wanglab/gogpt-training-data huggingface dataset:
Protein: Collagen alpha-1(XIII) chain (Q9R1N9)
Organism: Mus musculus (Mouse)
Function: Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin. At neuromuscular junctions, may play a role in acetylcholine receptor clustering.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9624150}; Single-pass type II membrane protein {ECO:0000269|PubMed:9624150}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q5TAT6}.
Interaction partners:
Sequence:
MVAERTRKAAASGSRGPGELGAPGPGTVALAEQCARLPSPGCCGLLALALCSLALSLLAHFRTAELQARVLRLEAERGEQQMEKAILGRVNQLLDEKWKFYSRRRREAPKMSPGCNCPPGPPGPTGRPGLPGDKGAIGMPGRVGIKGQPGEKGAPGDAGMSIVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEYPHREYPGGMLAALRSNPIMSLKLLPLLNSVRLAPPPVIKRRTFQGEQSQTGIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGVPGIAVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAIGGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKGEMVDYNGSINEALQEIRTLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAGPQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPCPLGEDGLPVQGCWNK
Protein: Trimethylguanosine synthase (EC 2.1.1.-) (Cap-specific guanine-N(2) methyltransferase) (snRNA/snoRNA cap hypermethylase) (Q09814)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the two serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Required for pre-mRNA splicing, pre-rRNA processing and small ribosomal subunit synthesis. Involved in nucleolar structural organization.
Subcellular location: Nucleus, Cajal body {ECO:0000269|PubMed:38828770}.
Interaction partners:
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D2
- Large ribosomal subunit protein bL36m
- Ribonucleases P/MRP protein subunit pop1
- UPF0587 protein C2D10.03c
- Probable RNA methyltransferase C2A9.10
- Uncharacterized protein C18B5.09c
- Small RNA 2'-O-methyltransferase
Sequence:
MNKNEELDEDELLKKCIICPPVPKALKKYWNNRYNLFSRFDEGIWLDYQSWYSVTPEKVAVAIAKSVVDFIQPELIIDAFSGCGGNTIQFAKYCPVISIEIDPIKIAMAKHNLEIYGIPSSRVTFIQGDVLDTFKSLQFAKDYRSLVFMSPPWGGPSYSGKTVYSLNDLNPYAFDVLFKEATRISPYVAAFLPRNTDVKELAAYGSIHNKPYITNFLFEGYAKAICCYFNMKGAIARKI
Protein: Embryonic abundant protein-like (Putative embryonic abundant protein) (S-adenosyl-L-methionine-dependent methyltransferases superfamily protein) (Q9M389)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pentatricopeptide repeat-containing protein At4g19191
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- At1g33030
- Paraxanthine methyltransferase 2
- F9L1.6
- Putative uncharacterized mitochondrial protein AtMg00280
- AT5G12460.1
- Fanconi anemia group E protein FANCE protein
Sequence:
MAALSEKEAEAYLDARPRYPIDWFKKIAARTQDHKFAWDVGTGNGQAAIGLVEHYENVVATDINEAQLQRAIKHSRISYHHTPTTISEDEMVDLLGGENSVDLIVAAQAVHFFDLNVFYNVAKRVLRKEGGLIAVWVYNDIIISHEIDPIMKRLVDSTLPFRTPIMNLAFDGYKTLTFPFETIGMGSEGKPITLDIPHKLSLKGFIGFLRSWQPAMKAKEKGVELINEDLITKFEEAWGDETQVKDVFYKAHMIVGKIPEEKFESDQVLSNKGRLLLETEVGRNQKRPQPSDEGDRQSKKQNTSEDDACKDKPSSVFSTHYRF
Protein: Oleoyl-12-hydroxylase FAH12 (EC 1.14.18.4) (Oleate Delta(12)-hydroxylase) (Oleate hydroxylase FAH12) (RcFAH12) (Phosphatidylcholine 12-monooxygenase) (Q41131)
Organism: Ricinus communis (Castor bean)
Function: Oleate hydroxylase involved in the biosynthesis of ricinoleate. It uses cytochrome b5 as an electron donor. May act on both oleic acid (18:1(9cis)) and eicosenoic acid (20:1(11cis)).
Subcellular location: Microsome membrane {ECO:0000269|PubMed:1417766}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- O-acyltransferase
- Diacylglycerol O-acyltransferase 2
- phospholipid:diacylglycerol acyltransferase
- Phosphatidylcholine: Diacylglycerol Acyltransferase
- phospholipid:diacylglycerol acyltransferase
Sequence:
MGGGGRMSTVITSNNSEKKGGSSHLKRAPHTKPPFTLGDLKRAIPPHCFERSFVRSFSYVAYDVCLSFLFYSIATNFFPYISSPLSYVAWLVYWLFQGCILTGLWVIGHECGHHAFSEYQLADDIVGLIVHSALLVPYFSWKYSHRRHHSNIGSLERDEVFVPKSKSKISWYSKYLNNPPGRVLTLAATLLLGWPLYLAFNVSGRPYDRFACHYDPYGPIFSERERLQIYIADLGIFATTFVLYQATMAKGLAWVMRIYGVPLLIVNCFLVMITYLQHTHPAIPRYGSSEWDWLRGAMVTVDRDYGVLNKVFHNIADTHVAHHLFATVPHYHAMEATKAIKPIMGEYYRYDGTPFYKALWREAKECLFVEPDEGAPTQGVFWYRNKY
Protein: Citrate synthase, peroxisomal (EC 2.3.3.16) (P08679)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Peroxisomal citrate synthase involved in the citrate homeostasis. Catalyzes the condensation of acetyl coenzyme A and oxaloacetate to form citrate. Citrate synthase is the rate-limiting enzyme of the tricarboxylic acid (TCA) cycle (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25982115}. Peroxisome {ECO:0000269|PubMed:2181273, ECO:0000269|PubMed:25982115}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Acetyl-coenzyme A synthetase 1
- Malate synthase 1
- Malate dehydrogenase, peroxisomal
- Acetyl-coenzyme A synthetase 2
- Malate dehydrogenase, cytoplasmic
- Citrate synthase, mitochondrial
- Pyruvate carboxylase 1
- Malate synthase 2
Sequence:
MTVPYLNSNRNVASYLQSNSSQEKTLKERFSEIYPIHAQDVRQFVKEHGKTKISDVLLEQVYGGMRGIPGSVWEGSVLDPEDGIRFRGRTIADIQKDLPKAKGSSQPLPEALFWLLLTGEVPTQAQVENLSADLMSRSELPSHVVQLLDNLPKDLHPMAQFSIAVTALESESKFAKAYAQGISKQDYWSYTFEDSLDLLGKLPVIAAKIYRNVFKDGKMGEVDPNADYAKNLVNLIGSKDEDFVDLMRLYLTIHSDHEGGNVSAHTSHLVGSALSSPYLSLASGLNGLAGPLHGRANQEVLEWLFALKEEVNDDYSKDTIEKYLWDTLNSGRVIPGYGHAVLRKTDPRYMAQRKFAMDHFPDYELFKLVSSIYEVAPGVLTEHGKTKNPWPNVDAHSGVLLQYYGLKESSFYTVLFGVSRAFGILAQLITDRAIGASIERPKSYSTEKYKELVKNIESKL
Protein: DNA (cytosine-5)-methyltransferase DRM2 (EC 2.1.1.37) (Protein DOMAINS REARRANGED METHYLASE 2) (Q9M548)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in de novo DNA methylation. Controls asymmetric and CpNpG methylation. Required for FWA gene silencing but not for the maintenance of SUP gene silencing. Functionally redundant to CMT3 to maintain non-CpG methylation. Involved in RNA-directed DNA methylation (RdDM). Acts as major DNA methyltransferase in the RdDM pathway, and is essential for RNA-directed de novo DNA methylation of cytosines in all sequence contexts. Associates with long non-coding RNA (lncRNA) produced by RNA polymerase V (Pol V). This association is dependent on AGO4 and IDN2, and results in DNA methylation of RdDM target loci.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:20410883}. Note=Peri-nucleolar.
Interaction partners:
- DNA
- Protein argonaute 4
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4
- Protein RDM1
- DNA
- DNA
- Protein DEFECTIVE IN MERISTEM SILENCING 3
- Endoribonuclease Dicer homolog 3
- RNA-dependent RNA polymerase 2
- DNA-directed RNA polymerase V subunit 1
Sequence:
MVIWNNDDDDFLEIDNFQSSPRSSPIHAMQCRVENLAGVAVTTSSLSSPTETTDLVQMGFSDEVFATLFDMGFPVEMISRAIKETGPNVETSVIIDTISKYSSDCEAGSSKSKAIDHFLAMGFDEEKVVKAIQEHGEDNMEAIANALLSCPEAKKLPAAVEEEDGIDWSSSDDDTNYTDMLNSDDEKDPNSNENGSKIRSLVKMGFSELEASLAVERCGENVDIAELTDFLCAAQMAREFSEFYTEHEEQKPRHNIKKRRFESKGEPRSSVDDEPIRLPNPMIGFGVPNEPGLITHRSLPELARGPPFFYYENVALTPKGVWETISRHLFEIPPEFVDSKYFCVAARKRGYIHNLPINNRFQIQPPPKYTIHDAFPLSKRWWPEWDKRTKLNCILTCTGSAQLTNRIRVALEPYNEEPEPPKHVQRYVIDQCKKWNLVWVGKNKAAPLEPDEMESILGFPKNHTRGGGMSRTERFKSLGNSFQVDTVAYHLSVLKPIFPHGINVLSLFTGIGGGEVALHRLQIKMKLVVSVEISKVNRNILKDFWEQTNQTGELIEFSDIQHLTNDTIEGLMEKYGGFDLVIGGSPCNNLAGGNRVSRVGLEGDQSSLFFEYCRILEVVRARMRGS
Protein: RAB10, member RAS oncogene family (Ras-related protein Rab-10 (EC 3.6.5.2)) (Zgc:92757) (Q6DGV5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
- RILP-like protein 2
- RAB3A-interacting protein
- Myosin VB
- Rab GDP dissociation inhibitor
- Rab GDP dissociation inhibitor
- C-myc promoter-binding protein
- DENN/MADD domain-containing 4B.
- DENN domain-containing protein 4C isoform X2
Sequence:
MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNAKSFENISKWLRNIDEHANEDVERMLLGNKCDMEDKRVVPKAKGEQIAKEHGIRFFETSAKANINIEKAFLTLAEDILKKTPVKEPNSENVDISTGGGVTGWKTKCCS
Protein: Formin homology 2 domain containing, isoform G (M9NFP9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIVKMEPDELITFRVQYLVDSDPLSACTAFPIPVRAPTYAFATTMPLANQLGTILRLLNAPQSIDDAAIQVYKDGDYGAYLDLESSLAEQAEEIEGVNVSRKNSLVVRTQLNVRVQAIIEKLLSAQGSDLRRALFSLKQVFQEDKDLVHAFVALGGLNCLVRVGNCADQNYQNYILRALGQVMLYVDGMNGVMKHEPTMQWLYSLIASNYRSVVKTALKLLLVFVEYAESNCYVLVSAIHAVDASQGTLPWSNIMRLLKDYDNADAELVIYATSLINKTLAGLNDQDSFYDESDLLEQQGMETVIQRYMSKPGTDLDLLDQLQLYEAVLKFEDGESDGQRLPQNSMRKTQRYRPGANTTERRKSRRHSTDNSPASLTKVLPTTVLRMTPTQATVDEDSSGSTNSTEFSGGLFNEKKPRDGAGVTPGLRRRRERAERHKSFLKEQQEAAANGIFAALEQREGLDMESEDQQLLLQLKRDHTVKDLTQKLSNLPMSPTQDSANRALVGDMSGLISKAKEGLAKSKSKGEISRSSSVDQDVKKSEPKKSENELHWEELVRNMTRPLNLCDLDFTDLRDDDEKDVLAPRSLGAGIPPPPPPLGGAIAPPPMMPPSLAPPPMYGYGGSLTNSVNSLNGSINGELVNGNNTIKKNKKTVKLFWKEVREDMIPQVVGKTIWDELPDANVDTQKLEHLFESRAKDLMTKKQQELNKSKEIIVLDHKRSNAINIAITKLPPPRAIKTAILKMDATVVTREGIDKLLNMLPTDEERGKIQEAQLSNPELPLGSAEQFLLTLASISELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNGAPVKGFQIEYLAKVPEVKDTVHKHSLLHHLCHMVMESSSDTSDLYSEIGPITRASKADFTDLAHNLNQLEAECKACWDRLKLIAKHDCPPPLKQKLVDFLADCAERIIILQIVHRRVMNRYRKFLLWLGMPQHSVAESRPNEFCRTLSEFALEYRTTRERVQQQLEKKANHRERNKTRGKLIIDMAKFKTKDDVADDELKKLLDTSSADQADGTLTWRRRRAEQLRSPITRQSEEQFTDGDDEILESLVKTATKAPGTRTTPRERKRTRHADRKSLRRTLKNGLTEEEKQHVAALIQTY
Protein: Lectin 9 (MtLec9) (Agglutinin LEC9) (Q2PP74)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi.
Interaction partners:
Sequence:
MALSSALIKIFITFLFLQNHVNSQYSSPSKPQPSLGSTISFSITKFDDESPNIFVKGDASISNGVLSLTKTDKYSGKPLQKSVGRATHLTPIHIWDETSGELADFSTSFSFIVNTNGSRLHGDGFTFFLGPLHFDLPKNSSGGYLGLFNPETALIPSQNPIVAIEFDSFTNGWDPASPSQYPHIGIDVGSIDSRATVNWPLDFVQTNALGEASINYNSESKRLSVFVAYPGSGKNATGVSFVVDLRSVLPEWVRVGFSAATGELVETHDIINWSFEAAL
Protein: Galectin (O45904)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSSTPQFLRWYEQNKPVPYRSVLQEKFEPGQTLIVKGSTIDESQRFTINLHSKTADFSGNDVPLHVSVRFDEGKIVLNSFSNGEWGKEERKSNPIKKGDSFDIRIRAHDDRFQIIVDHKEFKDYEHRLPLSSISHLSIDGDLYLNHVHWGGKYYPVPYESGLANGLPVGKSLLVFGTVEKKAKRFHVNLLRKNGDISFHFNPRFDEKHVIRNSLAANEWGNEEREGKNPFEKGVGFDLVIQNEEYAFQVFVNGERYISFAHRADPHDIAGLQISGDIELSGIQIQ
Protein: Long-chain-fatty acid-CoA ligase protein, putative (EC 6.2.1.3) (Q385W8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Fatty acyl CoA syntetase 1
- non-specific serine/threonine protein kinase
- Monoglyceride lipase, putative
- Monoglyceride lipase, putative
- Lipase-like protein, putative
- Fungal lipase-type domain-containing protein
- Fatty acyl CoA synthetase, putative
- Fatty acyl CoA synthetase 4
- Fatty acyl CoA synthetase 2
- Fatty acyl CoA synthetase 3
Sequence:
MRRLLGLTTLPGRNSFALQVGYRLGTSVAGTFYSESDTAAGASMNNDMRLGIVIKPQSTLVDLWEQAVKAWPMRRFLGAKVWVRGQLGYVWATYESIEQEASVMRTLLNQMGVGKGGRVVVISENRYEWVVVHLASLQLGAQFVVLPTNVTPKEAELVLKSTQARVLFVESTSAYTAVKGWVGEVGQLQHIICFEDQIGEGSYAVAISIASDVPEKTPARKDVTSEDTAMIMFSAGTTGPPKGVMLSHKNLVANVSSIYAHVGEAITHTDMFMSLCSWCVAGALTTELYQAICKGACVCIPPEQLEGFQDLPLVQPSVIVTVAQPFQRAYANIVDNIMNRSTLTKDLTRFTLGRITENRLMMQKPGSILRTASNIFLGKFKAQFGSELRIAFIIGSQLTRDQMELLADLDVFTVSTYGCLEAGGLIATDLDVPLRLKALPGVEIRVVNDKNEIVAPGYVGEVLIEAPHAMQGYFDVHIDPEEAKNSLVAYGGRTFVRTGDYGSMTGGWLTIKGNKDILIRLQNGTVVDPLEVEGTLIKSPFIKQIFVYGEGRPYLCALVVPNAKAIASHLRKVERRDGVPIVSEREKADCIRAELRRVSQGLPTRSHVRRFAFIEELTLANGFITCKYGFARQRVERHYVHYFDAMYDETPLFFGHAVDDYDDLF
Protein: F-box/LRR-repeat protein 17 (F-box and leucine-rich repeat protein 17) (F-box only protein 13) (Q9UF56)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteasome. The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (By similarity). The SCF(FBXL17) complex mediates ubiquitination and degradation of BACH1. The SCF(FBXL17) complex is also involved in the regulation of the hedgehog/smoothened (Hh) signaling pathway by mediating the ubiquitination and degradation of SUFU, allowing the release of GLI1 from SUFU for proper Hh signal transduction. The SCF(FBXL17) complex mediates ubiquitination and degradation of PRMT1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24035498}. Nucleus {ECO:0000269|PubMed:24035498, ECO:0000269|PubMed:27234298}. Note=Present in the cytoplasm and nucleus; more abundant in the cytoplasm. {ECO:0000269|PubMed:24035498}.
Interaction partners:
- Cullin-1
- S-phase kinase-associated protein 1
- Transcription regulator protein BACH1
- Kelch-like ECH-associated protein 1
- E3 ubiquitin-protein ligase RBX1
- Kelch-like protein 12
- Suppressor of fused homolog
Sequence:
MGHLLSKEPRNRPSQKRPRCCSWCRRRRPLLRLPRRTPAKVPPQPAAPRSRDCFFRGPCMLCFIVHSPGAPAPAGPEEEPPLSPPPRDGAYAAASSSQHLARRYAALAAEDCAAAARRFLLSSAAAAAAAAASASSPASCCKELGLAAAAAWEQQGRSLFLASLGPVRFLGPPAAVQLFRGPTPSPAELPTPPEMVCKRKGAGVPACTPCKQPRCGGGGCGGGGGGGGGGGPAGGGASPPRPPDAGCCQAPEQPPQPLCPPPSSPTSEGAPTEAGGDAVRAGGTAPLSAQQQHECGDADCRESPENPCDCHREPPPETPDINQLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWKQLDLSSRQQVTDELLEKIASRSQNIIEINISDCRSMSDNGVCVLAFKCPGLLRYTAYRCKQLSDTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVIAKGCLKLQRIYMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLTKLRNLSSLDLRHITELDNETVMEIVKRCKNLSSLNLCLNWIINDRCVEVIAKEGQNLKELYLVSCKITDYALIAIGRYSMTIETVDVGWCKEITDQGATLIAQSSKSLRYLGLMRCDKVNEVTVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNMSAASS
Protein: BRCA1-A complex subunit Abraxas 1 (Coiled-coil domain-containing protein 98) (Protein FAM175A) (Q6UWZ7)
Organism: Homo sapiens (Human)
Function: Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX.
Subcellular location: Nucleus {ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000305}.
Interaction partners:
- BRCA1-A complex subunit RAP80
- BRCA1-associated RING domain protein 1
- BRISC and BRCA1-A complex member 1
- Breast cancer type 1 susceptibility protein
- BRISC and BRCA1-A complex member 2
- Lys-63-specific deubiquitinase BRCC36
- Mediator of DNA damage checkpoint protein 1
- DNA endonuclease RBBP8
- E3 ubiquitin-protein ligase RNF8
- Double-strand break repair protein MRE11
Sequence:
MEGESTSAVLSGFVLGALAFQHLNTDSDTEGFLLGEVKGEAKNSITDSQMDDVEVVYTIDIQKYIPCYQLFSFYNSSGEVNEQALKKILSNVKKNVVGWYKFRRHSDQIMTFRERLLHKNLQEHFSNQDLVFLLLTPSIITESCSTHRLEHSLYKPQKGLFHRVPLVVANLGMSEQLGYKTVSGSCMSTGFSRAVQTHSSKFFEEDGSLKEVHKINEMYASLQEELKSICKKVEDSEQAVDKLVKDVNRLKREIEKRRGAQIQAAREKNIQKDPQENIFLCQALRTFFPNSEFLHSCVMSLKNRHVSKSSCNYNHHLDVVDNLTLMVEHTDIPEASPASTPQIIKHKALDLDDRWQFKRSRLLDTQDKRSKADTGSSNQDKASKMSSPETDEEIEKMKGFGEYSRSPTF
Protein: Thiol:disulfide interchange protein DsbG (P77202)
Organism: Escherichia coli (strain K12)
Function: Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.
Subcellular location: Periplasm.
Interaction partners:
- Thiol:disulfide interchange protein DsbD
- Disulfide bond formation protein B
- Thiol:disulfide interchange protein DsbE
- Thiol:disulfide interchange protein DsbA
Sequence:
MLKKILLLALLPAIAFAEELPAPVKAIEKQGITIIKTFDAPGGMKGYLGKYQDMGVTIYLTPDGKHAISGYMYNEKGENLSNTLIEKEIYAPAGREMWQRMEQSHWLLDGKKDAPVIVYVFADPFCPYCKQFWQQARPWVDSGKVQLRTLLVGVIKPESPATAAAILASKDPAKTWQQYEASGGKLKLNVPANVSTEQMKVLSDNEKLMDDLGANVTPAIYYMSKENTLQQAVGLPDQKTLNIIMGNK
Protein: Homeobox protein Mix.1 (P21711)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor which plays a regulatory role in the development of the embryo. Involved in the establishment of dorsal/ventral pattern in the early mesoderm. Activates the head organizer gene cer1 by acting synergistically with otx2 and siamois through the 5'-TAATCT-3' element of the cer1 promoter. Also binds as a complex with lhx1/lim1 and siamois to the 3x 5'-TAAT-3' element of the cer1 promoter.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MDGFSQQLEDLYPSCFSPCPSPLGFSEPVIQPFAMNLAPAAQKDFQQHPNRREVTKIPGAGEQSPVQNVRPKDAINPKEADPRSPTADASLVPASQRRKRTFFTQAQLDILEQFFQTNMYPDIHHREELARHIYIPESRIQVWFQNRRAKVRRQGAKATKPILAGHHYSGTSGANRAMFPSAPAPNSSSHQMTTSRAQVQPLKESQMNMFHQNQGFLPYPDSSCNVSRQRFLMSQPTPGAYHLPQASSNVYNQNVKSQNPLWNQQTTNRVYTNMMETVLDLSRRPSQQMPVQPMLMNSFQTNKNIKPEVYTTSPQIPVSTTSSQVSLFANQEPCHMSTTQGGTYGQISPISDSGVSDTSPEPSSDWEENVASVLLNL
Protein: Forkhead box protein N1 (Hepatocyte nuclear factor 3 forkhead homolog 11) (HFH-11) (HNF-3/forkhead homolog 11) (Winged-helix transcription factor nude) (Q61575)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator which regulates the development, differentiation, and function of thymic epithelial cells (TECs) both in the prenatal and postnatal thymus. Acts as a master regulator of the TECs lineage development and is required from the onset of differentiation in progenitor TECs in the developing fetus to the final differentiation steps through which TECs mature to acquire their full functionality. Regulates, either directly or indirectly the expression of a variety of genes that mediate diverse aspects of thymus development and function, including MHC Class II, DLL4, CCL25, CTSL, CD40 and PAX1. Regulates the differentiation of the immature TECs into functional cortical TECs (cTECs) and medullary TECs (mTECs). Essential for maintenance of mTECs population in the postnatal thymus. Involved in the morphogenesis and maintenance of the three-dimensional thymic microstructure which is necessary for a fully functional thymus. Plays an important role in the maintenance of hematopoiesis and particularly T lineage progenitors within the bone marrow niche with age. Essential for the vascularization of the thymus anlage. Promotes the terminal differentiation of epithelial cells in the epidermis and hair follicles, partly by negatively regulating the activity of protein kinase C.
Subcellular location: Nucleus.
Interaction partners:
- Autoimmune regulator
- Homeobox protein Hox-C13
- Proteasome subunit beta type-11
- Chorion-specific transcription factor GCMb
Sequence:
MVSLLPPQSDVTLPGSTRLEGEPQGDLMQAPGLPDSPAPQNKHANFSCSSFVPDGPPERTPSLPPHSPSIASPDPEQIQGHCTAGPGPGSFRLSPSEKYPGFGFEEGPAGSPGRFLKGNHMPFHPYKRHFHEDIFSEAQTAMALDGHSFKTQGALEAFEEIPVDMGDAEAFLPSFPAEAWCNKLPYPSQEHNQILQGSEVKVKPQALDSGPGMYCYQPPLQHMYCSSQPAFHQYSPGGGSYPVPYLGSPHYPYQRIAPQANAEGHQPLFPKPIYSYSILIFMALKNSKTGSLPVSEIYNFMTEHFPYFKTAPDGWKNSVRHNLSLNKCFEKVENKSGSSSRKGCLWALNPSKIDKMQEELQKWKRKDPIAVRKSMAKPEELDSLIGDKREKLGSPLLGCPPPGLAGPGPIRPMAPSAGLSQPLHPMHPAPGPMPGKNPLQDLLGGHAPSCYGQTYPHLSPSLAPSGHQQPLFPQPDGHLELQAQPGTPQDSPLPAHTPPSHGAKLMAEPSSARTMHDTLLPDGDLGTDLDAINPSLTDFDFQGNLWEQLKDDSLALDPLVLVTSSPTSSSMLPPPPAAHCFPPGPCLAETGNEAGELAPPGSGGSGALGDMHLSTLYSAFVELESTPSSAAAGPAVYLSPGSKPLALA
Protein: V-type proton ATPase subunit D (V-type proton ATPase subunit d) (Vacuolar proton pump subunit D) (Q6PJ05)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00029434}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029434}.
Interaction partners:
Sequence:
MSGKDRIEIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAMFTAGDFSTTVIQNVNKAQVKIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVIIPRIERTLAYIITELDEREREEFYRLKKIQEKKKILKEKSEKDLEQRRAAGEVLEPANLLAEEKDEDLLFE
Protein: Anti-mullerian hormone (E3UBG7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRLWCIFGLILLLPSTMVTLPHQGRLSDSLLGRCQEDPTPDHPGTGPGDKSSMEVGKGLGENALTVKETINSHPSAPHLPGDTPCFGRIPSHGEVIEDMLSALREGWGQESNLRKEVLTRFGACSHSDGAPIPALSTLAEEAKKEKHGLHVWHPTKELMESEVEGGGLVLTLHLPRPPLSNIKPVLLLAFRNPRTGALGAVTFTSHSLQPYKQTVCISEGTQFLILTGKQPEGKSKLKWRFNVDTKTPETGQKLSELRGFLIGDGTRNDVSVIPLVLFSTDRGTDERVTEKLSPSPAPSGTYTFLCELQKFLSDVMPPQTQSQPWAASVPLYSLDSLPPLSLGVSSSETLLARLLNSSAPTLFSFPTQGSVLQGHHGELSLQPALLEVLRQRLEEVLVQMRAEEVGKAGMDRLRRLQELSVLPKEGEEAPAGVGSPSETQYRALLLLKALQTVVGAWDVERGQRATRAGQKDPGNQHLCRLHSLTVSLEKYLLSPPEATIYNCQGVCSFPLTNGNNHAILLNSQVQSGLALERSPCCVPVDYEDLKVVELDEHGTNICYKPNMVAKECGCR
Protein: Uncharacterized protein C8D2.11 (O13647)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MGRPLIESSSNDHVANFNRKTKKLIDQALEHYNGRLPEQLENFSFENFVEVLDTESSVVNRVFEVLVREVAGSFRQRKRAHMPRTNTTAQVVQRQLAPSISTVFSRDSNDPLVDDMDQEYIL
Protein: Atypical kinase COQ8B, mitochondrial (EC 2.7.-.-) (AarF domain-containing protein kinase 4) (Coenzyme Q protein 8B) (Q566J8)
Organism: Mus musculus (Mouse)
Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway. Required for podocyte migration.
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:Q96D53}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q96D53}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96D53}. Cell membrane {ECO:0000250|UniProtKB:Q96D53}.
Interaction partners:
- Ubiquinone biosynthesis protein COQ9
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- All trans-polyprenyl-diphosphate synthase PDSS2
- Uncharacterized aarF domain-containing protein kinase 2
Sequence:
MWLELGAMLRRTCGPLGRAVRLPCGGALGPRPHWWGPCRSCLAQSVHQDQPGRGLSEDDIRRAREARLRKAPRPQLSDRSRERKVPASRISRLASFGGLAVGLGLGALAEVTKKSLPGGSLQHEGVSGLGSSPFLSEANAERIVQTLCTVRGAALKIGQMLSIQDNSFISPQLQRIFERVRQSADFMPRWQMMRVLEEELGKDWQDKVASLEEVPFAAASIGQVHQGLLKDGTEVAVKIQYPGVAQSIQSDVENLLALLKMSVGLPEGLFAEQSLQTLQQELAWECDYRREAACAQTFRKLLADDPFFRVPAVVQELCTTRVLGMELAGGIPLDQCQGLSQDIRNQICFQLLRLCLRELFEFRFMQTDPNWANFLYDASSHQVTLLDFGASRAFGTEFTDHYIEVVKAAADGDRDRVLQKSQDLKFLTGFETKAFSDAHVEAVMILGEPFAASGPYDFGAGETARRIQGLIPVLLRHRLRPPPEETYALHRKLAGAFLACARLHAHIACRDLFQDTYHRYWASRQTLPLPAAS