wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleoporin p58/p45 (58 kDa nucleoporin) (Nucleoporin-like protein 1) (Q9BVL2)
Organism: Homo sapiens (Human)
Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Cytoplasmic side {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70581}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70581}.
Interaction partners:
- Nuclear pore complex protein Nup93
- Nuclear pore glycoprotein p62
- Nucleoporin p54
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup85
Sequence:
MSTGFSFGSGTLGSTTVAAGGTSTGGVFSFGTGASSNPSVGLNFGNLGSTSTPATTSAPSSGFGTGLFGSKPATGFTLGGTNTGIATTITTGLTLGTPATTSAATTGFSLGFNKPAASATPFALPITSTSASGLTLSSALTSTPAASTGFTLNNLGGTTATTTTASTGLSLGGALAGLGGSLFQSTNTGTSGLGQNALGLTLGTTAATSTAGNEGLGGIDFSSSSDKKSDKTGTRPEDSKALKDENLPPVICQDVENLQKFVKEQKQVQEEISRMSSKAMLKVQEDIKALKQLLSLAANGIQRNTLNIDKLKIETAQELKNAEIALRTQKTPPGLQHEYAAPADYFRILVQQFEVQLQQYRQQIEELENHLATQANNSHITPQDLSMAMQKIYQTFVALAAQLQSIHENVKVLKEQYLGYRKMFLGDAVDVFETRRAEAKKWQNTPRVTTGPTPFSTMPNAAAVAMAATLTQQQQPATGPQPSLGVSFGTPFGSGIGTGLQSSGLGSSNLGGFGTSSGFGCSTTGASTFGFGTTNKPSGSLSAGFGSSSTSGFNFSNPGITASAGLTFGVSNPASAGFGTGGQLLQLKKPPAGNKRGKR
Protein: E3 ubiquitin-protein ligase RNF146 (EC 2.3.2.27) (Iduna) (RING finger protein 146) (RING-type E3 ubiquitin transferase RNF146) (Q9CZW6)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein (By similarity). Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation. Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21602803}. Nucleus {ECO:0000250}. Note=Translocates to the nucleus after DNA damage, such as laser-induced DNA breaks, and concentrates at DNA breaks. This translocation requires PARP1 activation and PAR-binding (By similarity). {ECO:0000250}.
Interaction partners:
- Poly [ADP-ribose] polymerase tankyrase-1
- Poly [ADP-ribose] polymerase tankyrase-2
- Axin-1
- Axin-2
- Ubiquitin-conjugating enzyme E2 D1
- Poly [ADP-ribose] polymerase 1
- Poly [ADP-ribose] polymerase 2
- SH3 domain-binding protein 2
Sequence:
MEMAGCGEIDHSINMLPTNKKANESCSNTAPSLTVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDKPTLLSPEELKAASRGNGEYAWYYEGRNGWWQYDERTSRELEDAFSKGKKNTEMLIAGFLYVADLENMVQYRRNEHGRRRKIKRDIIDIPKKGVAGLRLDCDTNTVNLARESSADGADSGSAQTGASVQLAVPSSTRPLTSVDGQLTSPVTPSPDAGISLEDSFAHLQLSGDSIAERSHRGEGEEDHESPSSGRVPDTSVEETESDASSDSEDAPVVVAQHSLTQQRPLVPNGNQTVADQSDRSGTDRSVAGGGTMSVNVRSRRPDGQCTVTEV
Protein: Microtubule-associated protein Jupiter (Q9I7K0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to all microtubule populations.
Subcellular location: Nucleus {ECO:0000269|PubMed:11742088, ECO:0000269|PubMed:16518797}. Cytoplasm {ECO:0000269|PubMed:11742088, ECO:0000269|PubMed:16518797}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11742088, ECO:0000269|PubMed:16518797}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11742088, ECO:0000269|PubMed:16518797}.
Interaction partners:
- MIP30042p
- Tyrosine--tRNA ligase
Sequence:
MAAYAAFKHVELYNVGKAKKRVLRPPGGGSSDIFGSEMPQTPRNVKNRMASNIFAAEKDNGVKNNVRQGAHRFYFIGDAPRRGQKTVDSHSRLFGEPTRPITPGKNHMKSSIPFGQNTEAVAAQKLLTTNGHYNGKSGSVSSASSSVSSSTENLKMNSGSRSEGNPVTGEGYKVVANEYSQRQESSNGGTPVINKNRIPPGGYSSGLW
Protein: Aminopeptidase (EC 3.4.11.-) (B0BCZ7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPDHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPGEQVLETVKNNIEWLKQHRNTIREWFFNLLESG
Protein: Phosphoenolpyruvate carboxylase 1 (AtPPC1) (PEPC 1) (PEPCase 1) (EC 4.1.1.31) (107-kDa PEPC polypeptide) (Q9MAH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. Contributes probably to the adaptation to inorganic phosphate (Pi) deprivation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Pyruvate, phosphate dikinase 1, chloroplastic
- Malate dehydrogenase, chloroplastic
- Phosphoenolpyruvate carboxykinase 1
- phosphoenolpyruvate carboxykinase
- Phosphoglycerate kinase 3, cytosolic
- Citrate synthase 4, mitochondrial
- Citrate synthase 3, peroxisomal
- Citrate synthase 5, mitochondrial
- Citrate synthase 1, peroxisomal
- Citrate synthase 2, peroxisomal
Sequence:
MANRKLEKMASIDVHLRQLVPGKVSEDDKLVEYDALLLDRFLDILQDLHGEDLRETVQELYEHSAEYEGKHEPKKLEELGSVLTSLDPGDSIVIAKAFSHMLNLANLAEEVQIAYRRRIKKLKKGDFVDESSATTESDLEETFKKLVGDLNKSPEEIFDALKNQTVDLVLTAHPTQSVRRSLLQKHGRIRDCLAQLYAKDITPDDKQELDEALQREIQAAFRTDEIKRTPPTPQDEMRAGMSYFHETIWKGVPKFLRRVDTALKNIGIEERVPYNAPLIQFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAATMYFNQIEDLMFEMSMWRCNDELRARADEVHANSRKDAAKHYIEFWKSIPTTEPYRVILGDVRDKLYHTRERAHQLLSNGHSDVPVEATFINLEQFLEPLELCYRSLCSCGDRPIADGSLLDFLRQVSTFGLSLVRLDIRQESDRHTDVLDAITTHLDIGSYREWSEERRQEWLLSELSGKRPLFGSDLPKTEEIADVLDTFHVIAELPADSFGAYIISMATAPSDVLAVELLQRECRVKQPLRVVPLFEKLADLEAAPAAVARLFSVDWYKNRINGKQEVMIGYSDSGKDAGRLSAAWQLYKAQEELVKVAKEYGVKLTMFHGRGGTVGRGGGPTHLAILSQPPDTINGSLRVTVQGEVIEQSFGEEHLCFRTLQRFTAATLEHGMRPPISPKPEWRALLDEMAVVATEEYRSVVFQEPRFVEYFRLATPELEYGRMNIGSRPSKRKPSGGIESLRAIPWIFAWTQTRFHLPVWLGFGSAIRHVIEKDVRNLHMLQDMYQHWPFFRVTIDLIEMVFAKGDPGIAALYDKLLVSEELWPFGEKLRANFEETKKLILQTAGHKDLLEGDPYLKQRLRLRDSYITTLNVCQAYTLKRIRDPSYHVTLRPHISKEIAESSKPAKELIELNPTSEYAPGLEDTLILTMKGIAAGLQNTG
Protein: LD33138p (Q9VW58)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
- SAM50-like protein CG7639
- Translocon-associated protein subunit gamma
- MICOS complex subunit Mic60
- Coiled-coil-helix-coiled-coil-helix domain containing 3
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- Metaxin-1 homolog
Sequence:
MTSQYLSQLITADKLSAEPWPEDATLYQPYEAEQILLPENASCLAVKAYLKMCNLPFLIRSCANAEHMSPGGRMTKLPFIRAGAFIFAEFEPIVNFVEQKELAIGSWQDEDEKADMRTYVSLVENIFTMAELYISFKNERVYKEVTAPRNGVVFPWPLNHMQNYGKRRNALRLLKVYQWDDLDIDSVIDKVAKCCETLEYKLKESPETPFFYGDQPCELDAIAFGHLFSILTTTLPNMALAQTVQKFQHLVEFCRFVDEKYFQTRCLPN
Protein: GRB2-associated-binding protein 1 (GRB2-associated binder 1) (Growth factor receptor bound protein 2-associated protein 1) (Q9QYY0)
Organism: Mus musculus (Mouse)
Function: Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Involved in the MET/HGF-signaling pathway.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 11
- Growth factor receptor-bound protein 2
- SHC-transforming protein 1
- Epidermal growth factor receptor
- Hepatocyte growth factor receptor
- Son of sevenless homolog 1
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Crk-like protein
- Fibroblast growth factor receptor substrate 2
- Adapter molecule crk
Sequence:
MSGGEVVCSGWLRKSPPEKKLKRYAWKRRWFVLRSGRLTGDPDVLEYYKNDHAKKPIRIIDLNLCQQVDAGLTFNKKEFENSYIFDINTIDRIFYLVADSEEDMNKWVRCICDICGFNPTEEDPVKPLTGSSQAPVDSPFAISTAPASSQMEASSVALPPPYQVISLPPHPDTLGLQDDPQDYLLLINCQSKKPEPNRTLFDSAKPTFSETDCNDNVPSHQTPASSQSKHGMNGFFQQQMMYDCPPSRLTSVSGESSLYNLPRSYSHDVLPKESPSSTEADGELYTFNTPSGTAGVETQMRHVSISYDIPPTPGNTYQIPRTFPESTLGQSSKLDTIPDIPPPRPPKPHPTHDRSPVETCGVPRTASDTDSSYCIPPPAGMTPSRSNTISTVDLNKLRKDASSQDCYDIPRTFPSDRSSSLEGFHSQYKIKSVLTAGGVSGEELDENYVPMNPNSPPRQHSGSFTEPIQEPNYVPMTPGTFDFSSFGMQVPPPAHMGFRSSPKTPPRRPVPVADCEPPPVDRNLKPDRKVKPAPLDIKPLSEWEELQAPVRSPITRSFARDSSRFPMSPRPDSVHSTTSSSDSHDSEENYVPMNPNLSGEDPNLFASNSLDGGSSPMNKPKGDKQVEYLDLDLDSGKSTPPRKQKSSGSGSSMADERVDYVVVDQQKTLALKSTREAWTDGRQSTESETPTKNVK
Protein: Apolipophorin 2 (Apolipophorin-II) (apoLp-II) (C0HKF4)
Organism: Galleria mellonella (Greater wax moth)
Function: Constitutes the major component of lipophorin, which mediates transport for various types of lipids in hemolymph. Acts by forming lipoprotein particles that bind lipoproteins and lipids (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:29289504}. Note=Secreted into hemolymph. {ECO:0000269|PubMed:29289504}.
Interaction partners:
Sequence:
DDKCSIGCKGSATAPTFLNGH
Protein: Uracil catabolism protein 2 (Q04411)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable transcriptional activator involved in uracil catabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL29A
- Oleate activated transcription factor 3
- Large ribosomal subunit protein uL24A
- Large ribosomal subunit protein uL24B
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL3
Sequence:
MDINSNASVSPRPDGLPMTAGYNSASGKVRNSIRSIINHPEDSARAKERSETNSPKNNGNKKPRKKRKTFSCDTCRRVKTRCDFEPFIGKCYRCNVLQLDCSLARNKDNEILNTLREDGLLKKINSINHNLGSFSHLNADSPNESQSSFEKNGTVNFDNYMIDKRLSSLEEHIKSLHQKMDLIITTAKMSYNSDIKGPGDDIQNVDFSSNKTYDSRLTSGSETIRKTGEYRKENLFLNGFKLKESPLKLLHDIDERLFPSKATSKAAKLAGQQRPYAVARVNFLHFYENNQELCHKLAKEFLVRSHFWIIPGGRKEIDVEYAHSHLFITSVFTIIAMSFADNDKYAAEQEILYPLVERLLTNTLTMFEKLTAFDIEAILYCCMFHISRKAKRYRQLKFNSLVLSNFALNSLLHVIDFYQIKDRVLVKEVYNPEDLYHLRILNSLTACYLEYSISYGDIREQDDMLKEFNKLVAKFPQANFGDDIKISEINLGDIVNGIFINLKNYFAQCLDDFNNDRYGGNADTFIFVFPELNYWLKNWEELLAKDGAGVLLFTFDFYHIMICRTFITEFSSTLKSNQRFLKLILNTMKEHSFSLLNGFLRLPPTLIRGAPIFTCHQLVYACLTLCDYLYWFDSSERQRVLSLCTKVYWHLSTIGEKMNEATDNVGKIIKSIIDTSKTRINFGSLSKENSDNDKMSTNANNYTGAGNLHAAKPATSPTNVGTLHENLSSSHFMIPDVDQFNSFEDFFQDFFDSLKPNSQKMFTSDKKTEQTT
Protein: Uncharacterized helicase C694.02 (EC 3.6.4.-) (Q9P7T8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C1020.05
Sequence:
MSEEIAKLTTVQNYRLVDLIGDFAGEELFLIDGDSLIFHILAKDSQFLAKNGVQILYAIYLLEKELARFKSARLNFCIVFFKNWEALYSQYDGILHASLLLFRRVAIRHLRKHVPVYVFKSLGDSQWSIFIAKHRPYGFMVLDSNQNTKEGGLVISDEQVMVFKSFIFFALSDGVPVALLGSYQFVDNKILVCILPSFFTRSSESVENASNLISDYLKKFGKPRQSIELPDIAVDACPSNASRIQTLSAAWLLLNEKSDLNVDLCKILIILTCMLEELSLNDRFQPAFPLYEDPAIQKFIISYLNATNTILQLLDSKVDGFHDIFDGRLFIRLVVDAALGEFCIPDICRESALSLWKLILDIAPDAGDLFDFPSLSSISKDLCVPIETPVSEIDISLTAYNDPVISPYYDTEEWNLEQREEPGIETVLDFSKLRINDKTMTSKRFDDLSATRKTGDNTKDRKQANKVRRQDQFFISHIQKYASSLTGAKGGQLKRQTIFTQGPNSTKESKQAVKEETSVKNSPKGKNTKNGKAEKEKPGKKSKAPKLSKAEQIRAEIAARKVEKEENKNEVIWNETKNDLGRIKDLNLRAGRLAQLLNTRTYDPYIENEMRLYRIRVLLSLWTACCVTDEGKEKNIKIAVEIFREISIVYPNPITKQVKAALDETLTALGFENVIRKMKKLESKPLSFPFVLPDLEDEEFDLEVPYTSPTFQLLHFGEYMERSMGSAPDSRVAFDPDEWQRETLDILDRDESVFVVAPTSSGKTFISFYAMEKVLRDNDDGVVIYVAPTKALVNQLSAEVYARFNKHYPHAGQTVWSVYTRDYRINNPTNCQVLITVPHVLQSMLLQPALANAWCPKIRRIIFDEIHCIGQMEDGLVEEQLLLLAPCPIVALSATVGNPQEFQVWLSALQRAHSYPIHLIVHEHRYSDLRKFVYGGAKEFNGLQEEGDLGQIAFIHPAAAMSFSDGSTTNLAFEPRDCLQLYYAMKLVSKGDFKISRKLDPDRYFEDIPFIKKVDAVGYEKKIKATIDTWASLPNAFAPNSPFQALIKHFCSEPQKVVNSQLELHNSAYSLDAISQNLLPMLKDLHSKELLPAICFNYDRQECEYLAEIVFKTLVEKEREWRENSEEWKEKMREYKKWQSTANQRAKQMEKFEKSATEKQKEQALKEAGDISWIEFFDPEEPSPEFSFAGAKSTYGKEELYRDLEALRRRQAVPEWYVDALYRGIGIHHSGLNRRYRQIVEVLFRCGQLTVVIATRTLSLGINMPCRTVVFLGDSLQLNALNFHQAAGRAGRRGFDLLGHVGFLGVPLHKIYRLLTTKLWDIQGQFPLTTSLVLQLSQLISGSQAGPFARDTIHALMDEPKFMANGSILSNQVNHHLRFVIEYLRREGLLDVYGNPINLASLTMHLYYTEPSNYAFMNLLKAGVFHKIAEKFATEKFEAMRDTVVILCHLFGRIRMNEQYVMTLEGSTDLAQSTVVLPPLPTEIADVLDAHDQRVLDLYKTYAWYYQKHGNIGVAANKLPLSNTTIEGSAKLPSSLSVGVMSEFCGLAGYNESMVGTTSSFLDKVPDGIFLKTSRLPIFEANKAPYNAYLLDFFTHGSVDMLIEQNNLKQSEIWFVLNDFSLVLATICSCLGNLLNLVTDEDIENAMSALEGSNAVQATTESEATGADWMQNMNGNYSTTLASPELEEKMDMNLFKVYCMFLEVRNQFDAKFRKMWA
Protein: Vomeronasal 2, receptor 120 (A0A3Q4EGL8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLIFVSVLLFLNFPVASCEPINPGCSLGMADAIFQDGDVLVDCHFVLLTVSIALQKIFHFLRFHLSFPMFIYRIHPNKYQYVIALNFAIEEINKNIHLLPNISLGYDMYSIVQYQATILEHSIRFLTGLKEAIPNYTCRKESKLIAVVTGTSWEFPSRISTILGLYKYPQNPLGLFEIYGIVFFTSLHIFFSHQLTFGPFDPMLSDHVKFPFIYQMAPEDTSLALGMVSLMVHFSWTWVGLIITENEKGIKFLSDLKREMKKNSVCAAFVQMLSLKYRYNWNDLLSTDPAIMGEMLHPFLKNIQFNNPSGDKVDLSHTGKLETKYDIFNFWNFPQGLGLKVKVGTFSSFLPRNKQFSLSDGMIEWGTKDKQTPLSVCSTSCAPGLMKSPQEGKASCCFDCHPCLENEISNETDSIQCIKCPDDQYANTEQTHCIPKAVTFLAYEDPLGMALACMALCFSALTALVLGVFVKHHETPIVKANNRTLSYILLISLILCFLCSLPFIGLPNMATCILQQMSFGVVFTIAVSTVLAKTVTVVLAFRSTVPGRRMRWILVSPNLIIPICTLIQMVLCAIWLGASAPFVDINAHNERGHITIMCNKGSATAFYCVLGYLGFLAMGTLTVAFWARNLPDIFNEAKFLTFSMLVFCSVWVTFLPVYHSTKGKVMVAVEVFSILASSAGLLGCIFVPKCYIILIRPKNGSFKGLRGTRVCK
Protein: C-C chemokine receptor type 2 (C-C CKR-2) (CC-CKR-2) (CCR-2) (CCR2) (CD antigen CD192) (O55193)
Organism: Rattus norvegicus (Rat)
Function: Key functional receptor for CCL2 but can also bind CCL7 and CCL12 (By similarity). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (By similarity). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (By similarity). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation (By similarity). Facilitates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression; signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity). Mediates the recruitment of macrophages and monocytes to the injury site following brain injury (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P41597}; Multi-pass membrane protein {ECO:0000255}. Note=The chemoattractant receptors are distributed throughout the cell surface; after stimulation with a ligand, such as CCL2, they are rapidly recruited into microdomain clusters at the cell membrane. {ECO:0000250|UniProtKB:P41597}.
Interaction partners:
Sequence:
MEDSNMLPQFIHGILSTSHSLFPRSIQELDEGATTPYDYDDGEPCHKTSVKQIGAWILPPLYSLVFIFGFVGNMLVIIILISCKKLKSMTDIYLFNLAISDLLFLLTLPFWAHYAANEWVFGNIMCKLFTGLYHIGYFGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVITSVVTWVVAVFASLPGIIFTKSEQEDDQHTCGPYFPTIWKNFQTIMRNILSLILPLLVMVICYSGILHTLFRCRNEKKRHRAVRLIFAIMIVYFLFWTPYNIVLFLTTFQEFLGMSNCVVDMHLDQAMQVTETLGMTHCCVNPIIYAFVGEKFRRYLSIFFRKHIAKNLCKQCPVFYRETADRVSSTFTPSTGEQEVSVGL
Protein: Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (EC 6.2.1.4) (GTP-specific succinyl-CoA synthetase subunit beta) (G-SCS) (GTPSCS) (Succinyl-CoA synthetase beta-G chain) (SCS-betaG) (A0A8I6AHY6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03221}.
Interaction partners:
Sequence:
MASAVAIAAQAGKLLRERSLRPRLLAVRSQAGHLTPRRWLNLQEYQSKKLMSEHGVRVQRFFVASTAKEAQEAAKRLNAKEIVLKAQILAGGRGKGVFDSGLKGGVHLTKDPKVVGQLAQQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSHNGPVLVGSPQGGVDIEEVAASSPELIFKEQIDIFEGIKDSQAQRMAENLGFLGSLKNQAADQIKKLYHLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAARYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTSDPKVEAILVNIFGGIVNCAIIANGITKACQELELKVPLVVRLEGESLSSPHSFPFPACSGPTHFLNCRKLG
Protein: Cyclic di-GMP-binding protein (Cellulose synthase regulatory subunit) (P37652)
Organism: Escherichia coli (strain K12)
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular location: Cell inner membrane; Single-pass type I membrane protein.
Interaction partners:
- Cellulose synthase catalytic subunit
- Endoglucanase
- Cellulose synthase operon protein C
- Cellulose biosynthesis protein BcsF
- Cyclic di-GMP binding protein BcsE
- Protein YhjR
- Cellulose biosynthesis protein BcsG
- Probable cyclic di-GMP phosphodiesterase PdeK
- Poly-beta-1,6-N-acetyl-D-glucosamine synthase
Sequence:
MKRKLFWICAVAMGMSAFPSFMTQATPATQPLINAEPAVAAQTEQNPQVGQVMPGVQGADAPVVAQNGPSRDVKLTFAQIAPPPGSMVLRGINPNGSIEFGMRSDEVVTKAMLNLEYTPSPSLLPVQSQLKVYLNDELMGVLPVTKEQLGKKTLAQMPINPLFISDFNRVRLEFVGHYQDVCEKPASTTLWLDVGRSSGLDLTYQTLNVKNDLSHFPVPFFDPSDNRTNTLPMVFAGAPDVGLQQASAIVASWFGSRSGWRGQNFPVLYNQLPDRNAIVFATNDKRPDFLRDHPAVKAPVIEMINHPQNPYVKLLVVFGRDDKDLLQAAKGIAQGNILFRGESVVVNEVKPLLPRKPYDAPNWVRTDRPVTFGELKTYEEQLQSSGLEPAAINVSLNLPPDLYLMRSTGIDMDINYRYTMPPVKDSSRMDISLNNQFLQSFNLSSKQEANRLLLRIPVLQGLLDGKTDVSIPALKLGATNQLRFDFEYMNPMPGGSVDNCITFQPVQNHVVIGDDSTIDFSKYYHFIPMPDLRAFANAGFPFSRMADLSQTITVMPKAPNEAQMETLLNTVGFIGAQTGFPAINLTVTDDGSTIQGKDADIMIIGGIPDKLKDDKQIDLLVQATESWVKTPMRQTPFPGIVPDESDRAAETRSTLTSSGAMAAVIGFQSPYNDQRSVIALLADSPRGYEMLNDAVNDSGKRATMFGSVAVIRESGINSLRVGDVYYVGHLPWFERVWYALANHPILLAVLAAISVILLAWVLWRLLRIISRRRLNPDNE
Protein: L-olivosyl-oleandolide 3-O-methyltransferase (EC 2.1.1.239) (Oleandomycin biosynthesis protein Y) (O87833)
Organism: Streptomyces antibioticus
Function: 3-O-methyltransferase involved in the synthesis of L-oleandrose, a sugar attached to oleandomycin, a macrolide antibiotic. Acts on monoglycosylated macrolactones and mediates the conversion of L-olivosyl-erythronolide B into its 3-O-methylated derivative, L-oleandrosyl-erythronolide B. Also able to methylate other monoglycosylated derivatives, such as L-rhamnosyl- and L-mycarosyl-erythronolide B.
Interaction partners:
Sequence:
MSYDDHAVLEAILRCAGGDERFLLNTVEEWGAAEITAALVDELLFRCEIPQVGGEAFIGLDVLHGADRISHVLQVTDGKPVTSAEPAGQELGGRTWSSRSATLLRELFGPPSGRTAGGFGVSFLPDLRGPRTMEGAALAARATNVVLHATTNETPPLDRLALRYESDKWGGVHWFTGHYDRHLRAVRDQAVRILEIGIGGYDDLLPSGASLKMWKRYFPRGLVFGVDIFDSRRATSRVSRRSAARQDDPEFMRRVAEEHGPFDVIIDDGSHINAHMRTSFSVMFPHLRNGGFYVIEDTFTSYWPGYGGPSGARCPSGTTALEMVKGLIDSVHYEERPDGAATADYIARNLVGLHAYQTTSSSSRRAINKEGGIPHTVPREPFWNDN
Protein: Interferon lambda receptor 1 (IFN-lambda R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Q8CGK5)
Organism: Mus musculus (Mouse)
Function: The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Determines the cell type specificity of the lambda interferon action. Shows a more restricted pattern of expression in the epithelial tissues thereby limiting responses to lambda interferons primarily to epithelial cells of the respiratory, gastrointestinal, and reproductive tracts. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Interleukin-10 receptor subunit beta
- Tyrosine-protein kinase JAK1
- Interferon lambda-2
- Interferon lambda-3
- Non-receptor tyrosine-protein kinase TYK2
- Interferon beta
- Interferon gamma
- Interleukin-10
- Interferon kappa
- Interferon epsilon
Sequence:
MWRADRWAPLLLFLLQSALGRPRLAPPRNVTLFSQNFTVYLTWLPGLGSPPNVTYFVTYQSYIKTGWRPVEHCAGIKALVCPLMCLKKLNLYSKFKGRVQAASAHGRSPRVESRYLEYLFDVELAPPTLVLTQMEKILRVNATYQLPPCMPSLELKYQVEFWKEGLGSKTLFPDTPYGQPVQIPLQQGASRRHCLSARTVYTLIDIKYSQFSEPSCIFLEAPGDKRAVLAMPSLLLLLIAAVAAGVAWKIMKGNPWFQGVKTPRALDFSEYRYPVATFQPSGPEFSDDLILCPQKELTIRNRPAPQVRNPATLQAGPERDSTEDEDEDTDYDDDGDSVQPYLERPLFISEKPRVMEHSETDESGVDSGGPWTSPVGSDGSSAWDSSDRSWSSTGDSSYKDEVGSSSCLDRKEPDQAPCGDWLQEALPCLEFSEDLGTVEEPLKDGLSGWRISGSLSSKRDLAPVEPPVSLQTLTFCWVNNPEGEEEQEDEEEEEEEEEEEDWESEPKGSNAGCWGTSSVQRTEVRGRMLGDYLVR