wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 1A, X-chromosomal (eIF-1A X isoform) (eIF1A X isoform) (Eukaryotic translation initiation factor 4C) (eIF-4C) (P47813)
Organism: Homo sapiens (Human)
Function: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Eukaryotic translation initiation factor 1
- Small ribosomal subunit protein uS19
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS17
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2 subunit 2
- Small ribosomal subunit protein uS10
Sequence:
MPKNKGKGGKNRRRGKNENESEKRELVFKEDGQEYAQVIKMLGNGRLEAMCFDGVKRLCHIRGKLRKKVWINTSDIILVGLRDYQDNKADVILKYNADEARSLKAYGELPEHAKINETDTFGPGDDDEIQFDDIGDDDEDIDDI
Protein: separase (EC 3.4.22.49) (Q4GYR1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Serine/threonine-protein kinase PLK
- Tyrosine phosphatase, putative
- Ubiquitin-conjugating enzyme E2, putative
- Double-strand-break repair protein rad21 homolog, putative
- Sister chromatid cohesion protein
- RNA-binding protein
- Serine/threonine-protein kinase, putative
- Serine/threonine-protein kinase PLK
- Cdc23 domain-containing protein
- Cell division cycle protein 16, putative
Sequence:
MRRTQVRNSRLHDIKDSPSNEAEVQAVLAAAKASEGDAWNAVRLLAGCARCTLQAGRGHLALPLIVASFELSPEPFRQLVGLQQLTVDGSQQQILQEIAENDAFTKNERGANGIMSTVLIVWHGVVVSVAQNGSCPKDFLRFSHCIAHLLSLLPGADGVVHEDLSACWLYNIIMFAHKCKCMKAVAHYLLEGMLADVSELPEDLRDASTLQSLPFAFRKWGAAKAFVHAGVRKHAVATMFKRLCLALYTEGCDDLRTVQREIDSRALAVTNALQQTFGSETSHYMVDFHRPLRMEAQHIALLCQHAMDEDQLCTPRGQFGCIRLACLLKRAANKIMAPTMNECKLVSLSSVVALALRHQYIDIAAEILQTGVETVDPSDESLLLWGKDLELVLAQNLSAHLPAAAQCPVKPVERARDEASSGVDDKVGVGTVGAPEPTQLLHEVVQGSLSDAEAVRVLALADDLTQLLPIGLTLLRGRGTLQQRLLADKIAVPFVIGALARLVQLLVNEGDMPLVRCFLPFIAHLCVGVPSRAHLLFTLQAIAAFAKGFPGDTGEWASIASALSQFSPLRSIDAAPSYCHTKAITTGRTFASRRRVFDALRVCRKTPKTMMHSYCQVQVSLLGEGGGVRLLRTTHVRTTADTRWEKVLRIEYLLLQLVEEMKIIERRNRDHLRSTDQGESPLCEDLPVSSLRSDISVGPVCCSVGGAQDARKAREEWWNERRALDRSIGAVVQSMQSPEGFGCWRAALCGELPDSCQVAVWDATKELLSGLGLPAQHEGDVSLVLAALPFVGDRHPEDGDLLFNPSHVGPTNPCGCCDETLRRLSTALEQELITHLDAKLVNEPTACRKACLHVLTAMHAVISEKKCNQPVDHGGEPEKRLTDGCYHVNLYEIPRTPVYLVLDNELHCLPFEGIDVLRHGSVSRVPTVSFVSTFTSTLGQRNDSCHSSGDYIEKGGKNAAGCAGTVCCVIDPAGVMSKTLRRLLPLCSRKGWVVKSHNSPPSARLLREMYRAGVRLYVYVGHGKGEQIIQRGELYERVPDPANFPSVFLMGCSSAYMDGGLTYDCYGMPYAFLHAGAPLFVGCLWHVTDGEIDRLTKRLLSFVSYGGGSGDDFGVCRTMAAGEALRLARKSCKLPYLTGCATVLYGMNLPLGGTPGGAM
Protein: Beta-monoglucosyldiacylglycerol synthase (Beta-MGS) (MGlcDAG synthase) (EC 2.4.1.336) (UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase) (P74165)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Glucosyltransferase involved in the biosynthesis of the non-bilayer-forming membrane lipid beta-monoglucosyldiacylglycerol which contributes to regulate the properties and stability of the membrane. Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding beta-glucosyl-DAG (1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor. Two types of DAG (dipalmitoyl-DAG (DPDAG) and 1-oleoyl-2-palmitoyl-DAG (OPDAG)) can be used as sugar acceptors, but OPDAG is preferred.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Monoglucosyldiacylglycerol epimerase
- Diacylglycerol kinase
- Sll1969 protein
- Uncharacterized protein sll0036
- Slr1508 protein
Sequence:
MPQFPWKDNDAELSPLEAFLAEWDDPEAEEEDFRNDFFRGSEGRRKKAAVMLMAIWTVVITLHYWVWGSWLVWALTGALSLQALRLMKATPEEAPPLLTGDASTVPYPQVCLMVAAKNEEAVIGKIVQQLCSLDYPGDRHEVWIVDDNSTDRTPAILDQLRQQYPQLKVVRRGAGASGGKSGALNEVLAQTQGDIVGVFDADANVPKDLLRRVVPYFASPTFGALQVRKAIANEAVNFWTRGQGAEMALDAYFQQQRIVTGGIGELRGNGQFVARQALDAVGGWNEQTITDDLDLTIRLHLHQWKVGILVNPPVEEEGVTTAIALWHQRNRWAEGGYQRYLDYWRWICTQPMGWKKKLDLFSFLLMQYLLPTAAVPDLLMALWQRRFPLLTPLSYLAIGFSCWGMYYGLKRLTPSEGESPWQQMPALLARTIGGTIYMFHWLIIMPAVTARMAFRPKRLKWVKTVHGAATEDALELKQS
Protein: Rifin (Q8IM85)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFALPLNILVYNQRNYYITPRHTKTTRSLCECKLYSPANYDSDPQMKEVMENYNRQTSDRFKEYDERMKTTRQKCREQCDKEIQKIILKDKLEKQMEQQLTKLETKITTEDIPTCVCEKSLADKVEKGCLKCGYGLGTVAPTVGLIGSVAVNVWKTTEIAAAIAAAEKTGAAQGAAAGLKAGVDAVITGLKERGVGLLCPKLLESIGDTIHYTDDGQIAKIILENLSTNCGVGNSLDKGTCMKIRIKLGMILPDDKIAPPDNIHIRQMMKEIVYEAKQASDVVAKNTADKVTKAAIKTSTEAIDAATYNWYTTISYSITAILIIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Thioredoxin reductase-like selenoprotein T (SelT) (EC 1.8.1.9) (P62341)
Organism: Homo sapiens (Human)
Function: Selenoprotein with thioredoxin reductase-like oxidoreductase activity (By similarity). Protects dopaminergic neurons against oxidative stress and cell death. Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion (By similarity). Plays a role in fibroblast anchorage and redox regulation (By similarity). In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation (By similarity). In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-induced insulin secretion (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q1H5H1}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Selenoprotein W
- Selenoprotein F
- Selenoprotein K
- Selenoprotein S
- Protein adenylyltransferase SelO, mitochondrial
- Selenoprotein N
- Selenoprotein M
- Selenoprotein H
- Migration and invasion enhancer 1
- Selenide, water dikinase 2
Sequence:
MRLLLLLLVAASAMVRSEASANLGGVPSKRLKMQYATGPLLKFQICVSUGYRRVFEEYMRVISQRYPDIRIEGENYLPQPIYRHIASFLSVFKLVLIGLIIVGKDPFAFFGMQAPSIWQWGQENKVYACMMVFFLSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDNEMKLNVHMDSIPHHRS
Protein: Probable heat shock protein transcriptional repressor HspR (MerR family) (O06302)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Chaperone protein DnaJ 1
- Chaperone protein DnaK
- Protein GrpE
- Heat-inducible transcription repressor HrcA
- Chaperone protein ClpB
- Chaperone protein DnaJ 2
- RNA polymerase sigma factor SigB
- RNA polymerase sigma factor SigA
Sequence:
MAKNPKDGESRTFLISVAAELAGMHAQTLRTYDRLGLVSPRRTSGGGRRYSLHDVELLRQVQHLSQDEGVNLAGIKRIIELTSQVEALQSRLQEMAEELAVLRANQRREVAVVPKSTALVVWKPRR
Protein: Nuclear pore complex protein Nup133 (A0A1L8H1I9)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein SEC13 homolog
- Nucleoporin Nup37
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein
- Nuclear pore complex protein Nup155
- WD_REPEATS_REGION domain-containing protein.
- Nuclear pore complex protein Nup93
- Uncharacterized protein
- Uncharacterized protein.
- Uncharacterized protein
Sequence:
MFPSPRAQGMGSARRPFNSRLTGGRKALGPGVTASSSPSALYSPVGRRVSASGARSTPSRVYLHPAASETVNYNVQLFGSSLPVKVMEALSNASADEPMAACIHEGGWAWLACNDRLIIWKISHSSSAKLMVCKELPLPLSDSEWSADLVDICAQTGDPAAAQSVALMAATPEGSSRYWPNILHEGTYIESYTEFGSSLCAFVTAVKGNSFILSSEKNQLVRLTPDASGKMNQRVLPQGQGMLSGIGRRVSTLFGILSPAVESTLCSVLWDKGDCFYTLTDSSINKWDLDDTSESQVLNWDMSRVLREYISDAIWGSESDYDDIKAGININYLSLNQNCDGLVILSAAWHPGDNPCQIYYTLVTVKDEGYNISDEITVEVTQFNPVFQARGMQLCQLVVPNFSSQACYLYTQEMIFACSTGTGRSTLPQEKIPFEAQGDNIVGAGSCEGWPVFFIRKSGMLTVVARETASVLPEHMEESLSSVSKSSRQAVVKDSRPDQIAHDDKTKHLKAAFLRYCRKDILGAQSMVDSLFSDSDMEPDDELDLAVNQISVDLIDDYPASDPRWAESVPEEAAGFSNTSLILLHQLEDKMKAHSFFVDFLHQVGLFSRLSTCQTKGMLVATRLLLSEHAEKLSAAIVLKNHHAKLPVLVNSAIQLALDKRMCTVPQNLTAADVYFREVSQMEIIFECLVDKEEADLESTSIDSVEWANIVVNVNTILKDMLHVACQYRQSKNSLYKNESGIQEPEHVPWTASSGTAGIRSVVTRQHGIILKVYPQADSGLRTILIEQLAALLNYLLDDYVTQLKSIDKLANEERYNILEMEYAQKRSELLSPLLILGQYAWASNLAEKYCDFDILVQICEMTDNQSRLQRYMTLFAEQNFSDFLFRWYLEKGKRGKLLSQPASQHGQLAAFLQAHDHLSWLHELNSQEFEKAHRTLQTLANMETRYFCKKKTLLGLSKLAALASDFQEDVLQEKVEEIAEQEHFLLHQETLPKKLLEEKQLDLNAMPVLAPFQLIQLYVCEENKRANENDFMKALDLLEYIGDDSEVDVEELKLEILCKAIKRDEWSATDGKDDPIEATKDSIFVKVLQNLLNKGIELKGYLPKAETLLQSEELNSLKTNSYFEFSLKANYECYMKMQS
Protein: ATP-binding cassette sub-family F member 2 (Q99LE6)
Organism: Mus musculus (Mouse)
Interaction partners:
- ATP-binding cassette sub-family E member 1
- Stress-induced-phosphoprotein 1
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL5
Sequence:
MPSDLAKKKAAKKKEAAKARQRPRKGHEENGDAVTEPQVAEEKIEEANGRETTGDGEVDLLTKELEDFEMKKAAARAVTGVLASHPNSTDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSEKTPLQCVMEVDTERAMLEREAERLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQDQIAHMKNYIARFGHGSAKLARQAQSKEKTLQKMMASGLTERVVSDKTLSFYFPPCGKIPPPVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEHLKSKLVDEEPQLTKRTHNV
Protein: Galactocerebrosidase (GALCERase) (EC 3.2.1.46) (Galactocerebroside beta-galactosidase) (Galactosylceramidase) (Galactosylceramide beta-galactosidase) (P54818)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes the galactose ester bonds of glycolipids such as galactosylceramide and galactosylsphingosine. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon (By similarity).
Subcellular location: Lysosome {ECO:0000250}.
Interaction partners:
- Acid ceramidase
- Arylsulfatase A
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Lysosomal acid glucosylceramidase
- Prosaposin
- Galactosylceramide sulfotransferase
- Sphingomyelin phosphodiesterase
- Alpha-galactosidase A
- Non-lysosomal glucosylceramidase
- Ceramide glucosyltransferase
Sequence:
MANSQPKASQQRQAKVMTAAAGSASRVAVPLLLCALLVPGGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSEILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYELDENYFRGYEWWLMKEAKKRNPDIILMGLPWSFPGWLGKGFSWPYVNLQLTAYYVVRWILGAKHYHDLDIDYIGIWNERPFDANYIKELRKMLDYQGLQRVRIIASDNLWEPISSSLLLDQELWKVVDVIGAHYPGTYTVWNAKMSGKKLWSSEDFSTINSNVGAGCWSRILNQNYINGNMTSTIAWNLVASYYEELPYGRSGLMTAQEPWSGHYVVASPIWVSAHTTQFTQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHQHSMCIRPYLPYYNVSHQLATFTLKGSLREIQELQVWYTKLGTPQQRLHFKQLDTLWLLDGSGSFTLELEEDEIFTLTTLTTGRKGSYPPPPSSKPFPTNYKDDFNVEYPLFSEAPNFADQTGVFEYYMNNEDREHRFTLRQVLNQRPITWAADASSTISVIGDHHWTNMTVQCDVYIETPRSGGVFIAGRVNKGGILIRSATGVFFWIFANGSYRVTADLGGWITYASGHADVTAKRWYTLTLGIKGYFAFGMLNGTILWKNVRVKYPGHGWAAIGTHTFEFAQFDNFRVEAAR
Protein: Uncharacterized protein (Q57ZN5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKKAWAQLERVLQPSSSRVNRSLITQQLEALYALPINCEAACRWEDAQRLFLRCNGHRPYYAGIMDQSTDNRLAVASFEENMLALQQRGLVCTTVGDKAPPCVGGGQTSRGLCRRSSIVCVNVGSCADLDLNMHEDCDETLLTLLHGVVVPYLHFRIVYGAGVSPPLVPRAPGPAICGASHDLSLQNELHIDSCVALLHPRGLCSSNCNNKAYRTAATLVRGAVSLATSDTLLHQRQDGCFTLHPDAMKLGSPRLFALQLWWNKEVGPLIQRGVEQSVKTDEVLSGAWIEVARKRVEELVERGGDDLPQPLRNMTRDDVAAFAADATLCWTLSAFDCNYKRLGPAQPACRLQFSEEARLSMALELMQTVKASLVKQPTGIPISELSATVCWPAASAWIGEKSLTEALTQFPAHFNVVNVEGKLVVMHGHLTGPSDNVTAEEVSEWLAAGHSEGLQKPCVAASPSDLTFHRETDLVVRAVAFLRKRHFGNVPVTYGELCGALLPKNNGKNDGDSDTLLNVLLRYDVLAADTAKGDSSINIQCGLRDGDAVRLSVREDRALRAFEAFRTTSRSAFQLYTEAIEPFFTCCRGAMRENGSCVVPLTLLERWLQVERLSLQSKELLDILRSAEGPYRIDEELCNVVLTNHTAKGEVLTPAFSLPATPPPPPPPAVSSRLTFEAQISRVLKTQRPDRLLHFVQTILHAVFDLILPHVSAPSGVPVRRLMRRIRWGSFVVTLGSLTSFVEAFDGLFFEVLSNASSHGEEKRDDVDLIVSAYKGPVSPWLLYARLIVRLFPADVDIPLGLIAEALSWSSRFAPMFGDLPSLLRRVGRQCRNGQLLAKVEMVRPVCDQDDACLWELLAKIRREAHLHHLERGSGETGQYVLLSETELYAYLPNDVKGERWNSTVKEEGARCLATTAVHRLPHFFEWHVDNTDTTTRYVRVVLPFSTPPTGVVCFVEEYVCPLLRQHKQTTIAELDEQLGWSHGAFDAHPAGSQAAGGTPSATSLCGLLRRYVESMHSPKIILEPQETTLSPLHHHVHVMPNPAVYTSPEDMLLLLNGLRISNEGITRVLPTHKPVSLFELISQQLDLHQPFREGLTTLERGSRWNVMLACESDSMDDCLQELDNCTGDILVWCEG
Protein: Neuropeptide FF receptor 2 (G-protein coupled receptor 74) (G-protein coupled receptor HLWAR77) (Neuropeptide G-protein coupled receptor) (Q9Y5X5)
Organism: Homo sapiens (Human)
Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11024015}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-FMRFamide-related neuropeptide FF
- Neuropeptide FF receptor 1
- Pro-FMRFamide-related neuropeptide VF
- Orexigenic neuropeptide QRFP
- Guanine nucleotide-binding protein subunit alpha-15
- Prolactin-releasing peptide
Sequence:
MNSFFGTPAASWCLLESDVSSAPDKEAGRERRALSVQQRGGPAWSGSLEWSRQSAGDRRRLGLSRQTAKSSWSRSRDRTCCCRRAWWILVPAADRARRERFIMNEKWDTNSSENWHPIWNVNDTKHHLYSDINITYVNYYLHQPQVAAIFIISYFLIFFLCMMGNTVVCFIVMRNKHMHTVTNLFILNLAISDLLVGIFCMPITLLDNIIAGWPFGNTMCKISGLVQGISVAASVFTLVAIAVDRFQCVVYPFKPKLTIKTAFVIIMIIWVLAITIMSPSAVMLHVQEEKYYRVRLNSQNKTSPVYWCREDWPNQEMRKIYTTVLFANIYLAPLSLIVIMYGRIGISLFRAAVPHTGRKNQEQWHVVSRKKQKIIKMLLIVALLFILSWLPLWTLMMLSDYADLSPNELQIINIYIYPFAHWLAFGNSSVNPIIYGFFNENFRRGFQEAFQLQLCQKRAKPMEAYALKAKSHVLINTSNQLVQESTFQNPHGETLLYRKSAEKPQQELVMEELKETTNSSEI
Protein: Lysosome-associated membrane glycoprotein 3 (LAMP-3) (Lysosomal-associated membrane protein 3) (CD antigen CD208) (Q5XI99)
Organism: Rattus norvegicus (Rat)
Function: Lysosomal membrane glycoprotein which plays a role in the unfolded protein response (UPR) that contributes to protein degradation and cell survival during proteasomal dysfunction. Plays a role in the process of fusion of the lysosome with the autophagosome, thereby modulating the autophagic process. Promotes hepatocellular lipogenesis through activation of the PI3K/Akt pathway. May also play a role in dendritic cell function and in adaptive immunity.
Subcellular location: Cell surface {ECO:0000250|UniProtKB:Q9UQV4}. Lysosome membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein {ECO:0000255}. Note=During dendritic cell maturation, detected on cytoplasmic vesicles (the MHC II compartment) that contain MHC II proteins, LAMP1, LAMP2 and LAMP3. Detected on lysosomes in mature dendritic cells. {ECO:0000250|UniProtKB:Q9UQV4}.
Interaction partners:
Sequence:
MPGQTSAVAVLLCLAVILHGYQIREKEFPEARGYLQYTATTTEQITAKPPLPLTNQTSHATLASRSKDDYIQTAAETSTFEDTAHITMKTAIPVTTKSLLPISSTSYTFVRTNNSHMTASSTEDTIGSGSITHLPFPTTRASLAAVNHITGRSTQLGGQTTLPKALFTPSHESTTTQRPTLSTIVSELTPTGKDRSTTSSVPLVPRPTFVTWSSPAKIGTYEVLNGSRLCIKAEMGIALIVQEKGLDSATQRHFNIDPSLTHASGKCGSQNSNLFLNFQGGSVNVTFTKEENLYYVSEVGAYLTISNTEKTYQGKSTMMMFETVVGHSFKCVSEQSIQLSAQLQMKTMNIHLQAFDFEGDSFGIVDECLSDYTVVLPVVGIIVVVLCVVGLGIYKIRQRRQSSAYQRI
Protein: Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 2 (Rhodanese domain-containing protein 2) (Q5T7W7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSSTSPDQGDDLENCILRFSDLDLKDMSLINPSSSLKAELDGSTKKKYSFAKKKAFALFVKTKEVPTKRSFECKEKLWKCCRQLFTDQTSIHRHVATQHADEIYHQTASILKQLAVTLSTSKSLSSADEKNPLKECLPHSHDVSAWLPDISCFNPDELISGQGSEEGEVLLYYCYHDLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDDLCKDDFKTSKGGAHCFPELRVGVFEEIVPMGISPKKISYKKPGIHLSPGEFHKEVEKFLSQANQEQSDTILLDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVCKEVFQLKGGIHKYLEEFPDGFYKGKLFVFDERYALSYNSDVVSECSYCGARWDQYKLCSTPQCRQLVLTCPACQGQGFTACCVTCQDKGSRKVSGPMQDSFKEECECTARRPRIPRELLQHVRQPVSPEPGPDADEDGPVLM
Protein: Cyclin-dependent kinase inhibitor (G5EEJ2)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- G1/S-specific cyclin-E
- F-box domain-containing protein
- G1/S-specific cyclin-D
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase inhibitor 1
- Proliferating cell nuclear antigen
- Mitogen-activated protein kinase mpk-1
- Importin N-terminal domain-containing protein
- Cyclin-dependent kinase 4 homolog
- Retinoblastoma-like protein homolog lin-35
Sequence:
MAATTAGDGKRKAARCLFGKPDPEEQVSRQLNSSLEEMYKKDSRKFNFDFSGGVPIVGSRGDYEFESISASEVPSFYREKIVRPRKIIARRNSTPVSDTVEMPSESPPVVESNETPLLIASTSTEVTVYEKPVTRSSAAKQSIEQQETYNLKQTKLTNYMPVRKRRSETCLVTAAVSMSRSVSIDSSMESCKEKRGSKIVHNNKGAPKRPLRFVASNVPKSAQSSTSDTVLVSSPRSPPAKKMTTSTRRSRRPIEAGDF
Protein: Non-structural protein S (NSs) (P21698)
Organism: Rift valley fever virus (strain ZH-548 M12) (RVFV)
Function: Plays a role in the escape of host innate immune response by promoting the degradation of host EIF2AK2/PKR and inhibiting host transcription. Cytoplasmic NSs interacts with host FBXW11 to degrade PKR whereas nuclear pool binds to host FBXO3 to target TFIIH subunit GTF2H1 for proteasomal degradation with the help of the linker protein SKP1. Removes FBXO3 isoform 1 from the nucleus. Forms nuclear amyloid-like filaments of about 12 nm in width that may sequester NSs binding partners, causing cell cycle arrest. Also aggragates in the cytosol as short fibrils late after host cell infection. Plays a role in cell morphology and/or motility, reduction of lamellipodia, cell spreading, and dissolution of adherens junctions.
Subcellular location: Host nucleus {ECO:0000269|PubMed:10233964, ECO:0000269|PubMed:25918396, ECO:0000269|PubMed:7108491}. Host cytoplasm {ECO:0000269|PubMed:25918396}.
Interaction partners:
Sequence:
MDYFPVISVDLQSGRRVVSVEYFRGDGPPRIPYSMVGPCCVFLMHHRPSHEVRLRFSDFYNVGEFPYRVGLGDFASNVAPPPAKPFQRLIDLIGHMTLSDFTRFPNLKEAISWPLGEPSLAFFDLSSTRVHRNDDIRRDQIATLAMRSCKITNDLEDSFVGLHRMIATEAILRGIDLCLLPGFDLMYEVAHVQCVRLLQAAKEDISNAVVPNSALIVLMEESLMLRSSLPSMMGRNNWIPVIPPIPDVEMESEEESDDDGFVEVD
Protein: High mobility group nucleosome-binding domain-containing protein 5 (Nucleosome-binding protein 1) (Nucleosome-binding protein 45) (NBP-45) (Protein GARP45) (Q9JL35)
Organism: Mus musculus (Mouse)
Function: Preferentially binds to euchromatin and modulates cellular transcription by counteracting linker histone-mediated chromatin compaction.
Subcellular location: Nucleus {ECO:0000269|PubMed:10692437, ECO:0000269|PubMed:19748358}. Note=Associates with nucleosomes in euchromatin and is largely excluded from constitutive heterochromatin.
Interaction partners:
- Non-histone chromosomal protein HMG-14
Sequence:
MPKRKAAGDVSQEPKRRSARLSAMPVPFTPELKPKRASTSRKTKTTNVVEENKDASTIPIPETKPEDVKDECNMENAENGEAKIMEAPIPKMEAEEVKEQINEDTEEDGGEKKEAVAAEAKDDELKANIQDVEKDEDGKEHKDTGEEVEDGKIEEEGLNEKPGTAKSEDAEVSKDEEEKGDNEKGEDGKEEGDEKEEEKDDKEGDTGTEKEVKEQNKEAEEDDGKCKEEENKEVGKEGQPEEDGKEDLHEEVGKEDLHEEDGKEGQPEEDGKEIHHEEDGKEGQPEEDGKEYLHEEDGEEGQPKEDQKEGQPEEDGKEDQPEEDGKEGQCKEDGKEGHHEEGGKEDLHEEDGKEKDGGKEDRKEEGEQEVAVDEGSDENKVEAEEEGAENKDFKQDGEKEEPLSIV
Protein: Tyrosine-protein phosphatase 1 (EC 3.1.3.48) (Protein-tyrosine phosphatase 1) (PTPase 1) (P27574)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in inhibiting the onset of mitosis. Dephosphorylates sty1/spc1 and wis1/spc2/sty2.
Subcellular location: Cytoplasm.
Interaction partners:
- Mitogen-activated protein kinase sty1
- Protein kinase wis1
- Protein phosphatase 2C homolog 1
- MAP kinase kinase kinase wis4
- Tyrosine-protein phosphatase 2
- M-phase inducer phosphatase
- Mitosis inhibitor protein kinase wee1
- Protein phosphatase 2C homolog 3
- Transcription factor atf1
- Protein kinase byr1
Sequence:
MNFSNGSKSSTFTIAPSGSCIALPPQRGVATSKYAVHASCLQEYLDKEAWKDDTLIIDLRPVSEFSKSRIKGSVNLSLPATLIKRPAFSVARIISNLHDVDDKRDFQNWQEFSSILVCVPAWIANYVTNAEVIGEKFRKESYSGDFGILDLDYSKVSGKYPSVIDNSPVKSKLGALPSARPRLSYSAAQTAPISLSSEGSDYFSRPPPTPNVAGLSLNNFFCPLPENKDNKSSPFGSATVQTPCLHSVPDAFTNPDVATLYQKFLRLQSLEHQRLVSCSDRNSQWSTVDSLSNTSYKKNRYTDIVPYNCTRVHLKRTSPSELDYINASFIKTETSNYIACQGSISRSISDFWHMVWDNVENIGTIVMLGSLFEAGREMCTAYWPSNGIGDKQVYGDYCVKQISEENVDNSRFILRKFEIQNANFPSVKKVHHYQYPNWSDCNSPENVKSMVEFLKYVNNSHGSGNTIVHCSAGVGRTGTFIVLDTILRFPESKLSGFNPSVADSSDVVFQLVDHIRKQRMKMVQTFTQFKYVYDLIDSLQKSQVHFPVLT
Protein: Dyslexia-associated protein KIAA0319-like protein (Adeno-associated virus receptor) (AAVR) (Q8IZA0)
Organism: Homo sapiens (Human)
Function: Possible role in axon guidance through interaction with RTN4R.
Subcellular location: Cytoplasmic granule membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:26814968}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:26814968}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:26814968}; Multi-pass membrane protein {ECO:0000305}. Note=Traffics from the plasma membrane to the trans-Golgi network. {ECO:0000269|PubMed:26814968}.
Interaction partners:
- Reticulon-4 receptor
Sequence:
MEKRLGVKPNPASWILSGYYWQTSAKWLRSLYLFYTCFCFSVLWLSTDASESRCQQGKTQFGVGLRSGGENHLWLLEGTPSLQSCWAACCQDSACHVFWWLEGMCIQADCSRPQSCRAFRTHSSNSMLVFLKKFQTADDLGFLPEDDVPHLLGLGWNWASWRQSPPRAALRPAVSSSDQQSLIRKLQKRGSPSDVVTPIVTQHSKVNDSNELGGLTTSGSAEVHKAITISSPLTTDLTAELSGGPKNVSVQPEISEGLATTPSTQQVKSSEKTQIAVPQPVAPSYSYATPTPQASFQSTSAPYPVIKELVVSAGESVQITLPKNEVQLNAYVLQEPPKGETYTYDWQLITHPRDYSGEMEGKHSQILKLSKLTPGLYEFKVIVEGQNAHGEGYVNVTVKPEPRKNRPPIAIVSPQFQEISLPTTSTVIDGSQSTDDDKIVQYHWEELKGPLREEKISEDTAILKLSKLVPGNYTFSLTVVDSDGATNSTTANLTVNKAVDYPPVANAGPNQVITLPQNSITLFGNQSTDDHGITSYEWSLSPSSKGKVVEMQGVRTPTLQLSAMQEGDYTYQLTVTDTIGQQATAQVTVIVQPENNKPPQADAGPDKELTLPVDSTTLDGSKSSDDQKIISYLWEKTQGPDGVQLENANSSVATVTGLQVGTYVFTLTVKDERNLQSQSSVNVIVKEEINKPPIAKITGNVVITLPTSTAELDGSKSSDDKGIVSYLWTRDEGSPAAGEVLNHSDHHPILFLSNLVEGTYTFHLKVTDAKGESDTDRTTVEVKPDPRKNNLVEIILDINVSQLTERLKGMFIRQIGVLLGVLDSDIIVQKIQPYTEQSTKMVFFVQNEPPHQIFKGHEVAAMLKSELRKQKADFLIFRALEVNTVTCQLNCSDHGHCDSFTKRCICDPFWMENFIKVQLRDGDSNCEWSVLYVIIATFVIVVALGILSWTVICCCKRQKGKPKRKSKYKILDATDQESLELKPTSRAGIKQKGLLLSSSLMHSESELDSDDAIFTWPDREKGKLLHGQNGSVPNGQTPLKARSPREEIL