSARLSAKPAPPKPEPKPRKTSAKKEPGAKISRGAKGKKEEKQEAGKEGTAPSENGETKAEEAQKTESVDNEGE
Protein: Heat shock transcription factor 34 (Heat shock transcription factor HSFB1) (Q43457)
Organism: Glycine max (Soybean) (Glycine hispida)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSQRSVPAPFLTKTYQLVEDQGTDQVISWGESGNTFVVWKHADFAKDLLPKYFKHNNFSSFVRQLNTYGFRKIVPDKWEFANEHFKRGQKELLSEIKRRKTVPQSSAHPPEAGKSGGDGNSPLNSGSDDAGSTSTSSSSSGSKNQGSVETNTTPSHQLSSENEKLKKDNETLSCELARARKQCDELVAFLRDRLMVGPDQIDRIMRQGSCGSENVVGEGGGGDCLKLFGVWLKGDTLTDKRNNHKRGREDQMGFGGPRLKESKPVVDFGAVNIMMKSNRVCN
Protein: Putative cell agglutination protein pfl4 (Adhesin pfl4) (Pombe flocculin 4) (Q7Z9I1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in agglutination during conjugation or other aspects of colony formation (By similarity). Induces flocculation when overexpressed.
Subcellular location: Cell surface {ECO:0000305|PubMed:17870620}.
Interaction partners:
- UPF0321 protein C569.02c
- Uncharacterized protein C553.10
- Uncharacterized protein PB18E9.04c
- Eukaryotic translation initiation factor 4E-2
Sequence:
MLFLRFFIFTFFTSIFTVVVSEPPVSAKFAKRVLSATSSSSSTCPEFITIFSEGPSEYITTIYPSSKSSGRGTTNHSTIYTTINSGTVASTYTVTLADGDVVVKDIEPTAGTVTTTITSGSHEFTTTLAEASGTVPGTVEVVEPLAGTVTTTIHSGSVEYNTTLATASGTVPGTVEVVEPAVGTVTTTIYSGSEEFTTTLASASGSISGTVEVIEPTAGTVTTTIYSGDQEYTTILAEASGTVPGTVEVIEPAVGTVTTTTYSGSVEYTTTLVPASGSVSGTVEVVEPAVGTVTTTLQSGSQAFTTTVPASGSVSGTVEVVQPTGGTVTNTVYEGSQTITSTLATASGTVPGTVEVILPGPSTIYSGTVATTITYDVSSTPASTVVVIPTAVCNGERGLQYAVYNYDISSSKNQFCATSGVTDVSSFTQPAYFGSSDLDQSSPLFTGVLSSSDSVPQWTSSYNLPGYPPDATAMGSTSSACKVIVYQFFFRVPVTDTFSLDVTNVDDVFYGWFGDKAISGWSNTNYDTYAYWHATNGQTGIASFSMGSLTADTYVPVRFVVANGAGKGGFDFSFVDSEGNSYNPTSYAYTATCTESFLPFGQGNGGVDN