wanglab/gogpt-training-data huggingface dataset:
Protein: Putative E3 ubiquitin-protein ligase XBAT31 (EC 2.3.2.27) (Ankyrin repeat domain and RING finger-containing protein XBAT31) (Protein XB3 homolog 1) (RING-type E3 ubiquitin transferase XB31) (Q94B55)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: No E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro.
Interaction partners:
- Putative E3 ubiquitin-protein ligase XBAT35
- Probable E3 ubiquitin-protein ligase RHY1A
- Probable protein phosphatase 2C 33
- C3H4 type zinc finger protein
- B-box zinc finger protein 18
- Putative E3 ubiquitin-protein ligase XBAT34
- F-box protein FBW2
- Small ribosomal subunit protein eS4z
Sequence:
MGQSMSCGSRPEHGIFASVQCGDIITIRRVMATEPSLLNQTTPYDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLAEVGANILMFDSVNRRTCLHYAAYYGHANCVQAILSAAQSSPVAVHWGYARFVNIRDDKGATPLHLAARQRRPECVNVLLDSGSLVCASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGRIPYVVAMKHKHGACGALLNPSSAEPLVWPSPLKFISELNDEAKLLLEQALMEANREREKTILKGTAYSLPSPSFSDTDDNMSEVSDTELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNPTTSTVTPPVCPFCRSTIACLVVAQNNNNNNEKSKSLDDVVVVDREAGDVSSSKFRKHRRSINLGEESSSFMGLSTIGSFGRITGRGSGRIAAENELMDKPIL
Protein: Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) (A0A2R8Y6L6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKNWDSLDEHGVCTADKDCEDAYRVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGADAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPALYRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVCCVLQGGRVPGQREDPAAGAVCLHAPEGPAQSWDGH
Protein: 5'-nucleotidase (5'-NT) (EC 3.1.3.35) (EC 3.1.3.5) (EC 3.1.3.89) (EC 3.1.3.91) (EC 3.1.3.99) (5'-deoxynucleotidase) (Ecto-5'-nucleotidase) (IMP-specific 5'-nucleotidase) (Thymidylate 5'-phosphatase) (CD antigen CD73) (P21588)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of nucleotide monophosphates, releasing inorganic phosphate and the corresponding nucleoside. AMP is the preferred substrate but can also hydrolyze CMP and GMP. Shows a preference for ribonucleotide monophosphates over their equivalent deoxyribose forms (By similarity). Other substrates include IMP, UMP, dAMP, dCMP, dTMP, NAD and NMN (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1770988, ECO:0000269|PubMed:2148114, ECO:0000269|PubMed:2298743}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2148114, ECO:0000269|PubMed:2298743}.
Interaction partners:
- Ectonucleoside triphosphate diphosphohydrolase 1
- Adenosine deaminase
- Purine nucleoside phosphorylase
- NAD-capped RNA hydrolase NUDT12
- Adenosine kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- AMP deaminase 2
- AMP deaminase 3
- AMP deaminase 1
- Uridine phosphorylase
Sequence:
MRPAAATAPKWLLLALSALLPLWPTAKSWELTIMHTNDVHSRLEQTSDDSTKCLNASLCVGGVARLFTKVQQIRKEEPNVLLLDAGDQYQGTIWFTVYKGLEVAHFMNLLGYDAMALGNHEFDNGVEGLIDPLLRNVKFPILSANIKARGPLAPQISGLYLPYKVLSVGGEVVGIVGYTSKETPFLSNPGTNLVFEDEVTALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVVGGHTNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKVEFDDKGNVVTSYGNPILLNSTIREDAAIKADINQWRIKLDNYSTQELGRTIVYLNGSAQECRFRECNMGNLICDAMINNNLRHPDEMFWNHVSMCIVNGGGIRSPIDERNNGTITWENLAAVLPFGGTFDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDISRKPWDRVVQLKVLCTKCRVPIYEPLEMDKVYKVVLPSYLVNGGDGFQMIKDELLKHDSGDQDISVVSEYISKMKVIYPAVEGRIKFSAASHYQGSFPLIILSFWAVILVLYQ
Protein: Lymphocyte activation gene 3 protein (LAG-3) (Activation-induced cytidine deaminase-linked autoimmunity protein) (Aida) (CD antigen CD223) [Cleaved into: Secreted lymphocyte activation gene 3 protein (sLAG-3)] (Q61790)
Organism: Mus musculus (Mouse)
Function: Lymphocyte activation gene 3 protein: Inhibitory receptor on antigen activated T-cells. Delivers inhibitory signals upon binding to ligands, such as FGL1. FGL1 constitutes a major ligand of LAG3 and is responsible for LAG3 T-cell inhibitory function. Following TCR engagement, LAG3 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation. May inhibit antigen-specific T-cell activation in synergy with PDCD1/PD-1, possibly by acting as a coreceptor for PDCD1/PD-1. Negatively regulates the proliferation, activation, effector function and homeostasis of both CD8(+) and CD4(+) T-cells. Also mediates immune tolerance: constitutively expressed on a subset of regulatory T-cells (Tregs) and contributes to their suppressive function. Also acts as a negative regulator of plasmacytoid dendritic cell (pDCs) activation. Binds MHC class II (MHC-II); the precise role of MHC-II-binding is however unclear.
Subcellular location: [Lymphocyte activation gene 3 protein]: Cell membrane {ECO:0000269|PubMed:8602528}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secreted lymphocyte activation gene 3 protein]: Secreted {ECO:0000269|PubMed:15557174, ECO:0000269|PubMed:17245433}. Note=Produced following cleavage of the main chain. {ECO:0000269|PubMed:17245433}.
Interaction partners:
- Galectin-3
- T-lymphocyte activation antigen CD80
- Galectin-9
- T-lymphocyte activation antigen CD86
- Fibrinogen-like protein 1
- Cytotoxic T-lymphocyte protein 4
- Programmed cell death 1 ligand 1
- Programmed cell death protein 1
- T-cell immunoreceptor with Ig and ITIM domains
- Alpha-synuclein
Sequence:
MREDLLLGFLLLGLLWEAPVVSSGPGKELPVVWAQEGAPVHLPCSLKSPNLDPNFLRRGGVIWQHQPDSGQPTPIPALDLHQGMPSPRQPAPGRYTVLSVAPGGLRSGRQPLHPHVQLEERGLQRGDFSLWLRPALRTDAGEYHATVRLPNRALSCSLRLRVGQASMIASPSGVLKLSDWVLLNCSFSRPDRPVSVHWFQGQNRVPVYNSPRHFLAETFLLLPQVSPLDSGTWGCVLTYRDGFNVSITYNLKVLGLEPVAPLTVYAAEGSRVELPCHLPPGVGTPSLLIAKWTPPGGGPELPVAGKSGNFTLHLEAVGLAQAGTYTCSIHLQGQQLNATVTLAVITVTPKSFGLPGSRGKLLCEVTPASGKERFVWRPLNNLSRSCPGPVLEIQEARLLAERWQCQLYEGQRLLGATVYAAESSSGAHSARRISGDLKGGHLVLVLILGALSLFLLVAGAFGFHWWRKQLLLRRFSALEHGIQPFPAQRKIEELERELETEMGQEPEPEPEPQLEPEPRQL
Protein: Toxic protein SymE (Putative endoribonuclease SymE) (EC 3.1.-.-) (P39394)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type I toxin-antitoxin (TA) system. Involved in the degradation and recycling of damaged RNA. It is itself a target for degradation by the ATP-dependent protease Lon.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:17462020}. Note=Purifies with ribosomes. {ECO:0000269|PubMed:17462020}.
Interaction partners:
- Small toxic protein TisB
- Small toxic polypeptide LdrD
- Small toxic protein ShoB
- Uncharacterized protein DinQ
- Endodeoxyribonuclease toxin RalR
- LexA repressor
Sequence:
MTDTHSIAQPFEAEVSPANNRHVTVGYASRYPDYSRIPAITLKGQWLEAAGFATGTAVDVKVMEGCIVLTAQPPAAEESELMQSLRQVCKLSARKQKQVQAFIGVIAGKQKVA
Protein: Uncharacterized protein (Q384K6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- ATP synthase, putative
- H
- V-type proton ATPase subunit C
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit a
- V-type proton ATPase subunit F
- 
- V-type ATPase, C subunit, putative
- V-type proton ATPase subunit
- Vacuolar ATP synthase subunit D, putative
Sequence:
MDFLFGTMFFAATGALGVFFTPFLTRDLVGLVRILCVTAAFCCWLSWALIYLSQVHPLLIPTRNIKKE
Protein: ADP-ribosylation factor-like protein 2-binding protein (ARF-like 2-binding protein) (Binder of ARF2 protein 1) (Q9D385)
Organism: Mus musculus (Mouse)
Function: Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23849777}. Mitochondrion intermembrane space {ECO:0000269|PubMed:23849777}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23849777}. Note=Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization (By similarity). {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor-like protein 2
- Cilia- and flagella-associated protein 20
Sequence:
MDALEEESFALSFSSASDAEFDAVVGCLEDIIMDDEFQLLQRNFMDKYYQEFEDTEENKLTYTPIFNEYISLVEKYIEEQLLERIPGFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRGLDLSSGLVVTSLCKSSSTPASQNNLRH
Protein: Guanine nucleotide-binding protein G(t) subunit alpha-1 (Transducin alpha-1 chain) (P04695)
Organism: Bos taurus (Bovine)
Function: Functions as signal transducer for the rod photoreceptor RHO. Required for normal RHO-mediated light perception by the retina (By similarity). Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs), such as the photoreceptor RHO. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Activated RHO promotes GDP release and GTP binding. Signaling is mediated via downstream effector proteins, such as cGMP-phosphodiesterase.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:23303210}. Membrane {ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:28655769}; Peripheral membrane protein {ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:28655769}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P20612}. Note=Localizes mainly in the outer segment in the dark-adapted state, whereas is translocated to the inner part of the photoreceptors in the light-adapted state. During dark-adapted conditions, in the presence of UNC119 mislocalizes from the outer segment to the inner part of rod photoreceptors which leads to decreased photoreceptor damage caused by light. {ECO:0000250|UniProtKB:P20612}.
Interaction partners:
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
- Rhodopsin
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 9
- Chaperone Ric-8A
- Guanine nucleotide-binding protein G
Sequence:
MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Protein: Degenerin deg-1 (Degeneration of certain neurons protein 1) (P24585)
Organism: Caenorhabditis elegans
Function: Probable sodium channel subunit. Required by a subset of neurons.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Acid-sensing ion channel 1
- Ion transport domain-containing protein
- Acid-sensing ion channel 1-like
- Acetylcholine receptor subunit alpha-type deg-3
- DEgenerin Like
- DEgenerin Like
- Ion transport domain-containing protein
Sequence:
MSNHHSKTKKTSMLGREDYIYSHDITNKNKKEKLNGASKNNDYNQDDDDETMKSKMMDFCDKTTAHGAKRVLIARNSFSKLMWGLIIFSFLLMFAYQASKLIFKFSAHEKITDISLKFDDVEFPAITFCNLNPYKKSLVMMVPSIRDTMDVYDNAKTHSKSEGEKKKPKVSRKQHSDASQQMVRELFAKEIEEGMVELKKSNKTLQSQNKSGRRRSQRSIENRRYEAIEAHCKCVGNIGMECIRFESPPRDPSSKCICTYDRDMEVAWPCFNISVWYDHECPLCHDDGYCESTLPSGTTSSDKWPCMCRNRGDTSERDDTPYCIGKAGVGKIEIRKLWLENNMTTTSTTTTTTTTPPPTTTSTTTTTTTTPPPTTTARPNQRAIVSNPETIKAMGFQGMTDGVAMLTRAKENLMFTMAALSDKQRIALSQSKHEFIEMCSFNGKECDIDEDFRLHVDPEFGNCFTFNYDVNNNYTSSRAGPMYGIRVLLFVNTSDYMSTSESSGVRLAIHPPTEYPFPDTFGYSAPVGFASSFGIKKKVMQRLPAPYGECVETKKVVDRNYIYAGYDYHPEGCHRSCFQNGLIDDCSCGDPRFPVPEGYRHCSAFNATARTCLEKNIGSVGDFHHITQKMDKCVCKQSCEEIIHEVTFSCSKWPSGATDLGDCDGMTESECEQYYRLNAAMIEVFYEQLNYELLQESEAYGLVNLIADFGGHLGLWLGFSVITVMEVCVLLVDMISLFFKSRHEEKLLRQSTKRKDVPEDKRQITVGSGRKSDAFVSI
Protein: Carbohydrate-binding domain-containing protein C2E1P3.05c (Q9P7F1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Putative aryl-alcohol dehydrogenase C977.14c
- Transposon Tf2-2 polyprotein
Sequence:
MLTQSLFLTVLTLALSLVSKTSASQCSPRYGTCGGIYYDGPTCCVVGSSCIYSNPWYSQCIPVDYTGPCAKLYQQCGGINYNGPTCCEPGSECIYNGPYYSQCIPVDIDPSSSSSSAASSTTSTTSSSSLVSSTTLTSSSPSAVSSTTSIPSISSTISSSVSTSSFTSLSSSGFSTVLSSTNTTSALPSSGWNVTGY
Protein: Small ribosomal subunit protein eS28 (40S ribosomal protein S28) (Q9W334)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein eL15
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL22
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein eS7
- FI01658p
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL21
Sequence:
MDKPVVWARVMKVLGRTGSQGQCTQVKVEFLGEQNRQIIRNVKGPVREGDILTLLESEREARRLR
Protein: Syncrip, isoform O (A0A0B4KH24)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLSQMEASKVQKDEGGGEALSRTILKTPSSFRTPSPIPSCSKMAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYGSWSWAWNHSTAWQSRWPTWQHQSSGGPNSATGGGSGSGGGTGGGGGSSAGGHRSGGAGSNRGVPWGVANASQRSWHPARQAATKFTSWSCIQNIHGG
Protein: ALA-interacting subunit 1 (AtALIS1) (ALA3 beta-subunit 1) (Q9LTW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the lipid transport activity of the ALA/ALIS P4-ATPase complex.
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein. Prevacuolar compartment membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=In a heterologous system, the final intracellular localization after exit from the endoplasmic reticulum is the prevacuolar compartment in the presence of ALA2 and the Golgi in the presence of ALA3.
Interaction partners:
- Phospholipid-transporting ATPase 3
- Phospholipid-transporting ATPase 10
- Phospholipid-transporting ATPase 2
- Probable phospholipid-transporting ATPase 12
- S-protein homolog 1
- Probable phospholipid-transporting ATPase 7
- Phospholipid-transporting ATPase 1
- Phospholipid-transporting ATPase 6
- Probable phospholipid-transporting ATPase 4
- Phosphatidylglycerophosphate phosphatase PTPMT1
Sequence:
MSSSNTPSSSAAAAGSIDSSAARRNSKRPKYSKFTQQELPACKPILTPGWVISTFLIISVIFIPLGVISLFASQDVVEIVDRYDSACIPLSDRANKVAYIQGTGNKSCTRTLIVPKRMKQPIYVYYQLENFYQNHRRYVKSRSDSQLRSVKDENQIDACKPEDDFGGQPIVPCGLIAWSLFNDTYVLSRNNQGLTVNKKGIAWKSDKEHKFGKNVFPKNFQKGNLTGGASLDPNKPLSDQEDLIVWMRTAALPTFRKLYGKIESDLEKGENIQVTLQNNYNTYSFSGKKKLVLSTTSWLGGKNDFLGIAYLTVGGICFVLALAFTVMYLVKPRRLGDPTYLSWNRIPGGR
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (A0A1D8PSE5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSNSVSEAESRGHKSLEIEEYQIEEYQIDNHTNDESSEILDPHQLNKVYRKLDLRIIPALWCLYFLTSFGSNCYGLTLTMNRAEGHSLAQQLHLTSKDTSTASALYYVGYIIFDVPMNLIMTKVSPQTWLARIVITVGLVYTCYHVLHNAGGVIAVRFISGVVGAGTWPGLSYYVSLWYPNDRSTRRIGYYFTAAQISAAVAGLVSAGFQKMDGVHGYTGWQWMYLVYGVITMTVGIALLWWLPDRPFIGVKSESNRLVEFYRKFTTPPHPLNEQEKELHRKDLEHRYKLLKWTWKDVVNIITDLRIWPLIIMYFGVVGTGFGLAVFGSTIIATNNPNLTSIQVSLLYAPIWLFDLGGILIITPFADRFKKFRALIFSGACVIIIVGMVVTTFAHGSWNKYGGLLIAGFGLGPTVPICMSWSAEIFQKRYGDVGNAVSAALVSGLGNLGSVTSTYALYSGWPEDKARLYRNSNMMLVLMLGVSIIASGVCQLIKDKVRQPK
Protein: Putative uncharacterized protein VPS69 (O13584)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MHTYIYIYTVYIQMVAFSPYRIVLPFVAFVDLASFSSFRSYQAFLRPFLRPFRHQTCSSYFALDLDFASAFVVPAASFVESLLAYQAYSAYQACLAYPACLACQAS
Protein: Transposon Ty1-MR2 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q04670)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIQAYHKEVNQLLKMKTWDTDRYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDPGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Myelin protein P0 (Myelin peripheral protein) (MPP) (Myelin protein zero) (P27573)
Organism: Mus musculus (Mouse)
Function: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P25189}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25189}.
Interaction partners:
- Myelin protein zero-like protein 1
- Periaxin
- E3 SUMO-protein ligase EGR2
- Transcription factor SOX-10
- Gap junction beta-1 protein
- Myelin P2 protein
- Pro-neuregulin-1, membrane-bound isoform
Sequence:
MAPGAPSSSPSPILAALLFSSLVLSPALAIVVYTDREIYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGAFKERIQWVGDPRWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKVPTRYGVVLGAVIGGILGVVLLLLLLFYLIRYCWLRRQAALQRRLSAMEKGRFHKSSKDSSKRGRQTPVLYAMLDHSRSTKAASEKKSKGLGESRKDKK
Protein: Membrane glycoprotein spo14 (SEC12-like protein) (Sporulation-specific protein 14) (Q10659)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the formation of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein sar1.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type II membrane protein. Note=Cycling between endoplasmic reticulum and the early Golgi.
Interaction partners:
- Small COPII coat GTPase sar1
- Sporulation-specific protein 3
- Sec14 cytosolic factor
- Uncharacterized protein C1259.08
- Protein sey1
- Protein rer1
- Cell cycle protein kinase spo4
- Sporulation-specific protein 2
- Sporulation-specific protein 15
- Sporulation-specific protein 13
Sequence:
MAELHLSFPAYSLCWINNHQMAVGGGGGTTKSGVKNKLKLLSYEDYEPEVGEGHTKFIEHGEIELKHSDDAVMSLGYFKNELIAGINNTIDGKLIDHLRLYGRKDKLFEEKNALRLTDFDNDEQYQRLCLFEPLHDAICISCTNKSFFIISKNDHKVLFEKHGSDVYDVSSTEDKLAIAVDDRVEIYDWNTFELVQVLYMPVERATVRGVSFLPNQSIVAAYNYIKDSKRFASLVRFDYSSKNQLWRFGMIRDLKNAKGVTCFCCDKENGMIIVAGADCSIRFMSLDLTKLSQVYKHSLPVTDMQLSPDSEALVSVSADGLLCLQFVGKFKNLSAVKLEDAGVILRLSLMFPFVLAILYFYLQLLFPDEKLDAIHRFFSFILHIFSKYTIRNYDL
Protein: Forkhead box protein P1 (Q58NQ4)
Organism: Gallus gallus (Chicken)
Function: Transcriptional repressor.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H334}.
Interaction partners:
- Uncharacterized protein.
- Ig-like domain-containing protein.
- Ig-like domain-containing protein.
- Interleukin-10
- Uncharacterized protein.
- Cytotoxic T-lymphocyte protein 4
- Interleukin-4
- Interferon gamma
- Interleukin-6
- GATA-binding factor 3
Sequence:
MMQESGTETKSNGSAIQNGASGGNHLLECSLREVRSNGETPSVEIGAADLTHLQQQQALQVARQLLLQQQQQQQQQQQQQQQQQVSGLKSPKRNDKQPALQVPVSVAMMTPQVITPQQMQQILQQQVLTPQQLQVLLQQQQALMLQQQQLQEFYKKQQEQLQLQLLQQQHAGKQPKEPQQQQVATQQLAFQQQLLQMQQLQQQHLLTLQRQGLLTIQPGQPTLPLQPLAQGMIPTELQQLWKEVTSSHTAEEAASNNHSSLDLSTTCVSSSAPSKTSLIINPHASTNGQLSVHTPKRESLSHEEHSHSHPLYGHGVCKWPGCEAVCEDFQSFLKHLNSEHALDDRSTAQCRVQMQVVQQLELQLAKDKERLQAMMTHLHVKSTEPKATPQPLNLVSSVTLSKTASEASPQSLPHTPTTPTAPITPVTQGPSVITTTSMHNVGPIRRRYSDKYNVPISSADIAQNQEFYKNAEVRPPFTYASLIRQAILESPEKQLTLNEIYNWFTRMFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEQEFQKRRPQKISGNPSLIKNIQTSHTYCTPLNAALQASMAENSIPLYTTASMGNPTLGNLANVMREELNGAMEHTNSNGSDSSPGRSPMQAMHPVHVKEEPLDPDENEGPLSLVTTANHSPDFDHDRDYEDEPVNEDIE