wanglab/gogpt-training-data huggingface dataset:
Protein: Complement C1q subcomponent subunit C (Q02105)
Organism: Mus musculus (Mouse)
Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
Subcellular location: Secreted.
Interaction partners:
- Complement C1q subcomponent subunit B
- Complement C1q subcomponent subunit A
- Complement C1r-A subcomponent
- Complement C1s-1 subcomponent
- Complement C1r-B subcomponent
- Complement C4-B
- Complement C1s-1 subcomponent
- Plasma protease C1 inhibitor
- Complement C2
- Calreticulin
Sequence:
MVVGPSCQPPCGLCLLLLFLLALPLRSQASAGCYGIPGMPGMPGAPGKDGHDGLQGPKGEPGIPAVPGTRGPKGQKGEPGMPGHRGKNGPRGTSGLPGDPGPRGPPGEPGVEGRYKQKHQSVFTVTRQTTQYPEANALVRFNSVVTNPQGHYNPSTGKFTCEVPGLYYFVYYTSHTANLCVHLNLNLARVASFCDHMFNSKQVSSGGVLLRLQRGDEVWLSVNDYNGMVGIEGSNSVFSGFLLFPD
Protein: eIF5-mimic protein 2 (Basic leucine zipper and W2 domain-containing protein 1) (Protein Orf) (Q7L1Q6)
Organism: Homo sapiens (Human)
Function: Translation initiation regulator which represses repeat-associated non-AUG (RAN) initiated translation probably by acting as a competitive inhibitor of eukaryotic translation initiation factor 5 (EIF5) function. Enhances histone H4 gene transcription but does not seem to bind DNA directly.
Interaction partners:
- eIF5-mimic protein 1
Sequence:
MNNQKQQKPTLSGQRFKTRKRDEKERFDPTQFQDCIIQGLTETGTDLEAVAKFLDASGAKLDYRRYAETLFDILVAGGMLAPGGTLADDMMRTDVCVFAAQEDLETMQAFAQVFNKLIRRYKYLEKGFEDEVKKLLLFLKGFSESERNKLAMLTGVLLANGTLNASILNSLYNENLVKEGVSAAFAVKLFKSWINEKDINAVAASLRKVSMDNRLMELFPANKQSVEHFTKYFTEAGLKELSEYVRNQQTIGARKELQKELQEQMSRGDPFKDIILYVKEEMKKNNIPEPVVIGIVWSSVMSTVEWNKKEELVAEQAIKHLKQYSPLLAAFTTQGQSELTLLLKIQEYCYDNIHFMKAFQKIVVLFYKAEVLSEEPILKWYKDAHVAKGKSVFLEQMKKFVEWLKNAEEESESEAEEGD
Protein: Endonuclease MutS2 (EC 3.1.-.-) (Ribosome-associated protein quality control-upstream factor) (RQC-upstream factor) (RqcU) (EC 3.6.4.-) (Q76DY7)
Organism: Thermus thermophilus
Interaction partners:
Sequence:
MRDVLEVLEFPRVRALLAERAKTPLGRELALALAPLPREEAEKRHELTGEALSYPYALPEAGTLREAYGRALAGARLSGPELLKAAKALEEAMALKEELLPLKNALSQVAEGIGDHTPFLERVRKALDEEGAVKDEASPRLAQIRRELRPLRQQILDRLYALMDRHREAFQDRFVTLRRERYCVPVRAGMAQKVPGILLDESESGATLFIEPFSVVKLNNRLQALRLKEEEEVNRILRDLSERLAKDEGVPKTLEALGLLDLVQAQAALARDLGLSRPAFGERYELYRAFHPLIPDAVRNSFALDEKNRILLISGPNMGGKTALLKTLGLAVLMAQSGLFVAAEKALLAWPDRVYADIGDEQSLQENLSTFAGHLRRLREMLEEATSHSLVLIDELGSGTDPEEGAALSQAILEALLERGVKGMVTTHLSPLKAFAQGREGIQNASMRFDLEALRPTYELVLGVPGRSYALAIARRLALPEEVLKRAEALLPEGGRLEALLERLEAERLALEAERERLRRELSQVERLRKALAEREARFEEERAERLKALEEEVRAELLKVEAELKALKEKARTEGKRDALRELMALRERYAKKAPPPPPPPGLAPGVLVEVPSLGKRGRVVELRGEEVLVQVGPLKMSLKPQEVKPLPEAEPGKPLLAKPRREVKEVDLRGLTVAEALLEVDQALEEARALGLSTLRLLHGKGTGALRQAIREALRRDKRVESFADAPPGEGGHGVTVVALRP
Protein: ActC (Q93P57)
Organism: Myxococcus xanthus
Interaction partners:
Sequence:
MTPPLVLLGSGYTLTRLAVAEARAGRDVLAATRDAARRAELERAGARVTDLEDALTRTAGAHVVVSVPPDAGLDTRIASALAGQVPARLVYLSSTGVYGRARGHVDEDTPVELSTPSSRERIEAESRYLPLGAMVMRIAGIYGPGRGIHTRLLSGALRLPEGGGGRISRIYVDDLVESIRVVLTRGEPGALYCVADDRSAPSEEPVAWLSQRLGVPMPPRIPLAQLNETLRGDRDISNARLKSLGWAPRYPDFISGYTALLKAEGHGAGPTQLVIRRLVAEDAEAFKALRLRGLRDNPESFAASVEEDSALSLEAVRGWLVGASQCVLGAFDGGQLVGALGLNRESRARLAHKAMVWGMYVAPEVRSRGVGRRLLTALIDEARKMGGLKCLLLAVSVGNAPAHALYRSLGFRTYGVEPNALKVGETFLDEELMVLTL
Protein: (-)-beta-phellandrene synthase 2, chloroplastic (EC 4.2.3.52) (Terpene synthase (-)betaphell2) (PcTPS-(-)betaphell2) (R9QMW3)
Organism: Pinus contorta (Shore pine) (Lodgepole pine)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-beta-phellandrene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MALVSVAPLVSMRRSLFSSPYELKSIDKTIPNLVMCRKRMLGRPSIRVSSTASVSNDDGVRRRVGDYRYNHWDEDLIDSLATSYEAPSYLKRADTLVEAIKDRFNSMGVDDGERMSPLTDLYQRLWMVDSVERLGIDRHFQNEIKSALDYVFRYFASSYWKEKGIGRGRQSAVTDLNSTALGLRTLRLHGYPVSSDVLENFKDHNGQFTCSGIQTEGEIRGVLNLFRASLIAFPGEKVMEEAEIFSTMYLKHALQKIAVSSLSQEIEYLLEYGWHTNPPRLEARMYMEVFPQDTIYEQKLVELAKVEFNIFHSLQKRELQSLTRWWKHYGFPQLSFTRHIHVEYYTFGSCIATDPKQSAFRLCFAKMSYFVTVLDDIYDTYGTMEELELFTAAIKRWDPSVVDCLPEYMKGVYMAVYDTVNEMAKEAEKVQGRDTLNYVRQAWELYIDAYMPEAKWISSGYLPTFQEYLDNSKISFGTRITILQPILTLGEPLPHEILQEIDFPAKFNDLISVILRLKGDTRCYKADRARGEEASSVSCYMKDNAGLTEEDAIHRINAMVHNLLKELNWELLKPDCNVPISCKKAAFDICRIFHHGYKYRDGYGDATIETKNLVKRTVLEPVPL
Protein: Probable deoxyhypusine synthase (DHS) (EC 2.5.1.46) (O94337)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Interaction partners:
- Deoxyhypusine hydroxylase
- Eukaryotic translation initiation factor 5A-2
- Eukaryotic translation initiation factor 5A-1
- Spermidine synthase
Sequence:
MDESLAKDAVFVASSKPSDLTTEVVGPDFNKYDERKKAGGPGITVEELVESYGKIGFQATNLHDAVTIINEMRNWRDPNPPEEKSDRATIFLGYTSNLISSGVREVLRYLVQHKCVDVIVTTAGGVEEDIIKCLGPTYVGDFHLDGKNLRAKGLNRIGNLIVPNDNYCRFEEWIFPILNKMVEEQETLGTHWTPSSFIRRLGKEINDESSVLYWAYKNNIPIYSPALTDGSIGDMLYFHTYKATPRPLVLDIVADIRNMNTHAVRANKSGIIILGGGVVKHHICNANLMRNGAEWSVYINSANEFDGSDAGARPDEAVSWGKIRGDAKKVKVYGEVSLLFPLIVAATFAK
Protein: Large ribosomal subunit protein uL16c (50S ribosomal protein L16, chloroplastic) (P0C441)
Organism: Oryza sativa (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MLSPKRTRFRKQHRGRMKGKSYRGNCICFGRYALQALEPTWITARQIEAGRRAMTRYARRGGKIWVRIFPDKPVTIRPTETRMGSGKGSPEYWVAVVKPGRILYEMGGVSETVARAAISIAASKMPIRSQFLRLEI
Protein: Translocation protein sec66 (Q9UUA4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon. sec66 is required to attach or retain sec72 in the sec63 complex (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Translocation protein sec63
- ER protein translocation subcomplex subunit sec67
- Translocation protein sec62
- Probable protein transport protein Sec61 subunit gamma
- Uncharacterized protein C19G7.17
- Protein transport protein sec61 subunit alpha
- Protein transport protein sec61 subunit beta
- Protein transport protein bos1
- Protein transport protein use1
- Protein transport protein sec20
Sequence:
MVSIYVPLIYITILMGSMYGVSRFVRKSKNQESKPVSEEWFGENYSRNIFFSLLQQNPPAEDTLLKAALVLRATEGLRRLMKLKVSRMALNNLLNRGGVGDELIRKFGRLEKETELELMDIAKTANSLQPGWNQFIFQTCNEIIENEKIHSIIDNIPKDIDSISQRWQTEKILYEAADEELRIQAQKELGVL
Protein: Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2'] (P36334)
Organism: Human coronavirus OC43 (HCoV-OC43)
Function: S1 attaches the virion to the cell membrane by interacting with sialic acid-containing cell receptors, initiating the infection.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}.
Interaction partners:
Sequence:
MFLILLISLPTAFAVIGDLKCTSDNINDKDTGPPPISTDTVDVTNGLGTYYVLDRVYLNTTLFLNGYYPTSGSTYRNMALKGSVLLSRLWFKPPFLSDFINGIFAKVKNTKVIKDRVMYSEFPAITIGSTFVNTSYSVVVQPRTINSTQDGDNKLQGLLEVSVCQYNMCEYPQTICHPNLGNHRKELWHLDTGVVSCLYKRNFTYDVNADYLYFHFYQEGGTFYAYFTDTGVVTKFLFNVYLGMALSHYYVMPLTCNSKLTLEYWVTPLTSRQYLLAFNQDGIIFNAEDCMSDFMSEIKCKTQSIAPPTGVYELNGYTVQPIADVYRRKPNLPNCNIEAWLNDKSVPSPLNWERKTFSNCNFNMSSLMSFIQADSFTCNNIDAAKIYGMCFSSITIDKFAIPNGRKVDLQLGNLGYLQSFNYRIDTTATSCQLYYNLPAANVSVSRFNPSTWNKRFGFIEDSVFKPRPAGVLTNHDVVYAQHCFKAPKNFCPCKLNGSCVGSGPGKNNGIGTCPAGTNYLTCDNLCTPDPITFTGTYKCPQTKSLVGIGEHCSGLAVKSDYCGGNSCTCRPQAFLGWSADSCLQGDKCNIFANFILHDVNSGLTCSTDLQKANTDIILGVCVNYDLYGILGQGIFVEVNATYYNSWQNLLYDSNGNLYGFRDYIINRTFMIRSCYSGRVSAAFHANSSEPALLFRNIKCNYVFNNSLTRQLQPINYFDSYLGCVVNAYNSTAISVQTCDLTVGSGYCVDYSKNRRSRGAITTGYRFTNFEPFTVNSVNDSLEPVGGLYEIQIPSEFTIGNMVEFIQTSSPKVTIDCAAFVCGDYAACKSQLVEYGSFCDNINAILTEVNELLDTTQLQVANSLMNGVTLSTKLKDGVNFNVDDINFSPVLGCLGSECSKASSRSAIEDLLFDKVKLSDVGFVEAYNNCTGGAEIRDLICVQSYKGIKVLPPLLSENQISGYTLAATSASLFPPWTAAAGVPFYLNVQYRINGLGVTMDVLSQNQKLIANAFNNALYAIQEGFDATNSALVKIQAVVNANAEALNNLLQQLSNRFGAISASLQEILSRLDALEAEAQIDRLINGRLTALNAYVSQQLSDSTLVKFSAAQAMEKVNECVKSQSSRINFCGNGNHIISLVQNAPYGLYFIHFSYVPTKYVTARVSPGLCIAGDRGIAPKSGYFVNVNNTWMYTGSGYYYPEPITENNVVVMSTCAVNYTKAPYVMLNTSIPNLPDFKEELDQWFKNQTSVAPDLSLDYINVTFLDLQVEMNRLQEAIKVLNQSYINLKDIGTYEYYVKWPWYVWLLICLAGVAMLVLLFFICCCTGCGTSCFKKCGGCCDDYTGYQELVIKTSHDD
Protein: Grainyhead-like protein 1 homolog (Transcription factor CP2-like 2) (Transcription factor LBP-32) (Q921D9)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3'. Important regulator of DSG1 in the context of hair anchorage and epidermal differentiation, participates in the maintenance of the skin barrier. There is no genetic interaction with GRHL3 no genetic interaction with GRHL3, no functional cooperativity due to diverse target gene selectivity during epithelia development.
Subcellular location: Nucleus {ECO:0000269|PubMed:18288204}.
Interaction partners:
Sequence:
MTQEYDNKRPVLVLQNEALYPQRRSYTSEDEAWKSFLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRERRSSAVKPEGEHPEPEHSKRNSIPNVTEQPLISAGENRVQVLKNVPFNIVLPHSNQLGIDKRGHLTAPDTTVTVSIATMPTHSIKTEIQPHGFAVGIPPAVYHSEPTERVVVFDRSLSTDQFSSGTQPPNAQRRTPDSTFSETFKEGVQEVFFPSELSLRMPGMNSEDYVFDNVSGNNFEYTLEASKSLRQKQGDSTMTYLNKGQFYPVTLKEGSSNEGIHHPISKVRSVIMVVFAEDKSREDQLRHWKYWHSRQHTAKQRCIDIADYKESFNTISNIEEIAYNAISFTWDINDEAKVFISVNCLSTDFSSQKGVKGLPLNIQIDTYSYNNRSNKPVHRAYCQIKVFCDKGAERKIRDEERKQSKRKVSDVKVQLLPSHKRTDITVFKPFLDLDTQPVLFIPDVHFTNLQRGSHVLSLPSEELEGEGSVLKRGPFGTEDDFGVPPPAKLTRTEEPKRVLLYVRKESEEVFDALMLKTPSLKGLMEAISDKYDVPHDKIGKIFKKCKKGILVNMDDNIVKHYSNEDTFQLQIEEAGGSYKLTLTEI
Protein: Tyrosine-protein phosphatase Lar-like (EC 3.1.3.48) (Protein-tyrosine phosphate 3) (Q9BMN8)
Organism: Caenorhabditis elegans
Function: Has a role in early neural and epidermal development; neuroblast movements during closure of the gastrulation cleft and epidermal morphogenesis. Vab-1 and ptp-3 may function redundantly within the same sets of neuronal precursors.
Subcellular location: Cell junction, adherens junction. Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Liprin-alpha
- Abnormal cell migration protein 21
- Cadherin-4
- ELKS/RAB6-interacting/CAST family member 2
- Ephrin receptor 1
- Liprin-beta homolog
- Nidogen
- Probable syndecan
- Ephrin-4
Sequence:
MIQFRNKNNSMNRIARHLRNVARRKGSSLLLFLMLSTVLVAAKEDDPARLVVRPDSSTVVDESKISFFCRADGNPLPSVIWRVNGKSITDHNRISIKSLATGLSTLRFERVSLDDNATVVSCSADNGVANPVVAEASLTVVPRDKVPIGFPQIELHPSLKSVEQGKTAYVSCRVRGDPRAKVLWLRDLIPLDIRADGRYSVSTIGNPGALMIQHAREEDQGKYECIARNTLGVAHSKAANLYVKVRRVPPYFSYKLERQYVVGVGGNINLTCVAVGYPMPRVFWKKTDLMVLDDPSTAPIGKNVLTLTHVESTENFTCVAVSALGNIEATTTVIAKELPPPPVNIVVSSVTSESVVITWKPPKYNEAINKYVVNYRLKYSEGRSSRGKTMETLENSLVIDGLVAFQTYEFTVRSAGPVGVGLESLPVEAQTKPSKPATAPVSPQARSLNRDSILVKWGPCEQPNGLITGYKVYYTNDLVTTPIREWKQHDAKSDEFMTTINGLEPDSRYFVRVIAQNSEGDSPLSTLVTVATRQGIPGQPPMLTVKALDSRRMQLTWDKPLYSSPVVGYTVRYNTSDGEKELTLTSPHEKHVVTGLHPDKYYYFRVAAYSDRGQGEFTEPMISKTIASIPLSSPTIVSAAATSSKSVEIRWKGPEQKKLNGVLTAYRINYFRLEDSKTANLESVEYDEDMDDSSSFLDRMSVVVPSDATSYVLSDLLPYSSYEITVAASTMDGYGPESSIRVVKTLEDVPSAPRNFNAELTSATSVKLTWDAPAAANGALLGYYVYLDRMVNGEPVVEKGSKKRIVMIRDSSKRYFELDSLDPNTEYSFRLNAFNRNGDGEFSERKSIITQGIPPEAPEIVSVSLDRDEPPVVARIEWKMPKMKPNETPIEKYNLWLRAQGYPDSYVKAKTVDGTDLSTTISGLWMGVVYDVLLAAENREGRSQNATETIATPVGSPDGEPIDVQYEVMKGKIVVSWRPPSEEKRNGNITSYKAILSAMDATADRYEQPVPAPSTSSTFEVNVRRAYLFKVAAATMKGIGPYSPVLTINPDPAALVGPPTNVRVEATSNSTAVVQWDFESQKADSFVVKYMHEPGNRMDTEKWKQLPVVSIDKENPKRFAVVSDLNAHKPYAFCVLAVKNNLTLNEQFNKVRVTNYMTNFQRQGPCSDPPTVLESVTPTYMVQNLRVLWKTSNSVQLTWEYNGPRNVGFYVNHTGRKDYVNHELQEKTMSTPGFGQDVDEKHREYLWTNLRPHMMYTIHVGVRTLPPGARKYWPQEVVTITDPTGPPFVDVPKLVDSSGTQPGQQMIRLTPATEEYGPISHYWIILVPANYSTEDVVNLDPIELEKATAEKRAQLARSLSVSPSKKLKRKASEVGDDSQSASYHPKEKRARRATVPGAYVTARLSADRVKQQYRNNQPFIVGDSQLYDGFTNYPLEHNLHYRLMMRAFAKNDVRTKDSFEQRAPMSEKLSRMYSDSVLTEPFTIKSALRGASQKSSPWVGACIAFLVLFSIVGMLICWWLRCNKKSAGRHPRHGSITKVALTGNIMNGGGGIPGETSKLLSTSNEYGRQIMNPYEQMNGNHHMESSMDLYPLPTSHSRSNGYAPVPVAIPSLPNNGNNMTTVSHPAVPIAELANHIERLRMNNNAGFQSEFESIETGQHFTWEHSSADMNKHKNRYANVAAYDHSRVVLSNVEGYPGMDYINANYVDGYDKPRSYIATQGPLPETFSDFWRMVWEEQSVTIVMLTNLEERSRVKCDQYWPSRGTATYGDIEVTLLESVHLAHYTMRTMRLKMVGEPEVREIKHLQYTAWPDHGVPDHPTPFLIFLKRVKTLNPNDAGPIISHCSAGIGRTGAFIVIDCMLERLRYDNTVDIYGCVTALRAQRSYMVQTEEQYIFIHDAVLDAVNSGSTEVPASRLHQHLHILSQPSADQLSGIDMEFRHLTTLKWTSNRCTVANLPVNRPKNRMLSAVPYDSNRVIMRLLPGADGSDYINASWIDGYKERGAYIATQAPTNETAADFWRAIWEHNSPIIAMLVRTNERGQEQCSDYWPLETGVQVGMLVVEPMAEYDMKHYHLREFRISDINTREVRTVRQFHFMEWPDVGKPHTADHFLDFVTQVHNTYAQFGCTGPITVHCCSGAGRTAVFIALSIILDRMRAEHVVDVFTTVKLLRTERQNMIQEPEQYHFLYLAAYEYLAAYDNFS
Protein: Starch-binding protein SusD (Starch-utilization system protein D) (Q8A1G2)
Organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Function: Major starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation.
Subcellular location: Cell outer membrane {ECO:0000305|PubMed:10986238, ECO:0000305|PubMed:9006015}; Lipid-anchor {ECO:0000305|PubMed:10986238, ECO:0000305|PubMed:9006015}.
Interaction partners:
- TonB-dependent receptor SusC
- Outer membrane protein SusE
- Glucan 1,4-alpha-glucosidase SusB
- Neopullulanase SusA
- Outer membrane protein SusF
- Alpha-amylase SusG
- SusC homolog
- Alpha-glucosidase
Sequence:
MKTKYIKQLFSAALIAVLSSGVTSCINDLDISPIDPQTGGSFDQQGVFVKGYAMLGVTGQKGIDGSPDLDGQDEGESGFYRTTFNCNELPTDECLWAWQENQDIPQLTSISWSPSSQRTEWVYVRLGYDITQYNFFLDQTEGMTDAETLRQRAEIRFLRALHYWYFLDLFGKAPFKEHFSNDLPVEKKGTELYTYIQNELNEIEADMYEPRQAPFGRADKAANWLLRARLYLNAGVYTGQTDYAKAEEYASKVIGSAYKLCTNYSELFMADNDENENAMQEIILPIRQDGVKTRNYGGSTYLVCGTRVAGMPRMGTTNGWSCIFARAAMVQKFFSNLEDVPMLPADVEIPTKGLDTDEQIDAFDAEHGIRTEDMIKAAGDDRALLYSGVGGGRRKIQTDAISGFTDGLSIVKWQNYRSDGKPVSHATYPDTDIPLFRLAEAYLTRAEAIFRQGGDATGDINELRKRANCTRKVQTVTEQELIDEWAREFYLEGRRRSDLVRFGMFTTNKYLWDWKGGAMNGTSVASYYNKYPIPVSDINNNRNMSQNEGYK
Protein: E3 ubiquitin protein ligase (EC 2.3.2.27) (C9JXC9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365038}.
Interaction partners:
Sequence:
MSGIGNKRAAGEPGTSMPPEKKAAVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESS
Protein: T. brucei spp.-specific protein (D6XFL1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- PDZ domain-containing protein
Sequence:
MSTTSSRTADDGLTELDGHVPGHFRLPTRGSQQPLDEDEDRALVSNGTGGDDGSCFSGDPHEVPHPEEPTQLNTRTLRRMQRAVAGGNIPLRADLLGGTNLRAQRTASAITAMSCTSGGMDAQSSGCDTSRAESKQKSNDVPLGRAHDSVANLSMASVESMCGSTVMPNILNRKNLDFFSAQLLSGGARLRQEFLSGEDVKPRGGEPSEMATADLPMSLWTEGGGSEHLSRFISQSDIGLNTEETRQGNAADSLSEATNPRTPANEEGMQSVMAEMGTFGSSSRIADPTTASEGSAQKK
Protein: Lysophosphatidic acid receptor 1 (LPA receptor 1) (LPA-1) (Lysophosphatidic acid receptor Edg-2) (P61794)
Organism: Rattus norvegicus (Rat)
Function: Receptor for lysophosphatidic acid (LPA). Plays a role in the reorganization of the actin cytoskeleton, cell migration, differentiation and proliferation, and thereby contributes to the responses to tissue damage and infectious agents. Activates downstream signaling cascades via the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Signaling inhibits adenylyl cyclase activity and decreases cellular cAMP levels. Signaling triggers an increase of cytoplasmic Ca(2+) levels. Activates RALA; this leads to the activation of phospholipase C (PLC) and the formation of inositol 1,4,5-trisphosphate. Signaling mediates activation of down-stream MAP kinases. Contributes to the regulation of cell shape. Promotes Rho-dependent reorganization of the actin cytoskeleton in neuronal cells and neurite retraction. Promotes the activation of Rho and the formation of actin stress fibers. Promotes formation of lamellipodia at the leading edge of migrating cells via activation of RAC1. Through its function as lysophosphatidic acid receptor, plays a role in chemotaxis and cell migration, including responses to injury and wounding. Plays a role in triggering inflammation in response to bacterial lipopolysaccharide (LPS) via its interaction with CD14. Promotes cell proliferation in response to lysophosphatidic acid. Required for normal skeleton development. May play a role in osteoblast differentiation. Required for normal brain development. Required for normal proliferation, survival and maturation of newly formed neurons in the adult dentate gyrus. Plays a role in pain perception and in the initiation of neuropathic pain.
Subcellular location: Cell surface {ECO:0000250|UniProtKB:P61793}. Cell membrane {ECO:0000250|UniProtKB:P61793}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q92633}. Endosome {ECO:0000250|UniProtKB:P61793, ECO:0000250|UniProtKB:Q92633}. Note=Prior to LPA treatment found predominantly at the cell surface. Internalized after LPA treatment. Colocalizes with RALA in endocytic vesicles after LPA treatment. {ECO:0000250|UniProtKB:P61793, ECO:0000250|UniProtKB:Q92633}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 4
- Lysophosphatidic acid receptor 6
- Lysophosphatidic acid receptor 5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 2
Sequence:
MAAASTSSPVISQPQFTAMNEQQCFYNESIAFFYNRSGKYLATEWNTVSKLVMGLGITVCVFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCICDIDHCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMSRHSSGPRRNRDTMMSLLKTVVIVLGAFIVCWTPGLVLLLLDVCCPQCDVLAYEKFFLLLAEFNSAMNPIIYSYRDKEMSATFRQILCCQRNENPNGPTEGSDRSASSLNHTILAGVHSNDHSVV
Protein: 5-hydroxytryptamine receptor 3B (5-HT3-B) (5-HT3B) (Serotonin receptor 3B) (Q9JHJ5)
Organism: Mus musculus (Mouse)
Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:O95264}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O95264}; Multi-pass membrane protein {ECO:0000255}. Note=Presumably retained within the endoplasmic reticulum unless complexed with HTR3A. {ECO:0000250|UniProtKB:O95264}.
Interaction partners:
- 5-hydroxytryptamine receptor 3A
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, kainate 4
- Noelin-3
- Glutamate receptor ionotropic, NMDA 3A
- Glutamate receptor 3
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor 4
- Glutamate receptor ionotropic, kainate 5
Sequence:
MILLWSCLLVAVVGILGTATPQPGNSSLHRLTRQLLQQYHKEVRPVYNWAEATTVYLDLCVHAVLDVDVQNQKLKTSVWYREVWNDEFLSWNSSLFDEIQEISLPLSALWAPDIIINEFVDVERSPDLPYVYVNSSGTIRNHKPIQVVSACSLQTYAFPFDIQNCSLTFNSILHTVEDIDLGFLRNREDIENDKRAFMNDSEWQLLSVSSTYHIRQSSAGDFAQIRFNVVIRRCPLAYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTNVLVGYTVFRVNMSDEVPRSAGCTPLIGVFFTVCMALLVLSLSKSILLIKFLYEERHSGQERPLMCLQGDSDAEESRLYLGAPRADVTESPVHQEHRVPSDTLKDFWFQFRSINNSLRTRDQIHQKEVEWLAILYRFDQLLFRIYLAVLGLYTVTLCSLWALWSRM
Protein: Protein MODIFIER OF SNC1 11 (Q9LZ08)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to the transfer of mature mRNA from the nucleus to the cytosol. May function before mRNAs enter nuclear pore and in the same mRNA export pathway as MOS3.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:21203492}.
Interaction partners:
- DEAD-box ATP-dependent RNA helicase 15
- THO complex subunit 4B
- THO complex subunit 3
- DEAD-box ATP-dependent RNA helicase 56
- THO complex subunit 2
- THO complex subunit 1
- Zinc finger CCCH domain-containing protein 17
- THO complex subunit 7A
- THO complex subunit 4D
- THO complex subunit 5A
Sequence:
MATNGEKVTATVVNGGGLSTGENPKKIVDLNTTELDRTDDILDGEVKGFSDSGEKKEETDSNGIGSTAGVDSGDISPVDDIQKKIRRAERFGVSVKLTEEEKRNSRAERFGTVAAAVVNGSEGTKKAEELKRKARADRFGVPSATSTTDKTEEEAKKKARLARFGKETKVDSAEENKRKARALRFSKEASADASSDLPEKQIIGKEAAVSGSAA
Protein: Sulfate/molybdate ABC transporter, permease protein (Q8TTZ4)
Organism: Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Sulfate/molybdate ABC transporter, ATP-binding protein
- Uncharacterized solute-binding protein MA_0280
- Molybdate ABC transporter, solute-binding protein
- Molybdenum ABC transporter, solute-binding protein
- Molybdenum ABC transporter, solute-binding protein
- Molybdate/tungstate import ATP-binding protein WtpC
- Phosphoadenosine phosphosulfate reductase
- Molybdenum-binding protein
Sequence:
MKAKNRKTRKFEPLTFVFSFLLLVLFLFIFLTLSNMIFEQITEDFSGLVKAAGNRSVISSIFLSLYAGFLATLLALLLGAPTGYILARFDFPGKRLVESIIDVPVVVPHTVAGIALLTVFGSRGLIGEPLESYIQFRDALPGIVVAMLFVSMPYLANSAREGFKSVDPRLENAARSLGAPLWKAFFFVTLPLSARYLLIGSVMTWARAISEFGAVVILAYYPMVGPTLIYDRFISYGLSASRPIAVLLILVTLSIFLVIRTLSAGWSIYDRD
Protein: Mitochondrial RNA binding protein (Q384M8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIRASIVKRMAPCTLFLNKGKVISWMSGRGFGFIEDDADKKQHFVHFSALQTETGGFRALTVGQEVEFEVASQDGRTRAENVTSPGGAKLPSGPRPPEGAGRGRGFGGGRGGRDFGGDRNSGRGRNDNQQGGQHQSFSDDF
Protein: Neuromedin-U receptor 2 (NMU-R2) (Q8BZ39)
Organism: Mus musculus (Mouse)
Function: Receptor for the neuromedin-U and neuromedin-S neuropeptides.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Neuromedin-U
- Neuromedin-S
- Neuromedin-U receptor 1
- Neurotensin/neuromedin N
- Neuropeptide S
Sequence:
MGKLENASWIHDSLMKYLNSTEEYLAYLCGPKRSDLSLPVSVVYALIFVVGVIGNLLVCLVIARHQTLKTPTNYYLFSLAVSDLLVLLLGMPLEVYELWHNYPFLFGPVGCYFKTALFETVCFASILSVTTVSIERYVAIVHPFRAKLESTRRRALRILSLVWSFSVVFSLPNTSIHGIKFQQFPNGSSVPGSATCTVTKPIWVYNFIIQATSFLFYILPMTLISVLYYLMGLRLKRDESLEADKVTVNIHRPSRKSVTKMLFVLVLVFAICWTPFHVDRLFFSFVDEWTESLAAVFNLIHVVSGVFFYLSSAVNPIIYNLLSRRFRAAFRNVVSPSCKWCHPQHRPQGPPAQKVIFLTECHLVELTEDAGPQFPCQSSIHNTQLTTVPCVEEVP