wanglab/gogpt-training-data huggingface dataset:
Protein: Protocadherin alpha 8 (Q91Y12)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLCLGGAVPDDQLLVLSLLLIAVWEVGSGQLHYSIPEEAKHGTFVGRIAQDLELQLPELVPGLFQLDSKGFGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPMFPATQKALFIPESRLLDSRFPLEGASDADVGSNALLTYRLSTNEHFSLDVPPNHEQVKPLGLVLRKPLDREEAAEIRLLLTATDGGKPELTGTVQLLITVLDVNDNAPVFDRSLYTVKLPENVPNGSLVIKVNASDLDEGVNGDVMYSFSSDVSSDIKSKFHMDTVSGEITVIGIIDFEESKAYKIPLEARDKGLPPLIGHCTVLVEVVDANDNAPQLNVKTLWLPVKEDAQLGKIIALISVIDLDSGINGQVTCSLTNHVPFKLVSTFKNYYSLVLDSALDRETISNYDVIVTARDGGSPSLLATASVSVEVADVNDNAPAFAQPEYTVFVKENNPPGAHIFTVSAVDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLQFQVSARDAGVPALGSNVTLQVFVLDENDNVPMLLGSGTGGSDGVFNQLLSRSVDPGHVVAKVRAVDADSGYNAWLSYELLSWPGSMRSPFRVGLYTGEISTTRSLDETDGTRQRLLVLVKDHGEPPLTATVTVLVSLVESGQAPKTSSRSSVGVTVPEPSLVDVNVYLIIAICAVSSLLVLTLLLYTALRCSATPTGGACGSGKPMLVCSSAAGTWSYSQQRRQRVCSGEGPPKTDLMAFSPGLPPCPGSAEPSVSLDSSEKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: Nucleotide sugar transporter SLC35B4 (Solute carrier family 35 member B4) (UDP-xylose and UDP-N-acetylglucosamine transporter) (Q8CIA5)
Organism: Mus musculus (Mouse)
Function: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for another nucleotide sugar. May couple UDP-alpha-D-glucuronate (UDP-GlcA) or UDP-alpha-D-xylose (UDP-Xyl) efflux to UDP-alpha-D-glucuronate (UDP-GlcA) influx into the ER lumen, which in turn stimulates glucuronidation and excretion of endobiotics and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q969S0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- AMP deaminase 2
- Solute carrier family 35 member C2
- AMP deaminase 3
- AMP deaminase 1
- UDP-sugar transporter protein SLC35A5
- GDP-fucose transporter 1
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Nucleotide sugar transporter SLC35D1
Sequence:
MRPAFAVGLVFAGCCSNVIFLELLARTHPGCGNIVTFAQFLFIAVEGFLFEANLGRKPPAIPIRYYAIMVTMFFTVSVVNNYALNLNIAMPLHMIFRSGSLIANMILGIIILKKRYSMFKYTSIALVSAGIFICTFMSAKQVTVQTGLSDKDGFQAFAWWLLGIAALTFALLMSARMGIFQETLYRQFGKHSKEALFYNHALPLPGFIFLASDIYDHVVLFNKSELYQVPVIGVTMPVMWFYLLMNVVTQYVCIRGVFILTTECTSLTVTLVVTLRKFVSLIFSILYFQNQFTMWHWLGTSFVFIGTLMYTEVWKNLGTTKSELQKDDKKD
Protein: ETT ergothioneine transporter (Uncharacterized protein LOC799908) (A0A0E4G213)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNLQDYEEQTAFLGAWGPFQKTVFSLLCLSIIPNGFTGLSIVFLGDTPAHHCRIPETLNLTAGWRNASVPRPQPHGDPRASRCYRLRLDLVKNYSDGGLLPGLDVNVSEIPREECADGWIYDKEIYSSTIVSEWDLVCSDDWKSPLTSSIFFCGVLTGSVISGPVSDRFGRKIVLFVTMAIQTLFTVVQVFSPSWQIFCFLFFIVGMGQISNYVAAFVLGMEILSSSVRDVYSTLGVCLFFSIGYMILPLAAFFLRDWRSLMLALTIPGFFYIPLWWFIPESPRWLLSQGRVQEAEAIIRKAAKINRVTAPDVIFPLMQSTEDAGGVQSFSVCELLKSSNIRYMTGLLCLIWMAVSIGYCALSLNTSSLHGNIYLNCLLSAVVEVPALLMAWLMLRLAPRRHCLASTLALGGLVLLLILLIPEDQSSVTLALVMLGKFGLSAAFSIIYPVTAELYPTVLRNTALGACSMSSRVGGISAPYFNYLGSYHRSLPYILIGGINVLSGLLSFLLPESRGSALPETIGQMQTVKGLKKHSPLNIISEEARI
Protein: Polycomb group RING finger protein 5 (RING finger protein 159) (Q3UK78)
Organism: Mus musculus (Mouse)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (By similarity). Plays a redundant role with PCGF3 as part of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females.
Subcellular location: Nucleus {ECO:0000269|PubMed:28596365}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28596365}. Note=Recruited by the non-coding RNA Xist to specific nuclear foci that probably correspond to the inactivated X chromosome. {ECO:0000269|PubMed:28596365}.
Interaction partners:
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- RING1 and YY1-binding protein
- Polycomb group RING finger protein 3
- YY1-associated factor 2
- Polyhomeotic-like protein 3
- Chromobox protein homolog 2
- Chromobox protein homolog 7
- Autism susceptibility gene 2 protein homolog
- Chromobox protein homolog 8
Sequence:
MATQRKHLVKDFNPYITCYICKGYLIKPTTVTECLHTFCKTCIVQHFEDSNDCPRCGNQVHETNPLEMLRLDNTLEEIIFKLVPGLREQELQRELEFWKKNKPQENGQDDISKVDKSKADEEGDENQDDKDYHRSDPQIAICLDCLRNNGQSGDNVVKGLMKKFIRCSTRVTVGTIKKFLSLKLKLPSSYELDVLCNGEIMGKDHTMEFIYMTRWRLRGENLCCLNCSASQVCSQDGTLYQSYPMVLQYRPRIDFG
Protein: MADS box transcription enhancer factor 2, polypeptide A (Myocyte enhancer factor 2A), isoform CRA_d (Myocyte enhancer factor 2A isoform 3) (A0A0S2Z4N0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGPPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGFVNSRASPNLIGATGANSLGKVMPTKSPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT
Protein: 2-5A-dependent ribonuclease (2-5A-dependent RNase) (EC 3.1.26.-) (Ribonuclease 4) (Ribonuclease L) (RNase L) (Q05921)
Organism: Mus musculus (Mouse)
Function: Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis. Might play a central role in the regulation of mRNA turnover (By similarity). Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11585831}. Mitochondrion {ECO:0000269|PubMed:11585831}.
Interaction partners:
- ATP-binding cassette sub-family E member 1
- ATP-dependent RNA helicase DHX33
- Interferon-induced, double-stranded RNA-activated protein kinase
- 2'-5'-oligoadenylate synthase 3
- 2'-5'-oligoadenylate synthase 2
- 2'-5' oligoadenylate synthase
- WD repeat-containing protein 90
- 2'-5'-oligoadenylate synthase-like protein 2
- Interferon-induced helicase C domain-containing protein 1
- 2'-5'-oligoadenylate synthase 1A
Sequence:
METPDYNTPQGGTPSAGSQRTVVEDDSSLIKAVQKGDVVRVQQLLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRRQTTKDKRRLKQGGATALMSAAEKGHLEVLRILLNDMKAEVDARDNMGRNALIRTLLNWDCENVEEITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSREGINIDARDNEGKTALLIAVDKQLKEIVQLLLEKGADKCDDLVWIARRNHDYHLVKLLLPYVANPDTDPPAGDWSPHSSRWGTALKSLHSMTRPMIGKLKIFIHDDYKIAGTSEGAVYLGIYDNREVAVKVFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLRLPREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGESQMVRRDLEDLGRLVLYVVMKGEIPFETLKTQNDEVLLTMSPDEETKDLIHCLFSPGENVKNCLVDLLGHPFFWTWENRYRTLRNVGNESDIKVRKCKSDLLRLLQHQTLEPPRSFDQWTSKIDKNVMDEMNHFYEKRKKNPYQDTVGDLLKFIRNIGEHINEEKKRGMKEILGDPSRYFQETFPDLVIYIYKKLKETEYRKHFPQPPPRLSVPEAVGPGGIQS
Protein: Serine/threonine kinase 24 (Q5JV99)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
KKTSYLTELIDRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLDRNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQR
Protein: Pummelig, isoform A (Pummelig, isoform F) (Pummelig, isoform G (EC 3.1.1.-, EC 3.1.1.1, EC 3.3.2.10)) (RE40534p) (Q5U191)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Hormone-sensitive lipase, isoform A
- triacylglycerol lipase
- Acyltransferase
- Lipid storage droplets surface-binding protein 2
Sequence:
MSEPLALASGGVVDPTAASTSVTISNLPQPTVALGSESKSSMDLEDPRNNRFFLWKWLCNWTSSSPTMLRAVEKKILSYVKLPYRGFFVDIGPAVGEADKIWTISMNTESKEVPLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRREMNINDMILLGHSMGGFIASSYALSHPERVKHLILADPWGFPEKPSDSTNGKTIPLWVRAIARVLTPLNPLWALRAAGPFGQWVVQKTRPDIMRKFQSTIEEDINLLPQYIHQCNAQNPSGESAFHTMMQSFGWAKHPMIHRIKDVRSDIPITFIYGSRSWIDSSSGEKIKSQRGSNMVDIKIVTGAGHHVYADKPDVFNRYVNETCDMYKVAGGKLITPLQLIRESTESDEEREPSLSTAKTVEVQPEVQPVPQPVTAADTSTPTADELAANIKPK
Protein: T3SS structure protein EscU (B7UMB8)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSEKTEKPTPKKLRDLKKKGDVTKSEEVMAAVQSLILFSFFSLYGMSFFVDIVGLVNTTIDSLNRPFLYAIREILGAVLNIFLLYILPISLIVFVGTVTTGVSQIGFIFAVEKIKPSAQKISVKNNLKNIFSVKSIFELLKSVFKLVIIVLIFYFMGHSYANEFANFTGLNAYQALVVVAFFVFLLWKGVLFGYLLFSVFDFWFQKHEGLKKMKMSKDEVKREAKDTDGNPEIKGERRRLHSEIQSGSLANNIKKSTVIVKNPTHIAICLYYKLGETPLPLVIETGKDAKALQIIKLAELYDIPVIEDIPLARSLYKNIHKGQYITEDFFEPVAQLIRIAIDLDY
Protein: Lipid transferase CIDEB (Cell death activator CIDE-B) (Cell death-inducing DFFA-like effector B) (Q9UHD4)
Organism: Homo sapiens (Human)
Function: Activates apoptosis.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:35939579}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O70303}; Peripheral membrane protein {ECO:0000250|UniProtKB:O70303}; Cytoplasmic side {ECO:0000250|UniProtKB:O70303}. Golgi apparatus {ECO:0000250|UniProtKB:O70303}. Cytoplasmic vesicle, COPI-coated vesicle {ECO:0000250|UniProtKB:O70303}. Note=Enriched at lipid droplet contact sites. {ECO:0000250|UniProtKB:O70303}.
Interaction partners:
- DNA fragmentation factor subunit alpha
- DNA fragmentation factor subunit beta
- Lysosome-associated membrane glycoprotein 1
- Apolipoprotein B-100
- Perilipin-1
Sequence:
MEYLSALNPSDLLRSVSNISSEFGRRVWTSAPPPQRPFRVCDHKRTIRKGLTAATRQELLAKALETLLLNGVLTLVLEEDGTAVDSEDFFQLLEDDTCLMVLQSGQSWSPTRSGVLSYGLGRERPKHSKDIARFTFDVYKQNPRDLFGSLNVKATFYGLYSMSCDFQGLGPKKVLRELLRWTSTLLQGLGHMLLGISSTLRHAVEGAEQWQQKGRLHSY
Protein: Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (PP2A-beta) (EC 3.1.3.16) (P62716)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of protein phosphatase 2A (PP2A), a serine/threonine phosphatase involved in the regulation of a wide variety of enzymes, signal transduction pathways, and cellular events. PP2A can modulate the activity of phosphorylase B kinase, casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62714}. Nucleus {ECO:0000250|UniProtKB:P62714}. Chromosome, centromere {ECO:0000250|UniProtKB:P62714}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P62714}. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. {ECO:0000250|UniProtKB:P62714}.
Interaction partners:
- Protein phosphatase 2 scaffold subunit A alpha
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Immunoglobulin-binding protein 1
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
- Ribosomal protein S6 kinase beta-1
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Immunoglobulin
- Shugoshin 1
Sequence:
MDDKAFTKELDQWVEQLNECKQLNENQVRTLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYPERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL
Protein: AP-2 complex subunit beta (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Clathrin assembly protein large beta chain) (P27351)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Beta adaptin is a subunit of the plasma membrane adaptor.
Subcellular location: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Interaction partners:
- AP-2 complex subunit alpha
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- AP-1 complex subunit gamma-1
- Clathrin heavy chain
- AP-1 complex subunit mu-1-I
- AP-1 complex subunit sigma-1
- AP-3 complex subunit delta
- Clathrin light chain
- AP-1 complex subunit beta-1
Sequence:
MSDQKVFARYKANEIVTDLQHFGVKKFKSNITRRKNALRKIIANLVLGNYGEMSVLFSELLKFWQIEDDLEVKRICHEYIRVIGALKPQQAREALPFIMDDFKSRDEKLQIMALRTLVLVPVKELSDQAFDCIISLVNHKSPPEQVTRTAIYALLDLDEIDHERVLGLSSILHDIVKAQSSSPEVIVAALHTLYSIHEKNANMEPFRIPLELAFDMLELLPELNEWNKATVLEVLTTSVVPQHYLDTHEMIELALPYLQQVNTYVVLNSLKFIMYLLNYVDVIKETLAEKLSNSVIALLDKPPELQFLVLRNVILLLLSRESSLLRLDISYFFIEYNDPIYIKDTKLECLYLLANKETLPRILEELEQYATDIDIQMSRKSVRAIGNLAVKLDEDSVHDCVAVLLDLLEFGVDYVVQEIISVFRNILRKYPNNFKANVTELVKHTEVVQEPESKNAMIWIITQYSDVIPNYLELFRVFSSNMFSETLEVQFSILNSAIKFFIRSPTKETEELCMDLLKGCIDHENNPDLRDKTLMYWRLLSLTKTSRISNAITFESLKSVLDGELPLIEMNTKLDPTVLEELELNIGTIVSIYLKPVSHIFRLNKTKLLPQSPILNPNKDLLPVVGNSFPPTGANRDRQNSESQSSTKSRKTAMMDDYDKPAEKINQLKGKRKSSSNNPSKLSRKPSTLLRKLSMKRPFS
Protein: Centromere-binding protein 1 (CBP-1) (Centromere promoter factor 1) (Centromere-binding factor 1) (P49379)
Organism: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Function: Required for chromosome stability and methionine prototrophy. It is involved in chromosomal segregation. Binds to a highly conserved DNA sequence (5'-RTCACRTG-3'), called CDEI, found in centromeres and in several promoters (By similarity).
Subcellular location: Nucleus. Chromosome, centromere.
Interaction partners:
- KLLA0D11902p
- KLLA0F20031p
- KLLA0D09977p
Sequence:
MSGKRSYQDDQLDVEEANKRHQMVDTLLRGSEDKDGDNDNSVYDDLLQDPEEVEKENKENRDGDKVGDDEHDVVKGESEGQAAEQSSADQNDENINVDVDPSVTAVARAAQHASQRREAGDEDEDEDEEEEEDEDDHVDIDDVDKDPDAVIDEDDDEEDEDQAQRRRGKKNIEGTGESNDSERATKIGESGSSNETAGADGSGDREDGSQPDGTEHDDEENGGAGAGGAAPRRGRKPGTETGSTAWKQQRKESHKEVERRRRQNINTAIEKLSDLLPVKETSKAAILSRAAEYIQKMKETETANIEKWTLQKLLGEQQVSSLTSANDKLEQELSKAYKNLEELKKKLKEAGIEDPTEEE
Protein: E3 ubiquitin ligase ICP22 (Immediate-early protein IE68) (Infected cell protein 22) (ICP22) (P89474)
Organism: Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Function: Functions as a E3 ubiquitin ligase and plays a role in the inhibition of innate immunity by preventing IFN-mediated signaling. Induces the ubiquitination and degradation of host STAT1, STAT2 and IRF9, resulting in the blockade of ISGF3 nuclear translocation.
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P04485}. Note=Localizes in small nuclear bodies early in infection then moves to a more diffuse distribution in viral compartments as infection progresses.
Interaction partners:
Sequence:
MADIPPDPPALNTTPANHAPPSPPPGSRKRRRPVLPSSSESEGKPDTESESSSTESSEDEAGDLRGGRRRSPRELGGRYFLDLSAESTTGTESEGTGPSDDDDDDASDGWLVDTPPRKSKRPRINLRLTSSPDRRAGVVFPEVWRSDRPIRAAQPQAPASLPGIAHAHRRSARQAQMRSGAAWTLDLHYIRQCVNQLFRILRAAPNPPGSANRLRHLVRDCYLMGYCRTRLGPRTWGRLLQISGGTWDVRLRNAIREVEAHFEPAAEPVCELPCLNARRYGPECDVGNLETNGGSTSDDEISDATDSDDTLASHSDTEGGPSPAGRENPESASGGAIAARLECEFGTFDWTSEEGSQPWLSAVVADTSSAERSGLPAPGACRATEAPEREDGCRKMRFPAACPYPCGHTFLRP
Protein: IP13255p (Prominin, isoform B) (A0AVW1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDQRNLTLPTPAATTIMSSSSAAMSAGFASLGGPTTSALTGSTIALATTTTTAPPTTTPATFFTYSIPGMDIAPGPFIFTYVSEFLSLITPEELPLDSIRDVLHKNTSLLDFASNAIKIESGFIALMSVFAILALVPLIATCAWCCGRRSTQEEVDHIRNAPCHIRDESLEESLRCRKSAGLVTLWVVFILLTLSDFSIFYANSRLSAGIEMTPEMVKSAVHDVEVFLKDTHLQIKQKLDNGFHVSVERVVKDLEDVDVLLGEPIQAEISAHTGLELAYDSLTTLSLANAELIYRVLMLQETVGRALKLSQEAAARMEELQIQLSVLQRQCTYRDRPLCDTLRIRSFEENGVVDALKTLQEDQSIFRMRYLGEIEFGATVKNLTSEVGVSRSIFSNFPQQVKHDTAYERNYTLEQLASIRHRTTANAQQLTSTVNGLLRRLEDTWSSLQPAYNELKEWADAYWSVGWIAGTVIVWVMLFMLMSYCCFLCESNAKSGVVFFIAVMLICLASICLTIFGVFSLAVGGNAEVFVCRSLYDEDYNMLGKLLDKPGYAYAREPQTGIIGELLRPVGVNRSVVNVGLGQALRGCEQNQASYNVFQLDAFVNTSKIADLRQFPKVSTAIDAISVSGRTLLSLTQSVQNILDNMLQTSSFNLTTYRSSVGAPTPEKDLATFIDQMQRVALQIQDVATSSRMTTLGSRSKRLQASILQPLENLQNEILYHLTALELQRDPWAKQVNQTLNHLKSIQSYLENKAGEICHNMTRDYRDRLKAYLTTSKATMESQLGDTTTKCRPFYDTFDASRTFLCRNMVDFINGLTFFIFLTLLLWAIGTPVGLNLITVQTRLNVMQAAQARSKGRHRRSDRSPEHEQRSGSRGRKKQRTSSSATSGRSGKRDQSRERSTSSTARPKPPLRRTATEETLDLADEESTPSRQQQQQPPPQRRQESDRERVRERDQRSRERELSRGRDASAMNTPVRSRSRQQLQRTGTDEFDLDDSDAYGAGGHLDADVAAARRTPPRGAPPPPPPPAAGLNSDRTVRWNEDETEDFDFEEVDAPKSPMYLSHNLQ
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q389Q0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MCCGRRISAETFILPALFLLTSYSIFSFCVFIFPRLLDALGQAFLQPFIRGIRQPTSATPLHVEHLLSISAGSWGLFGVSAVLFSFTVWAYVAAATTDPGRVPYAYHKGAPKSATLALKVSGAQHHCPVCAHYKPQRAHHCSRCRRCVLKYDHHCPWIGRCVGFFNYKLYLLVIFYTFLCTLWVVLLLLLACSSFAVQHYEAVNGQVRHRRVDMPAWDSRKCWAEAEALDRPHLRAKDLVVSAQAVAQLSLFEEFGVCPPFLGVYVCFLEAFIFLILSGSLLRKHWGLARRNLTTLDLVIQQTQIEQGICVRPPVNPFDIGVKGNLHQVFGDGDADGEHIHANFIARWFCRLLPVAAYPEQEQLRYASSVSSERSALVSTDPALWAGGAQASIPNYGTLQKGDLSGGVGQVTVIEGRGVCNVYHLSQVSSHVGSLLGQTFPTAVPLTSPTPV
Protein: DNA polymerase alpha subunit B (DNA polymerase alpha 70 kDa subunit) (DNA polymerase subunit II) (O89043)
Organism: Rattus norvegicus (Rat)
Function: Accessory subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis (By similarity). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1 (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- DNA primase large subunit
- DNA polymerase alpha catalytic subunit
- DNA primase
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon catalytic subunit
- DNA polymerase epsilon subunit
- DNA polymerase zeta catalytic subunit
- DNA polymerase delta subunit 2
- DNA replication licensing factor MCM4
- Replication factor C subunit 3
Sequence:
MAVSTQQLAEELQIFGLDCEDSLLEKLAELCTLYRQTEERMVSELIAFCTSAGKSCLTGEILSSFEHEVLNKKLSKACHSASKDNRHAGARDIVSIQELIEAEEEEETLLSAYTTPSKGPHKRVSSTPETPLTKRSISTRSPHQLLSPSSFSPSATPSQKYSSRTNRGEVVTTFGSAQGVSWSGRGGSGSISLKVMGYPEPLTSSYKTMFQQLPDIREVLTCKIEELGSELKEHYKIEAFTPLLVPAQEPVILLGQIGCDSNGRLNSKSVILEGDREHSSGAQIPVDVSELKDYSLFPGQVVIMEGFNTTGRRLTATKLYEGVPLPFYQPTEEEGDFEQTMVLVACGPYTTSDSITYDPLLDLISTINHDRPDVCILFGPFLDAKHEQVENCKLTSPFEDIFKQCLRTVIEGTRSSGSHLVFVPSLRDVHHEPVYPQPPFTFSELPREDKKRVQFVSEPCNLSINGVMFGLTSTDLLFHIGAEEICSSSGTSDRFSRILKHILTQRSYYPLYPPHEDMAIDYENFYTYAQLPVTPDVFIVPSELRYFVKDIFGCVCMNPGRLTKGQVGGTFGRLYLRRQPKGTDSEGRQGLSVAAQVVRI
Protein: Transcription factor CP2 (F8VX55)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU01313}.
Interaction partners:
Sequence:
MAWALKLPLADEVIESGLVQDFDASLSGIGQELGAGAYSMSDVLALPIFKQEESSLPPDNENKILPFQYVLCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKLGELPEINGKLVKSIFRVVFHDRRLQYTEHQQLEGWRWNRPGDRILDIDIPMSVGIIDPRANPTQLNTVEFLWDPAKRTSVFIQVHCISTEFTMRKHGGEKGVPFRVQIDTFKENENGEYTEHLHSASCQIKVFKPKGADRKQKTDREKMEKRTPHEKEKYQPSYETTILTECSPWPEITYVNNSPSPGFNSSHSSFSLGEGMVRPRLTIYVCQESLQLREQQQQQQQQQQKHEDGDSNGTFFVYHAIYLEELTAVELTEKIAQLFSISPCQISQIYKQGPTGIHVLISDEMIQNFQEEACFILDTMKAETNDSYHIILK
Protein: Uncharacterized inner membrane transporter YicL (P31437)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane protein YhaI
- Inner membrane symporter YicJ
- Alpha-xylosidase
Sequence:
MGSTRKGMLNVLIAAVLWGSSGVCAQYIMEQSQMSSQFLTMTRLIFAGLILLTLSFVHGDKIFSIINNHKDAISLLIFSVVGALTVQLTFLLTIEKSNAATATVLQFLSPTIIVAWFSLVRKSRPGILVFCAILTSLVGTFLLVTHGNPTSLSISPAALFWGIASAFAAAFYTTYPSTLIARYGTLPVVGWSMLIGGLILLPFYARQGTNFVVNGSLILAFFYLVVIGTSLTFSLYLKGAQLIGGPKASILSCAEPLSSALLSLLLLGITFTLPDWLGTLLILSSVILISMDSRRRARKINRPARHK
Protein: Lactase (G8Z4I7)
Organism: Emericella nidulans (Aspergillus nidulans)
Interaction partners:
Sequence:
MPESSSANDWENPRVFQRNRLKARAYWIPETSLLLNGDWDFNYVSSPLLAPSPTPSRLSGDGGEEKDAEQDQVEWKPIPVPGHWQLHGYGRPNYTNVIFPFPVDPPRVPSENPTGTYKRSFRVPSTWDRDAQLRLRFDGVDSAYHVWVNGVQVGYAQGSRNPAEFDISDQVDREKENEVFVRVYQWCDGSYIEDQDQWWLSGIFRDVTLIAFPSVSRIEDFRVTTTLDSEYHDAELHLAVDIASTEASTLHVELFDRASNGTLATEDKEIVGTGTYKLSLSVRNPRKWTAETPFLYDLEIALATRYDPSAILQKVHHRVGFRQVEIKNGNITVNGVPVLFRGVNRHDHHPLHGRAVPLDFVKEDLLLMKRHNINSVRCCHYPSTPQLFSMCDELGLWVMDEADLECHGFYDAVARPLDIPESMDYEERKKLTFAQAAEFTSNNPEWKAAYLDRAEQMVARDRNYASVVIWSLGNEAFYGANHAAMYRFIKEEDPTRPVHYEGDMEAKTADMYSFMYPSVDRITRLATEEGDAFTKPIVLCEYGHAMGNAPGGLAEYMNAFRTYRRLQGGWIWEWANHGLWLEEKGFYAYGGDFGDQPNDGSFVLDGLLYSNHTPTPGLVELRKAYEPIHAWYEDGRIRLQNRFDFAGLEGVQAGYRVEVLGEGMELIEAGTLEIPALRAGETGEIPFPSSFPSKATAGGETWLTVSFTTKHATPGLDANYEIAWFQHRLGSTAPSLPALTPAASFPIQTHSTKADHIITGADFTITFSRTTGLLTSWRIHSREILADSTSAGLTLGFWRPPTDNELPYDLGEWRRYGLDTLTSSLRKISLTEVDESMLEIRTEAYVSPPILAWGFEAETVYRITGDGALTVKAHVKPSGAKPVDVPRVGFDLVLADELDNASWFGLGPGESYADKKLSQKISIYSATTSELQTPYEVPQEGGNRMETRWLRLLNNRGRGVCVTRDADGDEEQAFQWVATRYSAESVERAKHPNELSPEKRVRVRLDVESAGVGTGACGPRTLEQYRVPCAERRFGFRIAPWTK