wanglab/gogpt-training-data huggingface dataset:
Protein: Active regulator of SIRT1 (40S ribosomal protein S19-binding protein 1) (RPS19-binding protein 1) (S19BP) (Q86WX3)
Organism: Homo sapiens (Human)
Function: Direct regulator of SIRT1. Enhances SIRT1-mediated deacetylation of p53/TP53, thereby participating in inhibition of p53/TP53-mediated transcriptional activity.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:17964266, ECO:0000269|PubMed:34516797}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-1
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS12
- WD repeat-containing protein 46
- Ribosomal RNA small subunit methyltransferase NEP1
- rRNA 2'-O-methyltransferase fibrillarin
- U3 small nucleolar ribonucleoprotein protein MPP10
- U3 small nucleolar ribonucleoprotein protein IMP3
- Ribosomal RNA-processing protein 7 homolog A
Sequence:
MSAALLRRGLELLAASEAPRDPPGQAKPRGAPVKRPRKTKAIQAQKLRNSAKGKVPKSALDEYRKRECRDHLRVNLKFLTRTRSTVAESVSQQILRQNRGRKACDRPVAKTKKKKAEGTVFTEEDFQKFQQEYFGS
Protein: Threonine--tRNA ligase, mitochondrial (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (P07236)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Leucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, mitochondrial
- Valine--tRNA ligase, mitochondrial
- Lysine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Probable proline--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, mitochondrial
Sequence:
MKIQLVRWHCSRNALWNRAFYSTRKATKNASSATPATMTSMVSQRQDLFMTDPLSPGSMFFLPNGAKIFNKLIEFMKLQQKFKFGFNEVVTPLIYKKTLWEKSGHWENYADDMFKVETTDEEKEEYGLKPMNCPGHCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPSQVKSEIFNSLKLIDIVYNKIFPFVKGGSGAESNYFINFSTRPDHFIGDLKVWNHAEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHLRKTHQVATIQLDFQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFWLNPYQAVIIPVNTKNVQQLDMCTALQKKLRNELEADDMEPVPLNDWHFNVDLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRKSFEKLTMSQIWEKFIELEKNYK
Protein: E3 ubiquitin-protein ligase RNF146 (EC 2.3.2.27) (Iduna) (RING finger protein 146) (RING-type E3 ubiquitin transferase RNF146) (Q5XIK5)
Organism: Rattus norvegicus (Rat)
Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein (By similarity). Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos (By similarity). Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner (By similarity). Does not affect PARP1 activation. Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest (By similarity). Promotes cell survival after gamma-irradiation. Facilitates DNA repair (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates to the nucleus after DNA damage, such as laser-induced DNA breaks, and concentrates at DNA breaks. This translocation requires PARP1 activation and PAR-binding (By similarity). {ECO:0000250}.
Interaction partners:
- Poly [ADP-ribose] polymerase
- Tankyrase 2
- Axin-2
- Poly [ADP-ribose] polymerase 1
- Ubiquitin-conjugating enzyme E2 D1
- Poly
Sequence:
MAGCGEIDHSLNMLPTNKKASETCSNTAPSLTVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDKPTLLSPEELKAASRGNGEYVWYYEGRNGWWQYDERTSRELEDAFSKGKKNTEMLIAGFLYVADLENMVQYRRNEHGRRRKIKRDIIDIPKKGVAGLRLDCDSNTVNLARESSADGADSGSAHTGASVQLPVPSSTRPLTSVDGQLTSPVTPSPDAGASLEDSFAHLQLSGDSIAERSHRGEGEEDHESPSSGRVPDTSTEETESDASSDIEDAPVVVAQHSLTQQRLLVSSANQTVAERSDRPVAGGGTMSVNVRSRRPDGQCTVTEV
Protein: Stress-activated protein kinase JNK (EC 2.7.11.24) (Q499Y8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368052}.
Interaction partners:
Sequence:
MELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDMWSVGCIMGEMIKGAVLFPGTDHIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR
Protein: Oleate-activated transcription factor (A0A1D8PKC2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Cwt1p
Sequence:
MTSEHKVSRNKPSLSCTNCRKRKTKCDRKQPCSACVKKINLSYTCAYDTPPKQFAINSDTPPTEYPARKRHKPETIDDAENPVQQELARLRKRIIELETSLQHAHTPKTPPENKNYPRNKPILSPTSSTCPNPIVNDEEIINFYEGYTPIQVKRNIRRVNYGPLSWIALMRKDPALNLAWKVLCSKDSYCIITNRWPRLTSENNALINISHNPEDEKNSNYMDKIFQKRVLEFEGYDEFVPYRSLYGRKESDTTNTEQPTTSDKSTSKPSSTTTTNPGPRLNFTQISLAKSIFDGRINPELHLIEKIKQIVPKRKVFWTLMDRFFTDIYPYFPFVDEESFKKELSRIFGTRTYTDLPFESIRIEKKLDLANIAICFILLRLTYLSFFNNRNCVNEFIMNSEEETVAKYIMQNPINLSTIEVANSCIQCFQFTRKSNITVFQAMLYMRIYRNCAPEESDGIDGGDSQVATALLVQMAYSLGLNREPDKFDVCNDEKVNHLGRKMWSFLMRSDLTQCYTLGNPTSIDPRNYDVRPPFVNDNNSNIEDREMEIAIVETFVYLNSELDLMRKMLDHVLDINNGAKINDLTRDVHDFEVILHDFFNVLGNVNAGKVKTDRESVIQYYHVIKLKIFLSMKTALVSLYFHIYLHYEKRFDSELSFFYLSKMYLIIRDDLIPAIGHTLIGKYSSKALVLNPNMQLALHKINQINLSCLIRVSYLVHMFEQKPNHEESMANDIVYSEHFNKLKSLMTNVRRTGDFVRVIMERIGSRYYYSWRIAKAHVGLFKMLSQPENYDKQLSGIRKLKSFQFTPKQLDELDNSIRILGKCAEKLVFYEDSVGMSPDFEMPFKPSEGDGNEKDQNQNDSKTTTTTTTTTTSDSTGISITPENNASAIVTPYSSLASPRLHLDNISNDYVDQMWFSMMAMKYDTLEPMGNNPDCQNCNSDDPNACPVSYNTRDNGVLGGTGGQLLTQQKQMTAQEQLAQQEITRQMQFGNENGYNNGFFLNSGFDLMDDGYFYG
Protein: 5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase (EC 2.5.1.147) (FO synthase subunit 2) (Q58826)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
Interaction partners:
- 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase
- Phosphoribosyl-AMP cyclohydrolase
- 2-phospho-L-lactate guanylyltransferase
- Uncharacterized protein MJ1432
- Phosphomethylpyrimidine synthase
- DNA/RNA-binding protein Alba
- Uncharacterized protein MJ1433
- Putative DNA repair glycosylase MJ1434
- Homocitrate synthase AksA
- 2-
Sequence:
MDPNKFREKEISKKEALELFEDNEIIFELFKFADSLRREEVGDIVTYVVNRNINFTNICVGNCRFCAFRANENDKHAYFLDIDEIAKRAVEAKKFGCTEVCIQGGLHPKIDTYYQAEILKAVHEATKPYGDIHIHAFSPMEVYFGAENAGLDIKEALKILKENGLNSMPGTAAEILDDDIRAELCPNKIKTKEWIYIIKEAHKLGIPTTATMMYGHIEEYKHWVNHLFIIKEIQEETNGFTEFVPLSFMHKYAPIYKEGKAKAGATGIEDLKVFAVSRIIFKGLIKNIQASWVKLGKKMVQVALRCGANDVGGTLIEESISRSAGAEHGVYMSVEEIRDMIKRVGLIPKERTTLYKILE
Protein: Lon protease (EC 3.4.21.53) (ATP-dependent protease La) (P0A9M0)
Organism: Escherichia coli (strain K12)
Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, UmuD and at least type II antitoxins CcdA, HipB and MazE. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system.
Subcellular location: Cytoplasm.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease ATP-binding subunit ClpX
- Chaperone protein DnaK
- ATP-dependent protease subunit HslV
- ATP-dependent protease ATPase subunit HslU
- ATP-dependent zinc metalloprotease FtsH
- Chaperone protein DnaJ
- Chaperonin GroEL
- Chaperone protein ClpB
- Protein GrpE
Sequence:
MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK
Protein: Cellular retinaldehyde-binding protein b (Retinaldehyde-binding protein 1b) (Q6P027)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Retinol dehydrogenase 5
- Retinal Mueller cells isomerohydrolase
- Dehydrogenase/reductase
- Bestrophin homolog
- Diacylglycerol O-acyltransferase 2
Sequence:
MAVVSGTFRMVSEEEQALRAKLEHLTVKDHGPVFEASTKVPDHTMQKAKDELNETDEKRTSAVKELRGIIKEKAETGDELAKGVQDTFGEKPDGVLVRFIRARKYDVNRAYELMKGYVRFRRDYPELFENLTPEAVRSTIEAGYPGILSSRDKYGRVVLLFNIENWDYEEITFDEILRAYCVILEKLLENEETQINGFCIIENFKGFTMQQASGIKPTELKKMVDMLQDSFPARFKAVHFIHQPWYFTTTYNVVKPLMKSKLLERVFVHGDDLENYFKEFDAEILPSDFDGKGSKYDGKITAAHLFD
Protein: Immunoglobulin heavy constant gamma 2C (A0A0A6YY53)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XKTTAPSVYPLAPVCGGTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPALLQSGLYTLSSSVTVTSNTWPSQTITCNVAHPASSTKVDKKIEPRVPITQNPCPPLKECPPCAAPDLLGGPSVFIFPPKIKDVLMISLSPMVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNRALPSPIEKTISKPRGPVRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATVLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLGK
Protein: Leucine-rich glioma-inactivated protein 1 (Q9JIA1)
Organism: Mus musculus (Mouse)
Function: Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors. Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:15857855}. Synapse {ECO:0000250|UniProtKB:Q8K4Y5}. Cytoplasm {ECO:0000269|PubMed:26269648}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:16787412}. Golgi apparatus {ECO:0000250|UniProtKB:O95970}. Secreted {ECO:0000250|UniProtKB:O95970}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:16787412}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O95970}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 22
- Disintegrin and metalloproteinase domain-containing protein 23
- Disks large homolog 4
- Disintegrin and metalloproteinase domain-containing protein 11
- Potassium voltage-gated channel subfamily A member 1
- Contactin-associated protein-like 2
- Contactin-2
- Voltage-dependent calcium channel gamma-2 subunit
- Glutamate receptor ionotropic, NMDA 1
- Inactive dipeptidyl peptidase 10
Sequence:
MESESSRRMGNACIPLKRIAYFLCLFSVVLLTEGKKPAKPKCPAVCTCSKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGSFLFTPSLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNLQTLPKDIFKGLDSLTNVDLRGNAFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKINSLSPKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKTFRNYDNITGTSTVVCKPIVIDTQLYVIVAQLFGGSHIYKRDGFANKFIKIQDIEVLKIRKPNDIETFKIEDNWYFVVADSSKAGFTTIYKWNGNGFYSHQSLHAWYRDTDVEYLEIARPPLALRTPHLILSSSSQRPVIYQWSKATQLFTNQTDIPNMEDVYAVKHFSVKGDVYICLTRFIGDSKVMKWGGSSFQDIQRMPSRGSMVFQPLQINNYQYAILGSDYSFTQVYNWDAEKAKFVKFQELNVQAPRSFTHVSINKRNFLFASSFKGNTQIYKHVIVDLSA
Protein: 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 (HMG-CoA reductase 1) (EC 1.1.1.34) (Ergosterol biosynthesis protein hmg1) (Q4WHZ1)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA). Hmg1 and hmg2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate (Probable). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase erg13A
- Hydroxymethylglutaryl-CoA synthase erg13B
- Mevalonate kinase erg12
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2
- Sterol 14-alpha demethylase cyp51A
- Sterol 14-alpha demethylase cyp51B
- Phosphomevalonate kinase erg8
- INSIG domain-containing protein
- Squalene epoxidase erg1
- Inosine-5'-monophosphate dehydrogenase
Sequence:
MATSLITRKLRSAEATNDVEPGWLKRQVTGVLQSISSHACQHPIHTIVVIALLASTTYVGLLEGSLFDSVRNSRNIAGQVDVDTLLQGSRNLRLGESTSWKWQVEDSLASQDYTGVNHLALTTFIFSDSLSKSSSIAPAATELPIPSNASAQPVPFTPNLFSPFSHDSSLAFTLPFDQVPQFLKAVQEIPDTSSDEDDGEQKKWIMRAARGSAYGSGGAIKLWLADAWGSFVDLIKHAETIDIVIMTLGYLSMHLSFVSLFFSMRRLGSNFWLAATVLFSGVFAFLFGLLVTTKLGVPINVLLLSEGLPFLVVTIGFEKPIILTRAVLTAAADNRGRAGQASSSTTKSIQDSIQTAIKEQGFEIIRDYCIEIAILIAGAASGVQGGLRQFCFLAAWILFFDCVLLFTFYTTILCIKLEINRIKRHITLRKALEEDGITHRVAENVASSNDWPLTESESSNKTSIFGRKLRSSSVRRFKILMVGGFVLVNVVNLSTIPFRDSSQGAGLPLLSRVSNVFAPTPIDPFKVAENGLDSIYVSAKSQMMETVVTVIPPIKYKLEYPSVYYAALGESRTFDIEYTDQFLDAVGGRVIESLLKSIEDPIISKWIIAALTLSIILNGYLFNAARWSIKEPEVAPVPAAPTVAVVEAKKEYPKIDLNPDTPKRSLEECEAFLKEKRAAYLSDEELIELSLRGKIPGYALEKTMENEDLMSRVDAFTRAVKIRRAVVARTPATSAITGSLECSKLPYKDYNYTLVHGACCENVIGYLPLPLGVAGPLTIDGQSYFIPMATTEGVLVASTSRGAKAINAGGGAVTVLTGDGMTRGPCVGFPTLARAAAAKVWIDSEEGRSILTAAFNSTSRFARLQHLKTALAGTYLYIRFKTTTGDAMGMNMISKGVEKALHVMATECGFDDMATISVSGNFCTDKKAAAINWIDGRGKSVVAEAIIPGDVVRSVLKSDVNALVELNTSKNLIGSAMAGSVGGFNAHASNIVTAVFLATGQDPAQNVESSSCITTMRNLNGNLQIAVSMPSIEVGTIGGGTILEAQSAMLDMLGVRGSHPTNPGDNARQLARIVAAAVLAGELSLCSALAAGHLVRAHMAHNRSAATTRTSTPVSAAVSAARGLTMSSSE
Protein: Zinc finger protein 346 (Double-stranded RNA-binding protein ZFa) (DsRBP-ZFa) (ZFa) (Just another zinc finger protein) (Protein jaz) (Q8AVN9)
Organism: Xenopus laevis (African clawed frog)
Function: Binds preferentially to dsRNA, but also to RNA-DNA hybrids.
Subcellular location: Nucleus {ECO:0000269|PubMed:9268652}. Cytoplasm {ECO:0000269|PubMed:9268652}. Note=Primarily nuclear. {ECO:0000269|PubMed:9268652}.
Interaction partners:
Sequence:
MADEFGNGDALDLPVGKDAVNSLIRENSHIFSDTQCKVCSAVLISESQKLAHYQSRKHANKVRRYMAINQGEDSVPAKKFKAAPAEISDGEDRSKCCPVCNMTFSSPVVAESHYIGKTHIKNLRLREQGGVKEGMVNQAKKTRTPTVATKSDNKMDHSDRAKFCKLCHSTFNNPLMAEQHYAGKKHKKQETKTQIMTIYTSSGQTPAQAPIPLNLNSPMPGSGSAGKGFSCDKCNIVLNSIEQYQAHVSGAKHKNQLMSMTPLSEEGHQAVVAPSAIASGSAGKGFSCDTCNIVLNSIEQYQAHISGAKHKNHLKSMTPLSEEGHTAAVAPSAFASGSAGKGFSCDTCNIVLNSIEQYQAHISGAKHKNHLMSMTPLSEEGHTAAVAPSAFASGSAGKGFSCDTCNIVLNSIEQYQAHVSGAKHKNQLMSMTPSSEEGLPSAVGPSAFASPLSAGGALSSGGPSGRGFCPSGDLTPKGPSSFGSLPPLGSLLPPLYPPAHSSQPYVHDDTMSPDGYNYFNEDFE
Protein: NAD-dependent malic enzyme, mitochondrial (NAD-ME) (EC 1.1.1.38) (Malic enzyme 2) (P23368)
Organism: Homo sapiens (Human)
Function: NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:1993674}.
Interaction partners:
- Fumarate hydratase, mitochondrial
- Pyruvate carboxylase, mitochondrial
- L-lactate dehydrogenase A chain
- Malate dehydrogenase, mitochondrial
- Citrate synthase, mitochondrial
- Pyruvate kinase PKLR
- Pyruvate kinase PKM
- L-lactate dehydrogenase A-like 6A
- L-lactate dehydrogenase A-like 6B
- L-lactate dehydrogenase C chain
Sequence:
MLSRLRVVSTTCTLACRHLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASSPPVITE
Protein: acetyl-CoA carboxylase (EC 6.4.1.2) (A0A0G2K5L6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVLLLFLTCLVFSCLTISWLKIWGKMTDSKPLSNSKVDASLLSSKEESFSASDQSEEHGDCSCPLTTPDQEELASHGGPVDASQQRNSVPSSHQKPPRNPLSSNDTCSSPELQTNRVAAPGSEVPEANGLPFPARPQTQRTGSPTREDKKQAHIKRQLMTSFILGSLDDNSSDEDPSASSFQTSSRKGSRASLGTLSQEAALNTADPESHTPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIETVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKISSTIVAQTLQIPTLPWSGSGLTVEWTEDSQHQGKCISVPEDVYEQGCVRDVDEGLQAAEKVGFPLMIKASEGGGGKGIRRAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPVSFETPLSPPIARGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDIMLGVVCGALNVADAMFRTCMTEFLHSLERGQVLPADSLLNIVDVELIYGGIKYVLKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGSSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLMQYTVEDGQHVEVGSSYAEMEVMKMIMTLNVQESGRVKYIKRPGAVLEAGCVVAKLELDDPSKVHAAQPFTGELPAQQTLPILGERLHQVFHSVLENLTNVMNGYCLPEPFFSMKLKDWVEKLMMTLRHPSLPLLELQEIMTSVAGRIPVPVEKAVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKVDREAFFMNTQSIVQLIQRYRSGTRGYMKAVVLDLLRRYLNVEHHFQQAHYDKCVINLREQFKPDMTRVLDCIFSHSQVAKKNQLVTMLIDELCGPDPTLSEELTSILKELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAMPINVSDPDLLRHSKELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVPTDTPLFSKACTSLYSEEDSKPSFFLSQSLQEEPIHILNVAIQCADHMEDERLVPVFRAFVQSKKHILVDYGLRRITFLIAQEREFPKFFTFRARDEFAEDRIYRHLEPALAFQLELSRMRNFDLTAVPCANHKMHLYLGAAKVKEGLEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRAMVMRYGSRLWKLRVLQAEVKINIRQTTSDCAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGSLHGMLINTPYVTKDLLQAKRFQAQSLGTTYVYDFPEMFRQALFKLWGSPEKYPKDILTYTELVLDSQGQLVEMNRLPGCNEVGMVVFKMRFKTPEYPEGRDTIVIGNDITFQIGSFGIGEDFLYLRASEMARTEGIPQIYLAANSGARMGLSEEIKQIFQVAWVDPEDPYKGFRYLYLTPQDYTQISSQNSVHCKHIEDEGESRYVIVDVIGKDSSLGVENLRGSGMIAGEASLAYEKNVTISMVTCRAIGIGAYLVRLGQRVIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSYIPKDNQSPVPIITPSDPIDREIEFTPTKAPYDPRWLLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRSVEVAVPADPANLDSEAKIIQQAGQVWFPDSAFKTAQVIRDFNQEHLPLMIFANWRGFSGGMKDMYEQMLKFGAYIVDSLRLFKQPVLIYIPPGAELRGGAWVVLDSSINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRRIDPVCKKLLGQLGTAQLPDKDRKELESQLKAREDLLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTTRTYFYWRLRRLLLEAQVKQEILRASPELSHEHTQSMLRRWFVETEGAVKAYLWDSNQVVVQWLEQHWSARDNLRSTIRENINYLKRDSVLKTIQSLVQEHPEATMDCVAYLSQHLTPAEQMQVVQLLSTTESPASH
Protein: Neutral sphingomyelinase activation associated factor (F1M974)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAFTRKRQREQQLQLYSKERFSLLLLNLEEYYFEQHTAFHVQHQGSPEERKIRGSLKICSKSVIFEPDAISQPILKIPLRDCLKIGKHGENGANKHFAKAKSLGISLIFSQVYFIKEHNIVAPYKIERGKMEYVFQLEVSGKVEDVVETLLQLHRASCLDKLGDQMAMITAILQSRLARTSFDKNRFQSVSEKLHMECKAEMVTPLVTNPGHVCITDTNLYFQPLNGYPKPVVQITLQDVRRIYKRRHGLMPLGLEVFCTEDDLCSDIYLKFYEPQDRDDLYFYIATYLEHHVAEHTAESYMLQWQRGHLSNYQYLLHLNNLADRSCNDLSQYPVFPWVISDYSSPELDLSNPATFRDLSKPVGALNPERLERLLTRYQEMPEPKFMYGSHYSSPGYVLFYLVRIAPEYMLCLQNGRFDNADRMFNSIAETWKNCLDGATDFKELIPEFYDEDASFLINSLKLDLGKRQGGQMVDDVELPAWASSPQDFLQKNKDALESSYVSEHLHEWIDLIFGYKQKGSEAIGAHNVFHPLTYEGGVDLNSIEDPDDKVAMLTQILEFGQTPKQLFVTPHPRRITPKFKSLSQASSYNASMTDSPVSPGEESFEDLTEESKTLAWNNITKLQLHEQYKIHKEAVTGIAVSCNGSSVFTTSQDSTLKMFSKESKMLQRSISFSNMALSSCLLLPGDTTVISSSWDNNVYFYSIAFGRRQDTLMGHDDAVSKICWHNDRLYSASWDSTVKVWSGVPAEMPGTKRHQFDLLAELEHDVSVNTINLNAVSTLLVSGTKEGLVNIWDLTTATLLHQISCHSGTVCDAAFSPDSRHVLSTGVDGCLNVIDVQTGMLISSMASEEPQRCFVWDGNSVLSGSRTGELLVWDLLGAKVSERIQGHTGAVTCIWMNEQCSSIITGGEDRQVMFWKLQY
Protein: Lymphotoxin-alpha (LT-alpha) (TNF-beta) (Tumor necrosis factor ligand superfamily member 1) (Q6FG55)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU368120}. Membrane {ECO:0000256|RuleBase:RU368120}.
Interaction partners:
Sequence:
MTPPERLFLPRVRGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q94AB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGGCCCCSSSRRADVDNGPAYYYYPRATEERVPLSSAHNRTSSAISTGVVVVDTNLETSSPDAYIPPPLPTPFDVPIGIPQTPASGEEATCVDIREVSVDSANTESAQETVDGITLGVPTTCSHKETDSKIQTEIDLESTEEIDPKLSKAVFIPIEEEEDCPICLEEYDIENPKLVAKCDHHFHLACILEWMERSETCPVCNKEMVFDSTLD
Protein: Cardiolipin synthase C (CL synthase) (EC 2.7.8.-) (P75919)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) from phosphatidylglycerol (PG) and phosphatidylethanolamine (PE).
Interaction partners:
- O-acetyl-ADP-ribose deacetylase
- Phosphatidylglycerophosphatase A
- Phosphatidylglycerophosphatase C
- Cardiolipin synthase B
- Cardiolipin synthase A
- Phosphatidylglycerophosphatase B
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidylserine decarboxylase proenzyme
- Phosphatidate cytidylyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
Sequence:
MPRLASAVLPLCSQHPGQCGLFPLEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVRLFNPFSFRLLRPLGYITDFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPLFSDLDVMAIGPVVEDVADDFARYWYCKSVSPLQQVLDVPEGEMADRIELPASWHNDAMTHRYLRKMESSPFINHLVDGTLPLIWAKTRLLSDDPAKGEGKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYARWRKKLLRYGVELYELKPTREQSSTLHDRGITGNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRFIQSQYDAAWQLRLDRWGRINWVDRHAKKEIILKKEPATSFWKRVMVRLASILPVEWLL
Protein: Paired box protein Pax-6 (A0A1W2PSA8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPD