wanglab/gogpt-training-data huggingface dataset:
Protein: Ceramide synthase LOH2 (CS2) (CSI) (EC 2.3.1.291) (Protein LONGEVITY ASSURANCE GENE ONE HOMOLOG 2) (LAG One Homolog 2) (LAG1 homolog 2) (LAG1 longevity assurance homolog 2) (Q9LJK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Prevents cell division in root meristems and promotes salicylic acid (SA) production and hypersensitive response (HR). Catalyzes the biosynthesis of ceramide sphingolipids with C(16) fatty acids, structural membrane lipids involved in membrane trafficking (e.g. early endosomes) and cell polarity (e.g. polar auxin transport related proteins); accepts only C16:0 fatty acids, but with a wide range of d18 sphingoid bases, such as sphinganine (d18:0) and palmitoyl-CoA. Mediates resistance to sphinganine-analog mycotoxins (SAMs, e.g. fumonisin B(1)) by restoring the sphingolipid biosynthesis. Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure (By similarity). Contributes to hypoxic conditions tolerance (e.g. submergences), especially in the dark, by promoting the formation of very-long-chain (VLC) ceramide species (22:1, 24:1 and 26:1) and of VLC unsaturated ceramides, which are modulating CTR1-mediated ethylene signaling leading to endoplasmic reticulum (ER)-to-nucleus translocation of EIN2 and EIN3.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8C172}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized CRM domain-containing protein At3g25440
- Sphinganine C4-monooxygenase 2
- Dihydroceramide fatty acyl 2-hydroxylase FAH2
- Ceramide kinase
- Sphinganine C4-monooxygenase 1
- Long chain base biosynthesis protein 2a
- TTF-type zinc finger protein with HAT dimerization domain-containing protein
- Long chain base biosynthesis protein 1
- 3-dehydrosphinganine reductase TSC10B
- 3-dehydrosphinganine reductase TSC10A
Sequence:
MESVSSRGGDPVVKPSMEVWHFQIAVYFAFGFFFLRLVLDRYVFQRIALWLLSTGSAPIKLNDAATRAKIVKCKESLWKLLYYAACDFFVLQVIYHEPWARDIKLYFHGWPNQELKLSIKLYYMCQCGFYVYGVAALLAWETRRKDFAVMMSHHVITIILLSYSYLTSFFRIGAIILALHDASDVFMETAKIFKYSEKEFGASVCFALFAVSWLLLRLIYFPFWIIRATSIELLDYLDMTSAEGTLMYYSFNTMLLMLLVFHIYWWYLICAMIVRLLKNRGKVGEDIRSDSEDDDD
Protein: E3 ubiquitin-protein ligase RNF12-A (EC 2.3.2.27) (RING finger protein 12-A) (RING-type E3 ubiquitin transferase RNF12-A) (XRnf12) (Q641J8)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as an E3 ubiquitin-protein ligase specific for ldb1, mediating ubiquitination and proteasome-dependent degradation of excess ldb1 in a RING-dependent manner. Does not degrade ldb1 bound to lhx1/lim1, nor lim1 itself and thus contributes to the establishment of proper ldb1-lhx1/lim1 stoichiometry and the formation of a ldb1-lhx1/lim1 complex. Interferes with Spemann organizer function and suppresses secondary axis formation induced by ldb1 and lhx1/lim1.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESADSTGKGSIEQSESQRQSQMDRLDREEAFYQFVNNLNEDDYRLMRDNNLLGTPGEITKEELLRRLQQIKEGPPQPSTEETRGDSVSTGGDPAEDSSNGDSIIDWLNSVRQTGNTTRSGQRGNQSWRAVSRTNPNSGDFRFSLEINVNRTSGNPSMPSLDQSAEMPGAEDMEVSSQGEAENEPEPIPIATRSAPAEVTVEEAPIQRGQRRARSRSPDQRRTRARTDRSRSPLHHAVDPPIRRAPHSSSQTVDTSNTEEAEGSSRTRHHVSSQVQNSSSSNETEGSSRTRQHIPARQQVLGTEGQSQSTVHLSNPETRSSSQTPQTDSSTNAETTGTGQRPPTIVLDLQVRRVRPGDYRQRDSIANRTRSRSQTPNNTVTYESERGGFRRTFSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLRQIMTGFGELSYFMYNDNDTDPNNPTAVSPTAAVPGEAQNNANAEVRAPSAEPTEPVAPVETDEGSNVSTTATRREGRNSRGAVTFEESGSLPFLSLAQFFLLNEDDDDQPRGLTKEQIDNLSTRNFGENDALKTCSVCITEYTEGNKLRKLPCSHEYHIHCIDRWLSENSTCPICRRAVLVASNRESIV
Protein: ZFHX2 protein (A2RRC6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATLNSASTTGTTPSPGHNAPSLPSDTFSSSTPSDPVTKDPPAASSTSENMRSSEPGGQLLESGCGLVPPKEIGEPQEGPDCGHFPPNDPGVEKDKEQEEEEEGLPPMDLSNHLFFTAGGEAYLVAKLSLPGGSELLLPKGFPWGEAGIKEEPSLPFLAYPPPSHLTALHIQHGFDPIQGFSSSDQILSHDTSAPSPAACEERHGAFWSYQLAPNPPGDPKDGPMGNSGGNHVAVFWLCLLCRLGFSKPQAFMDHTQSHGVKLTPAQYQGLSGSPAVLQEGDEGCKALISFLEPKLPARPSSDIPLDNSSTVNMEANVAQTEDGPPEAEVQALILLDEEVMALSPPSPPTATWGYTTACCVRGRHPPAWLCCNTCAHLPTAMPRPRGVCSCYRMAQPLRKDSQLFRAS
Protein: Major envelope protein (Protein P9) (P07581)
Organism: Pseudomonas phage phi6 (Bacteriophage phi-6)
Function: Essential for membrane formation.
Subcellular location: Virion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPFPLVKQDPTSKAFTEASERSTGTQILDVVKAPIGLFGDDAKHEFVTRQEQAVSVVSWAVAAGLIGELIGYRGARSGRKAILANIPFLA
Protein: E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (Huntingtin-interacting protein 2-interacting protein 3) (HIP2-interacting protein 3) (Protein DinG) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING finger protein BAP-1) (RING-type E3 ubiquitin transferase RING2) (Q99496)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation (By similarity). Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity (Probable). Association with the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes (By similarity). Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:21282530}. Cytoplasm {ECO:0000250|UniProtKB:Q9CQJ4}. Chromosome {ECO:0000250|UniProtKB:Q9CQJ4}. Note=Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells. Co-localizes with SAMD7 in nuclear polycomb bodies. {ECO:0000250|UniProtKB:Q9CQJ4}.
Interaction partners:
- Polycomb complex protein BMI-1
- E3 SUMO-protein ligase CBX4
- Polyhomeotic-like protein 1
- Polycomb complex protein BMI-1
- YY1-associated factor 2
- Polycomb group RING finger protein 6
- Chromobox protein homolog 7
- Chromobox protein homolog 2
- RING1 and YY1-binding protein
- Lysine-specific demethylase 2B
Sequence:
MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK
Protein: RE10012p (Q8SXL3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDKLKYSRCPLKKRPIMVEESSPEDHLSHDEGPVDLSVASAAVPMEPHWMAKSEPEPQPVPTELRRRFDAAMNQTKEQLARRIWEETREIARAFPDVFTREEIAKSLARLGYGEFELPPEEEVMEPEPEPEQHLPLRYTRDASPTIIKAEPSDEEQFPLRNYNNNLLKSIAEYEDCMKMQNIKEEIPPIPSPQLFYPPPTPLAEPEDLSVTQRRVLSENMNLQNVARALLSMQHMAPQHAPPPIDMEEDQENQDINQLKIKSSNDLYYQCQQCNKCYATYAGLVKHQQTHAYESTEYKIIRSQPGGSGAIVDQTEFCTDQASALIQAANVASAQSMQKPVGVPRYHCQDCGKSYSTYSGLSKHQQFHCPSAEGNQVKKVFSCKNCDKTYVSLGALKMHIRTHTLPCKCPICGKAFSRPWLLQGHIRTHTGEKPFSCQHCNRAFADRSNLRAHMQTHSDVKKYSCPTCTKSFSRMSLLAKHLQSGCQTEQSGGPSGSGGGFDQQQLQQHLQVYEEGHNPHQLYYAGSVGSSNGEEEEGGEYQMQPPAVY
Protein: Rho GTPase-activating protein 44 (Rho-type GTPase-activating protein RICH2) (RhoGAP interacting with CIP4 homologs protein 2) (RICH-2) (Q5SSM3)
Organism: Mus musculus (Mouse)
Function: GTPase-activating protein (GAP) that stimulates the GTPase activity of Rho-type GTPases. Thereby, controls Rho-type GTPases cycling between their active GTP-bound and inactive GDP-bound states. Acts as a GAP at least for CDC42 and RAC1. In neurons, is involved in dendritic spine formation and synaptic plasticity in a specific RAC1-GAP activity. Limits the initiation of exploratory dendritic filopodia. Recruited to actin-patches that seed filopodia, binds specifically to plasma membrane sections that are deformed inward by acto-myosin mediated contractile forces. Acts through GAP activity on RAC1 to reduce actin polymerization necessary for filopodia formation (By similarity). In association with SHANK3, promotes GRIA1 exocytosis from recycling endosomes and spine morphological changes associated to long-term potentiation.
Subcellular location: Cell projection, dendritic spine {ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24352656}. Recycling endosome {ECO:0000269|PubMed:23739967}. Presynapse {ECO:0000269|PubMed:23739967}. Cell projection, dendrite {ECO:0000250|UniProtKB:F1LQX4}. Note=In CA1 hippocampal synapses, detected at both presynaptic and postsynaptic sites (PubMed:23739967). Located in convoluted dendritic plasma membrane sections enriched in polymerized actin and myosin (patches) along dendrites where often emerge filopodia (By similarity). {ECO:0000250|UniProtKB:F1LQX4, ECO:0000269|PubMed:23739967}.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 3
Sequence:
MKKQFNRMRQLANQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLVEGSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAGAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSFGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIKYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQSEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEIEFNLTGSYGSPVHVNHNANYSSMPSPDMDPADRRQPEQARRPLSVATDNMMLEFYKKDGLRKIQSMGVRVMDTSWVARRGSSAGRKASCAPPSMQPPAPPSELAAPLPSPLPEQVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPGSIQGTPCPGTQLGPQPAASPSQLPADQSPHTLRKVSKKVAPIPPKVPFVQPGTVSDQPVGQPSPVSLSPTPPSTPSPYGLSYPPGYSMASGQLSPASAPPLASPSVFTSTLAKSRPTPKPRQRPTLPPPQPPSVSLSASSPQSTEHPMLDGMSPGESMSTDLVHFDVPSIHIELGSTLRLSPLEHARRHSATDKRDSEEESESTAL
Protein: Kinesin-like protein KIN-4A (AtKINESIN-4A) (Protein FRAGILE FIBER 1) (Q8GS71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Kinesin-like motor protein involved in the control of the oriented deposition of cellulose microfibrils. Its motor activity is directed toward the microtubule's plus end. It possesses the potential to drive long-distance transport of cargo along cortical microtubules. Regulates cell wall mechanics during cell elongation, by the regulation of primary and secondary walls deposition. Contributes to cortical microtubule-mediated trafficking of cell wall components.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25646318}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:12468730}. Note=Concentrated around the periphery of the cytoplasm. {ECO:0000269|PubMed:12468730}.
Interaction partners:
- CLIP-associated protein
- Protein CELLULOSE SYNTHASE INTERACTIVE 1
- Probable serine/threonine-protein kinase CST
- Kinesin-like protein KIN-10A
- Katanin p60 ATPase-containing subunit A1
- Kinesin-like protein KIN-5A
- Kinesin-like protein KIN-5C
- Interactor of constitutive active ROPs 5
- Endoglucanase 25
- L-type lectin-domain containing receptor kinase VIII.2
Sequence:
MESTPPPDDCSVKVAVHIRPLIGDERIQGCQDCVTVVTGKPQVQIGSHSFTFDHVYGSSGSPSTEMYEECAAPLVDGLFQGYNATVLAYGQTGSGKTYTMGTGCGDSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLLDPCTVNKSDTNNTGHVGKVAHVPGKPPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEQMRKINTDSPENGAYNGSLKEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRKDGAHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIRNKPVVNRDPVSSEMLKMRQQVEYLQAELSLRTGGSSCAEVQALKERIVWLETANEELCRELHEYRSRCPGVEHSEKDFKDIRADDIVGSVRPDGLKRSLHSIESSNYPMVEATTGDSREIDEEAKEWEHKLLQNSMDKELYELNRRLEEKESEMKLFDGYDPAALKQHFGKKIAEVEDEKRSVQEERNRLLAEIENLASDGQAQKLQDVHAQNLKALEAQILDLKKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKSSPREHSAGTNGFGTNGQTNEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVRAALAEELAVLRQVDEFAVKGLSPPRGKNGFARASSLSPNARMARISSLENMLVISSNSLVAMASQLSEAEERERAFTNRGRWNQLRSMGEAKNLLQYMFNSLAETRCQLWEKDVEIKEMKDQFKEIVGLLRQSELRRKEAEKELKLREQAIATSLGTPPSSVKHVAEDLSTPSPMTVPAQKQLKFTPGIANGKVRGPAAFLDTNKKMVPMGQVSMRKLSAVGKQGGRLWRWKRSHHQWIVQFKWKWQKPWRLSEWIRTSDETLLKSKPRLKALPNKIM
Protein: Regulatory protein E2 (P06790)
Organism: Human papillomavirus type 18
Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001}.
Interaction partners:
Sequence:
MQTPKETLSERLSCVQDKIIDHYENDSKDIDSQIQYWQLIRWENAIFFAAREHGIQTLNHQVVPAYNISKSKAHKAIELQMALQGLAQSAYKTEDWTLQDTCEELWNTEPTHCFKKGGQTVQVYFDGNKDNCMTYVAWDSVYYMTDAGTWDKTATCVSHRGLYYVKEGYNTFYIEFKSECEKYGNTGTWEVHFGNNVIDCNDSMCSTSDDTVSATQLVKQLQHTPSPYSSTVSVGTAKTYGQTSAATRPGHCGLAEKQHCGPVNPLLGAATPTGNNKRRKLCSGNTTPIIHLKGDRNSLKCLRYRLRKHSDHYRDISSTWHWTGAGNEKTGILTVTYHSETQRTKFLNTVAIPDSVQILVGYMTM
Protein: TIMELESS-interacting protein (Q91WA1)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the control of DNA replication and the maintenance of replication fork stability. Important for cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12875843}. Nucleus {ECO:0000269|PubMed:12875843}.
Interaction partners:
- Protein timeless homolog
- WD repeat and HMG-box DNA-binding protein 1
- Claspin
- DNA replication licensing factor MCM7
- DNA replication complex GINS protein SLD5
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM4
- Cell division control protein 45 homolog
- Replication protein A 70 kDa DNA-binding subunit
- DNA replication complex GINS protein PSF1
Sequence:
MLEQEENGLFEIPDYEHVEDETFPPFPPPASPERDPADAEPEEGSGSGVPVPPKRTVKRNLPKLDATRLTSERGLPALRHVFDKTKFKGKGHEAEDLKTLIRHMEHWAHRLFPKLQFEDFIDRVENLGNKKEVQTCLKRIRLDLPIVHEDFVNNNDEVGEANGPDVSATGFDPFLTSSSDSRKFASEPTRSLTEEQQQRIERNKQLALERRQAKLLSNSQSLENDVTVEENSTGEDQEESNGLNIDTADGPHDVPFASTHEEEQCKAEETQLDHTNLD
Protein: Cdi4 (P91654)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
QGSPAVSRNLACGRQLNRIKRDLFGSSKSAEGTANKTPFNSELERHQELATQKWGFDFRAGCPLAEKSPYIWERVSFQESSFAPEMYTLTRAAHVRPSVDASRSDMDILVNERSERENFGSNLVNSSLESNTDNESCYDSQDESLTMRLSSSSTTSTSSIVLRKRQPKITEFMKERKRLAQAPKKLSPAKAMRPVLPVRPPLPAPAPAWIWVGGTLWGDVEAAAPQLMLQIRWPTHRIAICNFIFYKPLRLCSIS
Protein: Nitrogen permease regulator 2 (Q57YB1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- adenylate cyclase
Sequence:
MKFHLQSVLLMALDVVKGPYLSCFAPVNPVEQGGDDQPRDVQGDVNKDSSRNKDMLHLPTNAGRFKAFSDVFVPKSEFCRRVMCLVEAESGILYLFYPEEISGVHYERKTLRYTLCFAFAVDTNLVTATAATVERLLRPYSFVLTRIVEGLREAEQRSGYMSRGLSHRLSTHCPSRGDCQQQQSKNDLIGQPSRSDFHEYGGGVSAEIHSVVGTTSFASPPTGDEALFRYAKGTSRVNVFLTPPQDSSGMQWTSLEALMGELFTFLGTDPKEGETKCPRPWATENTVSLRLCETFFIPVGHRAPPHLPQQHALDEVPVPVAAYEPEVFEHVDLVMHDVFRIVDGRRTIRQIVQVLAAECERYEDSDELLQRQGRIFSPASSQCAIHSVFAHSLHPVNFPGSRSAPEVGGLASSTASTNAHPRDALNTQRATPGLLSPPSAADICLTSPFPNTVCSGTCFSAPTVCTWSRTLQTSRYLPERQNAEEAANNSISDKLSVWCELELLVVEALQHLEVHNYVKIIRPIKMKYTYFATNALYSIMSDRSSPARQLLGKRMLLVEYMFHKEKGQRTSLQGSSGNQKRLQELAPEYRKNLEGLNSATRLTPPLAPLSAHDKGVAVDDEISREQQYHIKRERSSDTALPCSTSLRHSSTECLQDGDSSHDDVDVTPAAETNPDRHEATYTEVLINMAAAAALCALGKFSGSTIFSVQRDMQGHPQWSNAFANWEESCCKSLVEIAIINGWLVAQ
Protein: Tousled-like kinase, isoform I (Tousled-like kinase, isoform M) (Tousled-like kinase, isoform N (EC 2.7.11.1)) (B7Z120)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSPGAHLQMSPQNTSSLSQHHPHQQQQLQPPQQQQQHFPNHHSAQQQSQQQQQQEQQNPQQQAQQQQQILPHQHLQHLHKHPHQLQLHQQQQQQLHQQQQQHFHQQSLQGLHQGSSNPDSNMSTGSSHSEKDVNDMLSGGAATPGAAAAAIQQQHPAFAPTLGMQQPPPPPPQHSNNGGEMGYLSAGTTTTTSVLTVGKPRTPAERKRKRKMPPCATSADEAGSGGGSGGAGATVVNNSSLKGKSLAFRDMPKVNMSLNLGDRLGGSAGSGVGAGGAGSGGGGAGSGSGSGGGKSARLMLPVSDNKKINDYFNKQQTGVGVGVPGGAGGNTAGLRGSHTGGGSKSPSSAQQQQTAAQQQGSGVATGGSAGGSAGNQVQVQTSSAYALYPPASPQTQTSQQQQQQQPGSDFHYVNSSKAQQQQQRQQQQTSNQMVPPHVVVGLGGHPLSLASIQQQTPLSQQQQQQQQQQQQQQLGPPTTSTASVVPTHPHQLGSLGVVGMVGVGVGVGVGVNVGVGPPLPPPPPMAMPAAIITYSKATQTEVSLHELQEREAEHESGKVKLDEMTRLSDEQKSQIVGNQKTIDQHKCHIAKCIDVVKKLLKEKSSIEKKEARQKCMQNRLRLGQFVTQRVGATFQENWTDGYAFQELSRRQEEITAEREEIDRQKKQLMKKRPAESGRKRNNNSNQNNQQQQQQQHQQQQQQQNSNSNDSTQLTSGVVTGPGSDRVSVSVDSGLGGNNAGAIGGGTVGGGVGGGGVGGGGVGGGGGRGLSRSNSTQANQAQLLHNGGGGSGGNVGNSGGVGDRLSDRGGGGGGIGGNDSGSCSDSGTFLKPDPVSGAYTAQEYYEYDEILKLRQNALKKEDADLQLEMEKLERERNLHIRELKRILNEDQSRFNNHPVLNDRYLLLMLLGKGGFSEVHKAFDLKEQRYVACKVHQLNKDWKEDKKANYIKHALREYNIHKALDHPRVVKLYDVFEIDANSFCTVLEYCDGHDLDFYLKQHKTIPEREARSIIMQVVSALKYLNEIKPPVIHYDLKPGNILLTEGNVCGEIKITDFGLSKVMDDENYNPDHGMDLTSQGAGTYWYLPPECFVVGKNPPKISSKVDVWSVGVIFYQCLYGKKPFGHNQSQATILEENTILKATEVQFSNKPTVSNEAKSFIRGCLAYRKEDRMDVFALARHEYIQPPIPKHGRGSLNQQQQAQQQQQQQQQQQQQQSSTSQANSTGQTSFSAHMFGNMNQSSSS
Protein: Translocation protein SEC66 (Protein HSS1) (Sec62/63 complex 31.5 kDa subunit) (P33754)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC66 is required to attach or retain SEC72 in the SEC63 complex. It is essential for growth at elevated temperatures.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8257795}; Single-pass type II membrane protein {ECO:0000269|PubMed:8257795}.
Interaction partners:
- Protein translocation protein SEC63
- Translocation protein SEC62
- Protein transport protein SSS1
- Protein transport protein SEC61
- Translocation protein SEC72
- Protein transport protein SBH1
- Protein transport protein SBH2
- Endoplasmic reticulum chaperone BiP
- Protein RER1
- Mating factor alpha-1
Sequence:
MSEFNETKFSNNGTFFETEEPIVETKSISVYTPLIYVFILVVSLVMFASSYRKKQAKKISEQPSIFDENDAHDLYFQIKEMSENEKIHEKVLKAALLNRGAESVRRSLKLKELAPQINLLYKNGSIGEDYWKRFETEVKLIELEFKDTLQEAERLQPGWVQLFVMVCKEICFNQALSRRYQSILKRKEVCIKEWELKINNDGRLVN
Protein: 4-coumarate--CoA ligase-like 1 (EC 6.2.1.12) (4-coumarate--CoA ligase isoform 10) (At4CL10) (Q9LQ12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:23632852}.
Interaction partners:
- Trans-cinnamate 4-monooxygenase
- Cinnamoyl-CoA reductase 2
- Cinnamoyl-CoA reductase 1
- Cytochrome P450 84A1
- F5F19.5 protein
- Flavone 3'-O-methyltransferase 1
- Phenylalanine ammonia-lyase 3
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 4
- Phenylalanine ammonia-lyase 1
Sequence:
MESQKQEDNEYIFRSLYPSVPIPDKLTLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITLTHGDPEKGQGIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKILSINKK
Protein: 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-hydroxyanthranilate oxygenase) (3-HAO) (h3HAO) (3-hydroxyanthranilic acid dioxygenase) (HAD) (P46952)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:7514594}.
Interaction partners:
- Kynureninase
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
- Kynurenine 3-monooxygenase
- Catalase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Tryptophan 2,3-dioxygenase
- Glutamate decarboxylase 1
- Kynurenine formamidase
- Indoleamine 2,3-dioxygenase 1
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
Sequence:
MERRLGVRAWVKENRGSFQPPVCNKLMHQEQLKVMFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKPIPDQLLKEPPFPLSTRSIMEPMSLDAWLDSHHRELQAGTPLSLFGDTYETQVIAYGQGSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGTSYAWERTQGSVALSVTQDPACKKPLG
Protein: Aminodeoxychorismate synthase component 2 (ADC synthase) (ADCS) (EC 2.6.1.85) (4-amino-4-deoxychorismate synthase component 2) (Aminodeoxychorismate synthase, glutamine amidotransferase component) (P00903)
Organism: Escherichia coli (strain K12)
Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB.
Interaction partners:
- Anthranilate synthase component 1
- Aminodeoxychorismate synthase component 1
- Aminodeoxychorismate lyase
- Tryptophan biosynthesis protein TrpCF
- Bifunctional protein TrpGD
- Chorismate synthase
- Bifunctional chorismate mutase/prephenate dehydratase
- T-protein
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
Sequence:
MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFDVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLHR