wanglab/gogpt-training-data huggingface dataset:
Protein: Protein M2-1 (Envelope-associated 22 kDa protein) (Transcription antitermination factor M2-1) (Vp24) (P04545)
Organism: Human respiratory syncytial virus A (strain A2)
Function: Acts as a tetrameric transcription processivity factor that binds in a competitive manner to RNA and the phosphoprotein (P) to prevent premature termination during transcription. Transcription anti-terminator that enhances readthrough of intergenic junctions during viral transcription. Preferentially binds to poly(A)-rich sequences. Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding. Also, can activate host NF-kappa-B through association with host RELA.
Subcellular location: Virion {ECO:0000269|PubMed:23776214, ECO:0000269|PubMed:24760890}. Host cytoplasm {ECO:0000269|PubMed:11907323, ECO:0000269|PubMed:22675274, ECO:0000269|PubMed:27194388, ECO:0000269|PubMed:28916773, ECO:0000269|PubMed:29489893, ECO:0000269|PubMed:31649314}. Host nucleus {ECO:0000269|PubMed:15629770}. Note=Localizes in cytoplasmic inclusion bodies substructures called inclusion bodies associated granules (IBAGs) (PubMed:22675274, PubMed:28916773, PubMed:29489893, PubMed:31649314). Forms a layer between the matrix and nucleocapsid (PubMed:23776214, PubMed:24760890). {ECO:0000269|PubMed:22675274, ECO:0000269|PubMed:23776214, ECO:0000269|PubMed:24760890, ECO:0000269|PubMed:28916773, ECO:0000269|PubMed:29489893, ECO:0000269|PubMed:31649314}.
Interaction partners:
Sequence:
MSRRNPCKFEIRGHCLNGKRCHFSHNYFEWPPHALLVRQNFMLNRILKSMDKSIDTLSEISGAAELDRTEEYALGVVGVLESYIGSINNITKQSACVAMSKLLTELNSDDIKKLRDNEELNSPKIRVYNTVISYIESNRKNNKQTIHLLKRLPADVLKKTIKNTLDIHKSITINNPKESTVSDTNDHAKNNDTT
Protein: BAG family molecular chaperone regulator 5 (BAG-5) (Bcl-2-associated athanogene 5) (Q9UL15)
Organism: Homo sapiens (Human)
Function: Co-chaperone for HSP/HSP70 proteins. It functions as a nucleotide-exchange factor promoting the release of ADP from HSP70, thereby activating HSP70-mediated protein refolding. Has an essential role in maintaining proteostasis at junctional membrane complexes (JMC), where it may function as a scaffold between the HSPA8 chaperone and JMC proteins enabling correct, HSPA8-dependent JMC protein folding (By similarity). Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity).
Subcellular location: Note=In cardiomyocytes, localized at specialized membrane contact sites between T-tubules and the sarcoplasmic reticulum, known as junctional membrane complexes. {ECO:0000250|UniProtKB:Q8CI32}.
Interaction partners:
- Heat shock 70 kDa protein 1A
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 4
- BAG family molecular chaperone regulator 2
- Cyclin-G-associated kinase
- E3 ubiquitin-protein ligase CHIP
- BAG family molecular chaperone regulator 1
- Heat shock-related 70 kDa protein 2
- Ras-related protein Rab-7L1
- E3 ubiquitin-protein ligase parkin
Sequence:
MDMGNQHPSISRLQEIQKEVKSVEQQVIGFSGLSDDKNYKKLERILTKQLFEIDSVDTEGKGDIQQARKRAAQETERLLKELEQNANHPHRIEIQNIFEEAQSLVREKIVPFYNGGNCVTDEFEEGIQDIILRLTHVKTGGKISLRKARYHTLTKICAVQEIIEDCMKKQPSLPLSEDAHPSVAKINFVMCEVNKARGVLIALLMGVNNNETCRHLSCVLSGLIADLDALDVCGRTEIRNYRREVVEDINKLLKYLDLEEEADTTKAFDLRQNHSILKIEKVLKRMREIKNELLQAQNPSELYLSSKTELQGLIGQLDEVSLEKNPCIREARRRAVIEVQTLITYIDLKEALEKRKLFACEEHPSHKAVWNVLGNLSEIQGEVLSFDGNRTDKNYIRLEELLTKQLLALDAVDPQGEEKCKAARKQAVRLAQNILSYLDLKSDEWEY
Protein: Tachykinin-like peptide-II (P.nigriventer tachykinin peptides II) (PnTkP-II) (U29-ctenitoxin-Pn1b) (U29-CNTX-Pn1b) (P86299)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKDK
Protein: Claudin (A0A2R8Q922)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, tight junction {ECO:0000256|RuleBase:RU060637}. Cell membrane {ECO:0000256|RuleBase:RU060637}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU060637}.
Interaction partners:
- BCL2 modifying factor 1.
- Transmembrane protein 101
- non-specific serine/threonine protein kinase
- Claudin
- Tight junction protein 1a
Sequence:
MAVMVLQVLGLFLGIVGWCLESSSINSSVWKSSSHGEAVVTASSQFEGLWFSCASNSLGAIHCQRFKTTLGLPGYIQACRALMIIALILGLLSVVLASMGLKCTKLGSTSEEAKGKISLTAGIMFILSGLCVIVAVSWYAARVVQEFNDPFYGGTKYELGAGLYLGWAAAALCILGGGTLCTSFKGSSPAQTRGPGYNYSAAQPQKIYRSAPSDNSITKAYV
Protein: NRR repressor homolog 2 (Q5QM06)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Binds to and weakly represses NPR1/NH1-mediated transcriptional activation of LG2 in vitro.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5ZEF1}.
Interaction partners:
Sequence:
MEARLSTGEKTKKMATTSRPSSPLPPEEETAAETTTSEEEEQQQMERFYALVANVRALRAMFKEAALPSCREDDVSGGGGGEQRQKRPRAAPWRPAFEMAVFECGGGGGTTTDDIEAATTKGQDGNCKKGKRSEANAAAEEDKGEVIEGKPVAIAIVADGPGKSTTMPDSN
Protein: Ethanolamine ammonia-lyase small subunit (EAL small subunit) (EC 4.3.1.7) (Ethanolamine ammonia-lyase beta subunit) (Ethanolamine ammonia-lyase light chain) (Ethanolamine deaminase small subunit) (P19636)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Ethanolamine ammonia-lyase (EAL) allows bacteria to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12. It is spontaneously inactivated by its substrate and reactivated by EutA. Directly targeted to the BMC. May play a role in bacterial microcompartment (BMC) assembly or maintenance (By similarity).
Subcellular location: Bacterial microcompartment {ECO:0000255|HAMAP-Rule:MF_00601}.
Interaction partners:
- Bacterial microcompartment shell protein EutL
- Ethanolamine ammonia-lyase large subunit
- Ethanolamine ammonia-lyase reactivase EutA
- Probable ethanolamine permease EutH
- Acetate kinase EutQ
- Bacterial microcompartment shell protein EutK
- Corrinoid adenosyltransferase EutT
- Bacterial microcompartment shell protein EutS
- Probable acetate kinase EutP
- HTH-type DNA-binding transcriptional activator EutR
Sequence:
MDQKQIEEIVRSVMASMGQAAPAPSEAKCATTNCAAPVTSESCALDLGSAEAKAWIGVENPHRADVLTELRRSTVARVCTGRAGPRPRTQALLRFLADHSRSKDTVLKEVPEEWVKAQGLLEVRSEISDKNLYLTRPDMGRRLCAEAVEALKAQCVANPDVQVVISDGLSTDAITVNYEEILPPLMAGLKQAGLKVGTPFFVRYGRVKIEDQIGEILGAKVVILLVGERPGLGQSESLSCYAVYSPRMATTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR
Protein: Dachshund homolog 2 (Dach2) (Q925Q8)
Organism: Mus musculus (Mouse)
Function: Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator for SIX1 and SIX6. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. Is recruited with SIX6 to the p27Kip1 promoter in embryonal retina. SIX6 corepression seems also to involve NCOR1, TBL1, HDAC1 and HDAC3. May be involved together with PAX3, SIX1, and EYA2 in regulation of myogenesis. In the developing somite, expression of DACH2 and PAX3 is regulated by the overlying ectoderm, and DACH2 and PAX3 positively regulate each other's expression. Probably binds to DNA via its DACHbox-N domain.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein phosphatase EYA2
- X-linked interleukin-1 receptor accessory protein-like 2
Sequence:
MAVSAPPVISATSSSAGVPGGLFRAEPLYSSPGEPPRLTPNMINSFMANNHNGSVLGGGIGGGSGGSSNTNTNECRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVGGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCKLITRKDFETLFTDCTNARRKRQMTRKQAVNSSRPGRPPKRSLGVLQDNARLLPHAVPGLLSPGLITPTGITAAAMAEAMKLQKMKLMAMNTLQGNGSQNGTESEPDDLNSTTGGSESSWDKDKIQSPLAASGPQHGIAHAALAGQPGLGGAPTLNPLQQNHLLSNRLDLPFMMMPHPLLPVSLPPASVAMAMNQMNHLNTIANMAAAAQIHSPLSRAGASVIKERIPESPSPAPSLEESHRPGSQTSSHPSSSVSSSPSQMDHHSERMVMMPNNREELIVDQDNGQSIKKFQRDNKEEVPAQIPVMKSPLDKIQLAPGQALHPGFPGPFIFADSLSSVETLLTNIQGLLKVALDNARIQEKQIQQEKKELRIELFREREIRENLERQLAVELQSRSTMQKRLKKEKKAKRKLQEALEFESKRREQVEQALKQATSGDSGLRMLKDSGIPDIEIENSGTPHDSAAMQGGNYYCLAMAQQLCSA
Protein: Aquaporin TIP4-1 (Epsilon-tonoplast intrinsic protein) (Epsilon-TIP) (Tonoplast intrinsic protein 4-1) (AtTIP4;1) (O82316)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. Transports urea in yeast cells in a pH-independent manner.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14576283}; Multi-pass membrane protein {ECO:0000269|PubMed:14576283}. Note=Tonoplast.
Interaction partners:
- TIP41-like protein
- Vacuolar fusion protein MON1 homolog
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Thioredoxin-like protein YLS8
- AT4g33380/F17M5_140
- AP-2 complex subunit mu
- F-box protein SKIP16
- Actin-2
Sequence:
MKKIELGHHSEAAKPDCIKALIVEFITTFLFVFAGVGSAMATDSLVGNTLVGLFAVAVAHAFVVAVMISAGHISGGHLNPAVTLGLLLGGHISVFRAFLYWIDQLLASSAACFLLSYLTGGMGTPVHTLASGVSYTQGIIWEIILTFSLLFTVYATIVDPKKGSLDGFGPLLTGFVVGANILAGGAFSGASMNPARSFGPALVSGNWTDHWVYWVGPLIGGGLAGFIYENVLIDRPHVPVADDEQPLLN
Protein: LD04844p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Uncharacterized protein, isoform C) (Uncharacterized protein, isoform D) (Q9VYX8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- GH18858p
- FI16602p1
- Annexin B9
Sequence:
MSHSVTITRTTTSTTNTSYIVLNTGYLKTFPGILKLFELIIGASIVGILAFNYQDYHRYFYGQQDLFHYLMAVTFMIGTFCLLLACLTSLSTGGIIAKTIYELIYHSVAAILILVSSTILLLKLRDVKHDAYMAAGVLGLVNAVLYFISAFLAHRSYRGI
Protein: BZIP domain-containing protein (A7S1A3)
Organism: Nematostella vectensis (Starlet sea anemone)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- BZIP domain-containing protein
- mitogen-activated protein kinase
- Uncharacterized protein
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase 7
- Mitogen-activated protein kinase
- BZIP domain-containing protein
- BZIP domain-containing protein
Sequence:
MTDDKPFECTTPGCGQRFANNDHLESHKQKHQLSLKLGNLKPADLAHLADQTPTPTRFLKNLEEEGLFEDLENPFDQRLKETLRQQQNNNSNGMNIVSQAMTEAVEMVTSEHNGLTTSPTMISHNNQQNDSRRGIKRPRRSQEELDPDERRRKFLERNRAAATRCREKRKIWVQQLEKKADDLSNTNTQLQNEISLLRTEVAQLKSLLLAHKDCPVTIAQQK
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (A0A2R8Y7Y7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XLVRQHKAAQVAKEKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
Protein: Cuticle collagen rol-6 (Protein roller-6) (P20784)
Organism: Caenorhabditis elegans
Function: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. Involved in body morphogenesis.
Interaction partners:
- Cuticle collagen sqt-1
- Protein unc-119
- Myosin-4
- Forkhead box protein O
- Myosin-3
- Protein dumpy-20
- Cuticle collagen 6
- Insulin-like receptor
- Myosin-2
- Protein lgg-1
Sequence:
MTLTTATSGAIVFSGATLLVSLFAAASLYSQVSNIWNELDAEIANFRSLTEDMWVDMVKLGAGTASNRVRRQQYGGYGATGVQPPAPTPNPYGGYGASQPAPPEKFPDGIPNGGNQPKFPGGGFPDGPFPNGGGPRGGNQCQCTVENSCPPGPAGPEGEEGPDGHDGQDGVPGFDGKDAEDVQNTPPTGCFTCPQGPLGPQGPNGAPGLRGMRGARGQPGRPGRDGNPGMPGDCGPPGAPGSDGKPGSPGGKGDDGERPLGRPGPRGPPGEAGPEGPQGPTGRDAYPGQSGPQGEPGLQGYGGAAGEDGPEGPPGAPGLPGKDAEYCKCPGREGDAGRSARRHRKFQL
Protein: Large ribosomal subunit protein uL13 (60S ribosomal protein L13a) (Q5RK10)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAEGQVLVLDGRGHLLGRLAAIVAKQVLLGRKVVVVRCEGINISGNFYRNKLKYLAFLRKRMNTNPSRGPYHFRAPSRIFWRTVRGMLPHKTKRGQAALERLKVLDGIPPPYDKKKRMVVPAALKVVRLKPTRKFAYLGRLAHEVGWKYQAVTATLEEKRKEKAKIHYRKKKQLLRLRKQAEKNVEKKICKFTEVLKTNGLLV
Protein: Decaheme cytochrome c (B8CRH3)
Organism: Shewanella piezotolerans (strain WP3 / JCM 13877)
Interaction partners:
- Outer membrane protein MtrB
- Outer membrane protein
- Serine/threonine protein kinase
- Formate-dependent nitrite reductase
- Cytochrome c, putative
- EcxA zinc-binding domain-containing protein
- Decaheme cytochrome c MtrA
- Outer membrane protein, putative
- Serine protease, subtilase family
- Glucose/galactose transporter
Sequence:
MMKFFNLSATSKALLTAGVLSLAVSGCSGDDGTNGEDGKPGPVGTPIGEVSNVIADITSASVSEDGFLTVNFNLSDANGAAVFGMQQTDIGALSFGRVGAATEITPPAEGEEPSTRQIWLSYFNKDKGDGHFTGSSYFNGASSECTDCFTDNEDGSYSITIDKAIDTLGKYDYKADATSGIYMAVKAKNNAETTMVDNAFYYWQPAADIAADKPLQILANENCQTCHRPGQDGALAMHGSKHQTEEACSFCHTDYNSYMKEDADGNAYEYDGSIKAMAHNIHNTSAFQDEEKDEDGNVIQAAGIYPQLASNCQTCHAPDDSLNLTDAWKADQDAATCTSCHTTAPGWHGEEGGDYDEAHQVCSNCHSADGYARGAERAHYTENTNAQAAETKVTFNSMTYSAATETIVANMTVTHGDDTITLAQIDPSPYVWGGYTSAIVFNGVVDDDFVVNYQKVGFDKFAKGANGSIDVTFTDAEFKVAEVMGTEGVKAAFSSQLHVCFSSKGVVEDCKVEEDGTVSNSGPYAVSDTAYFNVDGTVVTESPRVQHAEMVACQQCHTTDIKHRFSNDMDGCASCHNGTRDKKGTGSSNLAYIVHSKHYLSDSSGDLFFKKTECQACHGEDGYSLSKIAGDAAPVAFGKENLGKDADGKDIWGEQLVVSPQTAACVSCHQAPYGLNDATASHIQGMGGILVQEGAELTTLGVPASDYELLNVQETCSTCHKDDAILEAHSNWGSSY
Protein: Formate dehydrogenase, cytochrome b556(fdo) subunit (Aerobic formate dehydrogenase cytochrome b556 subunit) (FDH-Z subunit gamma) (Formate dehydrogenase-O subunit gamma) (P0AEL0)
Organism: Escherichia coli (strain K12)
Function: Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Formate dehydrogenase-O major subunit
- Formate dehydrogenase-O iron-sulfur subunit
- Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit
- Formate dehydrogenase, nitrate-inducible, major subunit
- Protein FdhE
- Formate dehydrogenase, nitrate-inducible, cytochrome b556
- Formate dehydrogenase H
- Sulfur carrier protein FdhD
- S-formylglutathione hydrolase YeiG
- S-formylglutathione hydrolase FrmB
Sequence:
MKRRDTIVRYTAPERINHWITAFCFILAAVSGLGFLFPSFNWLMQIMGTPQLARILHPFVGVVMFASFIIMFFRYWHHNLINRDDIFWAKNIRKIVVNEEVGDTGRYNFGQKCVFWAAIIFLVLLLVSGVIIWRPYFAPAFSIPVIRFALMLHSFAAVALIVVIMVHIYAALWVKGTITAMVEGWVTSAWAKKHHPRWYREVRKTTEKKAE
Protein: Uncharacterized protein (Q8IFH6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLWRKQCACRTPEHPTKGYRSVNDSLQLMEIRRTSTPLNYKLLRAYQFLPYEVPFPPHTFASQQWREGENVEAHYALYQTCLCMYLVSSDMSLTVTNMLPALGIHEHDVHKVSRTLCAARCST
Protein: Importin subunit alpha-1 (Cell untimely torn protein 15) (Karyopherin subunit alpha-1) (Serine-rich RNA polymerase I suppressor protein) (O14063)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs. Has an essential role in mitotic chromosome condensation. Involved in nuclear protein import. Required for efficient nuclear import of both an SV40 nuclear localization signal-containing reporter protein and the pap1 component of the stress response MAP kinase pathway. Required for proper mitotic progression.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15937127, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9740803}.
Interaction partners:
- Importin subunit beta-1
- Importin-alpha re-exporter
- Importin subunit alpha-2
- Protein pim1
- Nucleoporin nup124
- Importin subunit beta-3
- Importin subunit beta-2
- GTP-binding nuclear protein spi1
- Ubiquitin-like-specific protease 1
- Nuclear cap-binding protein subunit 2
Sequence:
MSASSRFIPEHRRQNYKGKGTFQADELRRRRETQQIEIRKQKREENLNKRRNLVDVQEPAEETIPLEQDKENDLELELQLPDLLKALYSDDIEAQIQATAKFRKALSKETNPPIQKVIDAGVVPRFVEFLSHENNLLKFEASWALTNVASGSSNQTHVVVEANAVPVFVSLLSSSEQDVREQAVWALGNIAGDSPMCRDHVLQCGVLEPLLNIIESNRRLSMLRNSTWTLSNMCRGKNPQPDWNSISQVIPVLSKLIYTLDEDVLVDALWAISYLSDGANEKIQAIIDAGIPRRLVELLMHPSAQVQTPALRSVGNIVTGDDVQTQVIINCGALSALLSLLSSPRDGVRKEACWTISNITAGNSSQIQYVIEANIIPPLIHLLTTADFKIQKEACWAISNATSGGARRPDQIRYLVEQGAIKPLCNLLACQDNKIIQVALDGIENILRVGELDRANNPDKINLYAVYVEDAGGMDLIHECQNSSNSEIYQKAYNIIEKFFGEEDEIEELEPETVGDTFTFGTTQEPAGDFQFSATNAEDMAM
Protein: SUR7 family protein pun1 (O13729)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Contributes to the wild-type cellular response to nitrogen stress through signaling pathways that regulate the expression of genes involved in amino acid biosynthesis. Required for wild-type filamentous growth, cell growth, and cell-cell adhesion (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Cell membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Meiotically up-regulated gene 33 protein
- Probable glycosidase C21B10.07
- Uncharacterized protein C19C7.05
- Non-classical export protein 2 homolog
- Probable sphingolipid long chain base-responsive protein pil1
- Putative mannan endo-1,6-alpha-mannosidase C1198.07c
Sequence:
MGMGFNPIKALFTGIGTVCVGVGALLSILCIINQTQHNIAFQNIYFIQLNTTSIFSVANQTAVVNNTSNLLNELTGTLVDTLETYIDQGATDLIEQVEQEMKDVSELPDWYSIGLWNYCQGNSSDYTNPTYCSTPSPSYYFNPLTMLETSINNATGSQINITLPSEVDLGLKVLKGACYAMRAMYILGFIFFALTIVSIVISCLPFFGPLFLNVFSFFATIFTFIAAVIAVATYRIAISELEKNIEILNIPIVLGKKIYAYSFLSAAAGLAACILYFIGNLTSGYSPL
Protein: Major capsid protein VP5 (A0A346LU63)
Organism: Sulfolobus filamentous virus 1 (SFV1) (Sulfolobus virus SFV-1)
Function: Self-assembles to form a helical, filamentous nucleocapsid (Probable). Together with capsid protein 1, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).
Subcellular location: Virion {ECO:0000269|PubMed:32759221}.
Interaction partners:
Sequence:
MARKRTSKNDPLRMYLNYVRKLQTMGDAYDESAKYRIANFENGFKSLHMVENEFKQYLANVIDEAIKSGASPQDLPYVNEIKLALMKIFTSWLKYSNEKLGANEIAINVAGTATMTLTENLYGTRVSCEEAVSLINSIFAVWVGVEPFEAEEREGACLVTPRSPLPPVPISSPTGFSAPIQEVLQAKSPEEIIGVKGGA
Protein: Metalloprotease TIKI1 (EC 3.4.-.-) (TRAB domain-containing protein 2A) (F6PTN1)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway: expressed in the Spemann-Mangold organizer and is required for anterior-neural patterning in head formation in embryos. Acts by mediating the cleavage of the N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave wnt8.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MVIIWNIFLPAFLLVLAKASLRSSRDSANCKLNKKQSQLNSFLWTIKRDPPSYFFGTIHVPYTRVWDFIPENSKTAFQQSNIVYFELDLTDPYTISALTSCQMLPQGENLQNVLPRDIYRRLKRHLEYVKLMMPSWMTPDQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTEVDIKSRGVPVLDLYLAQEAERLKKRTGAVEQVEEQCHPLNGLNLSQVIFALNQTLLQQENLRAGSVQVPYSTEDLIKHYNCGDLNSIIFNHDSSQVPNFINSTLPPQERITAQEIDNYFRQELIYKRNERMGKRVKDLLEQFPEKSFFFAFGAGHFLGNNTVIDVLKRYGYDVLHTPAGRSIINNGKGKKNLLPSKFSSSSLPVGLSAPPCTVTSRIKQSINSHKDQESLPDILLDDDIDQLDKDERKYKKRKQRKEKHRHFSDLWVRIQESSTDTTPQIRIINGYITVEPHPREHGKDKYIKAAQSVSFSLSIPSAFLLLAWCFQQVAVLQ
Protein: Protein pob1 (BOI protein homolog) (O74653)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in cell elongation and separation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10436025}. Membrane {ECO:0000269|PubMed:10436025}; Peripheral membrane protein {ECO:0000269|PubMed:10436025}. Note=Membrane-associated at the cell tips during interphase.
Interaction partners:
- mRNA export factor elf1
- Elongation factor 3
- Cell division control protein 42 homolog
- 26S proteasome regulatory subunit rpn10
- Formin-3
- Polyubiquitin
- 26S proteasome regulatory subunit rpn11
- UV excision repair protein rhp23
- 26S proteasome regulatory subunit 7 homolog
- Ubiquitin conjugation factor E4
Sequence:
MASQRFVIALHSFPGKSSDELPLVEGRKYLLIKMDEEFGDGWWEGEDEQGNRGIFPASHVELISDERSDSSDSRRGKEDFSISTAEVTRSSLSSSRSTSSRSDKDSEKLYSNNSLSSSHSSILNGPLDSLSKPSVPSNFNSMFPSSKQEGPSPLLDNQPSSDLSNFNTIDADYNNASASTSAPATSASLKKVLSAEDSVRETITDIETALQNMSTSASRTPNDSSPLPYIENRPASSLAVSEKIQNVPNWSTEEVVEWLMNAGLGSVAPNFAENEITGEILLGLDSNVLKELNITSFGKRFEVLRKIQQLKDSYEQSLYEEYPQFAEPISVSQSSDSSSSIPKKSNDEAGGSPSKSSPTRPGFNDYVNRPTSVMPSLSNMIVSPDLDSSPSTDWNQYVIPPLATPSSRNSKSTQSAVPENVSRFDSNEPSATSPILKRSSPTDSISQNSGLPSRLTEPISSPSTSSIDVDKEGTSFPGLPYHSSKGNLYAPQPSSNVPTKFTGGASESSSVPPRPIPSAMKGKAPASAISIEALEELDPPKITTIDGESPSSISSRLPSSNLEQGSSSSVTKSPESMPDPSAKASSPVTSKGVSINEKSAVNNYATPLSKPQPKDTKGSKLGNTFVAPSPAASLPASPPVGTELKTRPTLRSVASSPLNKEPIGKRKSKRDIFGRQKVLPTGISEGLSNIPAKEAIKTADCHGWMRKRSDRYGVWKSRYFVLKGTRLSYYHSLNDASEKGLIDMTSHRVTKTDDIVLSGGKTAIKLIPPAPGAAKAAVMFTPPKVHYFTCENNEELHRWSSAFLKATVERDMSVPVLTTSRMPTISLSKAKELRTRPPSLLIDDENEANLTSSIGLKKNAKQKNKKSSKQK
Protein: Microtubule-associated tumor suppressor 1 homolog (F-box protein 27) (Inner centromere KinI stimulator) (Mitochondrial tumor suppressor 1 homolog) (Q7SZL5)
Organism: Xenopus laevis (African clawed frog)
Function: Regulates microtubule dynamics during mitosis by stimulating kif2c. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12919681}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12919681}. Chromosome {ECO:0000269|PubMed:12919681}. Midbody {ECO:0000269|PubMed:12919681}. Note=Chromosomal until metaphase. Located at the midbody during telophase.
Interaction partners:
Sequence:
MSVQTATTENRFQSTLDDNNGNNSESKNIARCPKYEWNANVNDQGPGVIDHSILDQQSDNEINKHYLLQSPNALELDSTLDYIGNAAGHCDTFNLKADKGCKTVNSSLLHENPGEEDETVDYINNELCNKMQDTLCPPSIPIQTSASDEIHKGLGAITDRGSAYNKIAEQSLCVQESTDYLCKMEPKWTVQAFFGDADKLCRNEANNLVDISTTDHKYDHNSSFGIFTLSLDFSDEKCMREDSLVLSGSEKPLSASILEGSALPNSSIDVFTGSVKKTDNIDGFCQGAELSLRDLDYLEVPHQKDSTETPQSKLSLTSEHSVFTSETSEVMLEVDARRVMDKTVESHLPNLRLSSNVGKEDSAPGASLEEFVSGSVPAVAPEELASNLIKDKNTIKNKESHGEAHSLESPARPDSSSSELKDLLSNLSGQNCEDTFIISSPNSGIGSKAFTSTPLPESKNMTFSVPVLESITENNELQQNLDAIKYDLEGLRHSSDSNIVTKPTNKKPAVGSVVGKAKKNEVISFPKPSFKNVKAKVLTRPSLQAKDSNPYASKTSPRSPPSLSNASSPAQSPRPLSSAVKTVQKRSVINQDMKTEAAIAKSQKQPITKQLFPTHSAHVPTHSKHALGKVPRAAALKHTQNETERASSSNSTRSSGSAAAALTCTAGSRVTENKSEKAKTSAKPSAPNVRLMGPNKIEQKGIIQPHFDKAQSLKEAKEGTVSADMDILANIVPLPTKLAIPSSRNLHKELILGIKNVASQPAKGRVQTTVQRRGSLGKNILTIRVSSPPREKPQVTVEGGLNSPKGRPISVKASAANGTGSLPRTRLPCRGTTLQRTASVSSVCSTQSELSNLSTRSTTTTSSIKTEDIPTAKCIRPNSASGALTAKSSIPRGRSQSLKVTQTVTGTKKSPSIIPTLPRSSGPALSLTKKLEARSLQNVEKNKQKTSPRGPVTQAQTPPVDPKSIELTKCKAACEQQRGVIENLKNLLSSSNQRFEALTVVVQQLINQREETLKKRKALSQELLNLRGDLVCASSTCERLEKEKNELLKAYEGILQKVKEEHHAELSDLEEKLKQFYTGECEKLQSIFIEEAEKYKNELQEKVDDLNTTHEAYRLQAETSQIETIHTLKEDYEKSLTELKDAKDKENKILEDSFKEKQAEVEKKILELKDVNESLKEKLKYEEEQRKLTKEKSVQKNPQVMYLEQELESLKAVLEIKNEKLHQQDKKLMQVEKLVETNTTLVERLNKCQQENEDLKARMVNHVALSRQLSTEQEVLQRSLEKESKANKRLSMENEELLWKLHNGDLCSPKKLSPSSPGIPFHPSRNSGSFSSPTVSPR