wanglab/gogpt-training-data huggingface dataset:
Protein: Ras-related protein Rab-30 (Q15771)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Required for maintaining the structural integrity of the Golgi apparatus, possibly by mediating interactions with cytoplasmic scaffolding proteins.
Subcellular location: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:22188167}. Cytoplasm {ECO:0000269|PubMed:22188167}. Golgi apparatus {ECO:0000269|PubMed:22188167}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 4
- GRIP and coiled-coil domain-containing protein 2
Sequence:
MSMEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEINGEKVKLQIWDTAGQERFRSITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYASNKVITVLVGNKIDLAERREVSQQRAEEFSEAQDMYYLETSAKESDNVEKLFLDLACRLISEARQNTLVNNVSSPLPGEGKSISYLTCCNFN
Protein: Suppressor of variegation 2-10, isoform M (A0A0B4K6T9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRKTRSQTARTQAENAATSSSPGHQSTSSAPIAVNPFDSTKYKECEQMVQMLRVVELQKILSFLNISFAGRKTDLQSRILSFLRTNLELLAPKVQEVYAQSVQEQNATLQYIDPTRMYSHIQLPPTVQPNPVGLVGSGQGVQVPGGQMNVVGGAPFLHTHSINSQLPIHPDVRLKKLAFYDVLGTLIKPSTLVPRNTQRVQEVPFYFTLTPQQATEIASNRDIRNSSKVEHAIQVQLRFCLVETSCDQEDCFPPNVNVKVNNKLCQLPNVIPTNRPNVEPKRPPRPVNVTSNVKLSPTVTNTITVQWCPDYTRSYCLAVYLVKKLTSTQLLQRMKTKGVKPADYTRGLIKEKLTEDADCEIATTMLKVSLNCPLGKMKMLLPCRASTCSHLQCFDASLYLQMNERKPTWNCPVCDKPAIYDNLVIDGYFQEVLGSSLLKSDDTEIQLHQDGSWSTPGLRSETQILDTPSKPAQKVEVISDDIELISDDAKPVKRDLSPAQDEQPTSTSNSETVDLTLSDSDDDMPLAKRRPPAKQAVASSTSNGSGGGQRAYTPAQQPQQSGRRHNRQVL
Protein: CDGSH iron-sulfur domain-containing protein 3, mitochondrial (Melanoma nuclear protein 13) (B1AR13)
Organism: Mus musculus (Mouse)
Function: Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P0C7P0}.
Interaction partners:
- CDGSH iron-sulfur domain-containing protein 1
- CDGSH iron-sulfur domain-containing protein 2
- Large ribosomal subunit protein bL17m
Sequence:
MGFRRLSFPTDFIFLFPNHICLPALSKPYQRREISSWLARWFPKDPAKPVVAQKTPIRLELVAGKTYRWCVCGRSKNQPFCDGSHFFQRTGLSPLKFKAQETRTVALCTCKATQRPPYCDGTHKSEQVQKAEVGSPL
Protein: KICSTOR complex protein kaptin (Actin-associated protein 2E4) (Q9Y664)
Organism: Homo sapiens (Human)
Function: As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids. In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:28199306}. Cell projection, lamellipodium {ECO:0000269|PubMed:10099934, ECO:0000269|PubMed:24239382}. Cell projection, stereocilium {ECO:0000250|UniProtKB:A0A1D5PJB7}. Note=Localization to lysosomes is amino acid-independent (PubMed:28199306). Colocalizes with F-actin (PubMed:24239382). {ECO:0000269|PubMed:24239382, ECO:0000269|PubMed:28199306}.
Interaction partners:
- KICSTOR complex protein ITFG2
- GATOR1 complex protein NPRL2
- GATOR1 complex protein NPRL3
- KICSTOR complex protein SZT2
- GATOR1 complex protein DEPDC5
- GATOR2 complex protein WDR24
- KICSTOR subunit 2
- Nucleoporin SEH1
- GATOR2 complex protein WDR59
- GATOR2 complex protein MIOS
Sequence:
MMGEAAVAAGPCPLREDSFTRFSSQSNVYGLAGGAGGRGELLAATLKGKVLGFRYQDLRQKIRPVAKELQFNYIPVDAEIVSIDTFNKSPPKRGLVVGITFIKDSGDKGSPFLNIYCDYEPGSEYNLDSIAQSCLNLELQFTPFQLCHAEVQVGDQLETVFLLSGNDPAIHLYKENEGLHQFEEQPVENLFPELTNLTSSVLWLDVHNFPGTSRRLSALGCQSGYVRVAHVDQRSREVLQMWSVLQDGPISRVIVFSLSAAKETKDRPLQDEYSVLVASMLEPAVVYRDLLNRGLEDQLLLPGSDQFDSVLCSLVTDVDLDGRPEVLVATYGQELLCYKYRGPESGLPEAQHGFHLLWQRSFSSPLLAMAHVDLTGDGLQELAVVSLKGVHILQHSLIQASELVLTRLRHQVEQRRRRLQGLEDGAGAGPAENAAS
Protein: DnaJ homolog subfamily C member 12 (J domain-containing protein 1) (Q9UKB3)
Organism: Homo sapiens (Human)
Subcellular location: [Isoform a]: Cytoplasm {ECO:0000269|PubMed:24122553}.
Interaction partners:
- DnaJ homolog subfamily B member 4
- DnaJ homolog subfamily B member 1
- Heat shock 70 kDa protein 4
Sequence:
MDAILNYRSEDTEDYYTLLGCDELSSVEQILAEFKVRALECHPDKHPENPKAVETFQKLQKAKEILTNEESRARYDHWRRSQMSMPFQQWEALNDSVKTSMHWVVRGKKDLMLEESDKTHTTKMENEECNEQRERKKEELASTAEKTEQKEPKPLEKSVSPQNSDSSGFADVNGWHLRFRWSKDAPSELLRKFRNYEI
Protein: GH10160p (Murashka, isoform C) (Q9VHC2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-conjugating enzyme E2-22 kDa
- Polyubiquitin
- Ubiquitin-like domain-containing protein
- GH17761p
Sequence:
MLNSNATGGNNHGGSSRRPFTRNSSSVRSQRGGGGGLGGRMVYSPHTHPHVQQQQQQQQQQQQQGQQRSSNNGNNNLWLGNSPWCNVNLNGGNSGNNNNNGGNNNNNNGGNISSNNNSNNVNNKDANPNCDVQTSNSSGTCIYNNSKAHHHHNNSNNNGHTQSHIHTNHSLHQGHHHPHHTQMHTPHYPHSSSPQQSNSYRQYPPHSYSPNSPHSNGHTNSNASNNPISQRSNPQAHPNQNQNSNFYEMCTGSGGSHTYGSMSVSLVRLNPARLCLTLGPVTPPAQRVVSFGHRSHSHSNSSSNTSSSDQNQHNPPPRSQNHHPNPHHSQYQYQYQYQYRYQYHPPHQYHPLHSPQQQTNRQSLPLTRTNSNSINATTFNSTNPTTNSNPTDVVNVNSCTDIIPYGSSSTSSSASSMLPQQQQHQINNASAPINSHSQGQGPGNSPNLGHNHQRGYNNGNNNRGIGNGIVNGNTNGPPDYMNYRRGVCPAQSRDYSGNGNGNNNGHGHNGRRYMSDNLNNPSSSMNGLINSGHHQRNYNDRNLNNHFGNSEQNGGPDHRDRAEGSSYNFMRNGGGSGGGGYGRNGSHYQHMAYGNNNGASTSTGGPGLMGELPSGSGLSGSSLSLNNGPGGLNSDSPSRKRRRISGRPPNGPQPQHRCPMAHMQQGSPPLRRPRLRDVATSTQQQQQQYGHQVHHPQQQQQQPPSNYHPMHHHQPQPHYVPQQQVPPPHVQRSPWDLGSSGGSSGGATSSSSVGPILQQVQAPPQPPSHQQAVGYPQAPPQPASLMVDLNLNQVPVNLQLRPSEPFWASFCTYPIPAQARLAPCHLHGVYTQPFPAAPPPGLAAPPLQQQHQPLIQAQQMISQATLTAQQQQRDVVAIATANLGPIEAPGAHGHPHAHPHAHPHAHQLPPGIHITPLSGAAAAAATHHLHSTAAAAAAVAAGAQITTAQQILFSSDRRTFPPHRRIPRFWTANHGHRHVLPPQSLAAHQAPVQIQATSGIINPGFLLNFLAMFPLSPYNQHDLSSGDTNETENYEALLSLAERLGEAKPRGLTRNEIDQLPSYKFNPEVHNGDQSSCVVCMCDFELRQLLRVLPCSHEFHAKCVDKWLRSNRTCPICRGNASDYFDGVDQQQQSQATAGAAAALSGTSGGSAGVAGTSEASAATANPQQSQAA
Protein: 40S ribosomal protein S27 (Q8IEN2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 40S ribosomal protein S21
- 40S ribosomal protein S24
- 60S ribosomal protein L13
- 60S ribosomal protein L35ae, putative
- 40S ribosomal protein S6
- 60S ribosomal protein L18-2, putative
- 60S ribosomal protein L6, putative
- 60S ribosomal protein L26, putative
- 40S ribosomal protein S11, putative
- 40S ribosomal protein S28e, putative
Sequence:
MNVDLLNPDPVEESKKHKLKRLIPTPNSYFMDVKCPGCLQITTLFSHAQNVVLCGSCNIMLCQPTGGKCKLTEGCSFRKKIE
Protein: L-asparaginase 2-2 (EC 3.5.1.1) (L-asparaginase II) (L-asparagine amidohydrolase II) (ASP II) (P0CX77)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Secreted. Periplasm.
Interaction partners:
Sequence:
MRSLNTLLLSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTDPSEIPEVIILYSYQGLNPELIVKAVKDLGAKGIVLAGSGAGSWTATGSIVNEQLYEEYGIPIVHSRRTADGTVPPDDAPEYAIGSGYLNPQKSRILLQLCLYSGYGMDQIRSVFSGVYGG
Protein: PLAC8 family protein (Q9CAJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAASQDKLDKMKLRQDYRNLWHSDLMGTVTADTPYCCISCLCGPCVSYMLRRRALYNDMSRYTCCAGYMPCSGRCGESKCPQLCLATEVFLCFGNSVASTRFLLQDEFNIQTTQCDNCIIGFMFCLSQVACIFSIVACIVGSDELSEASQILSCCADMVYCTVCACMQTQHKLEMDKRDGVFGSQPMGVPPAQQMSRFDQPVPPPVGYPQSYPPPAQGYPPASYPPPGYPQH
Protein: Golgi microtubule-associated protein, isoform B (Golgi microtubule-associated protein, isoform C) (Q9VXU1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MRDVLEHKTQLAGQVASLKQLQADRLVEHELSNARQQKQLDELRQTSSAAKKQQEELQRRVEQQEAELIEMQDLLDKRRQDTAELIERVRVAETERERLLKDLEETRQAKEKKTSESSSNSSSTGKHSEDEFIVVRQADATGSGSASGSDRDPDADVTSPPSKEKLRDRLVSLESQISELTLANTQLQDAQLEKQLSINMLGEQLVELEKRLRLSEAEKEQLQVNLQLRLQQLTVQNQELKLHAEAEQEGHAQNLEEQLGDLREDNQRLRQELKTSIAQAKFRQAIAEEKQEITDLDDADSEYGTFELDKLRALLQAEIEDRLDSSFPQQKLERAWNALKDRWHRLDLVEQRLVDVQNQQLVSEHEKKTLEADISQYILQCDELMKNNDLLLNELDKYKRNKLETIEEHHEETIVQLEAQLEEARQKLELASLSSQQQMETHLISSPEKTPVDSELLAKMEQKEQEYLQLQEQLAFAKTELDKRNKLLERNGEQLTKQQQQNQADQKKLEELSQLRETLQRRDEDLKELEEQLSAVRQDLDEKSIQMKISQDQHKLQLANLQNQLQADQEKLRELLQLQDKLEQQKELMEVDQNQQITIIKKELAETTNQLSECQERLTVKEAQLAEIQQQLQEVNEERTRLQEQLLTKEQESGLDSELAKRNQELEDQLLAKEQQLQLNQAELEKLQETLRVNEEQLLAKEEQLHAKESQLQSLESQLQGQLAADESQQLQQTIDGLGQEKNELIKVLQQKHQENTQYYAEIQRLQPFEQQVKELVKEREKLQDQVGFLKEKSDILTTNLLTEQTNQRLLQQQQAESQEQQASTLRDLERLRAHLLEIEELHTQETVELQRDLEESRSRQAILEQQVSKSSTAYTSASIRANQQAETLQAQHALLQQQRDELLAKLGQYEDRELKQQAALTNLQCALEQFQNDKDHDIEMATQRIRREMQAQLDRQGQLQLEMSGLQQQLAEANQGLRAAARLSDQLEAGQQTIAVLRDEVESLKEANGQLEQRLSSSESSQTDKIDKSLIKSLLIGYVVSGHAGDKQQVLRMISSVLDFNAQEADKVGLNKQQSSWLGAILGGGSATASAAGSSRGNENLVQAFVQFLEQESQPQAQSRPTLLSMTGQMDGVTSASATTSTAATSGHLPQASSSFSPATPAASQQDPAAPRTPPVGGSPQLLAMGSNEFAPTRNSSSILKDILSDS
Protein: Signal transducer and activator of transcription (O93599)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
- Tyrosine-protein kinase.
- Tyrosine-protein kinase
- Interferon regulatory factor 9.
- Proto-oncogene tyrosine-protein kinase Src
- Tyrosine-protein kinase JAK1
- Histone deacetylase 1
- Forkhead box protein O1-A
- Tyrosine-protein kinase.
- Suppressor of cytokine signaling 3
- Signal transducer and activator of transcription.
Sequence:
MAQWNQLQQLETRYLEQLYHLYSDSFPMELRQFLAPWIESQDWAYAANKESHATLVFHNLLGEIDQQYSRFLQENNVLYQHNLRRIKQHLQSKYLEKPMEIARIVARCLWEEQRLLQTATTAQQDGQVAHPTGTVVTEKQQILEHNLQDIRKRVQDMEQKMKMLENLQDDFDFNYKTLKSAGELSQDLNGNSQAAATRQKMSQLEQMLSALDQLRRQIVTEMAGLLSAMDFVQKNLTDEELADWKRRQQIACIGGPPNICLDRLETWITSLAESQLQIRQQIRKLEELQQKVSYKGDPIIQHRPALEEKIVDLFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKESGDVAAIRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRTNSDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNHPKNVNFFTKPPVGTWDQVAEVLSWQFSSTTKRGLTIEQLTTLAEKLLGPCVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSPKPPGTFLLRFSESSKEGGITFTWVEKDINGKTQIQSVEPYTKQQLNSMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPEAHPDTEFPDTGCVTQPYLKTKFICVTPCPSVFMDFPDSELLGNGFPGTNSGNTSDLFPMSPRTLDSLMHNEAAEANPGPLESLTLDMELSSDHASPMREGFAASTVSDMDTCRNA
Protein: CD55 molecule (Cromer blood group) (Decay-accelerating factor CD55) (Q9GLM2)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MSPLPRSAPAVRRLMGGQTPPPLLLLLLLLCIPAAQGDCSLPPDVPNAQPDLRGLASFPEQTTITYKCNKGFVKVPGMADSVLCLNDKWSEVAEFCNRSCDVPTRLHFASLKKSYSKQNYFPEGFTVEYECRKGYKRDLTLSEKLTCLQNFTWSKPDEFCKKKQCPTPGELKNGHVNITTDLLFGASIFFSCNAGYRLVGATSSYCFAIANDVEWSDPLPECQEISPTVKAIPAVEKPITVNFPATKYPAIPRATTSFHSSTSKNRGNPSSGMRIMSSGTMLLIAGGVAVIIIIVALILAKGFWHYGKSGSYHTHENNKAVNVAFYNLPATGDAADVRPGN
Protein: Lipoxygenase (EC 1.13.11.-) (Q6X5R6)
Organism: Nicotiana attenuata (Coyote tobacco)
Interaction partners:
Sequence:
KPQLHQTSESKKTLIPWSATKSFTSGEILASFPINILSKNIRQNPKKNFRVHYYAANSTKAVLSSTEKSTSVKAVVTVQKTVGGTNLAWTRGLDDIGDLLGKTLLLWIVAAEFDPKTGIKKPSIKTFAHRGRDVDDDTHYEADFVIPEDFGEVGAVLVENEHHKEMYVKNIVIDGFPHGKVHITCNSWVHSKFDNPEKRIFFTNKSYLPSQTPSAIKRLRERELVIMRGDGYGERKQFERIYDYDVYNDIGDPDANDDAKRPVLGGQEFPYPRRCRTGRPRSKTDPLSESRSNFVYVPRDEAFSEVKSLTFSGNTLYSVLHAVVPALESVAVDDPNAGFPHFPAIDSLFNVGVRLPPLNDKSSLLNIIPRLIKAISDTQKDVLLFETPELLQRDKFSWFKDVEFARQTLAGLNPYSIRLVTEWPLKSKLDPEIYGPPESAITKELIELEIAGFMTVEEAVKQKKLFILDYHDLLLPYVNKVNELKGRVLYGSRTLFFLTPDGTLRPLAIELTRPPVHDKPQWKEVYCPTWHATGSWLWKLAKAHVLAHDSGYHQLVSHWLRTHCATEPYIIATNRQLSAIHPIYRLLHPHFRYTMEINALAREALINANGIIESSFFPGKYAMELSSVAYDLEWRFDREALPEDLISRGMAVKDPNAPYGLKLTIEDYPFANDGLVLWDILIQWVTDYVNHYYTETKLIESDTELQAWWTEIKNVGHGDKKDEPWWPELKTPDDLIGIITTIVWVTSGHHAAVNFGQYSYAGYFPNRPTTARAKMPTEDPTDEEWENFLKRPEDALLKCFPSQMQATKVMAILDVLSNHSPDEEYIGEKIEPYWAEDPVINAAFEKFSGRLKELEGIIDGRNADSNLMNRNGAGVVPYELLKPFSGPGVTGKGVPYSISI
Protein: Catalase isozyme C (CAT-C) (OsCatC) (EC 1.11.1.6) (Protein NITRIC OXIDE EXCESS 1) (Q10S82)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Responsible for the redox homeostasis in leaves. Prevents nitric oxide (NO) accumulation and subsequent NO-mediated leaf cell death as well as the S-nitrosylation of specific proteins (e.g. glyceraldehyde 3-phosphate dehydrogenase and thioredoxin) by degrading H(2)O(2). Involved in photorespiration. Promotes drought stress tolerance and recovery (Ref.13). Involved in NO-mediated enhanced tolerance to zinc oxide nanoparticles (ZnO NPs)-induced phytotoxicity. Participates in melatonin-mediated detoxification.
Subcellular location: Peroxisome {ECO:0000269|PubMed:26900141, ECO:0000305|PubMed:21398647}. Glyoxysome {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:29581216}.
Interaction partners:
- Os09g0544900 protein
- Peroxisomal
- Catalase isozyme A
- Catalase isozyme B
- Glycolate oxidase 3
- Os01g0357200 protein
- Os06g0211300 protein
- Os02g0765800 protein.
- Superoxide dismutase 2, chloroplastic
- Superoxide dismutase, mitochondrial
Sequence:
MDPYKHRPSSSFNGPLWSTNSGAPVWNNNNSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDITHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHVQENWRILDFFSHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATQDLYDSIAAGNFPEWKLFIQTIDPDHEDRFDFDPLDVTKTWPEDIVPLQPVGRMVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYLLLPPNAPKCAHHNNHYDGFMNFMHRDEEVDYFPSRYDPAKHAPRYPIPSATLTGRREKVVIAKENNFKQPGERYRSWDPARQDRFIKRWIDALSDPRLTHEIRSIWLSYWSQADRSLGQKLASRLSAKPSM
Protein: Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (Q9W734)
Organism: Gallus gallus (Chicken)
Function: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta. Acts as a mediator of TGF-beta and BMP anti-inflammatory activities. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of pro-inflammatory genes. Blocks the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase.
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog.
- SMAD specific E3 ubiquitin protein ligase 2.
- Mothers against decapentaplegic homolog 5
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog
- receptor protein serine/threonine kinase
- Bone morphogenetic protein receptor type-1B
Sequence:
MFRSKRSGLVRRLWRSRVIPERDGGDGNGQSSERNATAVTAEGQRMAQPRRAQEGEGRPVRCCLFAERPGPELPPPPPPPPPGGASPPGPGGGEARSRLVLLERELKAVTYALLKRLKERSLHSLLQAVESRGGTPGGCVLVARGELRLGAARRPPPHLLLGKLFRWPDLQHPAELKALCECQSFGAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPNDEQKPLDLSDSTLSYTETEATNSPNVTPGEFSDASTSPDAVKRSHWCNVAYWEHRTRVGRLYTVYEQSVSIFYDLPQGNGFCLGQLNLENRSETVRRTRSKIGYGILLSKEPDGVWAYNRSEHPIFVNSPTLDIPNCRTLIVRKVMPGYSIKVFDYEKSCLLQHTAELDYADGPYDPNSVRISFAKGWGPCYSRQFITSCPCWLEILLSNNR
Protein: RNA 3'-terminal phosphate cyclase (RNA cyclase) (RNA-3'-phosphate cyclase) (EC 6.5.1.4) (O77264)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O00442}. Nucleus {ECO:0000269|PubMed:25961792}.
Interaction partners:
- RNA-splicing ligase RtcB homolog
- LD10780p
- FI08810p
- U3 small nucleolar RNA-associated protein 18 homolog
- GH01043p
- Bystin
- RE67794p
- Lethal
- LD47749p
- LD47550p
Sequence:
MDAEKMLEIDGSYLEGGGQALRNALSLSCILGKPVRVVKIRASRPSPGLSHQHLHGLNLLRDITNADVVGNYLLSSTVEFTPRTILDNTYRVETHTAASITLIYQMALPVLLFAGRPSRLIVSGGTNVDFAPPVEYMQEVLLPNLKHFGVSFDLKVQRYGFYPRGQGRCQLDVQPVTKLNSGKLVAFGRIKSVSGVAYCAGRLPVNIAIDMQQTAQREIHRLWPSQQCSIEPIKHSRQKAFHNGAGILMTVNTTSDVVLGASALGKKRIDGHVLGSEASCQLGDYMRKQVCVDDYMQDQLIIYMALAVGRSTMRTGKLTNHTRTAINVAEQMTGVKFDVAMEPGGQMLVSCKGLGHVNKLI
Protein: Ribonucleoside-diphosphate reductase large subunit-like protein (Viral inhibitor of RIP activation) [Cleaved into: N-terminal peptide; 116 kDa peptide] (Q06A28)
Organism: Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus)
Function: Provides optimal viral replication conditions by promoting host cell survival and avoiding the host inflammatory response linked to NF-kappa-B activation. Blocks RIPK1 ubiquitination, thereby preventing NF-kappa-B activation and virally induced inflammatory response. Prevents host necroptosis by targeting RIPK3 thereby preventing the formation of necroptotic RIPK1-RIPK3 complexes. Also inhibits ZBP1-induced necroptosis. Does not have ribonucleotide reductase activity. Betaherpesviruses probably use another strategy to expand the dNTP pool in a quiescent host cell.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04027, ECO:0000269|PubMed:15047841}. Host cytoplasm. Note=Starts to be expressed at 12 hours after infection and accumulates in the cytoplasm of the infected cells. {ECO:0000255|HAMAP-Rule:MF_04027, ECO:0000269|PubMed:15047841}.
Interaction partners:
Sequence:
MDRQPKVYSDPDNGFFFLDVPMPDDGQGGQQTATTAAGGAFGVGGGHSVPYVRIMNGVSGIQIGNHNAMSIASCWSPSYTDRRRRSYPKTATNAAADRVAAAVSAANAAVNAAAAAAAAGGGGGANLLAAAVTCANQRGCCGGNGGHSLPPTRMPKTNATAAAAPAVAGASNAKSDNNHANATSGAGSAAATPAATTPAATAVENRRPSPSPSTASTAPCDEGSSPRHHRPSHVSVGTQATPSTPIPIPAPRCSTGQQQQQPQAKKLKPAKADPLLYAATMPPPASVTTAAAAAVAPESESSPAASAPPAAAAMATGGDDEDQSSFSFVSDDVLGEFEDLRIAGLPVRDEMRPPTPTMTVIPVSRPFRAGRDSGRDALFDDAVESVRCYCHGILGNSRFCALVNEKCSEPAKERMARIRRYAADVTRCGPLALYTAIVSSANRLIQTDPSCDLDLAECYVETASKRNAVPLSAFYRDCDRLRDAVAAFFKTYGMVVDAMAQRITERVGPALGRGLYSTVVMMDRCGNSFQGREETPISVFARVAAALAVECEVDGGVSYKILSSKPVDAAQAFDAFLSALCSFAIIPSPRVLAYAGFGGSNPIFDAVSYRAQFYSAESTINGTLHDICDMVTNGLSVSVSAADLGGDIVASLHILGQQCKALRPYARFKTVLRIYFDIWSVDALKIFSFILDVGREYEGLMAFAVNTPRIFWDRYLDSSGDKMWLMFARREAAALCGLDLKSFRNVYEKMERDGRSAITVSPWWAVCQLDACVARGNTAVVFPHNVKSMIPENIGRPAVCGPGVSVVSGGFVGCTPIHELCINLENCVLEGAAVESSVDVVLGLGCRFSFKALESLVRDAVVLGNLLIDMTVRTNAYGAGKLLTLYRDLHIGVVGFHAVMNRLGQKFADMESYDLNQRIAEFIYYTAVRASVDLCMAGADPFPKFPKSLYAAGRFYPDLFDDDERGPRRMTKEFLEKLREDVVKHGIRNASFITGCSADEAANLAGTTPGFWPRRDNVFLEQTPLMMTPTKDQMLDECVRSVKIEPHRLHEEDLSCLGENRPVELPVLNSRLRQISKESATVAVRRGRSAPFYDDSDDEDEVACSETGWTVSTDAVIKMCVDRQPFVDHAQSLPVAIGFGGSSVELARHLRRGNALGLSVGVYKCSMPPSVNYR
Protein: Large ribosomal subunit protein uL23A (60S ribosomal protein L25-A) (Q10330)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This protein binds to a specific region on the 26S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL22
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL30A
Sequence:
MSVAKAKGAQKTVQKGIHNKVAKKVRTSTTFRRPKTLQLSRKPKYARKSVAHAPRLDEYKIIVNPINSESAMKKIEDDNTLVFHVHLKANKFTIKEAVRKLYSVEPVKINTLIRPNGTKKAFVKLSADADALDVANRIGFL
Protein: Adenosine 5'-monophosphoramidase HINT3 (EC 3.9.1.-) (Histidine triad nucleotide-binding protein 3) (HINT-3) (Q9NQE9)
Organism: Homo sapiens (Human)
Function: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase. Hydrolyzes 3-indolepropionic acyl-adenylate and fluorogenic purine nucleoside tryptamine phosphoramidates in vitro.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17870088}. Nucleus {ECO:0000269|PubMed:17870088}. Note=Localized as aggregates in the cytoplasm and the nucleus.
Interaction partners:
- Adenosine 5'-monophosphoramidase HINT2
- Adenosine 5'-monophosphoramidase HINT1
Sequence:
MAEEQVNRSAGLAPDCEASATAETTVSSVGTCEAAGKSPEPKDYDSTCVFCRIAGRQDPGTELLHCENEDLICFKDIKPAATHHYLVVPKKHIGNCRTLRKDQVELVENMVTVGKTILERNNFTDFTNVRMGFHMPPFCSISHLHLHVLAPVDQLGFLSKLVYRVNSYWFITADHLIEKLRT
Protein: Corticotropin-releasing factor receptor 2 (CRF-R-2) (CRF-R2) (CRFR-2) (CRF-RB) (Corticotropin-releasing hormone receptor 2) (CRH-R-2) (CRH-R2) (Q60748)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Urocortin-2
- Corticoliberin
- Urocortin-3
- Urocortin
- Corticotropin-releasing factor receptor 1
- Corticotropin-releasing factor-binding protein
- Pro-opiomelanocortin
- Guanine nucleotide-binding protein G
Sequence:
MDAALLLSLLEANCSLALAEELLLDGWGVPPDPEGPYTYCNTTLDQIGTCWPQSAPGALVERPCPEYFNGIKYNTTRNAYRECLENGTWASRVNYSHCEPILDDKQRKYDLHYRIALIVNYLGHCVSVVALVAAFLLFLVLRSIRCLRNVIHWNLITTFILRNIAWFLLQLIDHEVHEGNEVWCRCITTIFNYFVVTNFFWMFVEGCYLHTAIVMTYSTEHLRKWLFLFIGWCIPCPIIIAWAVGKLYYENEQCWFGKEAGDLVDYIYQGPVMLVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDLSQIVFIYFNSFLQSFQGFFVSVFYCFFNGEVRAALRKRWHRWQDHHALRVPVARAMSIPTSPTRISFHSIKQTAAV