wanglab/gogpt-training-data huggingface dataset:
Protein: Diphthamide biosynthesis protein 3 (CSL-type zinc finger-containing protein 2) (Diphtheria toxin and Pseudomonas exotoxin A sensitivity-required protein 1) (Q6VUC1)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase. Acts as an electron donor to reduce the Fe-S cluster in DPH1-DPH2 keeping the [4Fe-4S] clusters in the active and reduced state. Restores iron to DPH1-DPH2 iron-sulfur clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an iron atom to reform [4Fe-4S] clusters, in a manner dependent on the presence of elongation factor 2 and SAM. Associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96FX2}. Nucleus {ECO:0000250|UniProtKB:Q96FX2}.
Interaction partners:
Sequence:
MAVFHDEVEIEDFQYDEDSETYFYPCPCGDNFSITKEDLENGEDVATCPSCSLIIKVIYDKDQFMCGETVPAPSTNKELVKC
Protein: Protein N-terminal asparagine amidohydrolase (EC 3.5.1.121) (Protein NH2-terminal asparagine amidohydrolase) (PNAA) (Protein NH2-terminal asparagine deamidase) (PNAD) (Protein N-terminal Asn amidase) (Protein NTN-amidase) (Q64311)
Organism: Mus musculus (Mouse)
Function: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q28955}.
Interaction partners:
- L-selectin
- Mucosal addressin cell adhesion molecule 1
- Carbohydrate sulfotransferase 4
- Protein N-terminal glutamine amidohydrolase
- C-C chemokine receptor type 7
- Arginyl-tRNA--protein transferase 1
- Carbohydrate sulfotransferase 2
- P-selectin
- Glycosylation-dependent cell adhesion molecule 1
- Vascular cell adhesion protein 1
Sequence:
MPLLVDGQRVRLPRSAVELVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGSDTKAEVPLIMSSIKSFSEHAECGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDKQDDDIHLVTLCVTELNDREENENHFPIIYGIAVNIKTAEIYRASFQDRGPEEQLRAARALAGGPMISIYDAKTEQLRIGPCSWTPFPQVDFWLQQDDKQILESLSTSPLAEPPHFVEHIRSTLMFLKKFPSPENILFPGNKALLYKKNKDGLWEKISSPGS
Protein: Phosphatidate cytidylyltransferase 1 (EC 2.7.7.41) (CDP-DAG synthase 1) (CDP-DG synthase 1) (CDP-diacylglycerol synthase 1) (CDS 1) (CDP-diglyceride pyrophosphorylase 1) (CDP-diglyceride synthase 1) (CTP:phosphatidate cytidylyltransferase 1) (Q92903)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol. Exhibits almost no acyl chain preference for PA, showing no discrimination for the sn-1/sn-2 acyl chain composition of PAs. Plays an important role in regulating the growth of lipid droplets which are storage organelles at the center of lipid and energy homeostasis. Positively regulates the differentiation and development of adipocytes (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25375833, ECO:0000269|PubMed:26946540, ECO:0000269|PubMed:31548309}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidate cytidylyltransferase, mitochondrial
- Cardiolipin synthase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Phosphatidate cytidylyltransferase 2
- Phospholipase D1
- Phospholipase D2
- Phospholipid phosphatase 2
Sequence:
MLELRHRGSCPGPREAVSPPHREGEAAGGDHETESTSDKETDIDDRYGDLDSRTDSDIPEIPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQVKCFHEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLIRYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMIWFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVVFGFIAAYVLSKYQYFVCPVEYRSDVNSFVTECEPSELFQLQTYSLPPFLKAVLRQERVSLYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRGPNPSKVLQQLLVLQPEQQLNIYKTLKTHLIEKGILQPTLKV
Protein: Killer cell lectin-like receptor subfamily F member 2 (Lectin-like receptor F2) (Activating coreceptor NKp65) (D3W0D1)
Organism: Homo sapiens (Human)
Function: C-type lectin-like receptor involved in natural killer cell mediated cytotoxicity and cytokine secretion in keratinocytes via its interaction with CLEC2A.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20194751}; Single-pass type II membrane protein {ECO:0000269|PubMed:20194751}.
Interaction partners:
- C-type lectin domain family 2 member A
- C-type lectin domain family 2 member B
Sequence:
MENEDGYMTLSFKNRCKSKQKSKDFSLYPQYYCLLLIFGCIVILIFIMTGIDLKFWHKKMDFSQNVNVSSLSGHNYLCPNDWLLNEGKCYWFSTSFKTWKESQRDCTQLQAHLLVIQNLDELEFIQNSLKPGHFGWIGLYVTFQGNLWMWIDEHFLVPELFSVIGPTDDRSCAVITGNWVYSEDCSSTFKGICQRDAILTHNGTSGV
Protein: Ectopic P granules protein 6 (Q86MP3)
Organism: Caenorhabditis elegans
Function: Component of the epg-6/atg-2 complex, which is involved in the generation of autophagosomes from omegasomes and in the distribution of atg-9 and atg-13 during the autophagy-mediated degradation of protein aggregates. Binds to phosphatidylinositols on preautophagosomes, which are early autophagic structures, to promote autophagosome formation. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P), but more weakly to phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Involved in autophagy-mediated degradation of ribosomal RNA and ribosomal proteins in lysosomes, which is essential for maintaining nucleotide homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21802374}. Preautophagosomal structure membrane {ECO:0000305|PubMed:21802374}; Peripheral membrane protein {ECO:0000305|PubMed:21802374}. Note=Localizes to the cytoplasm of all cells during embryogenesis. {ECO:0000269|PubMed:21802374}.
Interaction partners:
- Autophagy-related protein 2
- Autophagy-related protein 9
- Autophagy-related protein 5
- Ubiquitin-like protein atg-12
- Ectopic P granules protein 5
- MRG domain-containing protein
- Ubiquitin-like modifier-activating enzyme ATG7
- Protein lgg-1
- Autophagy-related protein 101
- Ubiquitin-like-conjugating enzyme ATG3
Sequence:
MSKKEETIFFRIEKENRPESSKKEEDENSTEEMTTLNHASVTLDHSAFAIADKDGFKMYQLNPLHFRMYKDYVIKVGPVRLVKQDGNSRRIIYVSALAGGRFAQNNLMIFDVARNEEYFEITTPSRYGPITNIHVSPNRLVALNPNRMFVWTYPDDIKQIRSEDIRSNPKGISAMSYDPTTAACYLAYPGFKTGSVQIMHLNALTARESKSPIVIEAHLTDIAQVALNCQGTLVATGSTKGTVIRVFDARTKGPLYELRRGTVQAHLQCMAFSPCSSYLAVASDKGTLHMFGIRDAEPQKKKNVLERSRGSSSIVKIQLDRPVMAIGFGKIPETPKNLQSIIAICADATYWRHEFYKDNTGNFTSHFGSYDELIEVANDSSFFRTPVE
Protein: Regulator of G-protein signaling 2 (RGS2) (Cell growth-inhibiting gene 31 protein) (G0/G1 switch regulatory protein 8) (P41220)
Organism: Homo sapiens (Human)
Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. It is involved in the negative regulation of the angiotensin-activated signaling pathway. Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle (By similarity). Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:11278586, ECO:0000269|PubMed:17901199, ECO:0000269|PubMed:28784619}. Cytoplasm {ECO:0000269|PubMed:11278586, ECO:0000269|PubMed:17901199}. Nucleus, nucleolus {ECO:0000269|PubMed:11278586, ECO:0000269|PubMed:17901199}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17901199}. Cytoplasm {ECO:0000269|PubMed:17901199}. Nucleus, nucleolus {ECO:0000269|PubMed:17901199}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:17901199}. Cytoplasm {ECO:0000269|PubMed:17901199}. Nucleus, nucleolus {ECO:0000269|PubMed:17901199}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:17901199}. Mitochondrion {ECO:0000269|PubMed:17901199}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- cGMP-dependent protein kinase 1
- Adenylate cyclase type 3
- cGMP-dependent protein kinase 2
- Neurabin-2
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit beta-5
- Glycerophosphodiester phosphodiesterase 1
- Guanine nucleotide-binding protein subunit alpha-14
Sequence:
MQSAMFLAVQHDCRPMDKSAGSGHKSEEKREKMKRTLLKDWKTRLSYFLQNSSTPGKPKTGKKSKQQAFIKPSPEEAQLWSEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKTLIAQNIQEATSGCFTTAQKRVYSLMENNSYPRFLESEFYQDLCKKPQITTEPHAT
Protein: Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (Cyclophilin D) (Cyclosporin-sensitive proline rotamase 5) (Rotamase D) (P35176)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:8377189}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FPR2
- FK506-binding protein 1
- Ran-specific GTPase-activating protein 1
- Non-selective voltage-gated ion channel 1
- Cytochrome c isoform 2
- Cytochrome c isoform 1
- ADP,ATP carrier protein 2
Sequence:
MKLQFFSFITLFACLFTTAIFAKEDTAEDPEITHKVYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLTISRDPKMGYLNSIFHRVIPNFMIQGGDFTHRSGIGGKSIFGNTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVIIVESGELETVPLDNKDAAKLQEEIKAEASEAAHDEL
Protein: McKusick-Kaufman syndrome (McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin) (Mkks protein) (Q7ZVV0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSRISKKKPALCTDEPLSNSTICQKITLLRNILSTAYGPTGRLKQIHNNVGGHVLTTSTSTALLKRLEMSEPLLKLISTALQHHTTRYSDSGLFMGIFTLTLIENTKKYGLRTSTAIKVYKHLVEQCNVYLKGDSCGCKVPVEFSSCDSLVALARSMITSKPACMLDSREMQQISSLITQAFLYSIPCNSSGTACFGRTVTIGIEGQSVNHSSVFPGLLLDVPEMLLPGDLERLGDGPFKVVLFGVSLSGDISEVGDVALEVHRGLNPERDLLQQLLKIGEQAVKDKVSLFACQKVVHPVLQHYLREHEVVVIERLGLALMEPFAKITGARAVASLFSLVPMEAYGLVAGLCFQDCGSKKLLQLLSSKHAAISTMVLCHRNETMLEELKMTCQRAEHVLRLTLREPYALLGGGCTETQLATHISHMNQSTAPTTAAALGISHSEFLMAVESFRSSLLAVALSLEHDGQDCLIDLTYGHRWVMDISSQTEVKHTCGCGLLEDRSNLEKTHLNTACQTFSPVFLENSDTQPKVLDSFSAKLNALNVAVEMASLVLDVKYIIKDVN
Protein: Retrotransposon hot spot (RHS) protein, putative (Q584M6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRANSPAAPQGNNENQQVAGNIEGPMRRPRDENVPPPAAAAAAAAQPPQIRQRTEERPNWTMDSKVRNVLLEDALLQRYEVLRNMKLHDLLNQYFSNTYNTENVAMFLFVKNPRRYIVDAEILEDIQGTDEFKTVKTAIDLSEKVEYLDEKEIYYLSQWEEKGTVEIREFVGPMARGRLDGALAAAKRAEKRAVLAAGGAVELKGLYDSIYNAKWSYVMSGYRREPLGMKVFDGRPQSIWTEAEVDITPDPTNVDAEIEERPDGLEIFVLTSEEGWPYNRFKTSDTERCEEIYKHVYIRREIMRVWYIIQRGLQTWWVERTARITPRHIVIGTPGIGKSYGVGSFLLYSLLHFHDGMFNVIAYFVGKIAYLIYNKKPGEEGRVERYKVPEDAVDAIAALVFEKKRGHIIVDIGNELLIPPGELRHLDWGITVLTSPDTAHYEEWEKDTGSRHIIINCDDVRDMKAFVAWKNLSVALGEKVSNTAKQELRGRLKDEWETVKQRIAVAGPVPRAVYDAVGHGVRMEAMAKKIRGLDANDKSGYEDLFRSSVNWQTEKVSHKLVQIVRARGNGVSGDSYRCKELSGHIRILLLWALLGITARKTAESQLMMGNRSAASISFESHALFAIVNPQVLEVMAKNLRHLRPPEKLRGKQSILSSMTPQQLCLTGSEFLPTAGQQPIEKCEYMVLYTPSTANEPVVDGFFFVEGRFTMSPGRQAKKAPKPKTIVLLQITKLDRHPTTTAKVKKFRENIASYFSDWNTFSGNMAWEMIYINSVDGAVITNWQKCEANDDEVIPARQAEQLQTFWETIEQFQVTLRDEMNAQLMIAFQKAEKAQGR
Protein: Protein transport protein Sec61 subunit alpha isoform 1 (Sec61 alpha-1) (P61620)
Organism: Mus musculus (Mouse)
Function: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides. May cooperate with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post-translational transport of small presecretory proteins. The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex. The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER. Controls the passive efflux of calcium ions from the ER lumen to the cytosol through SEC61 channel, contributing to the maintenance of cellular calcium homeostasis (By similarity). Plays a critical role in nephrogenesis, specifically at pronephros stage.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61619}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes exclusively in granular structures in the endoplasmic reticulum (ER). {ECO:0000250|UniProtKB:P61619}.
Interaction partners:
- Translocation protein SEC63 homolog
- Protein transport protein Sec61 subunit gamma
- Protein transport protein Sec61 subunit beta
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS3
Sequence:
MAIKFLEVIKPFCVILPEIQKPERKIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSADPFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFGMIITIGQSIVYVMTGMYGDPSEMGAGICLLITIQLFVAGLIVLLLDELLQKGYGLGSGISLFIATNICETIVWKAFSPTTVNTGRGMEFEGAIIALFHLLATRTDKVRALREAFYRQNLPNLMNLIATIFVFAVVIYFQGFRVDLPIKSARYRGQYNTYPIKLFYTSNIPIILQSALVSNLYVISQMLSARFSGNLLVSLLGTWSDTSSGGPARAYPVGGLCYYLSPPESFGSVLEDPVHAVVYIVFMLGSCAFFSKTWIEVSGSSAKDVAKQLKEQQMVMRGHRETSMVHELNRYIPTAAAFGGLCIGALSVLADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF
Protein: Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53) (P62141)
Organism: Mus musculus (Mouse)
Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62140}. Note=Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. {ECO:0000250|UniProtKB:P62140}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 12A
- Protein phosphatase 1 regulatory subunit 12B
- Protein phosphatase 1 regulatory subunit 12C
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Eukaryotic translation initiation factor 2 subunit 1
- WD repeat-containing protein 82
- Retinoblastoma-associated protein
- Protein phosphatase 1 regulatory subunit 7
- Protein phosphatase 1 regulatory subunit 14A
Sequence:
MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR
Protein: 15-cis-phytoene synthase (EC 2.5.1.32) (F4KGX7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSSVAVLWVATSSLNPDPMNNCGLVRVLESSRLFSPCQNQRLNKGKKKQIPTWSSSFVRNRSRRIGVVSSSLVASPSGEIALSSEEKVYNVVLKQAALVNKQLRSSSYDLDVKKPQDVVLPGSLSLLGEAYDRCGEVCAEYAKTFYLGTLLMTPERRKAIWAIYVMLKVDFYKQSIVALVWCRRTDELVDGPNASHITPMALDRWEARLEDLFRGRPFDMLDAALADTVARYPVDIQPFRDMIEGMRMDLKKSRYQNFDDLYLYCYYVAGTVGLMSVPVMGIDPKSKATTESVYNAALALGIANQLTNILRDVGEDARRGRVYLPQDELAQAGLSDEDIFAGKVTDKWRNFMKMQLKRARMFFDEAEKGVTELSAASRWPVWASLLLYRRILDEIEANDYNNFTKRAYVGKVKKIAALPLAYAKSVLKTSSSRLSI
Protein: Carlactonoate CLA methyltransferase (CLA methyltransferase) (EC 2.1.1.-) (O23234)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F22F7.17 protein
- Cytochrome P450 711A1
Sequence:
MDKKDMEREFYMTGGDGKTSYARNSSLQKKASDTAKHITLETLQQLYKETRPKSLGIADLGCSSGPNTLSTITDFIKTVQVAHHREIPIQPLPEFSIFLNDLPGNDFNFIFKSLPDFHIELKRDNNNGDCPSVFIAAYPGSFYGRLFPENTIHFVYASHSLHWLSKVPTALYDEQGKSINKGCVSICSLSSEAVSKAYCSQFKEDFSIFLRCRSKEMVSAGRMVLIILGREGPDHVDRGNSFFWELLSRSIADLVAQGETEEEKLDSYDMHFYAPSADEIEGEVDKEGSFELERLEMLEVKKDKGNTEGDISYGKAVAKTVRAVQESMLVQHFGEKILDKLFDTYCRMVDDELAKEDIRPITFVVVLRKKL
Protein: Deoxyribonuclease-2-alpha (EC 3.1.22.1) (Acid DNase) (Deoxyribonuclease II alpha) (DNase II alpha) (Lysosomal DNase II) (P56542)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the clearance of nucleic acids generated through apoptosis, hence preventing autoinflammation. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver and bone marrow, where it degrades nuclear DNA expelled from erythroid precursor cells.
Subcellular location: Lysosome.
Interaction partners:
- Deoxyribonuclease-2-beta
- Deoxyribonuclease-1-like 2
- Deoxyribonuclease gamma
- Deoxyribonuclease-1
Sequence:
MATLRSLLLAALLWVPAEALSCYGDSGQPVDWFVVYKLPAHSGSRDTPKGLTYKYMDQNSDGWQDGVGYINSSEGAVGRSLQPLYRKNSSQLAFLLYNDQPPKSSSARDSTGHGHTKGVLLLDQEGGFWLVHSVPRFPPPASSGAYTWPPNAQTFGQTLLCVSLPFTQFARIGKQLTYTYPLVYDHKLEGFFAQKLPDLETVIKNQHVLHEPWNSSVILTSQAGATFQSFAKFGKFGDDLYSGWLAEALGTNLQVQFWQNSPGILPSNCSGAYQVLDVTQTGFPGPSRLTFSATEDHSKWCVAPQGPWACVGDMNRNKAETHRGGGTVCTQLPSFWKAFQSLVKDWKPCIEGS
Protein: Transcriptional regulatory protein ASH1 (Q5A5Q6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the RPD3C(L) histone deacetylase complex (HDAC). Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Controls filamentous growth and required for full virulence in a mouse model of disseminated candidiasis.
Subcellular location: Nucleus {ECO:0000269|PubMed:12073088, ECO:0000269|PubMed:12446785, ECO:0000269|PubMed:19779551}. Note=Preferentially accumulates in daughter cell nuclei of budding-yeast form to the hyphal tip cells in growing filaments.
Interaction partners:
- SWI5-dependent HO expression protein 3
Sequence:
MSLVQSAMFNHHMGPSHTRSRSFELFQEAKTLRVAACKRSYSDDLNISTKRARTAPPSPPYETATPTRASRLVISNLVKPTSNLRSRSLSPNKKFSSPLSPSSSPIATVTSPISSPQNIKIKLPSISDALNLPPITSKEPVKLKPIVPTVSLDYFDTYKPNDENWRYGLLDKIAKESKHFHLNQYNYLNDHAKPSFDSKLSSKIQQSSIANGKKINFPYESNYTYLNKTYLNDVKNYPEYLELAAESLLQLKERQLPPPPLQSHQKQHPPPPPHLPVQGLLPVPAPPVSHFSSSYTTPQAPTFYHPPSQQQQQTPPPQTLHHQQPQPPISTHKFIPISPPSAKKSRSDLLKSPPKHHHHHAPRVCISCGSDQSPCWRPSWSIKQGQLCNSCGLRYKKTKARCLNDKCKKIPAKGEWTLMQSKGKETFEDGIEGYSCIACGWRVEVLPKS
Protein: Mitochondrial import inner membrane translocase subunit TIM18 (Q08749)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. Its role in the complex is unclear but it may be involved in the assembly and stabilization of the TIM22 complex.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:10648604, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:10648604, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Succinate dehydrogenase cytochrome b subunit
- Mitochondrial import inner membrane translocase subunit TIM12
- Mitochondrial import inner membrane translocase subunit TIM22
- Mitochondrial import inner membrane translocase subunit TIM54
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM10
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Mitochondrial inner membrane protein SHH3
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM8
Sequence:
MLLFPGLKPVLNASTVIVNPVRAVFPGLVLSTKRSFYSINRLNAENKINDIANTSKEASSSVQMFKPPEFSQFKDSYQKDYERIAKYTLIPLTMVPFYASFTGGVINPLLDASLSSIFLIYLQYGFTSCIIDYIPKEKYPRWHKLALYCLYGGSMLSLYGIYELETKNNGFVDLVKKLWNENDDHLYIFGRN