wanglab/gogpt-training-data huggingface dataset:
Protein: Probable small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (Sm-E) (SmE) (Q9VLV5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62304}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62304}.
Interaction partners:
- Probable small nuclear ribonucleoprotein Sm D1
- Probable small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D3
- Probable small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein F
- Lsm10
- U1 small nuclear ribonucleoprotein A
- U6 snRNA-associated Sm-like protein LSm5
- U1 small nuclear ribonucleoprotein C
Sequence:
MSFKGNPKVQKVMVQPINLIFRYLQNRSRVQVWLYENISLRIEGHIVGFDEYMNLVLDDAEEVYVKTRQRRNLGRIMLKGDNITLIQNVSPTKD
Protein: Secapin (P02852)
Organism: Apis mellifera (Honeybee)
Function: Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities (By similarity). Displays antimicrobial activity against bacteria and fungi (By similarity). Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent (By similarity). Not toxic to mice but does induce slight sedation at higher doses (from 40 mg/kg). At a dose of 80 mg/kg, sedation occurs 15 minutes after injection and is accompanied by piloerection and hypothermia.
Subcellular location: Secreted {ECO:0000269|PubMed:631126, ECO:0000305|Ref.3}.
Interaction partners:
Sequence:
MKNYSKNATHLITVLLFSFVVILLIIPSKCEAVSNDMQPLEARSADLVPEPRYIIDVPPRCPPGSKFIKNRCRVIVP
Protein: Endonuclease (EC 3.1.30.-) (Q5BB95)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- ribonuclease Z
- Ribosome biogenesis protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
Sequence:
MSKATVAAIAAASAATGAGITALFYSRPSPQQQKPATATPTTAPAPPTAPVAVPVPTQPASPSLASKSATATGPVDPAGIYQYGFPGPIADTITSLPLTGAYDRRTRNPSWVAEHITPASLASKNADRKHSTFFEDSTIPPLFRAKLADYFRSGYDRGHQVPAADAKWSQEAMDGTFALTNMCPQVGEGFNRDYWAHFEEFCRDLTKRYPSVRIITGPLYLPHRDADGKWRVNYEVIGTPPNVAVPTHFYKVVYAEEGPGLPSGKVALGAFVLPNARISNDKRLAEFEVPLEAVERASGLEFASKLEPTRRKRLCQEVRCDIVVREFNNAKKKA
Protein: Myocardin related transcription factor A (A0A0G2JXC5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Serum response factor
- Hydroxyacid-oxoacid transhydrogenase, mitochondrial
- Hydroxysteroid dehydrogenase-like protein 2
- Sorbitol dehydrogenase
- 2-hydroxyacyl-CoA lyase 2
- 2-hydroxyacyl-CoA lyase 1
- Transforming protein RhoA
Sequence:
MGGVTITKAKVDFSSVVCLPPSVIAVNGLDGGGAGENDEEPVLLSLSAAPSPQSEAVANELQELSLQPELTLGLHPGRNPNLPPLSERKNVLQLKLQQRRTREELVSQGIMPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERSELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEALIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLESRASDLLPSATSISPTQVLSQLPMAPDPGETLFLAEQPPLPPPPLLPPSLTSGSIVPTAKPAPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDKGAPAMDSSYAKILQQQQLFLQLQILNQQQQQQQQQHYNYQAILPAPPKPSGETPGSSAPTPSRSLSTSSSSSSGTPGPGGLARQNSTALAGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQVSPAPGAPKAPATTSVLSKAGEVVVAFPAALLSTGSALVTAGLAPAEMVVATVTSNGMVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDAFGEMVTSPLTQLTLQASPLQIVKEEGARAASCCLSPGARAELEGLDKDQMLQEKDKQIEELTRMLQQKQQLVELLRLQLEQQKRAQQPAPASSPVKRESSFSSCQLSCQPQGAARAFGPGLVVPTTNHGDAQAPAPESPPVVVKQEAGPPEPDLAPASQLLLGSQGTSFLKKVSPPTLVTDSTGTHLILTVTNKSADGPGLPTGSPQQPLSQPGSPAPGPPAQMDLEHPPQPSFATPTSLLKKEPPGYEETVTQQPKQQENGSSSQHMDDLFDILIQSGEISADFKEPPSLPGKEKSPPAEAYGPPLTPQPSPLSELPQAAPPPGSPTLPGRLEDFLESSTGLPLLTSGHEGPEPLSLIDDLHSQMLSSSAILDHPPSPMDTSELHFAPEPSSGMGLDLAVGHLDSMDWLELSSGGPVLSLAPLSTTAPSLFSMDFLDGHDLQLHWDSCL
Protein: T cell receptor beta variable 29 (A0A0G2LB96)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRVRLISAVVLCFLGTGLVDMKVTQMPRYLIKRMGENVLLECGQDMSHETMYWYRQDPGLGLQLIYISYDVDSNSEGDIPKGYRVSRKKREHFSLILDSAKTNQTSVYFCASSL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8JHD9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKCLESPVGKRKRSLAVSSSQDPSFSGLNQLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSGGQGQQAQTPTGF
Protein: V-type proton ATPase catalytic subunit A (C8V5T7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Vacuole membrane {ECO:0000256|ARBA:ARBA00029427}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029427}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029427}.
Interaction partners:
- Vacuolar proton pump subunit B
- Vacuolar ATP synthase subunit D, putative
- V-type proton ATPase subunit
- V-type proton ATPase subunit F
- V-ATPase proteolipid subunit Ppa1, putative
- V-type proton ATPase subunit H
- V-type proton ATPase subunit C
- V-type proton ATPase subunit G
- V-type proton ATPase subunit a
- V-type proton ATPase subunit a
Sequence:
MAPSGKGSSSSEDAQLGAVFSVSGPVVVAENMIGCAMYELCRVGHDQLVGEVIRIDADKATIQVYEETAGLTVGDPVMRTGKPLSVELGPGLMETIYDGIQRPLKAISDESGSIYIPRGIKVNALDRKKKWDFKPGKYKVGDHITGGDIWGTVFENSLLNDHKILLPPRAKGTITRIAEAGSYTVEEQLLEIEFNGVKTTHGMMHTWPVRVPRPVNEKQSADSPFIVGQRVLDSLFPSVLGGTVCIPGAFGCGKTVISQSVSKFSNSDVIVYVGCGERGNEMAEVLMDFPELSIDIGGRKEPIMKRTCLIANTSNMPVAAREASIYTGITIAEYFRDQGKNVAMMADSSSRWAEALRELSGRLGEMPADQGFPAYLGAKLASFYERAGKSTALGSPEREGSVSIVAAVSPPVR
Protein: Transcription elongation factor SPT4 (Chromatin elongation factor SPT4) (P32914)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. The complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene. Structural and functional component of the centromeric and heterochromatic loci linking chromatin structure with kinetochore function and gene silencing.
Subcellular location: Nucleus {ECO:0000269|PubMed:15057281}. Chromosome, centromere {ECO:0000269|PubMed:15057281}. Chromosome {ECO:0000269|PubMed:19683497}. Note=Centromere and heterochromatin (PubMed:15057281). Associates with the coding region of HTA1 (PubMed:19683497). {ECO:0000269|PubMed:15057281, ECO:0000269|PubMed:19683497}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB7
- Transcription elongation factor SPT6
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB9
- Transcription elongation factor SPT5
- Transcription elongation factor S-II
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MSSERACMLCGIVQTTNEFNRDGCPNCQGIFEEAGVSTMECTSPSFEGLVGMCKPTKSWVAKWLSVDHSIAGMYAIKVDGRLPAEVVELLPHYKPRDGSQVE
Protein: Phosphatidylinositol 3-kinase (Q55FX5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Phosphatidylinositol 3-kinase
- Phosphatidylinositol 3-kinase 1
- Phosphatidylinositol 3-kinase 3
- Phosphatidylinositol 3-kinase 2
- Inositol 5-phosphatase 4
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- LIM-domain containing phosphatase
- PIPK domain-containing protein
- phosphoinositide 5-phosphatase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
Sequence:
MLLEDEELTYQSLLVSTESDDEGDTNNLLSIGSGGEKTAVELDSIFSLSPQSATSPPLSPPSPNPTRTKPAVPPRSFNSLDENETLTFKKEPILPKSSNESLLGSVPNEQKNDKSPLKSTEPTTISTVQQPIVQQQPIVQQQPIVQQQLQQQQQQQLQQQEVMEPQHWSNYLSMKPLKQTLNEIPIQVQVKDNYFIMGCNKNFTSSEFKSYLVSNLESMIQAIKVGTFATNDISSETIAFKKNAVICDLFTDSIQQRPTSIPSLIVLKPGMQDLFKGNSRAFIGSPIVNSNNNVNNNINNSNSNSNNNNINNSLDGFKLSTSLQTPSVNLSLLHNNIQNLISNNGNSGPSSINSSCSSSSSNNGNTTNYSSSIGNEYKQPISGSLIFNNNKTLGRNANFSLGEQRDNNAKLRQQKKKLTAIQISSLLGEPLNWSNTENEIKYFRNLAEQIFDFQTLDERDRVKITIAPVTNAHPDPLLPSTFRVRFYLPPDNHSTTINVMSSDTVTNLIEKVIAKHNNSTKLISSDHTPSDYVIRITGTSDHVLKTDELVTNLIVVRNRLQRKKDIKFSLVHKTSLPKIYIDGHSPEICTLKNNNNNNNINNNNNNNNNNNNNINNNNSENGNIQQPYGSPINILQFPISPRSENNVNSNNNNNYNNYNNNNNSNKGNNSNRSILLYEINRPFEIRIICLENLVLPLFQKYLGSECNNFNDVKLTIMVELCHGEDVLTEPMETVIKLGSNPLWCEWLRSALLMSNIPRASKLCFTAYAQQGDKQQAKVSIGWADLQLIDYHSQLLSGVISLILWPGARTDIPDFNVPSPSLVIEFCQFPFPVVFPKPEMMERTEIRDYVESRKEDTERLEELIRKDSLYVLTETDKKFIWLYRMHLQKIPSSLPKVLQSLNWNNPQEVKEAHRLLSIWSTLSPLEALELLDSKFADELVREYAVNCLHSLADSELALYLLQLVQSLKHEPYHNSALCRFLIRRALNNRAVIGHPFFWHLEAEMHNPKISERYSLVLETFLKGCGNQRHEFVKQMEVVTKLQTIAKLVKEASPNKRKNLLHEELNKMSWPNTFHLPISPSTETCGVIVSECRWLDSFTVPLYLVFQNVDPVGEPIAVIFKNGDDLRQDILTLQMISVMDNIWKQNGLDLHLSIYNVTAINEDTGFIEVVPDSDTTANIQKAAGGVTAAFTKTPLSNWLRERNQSDPDYEYAVGNFTHSLAGYCVATFILGISDRHNDNIMVSKSGHLFHIDFAHFLGNIMKFHGYKREKAPFVLTPEFAHVMGGEKSLSFKFFSDLCCLSYKFLRNHRNLFINLFSLMISTGIPELSTKADISYLKEAFLLDVSDEEAGASFERLIQKSLKTKTTQVMFAMHILAHSGTSSDD
Protein: Wtf element wtf7 (Q7Z9I5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May act in meiotic drive.
Subcellular location: Spore membrane {ECO:0000250|UniProtKB:A0A482APM8, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSGSYAPIEDSADELSVHSGNDNEIDLEKGLLPKCNTGNGGTTPCSEPPHYDSDAVVEMDMYENNIYMRTFKLRPFAKSGVTNSSNVVFQMKTYENNRHMQTFRLRPFAKNGVTNGVKLAQSLFLLLPFNFIFFACLFFRKASFTDFSLMGWILFGIWCLTCFLSSFILYAYHESWTKFARERSQEFSLILFGLLFPGIVTMVVFYALYMRSMYG
Protein: Protein JINGUBANG (O48716)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of pollen germination. Prevents pollination in moist environments by inhibiting jasmonic acid synthesis. Stabilizes pollen tube growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:27468890}. Cytoplasm {ECO:0000269|PubMed:27468890}. Note=The nuclear protein is functional. {ECO:0000269|PubMed:27468890}.
Interaction partners:
- Transcription factor TCP4
- Rho GTPase-activating protein REN1
- Probable magnesium transporter NIPA1
- Protein APEM9
- Protein NPG1
- Tetratricopeptide repeat protein SKI3
- GTP-binding protein-like protein
- Zinc finger CCCH domain-containing protein 3
Sequence:
MFTEADSIPRAKYANMMHSDPNLSSTMTQQTEEEYGIRNSSASAVGTGMYDRMSCEGSPMMMSPWNQATPFTQTQWSTVEENLPQNGLIGSLVREEGHIYSLAATKDLLYTGSDSKNIRVWKNLKEFSAFKCNSGLVKAIVISGEKIFTGHQDGKIRVWKVSPKNQSLHKRSGTLPTLKDIFKASLKPRNYVEVKKHRTALWIKHADAVSCLSLNDEQGLLYSASWDRTIKVWRIADSKCLESIPAHDDAVNSVVSTTEAIVFSGSADGTVKAWKRDQQGKYTKHTLMQTLTKQESAVTALAVSKNGAAVYFGSSDGLVNFWEREKQLNYGGILKGHKLAVLCLEVAGSLVFSGSADKTICVWKRDGNIHTCLSVLTGHTGPVKCLAVEADREASERRDKKWIVYSGSLDKSVKVWGVSESFIDMNQMSMMQQQQQQHVISHSEPFMSDGSFSSSAGGASSHRRH
Protein: Vacuolating cytotoxin putative domain-containing protein (O25330)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Toxin-like outer membrane protein
Sequence:
MTYRSSKTDLKNERFSKNRSFKGIKKKIAKKYTIKNSPLTIYSLKTHSNPSLSINKKIFLGLGFVSALSAEDYNSSVYWLNSVNENNNNKSYYISPLRTWAGGNRNFTQNYNNSQLYIGTKNASSTPNHSSVWFGEKGYVGFITGVFKAKDIFITGAVGSGNEWKTGGGAILVFESSNELSANGAYFQNNRAGTQTSWINLISNNSVNLTNTDFGNQTPNGGFNAMGRKITYNGGIVNGGNFGFDNVDSNGATTISGVTFNNNGALTYKGGNGIGGSITFTNSNINHYKLNLNANSVTFNNSALGSMPNGNANTIGNAYILNASNITFNNLTFNGGWFVFNIPDAHVNFQGTTTINNPTSPFVNMTGKVTINPNAIFNIQNYTPSIGSAYTLFSMKNGSITYNDVNNLWNIIRLKNTQATKDADKNHTSSNNNTHTYYVTYNLGGTLYNFRQIFSPDSIVLQSVYYGANNLYYTNSVNIHDNVFNLKNINDDKADTIFYLNGLNTWNYTNARFTQTYGGKNSALVFNATTPWANGSIPKSNSTVRFGGYEGVNWGKTGYITGTFTADRVYITGNMMTGNGAQTGGGATLNFVGATEINIAGATFKNLKTTSQNSYMTFMALGDSSGSAKINVSQSDFYDWTGGGYDFTGNGVFDSVNFNKAYYKFQGTENSYNFKNTNFLAGNFKFQGKTTIEKSVLSDASYTFDGTNNTFTEDKFNNGSFNFSHAEQTDAFNNNSFNGGSFSFNAKQVNFSGNSFNGGVFNFNNTPKVSFTDDTFNVNNQFKINGTQTTFTFNKGVVFNMQGLLSSLSVGTTYQLLNAKSVDYKDNNALYQMLRWISGENPSGTLVNKDQSAPNSAKIYNVHFTDNGLTYYIKENFNNGITLTRLCTLGYTHCVNIDNDAFNLKNVNNNASNTVFYLNGMTTWKIAGTGVFTQDYSGANSVLVFNQTTPFLAGANPTSNSVVSFGKTSGAEWGLVGYIQGVFKANQIDITGTIRSGNGAKTGGGATLVFNAQKRLNIANAHLNNDKAGLQNSWMNFIVNNGNLNVTNAKFSNQTPHGGFNLKANNITWDKGSVNGGGNFGVDNADSNGATTISGVTFNNNGTLIYKGGENSAGNSLTLENNTFNSYNINAKAQNLIFNNNSFNGGSYSFNDTKNTTFKGTNTLINSDPFSRLKGSVSIENNSVFNIERDLTDKTTYTLLSGNSIKYNNQALAGQCFFKKFMEFNPLWWRTRDSIKSG
Protein: GH18625p (Q9W3Z4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Syntaxin-5
- FI05230p
- LD39211p
- Golgi SNAP receptor complex member 1
Sequence:
MEIGNDQSYQDFFDKLRSESGPRNLRQIFEDDDRPLANESSSLRYQPGSSKKLQAGKRPAMTRSSTQETGDSPPAAWNTAIAKVVHAYRSSENVGRVGLALSILGEMEASKLIVYRSKSQVLTTLQLTPRGGKVILRESYLQFYDDEQRFWSLRFDKEPDEKEFITFMVKNKLPVEHYLSEISSSSSASPSREDLSKIRTKATVTKTTPNPPQPQPRSRVTLPTLEKADDEERERETETPSNEDVIVTPVPRPIGSSNAHRKLSASSLAVANASTSSDTPLAVTTLDKYLDEQRASGALMEHKMDAILQAMNRMGGQSSVAPKKPSDPLLERDSEDEMLELEQKLLNLKRENRALMRNLKAREQALEDLRCSACALCEELLVQNGELKSQNAQLLLASQHISDSSTAASPAHCRNCESSSRQIAKMQLHISALQEALRIFQKSGDSSSSSGRL
Protein: C-X-C chemokine receptor type 2 (High affinity interleukin-8 receptor B) (F1Q8T9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Chemokine
- Stromal cell-derived factor 1
- Chemokine
- C-X-C motif chemokine 19 precursor
- Chemokine
- C-C motif chemokine
- Beta-arrestin-1
- Arrestin, beta 2a.
- Arrb2b protein
- Macrophage migration inhibitory factor
Sequence:
METATTEFPFTLMTPCPETVKNLNSTVLVVIYIIVFCLSLLGNTVVIFVVFFMDNRRTSTDLYLMHLAVADLLFSLTLPFWVAYLHAGHWPFGTIMCKMISGVQEVTFYCSVFMLACISIDRYMAIVKATQFLNRKLHLIGFVCALVWLCAALLSLPVMVHREAITYDGVEYICEDNVTAESTDSWRMSLRIIRHTLGFFLPLTVMMFCYGFTMFTLCHTRNSQKQKAMRVILSVVLAFIICWLPHNIIEFTDILMRAGQVEETCQLRDNIDVALYATQVMAFAHCAINPILYAFIGKKFRNQLLISLFKKGLFGRNMLSRYGAGSFQSSGSTRQMSVTL
Protein: Heat stress transcription factor A-1e (AtHsfA1e) (AtHsf-06) (Heat shock factor protein 2) (HSF 2) (Heat shock transcription factor 2) (HSTF 2) (Q9SCW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Chaperone protein ClpB1
- Myeloid leukemia factor
- Dehydration-responsive element-binding protein 2A
- Heat shock protein 90-1
Sequence:
MGTVCESVATAKSSTAVMSSIPPFLSKTYDMVDDPLTDDVVSWSSGNNSFVVWNVPEFAKQFLPKYFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEGFLRGQKQILKSIVRRKPAQVQPPQQPQVQHSSVGACVEVGKFGLEEEVERLQRDKNVLMQELVRLRQQQQVTEHHLQNVGQKVHVMEQRQQQMMSFLAKAVQSPGFLNQFSQQSNEANQHISESNKKRRLPVEDQMNSGSHGVNGLSRQIVRYQSSMNDATNTMLQQIQQMSNAPSHESLSSNNGSFLLGDVPNSNISDNGSSSNGSPEVTLADVSSIPAGFYPAMKYHEPCETNQVMETNLPFSQGDLLPPTQGAAASGSSSSDLVGCETDNGECLDPIMAVLDGALELEADTLNELLPEVQDSFWEQFIGESPVIGETDELISGSVENELILEQLELQSTLSNVWSKNQQMNHLTEQMGLLTSDALRK
Protein: Cadherin 10 (F1LR98)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
Interaction partners:
- Cadherin 3
- Cadherin-2
Sequence:
MSIYSFLRLFVLWACLPQFCCPELTFRRTPGLQQMTAESHVPRGDGKILHRQKRGWMWNQFFLLEEYTGSDYQYVGKLHSDQDKGDGSLKYILSGDGAGTLFIIDEKTGDIHATRRIDREEKAFYTLRAQAINRRTLRPVEPESEFVIKIHDINDNEPTFPEEIYTASVPEMSVVGTSVVQVTATDADDPSYGNSARVIYSILQGQPYFSVEPETGIIRTALPNMNRENKEQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQNTIHLRVLESSPVGTAVGSVKATDADTGKNAEVDYRIIDGDGTDMFDIITEKDTQEGIITVKKPLDYENRRLYTLKVEAENTHVDPRFYYLGPFKDTTIVKISIEDVDEPPVFSRSSYLFEVHEDIEVGTIIGTVMARDPDSTSSPIRFTLDRHTDLDRIFNIHSGNGSLYTSKPLDRELSQWHNLTVIAAEINNPKETTRVSVFVRILDVNDNAPQFAVFYDTFVCENARPGQLIQTISAVDKDDPLGGQKFFFSLAAVNPNFTVQDNEDNTARILTRKNGFNRHEISTYLLPVVISDNDYPIQSSTGTLTIRVCACDSQGNMQSCSAEALLLPAGLSTGALIAILLCIIILLVIVVLFAALKRQRKKEPLILSKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPAAIEEKKLRRDIIPETLFIPRRTPTAPDNTDVRDFINERLKEHDLDPTAPPYDSLATYAYEGNDSVAESLSSLESGTTEGDQNYDYLREWGPRFNKLAEMYGGGESDKDA
Protein: Sulfhydryl oxidase 2 (EC 1.8.3.2) (Neuroblastoma-derived sulfhydryl oxidase) (Quiescin Q6-like protein 1) (Q6ZRP7)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosis.
Subcellular location: Membrane {ECO:0000269|PubMed:14633699}; Single-pass membrane protein {ECO:0000269|PubMed:14633699}. Secreted {ECO:0000269|PubMed:14633699}. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Seems to be predominantly targeted to the nuclear and outer plasma membrane.
Interaction partners:
- FAD-linked sulfhydryl oxidase ALR
- Thioredoxin
Sequence:
MAAAGAAVARSPGIGAGPALRARRSPPPRAARLPRLLVLLAAAAVGPGAGGAARLYRAGEDAVWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYPTFRYFKAFTKEFTTGENFKGPDRELRTVRQTMIDFLQNHTEGSRPPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTRALDGDKAFLEKLGVSSVPSCYLIYPNGSHGLINVVKPLRAFFSSYLKSLPDVRKKSLPLPEKPHKEENSEIVVWREFDKSKLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDLVNNKMRISGIFLTNHIKWVGCQGSRSELRGYPCSLWKLFHTLTVEASTHPDALVGTGFEDDPQAVLQTMRRYVHTFFGCKECGEHFEEMAKESMDSVKTPDQAILWLWKKHNMVNGRLAGHLSEDPRFPKLQWPTPDLCPACHEEIKGLASWDEGHVLTFLKQHYGRDNLLDTYSADQGDSSEGGTLARGEEEEKRLTPPEVSHGDRDTQSVRPPGALGPRPALPESLHHSLDGKLQSLDGPGAHKEVGGAAPFLGVDFSSLDMSLCVVLYVASSLFLMVMYFFFRVRSRRWKVKHHHPAV
Protein: t-SNARE coiled-coil homology domain-containing protein (Q2U502)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
- Uncharacterized protein
- Protein transport protein BOS1
- Protein transport protein SEC22
- Golgi SNAP receptor complex member 1
- Uncharacterized protein
- Uncharacterized protein
- t-SNARE coiled-coil homology domain-containing protein
- V-SNARE coiled-coil homology domain-containing protein
- Soluble NSF attachment protein
- Synaptobrevin homolog YKT6
Sequence:
MTGPSIQDRTGEFHAILGQAQKRVATNKVGSQRQALLSDSQRRQANGSANGGAQPGRRSEFARRAVEIGRGITATTAKLQRLAELAKRKTLFDDKPVEISELTYVIKQDLASLNQQIASLQALTLSQHPKSNRSKADQEGEHNDNVVVMLQGKLADVGANFKEVLEVRTKNIQASRSRTENFVSSVSSKSQAALDTQRSDSPLYTSGRRTPQPGGSSDLLTLEPSNPSPLGRPSMHSDQQLLVMEEAQTSNSYIQARGEAIDAIERTINELGGIFGQLAQMVSEQSEMIQRIDANTEDVVDNVQGAQRELMKYWTRVSGNRWLIAKMFGVLMIFFLLWVLISG
Protein: Low-affinity putrescine importer PlaP (Putrescine low affinity permease) (P0AA47)
Organism: Escherichia coli (strain K12)
Function: Putrescine importer. Required for induction of type 1 pili-driven surface motility.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein YoeI
Sequence:
MSHNVTPNTSRVELRKTLTLVPVVMMGLAYMQPMTLFDTFGIVSGLTDGHVPTAYAFALIAILFTALSYGKLVRRYPSAGSAYTYAQKSISPTVGFMVGWSSLLDYLFAPMINILLAKIYFEALVPSIPSWMFVVALVAFMTAFNLRSLKSVANFNTVIVVLQVVLIAVILGMVVYGVFEGEGAGTLASTRPFWSGDAHVIPMITGATILCFSFTGFDGISNLSEETKDAERVIPRAIFLTALIGGMIFIFATYFLQLYFPDISRFKDPDASQPEIMLYVAGKAFQVGALIFSTITVLASGMAAHAGVARLMYVMGRDGVFPKSFFGYVHPKWRTPAMNIILVGAIALLAINFDLVMATALINFGALVAFTFVNLSVISQFWIREKRNKTLKDHFQYLFLPMCGALTVGALWVNLEESSMVLGLIWAAIGLIYLACVTKSFRNPVPQYEDVA
Protein: Nuclear factor erythroid 2-related factor 2 (C9J0Y1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAF
Protein: F-box and leucine-rich repeat protein 18 (F8VQK6)
Organism: Mus musculus (Mouse)
Interaction partners:
- Cullin-1
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase RBX1
- Expressed sequence C85627
Sequence:
MSSEEEAAAEAAGDTHLLGFSDEILLHILSHVPSTDLVLSVRRTCRKLAALCLDKSLVHTVLLQKDYQASEEKVKQLVKEIGREIQQLNMAGCYWLSGSTIEHVARCHSLVKVNLSGCHLTSLRLSKVLSALQHLRSLAIDVSPGFDASQLSSECKATLSRVQELKQTLFTPSYGVVPCCASLQKLLLYFEILDRTREGAVLSGQLMVGQSNVPHYQNLRVFYARLAPGYINQEVVRLYLAVLSDRTPENLHAFLISVPGSFAESGATKNLLDSMARNVALDALQLPKSWLNGSTLLQHMKFNNPFYFSFSRCTLSGGHLIQRLINGGKDLRSLASLNLSGCVHCLSADSLLRKAEDDIDSSILETLVESCCNLHHLNLSAAHHHSSDGLGRHLCQLLARLCHLRSLSLPVCSVADSAPRPDRAPAPPAMHAVPRGFGKKVRIGVQTCPNPFVGQSAPQPASVFWSLLKKLPFLEHLELIGSNFSSAMPRNEPAIRNSLPPCSRAQNVGDSEVAAIGQLTFLRHLTLAQLPGMLTGSGLVSIGLQCQHLQSLSLANLGMMGKVVYMPALADMLKHCKRLKDLRLEQPYFNANAQFFQALGQCSSLQRLCLVSRSGTLQPDAVLAFMARCLQVVMCHMFTGESLTTCKSLQQSLLRSFQAERPALNVVIFPLLHEGLTDVIRDVPMLHLDEITLFKSRVAEEPPNLWW
Protein: V-type proton ATPase subunit C (Q5A2U9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- V-type proton ATPase subunit F
- H
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit G
- V-type proton ATPase subunit a
- V-type proton ATPase subunit
- H
- V-type proton ATPase subunit B
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
Sequence:
MSSNSVAKIAEYLILSLPQSTHAHEWLEQSLNNGKQPLYNLKIPDFQSGTLDSLVQESEELNKIDHQLGSSVNKVVEILNSINPQTSSGSSSSSSRIVQSRSIFDYIENFQWNSSKYRLDKPISQLVKMISQEAITLDNDVRTSYQSYQSAKSNFLAADRKKNGDLSIKSLHEIVKPEQFVLDSEHLTTILIAVPNNLLDDFHKNYETLTSFVIPRSAELIAKDQEFHLFTVTLFKKYQQEFINNAREHRWHPRTDFTYSEEILNELRKEFDLTQATELKLKNDLIRLTKTAYSDIMANWFHIKIIRTYVEAVLKYGLPPQFDNYLIKFNESNLKNVDKAKKELIAKFNYLGGNGYTTGNNNSSNLHEYASLVDTEYQPFVLYELEIV
Protein: Myosin light chain smooth muscle isoform (Q6W5H0)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
Sequence:
MCDFSEEQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVMKVLGNPKSDEMNLKTLNFEQFLPMMQTIAKNKDQGCFEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEVEQLVAGHEDSNGCINYEELVRMVLSG
Protein: DNA-directed RNA polymerases II, IV and V subunit 9A (Q6NLH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements. Required for RNA silencing.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P32529}.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 12
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases IV and V subunit 3B
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases II and IV subunit 5A
- DNA-directed RNA polymerases IV and V subunit 2
- DNA-directed RNA polymerases II, IV and V subunit 6A
Sequence:
MSTMKFCRECNNILYPKEDKEQKILLYACRNCDHQEVADNSCVYRNEVHHSVSERTQILTDVASDPTLPRTKAVRCSKCQHREAVFFQATARGEEGMTLFFVCCNPNCGHRWRE