wanglab/gogpt-training-data huggingface dataset:
Protein: Homeobox protein Hox-C10 (Homeobox protein Hox-3.6) (P31257)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-C11
- Homeobox protein Hox-C9
Sequence:
MTCPRNVTPNSYAEPLAAPGGGERYNRNAGMYMQSGSDFNCGVMRGCGLAPSLSKRDEGGSPNLALNTYPSYLSQLDSWGDPKAAYRLEQPVGRPLSSCSYPPSVKEENVCCMYSAEKRAKSGPEAALYSHPLPESCLGEHEVPVPSYYRASPSYSALDKTPHCAGANEFEAPFEQRASLNPRTEHLESPQLGGKVSFPETPKSDSQTPSPNEIKTEQSLAGPKASPSESEKERAKTADSSPDTSDNEAKEEIKAENTTGNWLTAKSGRKKRCPYTKHQTLELEKEFLFNMYLTRERRLEISKTINLTDRQVKIWFQNRRMKLKKMNRENRIRELTSNFNFT
Protein: CCR4-NOT transcription complex subunit 8 (EC 3.1.13.4) (CAF1-like protein) (CALIFp) (CAF2) (CCR4-associated factor 8) (Caf1b) (Q9UFF9)
Organism: Homo sapiens (Human)
Function: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT7. Catalytic component of the CCR4-NOT complex which is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12771185}. Nucleus {ECO:0000269|PubMed:12771185}.
Interaction partners:
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 6-like
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 3
- CCR4-NOT transcription complex subunit 6
- CCR4-NOT transcription complex subunit 2
- CCR4-NOT transcription complex subunit 4
- Protein PAT1 homolog 1
- CCR4-NOT transcription complex subunit 10
- CCR4-NOT transcription complex subunit 11
Sequence:
MPAALVENSQVICEVWASNLEEEMRKIREIVLSYSYIAMDTEFPGVVVRPIGEFRSSIDYQYQLLRCNVDLLKIIQLGLTFTNEKGEYPSGINTWQFNFKFNLTEDMYSQDSIDLLANSGLQFQKHEEEGIDTLHFAELLMTSGVVLCDNVKWLSFHSGYDFGYMVKLLTDSRLPEEEHEFFHILNLFFPSIYDVKYLMKSCKNLKGGLQEVADQLDLQRIGRQHQAGSDSLLTGMAFFRMKELFFEDSIDDAKYCGRLYGLGTGVAQKQNEDVDSAQEKMSILAIINNMQQ
Protein: UDP-galactose translocator (Solute carrier family 35 member A2) (UDP-galactose transporter) (UDP-Gal-Tr) (UGT) (mUGT1) (Q9R0M8)
Organism: Mus musculus (Mouse)
Function: Transports uridine diphosphate galactose (UDP-galactose) from the cytosol into the Golgi apparatus. It functions as an antiporter that exchanges UDP-galactose for UMP (By similarity). It is also able to exchange UDP-galactose for AMP and CMP, and to transport UDP-N-acetylgalactosamine (UDP-GalNAc) and other nucleotide sugars (By similarity). As a provider of UDP-galactose to galactosyltransferases present in the Golgi apparatus, it is necessary for globotriaosylceramide/globoside (Gb3Cer) synthesis from lactosylceramide (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:P78381}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
- UDP-glucuronosyltransferase 1A1
Sequence:
MAAVGVGGSTAAAGAGAVSSGALEPGSTTAAHRRLKYISLAVLVVQNASLILSIRYARTLPGDRFFATTAVVMAEVLKGLTCLLLLFAQKRGNVKHLVLFLHEAVLVQYVDTLKLAVPSLIYTLQNNLQYVAISNLPAATFQVTYQLKILTTALFSVLMLNRSLSRLQWASLLLLFTGVAIVQAQQAGGSGPRPLDQNPGAGLAAVVASCLSSGFAGVYFEKILKGSSGSVWLRNLQLGLFGTALGLVGLWWAEGTAVASQGFFFGYTPAVWGVVLNQAFGGLLVAVVVKYADNILKGFATSLSIVLSTVASIRLFGFHLDPLFALGAGLVIGAVYLYSLPRGAVKAIASASASGPCIHQQPPGQPPPPQLSSRGDLTTEPFLPKSVLVK
Protein: Dual specificity protein phosphatase CDC14B (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog B) (O60729)
Organism: Homo sapiens (Human)
Function: Dual-specificity phosphatase involved in DNA damage response. Essential regulator of the G2 DNA damage checkpoint: following DNA damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a key activator of the anaphase promoting complex/cyclosome (APC/C). Dephosphorylates SIRT2 around early anaphase. Dephosphorylation of FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1, preventing entry into mitosis. Preferentially dephosphorylates proteins modified by proline-directed kinases.
Subcellular location: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Following DNA damage, translocates from the nucleolus to the nucleoplasm and interacts with FZR1/CDH1.
Interaction partners:
- Dual specificity protein phosphatase CDC14A
- Fizzy-related protein homolog
- Mitogen-activated protein kinase 6
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 1
- Cell division cycle protein 16 homolog
- Cell division cycle protein 23 homolog
Sequence:
MKRKSERRSSWAAAPPCSRRCSSTSPGVKKIRSSTQQDPRRRDPQDDVYLDITDRLCFAILYSRPKSASNVHYFSIDNELEYENFYADFGPLNLAMVYRYCCKINKKLKSITMLRKKIVHFTGSDQRKQANAAFLVGCYMVIYLGRTPEEAYRILIFGETSYIPFRDAAYGSCNFYITLLDCFHAVKKAMQYGFLNFNSFNLDEYEHYEKAENGDLNWIIPDRFIAFCGPHSRARLESGYHQHSPETYIQYFKNHNVTTIIRLNKRMYDAKRFTDAGFDHHDLFFADGSTPTDAIVKEFLDICENAEGAIAVHCKAGLGRTGTLIACYIMKHYRMTAAETIAWVRICRPGSVIGPQQQFLVMKQTNLWLEGDYFRQKLKGQENGQHRAAFSKLLSGVDDISINGVENQDQQEPEPYSDDDEINGVTQGDRLRALKSRRQSKTNAIPLTVILQSSVQSCKTSEPNISGSAGITKRTTRSASRKSSVKSLSISRTKTVLR
Protein: Mediator of RNA polymerase II transcription subunit 16 (Protein SENSITIVE TO FREEZING 6) (F4JGZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Involved in the regulation of the circadian clock, in the control of flowering time, in freezing- and osmotic-stress tolerance and in both salicylic acid- and jasmonate-mediated defense gene expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:19067974}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 25
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 32
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 19a
- Mediator of RNA polymerase II transcription subunit 15a
- Mediator of RNA polymerase II transcription subunit 33A
Sequence:
MNQQNPEEEVSLVNNSGGGGIIEAPAIVEEKEEEGLQQKQEETIESTDPILVVVEEKLLEKSVDGEKEDDNSSSSNMEIDPVSPATVFCVKLKQPNSNLLHKMSVPELCRNFSAVAWCGKLNAIACASETCARIPSSKANTPFWIPIHILIPERPTECAVFNVVADSPRDSVQFIEWSPTSCPRALLIANFHGRITIWTQPTQGSANLVHDATSWQCEHEWRQDIAVVTKWLTGASPYRWLSSKPSSGTNAKSTFEEKFLSQSSESSARWPNFLCVCSVFSSGSVQIHWSQWPSNQGSTAPKWFSTKKGLLGAGPSGIMAADAIITDSGAMHVAGVPIVNPSTIVVWEVTPGPGNGLQATPKISTGSRVPPSLSSSSWTGFAPLAAYLFSWQEYLISEIKQGKKPSDQDSSDAISLSCSPVSNFSAYVSPEAAAQSAATTTWGSGVTAVAFDPTRGGSVIAVVIVEGQYMSPYDPDEGPSITGWRVQRWESSVQPVVLHQIFGNPTSNFGGQVPTQTVWVSRVDMSIPPTKDFKNHQVAAAGPSVDAPKEPDSGDEKANKVVFDPFDLPSDIRTLARIVYSAHGGEIAIAFLRGGVHIFSGPTFSPVENYQINVGSAIAAPAFSPTSCCSASVWHDAAKDCAMLKIIRVLPPALPRNQSKVDQSTWERAIAERFWWSLLVGVDWWDAVGCTQSAAEDGIVSLNSVIAVMDADFHSLPSTQHRQQYGPNLDRIKCRLLEGTNAQEVRAMVLDMQARLLLDMLGKGIESALVNPSALVFEPWRVDGETITGINPEAMAVDPALVSSIQAYVDAVLDLASHFITRLRRYASFCRTLASHAASAGTGSNRNNVTSPTQNASSPATPQVFPDKSLYLAVGQPTTTTTTTATTNSSGSSHVQAWMQGAIAKISSSNDGSNSTASPISGSPTFMPISINTGTFPGTPAVRLIGDCHFLHRLCQLLLFCFLQRSSRFPQRNADVSSQKLQTGATSKLEEVNSAKPTPALNRIEDAQGFRGAQLGTGVKGIDENSARTTKMGSGNAGQGYTYEEVRVLFHILMDLCKRTSGLAHPLPGSQVGSGNIQVRLHYIDGNYTVLPEVVEAALGPHMQNMPRPRGADAAGLLLRELELHPPSEEWHRRNLFGGPGSEPEDMILTDDVSKLSNSLDLPDTNFSGICDGYNRVHSLWPRKRRMSERDAAFGSNTSVGLGAYLGIMGSRRDVVTATWKTGLEGVWYKCIRCLRQTSAFASPGATKQPNPNERETWWTSRWVYCCPMCGGTWVRVV
Protein: Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 (Glucosaminyl N-deacetylase/N-sulfotransferase 3) (NDST-3) (hNDST-3) (N-heparan sulfate sulfotransferase 3) (N-HSST 3) [Includes: Heparan sulfate N-deacetylase NDST3 (EC 3.-.-.-); [heparan sulfate]-glucosamine N-sulfotransferase NDST3 (EC 2.8.2.8)] (O95803)
Organism: Homo sapiens (Human)
Function: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Sulfotransferase 1C3
- Sulfotransferase 1C4
- Heparan sulfate 2-O-sulfotransferase 1
- Sulfotransferase 1B1
Sequence:
MSFIMKLHRHFQRTVILLATFCMVSIIISAYYLYSGYKQENELSETASEVDCGDLQHLPYQLMEVKAMKLFDASRTDPTVLVFVESQYSSLGQDIIMILESSRFQYHIEIAPGKGDLPVLIDKMKGKYILIIYENILKYINMDSWNRSLLDKYCVEYGVGVIGFHKTSEKSVQSFQLKGFPFSIYGNLAVKDCCINPHSPLIRVTKSSKLEKGSLPGTDWTVFQINHSAYQPVIFAKVKTPENLSPSISKGAFYATIIHDLGLHDGIQRVLFGNNLNFWLHKLIFIDAISFLSGKRLTLSLDRYILVDIDDIFVGKEGTRMNTNDVKALLDTQNLLRAQITNFTFNLGFSGKFYHTGTEEEDEGDDCLLGSVDEFWWFPHMWSHMQPHLFHNESSLVEQMILNKKFALEHGIPTDMGYAVAPHHSGVYPVHVQLYEAWKKVWNIKITSTEEYPHLKPARYRRGFIHKNIMVLPRQTCGLFTHTIFYKEYPGGPKELDKSIQGGELFFTVVLNPISIFMTHLSNYGNDRLGLYTFVNLANFVKSWTNLRLQTLPPVQLAHKYFELFPDQKDPLWQNPCDDKRHRDIWSKEKTCDRLPKFLVIGPQKTGTTALYLFLVMHPSILSNSPSPKTFEEVQFFNRNNYHRGIDWYMDFFPVPSNVTTDFLFEKSANYFHSEEAPKRAASLVPKAKIITILIDPSDRAYSWYQHQRSHEDPAALKFSFYEVISAGPRAPSELRALQKRCLVPGWYASHIERWLVYFPPFQLLIIDGQQLRTDPATVMDEVQKFLGVLPHYNYSEALTFDSHKGFWCQLLEEGKTKCLGKSKGRKYPPMDSDSRTFLSSYYRDHNVELSKLLHKLGQPLPSWLRQELQKVR
Protein: Ubiquitin-related modifier 1 homolog (Q7KU86)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln) (By similarity). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3 (By similarity). The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U (By similarity). Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as Jafrac1, Ciao1, Eip71CD and GILT1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates (By similarity). Plays a role in the regulation of JNK signaling in response to oxidative stress.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03048, ECO:0000269|PubMed:26715182}.
Interaction partners:
- Adenylyltransferase and sulfurtransferase MOCS3
- Peripheral plasma membrane protein CASK
- Peroxiredoxin-5
- Cytoplasmic tRNA 2-thiolation protein 2
- Calcium/calmodulin-dependent protein kinase type II alpha chain
- E1 ubiquitin-activating enzyme
- Cytoplasmic tRNA 2-thiolation protein 1
Sequence:
MGTPELKIILEFSAGAELLFGNIKRRELNLDGKQKWTIANLLKWMHANILTERPELFLQGDTVRPGILVLINDTDWELLGELDYELQPNDNVLFISTLHGG
Protein: Cytochrome b (Q2F965)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MTIRNQRFSLLKQPIYSTLNQHLIDYPTPSNLSYWWGFGSLAGICLVIQIVTGVFLAMHHTPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFLIVVHLHIFRGLYHASYSSPREFVWCLGVVIFLLMIVTAFIGYVPPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNATLNRFFSLHHLLPLILVGASLLHLAALHQYGSNNPLGVHSEMDKIASYPYFYVKDLVGRVASAIFFSIWIFFAPNVLGHPDNYIPANPMPTPPHIVPEWYFLPIHAILRSIPDKAGGVAAIAPVFISLLALPFFKEMYVRSSSFRPIHQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQIPSFFFFLFFAITPIPGRVGRGIPKYYTDETHRTGSVS
Protein: A-kinase anchor protein 8-like (AKAP8-like protein) (Neighbor of A-kinase-anchoring protein 95) (Neighbor of AKAP95) (Q9R0L7)
Organism: Mus musculus (Mouse)
Function: Could play a role in constitutive transport element (CTE)-mediated gene expression by association with DHX9. Increases CTE-dependent nuclear unspliced mRNA export. Proposed to target PRKACA to the nucleus but does not seem to be implicated in the binding of regulatory subunit II of PKA. May be involved in nuclear envelope breakdown and chromatin condensation. May be involved in anchoring nuclear membranes to chromatin in interphase and in releasing membranes from chromating at mitosis. May regulate the initiation phase of DNA replication when associated with TMPO isoform Beta. Required for cell cycle G2/M transition and histone deacetylation during mitosis. In mitotic cells recruits HDAC3 to the vicinity of chromatin leading to deacetylation and subsequent phosphorylation at 'Ser-10' of histone H3; in this function seems to act redundantly with AKAP8. May be involved in regulation of pre-mRNA splicing (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus matrix {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus speckle {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9ULX6}. Cytoplasm {ECO:0000250|UniProtKB:Q9ULX6}. Note=Colocalizes with PRPF40A in the nuclear matrix. Nuclear at steady state but shuttles between the nucleus and cytoplasm. The shuttling property has been questioned. Colocalizes with EBNA-LP in PML bodies. {ECO:0000250|UniProtKB:Q9ULX6}.
Interaction partners:
- ATP-dependent RNA helicase A
Sequence:
MSYTGFVQGSETTLQSTYCDTSAQPTCDYGYGTWNSGTNRGYENYGYGYGYGQDNTTNYGYGMATSHSWEMASSDTNANPSASGSASADSVLSRINQRLDMMPHLETDMIQGGVYGSGGGERYDSYEACDSRAILSERDLYRSSYDYGELDPEMEMAYEGQYDAYRDQFRMRGGDTFGPRAQGWARDARSGRPMASGYGRMWEDPMGARGQCMPGASRLPSLFSQNIIPEYGMFQGMRGGGAFSGGSRFGFGFGNGMKQMRRTWKTWTTADFRTKKKKRKQGGSPDEPDSKATRTDCSDNSDSDNDEGTEGEAAEGTESAEAMEKGSRVDGEDEEGKEDGREEGKEDPEKGALTAQDESSQAKRKLQASKKSQDKQKKRQRDRMVERIQFVCSLCKYRTFYEDEMGSHLDSKFHKEHFKYVGTKLPKQTADFLQEYVTNKTKKTEELRKTVEDLDGLIQQIYRDQDLTQEIAMEHFVKKVEAAHCAACDLFIPMQFGIIQKHLKTMDHNRNRRLMMEQSKKSSLMVARSILNNKLISKKLERYLKGENPFTDNPEEEKEQDEVEAGALDEGAPSEATELTEGVPAQPPVPLEPAPGTTTPPPPPPPEEEESPVPLLGGALQCQIRGIPGLDMEDDEEGGGGP
Protein: Na(+)-translocating NADH-quinone reductase subunit D (Na(+)-NQR subunit D) (Na(+)-translocating NQR subunit D) (EC 7.2.1.1) (NQR complex subunit D) (NQR-1 subunit D) (Q57095)
Organism: Vibrio alginolyticus
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00428, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00428}.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- NADH:ubiquinone reductase
- FAD:protein FMN transferase
- Electron transport complex subunit RsxD
- Electron transport complex subunit RsxG
Sequence:
MSSAQNVKKSILAPVLDNNPIALQVLGVCSALAVTTKLETAFVMTLAVTFVTALSNFSVSLIRNHIPNSVRIIVQMAIIASLVIVVDQVLKAYLYDISKQLSVFVGLIITNCIVMGRAEAFAMKSAPVPSLIDGIGNGLGYGFVLITVGFFRELFGSGKLFGLEVLPLVSNGGWYQPNGLMLLAPSAFFLIGFLIWVIRILKPEQVEAKE
Protein: Small ribosomal subunit protein eS8B (40S ribosomal protein S8-B) (Q9P7B2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein eS21
- Elongation factor 3
- mRNA export factor elf1
Sequence:
MGITRDSRHKRSATGAKRAQYRKKRKFELGRQPSNTRIGPKRIHEVRVRGGNKKFRALRLDSGNFSWGSEGVSKKTRIIQVAYHPSNNELVRTNTLTKSAIVQIDAAPFRVWYETHYGILMGSKGKKATATPTPKSKHVQRKHSARLGDSKVDSALETQFAAGRLYAVVSSRPGQSGRCDGYILEGEELHFYLRRMAPKK
Protein: Glutathione synthetase (GSH synthetase) (GSH-S) (EC 6.3.2.3) (Glutathione synthase) (P48637)
Organism: Homo sapiens (Human)
Function: Catalyzes the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner. Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells and is required for numerous processes including the protection of cells against oxidative damage, amino acid transport, the detoxification of foreign compounds, the maintenance of protein sulfhydryl groups in a reduced state and acts as a cofactor for a number of enzymes. Participates in ophthalmate biosynthesis in hepatocytes (By similarity).
Interaction partners:
- Glutamate--cysteine ligase catalytic subunit
- Glutamate--cysteine ligase regulatory subunit
- Glutathione hydrolase 6
- Glutathione reductase, mitochondrial
- Glutathione hydrolase 1 proenzyme
- Glutathione hydrolase 7
- Glutathione hydrolase 5 proenzyme
- Hematopoietic prostaglandin D synthase
- Glutathione S-transferase omega-1
- Glutathione peroxidase 3
Sequence:
MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSALLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVFLGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKILSNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFEDISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQLAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSRFVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVVQCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV
Protein: Histone H3-like 3 (Q9LR02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- Protein TONSOKU
- Histone H2B.6
- Chromo domain-containing protein LHP1
- Lysine-specific demethylase ELF6
- DNA
- Histone acetyltransferase GCN5
- Histone-lysine N-methyltransferase CLF
- Histone-lysine N-methyltransferase ASHH2
- Chromatin structure-remodeling complex protein SYD
Sequence:
MARTKQTARKSHGGKAPRTLLATKAARKSAPTTGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDYKTDLRFQSHAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDVQLARRIRGERA
Protein: DNA-binding protein RFX2 (Regulatory factor X 2) (Q32NR3)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that acts as a key regulator of ciliogenesis. Specifically regulates expression of genes required for cilium assembly and function. Recognizes and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on promoters. Required for neural tube closure and neural ciliogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:B2GV50, ECO:0000255|PROSITE-ProRule:PRU00858}. Cytoplasm {ECO:0000250|UniProtKB:B2GV50}. Note=Mainly expressed in the nucleus and at lower level in cytoplasm. {ECO:0000250|UniProtKB:B2GV50}.
Interaction partners:
Sequence:
MQNSDSGSDSATSVALRTSTSAQAPVVQPVPASQQVQTVQHVYPAQVQYVEGDTVYTNGAIRTAYSYNAETQIYAPSSGSSYFDSQGGGAQVTTVVSSPTAIPSHSMVGITMDVSGSQIISSSGAYLIHGGLENSRHTPSHTSRTFPATLEMAIENLQKNEGITSHKSSLLNSHLQWLLDNYETAEGVSLPRSSLYNHYLRHCQDHKLDPVNAASFGKLIRSVFMGLRTRRLGTRGNSKYHYYGIRLKPDSPLNRIQEDAQYMAIRQQPIHQKQRYRPAQKIDGMGENPANSSQHASPEQSVAAQSQHHQQFIDTSHVFPDFPAPDLGSLLLPEGITMTDIKNLQLMYRRHCEATIDVVMNLQFQYIEKLWQAFWNSKPSSPDGSNPMSSEDEQEPIIPNEKLMVLCKYEPIMRWMRNCDHILYQALVEILIPDVLRPVPSTLTQAIRNFAKSLEGWLTNAMCDFPQQIVHAKVGVVSAFAQTLRRYTSLNHLAQAARAVLQNTSQINQMLSDLNRVDFANVQEQASWVCQCDEGMVQKLEQDFKLTLQQQSSLDQWANWLDNVVTQVLKPHEGSTSFPKAARQFLLKWSFYSSMVIRDLTLRSAASFGSFHLIRLLYDEYMFYLVEHRVAQATGETPIAVMGEFSDFASMSPVQMDKDDVSELGSDTEGDPHISGQPPVKRERVELNHSMQEM
Protein: Threonine--tRNA ligase, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (P52709)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Histidine--tRNA ligase
- Leucine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Obg-like ATPase 1
- Asparagine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
Sequence:
MRLNCFRIFVHIQKPTQIFKPFYRSLSSEASDKYHFVNGHKMSKAPTDMAPWPAFIEERIKLWDKLKAEYDAEIAAKESEPIQITLPDGKIHEGKTWRTTPFEIAERISKGLAEAAVIAKVNGAVWDLDRPFEGNAKLELLKFDDDEAKQVFWHSSAHVLGEAMERYCGGHLCYGPPIQEGFYYDMWHENRTICPDDFPKIDQIVKAAVKDKQKFERLEMTKEDLLEMFKYNEFKVRIITEKIHTPKTTVYRCGPLIDLCRGPHVRHTGKVKAMAITKNSSSYWEGKADAESLQRLYGISFPDSKQLKEWQKLQEEAAKRDHRKLGKEHDLFFFHQLSPGSAFWYPKGAHIYNKLVDFIRKQYRRRGFTEVITPNMYNKKLWETSGHWQHYSEDMFKIEVEKEEFGLKPMNCPGHCLMFGHMPHTYNELPFRFADFGVLHRNEMSGALTGLTRVRRFQQDDAHIFCRQDQISEEIKQCLDFLEYAYEKVFGFTFKLNLSTRPEGFLGNIETWDKAEADLTNALNASGRKWVLNPGDGAFYGPKIDITIQDALKRNFQCATIQLDFQLPNQFDLSYFDEKGEKQRPVMIHRAVLGSVERMTAILTESYGGKWPFWLSPRQCKIITVHESVRDYANDVKKQIFEAGFEIEYEENCGDTMNKQVRKAQLAQFNFILVIGAKEKENGTVNVRTRDNAVRGEVALDKLISKFRRFADEYVADTEKSEEWA
Protein: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (NMN/NaMN adenylyltransferase 3) (Nicotinamide-nucleotide adenylyltransferase 3) (NMN adenylyltransferase 3) (Nicotinate-nucleotide adenylyltransferase 3) (NaMN adenylyltransferase 3) (EC 2.7.7.18) (Pyridine nucleotide adenylyltransferase 3) (PNAT-3) (EC 2.7.7.1) (Q96T66)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects against axonal degeneration following injury.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12574164, ECO:0000269|PubMed:16118205}.
Interaction partners:
Sequence:
MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWKGKSTQSTEGKTS