wanglab/gogpt-training-data huggingface dataset:
Protein: EF-hand domain-containing protein (G5EFB0)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MEQHLPKNDKKALSEWLERTEPYFMGIFCLECVLKVIAFGFALHKGSYLRSGWNIMDFIVVVSGVVTMLPFSPATQTANQPVDSVDLRTLRAVRVLRPLKLVSGIPSLQVVLKSILCAMAPLLQIGLLVLFAIIIFAIIGLEFYSGAFHSACYNERGEIENVSERPMPCTNKTSPMGVYNCDVKGTTCLQKWIGPNYGITSFDNIGFAMITVFQCITMEGWTTVMYYTNDSLGSTYNWAYFIPLIVLGSFFMLNLVLGVLSGEFAKERERVENRREFLKLRRQQQIERELNGYLEWILTAEEVILKEDRTTEEEKAAIMEARRRAANKKLKQASKQQSTETEEDFEEDEDEMEEEYVDEAERKKRGCCHSVGKFIKQLRIQIRIMVKTQIFYWSVITLVFLNTCCVASEHYGQPQWFTDFLKYAEFVFLGIFVVEMLLKLFAMGSRTYFASKFNRFDCVVIVGSAAEVIWAEVYGGSFGISVMRALRLLRIFKLTSYWVSLRNLVRSLMNSMRSIISLLFLLFLFILIFALLGMQLFGGRFNFPTMHPYTHFDTFPVALITVFQILTGEDWNEVMYLAIESQGGIYSGGWPYSIYFIVLVLFGNYTLLNVFLAIAVDNLANAQELTAAEEADEKANEIEEESEELDEQYQEGDHCTIDMEGKTAGDMCAVARAMDDLDEECEEEESPFGGPKPMVPYSSMFFLSPTNPFRVLIHSIVCTKYFEMMVMTVICLSSVSLAAEDPVDEENPRNKVLQYMDYCFTGVFACEMLLKLIDQGILLHPGSYCRDFWNILDGIVVTCALFAFGFAGTEGSAGKNLNTIKSLRVLRVLRPLKTIKRIPKLKAVFDCVVNSLKNVFNILIVYFLFQFIFAVIAVQLFNGKFFFCTDKNRKFANTCHGQFFVYDNQNDPPRVEQREWRLRPFNYDNTINAMLTLFVVTTGEGWPGIRQNSMDTTFEDQGPSPFFRVEVALFYVMFFIVFPFFFVNIFVALIIITFQEQGEAELSEGDLDKNQKQCIDFALNARPRSLFMPEDKNSTKYRIWRLVTSPPFEYFIMTMICCNTLILMMKYYNNPLFYEEILRLFNTALTAVFTVESILKILAFGVRNYFRDGWNRFDFVTVVGSITDALVTEFGGHFVSLGFLRLFRAARLIRLLQQGYTIRILLWTFVQSFKALPYVCLLIGMLFFIYAIVGMQVFGNIWLNAATEINRHNNFQSFFNAVILLFRCATGEGWQDIMMAAVQGKDCARAGSAEINFEKGQTCGSNVSYAYFTSFVFLSSFLMLNLFVAVIMDNFDYLTRDSSILGPHHLDEFIRVWADYDPAATGRIHYSEMYEMLRIMAPPVGFGKKCPYRLAYKHLIRMNMPVAEDGTVHFTTTLFALIRESLSIKMRPVEEMDEADEELRLTLKKIWPLKAKKNMVDLVVPPNHELCFQKLTVGKIYAGLLILENYRARKSGTERQSNDSVPPNFSENDEMRCSTGFRKIPTSHRSVDKDCLAEAYDRWSLQRKLPNRNILPTLHNRQRKPLR
Protein: AMP-binding protein (Q729U8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- DNA-binding protein
- Pyruvate:ferredoxin oxidoreductase
- Malate synthase G
- Phosphate acetyltransferase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha
- Acetate kinase
- Citramalate synthase
- Succinate--CoA ligase subunit alpha
- Pyruvate ferredoxin oxidoreductase, alpha subunit
- Acetate--CoA ligase
Sequence:
MDKLTFASYDEFLRVFSLDAPETFNFAFDVLDAMANETPDRLAIAHVDDAGVRRDYTFAWLADASARLANALKARGVRKGHRVMLVLHRRIEFWVSMLALHRLGAVAIPAPAQLTPKDIVFRVERAQVRAVIVDDGITDRIEAARPDCPTLSVLVQCGGTPLPDGWCDYEALCADASPSFPRPTAPDELACGEDPLLIFFSSGTTGMPKMVEHVHTYPLGHLVTGMYWHDLRPGDLHLTVADTGWGKAVWGKFYGQWMAGAAVFVYDFRGKFDPEALLDVVAKNGVTTFCAPPTVYRFLVRADLSRYDLSKLRHCTTAGELLNESVFHGWKAATGLSIYEGYGQTETTLQIATLSCMEAKPGSIGRPMPGWGITLLDHEGKECPTGEEGEICIRISDGLPVGLFRGYVEDAEKTASVMFDGYYHTGDKAWMDEDGYLWFLGRVDDLIKSSGYRIGPFEVESALVAHPAVVEAAVTGVPDPLRGQAVKATIVLAAGYEAGEVLTKELQDHVKKVTAPYKYPRIVEYVAELPKTISGKIKRAEIRQRDSEKSA
Protein: Ribonucleoside-diphosphate reductase subunit M2 B (EC 1.17.4.1) (TP53-inducible ribonucleotide reductase M2 B) (p53-inducible ribonucleotide reductase small subunit 2-like protein) (p53R2) (Q7LG56)
Organism: Homo sapiens (Human)
Function: Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage.
Subcellular location: Cytoplasm. Nucleus. Note=Translocates from cytoplasm to nucleus in response to DNA damage.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- Ribonucleoside-diphosphate reductase subunit M2
- Cellular tumor antigen p53
- DNA polymerase subunit gamma-1
- Adenylate kinase 9
- Thymidylate kinase
- GTP:AMP phosphotransferase AK3, mitochondrial
- Guanylate kinase
- DNA polymerase subunit gamma-2
- Deoxyguanosine kinase, mitochondrial
Sequence:
MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFSKVFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
Protein: Retinol-binding protein 3 (F1Q9N9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAQALVLLVSLLFFSNVAHCNFSPTLIADMAKIFMDNYCSPEKLTGMEEAIDAASSNTEILSISDPTMLANVLTDGVKKTISDSRVKVTYEPDLILAAPPAMPDIPLEHLAAMIKGTVKVEILEGNIGYLKIQHIIGEEMAQKVGPLLLEYIWDKILPTSAMILDFRSTVTGELSGIPYIVSYFTDPEPLIHIDSVYDRTADLTIELWSMPTLLGKRYGTSKPLIILTSKDTLGIAEDVAYCLKNLKRATIVGENTAGGTVKMSKMKVGDTDFYVTVPVAKSINPITGKSWEINGVAPDVDVAAEDALDAAIAIIKLRAEIPALAQAAATLIADNYAFPSIGEHVAEKLEAVVAGGEYNLISTKEDLEERLSEDLLKLSEDKCLKTTSNIPALPPMNPTPEMFIALIKSSFQTDVFENNIGYLRFDMFGDFEHVATIAQIIVEHVWNKVVDTDALIIDLRNNIGGHASSIAGFCSYFFDADKQIVLDHIYDRPSNTTRDLQTLEQLTGRRYGSKKSVVILTSGVTAGAAEEFVFIMKRLGRAMIIGETTHGGCQPPETFAVGESDIFLSIPISHSDTAQGPSWEGAGIAPHIPVPAGAALDTAKGMLNKHFSGQK
Protein: Thrombospondin-related anonymous protein (Q76NM2)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Small ribosomal subunit protein eS30
- Circumsporozoite protein
- 40S ribosomal protein S15A, putative
Sequence:
MNHLGNVKYLVIVFLIFFDLFLVNGRDVQNNIVDEIKYREEVCNDEVDLYLLMDCSGSIRRHNWVNHAVPLAMKLIQQLNLNDNAIHLYASVFSNNAREIIRLHSDASKNKEKALIIIKSLLSTNLPYGKTNLTDALLQVRKHLNDRINRENANQLVVILTDGIPDSIQDSLKESRKLSDRGVKIAVFGIGQGINVAFNRFLVGCHPSDGKCNLYADSAWENVKNVIGPFMKAVCVEVEKTASCGVWDEWSPCSVTCGKGTRSRKREILHEGCTSELQEQCEEERCLPKREPLDVPDEPEDDQPRPRGDNFAVEKPNENIIDNNPQEPSPNPEEGKGENPNGFDLDENPENPPNPPNPPNPPNPPNPPNPDIPEQEPNIPEDSEKEVPSDVPKNPEDDREENFDIPKKPENKHDNQNNLPNDKSDRYIPYSPLSPKVLDNERKQSDPQSQDNNGNRHVPNSEDRETRPHGRNNENRSYNRKHNNTPKHPEREEHEKPDNNKKKAGSDNKYKIAGGIAGGLALLACAGLAYKFVVPGAATPYAGEPAPFDETLGEEDKDLDEPEQFRLPEENEWN
Protein: 3CxxC-type domain-containing protein (O45925)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MFAYDRLALDLAVFNLKDVDSGNSSSSERSSPPTRIMSQAQNINDESGSSGYGSPTRTPLASPSNDIFSSVLPLQVQRAFSAQSPEEITRHFGVSPSPQAVKPVPEVQQQREQAQVSQTSAQGLAAVDGFSMAEIAGFAELLSSPKKTPPPRYQCHICYATGHHYISDCPQRFNTPYDELTPYQGRKKCYGEFTCQLCKRKWNSQNSVANEPQSCIKCHVPVFPHKQLPVEKAVTLGLIKAQNVTKVAPIGHGRPPARKHEEISRRH
Protein: Cyclin D binding myb like transcription factor 1 (E7EPA0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTVEEDSDTVTVETVNSVTLTQDTEGNLILHCPQNEADEIDSEDSIEPPHKRLCLSSEDDQSIDDSTPCISVVALPLSENDQSFEVTMTATTEVADDEVTEGTVTQIQILQNEQLDEISPLGNEEVSAVSQAWFTTKEDKDSLTNKGHKWKQGMWSKEEIDILMNNIERYLKARGIKDATEIIFEMSKDERKDFYRTIAWGLNRPLFAVYRRVLRMYDDRNHVGKYTPEEIEKLKELRIKHGNDWATIGAALGRSASSVKDRCRLMKDTCNTGKWTEEEEKRLAEVVHELTSTEPGDIVTQGVSWAAVAERVGTRSEKQCRSKWLNYLNWKQSGGTEWTKEDEINLILRIAELDVADENDINWDLLAEGWSSVRSPQWLRSKWWTIKRQIANHKDVSFPASADSPATVDSETITLNSGTLQTFEILPSFHLQPTGTPGTYLLQTSSSQGLPLTLTASPTVTLTAAAPASPEQIIVHALSPEHLLNTSDNVTVQCHTPRVIIQTVATEDITSSISQAELTVDSDIQSSDFPEPPDALEADTFPDEIHHPKMTVEPSFNDAHVSKFSDQNSTELMNSVMVRTEEEISDTDLKQEESPSDLASAYVTEGLESPTIEEQVDQTIDDETILIVPSPHGFIQASDVIDTESVLPLTTLTDPILQHHQEESNIIGSSLGSPVSEDSKDVEDLVNCH
Protein: Probable alpha,alpha-trehalose-phosphate synthase [UDP-forming] 11 (EC 2.4.1.15) (Trehalose-6-phosphate synthase 11) (AtTPS11) (Q9ZV48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Alkaline-phosphatase-like family protein
- Terpenoid synthase 3, chloroplastic
- Putative inactive
- S-
- Trehalase
- Probable trehalose-phosphate phosphatase H
- Probable trehalose-phosphate phosphatase E
- Probable trehalose-phosphate phosphatase G
- Trehalose-phosphate phosphatase A
Sequence:
MSPESWKDQLSLVSADDYRIMGRNRIPNAVTKLSGLETDDPNGGAWVTKPKRIVVSNQLPLRAHRDISSNKWCFEFDNDSLYLQLKDGFPPETEVVYVGSLNADVLPSEQEDVSQFLLEKFQCVPTFLPSDLLNKYYHGFCKHYLWPIFHYLLPMTQAQGSLFDRSNWRAYTTVNKIFADKIFEVLNPDDDYVWIHDYHLMILPTFLRNRFHRIKLGIFLHSPFPSSEIYRTLPVRDEILKGFLNCDLVGFHTFDYARHFLSCCSRMLGLDYESKRGYIGLEYFGRTVSIKILPVGIHMGQIESIKASEKTAEKVKRLRERFKGNIVMLGVDDLDMFKGISLKFWAMGQLLEQNEELRGKVVLVQITNPARSSGKDVQDVEKQINLIADEINSKFGRPGGYKPIVFINGPVSTLDKVAYYAISECVVVNAVRDGMNLVPYKYTVTRQGSPALDAALGFGEDDVRKSVIIVSEFIGCSPSLSGAIRVNPWNIDAVTNAMSSAMTMSDKEKNLRHQKHHKYISSHNVAYWARSYDQDLQRACKDHYNKRFWGVGFGLFFKVVALDPNFRRLCGETIVPAYRRSSSRLILLDYDGTMMDQDTLDKRPSDDLISLLNRLCDDPSNLVFIVSGRGKDPLSKWFDSCPNLGISAEHGYFTRWNSNSPWETSELPADLSWKKIAKPVMNHYMEATDGSFIEEKESAMVWHHQEADHSFGSWQAKELLDHLESVLTNEPVVVKRGQHIVEVKPQGVSKGKVVEHLIATMRNTKGKRPDFLLCIGDDRSDEDMFDSIVKHQDVSSIGLEEVFACTVGQKPSKAKYYLDDTPSVIKMLEWLASASDGSKHEQQKKQSKFTFQQPMGQCRKKA
Protein: Galactokinase 1 (Q5RKH2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Galactose-1-phosphate uridylyltransferase
- Galactose mutarotase
- UDP-glucose 4-epimerase
- Interleukin-11 receptor subunit alpha
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- Xylulose kinase
- Phosphoglucomutase-1
- UTP--glucose-1-phosphate uridylyltransferase
- Mannose-6-phosphate isomerase
Sequence:
MAAWRPPRVEELLAEARRAFMEEFGAEPELAVSAPGRVNLIGEHTDYNQGLVLPMALELVTVMVGSPRTDGLVSLLTTSKDADEPQRLQFPLPSAQWSLEPGIPQWANYVKGVIQYYPASPLCGFSAVVVSSVPLGGGLSSSASLEVATYAFLQQLCPDSGSIAARAQVCQRAEHSFAGVPCGIMDQLIALLGQKGYALLIDCRSLETSLVPLSDPKLTVLITNSNVRHSLASSEYPIRRRQCEEVAQALGKESLREVRMEELEAGRELMSKEGFRRARHVVSEIRRTAQGAAALSRGDYKAFGRLMVESHYSLRDDYEVSCPELDLLVEAALSVPGVYGSRMTGGGFGGCTVTLLEASVAPLVMHHIQEQYSGTATFYLTQAADGAQVLSL
Protein: UDP-glycosyltransferase 79 (OsUGT79) (EC 2.4.1.-) (Deoxynivalenol-UDP-glucosyltransferase) (Q7XT97)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the detoxification of the Fusarium mycotoxin deoxynivalenol by the transfer of glucose from UDP-D-glucose to the hydroxyl group at C-3, forming deoxynivalenol-3-O-beta-D-glucoside.
Interaction partners:
Sequence:
MGSMSTPAASANGGQVLLLPFPAAQGHTNPMLQFGRRLAYHGLRPTLVTTRYVLSTTPPPGDPFRVAAISDGFDDASGMAALPDPGEYLRTLEAHGARTLAELLLSEARAGRPARVLVYDPHLPWARRVARAAGVATAAFLSQPCAVDLIYGEVCARRLALPVTPTDARGLYARGVLGVELGPDDVPPFVAAPELTPAFCEQSIEQFAGLEDDDDVLVNSFSDLEPKEAAYMESTWRAKTIGPSLPSFYLDDGRLRSNTAYGFNLFRSTVPCMEWLDKQPPRSVVLVSYGTVSTFDVAKLEELGNGLCNSGKPFLWVVRSNEEHKLSVQLRKKCEKRGLIVPFCPQLEVLAHKATGCFLSHCGWNSTLEAIVNGVPLVAMPHWADQPTISKYVESLWGMGVRVQLDKSGILQREEVERCIREVMDGDRKEDYRRNATRLMKKAKESMQEGGSSDKNIAEFAAKYSN
Protein: Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase) (O00418)
Organism: Homo sapiens (Human)
Function: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.
Interaction partners:
- Elongation factor 2
- Calmodulin-1
- Ribosomal protein S6 kinase beta-1
- Calmodulin-1
- Protein kinase C alpha type
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit gamma-2
- Protein kinase C beta type
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- Protein kinase C gamma type
Sequence:
MADEDLIFRLEGVDGGQSPRAGHDGDSDGDSDDEEGYFICPITDDPSSNQNVNSKVNKYYSNLTKSERYSSSGSPANSFHFKEAWKHAIQKAKHMPDPWAEFHLEDIATERATRHRYNAVTGEWLDDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRDVYFEDVRLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRPGKPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTETGTDFGDGNLGVRGMALFFYSHACNRICESMGLAPFDLSPRERDAVNQNTKLLQSAKTILRGTEEKCGSPQVRTLSGSRPPLLRPLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFSDLDNMASRDHDHLDNHRESENSGDSGYPSEKRGELDDPEPREHGHSYSNRKYESDEDSLGSSGRVCVEKWNLLNSSRLHLPRASAVALEVQRLNALDLEKKIGKSILGKVHLAMVRYHEGGRFCEKGEEWDQESAVFHLEHAANLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDGMQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE
Protein: Endoplasmic reticulum membrane protein 65 (O60067)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in membrane protein folding.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein slp1
Sequence:
MGSNTSPGQADPLESENESSLTSRFLPNKRDGGKDNESVIPEKEEPDLNEPVLAVPLPKSRYALTKRSSSSEYPRRSASTSAKKNVIPITRSYSTTFFSKTNDQPTVTGNQDKPISRLRASKLQIQNFWNYICFELLANDTVPANPIKEKHVENFLATPYAIEKTFLFGWFVSVDSFLYIFTLFPIRVLISFFTLSRCIFQGLFSTFFHRNSSPNRSLPRSRKIDLLKLLLIFSTSILIRKIDVSRLYHIIRAQASIRFYVLYNVLEIADRLCCALGQDVLDCLFSNHILSFNFWNPAGWMTFFYYFAISLAYMVLHTLVLLYQIITLNVTVNSYSNAVLALLMSNQLVEIKGAVFKKFEKENLFQLTCSDVVERFQITIMVIIIFLRNLAELYTTSSLDQPLLTFKRLKTLLAPFFWVIGSELFVDWLKHAFIIKFNYIKPSIYSRFTDVLCHDYVASGAQLTQTVTGCSQQVARRMGLPVLPLVCVFIRTSMQTWSMFRSTHSMKQEIAKSIGTIFPTKDNYVYYLPNKEANTYNAGKEASWETLLLSVVRGKSGIAFLFFMAIMLKLLLGKAILAITQSRYESMQQREEKINSWERERKANNFFRGHIEIDKKTKDFLNNSKDDLPVPKSPLLTLERYAMHSKRIW
Protein: Protein peanut (P40797)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in cytokinesis and possibly cellularization. Also acts as an enhancer of the sina gene, thus having a role in photoreceptor development. May be involved in p53-dependent apoptosis.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:8181057}; Peripheral membrane protein {ECO:0000269|PubMed:8181057}. Cleavage furrow {ECO:0000269|PubMed:8181057}. Cytoplasm, cell cortex {ECO:0000269|PubMed:15818553}. Note=Localized to the cleavage furrow of dividing cells during cytokinesis and to the intercellular bridge connecting postmitotic daughter cells. Equally found on the cell surfaces of the embryonic central nervous system and on the apical membranes of developing photoreceptor cells in the eye imaginal disk (PubMed:8181057). Colocalizes with hil at the cell cortex (PubMed:15818553). {ECO:0000269|PubMed:15818553, ECO:0000269|PubMed:8181057}.
Interaction partners:
- Septin-2
- Septin-1
- Septin
- Anillin
- Origin recognition complex subunit 6
- Septin-interacting protein 1
- Septin
Sequence:
MNSPRSNAVNGGSGGAISALPSTLAQLALRDKQQAASASASSATNGSSGSESLVGVGGRPPNQPPSVPVAASGKLDTSGGGASNGDSNKLTHDLQEKEHQQAQKPQKPPLPVRQKPMEIAGYVGFANLPNQVYRKAVKRGFEFTLMVVGASGLGKSTLINSMFLSDIYNAEQYPGPSLRKKKTVAVEATKVMLKENGVNLTLTVVDTPGFGDAVDNSNCWVPILEYVDSKYEEYLTAESRVYRKTISDSRVHCCLYFIAPSGHGLLPLDIACMQSLSDKVNLVPVIAKADTMTPDEVHLFKKQILNEIAQHKIKIYDFPATLEDAAEEAKTTQNLRSRVPFAVVGANTIIEQDGKKVRGRRYPWGLVEVENLTHCDFIALRNMVIRTHLQDLKDVTNNVHYENYRCRKLSELGLVDGKARLSNKNPLTQMEEEKREHEQKMKKMEAEMEQVFDMKVKEKMQKLRDSELELARRHEERKKALELQIRELEEKRREFEREKKEWEDVNHVTLEELKRRSLGANSSTDNVDGKKEKKKKGLF
Protein: Developmentally regulated protein (Q38EX9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLVHLDKWWKSKAHRRIKGARGARFASLKFHVLFLGSVICFVEWVMRSTDCYEDPSYHIAPPPVAPPPPLAASIGYALSREMPHLRVMELEKGIPSHLPKTRGVDYVLLRSEGRFV
Protein: Granzyme B (EC 3.4.21.79) (Fragmentin) (Natural killer cell protease 1) (RNKP-1) (P18291)
Organism: Rattus norvegicus (Rat)
Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (By similarity). It cleaves after Asp. Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death (By similarity). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution (By similarity). Cleaves caspase-3 and -9 (CASP3 and CASP9, respectively) to give rise to active enzymes mediating apoptosis. Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:9765264}. Cytolytic granule {ECO:0000250|UniProtKB:P10144}. Note=Delivered into the target cell by perforin. {ECO:0000250|UniProtKB:P10144}.
Interaction partners:
- Caspase-3
- Caspase-8
- Poly [ADP-ribose] polymerase 1
- BH3-interacting domain death agonist
- Interferon gamma
- Caspase 7, isoform CRA_c
- DNA fragmentation factor subunit alpha.
- Perforin-1
- Tubulin alpha chain
- Tubulin alpha-8 chain
Sequence:
MKLLLLLLSFSLAPKTEAGEIIGGHEAKPHSRPYMAYLQIMDEYSGSKKCGGFLIREDFVLTAAHCSGSKINVTLGAHNIKEQEKMQQIIPVVKIIPHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKCESYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKKVAAGIVSYGQNDGSTPRAFTKVSTFLSWIKKTMKKS
Protein: p44-36 outer membrane protein (Q2GIU4)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MRSRSKLFLGSVMMSMAIVMAGNDVRAHDDVSALETGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDKLTAALAKTSGKDFVQFAKAVGVSHPSIDGKVCKTKKEGSGSNQFGKYAGETANGSSASKAEVAVCGAAGNHSSGGSTVAETLKNFVSATLKGDGSKNWPTSTIAASNGGTPTPVTNDNAKAVAKDLVQELTPEEKTIVAGLLAKTIEGGEVVEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGIHYTNHL
Protein: methylmalonate-semialdehyde dehydrogenase (CoA acylating) (EC 1.2.1.27) (A0A024R6G4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAALLAAAAVRARILQVSSKVKSSPTWYSASSFSSSVPTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSSPAVVMPTMGR
Protein: Serine/threonine-protein kinase flr-4 (EC 2.7.11.1) (Fluoride-resistant protein 4) (Q9NLA1)
Organism: Caenorhabditis elegans
Function: Probable serine-threonine protein kinase involved in the control of defecation rhythms. Required to increase the length of defecation cycle period. Acts in a cell-functional rather than developmental aspect in the regulation of defecation rhythms.
Subcellular location: Membrane {ECO:0000305|PubMed:15647385}; Multi-pass membrane protein {ECO:0000305|PubMed:15647385}.
Interaction partners:
- Bursicon
- Glycoprotein Hormone
- FLR-1
- CYtochrome P450 family
- CYtochrome P450 family
- CYtochrome P450 family
- Large ribosomal subunit protein uL2 C-terminal domain-containing protein
Sequence:
MPINYNRNAVELKLSSQLLQWLDQRLPLGDPMRIPSIDSYKYIQDLGKGRFGTVCKFSNGNTFETVKKVDLTIFNHWTQSETKVSNRLDTFLYEFRHLHKVTNDNNRIVNFLGIYADSNQMYIMSEYLPRGSVKDLLVKETLGEDTAIKYLMETVEALDYLHNLSPPVIHRDIKAANLLITSNDSIKLANFGLVRDLAVDGFGIAIASEITLDFRATLLYVAPEVLSSALGPGNRNAYELPADIWALGCTFIEMLLKRPPHFEYFGHIDEIPKVLLGYAKSEDGKVLPYTSEVLVPSSSNCVQKIVDLVFIKSPEHRPNTHKLRIQIKKILDDDSESEEETDISHPISNSNTDSSTAISHNHSNDRKVGRAGTCLPIESMEYAAVRKELKKRSKPKSNNIMQIFVASGYYLSRILYFLNILTRSICYLLLFLSLGITALGSFLLISYFVVRFVRYLIAINCNCDLMQPQYLIISGILIVLMFALLFSCCMVALGEYKFRMANQTLDGSKFYLPRPQKSAVLCGITVITGKEDAKDTAQNMEEEIHLTPSVRRNHDDYYYDESSGPANEEN
Protein: Putative ATP-dependent RNA helicase ste13 (EC 3.6.4.13) (Q09181)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export (By similarity).
Subcellular location: Cytoplasm, P-body {ECO:0000250}. Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. {ECO:0000250}.
Interaction partners:
- Enhancer of mRNA-decapping protein 3
- LSM1-LSM7 complex subunit lsm1
- Protein sum2
- mRNA decapping complex subunit 2
- General negative regulator of transcription subunit 1
- LSM complex subunit lsm7
- Deadenylation-dependent mRNA-decapping factor pdc2
- mRNA-decapping enzyme subunit 1
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- General negative regulator of transcription subunit 3
Sequence:
MAESLIQKLENANLNDRESFKGQMKAQPVDMRPKTEDVTKTRGTEFEDYYLKRELLMGIFEAGFERPSPIQEESIPIALSGRDILARAKNGTGKTAAFVIPSLEKVDTKKSKIQTLILVPTRELALQTSQVCKTLGKHMNVKVMVTTGGTTLRDDIIRLNDTVHIVVGTPGRVLDLAGKGVADFSECTTFVMDEADKLLSPEFTPIIEQLLSYFPKNRQISLYSATFPLIVKNFMDKHLNKPYEINLMDELTLRGVTQYYAFVDESQKVHCLNTLFSKLQINQSIIFCNSTNRVELLAKKITELGYSCFYSHAKMLQSHRNRVFHNFRNGVCRNLVCSDLLTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHRGLAISFISWADRFNLYRIENELGTEIQPIPPSIDPSLYVFPNGDYQIPRPLTASADQVLAAQQAKGQEGYHNRPNNNRGGHPRGGGNRGGYRQSNRQPRYRGQQKAD
Protein: Interleukin-27 subunit beta (IL-27 subunit beta) (IL-27B) (Epstein-Barr virus-induced gene 3 protein) (EBV-induced gene 3 protein) (Q14213)
Organism: Homo sapiens (Human)
Function: Associates with IL27 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines.
Subcellular location: Secreted {ECO:0000269|PubMed:9342359}.
Interaction partners:
- Interleukin-27 subunit alpha
- Interleukin-27 receptor subunit alpha
- Interleukin-12 subunit alpha
- Interleukin-6 receptor subunit beta
- Calnexin
- Probable non-functional immunoglobulin heavy variable 3-16
- Immunoglobulin heavy variable 3-43D
- Signal transducer and activator of transcription 1-alpha/beta
- Signal transducer and activator of transcription 4
- Interleukin-12 receptor subunit beta-2
Sequence:
MTPQLLLALVLWASCPPCSGRKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSFIATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVLNVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK
Protein: N6-succino-2-amino-2'-deoxyadenylate synthase (EC 6.3.4.25) (2-amino-2'-deoxyadenylo-succinate synthase) (PurZ) (A0A2H5BHJ6)
Organism: Acinetobacter phage SH-Ab 15497
Function: Involved in the synthesis of the atypical nucleotide dZTP (2-amino-2'-deoxyadenosine-5'-triphosphate). Catalyzes the condensation of aspartate with deoxyguanylate into dSMP (N6-succino-2-amino-2'-deoxyadenylate), which undergoes defumarylation and phosphorylation respectively by host PurB and guanylate/nucleoside diphosphate kinases to give dZTP. dZTP is integrated into the viral genome instead of adenine by the viral DNA polymerase. This Z-base probably completely replaces adenosine and forms a triple bond to the opposite T-base. The resulting non-standard viral DNA is called Z-genome. The chemically modified DNA is probably harder for the host bacteria to digest with nucleases or restriction enzymes (Probable).
Interaction partners:
Sequence:
MKKATVICDMQFGSTGKGLIAGFLAERDQPDVVVTAWSANAGHTYINREGRKWVHCMLANGIVSPKLKAVLIGGGSQMSIPTLISEIMGSLDILQGKSILIHENACIIQQRHVEEEAGPMTKIGSTKKGCGAAMMEKIRRNPESKIVAKDFIDDGLEIPDFKLDGTVGFKDISRHFEELGVCIKVVSNEVYLAVLHKAERVQVEGAQGFSLGLHNGFYPYVTSRECTPAQICSDCNVPISMVDKVVGTMRTYPIRVANRFDDEGKMVGWSGPCYSDQTELTWEQMGVTPEKTTVTKLTRRIFSFSRMQTRQAMLVCMPDEIFLNFANYCASEDELASIIEVISNEGGDVSYIGWGDSAAHIETTLEGDWSDDTNPLFNQYNKSSNIA