wanglab/gogpt-training-data huggingface dataset:
Protein: Malate dehydrogenase 2, cytoplasmic (EC 1.1.1.37) (Cytosolic NAD-dependent malate dehydrogenase 2) (cNAD-MDH2) (Cytosolic malate dehydrogenase 2) (Cytosolic MDH2) (P57106)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Fumarate hydratase 1, mitochondrial
- Malate synthase
- Citrate synthase 3, peroxisomal
- Citrate synthase 2, peroxisomal
- NAD-dependent malic enzyme 2, mitochondrial
- Citrate synthase 4, mitochondrial
- Citrate synthase 1, peroxisomal
- Citrate synthase 5, mitochondrial
- NAD-dependent malic enzyme 1, mitochondrial
- Fumarate hydratase 2
Sequence:
MAKEPVRVLVTGAAGQIGYALVPMIARGIMLGADQPVILHMLDIPFAAEALNGVKMELVDAAFPLLKGVVATTDAVEACTGVNVAVMVGGFPRKEGMERKDVMSKNVSIYKSQASALEKHAAPNCKVLVVANPANTNALILKEFAPSIPEKNITCLTRLDHNRALGQVSERLSVPVSDVKNVIIWGNHSSTQYPDVNHATVKTSVGEKPVRELVKNDEWLNGEFISTVQQRGAAIIKARKLSSALSAASSACDHIRDWVVGTPEGTFVSMGVYSDGSYNVPAGLIYSFPVTCRNGEWTIVQGLPIDDASRKKMDLTAEELKEEKDLAYSCLS
Protein: Leucine-rich repeat and IQ domain-containing protein 3 (Leucine-rich repeat-containing protein 44) (A6PVS8)
Organism: Homo sapiens (Human)
Interaction partners:
- Transmembrane channel-like protein 7
- Fucose-1-phosphate guanylyltransferase
- Protein FAM227B
Sequence:
MFHGTVTEELTSHEEWSHYNENIREGQKDFVFVKFNGLHLKSMENLQSCISLRVCIFSNNFITDIHPLQSCIKLIKLDLHGNQIKSLPNTKFWNGLKNLKLLYLHDNGFAKLKNICVLSACPTLIALTMFDCPVSLKKGYRHVLVNSIWPLKALDHHVISDEEIIQNWHLPERFKACNHRLFFNFCPALRKGTTYEEEINNIKHITSKINAILAHNSPVLIVQRWIRGFLVRKNLSPVFFHKKKQQEKIIRGYEAKWIYITKGYEDKLLKDLFFKPETNIKGKLAYWKHNIYYPVDLKNSSEHRKHVSSILCELKPKDLGMKSKTSRHLIQKGQESEDEIVDEKLDTSFRISVFKLPIYTSGSLKNNAVLREKKQHFFPAYPQPIYTTHPKPIIKKDIRLERSMKEFFAPQRAGMKLRTFSDIDKYYTEQKKQEYHKEKVRVVAMAQVARERVRVAVNEHLNQKKYATQKLIEENKETIQNSLRQVWQNRFNYLEKARERKALFLKEKSQKASERLLVQNLNNERTLLTRGLLKIDRLEKNEAVLKEKSLIVKQKLKAEKYRKNLLKEMKKVRSQEIYKRHCEEKFVMDMIAFEKACERLQDAKTKVAIVKTNLDFKVPNGLIK
Protein: Aspergillopepsin-1 (EC 3.4.23.18) (Acid protease A2) (Aspartic protease pepA) (Aspergillopepsin I) (Aspergillopepsin O) (PEPO) (Aspergillopeptidase A) (PEPA) (Q06902)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A. Hydrolyzes bovine chymotrysinogen A between positions 'Arg-15' and 'Ile-16'.
Subcellular location: Secreted {ECO:0000269|PubMed:8138}.
Interaction partners:
- Alkaline protease 1
Sequence:
MVILSKVAAVAVGLSTVASALPTGPSHSPHARRGFTINQITRQTARVGPKTASFPAIYSRALAKYGGTVPAHLKSAVASGHGTVVTSPEPNDIEYLTPVNIGGTTLNLDFDTGSADLWVFSEELPKSEQTGHDVYKPSGNASKIAGASWDISYGDGSSASGDVYQDTVTVGGVTAQGQAVEAASKISDQFVQDKNNDGLLGLAFSSINTVKPKPQTTFFDTVKDQLDAPLFAVTLKYHAPGSYDFGFIDKSKFTGELAYADVDDSQGFWQFTADGYSVGKGDAQKAPITGIADTGTTLVMLDDEIVDAYYKQVQGAKNDASAGGYVFPCETELPEFTVVIGSYNAVIPGKHINYAPLQEGSSTCVGGIQSNSGLGLSILGDVFLKSQYVVFDSQGPRLGFAAQA
Protein: C3H1-type domain-containing protein (Q57Y78)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFLPEQSNIPGSVTYVSRAAGIPSSSTTQQYQGGECMGVPSELDAIDGGCAWRTASKGVCASQLPRGGSVAVSVSAPFIHLTDWGDATVSTREISDNAAEVPAARSIGNREGVDGSLTSSVFPSGDVNSTIDLPISLVNSALPNQEKNNMEFQDDCLAHVFSRPESPFKDFSAESEDPFTIMQTRSVTCNPNIWEVEGKDVQSSLIHDAVKVGMSQITPSLFSPITEAMESAIDKVKVAPDGLNDCRTVGPQQPTEEQRIPVVDPQRSKLHVPLSSIIPTKALGGRVSFPSLCLLFQSGRCLRGASCYQMHIDPQVVQRLRQINESLPYCCAFHGECNANKWDAEANAHRTILIKGAAVPLSRVAYTNGLERFVLKNNASRSLNTCAVCRLHGKPGGCRYGADCWYVHICRDVLKELVATIKLDLEDPGSEDQCKVPTKTESTGNRVVSGDLLGALSQQQNRRKQQNYPTVAFHPSKSPTMSHLHKGRSIVSSERDGTHSGKLSSHGSASTNTFSARASPTVGQITSDGTTCRNVLVQQRPPVYEDGPLGETRHGLATTMRLHGVAFPVTDPSEEKSVPSPSQFSLNDRQSVTPISGREVSTPSVPCCAMYFPQKQSSVAPCPQPMQNGHTVWPSTVLVPSTTVMYPMISATGLPVASAQQQMGTDGQTYGPFCFVSGREDGFRNLCLPMYGSGKGNMPSQVPLHVPF
Protein: diguanylate cyclase (EC 2.7.7.65) (Q9I4M8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- EAL domain-containing protein
- Cyclic di-GMP phosphodiesterase RocR
- Cyclic di-GMP phosphodiesterase PA4781
- cyclic-guanylate-specific phosphodiesterase
- cyclic-guanylate-specific phosphodiesterase
- Cyclic di-GMP phosphodiesterase PA2567
- cyclic-guanylate-specific phosphodiesterase
- GGDEF domain-containing protein
Sequence:
MARTTLESIQHAIEVNSSLALPIALENLSRLTHLALLTVPFNLIHILVFSLKDFRPDLGHQLWRQEIMYAHGAMALLFGGIGLLALWLRRQPPKLWRMRLLILLGGAGIIGFGVAIACIDQRITSNITPLLLACFACAMFILIRPAYAVPFYGLAMLAFEVAMDHAQADPQLRLSNQANGLTAFGLGLLLSLILWHGHVRNLRQQRKLELQRQELEEKNRQLEYLAGHDPLTGLFNRREFDQLVLMELARIARQPQPLSLLMVDLDHFKYINDRYGHPFGDEVIRHAANLLRGNTRSSDSVARLGGEEFLLLLPDTAEQQARSLAEKLRERLEGTPLATQDGVLCLTASFGVASLDGGGQASYEQLYSAADQALYRAKSSGRNRVEVIRLASLAESLR
Protein: GM14014p (Spoonbill, isoform A) (Spoonbill, isoform D) (Spoonbill, isoform E) (Q9W4C4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSGRPLLYLSLPGVAFILGVFWFRRRYKNCLDKPDDEDSSAINDSSIEPTVQARKANGVLQNGKLPQQSASKSMNINGTLVNGSGSGSGSSSDEKDSPTTMLYGKSAPIKIQSNGRTSNGKHQQQIDSEILKSKIQDAEHKTLCSIDEDFENLSSPRDLPDSVNTRVSFYNRKATQKTVEPVVIKATRTPKISPENSFLDTNYTNKECEQNNNCEPKEEPSKKEADQEELEQDQEQTVLKEEVVDSNGNQKRNVDAASPSLSICSVQSGDSGKGSSLPRSEATRVKTTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQRLPAKRYPNFTMQRIHFALPQTIVPLSTESLYNLQLKLIEGINNDVVVSAVLSGSHIFIQHPLHPSHPSLPLLQKQLYDSYSTMEAPLLPSLELSAVCVIPINDVWYRVQIVDTDPEDEERCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEPIGGTWSIEAAEILNKLTKGIVLQAQVAGYNSHNLPEIFLFASLGPNNVIFINKELVGRKLAKWVEMSD
Protein: Selenocysteine-specific elongation factor (EC 3.6.5.-) (Elongation factor sec) (Eukaryotic elongation factor, selenocysteine-tRNA-specific) (mSelB) (Q9JHW4)
Organism: Mus musculus (Mouse)
Function: Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Selenocysteine insertion sequence-binding protein 2
- Ubiquitin-like protein FUBI
- O-phosphoseryl-tRNA
- L-seryl-tRNA
- Eukaryotic translation initiation factor 2 subunit 2
- tRNA selenocysteine 1-associated protein 1
- Eukaryotic translation initiation factor 2 subunit 1
- Selenide, water dikinase 1
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS6
Sequence:
MAGRRVNVNVGVLGHIDSGKTALARALSTTASTAAFDKQPQSRERGITLDLGFSCFVVPLPGAEPGSSDTLLQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLAEGKRQAAIDKMTKKMQKTLENTKFRGAPIIPVAAKPGGPEAPETEAPQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCAPESLHTVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRTLFFSPAPDSFDLEPVLDSFDLSREYLFQEQYLCKDSMPTATEGDDEADPKAGHAPGGHCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGVLLQGLEDKNYIESFLPALRVYKLKHKHGLVERVMDDYSVIGRSLFKKETNIQLFVGLKVQLSTGEQGIIDSAFGQSGKFKIHIPGGLSPESKKILTPTLKKRSRAGRGETTKPEEGTERPEPIQPVTLNLSFKRYVFDTQKRMVQTP
Protein: Fascin (A0A384MEG1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR005682}.
Interaction partners:
Sequence:
MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVARPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTATGGVQSTASSKNASCYFDIEWRDRRITLRASNGKFVTSKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVAIKVGGRYLKGDHAGVLKASAETVDPASLWEY
Protein: Large ribosomal subunit protein uL16m (54S ribosomal protein L16, mitochondrial) (YmL47) (P38064)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein mL40
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL5m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL36m
Sequence:
MFPYLTRMNLSIKMGGLTLKESSPNAFLNNTTIARRFKHEYAPRFKIVQKKQKGRVPVRTGGSIKGSTLQFGKYGLRLKSEGIRISAQQLKEADNAIMRYVRPLNNGHLWRRLCTNVAVCIKGNETRMGKGKGGFDHWMVRVPTGKILFEINGDDLHEKVAREAFRKAGTKLPGVYEFVSLDSLVRVGLHSFKNPKDDPVKNFYDENAKKPSKKYLNILKSQEPQYKLFRGR
Protein: Zinc/iron permease (Q556U8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSLVPPNFLTLNVCQDAFNNLFSLYFSEHDHDHEEDGGGGHEGHIHAGVSCEEDPDKQYSRPIHIAAIFIILACSIFGTVIPIVATHVKKLRIPRYAIIVGKSIGIGVVLSCALIHMLLPAVVALGSDCLPDSWHEGYEAYPYLFALLAGIVMQFIDFTVLQYLTHKEQKKSMSLDSSTKTDNSLKEVHTTGNVENCHGSHVHGGLLMDPAALKTIEAYLLEFGITVHSVFIGLAVGVVDDKILKALLVALAFHQFFEGVALGSRIADAKLTSHWHEALLTAIFSFSAPVGIAIGVGVASTLNVNGATYLIVQGVFDSVCAGILLYIGFSLMIKDFPEDMEQLCKGKKFEYLLRAGLFIGLWLGAAMMAFIGKYL
Protein: FAD synthetase 2, chloroplastic (EC 2.7.7.2) (AtRibF2) (FAD pyrophosphorylase 2) (FMN adenylyltransferase 2) (Flavin adenine dinucleotide synthase 2) (Q8VZR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18713732}.
Interaction partners:
- Bifunctional riboflavin kinase/FMN phosphatase
- Nudix hydrolase 23, chloroplastic
- FAD synthetase 1, chloroplastic
- Flavin mononucleotide hydrolase 1, chloroplatic
- Purple acid phosphatase 4
- Purple acid phosphatase 7
- Purple acid phosphatase 8
- Purple acid phosphatase 3
- Alkaline-phosphatase-like family protein
- Purple acid phosphatase 17
Sequence:
MLCGGSRVLQHLSDHNHHNSIGLGLGFCGAKIVQLSSFFLRPSQAMAKSHHFSRKLRQRMISSFGSHCRTSGEVPILHNCFSQREDDPELPVEGLSPVSGGIVALGKFDALHIGHRELTIQASRIGAPYLLSFVGMAEVLGWEPRAPIVAKCDRQRVLTSWASYCGDRAPEEYEIEFASVRHLTPRQFVEKLSKELRVCGVVAGENYRFGYKASGDASELVRLCEECGITACIINSVMDMKQGSAKRDSGDSKDRGQVSSTRVRQALAAGDMRYVSELLGRAHRLILRVRTQDMPSERMISVPRSSILNLPPGIGIYKACLLLVGDESSVPCTVVVDTSNIHVETEEVRLCNLDWSQEFRLVSVEFG
Protein: Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial (EC 1.14.13.-) (2-methoxy-6-polyprenolphenol 4-hydroxylase) (EC 1.14.15.-) (Q9Y7Z9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:24911838}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03193}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03193}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Ubiquinone biosynthesis protein coq4, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Atypical kinase COQ8, mitochondrial
- Ubiquinone biosynthesis protein coq9
- Ubiquinone biosynthesis protein coq11
- Thiol-specific monooxygenase
- Decaprenyl-diphosphate synthase subunit 2
Sequence:
MSSLVLRGVSRVEMPTISPTLGIYTRKFASQKILQRQFDVVIVGSGPVGLALAAGLQSNPVTQSLKVGLLDIQDTMKLKDWKFETYSNRCSSLTNHTRMFFDKIGAWDFARKDRIQPFQHILASDGLTNSSIHLDQKPGSEPMAFMSENVNLQYALLNSIIDKMNNNIKKPNLEFLMPCTITKLSKGENIYRTHIHTTTHGELTTKLLIGADGRNSIVRKYANISMPGWNYLTHAVVGTLKIDPLKGPAVAFQRFLPTGPLAYLPLPDNNATFVWSTRPHIASKLLRLPEETFVKFLNASFRLDYPDLSYLYQMDFSEPSKVNEQLDWRLQVKRNSNMQVPPVITEIVSGSRAAFPLRLAHVDEYVKEGIALCGDAAHNTHPLAGQGLNTGIQDVESLISALSFAIKHGQDIGSVFSLQPYFRDRYFKNHVYLGVVDKFHKLYAMENPVVTSVRTLGLSLFDRSASLKNFILSTVANGI
Protein: Cytosolic carboxypeptidase 3 (EC 3.4.17.-) (ATP/GTP-binding protein-like 3) (Protein deglutamylase CCP3) (Q8NEM8)
Organism: Homo sapiens (Human)
Function: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK. May catalyze the hydrolysis of aspartate from the carboxy-terminus of target proteins. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of target proteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CDP0}.
Interaction partners:
- Complement C3
- Membrane cofactor protein
Sequence:
MSEDSEKEDYSDRTISDEDESDEDMFMKFVSEDLHRCALLTADSFGDPFFPRTTQILLEYQLGRWVPRLREPRDLYGVSSSGPLSPTRWPYHCEVIDEKVQHIDWTPSCPEPVYIPTGLETEPLYPDSKEATVVYLAEDAYKEPCFVYSRVGGNRTPLKQPVDYRDNTLMFEARFESGNLQKVVKVAEYEYQLTVRPDLFTNKHTQWYYFQVTNMRAGIVYRFTIVNFTKPASLYSRGMRPLFYSEKEAKAHHIGWQRIGDQIKYYRNNPGQDGRHYFSLTWTFQFPHNKDTCYFAHCYPYTYTNLQEYLSGINNDPVRSKFCKIRVLCHTLARNMVYILTITTPLKNSDSRKRKAVILTARVHPGETNSSWIMKGFLDYILGNSSDAQLLRDTFVFKVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMVHRLMEKREVILYCDLHGHSRKENIFMYGCDGSDRSKTLYLQQRIFPLMLSKNCPDKFSFSACKFNVQKSKEGTGRVVMWKMGIRNSFTMEATFCGSTLGNKRGTHFSTKDLESMGYHFCDSLLDYCDPDRTKYYRCLKELEEMERHITLEKVFEDSDTPVIDITLDVESSSRGSDSSESIDSLTYLLKLTSQKKHLKTKKERNSTIASHQNARGQEVYDRGHLLQRHTQSNSDVKDTRPNEPDDYMVDYFRRQLPNQGLAHCKLRLPGSRHSPASASRVAGTTGTRHHTWLIFVFLVEMGKKIPLKGTDLYGNCFKVTSLQSPMGKQTSTWTEKTRIPTEDLHHNLKSKIKECISFQSKKTGINWTDDEKRSYKDKGIVQTQEILQYLLPIVHSTKNMQTTQIKQLFNPRTNFQIQHQLNPATCRNIKKYSTSWTAPRNHPFVIQGDVMANSSEWVQSKPHRSLESLSPLKGPKKNKHSQIWAIKNEDIKPLSSKWETASSSFGMDANVLKYKSLQAEETNQQSSKHTALHLTKNKDEQANKNDGQPTLYLKFQRES
Protein: ATP-dependent DNA helicase Q5 (EC 5.6.2.4) (DNA 3'-5' helicase RecQ5) (DNA helicase, RecQ-like type 5) (RecQ5) (RecQ protein-like 5) (O94762)
Organism: Homo sapiens (Human)
Function: DNA helicase that plays an important role in DNA replication, transcription and repair. Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability. Associates also with POLR1A and enforces the stability of ribosomal DNA arrays. Plays an important role in mitotic chromosome separation after cross-over events and cell cycle progress. Mechanistically, removes RAD51 filaments protecting stalled replication forks at common fragile sites and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination.
Subcellular location: [Isoform Beta]: Nucleus, nucleoplasm {ECO:0000269|PubMed:10710432, ECO:0000269|PubMed:23180761, ECO:0000269|PubMed:23715498}. Nucleus {ECO:0000269|PubMed:23180761}. Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks. Re-localizes from the nucleolus into the nucleus after replicative stress and significantly associates with WRN during S-phase (PubMed:23180761). {ECO:0000269|PubMed:20643585, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22973052, ECO:0000269|PubMed:23180761, ECO:0000269|PubMed:23715498}.; SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm {ECO:0000269|PubMed:10710432}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm {ECO:0000269|PubMed:10710432}.
Interaction partners:
- Fanconi anemia group M protein
- DNA repair protein RAD51 homolog 1
- DNA topoisomerase 3-alpha
- F-box DNA helicase 1
- Regulation of nuclear pre-mRNA domain-containing protein 1B
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB4
- Structure-specific endonuclease subunit MUS81
- DNA-directed RNA polymerase II subunit RPB1
- DNA replication ATP-dependent helicase/nuclease DNA2
Sequence:
MSSHHTTFPFDPERRVRSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCFRANLFYDVQFKELISDPYGNLKDFCLKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKASDKATIMAFDALVTFCEELGCRHAAIAKYFGDALPACAKGCDHCQNPTAVRRRLEALERSSSWSKTCIGPSQGNGFDPELYEGGRKGYGDFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMQLRKGKDPKIEEFVPPDENCPLKEASSRRIPRLTVKAREHCLRLLEEALSSNRQSTRTADEADLRAKAVELEHETFRNAKVANLYKASVLKKVADIHRASKDGQPYDMGGSAKSCSAQAEPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSIARFFCRRVESPALLASAPEAEGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPSTCPPRDQGTPEVQPTPAKDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTAQDPFQLSAPGVSLKEAANVVVKCLTPFYKEGKFASKELFKGFARHLSHLLTQKTSPGRSVKEEAQNLIRHFFHGRARCESEADWHGLCGPQR
Protein: Heme oxygenase PigA (EC 1.14.99.58) (G3XCZ8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in heme degradation. Catalyzes the degradation of heme to biliverdin, with the release of iron. Forms biliverdin delta (70%) and beta (30%).
Interaction partners:
- Heme uptake outer membrane receptor HasR
- Heme/hemoglobin uptake outer membrane receptor PhuR
- Bacterioferritin BfrB
- Bacterial ferritin
- Bacteriophytochrome
- ferroxidase
- Ferrochelatase
- Protoheme IX farnesyltransferase 2
- Protoheme IX farnesyltransferase 1
- Heme oxygenase, BphO
Sequence:
MDTLAPESTRQNLRSQRLNLLTNEPHQRLESLVKSKEPFASRDNFARFVAAQYLFQHDLEPLYRNEALARLFPGLASRARDDAARADLADLGHPVPEGDQSVREADLSLAEALGWLFVSEGSKLGAAFLFKKAAALELDENFGARHLAEPEGGRAQGWKSFVAILDGIELNEEEERLAAKGASDAFNRFGDLLERTFA
Protein: Cytokine receptor-like factor 1 (Cytokine receptor-like molecule 3) (CRLM-3) (Cytokine-like factor 1) (CLF-1) (Novel cytokine receptor 6) (NR6) (Q9JM58)
Organism: Mus musculus (Mouse)
Function: In complex with CLCF1, forms a heterodimeric neurotropic cytokine that plays a crucial role during neuronal development (By similarity). Plays a role in the initiation and/or maintenance of suckling in neonatal mice. May also play a regulatory role in the immune system (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Cardiotrophin-like cytokine factor 1
- Interleukin-27 subunit alpha
- Ciliary neurotrophic factor receptor subunit alpha
- Leukemia inhibitory factor receptor
- Ciliary neurotrophic factor
Sequence:
MPAGRPGPVAQSARRPPRPLSSLWSPLLLCVLGVPRGGSGAHTAVISPQDPTLLIGSSLQATCSIHGDTPGATAEGLYWTLNGRRLPSELSRLLNTSTLALALANLNGSRQQSGDNLVCHARDGSILAGSCLYVGLPPEKPFNISCWSRNMKDLTCRWTPGAHGETFLHTNYSLKYKLRWYGQDNTCEEYHTVGPHSCHIPKDLALFTPYEIWVEATNRLGSARSDVLTLDVLDVVTTDPPPDVHVSRVGGLEDQLSVRWVSPPALKDFLFQAKYQIRYRVEDSVDWKVVDDVSNQTSCRLAGLKPGTVYFVQVRCNPFGIYGSKKAGIWSEWSHPTAASTPRSERPGPGGGVCEPRGGEPSSGPVRRELKQFLGWLKKHAYCSNLSFRLYDQWRAWMQKSHKTRNQDEGILPSGRRGAARGPAG
Protein: Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (S4S3R8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTREVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP
Protein: Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (Ca(2+)-inhibitable adenylyl cyclase) (P30803)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1618857, ECO:0000269|PubMed:8428899}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:P84309}.
Interaction partners:
- Adenylate cyclase type 2
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 4
- G protein subunit alpha L.
- Adenylate cyclase type 7
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
Sequence:
MSGPRSASPPGCAATRGGPEHRAAWGEAEARANGHPHAAGGATRGCSKKPGGAVTPQLQQQQQQQQHEQQHEQQQHEQQQHVQQQQRLAKRWRGDDDPPLGGDDPLAGGFGFSFRSRSAWQERGGDDCGRGSRRRRRGAAGGGSSRAPPAGGGGGPAAAGGAEVRPRSVELGLDERRGRGRAEPEPEAEAGAPGGDRGARDGDGPAGPGACCRALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLRLPHLAVLAAAVGVILVMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRANAQDRFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSVFMLSFYLTCFLLLTLVVFVSVIYSCVKLFPGPLQSLSRKIVRSKTNSTLVGVFTITLVFLSAFVNMFMCNSEDLLGCLADEHNISTSRVNACHVAASAANLSLGDEQGFCGTPWPSCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLVVEVPRVTLFDNADLLVTANAIDFNNNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRVLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS