wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase RNF130 (EC 2.3.2.27) (G1-related zinc finger protein) (Goliath homolog) (RING finger protein 130) (RING-type E3 ubiquitin transferase RNF130) (Q8VEM1)
Organism: Mus musculus (Mouse)
Function: Acts as an E3 ubiquitin-protein ligase (By similarity). May have a role during the programmed cell death of hematopoietic cells.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q86XS8}.
Interaction partners:
- Protein FAM131B
Sequence:
MSGAARAGPARLAALALLTCSLWPTRADNASQEYYTALINVTVQEPGRGTPLTFRIDRGRYGLDSPKAEVRGQVLAPLPIHGVADHLGCDPQTRFFVPPNIKQWIALLQRGNCTFKEKISRAAFHNAVAVVIYNNKSKEEPVTMTHPGTGDIIAVMITELRGKDILSYLEKNISVQMTIAVGTRMPPKNFSRGSLVFVSISFIVLMIISSAWLIFYFIQKIRYTNARDRNQRRLGDAAKKAISKLTTRTVKKGDKETDPDFDHCAVCIESYKQNDVVRVLPCKHVFHKSCVDPWLSEHCTCPMCKLNILKALGIVPNLPCTDNVAFDMERLTRTQAVNRRAALGDLAGDSSLGLEPLRTSGISPLPQDGELTPRTGEINIAVTKEWFIIASFGLLSALTLCYMIIRATASLNANEVEWF
Protein: Putative synaptotagmin-14-like protein (Synaptotagmin XIV protein pseudogene 1) (Synaptotagmin XIV-derived protein) (Synaptotagmin XIV-like protein) (Q58G82)
Organism: Homo sapiens (Human)
Function: Plays a role in melanocyte differentiation; enhances dendrite outgrowth, melanin content and tyrosinase activity through the modulation of ERK and/or CREB pathways.
Interaction partners:
Sequence:
MLEGFQILVQNTVQGTIHKIKCVCDSQMSVSEMSCSESTSACQSLEDGSVPEILISLLYNATNGRLSAEVIKGSHLKNWAANRPPNTYVKLTLRKSTDQEMSKCKISIRRGRPNPVYKETFVFKVTLFQLSHVTLMLSVYNKSSMRRKMIGWIYLGLNSSGEELNHWTEMKESKGRQVRRWQALLESR
Protein: Small ribosomal subunit protein eS12 (40S ribosomal protein S12) (P48589)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein uL11A
- Small ribosomal subunit protein eS17B
- Small ribosomal subunit protein eS28B
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein eS1B
- Small ribosomal subunit protein eS25A
- Essential nuclear protein 1
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL27A
- Small ribosomal subunit protein eS8A
Sequence:
MSDVEEVVEVQEETVVEQTAEVTIEDALKVVLRTALVHDGLARGLRESTKALTRGEALLVVLVSSVTEANIIKLVEGLANDPENKVPLIKVADAKQLGEWAGLGKIDREGNARKVVGASVVVVKNWGAETDELSMIMEHFSQQ
Protein: Lymphocyte activation gene 3 protein (LAG-3) (CD antigen CD223) [Cleaved into: Secreted lymphocyte activation gene 3 protein (sLAG-3)] (P18627)
Organism: Homo sapiens (Human)
Function: Lymphocyte activation gene 3 protein: Inhibitory receptor on antigen activated T-cells. Delivers inhibitory signals upon binding to ligands, such as FGL1 (By similarity). FGL1 constitutes a major ligand of LAG3 and is responsible for LAG3 T-cell inhibitory function (By similarity). Following TCR engagement, LAG3 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation (By similarity). May inhibit antigen-specific T-cell activation in synergy with PDCD1/PD-1, possibly by acting as a coreceptor for PDCD1/PD-1 (By similarity). Negatively regulates the proliferation, activation, effector function and homeostasis of both CD8(+) and CD4(+) T-cells. Also mediates immune tolerance: constitutively expressed on a subset of regulatory T-cells (Tregs) and contributes to their suppressive function (By similarity). Also acts as a negative regulator of plasmacytoid dendritic cell (pDCs) activation (By similarity). Binds MHC class II (MHC-II); the precise role of MHC-II-binding is however unclear.
Subcellular location: [Lymphocyte activation gene 3 protein]: Cell membrane {ECO:0000269|PubMed:1380059, ECO:0000269|PubMed:1692078, ECO:0000269|PubMed:9634475}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secreted lymphocyte activation gene 3 protein]: Secreted {ECO:0000250|UniProtKB:Q61790}. Note=Produced following cleavage of the main chain. {ECO:0000250|UniProtKB:Q61790}.
Interaction partners:
- Galectin-9
- C-type lectin domain family 4 member G
- Galectin-9C
- Fibrinogen-like protein 1
- Galectin-9B
- T-lymphocyte activation antigen CD80
- Galectin-3
- T-lymphocyte activation antigen CD86
- Programmed cell death 1 ligand 1
- Cytotoxic T-lymphocyte protein 4
Sequence:
MWEAQFLGLLFLQPLWVAPVKPLQPGAEVPVVWAQEGAPAQLPCSPTIPLQDLSLLRRAGVTWQHQPDSGPPAAAPGHPLAPGPHPAAPSSWGPRPRRYTVLSVGPGGLRSGRLPLQPRVQLDERGRQRGDFSLWLRPARRADAGEYRAAVHLRDRALSCRLRLRLGQASMTASPPGSLRASDWVILNCSFSRPDRPASVHWFRNRGQGRVPVRESPHHHLAESFLFLPQVSPMDSGPWGCILTYRDGFNVSIMYNLTVLGLEPPTPLTVYAGAGSRVGLPCRLPAGVGTRSFLTAKWTPPGGGPDLLVTGDNGDFTLRLEDVSQAQAGTYTCHIHLQEQQLNATVTLAIITVTPKSFGSPGSLGKLLCEVTPVSGQERFVWSSLDTPSQRSFSGPWLEAQEAQLLSQPWQCQLYQGERLLGAAVYFTELSSPGAQRSGRAPGALPAGHLLLFLILGVLSLLLLVTGAFGFHLWRRQWRPRRFSALEQGIHPPQAQSKIEELEQEPEPEPEPEPEPEPEPEPEQL
Protein: CTD nuclear envelope phosphatase 1 (EC 3.1.3.16) (Serine/threonine-protein phosphatase dullard) (Q3TP92)
Organism: Mus musculus (Mouse)
Function: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Nuclear envelope phosphatase-regulatory subunit 1
- Phosphatidate phosphatase LPIN2
- Phosphatidate phosphatase LPIN1
- Phosphatidate phosphatase LPIN3
Sequence:
MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPLSRNRLAQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQHCTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW
Protein: Chromatin target of PRMT1 protein (Friend of PRMT1 protein) (Small arginine- and glycine-rich protein) (SRAG) (Q9CY57)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the ligand-dependent activation of estrogen receptor target genes (By similarity). May play a role in the silencing of fetal globin genes. Recruits the 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. Required for the tumorigenicity of glioblastoma cells. Binds to 5-hydroxymethylcytosine (5hmC) and associates with the methylosome complex containing PRMT1, PRMT5, MEP50 and ERH. The CHTOP-methylosome complex associated with 5hmC methylates H4R3 and transactivates genes involved in glioblastomagenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:19254951}. Nucleus, nucleolus {ECO:0000269|PubMed:19254951}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}. Nucleus speckle {ECO:0000269|PubMed:19858291}. Note=Mostly associated with facultative heterochromatin. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur (By similarity). {ECO:0000250|UniProtKB:Q9Y3Y2, ECO:0000269|PubMed:19858291}.
Interaction partners:
- Spliceosome RNA helicase Ddx39b
- SAP domain-containing ribonucleoprotein
- THO complex subunit 4
- Aly/REF export factor 2
- THO complex subunit 5 homolog
- Polymerase delta-interacting protein 3
- THO complex subunit 1
- UAP56-interacting factor
- THO complex subunit 7 homolog
- ATP-dependent RNA helicase DDX39A
Sequence:
MAAQSAPKVVLKSTTKMSLNERFTNMLKNKQPMPVNIRASMQQQQQLASARNRRLAQQMENRPSVQAALKLKQKSLKQRLGKSNIQARLGRPIGALARGAIGGRGLPIIQRGLPRGGLRGGRATRTLLRGGMSLRGQNLLRGGRAVAPRMGLRRGGVRGRGGPGRGGLGRGAMGRGGIGGRGRGMIGRGRGGFGGRGRGRGRGRGALTRPVLTKEQLDNQLDAYMSKTKGHLDAELDAYMAQTDPETND
Protein: Microtubule-associated protein RP/EB family member 3 (EB1 protein family member 3) (EBF3) (End-binding protein 3) (EB3) (RP3) (Q6PER3)
Organism: Mus musculus (Mouse)
Function: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24706950}. Note=Associated with the microtubule network. Detected at the plus end of microtubules. {ECO:0000269|PubMed:24706950}.
Interaction partners:
- Drebrin
- Dynactin subunit 1
- Microtubule-associated protein RP/EB family member 1
- CAP-Gly domain-containing linker protein 1
- Ankyrin-3
- SRC kinase signaling inhibitor 1
- CAP-Gly domain-containing linker protein 2
- Cytoskeleton-associated protein 5
- Src substrate cortactin
- Hematopoietic lineage cell-specific protein
Sequence:
MAVNVYSTSVTSENLSRHDMLAWVNDSLHLNYTKIEQLCSGAAYCQFMDMLFPGCVHLRKVKFQAKLEHEYIHNFKVLQAAFKKMGVDKIIPVEKLVKGKFQDNFEFIQWFKKFFDANYDGKDYNPLLARQGQDVAPPPNPGDQIFNKSKKLIGTAVPQRTSPTGPKNMQTSGRLSNVAPPCILRKNPPSARNGGHEADAQILELNQQLLDLKLTVDGLEKERDFYFSKLRDIELICQEHESENSPVISGIIGILYATEEGFAPPEDDEIEEHQQEDQDEY
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9VV48)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}.
Interaction partners:
- Not1, isoform H
- E3 ubiquitin-protein ligase listerin
- LD08718p
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 3
- Protein associated with topo II related - 1, isoform A
Sequence:
MPIQAPSWTDFLNCPICCNEFAASQRCPVSLGCGHTICKLCLTTLYNRQCPFDQTVIVSDIDNLPINHALLQLVKDSELLELAPPPPSVQKLEPEHLKCYQLGQRCIEELALHLKSFLNLNGNGNLLTRPMLRKLVTLVNCQLMEEEGRVRALRAARSLGERTVTELILQHQNPQQLSSNLWAAVRTRGCQFLGPAMQEEVLKLVLLALEEGSALSRKVLVMFVVQRLEPKFPQASKTSIGHVVQLLYRASCFKVSKREADSSLMQLKEEFRTYDALRREHDAQIVQIATEAGLRIAPEQWSSLLYGDVMHKSHMQSIIDKLQTPSSFAQSVQELVIALQRTSDPAKLSSLHHHLKYLANIDPCAEVAPWSVLAEALDAVRHSVVGLVNFLQHHGVRKAQDGISGGGSGGTTNSNPKYKISLCRDLNVRRVCPRGSSCTFAHSQEEVERYRARNRGKHMKTPLALQGPPAVGVGAIKKPLGEQEGPPLGNMPPMLPMSPMHYMGSPRGYLDPSLGLSPGGGLPPSHHSPITRLIVPSRYDSRFSGFGGGTPRIPSPREYQANPVAPTQRNANPPNFSVNSNLHKGYMLPASGGDVFHLANPWEQAYLAQQQHPPQHPQQQQPPSSKPNPSRPLSILPATADTSFFEKKPPNSVSIDLDRVPEVNVDAVPLFRRSNNNHNNNNSNSHNNNNNNHGSSLLFWNNTGKDSANFVRSDSILDDDASTFDVPTGSSMLSIYGPICPKSSTTGNWNNFDLGYGGFKSDRNDSFNANKQQQPMWGRKPQLMSEDSFEGGIDSGMMLQLEKNLVDIVDPDDSGIKVD
Protein: Homeobox protein prospero (P29617)
Organism: Drosophila melanogaster (Fruit fly)
Function: Homeodomain protein that controls neuronal identity. As a transcriptional factor, regulates the expression of ftz, eve and en in a subset of neuroblast progeny and modulates the transcriptional activity of other homeodomain proteins such as Dfd. Required for proper neuronal differentiation, axonal outgrowth and pathfinding of most or all neurons and their precursors in central and peripheral nervous systems. Regulates asymmetric stem cell self-renewal together with brat.
Subcellular location: Nucleus {ECO:0000269|PubMed:1540176, ECO:0000269|PubMed:1720353, ECO:0000269|PubMed:18342578, ECO:0000269|PubMed:1842358, ECO:0000269|PubMed:20152183, ECO:0000269|PubMed:23056424}. Cytoplasm, cell cortex {ECO:0000269|PubMed:16564014, ECO:0000269|PubMed:23056424}. Cytoplasm {ECO:0000269|PubMed:18342578}. Note=Dispersed in the cytoplasm of mitotic ganglion mother cells (GMCs) and neuroblast-like cell type. {ECO:0000269|PubMed:18342578}.
Interaction partners:
- Miranda, isoform A
Sequence:
MMSSEEYEADCFGLYSDENNVLLKANEPETTAATKQQHQPQFQQQQQQQQQQQQHHHQHQQPPPSSNGHTSPIPSQVNGDGSAANCGESGKTNTNTGSHSHSNSGNTNTDADKEQEREKAKEKANEEESEDSDDDVVVVLEGCEGNASSSSSSSNSNSNASSNNHKAAATTTTTATTANHCNRSGGSSRSHRSARSSRQISQSTAVGKTTTCAAKKPTAAQATTTTAKNSNSNSNVNVNVNVNSNGSGNGNANSKVNRRSRQRSLSKDINNQPASSNSNSNSSNNSSNSNGGATATAAGFMSSAAAAAAGAAGGGALFQPQSVSTANSSSSNNNNSSTPAALATHSPTSNSPVSGASSASSLLTAAFGNLFGGSSAKMLNELFGRQMKQAQDATSGLPQSLDNAMLAAAMETATSAELLIGSLNSTSKLLQQQHNNNSIAPANSTPMSNGTNASISPGSAHSSSHSHQGVSPKGSRRVSACSDRSLEAAAADVAGGSPPRAASVSSLNGGASSGEQHQSQLQHDLVAHHMLRNILQGKKELMQLDQELRTAMQQQQQQLQEKEQLHSKLNNNNNNNIAATANNNNNTTMESINLIDDSEMADIKIKSEPQTAPQPQQSPHGSSHSSRSGSGSGSHSSMASDGSLRRKSSDSLDSHGAQDDAQDEEDAAPTGQRSESRAPEEPQLPTKKESVDDMLDEVELLGLHSRGSDMDSLASPSHSDMMLLDKDDVLDEDDDDDCVEQKTSGSGCLKKPGMDLKRARVENIVSGMRCSPSSGLAQAGQLQVNGCKKRKLYQPQQHAMERYVAAAAGLNFGLNLQSMMLDQEDSESNELESPQIQQKRVEKNALKSQLRSMQEQLAEMQQKYVQLCSRMEQESECQELDQDQDVEQEQEPDNGSSDHIELSPSPTLTGDGDVSPNHKEETGQERPGSSSPSPSPLKPKTSLGESSDSGANMLSQMMSKMMSGKLHNPLVGVGHPALPQGFPPLLQHMGDMSHAAAMYQQFFFEQEARMAKEAAEQQQQQQQQQQQQQQQQQQEQQRRFEQEQQEQQRRKEEQQQQIQRQQQHLQQLQQQQMEQQHVATAAPRPQMHHPAPARLPTRMGGAAGHTALKSELSEKFQMLRANNNSSMMRMSGTDLEGLADVLKSEITTSLSALVDTIVTRFVHQRRLFSKQADSVTAAAEQLNKDLLLASQILDRKSPRTKVADRPQNGPTPATQSAAAMFQAPKTPQGMNPVAAAALYNSMTGPFCLPPDQQQQQQTAQQQQSAQQQQQSSQQTQQQLEQNEALSLVVTPKKKRHKVTDTRITPRTVSRILAQDGVVPPTGGPPSTPQQQQQQQQQQQQQQQQQQQQASNGGNSNATPAQSPTRSSGGAAYHPQPPPPPPPMMPVSLPTSVAIPNPSLHESKVFSPYSPFFNPHAAAGQATAAQLHQHHQQHHPHHQSMQLSSSPPGSLGALMDSRDSPPLPHPPSMLHPALLAAAHHGGSPDYKTCLRAVMDAQDRQSECNSADMQFDGMAPTISFYKQMQLKTEHQESLMAKHCESLTPLHSSTLTPMHLRKAKLMFFWVRYPSSAVLKMYFPDIKFNKNNTAQLVKWFSNFREFYYIQMEKYARQAVTEGIKTPDDLLIAGDSELYRVLNLHYNRNNHIEVPQNFRFVVESTLREFFRAIQGGKDTEQSWKKSIYKIISRMDDPVPEYFKSPNFLEQLE
Protein: Retinoic acid receptor RXR-beta (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta) (P28702)
Organism: Homo sapiens (Human)
Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE).
Subcellular location: Nucleus {ECO:0000269|PubMed:1310259, ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:28167758}.
Interaction partners:
- Oxysterols receptor LXR-alpha
- Oxysterols receptor LXR-beta
- Retinoic acid receptor alpha
- Retinoic acid receptor beta
- Peroxisome proliferator-activated receptor gamma
- Nuclear receptor coactivator 2
- Peroxisome proliferator-activated receptor delta
- Retinoic acid receptor gamma
- Retinoic acid receptor RXR-gamma
- Retinoic acid receptor RXR-alpha
Sequence:
MSWAARPPFLPQRHAAGQCGPVGVRKEMHCGVASRWRRRRPWLDPAAAAAAAVAGGEQQTPEPEPGEAGRDGMGDSGRDSRSPDSSSPNPLPQGVPPPSPPGPPLPPSTAPSLGGSGAPPPPPMPPPPLGSPFPVISSSMGSPGLPPPAPPGFSGPVSSPQINSTVSLPGGGSGPPEDVKPPVLGVRGLHCPPPPGGPGAGKRLCAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYSCRDNKDCTVDKRQRNRCQYCRYQKCLATGMKREAVQEERQRGKDKDGDGEGAGGAPEEMPVDRILEAELAVEQKSDQGVEGPGGTGGSGSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSSLPLDDQVILLRAGWNELLIASFSHRSIDVRDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMRMDKTELGCLRAIILFNPDAKGLSNPSEVEVLREKVYASLETYCKQKYPEQQGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQLA
Protein: Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A) (Q9JIM0)
Organism: Rattus norvegicus (Rat)
Function: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P49959}. Chromosome {ECO:0000250|UniProtKB:P49959}. Chromosome, telomere {ECO:0000250|UniProtKB:P49959}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P49959}.
Interaction partners:
- DNA repair protein RAD50
- Nibrin
- Breast cancer type 1 susceptibility protein homolog
- DNA endonuclease RBBP8
- Serine-protein kinase ATM
- BRCA1-associated RING domain protein 1
- DNA 5'-3' helicase
- X-ray repair cross-complementing protein 6
- Exonuclease 1
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
Sequence:
MSPTDPLDDEDTFKILVATDIHLGFMEKDAVRGNDTFVTFDEILRLALENEVDFILLGGDLFHENKPSRKTLHSCLELLRKYCMGDRPVQFEIISDQSVNFGFSKFPWVNYRDGNLNISIPVFSIHGNHDDPTGADALCALDVLSCAGFVNHFGRSMSVEKVDISPVLLQKGSTKLALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECKIGPTRNEQQLFYVSQPGSSVVTALSPGETVKKHVGLLRVKGRKMNMQKLPLRTVRQFFMEDVVLANHPSLFNPDNPKVTQAIQSFCLEKIEEMLDSAERERLGNPQQPEKPLIRLRVDYSGGFEPFNVLRFSQKFVDRVANPKDVIHFFRHREQKGKTGEEINFGKLIIKPASEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEKTQRFLKERHIDALEDKIDEEVRRFRESRQRNTNEEDDEVREAMSRARALRSQSENAASAFSADDLSFDITEQTADDSDDSQSAVPSRGRGRGRGRRGGRGQSTAPRGGSQRGRDTGLGISTRGRSSKATASTSRNMSIIDAFRSTRQQPSRNVATKNYSETIEVDESDDDDSFPTSSRADQRWSGTAPSKRMSQSQTAKGVDFESDEDDDDDPFMSGSCPRRNRR
Protein: Very-long-chain enoyl-CoA reductase (EC 1.3.1.93) (Enoyl-CoA reductase) (AtECR) (Protein ACQUIRED OSMOTOLERANCE-DEFECTIVE 2) (Protein ECERIFERUM 10) (Synaptic glycoprotein SC2-like protein) (Q9M2U2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Required for the elongation of fatty acids precursors of sphingolipids, storage lipids and cuticular waxes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15829606}; Multi-pass membrane protein {ECO:0000269|PubMed:15829606}.
Interaction partners:
- Very-long-chain
- Very-long-chain 3-oxoacyl-CoA reductase 1
- 3-ketoacyl-CoA synthase 6
- Protein ECERIFERUM 2
- 3-ketoacyl-CoA synthase 9
- 3-ketoacyl-CoA synthase 2
- Protein ECERIFERUM 26-like
- Protein ECERIFERUM 26
- Peptidyl-prolyl cis-trans isomerase PASTICCINO1
- Very-long-chain
Sequence:
MKVTVVSRSGREVLKAPLDLPDSATVADLQEAFHKRAKKFYPSRQRLTLPVTPGSKDKPVVLNSKKSLKEYCDGNNNSLTVVFKDLGAQVSYRTLFFFEYLGPLLIYPVFYYFPVYKFLGYGEDCVIHPVQTYAMYYWCFHYFKRILETFFVHRFSHATSPIGNVFRNCAYYWSFGAYIAYYVNHPLYTPVSDLQMKIGFGFGLVCQVANFYCHILLKNLRDPSGAGGYQIPRGFLFNIVTCANYTTEIYQWLGFNIATQTIAGYVFLAVAALIMTNWALGKHSRLRKIFDGKDGKPKYPRRWVILPPFL
Protein: Transcription initiation factor TFIID subunit 12 (A0A1D8PSN1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 13
- TAFII28-like protein domain-containing protein
- TAFII55 protein conserved region domain-containing protein
- Transcription initiation factor TFIID subunit 4
- Taf145p
Sequence:
MNNGSQNQSANNGQQPQQQINLQNIPPQQLAQLVTAMRTAYDQAKNSTNEAERQQHFNRAENIRRLLARYQAQKNRLQQQQQQQQQQQQQRTQQQTQQQTQQQRNLTEHQRQIQAVQAQAQALAQMNNNENFNAMSNNQVGTPMMQQQSPNMMLQSPMMQQKQTNVGTPMRQQSPLMTQQSPPEQFQAQKSNPTPQPQVQQNVQQMNQNNVIRNNAIVGTNGAAPGQINGVPIANSNITMERFNQIRQKLTEVQRRVQLLEQTKKTGNVTPEQIQQIDKEIIECKAKFQQYQKVGIYIRNQLVLQAKAQQQRQLQQRQQQQQQQQQQNNNLKSAQNQNQNQNQNQNQNQNQNQNQIQGVQSAGQTPQQQSFSPQLQAAQQQQFMGNSQQQQQQQQQQLRNANKSALQGQAPSQAPTPLPVRPTPQSQPTAQAGVASQAATSGFRASQPTPSQTSRTGSALQQRAPSRQASSTPQSQFQPPLPSESRHPSATTSEKPLPQQPGSGTAKSPSVAATPAQNNGTVTARSASPVATTTDSATTGRSGTPQQQSRSRSGSSLNLAGITRQSVPSLPISSSINVKQPTITTFNSINDTRPSLTGGAANPMSILLDTPAITKLPTFDIEGDTGVIDSSTSGRVLNKRKLGDLINTIGVDEGDGKTSIDGNVEEFLLDLADEFIHSVTSFACRLAKHRKVDSIEARDVQLHLDKNWNIKIPGYAMDEIRNTRKIQPSNSYSQKVQGVEVSKAVNDDNA
Protein: Citrate synthase (EC 2.3.3.16) (Q86AV6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15225305}.
Interaction partners:
- malate synthase
- Probable aconitate hydratase, mitochondrial
- Probable cytoplasmic aconitate hydratase
- Probable ATP-citrate synthase
- Probable malate dehydrogenase 2, mitochondrial
- Probable malate dehydrogenase 3
- Probable malate dehydrogenase 1
- ATP citrate synthase
- isocitrate lyase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Sequence:
MSSNSQEDNNKTTEKKNTLTVIDNRTGKSYEIPINHETVKSIDFRAIKEQSIDFGTMIYDPGYYNTAVCKSQITYIDGDRGILEYRGYPIEQLAEKSSFLEVSYLLIYGDLPSKEQSNLWNTKIMNHTFIHENLISMMKSFRYDAHPMGMLISSLSAMSTFYPEANPALAGVDIYKNKQLMNKQIFRILGKLPTIAACAYRHRIGRPYNDPSNTLSYTENFLYMLDRLSESNYKPHPVLTRALDKLFIIHADHELNCSTATMRQIASTLVDPYTACAGSAGALYGPLHGGANEAVLRMLEAIGTIENIPKFIEQVKQKKQRLMGFGHRVYKSYDPRAKILKTVTMEIFALLGKNPLMQIATELERLALSDSYFIERQLYPNVDFYSGIIYKSMGFPTDMFPVLFSIPRAAGWLAHWVEELADPELRIFRPRQIYMGRRNMNYVPMDARQVQQHNSGEKLSSFSSGFDRRRDVSEELFNFEDGAIPKTATGSKSQLSASIEQSFGEKISPQSH
Protein: Trihelix transcription factor GT-3a (Trihelix DNA-binding protein GT-3a) (Q9SDW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that binds specifically to the core DNA sequence 5'-GTTAC-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:15044016}.
Interaction partners:
- Trihelix transcription factor ASIL1
- Trihelix transcription factor ASIL2
- RING/FYVE/PHD zinc finger superfamily protein
- Trihelix transcription factor GTL2
- Protein FIP2
- Trihelix transcription factor ASR3
- Probable protein phosphatase 2C 47
- Protein indeterminate-domain 6
- Trihelix transcription factor GT-3b
- At5g63780
Sequence:
MDRRNPFQHHHHHHQLHHHLIQQQQLPPPPLSTTATMDPGGGGGGGERIPQWSIEETKELLAIREELDQTFMETKRNKLLWEVVAAKMADKGFVRSAEQCKSKWKNLVTRYKACETTEPDAIRQQFPFYNEIQSIFEARMQRMLWSEATEPSTSSKRKHHQFSSDDEEEEVDEPNQDINEELLSLVETQKRETEVITTSTSTNPRKRAKKGKGVASGTKAETAGNTLKDILEEFMRQTVKMEKEWRDAWEMKEIEREKREKEWRRRMAELEEERAATERRWMEREEERRLREEARAQKRDSLIDALLNRLNRDHNDDHHNQGF