wanglab/gogpt-training-data huggingface dataset:
Protein: Tubulin glycylase 3A (dmTTLL3A) (EC 6.3.2.-) (Q9VM91)
Organism: Drosophila melanogaster (Fruit fly)
Function: Polylycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved both in the side-chain initiation and elongation steps of the polyglycylation reaction by adding a single glycine chain to generate monoglycine side chains and by elongating monoglycine side chains to polyglycine side chains.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19524510}.
Interaction partners:
Sequence:
MQTRPSSEPHRSRDQVTDGDRNRDQPQKCASATLAKKPVTPPAAPPPTPSNRVVAPLTVPVIQLTPAQSDSPVKLARPATPKETAISVPDHSNKENQPARTPPPSKSCPLGAPTNYVARRTWITTERMNELRRKAQEAAKQNKIFTIRGCFNSVRNALLMRGWVEKLDVHRKVMPAGQMTYEDLTQRLPKRKAGETRRQYVQKCERNIMSRFLEHMPVDFLWTNRKEKCDYIDQAKNPGMTINKFHRAPFTSKEGLCSQLRDFHWFFEEGTAEMYFPRCYNVWSPEELGEFIENFKLTACVAFLRAMLCKYHKQGSDAVFSCSGKIPYSAIDFAYKRLVEYIDSCQHNDIDFEDPPKIWEHDWDAFLFQHQQLVNEDGRIQHDGGQRLEPMVKSCLSLVDKMKVHWPQYSLDGYQNMWIVKPANKCRGRGIILMDNLKKILGVVNLSIASKSRYVVQKYIERPLILFQTKFDIRQWFLITNTQPLVVWFYRESYLRFSSQEYSLSNHHESVHLTNYAIQKKYTNGKRDKRLPSENMWDCYSFQAYLRQIGKYNMWLERIFPGMRKAIVGCMLASQENMDRRPNTFELFGADFMICENFYPWLIEINSSPDLGATTSVTARMCPQCLEDVVKVVIDRRTDPKAELGNFELAYRQVVPPTPAYMGLNLFVKGKQVLQKANHGGGHGHYYYQQQRKERSLATSSVYRQRSAIIHPATSISRIHRAMPTFNATEYMEKYMVEPLSSSRSSLCSQLPQKSPSAAPALTATPSGATSSYILKQAGRSITQLLSATHKRNTGGSLSGEQVQSTALPPKRQRSCGPRLSSTNPVESTEKKFKILIKNYSSNGNENMQDARPEVANSATATAISERKWRSLRNIAATAGGSSNLAARSKGPPLIAPPSLPTRRLTRTKSEIDSTGMHAIGRTFGRKSNGPRLPISISVQALHRGEPIVAALKQATSELQLSQAQMMSPRTALANKLNGSTLMVPASALPVG
Protein: Transcription factor atf31 (Q09771)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Zinc finger protein rsv1
- Transcription factor pcr1
- Zinc finger protein rsv2
- Mitogen-activated protein kinase sty1
- Transcription factor atf21
Sequence:
MTYETNTPTEESIIPKHEDGEEYNSIYLSRFEKDISISQTLDFSQFMQTQILLTAKRKALELGDDRSPINNDPYNIRRSDFDELSEYTASKSPSIISEASHNSPSRELDDSGDENTSKLTGTKQSMLKARNRQAAQKCRIKKKKYLQTLQDQVNYYTSENKELLQSANDLREEIIKLRTLVFAHRDCPVSKACSKALFLMGKEKPLTPP
Protein: Uncharacterized protein C26F1.08c (Q10495)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- SAGA complex subunit Spt3
- SAGA complex subunit Ngg1
- SAGA complex subunit Sgf29
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex/transcription factor TFIID complex subunit Taf10
- NuA4 acetyltransferase complex subunit Tra2
- SAGA complex/NuA4 acetyltransferase complex subunit Tra1
- Uncharacterized threonine-rich GPI-anchored glycoprotein PJ4664.02
- SAGA complex subunit Ada2
Sequence:
MNFHHGWTFHKLRKNEHFLKYSAIFYSLLKPVVALFACQCLVLIRPLARKIGSFPFLILTFHTLFYPIQNTVGAQFEVIGQSLMGTAVGVTWGIITKLFATAANRNHGDGSPILATSLALASFISAYIRSRYGYRFFCIIWIFIDCFLLTRDPFEKTIAKSFYISLVYPSLIAAGVVSLVTILVPPMRMASDLVGQSGLDHLNKIMQSLNFSVENFFPSDESVSFSSSSSVIKRMFKEHESVLRNSMDDFHTAISSSEIELNYSNVSVSTLKLLEPKFERITLAMSAQLAASFTLYETYNFSIYKNQDKEVEGDIRVSELRFSLPESTEVQQKRNIFTPQYQLHINGSLRAKVRPKDSKDRIVNLSNLYFSNVDHMSSLILGSLKLAHAIMKWLVSDVEHIPDERLRECIESLQEIDSKEENLMTEIFCTAFKETKKVNDFGGFEEIEDEEEVLVIAYYLFNLFEVAREVKNLLLLLEGLKAQRHNKPKLFFRKFNLSLFDKQKYANYAISALLTHFTAGDADKCDDEAPDDASGEEDDSPKVLNDQSFFDSVRYPLKFFLRKMRRKCWRVYHFTARSKDVRYGLKMAIGIGLLSIVAFQKSTAARYTLWNGQWSLISTLFVLEVTVSTTLRVGLFRTLGTLSGAVYAYAAWEVSQGWSYAIATLTFAISWVSCYVKYNTEYSGIATVFNITFPPILYGSYLKTSTISPFHLACIRFIVVNVGIGMAIVVNIVVFPYLARRVLKYKLGQASLLSLKQYTTLSDYLLSRNLYTNLTICEGYKKQISSLLVTARKLLQLVNMEFNLKGPFPVGIYNDLIIKLENLGIRLVVLNRVRSRFGLYLYYDVVKNMIDYRKDLIVSMTLTFYILYNSIMSKAPIPYFVPSCRQALWNLRLAIEEEGKRRFVTNGGILAQGAGSDGVAKDVPENHSWLPAQKNFFLYYVECQVIGDIVTDLEYSISLVRRINGEKENETIGKKMA
Protein: Myeloproliferative leukemia virus oncogene (Q1ERS7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
LFSRCHFKSRNDSVIHILVEVTTAQGAIHSYLGSPFWIRQAVLLPTPSLHWREISSGRLELEWQHPSPWAAQETCYQLRYTGEGHEDWKVLEPSLGAQGGTLELRPRARYSLQLRARLNGPTYQGPWSAWSPPARVSTGSETAWIHLVTALLLVLSLSALLGLLLLKWQFPAHYRRLRHALWPSLPDLHRVLGQYLRDTAALSPSKATVTDSCEEVEPSLLEILPKSPERTPLPLCPSQP
Protein: CbbX protein (Q3IYC4)
Organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides)
Interaction partners:
- CbbY family protein
- Ribulose bisphosphate carboxylase small subunit
- Ribulose bisphosphate carboxylase large chain
- Phosphoglycolate phosphatase
- Caspase-1, p20
- HTH-type transcriptional regulator CbbR
- Sel1 repeat-containing protein
- phosphoglycolate phosphatase
- phosphoglycolate phosphatase
- Glycerol kinase
Sequence:
MTDAATAPTSIDLRAEYEGSGAKEVLEELDRELIGLKPVKDRIRETAALLLVERARQKLGLAHETPTLHMSFTGNPGTGKTTVALKMAGLLHRLGYVRKGHLVSVTRDDLVGQYIGHTAPKTKEVLKRAMGGVLFIDEAYYLYRPDNERDYGQEAIEILLQVMENNRDDLVVILAGYADRMENFFQSNPGFRSRIAHHIEFPDYSDEELFEIAGHMLDDQNYQMTPEAETALRAYIGLRRNQPHFANARSIRNALDRARLRQANRLFTASSGPLDARALSTIAEEDIRASRVFKGGLDSERRAAEALAR
Protein: Homeobox protein engrailed-1 (Homeobox protein en-1) (Mo-En-1) (P09065)
Organism: Mus musculus (Mouse)
Function: Required for proper formation of the apical ectodermal ridge and correct dorsal-ventral patterning in the limb.
Subcellular location: Nucleus.
Interaction partners:
- Paired box protein Pax-2
- Hepatocyte nuclear factor 3-beta
- Nuclear receptor subfamily 4 group A member 2
- Sonic hedgehog protein
- Proto-oncogene Wnt-1
Sequence:
MEEQQPEPKSQRDSGLGAVAAAAPSGLSLSLSPGASGSSGSDGDSVPVSPQPAPPSPPAAPCLPPLAHHPHLPPHPPPPPPPPPPPPQHLAAPAHQPQPAAQLHRTTNFFIDNILRPDFGCKKEQPLPQLLVASAAAGGGAAAGGGSRVERDRGQTGAGRDPVHSLGTRASGAASLLCAPDANCGPPDGSQPATAVSAGASKAGNPAAAAAAAAAAAAAAVAAAAAAASKPSDSGGGSGGNAGSPGAQGAKFPEHNPAILLMGSANGGPVVKTDSQQPLVWPAWVYCTRYSDRPSSGPRTRKLKKKKNEKEDKRPRTAFTAEQLQRLKAEFQANRYITEQRRQTLAQELSLNESQIKIWFQNKRAKIKKATGIKNGLALHLMAQGLYNHSTTTVQDKDESE
Protein: Serine protease HTRA2, mitochondrial (EC 3.4.21.108) (High temperature requirement protein A2) (HtrA2) (Omi stress-regulated endoprotease) (Serine protease 25) (Serine proteinase OMI) (O43464)
Organism: Homo sapiens (Human)
Function: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive.
Subcellular location: Mitochondrion intermembrane space. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 truncated BID/tBID.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:10644717}.
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Tumor necrosis factor receptor superfamily member 1A
- Baculoviral IAP repeat-containing protein 2
- Serine/threonine-protein kinase PINK1, mitochondrial
- Cytochrome c
- Baculoviral IAP repeat-containing protein 3
- Diablo IAP-binding mitochondrial protein
- Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6
- Presenilin-associated rhomboid-like protein, mitochondrial
- Presenilin-associated rhomboid-like protein, mitochondrial
Sequence:
MAAPRAGRGAGWSLRAWRALGGIRWGRRPRLTPDLRALLTSGTSDPRARVTYGTPSLWARLSVGVTEPRACLTSGTPGPRAQLTAVTPDTRTREASENSGTRSRAWLAVALGAGGAVLLLLWGGGRGPPAVLAAVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSSSGISGSQRRYIGVMMLTLSPSILAELQLREPSFPDVQHGVLIHKVILGSPAHRAGLRPGDVILAIGEQMVQNAEDVYEAVRTQSQLAVQIRRGRETLTLYVTPEVTE
Protein: T-box brain protein 1 (T-brain-1) (TBR-1) (TES-56) (Q16650)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor involved in multiple aspects of cortical development, including neuronal migration, laminar and areal identity, and axonal projection. As transcriptional repressor of FEZF2, it blocks the formation of the corticospinal (CS) tract from layer 6 projection neurons, thereby restricting the origin of CS axons specifically to layer 5 neurons (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:25232744, ECO:0000269|PubMed:30250039}.
Interaction partners:
- Fez family zinc finger protein 2
- Peripheral plasma membrane protein CASK
- Paired box protein Pax-6
- DNA-binding protein SATB2
- B-cell lymphoma/leukemia 11B
- Neurogenic differentiation factor 6
- Forkhead box protein P2
- Homeobox protein cut-like 1
- Forkhead box protein G1
- Homeobox protein EMX1
Sequence:
MQLEHCLSPSIMLSKKFLNVSSSYPHSGGSELVLHDHPIISTTDNLERSSPLKKITRGMTNQSDTDNFPDSKDSPGDVQRSKLSPVLDGVSELRHSFDGSAADRYLLSQSSQPQSAATAPSAMFPYPGQHGPAHPAFSIGSPSRYMAHHPVITNGAYNSLLSNSSPQGYPTAGYPYPQQYGHSYQGAPFYQFSSTQPGLVPGKAQVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNISGLDPTAHYNIFVDVILADPNHWRFQGGKWVPCGKADTNVQGNRVYMHPDSPNTGAHWMRQEISFGKLKLTNNKGASNNNGQMVVLQSLHKYQPRLHVVEVNEDGTEDTSQPGRVQTFTFPETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDTIYTGCDMDRLTPSPNDSPRSQIVPGARYAMAGSFLQDQFVSNYAKARFHPGAGAGPGPGTDRSVPHTNGLLSPQQAEDPGAPSPQRWFVTPANNRLDFAASAYDTATDFAGNAATLLSYAAAGVKALPLQAAGCTGRPLGYYADPSGWGARSPPQYCGTKSGSVLPCWPNSAAAAARMAGANPYLGEEAEGLAAERSPLPPGAAEDAKPKDLSDSSWIETPSSIKSIDSSDSGIYEQAKRRRISPADTPVSESSSPLKSEVLAQRDCEKNCAKDISGYYGFYSHS
Protein: Protein unc-119 homolog B (Protein unc-119 homolog 1) (Q90Z08)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Plays a key role in localization of proteins to the primary cilium membrane.
Subcellular location: Cell projection, cilium {ECO:0000250}.
Interaction partners:
- Protein XRP2
- ADP-ribosylation factor-like protein 3
- Nephrocystin-3
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- ADP-ribosylation factor-like 2
- ADP-ribosylation factor-like protein 3
- Peptidyl-prolyl cis-trans isomerase E
Sequence:
MNSQSSRNETAATAVNGSDSAAASRDHKSGGGVLKRLKSRRNQVDRRPVTEEELRALGRDITPDEVLGLRAVARDYLCKLEDNIYNIDFTRFKIRDLETGTVLFEIAKPPHCDLDEEDDENRDADTSAGRFVRYQFTPAFLKLRTVGATVEFTVGDQPVTNFRMIERHYFQDRLLKSFDFDFGFCIPNSRNTCEHIYEFPQLPEDLIRLMIEHPYETRSDSFYFVDNKLIMHNKADYAYNGGQ
Protein: JmjC domain-containing histone demethylation protein 1 (EC 1.14.11.27) (Lysine (K)-specific demethylase 2) ([Histone-H3]-lysine-36 demethylase 1) (Q9VHH9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- Polycomb group protein Psc
- GEO03726p1
- LD37257p
- Protein suppressor 2 of zeste
- Lysine-specific demethylase 3
- Polycomb group RING finger protein 3
- Probable lysine-specific demethylase 4A demethylase 4A) demethylase 4A)
- Probable lysine-specific demethylase 4B demethylase 4B)
- Histone-lysine N-methyltransferase E
Sequence:
MSTAVETGSSPAKSNSNNSSSGGNNNNGNGNLSPNAKGVQRRQLRERKQRKLYLEEWSLGDEDGEGTRGFSVAEKLESSKFAQAGMVREMRGCDLTVAFLQQHGFNIPLLFRDKAGLGLRMPDPQEFTVNDVRLCVGSRRLLDVMDVNTQKNLQMTMKEWQQYYDSPQKDRLLNVISLEFSHTRLDRFVQSPEIVRQIDWVDVVWPKQLKDAQREGTNLLGGMMYPKVQKYCLMSVKNCYTDFHIDFGGTSVWYHILRGSKVFWLIPPTDRNLQLYEKWVLSGKQADIFFGDTVEKCARVYLTAGNTFFIPTGWIHAVYTPTQSLVFGGNFLHSFGIVKQLKTASVEDSTKVPQKFRYPFFTEMLWYVLARYVHTLLGHSHLEGEASLSEDEMAARPHTHLTHHELFGLKEIVMYLYDLPPQKKNVPSLVLDPVALIKDVRSLVERHCKDQQDLAITGVSVLKSPPGSQPPFLLYDRTRVKQEIKQEIARKNAEVIREQQQLEAGRAREAESDTSQSTGVGSVIGMGAGVEYSNGVMKKEQLENGSGVTVGGHGSQPEATFALPTDTLKYRPPKKMHLATALVAAAASSSSGGGGPVAGVGGSAVVGSSHSPTGGGVGPVTGAGGAISVIATSSSYIEGGQVGGILNMDNCHSPEGGGAKLSPNLTGTGQPRRRRTRCKNCAACQRSDCGTCPFCMDMVKFGGPGRAKQTCMMRQCLSPMLPVTAQCVYCHLDGWRQTPVSPQTKQLASADGPSALMECSVCYEIAHPDCALSQLDGTEDAADAKGIVNEDLPNSWECPSCCRSGKNYDYKPRHFRARQKSSEVRRVSVSHGQGGAEGHADGNTLLPPPVGQYNDFVFTSESEMESGTVSGHMTHWKHGMKRHHQLEVKTERNNSCDTPSPGISPNAIGGDSKVGKRRKSDDGTSVSSSMHESNDAPCGSSAEGAGGAGNANVSTNQWSGSGGGGGSRKKNSIRSQLAQQMLNSSTRVLKKPQYVVRPASGTGSSSSSGNGGSASATNGISNGSNQSGANSCGAGNGERGTNNGGLSGSNGLGNQHYSSSQNLALDPTVLKIIFRYLPQDTLVTCCSVCKVWSNAAVDPDLWKKMNCSEHKMSASLLTAIVRRQPEHLILDWTQIAKRQLAWLVARLPALKNLSLQNCPIQAVLALHTCLCPPLQTLDLSFVRGLNDAAIRDILSPPKDSRPGLSDSKTRLRDLKVMKLAGTDISDVAVRYITQSLPYLRHLDLSSCQRITDAGVAQIGTSTTATARLTELNLSACRLVSENALEHLAKCEGLIWLDLRHVPQVSTQSVIRFASNSKHDLCVRDIKLVERRRRNSTTANRSWHHD
Protein: Espin (Autosomal recessive deafness type 36 protein) (Ectoplasmic specialization protein) (B1AK53)
Organism: Homo sapiens (Human)
Function: Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimension, dynamics and signaling capacities of the actin filament-rich microvilli in the mechanosensory and chemosensory cells. Required for the assembly and stabilization of the stereociliary parallel actin bundles. Plays a crucial role in the formation and maintenance of inner ear hair cell stereocilia (By similarity). Involved in the elongation of actin in stereocilia. In extrastriolar hair cells, required for targeting MYO3B to stereocilia tips, and for regulation of stereocilia diameter and staircase formation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9ET47}. Cell projection, stereocilium {ECO:0000269|PubMed:29572253}. Cell projection, microvillus {ECO:0000269|PubMed:29572253}.
Interaction partners:
- Myosin-IIIb
- Myosin-IIIa
- Unconventional myosin-XV
- Epidermal growth factor receptor kinase substrate 8
- Whirlin
- Fascin
- Epidermal growth factor receptor kinase substrate 8-like protein 2
- Twinfilin-2
- Unconventional myosin-Ia
- Unconventional myosin-VIIa
Sequence:
MALEQALQAARQGELDVLRSLHAAGLLGPSLRDPLDALPVHHAARAGKLHCLRFLVEEAALPAAARARNGATPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISADLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLRTVENLSVEHRVLSRDPSAELEAKQPDSGMSSPNTTVSVQPLNFDLSSPTSTLSNYDSCSSSHSSIKGQHPPCGLSSARAADIQSYMDMLNPELGLPRGTIGKPTPPPPPPSFPPPPPPPGTQLPPPPPGYPAPKPPVGPQAADIYMQTKNKLRHVETEALKKELSSCDGHDGLRRQDSSRKPRAFSKQPSTGDYYRQLGRCPGETLAARPGMAHSEEVRARQPARAGCPRLGPAARGSLEGPSAPPQAALLPGNHVPNGCAADPKASRELPPPPPPPPPPLPEAASSPPPAPPLPLESAGPGCGQRRSSSSTGSTKSFNMMSPTGDNSELLAEIKAGKSLKPTPQSKGLTTVFSGIGQPAFQPDSPLPSVSPALSPVRSPTPPAAGFQPLLNGSLVPVPPTTPAPGVQLDVEALIPTHDEQGRPIPEWKRQVMVRKMQLKMQEEEEQRRKEEEEEARLASMPAWRRDLLRKKLEEEREQKRKEEERQKQEELRREKEQSEKLRTLGYDESKLAPWQRQVILKKGDIAKY
Protein: RING finger protein Z (Protein Z) (Zinc-binding protein) (O73557)
Organism: Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
Interaction partners:
Sequence:
MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAAPTAPPTGAADSIRPPPYSP
Protein: Conserved protein (P96837)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Endonuclease 8 2 lyase Nei 2)
- Uncharacterized protein Rv0083
- Probable ATP-dependent helicase Lhr
- DNA 3'-5' helicase
- Putative bifunctional exonuclease/endonuclease protein Rv2191
Sequence:
MDELPWPVLGSEVLAAKAIPERAMRQLYEPVYPGVYAPAGVELTARQRAHAAWLWSRRRAVVAGNSAAALLGAKWVNPALDAELVHANRKPPPRIVVHTDRLAPHETVAVDGVAVTTPARTAFDIGRRTPSRLQAVQRLDALANSTDVKVADVQAVIAEHTGARGLVRLRAVLPLIDGGAESPQETWTRLVLIDAGLPKPQTQIRVFDDYGDFVARIDLGYEQLRVGVEYDGPQHWTDPAQRARDIERSTALLDLGWTIIRVTSELLWYRRGTFVGRVDAAMRAAGWRP
Protein: Envelope glycoprotein E (gE) (Q9J3M8)
Organism: Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3)
Function: Envelope glycoprotein that binds to the potential host cell entry receptor IDE.
Subcellular location: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell junction {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN), maybe through an interaction with PACS-1 sorting protein. The heterodimer gE/gI then redistributes to cell junctions to promote cell-cell spread later in the infection (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MGTVNKPVVGVLMGFGIITGTLRITNPVRASVLRYDDFHIDEDKLDTNSVYEPYYHSDHAESSWVNRGESSRKAYDHNSPYIWPRNDYDGFLENAHEHHGVYNQGRGIDSGERLMQPTQMSAQEDLGDDTGIHVIPTLNGDDRHKIVNVDQRQYGDVFKGDLNPKPQGQRLIEVSVEENHPFTLRAPIQRIYGVRYTETWSFLPSLTCTGDAAPAIQHICLKHTTCFQDVVVDVDCAENTKEDQLAEISYRFQGKKEADQPWIVVNTSTLFDELELDPPEIEPGVLKVLRTEKQYLGVYIWNMRGSDGTSTYATFLVTWKGDEKTRNPTPAVTPQPRGAEFHMWNYHSHVFSVGDTFSLAMHLQYKIHEAPFDLLLEWLYVPIDPTCQPMRLYSTCLYHPNAPQCLSHMNSGCTFTSPHLAQRVASTVYQNCEHADNYTAYCLGISHMEPSFGLILHDGGTTLKFVDTPESLSGLYVFVVYFNGHVEAVAYTVVSTVDHFVNAIEERGFPPTAGQPPATTKPKEITPVNPGTSPLLRYAAWTGGLAAVVLLCLVIFLICTAKRMRVKAYRVDKSPYNQSMYYAGLPVDDFEDSESTDTEEEFGNAIGGSHGGSSYTVYIDKTR
Protein: Protein Lines homolog 1 (Wnt-signaling molecule Lines homolog 1) (Q8NG48)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKVFCEVLEELYKKVLLGATLENDSHDYIFYLNPAVSDQDCSTATSLEWANTCGIQGRHQPISVGVAPIAVAPVCLKTNSQMSGSREVMLLQLTVIKVMTTRILSVKTEFHAKEQYRDVIKILLESAKVDSKLICMFQNSDKLLSHMAAQCLALLLYFQLREKITLSNSWIAFCQKNLSEYSESNKAIYCLWTLTAIIKEIFKDSCSQKTEILKQFLTHFDTIFEVFYNSLFSQHFENCRDTSKIVNILMCFLDLLELLIASRIHLKLHFTCQRILFLKPSCMLEVITWPIQAFVKRKVIIFLKKCLLCKVGEDLCRGSVPALMPPDHHVAVDMLALANAVLQAVNSGLLKTLSVYEKHSFFGGDEVQPECELITSPDHVILRAASLVIMKSLEIKFQNYSSASEVKVDLQRFMSELLTFLKPHLQPSLQLHNPCKWLSRVFIEQDDDMLEAAKASLGIYLTLTRGCEATESLTQGKEMWDHHTHENGYNPHCIFLFFLKNIGFDSTVLLDFLISSETCFLEYFVRYLKLLQKDWDNFFTICNNFDATESKYDISICGCVPSLVQDQSSNQTIPHRLTAPHSHRDVCARHSWASDAPSEPLKAVMSKGAHTMCASSLSSPRASQSLVDYDSSDDSDVESTEQCLANSKQTSLHQQATKEIQDAAGTSRDKKEFSLEPPSRPLVLKEFDTAFSFDCEVAPNDVVSEVGIFYRIVKCFQELQDAICRLQKKNLFPYNPTALLKLLKYIEVISNKTMNTL
Protein: Gibberellin 3-beta-dioxygenase 2 (EC 1.14.11.15) (GA 3-oxidase 2) (OsGA3ox2) (Gibberellin 3 beta-hydroxylase 2) (Protein DWARF18) (Q9FU53)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the 3-beta-hydroxylation of the inactive gibberellin precursors, leading to the formation of bioactive gibberellins. In vitro, converts the precursors GA20, GA5, GA44 and GA9 to the corresponding 3-beta-hydroxylated active products GA1, GA3, GA38 and GA4, respectively. Involved in the production of bioactive GA for vegetative growth and development. Controls the elongation of the vegetative shoot and plant height by the regulation of active gibberellin levels (Ref.7).
Interaction partners:
- Gibberellin 20 oxidase 3
- Gibberellin 2-beta-dioxygenase 1
- Gibberellin 20 oxidase 1
- Gibberellin 2-beta-dioxygenase 2
- Os05g0514600 protein
- Gibberellin 2-beta-dioxygenase 5
- Gibberellin 2-beta-dioxygenase 6
- Os02g0630300 protein
- Os05g0208550 protein
- Gibberellin 2-beta-dioxygenase 3
Sequence:
MPTPSHLKNPLCFDFRAARRVPETHAWPGLDDHPVVDGGGGGGEDAVPVVDVGAGDAAARVARAAEQWGAFLLVGHGVPAALLSRVEERVARVFSLPASEKMRAVRGPGEPCGYGSPPISSFFSKLMWSEGYTFSPSSLRSELRRLWPKSGDDYLLFCDVMEEFHKEMRRLADELLRLFLRALGLTGEEVAGVEAERRIGERMTATVHLNWYPRCPEPRRALGLIAHTDSGFFTFVLQSLVPGLQLFRRGPDRWVAVPAVAGAFVVNVGDLFHILTNGRFHSVYHRAVVNRDRDRVSLGYFLGPPPDAEVAPLPEAVPAGRSPAYRAVTWPEYMAVRKKAFATGGSALKMVSTDAAAAADEHDDVAAAADVHA
Protein: Inosine triphosphate pyrophosphatase (ITPase) (Inosine triphosphatase) (EC 3.6.1.9) (Hydroxylaminopurine sensitivity protein 1) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) (P47119)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and 5-bromodeoxyuridine 5'-triphosphate (BrdUTP) to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Adenylosuccinate synthetase
- Adenine phosphoribosyltransferase 2
- Adenine phosphoribosyltransferase 1
- Nucleoside diphosphate kinase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- GMP synthase
- Guanylate kinase
- Bifunctional purine biosynthesis protein ADE16
- AMP deaminase
- Bifunctional purine biosynthesis protein ADE17
Sequence:
MSNNEIVFVTGNANKLKEVQSILTQEVDNNNKTIHLINEALDLEELQDTDLNAIALAKGKQAVAALGKGKPVFVEDTALRFDEFNGLPGAYIKWFLKSMGLEKIVKMLEPFENKNAEAVTTICFADSRGEYHFFQGITRGKIVPSRGPTTFGWDSIFEPFDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYLYQNDF