wanglab/gogpt-training-data huggingface dataset:
Protein: Central pair complex 1 (Q6J4H1)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Interaction partners:
- adenylate kinase
- EF-hand domain-containing protein
- PF6 protein
- Sperm-associated antigen 6
- Central apparatus associated protein C1a-32
- Flagellar associated protein 174
- Cilia- and flagella-associated protein 46
- Central apparatus associated protein C1a-34
- Fibronectin type-III domain-containing protein
- Central apparatus associated protein C1a-86
Sequence:
MSELLRKWLADELGLPVTDNLEQDFASGFLFAQLFSKYNLQPDVDHFDTKRMPDAMINNYTRLQPTFTNLGVHMDTRVANMLIREESGVAPRLLYSIKQNLGSIQKTLTKHMHTGNLGRTLGASVSPSRGLLEAQKHNTSKEKFESGTHRHFEDTLRSQAANPNAIMESMALAKFTEEGIRQQREALGGLLRDRAQHTAQRDTFRANQMDKLGSARSDKAQRLERDEAVHAALLKRKEEMEREELRVELALSEKARRRKLEELHHAALDVHGGIDAFEINMKRLVRGDQGQEGEEVVAPPAGRTPLEHMEQLKSRAAATAKLLEDTAAYMRGVKDARADEVASKREREARRRKMVVEQQAAASSAERKAQMESLLTALQRQSAEEQRLAARLWQVSQEKEVMRENRLLRERQYAERRERDWEETLRREVELHRSMRETYEAEAALEMEAWRAAQQARAEAKSAKHAAFARDVAYQLVSLAERSAEYRAATGNLVPRREWREWLTMFVAGDPQLGPPAPPVGAEAEAAEAEVREACLRVGRALVDDYLACAGDWLRVDGPIGHDELLGQIVGELAVLARQPPPQPELPAIETLPLRLAVLGAPFAGKTCVAQELSRRYKLRVLEPEALVAEAMAAAQEFEAATGVPADQVPEAAPQEDGDAAAAAELQAGSASRPGTAATAAAGPSAKARLGAQIAAALKAGGDVPDEALVGLVVLGMKESKDWAPPVEVDPKAKGKAAPKPAAPPAGSKSAGAPAAPHPDTGRGFVVDGFPRTAAQAVLLERMLTGLDLDSEQALIDAASVIAPPPASALPQVARPLVSGLDAVVVCGLADPELALKRALGRRLDPQTGRVYHLEFDPPPSNDPGLSARLQEVADASNDAQQIQHRLMSQAELAGPLDDWLRRFSRLRRPVDGSGPLGEVLASAGDIAEGLLRAKAAAASCRSAAEAAHKARASAEQAHEFAELAQAAAESAARELLTAKKAEIQAAALLAGGKNPDPAATEVLKAQAAAKCAEQLKVARGAVADANGHAERAANSAAAASEAVDRAHKSLGDAEISAHAETEAAAAATEAEKAARGAQEAASKALAAKEAAAVAAAEAERFAAASDLPADATVNLGHRPDAHATGAHAVSTSGGAPASGNGTASGEAAAPAPEPLVRELAASLHEEWKTLETGYLEGLALGFASLAEQHAEAQRHFAGLRGRFQDLLQRPDEKPALVARFLTTFNAVEADLRGNKEARGELLLRAEELRDALWALCDKKMEEAEAQRAAVASDTFVPDHCATLAQQFVALAQVEGDRFAAALNFLRSHAHSKWLPLFPPGREPPSLALPDVAAPDLLSGAVPPELKDKIDPKAKTSVPMPAWVASLEQRAAPLALATKLLLALAKTTATSWEPGAEDPKKAKKDAAAKAGAGAKGKGKGGEEEAPEADPRVVEGLNGELLDGCGRELAILEARLQLLAERCLGQMDEMAALASGTVSRLGEWVRERYRSECAAVAALDKVCKAAAAAGQPLPHDLRLQDEFLLLDEGSLLVQEDAALPRPYPREGVPAGGLLSTKQLGALTAAFLSAAPSGYMRLQEAADMLCRLAAEGALPEPWRGTSVASMLGALRLYDPLHSTYLDWREFVAHLVVASFPLIARADCAEMADQIDICAEVDKDHDGLLSQEEWSTAELWFQYRAAQPGALQAEVPEASGEAGAEAGTGSGSESDAGPRSTLLADGEKWPEADTVSRAGTPPPDDEQYDSPAALKQVLWALFSAPAADGTPRLDYRACLLYLCADRDAFAGIKKAFSVATANISNNARASADQVFRIAYPLGAEPGQELHRSPFSKVDVAAVVKAVWESRAGQPAVAAGAAGTGPAGARGATPPQAATAAARGASAKNTAGAAAPAASGEASVTAEQLMYSAGGERFVKRMLERYAWKDAFVATRL
Protein: Zinc finger protein 16 (Zinc finger protein KOX9) (P17020)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator. Promotes cell proliferation by facilitating the cell cycle phase transition from the S to G2/M phase. Involved in both the hemin- and phorbol myristate acetate (PMA)-induced erythroid and megakaryocytic differentiation, respectively. Also plays a role as an inhibitor of cell apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16628192}.
Interaction partners:
- NADPH oxidase 4
Sequence:
MPSLRTRREEAEMELSVPGPSPWTPAAQARVRDAPAVTHPGSAACGTPCCSDTELEAICPHYQQPDCDTRTEDKEFLHKEDIHEDLESQAEISENYAGDVSQVPELGDLCDDVSERDWGVPEGRRLPQSLSQEGDFTPAAMGLLRGPLGEKDLDCNGFDSRFSLSPNLMACQEIPTEERPHPYDMGGQSFQHSVDLTGHEGVPTAESPLICNECGKTFQGNPDLIQRQIVHTGEASFMCDDCGKTFSQNSVLKNRHRSHMSEKAYQCSECGKAFRGHSDFSRHQSHHSSERPYMCNECGKAFSQNSSLKKHQKSHMSEKPYECNECGKAFRRSSNLIQHQRIHSGEKPYVCSECGKAFRRSSNLIKHHRTHTGEKPFECGECGKAFSQSAHLRKHQRVHTGEKPYECNDCGKPFSRVSNLIKHHRVHTGEKPYKCSDCGKAFSQSSSLIQHRRIHTGEKPHVCNVCGKAFSYSSVLRKHQIIHTGEKPYRCSVCGKAFSHSSALIQHQGVHTGDKPYACHECGKTFGRSSNLILHQRVHTGEKPYECTECGKTFSQSSTLIQHQRIHNGLKPHECNQCGKAFNRSSNLIHHQKVHTGEKPYTCVECGKGFSQSSHLIQHQIIHTGERPYKCSECGKAFSQRSVLIQHQRIHTGVKPYDCAACGKAFSQRSKLIKHQLIHTRE
Protein: Transmembrane protein 131 homolog (Q18264)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:32095531}.
Interaction partners:
Sequence:
MVPSIHKTSNRYRTIYFFLISLLITSTFADQQAWPLPEEVSASQLHEIPVLHTAFVQIGEELHYLNHPIRPENVHQLPVYDSIKGVCEGNCPKEANKNHATKTFNVLKLSGKGKLPMEMDPPMMDFGQNSVGTAQKRKIYIRNMRNEQIFLDAVVVNSIEFQASYFEQYKLEPHGVTSLEVVFLPREIGKRSTIVHFYTSVGVFTYKMQGNCDSNPYRISPFTGYRLPMNSSISKPIVIFNPYAYTMRITEIGTSGGNAHIELPHEVDSKLAEEPLQYWDIRPYQSKQIATLVLVGATSENSTVFVRIGSEIYLSSEHRKPNTDIYLTVPIEVLKRRGVYATDEILDFGLIRQGMKSEAKVFSVVQYQIGGRLEFETLYVEKGDHTAIYMEFASHPPIIVYPPTKGSVTLGPKADLVKVYLEGNRVQMSPQQQMKHISGHIIAVSRGGNYNVSIPYRADVFRGDLLPIGNDLSIQEDLRPPHQRIIRIENQLPFDVAIFNITLAPELVSHFSVRLIDRTALIRSGHISPVFVLKYNKKLPPTFDNSTIYLHTNVSTFNLSLSTYTGRMNVELISVDKNSFDFGFVERNDTRTIRFVVWNHNRAEMRLKNLAVPHRSAYRLYEVGVKSIGNFSDVRNDERLEYVEATDVDIPPMKGKIFDLELKVPSDGVVRNGNIIFETDLESKIFGVTYQVSTGSLQSIPEEICFGQTFPSKLVYRTLQVFNSFDEDMTVTRLTTLNEDPRFFFEGFDPKNPPVLRSGRLTNLGRVMFSPSAPCEHDYCYLGLPLGSSDGAWFTHGLTLPSNLPEIDSYLYKQLRKKYDALVNSGKHHINTTIILDTDKAKNIKIKTSAELVWPRLLTRNSIHFPLTALGNFTIVNLTLANPTNVPVAIQVIPLVIYPDAESLVELMRPNLVSELTDHVEMNETLMFSLRDTELFTLKSDSPVPKLREAFEYHLNHEMPRYNNEINIPRFTLSMILKPHMKIRLRLGFLPSDYTLRSSLLLIRNNLTAIEPVVMYGKGARIGVKVEGAEARSKKPLLFEIRHDHLTDCNNPKRLMHKLHSTLTVRRPFQVMNSGEVQFTVTNMSINGVPCENRGFRILNCYPFRLQPNETYALDIAYTPDFLTTTNEADLQLYMHMNGSAWIFPLASTVPGDMLAKCHQALPRPPFENIMYYSCVTALIFCLVCVLACAYLEGDRAIAVAIRQQFAIPRHVFDLNNLNKNNSTTTPVPTVPSTAKPESSIKKPTPATRPSTLRASSDAWLISRLLIGLANFIVKCVHLFWKWSLFWRREKADDKQSKSAKVTKKKNPVTMQKVEEFRQMLEYVGQQKRQQNSGELAPEFDEVEEEELAEMWAQRKDSGAQSSVVTDPEPPMSKSQRKKKRAAQQKENNNLEAPIIVQPVVQSPPVQNKMEPAKKTTPGPSPKPKGNNQRKKHVQVPPVTKTPVTPKTSIPPPTEPEKPIKPSEQKKPNAIPVERPKQPTPSKARTPSKTPSQSNRAQHPASSPAPIAPTSAPTDDFVHVPPTSLTSPDLFYRQFLSSMGMPMDAGMWDTPAAQAAMPFMNLWNYGGPLSAEQMEDLIRQASGVAPITNDSEGTTVTTPSDIGMTWGTSGHLGGDEESIGGEAAPDWIDEDVNVDDAEMDFSSMSAASKDIFKDDDIDNFNQQMKRQRSPSQASSTLSRKLENSPQKMGSRRLTIGSEKKNNQSSSSALNPNYDFTRTPGNPNRMQMSQNSIQPAPPATSIWGDNSNSDPWGTNTVSNPLSELEDDPLSLSHLGINLASTESSATGPMFTMFSGPEFNLWSSSSLFHPPTQQPSTSQMPQDTDNENDEKNN
Protein: RNA exonuclease 2 (F5GYG5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLGGSLGSRLLRGVGGSHGRFGARGVREGGAAMAAGESMAQRMVWVDLEMTGLDIEKDQIIEMACLITDSDLNILAEGPNLIIKQPDELLDSMSDWCKEHHGKQAEYEFLSFVRQQTPPGLCPLAGNSVHEDKKFLDKYMPQFMKHLHYRIIDVSTVKELCRRWYPEEYEFAPKKAASHRALDDISESIKELQFYRNNIFKKKIDEKKRKIIENGENEKTVS
Protein: Thymidine kinase b (AtTK1b) (EC 2.7.1.21) (F4KBF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of the salvage pathway for purine and pyrimidine deoxyribonucleotide synthesis. Phosphorylates preferentially purines over pyrimidines.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04183}.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- dCMP deaminase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Thymidylate kinase
- At1g72040
- Cytidine deaminase 5
- Cytidine deaminase 2
- Cytidine deaminase 3
Sequence:
MFGVSMRTLISPSLAPFSLHLHKPSLFSTALRFSFSINNITPTNSPPSTISTRKLQTKATRVTSSSSSQPLSSSSPGEIHVVVGPMFSGKTTTLLRRILAERETGKRIAIIKSNKDTRYCTESIVTHDGEKYPCWSLPDLSSFKERFGFDDYENRLDVIGIDEAQFFGDLYEFCREAADKEGKTVIVAGLDGDFMRRRFGSVLDLIPIADTVTKLTSRCEVCGKRALFTMRKTEEKETELIGGAEVYMPVCRSHYVCGQNVLETARAVLDSSNNHSVVASSL
Protein: Clotting factor G beta subunit (EC 3.4.21.85) [Cleaved into: Clotting factor G beta subunit light chain; Clotting factor G beta subunit heavy chain] (Q27083)
Organism: Tachypleus tridentatus (Japanese horseshoe crab)
Function: Component of the heterodimer clotting factor G which may play a role in defense mechanisms against fungi (Probable). Initiates a (1->3)-beta-glucan-sensing clotting pathway whereby the alpha subunit binds to glucans containing (1->3)-beta linkages, which are components of the fungal cell wall, and the beta subunit catalyzes the activation of proclotting enzyme.
Interaction partners:
Sequence:
MDISFLVFITLSMALFSSNVTGTSVTSRVRRGINEKHCGFRPVITRIIGGGIATPHSWPWMVGIFKVNPHRFLCGGSIINKVSVVTAAHCLVTQFGNRQNYSIFVRVGAHDIDNSGTNYQVDKVIVHQGYKHHSHYYDIGLILLSKPVEYNDKIQPVCIPEFNKPHVNLNNIKVVITGWGVTGKATEKRNVLRELELPVVTNEQCNKSYQTLPFSKLNRGITNDMICAGFPEGGKDACQGDSGGPLMYQNPTTGRVKIVGVVSFGFECARPNFPGVYTRLSSYVNWLQEITFGQSLASLFEVVPIFIPE
Protein: Matrix metalloproteinase 1, isoform J (EC 3.4.24.-) (Matrix metalloproteinase 1, isoform L) (A0A0B4K7H5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTNCQSSVFIVVGTLFSIMAAAQSAPVSTTTQAEIYLSQFGYLPASARNPASSGLHDQRTWVSAIEEFQSFAGLNITGELDAETMKLMSLPRCGVRDRVGTGDSRSKRYALQGSRWRVKNLTYKISKYPKRLKRVDVDAEIGRAFAVWSEDTDLTFTRKTSGPVHIEIKFVESEHGDGDAFDGQGGTLAHAFFPVFGGDAHFDDAELWTIGSPRGTNLFQVAAHEFGHSLGLSHSDQSSALMAPFYRGFEPVFKLDEDDKAAIQSLYGRKTNQLRPTNVYPATTQRPYSPPKVPLDDSICKDSKVDTLFNSAQGETYAFKGDKYYKLTTDSVEEGYPQLISKGWPGLPGNIDAAFTYKNGKTYFFKGTQYWRYQGRQMDGVYPKEISEGFTGIPDHLDAAMVWGGNGKIYFFKGSKFWRFDPAKRPPVKASYPKPISNWEGVPNNLDAALKYTNGYTYFFKGDKYYRFHDARFAVDSATPPFPRPTAHWWFGCKNTPSSTGFKRRGYKNKNN
Protein: Ubiquitin thioesterase OTUB1 (EC 3.4.19.12) (Deubiquitinating enzyme OTUB1) (OTU domain-containing ubiquitin aldehyde-binding protein 1) (Otubain-1) (Ubiquitin-specific-processing protease OTUB1) (B2RYG6)
Organism: Rattus norvegicus (Rat)
Function: Hydrolase that can specifically remove compared to 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19343716}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 N
- Ring finger protein 128
- Ubiquitin-conjugating enzyme E2 D1
- Ubiquitin carboxyl-terminal hydrolase 8
- TNF receptor-associated factor 6
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eL40 fusion protein
- OTU domain-containing protein 3
- TNF receptor-associated factor
- Ubiquitin-conjugating enzyme E2 S
Sequence:
MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHVFPEGSEPKVYLLYRPGHYDILYK
Protein: Killer cell lectin-like receptor subfamily I member 1 (Q5DT39)
Organism: Rattus norvegicus (Rat)
Function: Lectin-like receptor for natural killer (NK) cells. Heterodimer formation with KLRE1 mediates inhibition of NK cell cytolytic activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15650876}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPHSKHRDYTADKQDIPYTELKACKSPWKHRTPAVKQSPVVLSEEQLKYAELTFHRTPQLQPRKQTVRRKRQGPKSAVWRVVTCVLGVLCVVLMITMGILVPKLFSGQEEQYRETSLHHLLKNDSSCDPCSHDWIAFGNNFYLFFRGTKSWAESKSACEELNSHLLDIDSKAELENLLLFEINGWILVKKNQTNWSSSENETKLQHTLIDEKKNHSCRYLRGSQFIADDCSSKKPYACEFNKM
Protein: Sodium-dependent nutrient amino acid transporter 1 (B4L7U0)
Organism: Drosophila mojavensis (Fruit fly)
Function: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELKTMPHNGANGSPQHNNNNNSNNNNNVSSDTKTDNNEKEAQKKDEGRTNWSNGIEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIIGQFTSQGTVKIWSICPSFVGVGYGQAFATICIITYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSIPTEFVETALGNTTSALAQQANTLSNTTKLQSSSELYFLNVVIKEKSDISDGIGIPDWKLTIALFVSWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFALLGRAVTLEGAVDGIIFFLQPQWGELLNPIVWKEAVVQCFFSLAVGCGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLKAENIRDVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKSWKYWKVALATSACGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELSGIVWIYGLQNFCDDIEFMSNKNVSMYWRLCWSFFTPVMMIVIFIYSMATIQPIKYSDQYFPLAGDVAGWLLFAVGAAQFPLWGWWYIATHRHGSCAESIKASLKPSSKWGPASPENRQAWLLFKSDLAAKRANEAKSNKFGFFQQKLRNMCGK
Protein: MADS-box protein, GGLO1 (Q9ZS26)
Organism: Gerbera hybrida (Daisy)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRGKIEIKRIENTSNRQVTYSKRKNGIIKKAKEITVLCDANVSLVIYGSSGKMYEYCSPKTNLIDMLDRYQRLSGNKLWDAKHENLQNEIDRIKKENESMQIELRHLKGEDITSLNYEELIAYEDALENGLTNIREKKDEIPKIMRKHEQVLEEENKHLMYLVQQSEMAAMGDYQAAHEPFSFRVQPMQPNLHERM
Protein: CD320 antigen (Transcobalamin receptor) (TCblR) (CD antigen CD320) (Q9Z1P5)
Organism: Mus musculus (Mouse)
Function: Receptor for transcobalamin saturated with cobalamin (TCbl). Plays an important role in cobalamin uptake. Plasma membrane protein that is expressed on follicular dendritic cells (FDC) and mediates interaction with germinal center B cells. Functions as costimulator to promote B cell responses to antigenic stimuli; promotes B cell differentiation and proliferation. Germinal center-B (GC-B) cells differentiate into memory B-cells and plasma cells (PC) through interaction with T-cells and follicular dendritic cells (FDC). CD320 augments the proliferation of PC precursors generated by IL-10.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9NPF0}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9NPF0}.
Interaction partners:
- Transcobalamin-2
Sequence:
MARGGAGRAVALGLVLRLLFGLRTGLEAAPAPAHTRVQVSGSRADSCPTDTFQCLTSGYCVPLSWRCDGDQDCSDGSDEEDCRIESCAQNGQCQPQSALPCSCDNISGCSDVSDKNLNCSRPPCQESELHCILDDVCIPHTWRCDGHPDCLDSSDELSCDTDTEIDKIFQEENATTTRISTTMENETSFRNVTFTSAGDSSRNPSAYGVIAAAGVLSAILVSATLLILLRLRGQGYLPPPGLLVAVKESLLLSERKTSLI
Protein: Tachykinin-related peptide 4 (TKRP-4) (P86578)
Organism: Nezara viridula (Southern green stink bug) (Cimex viridulus)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
SPASGFFGMR
Protein: Lysophosphatidic acid receptor 3 (LPA receptor 3) (LPA-3) (Lysophosphatidic acid receptor Edg-7) (Q9UBY5)
Organism: Homo sapiens (Human)
Function: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. May play a role in the development of ovarian cancer. Seems to be coupled to the G(i)/G(o) and G(q) families of heteromeric G proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Lysophosphatidic acid receptor 6
- Lysophosphatidic acid receptor 4
- Lysophosphatidic acid receptor 5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 2
- Lysophosphatidic acid receptor 1
- Proteinase-activated receptor 1
- Angiotensinogen
- Muscarinic acetylcholine receptor M1
Sequence:
MNECHYDKHMDFFYNRSNTDTVDDWTGTKLVIVLCVGTFFCLFIFFSNSLVIAAVIKNRKFHFPFYYLLANLAAADFFAGIAYVFLMFNTGPVSKTLTVNRWFLRQGLLDSSLTASLTNLLVIAVERHMSIMRMRVHSNLTKKRVTLLILLVWAIAIFMGAVPTLGWNCLCNISACSSLAPIYSRSYLVFWTVSNLMAFLIMVVVYLRIYVYVKRKTNVLSPHTSGSISRRRTPMKLMKTVMTVLGAFVVCWTPGLVVLLLDGLNCRQCGVQHVKRWFLLLALLNSVVNPIIYSYKDEDMYGTMKKMICCFSQENPERRPSRIPSTVLSRSDTGSQYIEDSISQGAVCNKSTS
Protein: GEO08286p1 (PTIP associated 1) (RE09126p) (RH21749p) (Q9VYZ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- PAX-interacting protein 1
- LD02225p
- Histone-lysine N-methyltransferase trr
- Nuclear receptor coactivator 6, isoform F
- HL01030p
- Retinoblastoma-binding protein 5 homolog
- Protein will die slowly
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Host cell factor
- Protein dpy-30 homolog
Sequence:
MATDVEPAANTADKFSANAEELEGYYLMLEAGNIPELQWQFPGRRAPSPEAGSGGNSKELEQATDAIEQEPQKANDFDFSDDVAPTQMRVRSQTSTPKSAKKKTANFAGVMETLKKKNAESS
Protein: Sporulation-specific protein 16 (P17122)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Necessary for efficient spore formation.
Interaction partners:
- Protein ZIP2
- Sporulation-specific protein 22
- Chromosome stability protein 9
- MutS protein homolog 4
- Synaptonemal complex protein ZIP1
- MutS protein homolog 5
- ATP-dependent DNA helicase MER3
- Protein ECM11
- Grand meiotic recombination cluster protein 2
- Protein RED1
Sequence:
MSEFFWDVQKIQEISNVEEHSVVKCVTVNTSRLISQLNEELQDEESGVNFIVTQLQLLINNVYEKIQKSPGVPAHRSLMINLNFTRLKFSIAYWDILLERSLDLINGPSKTGARYFITEVTPVDRSRYVENNQYFLAFKANQRLTRNSVDMDEFIDFEILIKQIIFDLFKKNGIPDQDFEAILSRFHNLESLVVAFNE
Protein: E3 ubiquitin-protein ligase ZNF598 (EC 2.3.2.27) (Zinc finger protein 598) (Q86UK7)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that plays a key role in the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation. Required for ribosomes to terminally stall during translation of poly(A) sequences by mediating monoubiquitination of 40S ribosomal protein RPS10/eS10, RPS20/uS10 and RPS3/uS3. Stalling precludes synthesis of a long poly-lysine tail and initiates the RQC pathway to degrade the potentially detrimental aberrant nascent polypeptide. Also acts as a component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28757607}.
Interaction partners:
- GRB10-interacting GYF protein 2
- GRB10-interacting GYF protein 1
- Eukaryotic translation initiation factor 4E type 2
- Small ribosomal subunit protein RACK1
- Activating signal cointegrator 1 complex subunit 3
- E3 ubiquitin-protein ligase listerin
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS10
- Small ribosomal subunit protein uS3
- Ribosome quality control complex subunit NEMF
Sequence:
MAAAGGAEGRRAALEAAAAAAPERGGGSCVLCCGDLEATALGRCDHPVCYRCSTKMRVLCEQRYCAVCREELRQVVFGKKLPAFATIPIHQLQHEKKYDIYFADGKVYALYRQLLQHECPRCPELPPFSLFGDLEQHMRRQHELFCCRLCLQHLQIFTYERKWYSRKDLARHRMQGDPDDTSHRGHPLCKFCDERYLDNDELLKHLRRDHYFCHFCDSDGAQDYYSDYAYLREHFREKHFLCEEGRCSTEQFTHAFRTEIDLKAHRTACHSRSRAEARQNRHIDLQFSYAPRHSRRNEGVVGGEDYEEVDRYSRQGRVARAGTRGAQQSRRGSWRYKREEEDREVAAAVRASVAAQQQEEARRSEDQEEGGRPKKEEAAARGPEDPRGPRRSPRTQGEGPGPKETSTNGPVSQEAFSVTGPAAPGCVGVPGALPPPSPKLKDEDFPSLSASTSSSCSTAATPGPVGLALPYAIPARGRSAFQEEDFPALVSSVPKPGTAPTSLVSAWNSSSSSKKVAQPPLSAQATGSGQPTRKAGKGSRGGRKGGPPFTQEEEEDGGPALQELLSTRPTGSVSSTLGLASIQPSKVGKKKKVGSEKPGTTLPQPPPATCPPGALQAPEAPASRAEGPVAVVVNGHTEGPAPARSAPKEPPGLPRPLGSFPCPTPQEDFPALGGPCPPRMPPPPGFSAVVLLKGTPPPPPPGLVPPISKPPPGFSGLLPSPHPACVPSPATTTTTKAPRLLPAPRAYLVPENFRERNLQLIQSIRDFLQSDEARFSEFKSHSGEFRQGLISAAQYYKSCRDLLGENFQKVFNELLVLLPDTAKQQELLSAHTDFCNREKPLSTKSKKNKKSAWQATTQQAGLDCRVCPTCQQVLAHGDASSHQALHAARDDDFPSLQAIARIIT
Protein: Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase) (O08796)
Organism: Mus musculus (Mouse)
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
- Ribosomal protein S6 kinase beta-1
- Protein kinase C alpha type
- 5'-AMP-activated protein kinase subunit gamma-2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Protein kinase C beta type
- Protein kinase C gamma type
- 5'-AMP-activated protein kinase subunit gamma-1
- 5'-AMP-activated protein kinase subunit beta-1
Sequence:
MADEDLIFCLEGVDGGRCSRAGHNADSDTDSDDDEGYFICPITDDHMSNQNVSSKVQSYYSNLTKTECGSTGSPASSFHFKEAWKHAIEKAKHMPDPWAEFHLEDIATEHATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYFEDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRICQSMGLTPFDLSPREQDAVNQSTRLLQSAKTILRGTEEKCGSPRIRTLSSSRPPLLLRLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFGDLDNMGPRDHDRMDNHRDSENSGDSGYPSEKRSDLDDPEPREHGHSNGNRRHESDEDSLGSSGRVCVETWNLLNPSRLHLPRPSAVALEVQRLNALDLGRKIGKSVLGKVHLAMVRYHEGGRFCEKDEEWDRESAIFHLEHAADLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRHSMILVARAFDTGLNLSPDRCQDWSEALHWYNTALETTDCDEGGEYDGIQDEPQYALLAREAEMLLTGGFGLDKNPQRSGDLYTQAAEAAMEAMKGRLANQYYEKAEEAWAQMEE
Protein: Ras association (RalGDS/AF-6) and pleckstrin homology domains 1 (S4R2K5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XSWKKRYFLLRASGIYYVPKGKAKVSRDLVCFLQLDHVNVYYGQDYRNKYKAPTDCCLALKHPQIQKKSQYIKYLCCDDARTLHQWVNGIRIAKYGKQLYTNYQEALKRTESAYDWTSLSSSSIKSGSSSSSIPESQSNHSNQSDSGVSDTLPTGHIRSQSTVSSIFSEAWKRGTQLEESSKRTRVQFPAPSSGNSKPPITPAPKDPMSSSGLQGT
Protein: 6-phosphogluconate phosphatase (EC 3.1.3.-) (P31467)
Organism: Escherichia coli (strain K12)
Function: Catalyzes strongly the dephosphorylation of 6-phosphogluconate (6P-Glu) and slightly the dephosphorylation of dihydroxyacetone phosphate (DHAP) and phosphoenolpyruvate (PEP). Also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates.
Interaction partners:
- GMP/IMP nucleotidase YrfG
- Pyrimidine 5'-nucleotidase YjjG
- Inner membrane protein CbrB
- Fructose-1-phosphate phosphatase YqaB
- Hexitol phosphatase B
- Beta-phosphoglucomutase
Sequence:
MSRIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHVYRAEVARLFDSELEAIEGAGALLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQLPELWKARGWDITA
Protein: Uncharacterized calcium-binding protein C613.03 (O74903)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16823372}. Golgi apparatus lumen {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Low molecular weight phosphotyrosine protein phosphatase
Sequence:
MKFSTVGFLFSTILFKSAFAGWMDTHMKDEHHIDKYTDESFFRLHDLGKKGYWSDQDILSLYGLFENDEVPFVKKNEVLVDVLKKCDPSGNRRITLDEFLAFRKNGGELTDFGFPGHHGDEEEEFEMHHVEKYHPAGLDEPDENWNHPEDIEHFQKHDEIFHGDKKPEERRKHFVKYNNIPDKYRRVSI
Protein: RE74364p (Q8SYB4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLKAAKIPLFFALLGAVCIQAVVVGPQPLHNNNRNGYRYNGPAHKYLPSEESHSHGSPLDSSHQHDQQGPSNAYNSHHYPAQEQHGQGAPEHDHQQKEVDSWQTALSQQQHESFGNQQNHQNAYSEGPVYQHYQGFNHQQHYGLSQQQQHESYGQEHYQQSPNQLQHHQSQHANEYAYEPAHFQQQQQHHEIQSHKQHQQRKEHWNFVQEQQPQNHEPWQSSHGFQQHQQQHSNRFESQLPLREDLWQPIRELDLEKLPSAEAHASSHKTVAAPGRDVKLVPSYTLSSDFEHDRFIGLDSTDTRLLTQSLPDAYRKQLFSSPPEPSSLAQGHNQQHKPGSAAYGGSHGPSLGESTSDFLQMQSHSYQLPSTFTTHTEWTQDKEQHQHNPQQQATGNRQYSASAFAVSPSYLHASEASQPPKNSLPHPSRDFQPPYY
Protein: Nucleoporin 62 like (Zgc:172056 protein) (A8WFZ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
Sequence:
MAFNFGQTGTGGFNFGTPKTTAAATTGFGVPQGSSTPAGGGFSFGANQPQTQNFGNPPSQIAGLLAQPTQNNGSTQGGFSFGAQTQSTTAGGGFSFGGSLPKLSTPAAPQPATTGVSLGASTTGTGFSLGGLTPQTTAAQQPMGGFSFGAPKVQAASVAPAQPTPVLSLGVQPTTGLSLGAPTAASIASTTAINFGIKTSATPAPASTALSSQSSTAPVSSLFANPIASTPVTGFTLGSSTASVAPVMTSGSSAPASLSLKPLGAVPAITTAAASTGATTGFSLGLKTAASTALASTTATSTTVVTASTAPVMSYAQLEALINKWSSELEDQERHFLQQATQVNAWDRMLVENGEKITALHKDMEKVKLDQRRLDQELDFILSQQKELEDLLSPLEESVKEQSGTIYMQNADEERERTYKLAENVDAQLKRMSQDLKEIIEHLNTSSGPADTADPLQQICKILNAHMDSLQWVEQNSVLLQRRVEEVSKLCESRSKEQEKSFRLNFQ
Protein: Crp-family transcriptional regulator (Q9KYY6)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Interaction partners:
- Sugar phosphotransferase
- Sulfatase
- ABC-transport protein, membrane component
- ABC-transport protein, ATP-binding component
- Regulatory protein
- Formylglycine-generating enzyme
Sequence:
MTGMQMPSGVHALVRRTHEERVMRALQENGAMSRGEIARVVGLSRTTLSEITGNLLQRGAIVVVDTDASRREGSGRPAERLALDPASAQFMGVDFGHRRVHVVVADAAHEIMVSGSVRYEDTATWPTRTERALELVDRLSGEAGVHYGALQGIGIGVPGPYPAPEGAAWPRATPGTTVLRPAPEGVDVAFAERFDAPVIVDNNTRLAALAEAISGADSVADLVYVRLSDGVGGGLVVGGQLVTGSSGLAGELGHVTVEPAGRPCRCGKRGCLETVASVPGILAACWEFGLRLENLDDLAAAVRRAHPVVDRVLREAAGALGRVVGAATMMLNPAKVVIGGEITRLAPVLVEQVAATLAAEIFPTASAGPVVAAARLSDDDGAIGALAAVFHSSPLLARYPETADVKGRSDAPHSATEGAAHVRP