wanglab/gogpt-training-data huggingface dataset:
Protein: Rho-related GTP-binding protein RhoC (Silica-induced gene 61 protein) (SIG-61) (Q62159)
Organism: Mus musculus (Mouse)
Function: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow {ECO:0000250}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. {ECO:0000250}.
Interaction partners:
- Formin-like protein 2
- Protein diaphanous homolog 1
- Rho-associated protein kinase 2
- Rho GDP-dissociation inhibitor 1
- Rho-associated protein kinase 1
- Rho guanine nucleotide exchange factor 11
- Formin-like protein 3
- Serine/threonine-protein kinase N3
- Serine/threonine-protein kinase N1
- Rhotekin
Sequence:
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRQDEHTRRELAKMKQEPVRSEEGRDMANRISAFGYLECSAKTKEGVREVFEMATRAGLQVRKNKRRRGCPIL
Protein: HasR protein (Q79AD2)
Organism: Serratia marcescens
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
Sequence:
MFIHKGTTPAGRLATAVRAALAAMMLTQPAVALAAQAEASSAQAAQQKNFNIAAQPLQSAMLRFAEQAGMQVFFDEVKLDGMQAAALNGSMSVEQGLRRLIGGNPVAFRLQPQGQIVLSRLPTANGDGGALALDSLTVLGAGGNNANDWVYDEPRSVSVISREQMDNRPARHAADILEQTTGAYSSVSQQDPALSVNIRGIQDYGRVNMNIDGMRQNFQKSGHGQRNGTMYIDSELLSGVTIDKGTTGGMGSAGTLGGIATFNTVSASDFLAPGKELGGKLHASTGDNGTHFIGSGILALGNETGDILLAASERHLGDYWPGNKGDIGNIRINNDTGNYDRYAESIKNNKIPDTHYRMHSRLAKVGWNLPANQRLQLSYLQTQTASPIAGTLTNLGTRPPYELGWKRTGYTDVMARNAAFDYSLAPEDVDWLDFQAKLYYVDTQDDSDTYSTSSLLDNGYATRTRLRTYGAQAQNTSRFSLAPGHDFRANYGLEFYYDKATSDSSRQGMEGVTPAGNRSVASLFANLTYDYDGWLTLEGGLRYDRYRLRGQTGLSYPDLAKDGQRYTIDNPCKALRLTGCSTTTREDWDVDRDQGKLSPTLAVAVRPGVEWLELYTTYGKSWRPPAITETLTNGSAHSSSTQYPNPFLQPERSRAWEVGFNVQQPDLWFEGDRLVAKVGYFDTKVDNYINLAIDRNKPGLVQPSIGNAAYVNNLSKTRFRGLEYQLNYDAGVFYADLTYTHMIGKNEFCSNKAWLGGRLRYGDGSRRGNFYVEPDAASNDFVTCDGGTQFGSAAYLPGDRGSVTLGGRAFDRKLDAGVTVRFAPGYQDSSVPSNYPYLADWPKYTLFDLYASYKLTDSLTLRGSVENLTNRAYVVSYGETLANTLGRGRTVQGGVEYRF
Protein: Epoxide hydrolase 1 (EC 3.3.2.9) (Epoxide hydratase) (Microsomal epoxide hydrolase) (mEH) (P07099)
Organism: Homo sapiens (Human)
Function: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water (By similarity). Plays a role in the metabolism of endogenous lipids such as epoxide-containing fatty acids. Metabolizes the abundant endocannabinoid 2-arachidonoylglycerol (2-AG) to free arachidonic acid (AA) and glycerol.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:24958911}; Single-pass type III membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P07687}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:P07687}.
Interaction partners:
- Glutathione S-transferase P
- Glutathione S-transferase Mu 1
- Cytochrome P450 1A1
- Cytochrome P450 2E1
- Glutathione S-transferase A1
- Cytochrome P450 1B1
- Cytochrome P450 2C9
- Cytochrome P450 1A2
- Glutathione S-transferase Mu 3
- Hematopoietic prostaglandin D synthase
Sequence:
MWLEILLTSVLGFAIYWFISRDKEETLPLEDGWWGPGTRSAAREDDSIRPFKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNEFDWKKQVEILNRYPHFKTKIEGLDIHFIHVKPPQLPAGHTPKPLLMVHGWPGSFYEFYKIIPLLTDPKNHGLSDEHVFEVICPSIPGYGFSEASSKKGFNSVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNMALVLSNFSTLTLLLGQRFGRFLGLTERDVELLYPVKEKVFYSLMRESGYMHIQCTKPDTVGSALNDSPVGLAAYILEKFSTWTNTEFRYLEDGGLERKFSLDDLLTNVMLYWTTGTIISSQRFYKENLGQGWMTQKHERMKVYVPTGFSAFPFELLHTPEKWVRFKYPKLISYSYMVRGGHFAAFEEPELLAQDIRKFLSVLERQ
Protein: Temporin-1Tl (TL) (Temporin-L) (P57104)
Organism: Rana temporaria (European common frog)
Function: Amphipathic alpha-helical antimicrobial peptide with potent activity against both Gram-negative and Gram-positive bacteria, and against fungi. Mainly acts by causing perturbation of bilayer integrity of both neutral and negatively charged membranes, probably by forming pore-like openings. Also displays anti-leishmania activity by damaging parasite membrane (By similarity). Shows hemolytic activity. Also shows cytotoxicity against cancer cell lines. Strongly binds to lipopolysaccharides (LPS) and its lipid A portion (Probable). Improves temporin-A and temporin-B activities by preventing their homo-oligomerization in LPS. In vivo, its simultaneous administration with beta-lactam antibiotics produces the highest antimicrobial activities and the strongest reduction in plasma LPS and TNF-alpha levels, resulting in the highest survival rates in rat models of septic shock.
Subcellular location: Secreted {ECO:0000269|PubMed:34235566, ECO:0000269|PubMed:9022710}. Target cell membrane {ECO:0000269|PubMed:31358802}. Note=Contact and insertion into membrane begin at the N-terminus. {ECO:0000269|PubMed:31358802}.
Interaction partners:
Sequence:
FVQWFSKFLGRIL
Protein: Actin-binding LIM protein 1 (abLIM-1) (Actin-binding LIM protein family member 1) (Actin-binding double zinc finger protein) (LIMAB1) (Limatin) (O14639)
Organism: Homo sapiens (Human)
Function: May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the cytoskeleton. {ECO:0000250}.
Interaction partners:
- Actin-binding LIM protein 3
- Cell division control protein 42 homolog
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 3
- Actin-binding Rho-activating protein
Sequence:
MPAFLGLKCLGKLCSSEKSKVTSSERTSARGSNRKRLIVEDRRVSGTSFTAHRRATITHLLYLCPKDYCPRGRVCNSVDPFVAHPQDPHHPSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGEYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKETTFSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGAPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYDDKQERQSLGESPRTLSPTPSAEGYQDVRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPGNEPSSGRNSPLPYRPDSRPLTPTYAQAPKHFHVPDQGINIYRKPPIYKQHAALAAQSKSSEDIIKFSKFPAAQAPDPSETPKIETDHWPGPPSFAVVGPDMKRRSSGREEDDEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKESRERSSLLASRYDSPINSASHIPSSKTASLPGYGRNGLHRPVSTDFAQYNSYGDVSGGVRDYQTLPDGHMPAMRMDRGVSMPNMLEPKIFPYEMLMVTNRGRNKILREVDRTRLERHLAPEVFREIFGMSIQEFDRLPLWRRNDMKKKAKLF
Protein: GH03013p (Q961W2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGSPLTSPVSKNGYESSRTVEKSSTYKSTSNYVTDSNIRASPSLYGTAERLRRTGSPEPRIDHSSNVRVSSMKPASARRDSWDVINKTKHMLSHNSLESLANMTEKQLNTELQYNRPDLDHETHRNTQYNKFALHKQQQQQSDYRRDSPDDGERYKPSAITVKSHSNNTYTDKSGGYTKTVKESSEHVVTESNGHGPSPGYGYSSLSRFRPIDGNATGARAIRVQDIPNGSIGRPVEFEIDGSRAGSGNLEILVNGGRVTSSVRSLGGQRFIASFTPHEHGTHTVQITFNGETVPGSPWHAEIMSSPGLTALGESTRLVPANTPAVFEILPPPGQSLSKGECVATVLTPSKSKLNARVTHEAANGAARIEFVPTEVGTHVIDASINGTKIAGGPLIAKVYDSSLIQVTEVNGGVVGQACQFRVDASAAGEGQLEISINEGEVPNHVQVVGGGRCLVSFTPEQAKSHLIDIKFNGETVRGCPFVCAVADTSRVLLNLSNLELIPVNRPSSFHITVSGGGAAELAVSVRGPQGELPVRVTGDIHAGFTAEFTPTTVGGHSINVEYNGFAVQGTPFLAKSYDASKVVVGSVSRGTMGRPVQFTVDAGDAGEGNLEITISAKGQNIPTQVHPQGSARFSVSFVPTESCEHTINVSFNKMPVPGCPITVSISGGVAGPQVSLGGPGPVHQTNSFVINHNGGRLEDIEVNVEGRRNLLY
Protein: Mimecan (Osteoglycin) (Osteoinductive factor) (OIF) (P20774)
Organism: Homo sapiens (Human)
Function: Induces bone formation in conjunction with TGF-beta-1 or TGF-beta-2.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8MJF1}.
Interaction partners:
- Osteomodulin
- Asporin
- Lumican
- Keratocan
- Fibromodulin
- Prolargin
- Collagen alpha-1
- Versican core protein
- Aggrecan core protein
- Decorin
Sequence:
MKTLQSTLLLLLLVPLIKPAPPTQQDSRIIYDYGTDNFEESIFSQDYEDKYLDGKNIKEKETVIIPNEKSLQLQKDEAITPLPPKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADIPNLRRLDFTGNLIEDIEDGTFSKLSLLEELSLAENQLLKLPVLPPKLTLFNAKYNKIKSRGIKANAFKKLNNLTFLYLDHNALESVPLNLPESLRVIHLQFNNIASITDDTFCKANDTSYIRDRIEEIRLEGNPIVLGKHPNSFICLKRLPIGSYF
Protein: Geminin homolog (G5EEM1)
Organism: Caenorhabditis elegans
Function: Inhibits DNA replication by binding to the DNA replication licensing factor cdt-1. Its interaction with cdt-1 prevents the cdt-1 loading of the mini-chromosome maintenance (MCM) complex onto DNA and therefore DNA replication licencing.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O75496}. Nucleus {ECO:0000250|UniProtKB:O75496}. Note=Mainly cytoplasmic, but can be re-localized to the nucleus. {ECO:0000250|UniProtKB:O75496}.
Interaction partners:
- RING-type domain-containing protein
- Origin recognition complex subunit 2
- RING-type E3 ubiquitin transferase
- TPR_REGION domain-containing protein
- Organ specific protein
- Major sperm protein
- Serine/threonine-protein phosphatase
Sequence:
MSRIGLQQLNNSARNSPFGSEKATGTKQIPEPLKLTAQLKKYQPITPSPLASATTITPVLSPFDVFCDDDQEAKNVETQMFEYGTVSTQTIINVPHVQPKITEADLTSEKPTVNYLRVMADRLQMDLDDEMDRNQRLVAELGDLDEKMRKIDDDTEILLEVLADIDEEQQTDEEIGTAQL
Protein: Beta-2-microglobulin (Q92004)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKYILSIVVLGLIYSAVEAKESPPKVQVYSRNPGNFGDKNTLICHVSGFHPPDISIQLLKNGVEIPDAKQTDLAFEQGWQFHLTKSVGFTPASGEEYTCRVRHLKNLKTYTWEADM
Protein: Phospholipid scramblase (Q8SZE1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMQMSEYKVLPQNAPQDENGAVVLQPQAANVGNNANGPENWMSIPVGMPNCPQGLEYLTALDQLLVSQKIEKLELLTGFETKNRFKVKNSLGQNVYFAYEESDCCTRNMLGRSRPFEMKILDNFQNEVLHLYRPFKCDILCCFPSCMNAVEVSAPPGQVIGSVSGLHLHAAQVQHQEHMRRYRPADRGTRLSLQVLQRYQLQGIERQQRGDRQNQQTMVRTGKGAVHRCGLLQRHLPPESGCPHEGAHIRSALFD
Protein: Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) (Q14AX6)
Organism: Mus musculus (Mouse)
Function: Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors.
Subcellular location: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalized with nuclear speckles throughout interphase. {ECO:0000250}.
Interaction partners:
- Cyclin-K
- Cyclin-T1
- DNA damage-binding protein 1
- Cyclin-T2
- DNA-directed RNA polymerase II subunit RPB1
- Cyclin-H
- Transcription elongation factor SPT5
- Cyclin-dependent kinase 13
- Bromodomain-containing protein 4
- Transcription elongation factor SPT6
Sequence:
MPNSERHGGKKDGSGGASGTSQPSSGGGSSNSRERHRLVSKHKRHKSKHSKDVGLVTPEAASLGTIIKPLVEYDDISSDSDTFSDDTAFKSDRRENEERRGTDRSDRLHRHRHHQHRRSRDLLKTKQTEKEKNQEVSKSGSMKDRVSGSSKRSVEGSDDYGKAQLSKSGSKESRSSKMHKEKTRKERELKSGYKDRSKSHRKRETPKSYKTVASPKRRSRSPHRKWSDSSKQDDSPSGASYGQDYDLSPPRSHTSSNYDSYKKSPGSTSRRQSISPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSGSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKSSPIILPKKEKLEVKESGLESKKLPRSIKSEKSTPDTELVTVAHSNPEVKHCLDTGKVRLDENLQKHPAKDLKAQGTKDVKPVAPKEVIVTSKETETSEKETLPPLPTITSPPPLPATTPPPQTPPLPPLPPLPAIPLQPPLPPPQPPFSQVPVSSTSILPSSPHPRTSTLSSQTNSQPPVQVSMKTQVSITAAIPHLKTSTLPPLPLPPLLPGDDDMDSPKETLPSKPAKKEKEQRTRHLLTDLPLPPELPGGDPSPPDSPEPKAITPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMAPPDLPHWQDCHELWSKKRRRQRQSGIVIEDPPPSKASRKETTSGTTAEPVKNNSPAPPQPAPVKAEPGPGDAVGLGDITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEASSQQQDSESIAPEESLKEVPSVPVVLPPAEQTTPEASNTPADMQNVLAVLLSQLMKTQEPAGNLEENTNDKNSGPQGPRRTPTMPQEEAAACPPHILPPEKRPPEPPGPPPPPPPPPLVEGDLSSAPQELNPAVTAALLQLLSQPEAEPPGHLPHEHQALRPMEYSTRSHPNRTYGNTDGPETGFSSADTDERSSGPALTESLVQTPVKNRTFSGSVSHLGESNSYQGTGSVQFPGDQDLRFTRVPLALHSVVGQPFLKSEGNSNSVVHAETKLQNYGELGPGTTGANSSGTTLQWGGPAQSYGKPYRGAARVLPRGGRGRGVPY
Protein: Pteridine transporter, putative (Q38A66)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSFAPTRSLPNEVNEPLPTLQSEESGEATYVHPDARALFNKVPCLRRLPMFGTAAEGYGPKAVMSISLSYFLCKGLSDYLVRDSLLAMFTQRFGVDVSVYQRLSNVANMGWSVKPLTAVVSDIFPLFGYSKRWYMFISCLIGPLLSLGFGLLPGKESSAAIGAALVFLCCFTKANVDILAEGHYSRMMRRVPAPGPALVSWIWWFIIAGSFVSSSVVGPLGDAKIPQVASFIASVVQILVLPFFIFNWFGELPNREERYGDALLLYKKEREEREKKCDPFSDSLTQPDRAINSESNPLSTEGPDAAGLVPYEGGAPTGDGDLSSFHFQEPGSCCCGVFEYNKEVVERNGRATVYSILIGLFVLVVAVTSVLGSTTYLTVVAIVVSLLHCSFNFYAFPLIIAKANLFGYLQRATSVSFPGALSNFFIAEADCLADGPHFSFAFYQTVGGIISCAASIVGIMLFNYIFSKRTYRMTYLSTLSLGIFSSIFDLVLVMRWNRPHVSDHALYIMGDAIISPVISMLNWMPQIVLLSRLCPRGSESTVYSILAASSNLGASMGSVVGSVVMEYALPVSSKLPCNFENLKWLVVIAGFLAPLLQIPMVFTLLPRARMCDDLDVDNATAKKKSEIQKEVAEVQESGST
Protein: Putative asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (P9WN33)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Adenylosuccinate synthetase
- Argininosuccinate synthase
- Aspartate carbamoyltransferase catalytic subunit
- L-asparaginase
- L-aspartate oxidase
- Aspartokinase
- Glutamate decarboxylase
- Aspartate 1-decarboxylase
- Cytochrome c oxidase subunit 2
- Probable cytochrome c oxidase polypeptide 4
Sequence:
MCGLLAFVAAPAGAAGPEGADAASAIARASHLMRHRGPDESGTWHAVDGASGGVVFGFNRLSIIDIAHSHQPLRWGPPEAPDRYVLVFNGEIYNYLELRDELRTQHGAVFATDGDGEAILAGYHHWGTEVLQRLRGMFAFALWDTVTRELFCARDPFGIKPLFIATGAGGTAVASEKKCLLDLVELVGFDTEIDHRALQHYTVLQYVPEPETLHRGVRRLESGCFARIRADQLAPVITRYFVPRFAASPITNDNDQARYDEITAVLEDSVAKHMRADVTVGAFLSGGIDSTAIAALAIRHNPRLITFTTGFEREGFSEIDVAVASAEAIGARHIAKVVSADEFVAALPEIVWYLDEPVADPALVPLFFVAREARKHVKVVLSGEGADELFGGYTIYREPLSLRPFDYLPKPLRRSMGKVSKPLPEGMRGKSLLHRGSLTLEERYYGNARSFSGAQLREVLPGFRPDWTHTDVTAPVYAESAGWDPVARMQHIDLFTWLRGDILVKADKITMANSLELRVPFLDPEVFAVASRLPAGAKITRTTTKYALRRALEPIVPAHVLHRPKLGFPVPIRHWLRAGELLEWAYATVGSSQAGHLVDIAAVYRMLDEHRCGSSDHSRRLWTMLIFMLWHAIFVEHSVVPQISEPQYPVQL
Protein: La-related protein 1B (La ribonucleoprotein domain family member 1B) (La ribonucleoprotein domain family member 2) (La-related protein 2) (Q659C4)
Organism: Homo sapiens (Human)
Interaction partners:
- La-related protein 1
Sequence:
MENWPTPSELVNTGFQSVLSQGNKKPQNRKEKEEKVEKRSNSDSKENRETKLNGPGENVSEDEAQSSNQRKRANKHKWVPLHLDVVRSESQERPGSRNSSRCQPEANKPTHNNRRNDTRSWKRDREKRDDQDDVSSVRSEGGNIRGSFRGRGRGRGRGRGRGRGNPRLNFDYSYGYQEHGERTDQPFQTELNTSMMYYYDDGTGVQVYPVEEALLKEYIKRQIEYYFSVENLERDFFLRGKMDEQGFLPISLIAGFQRVQALTTNLNLILEALKDSTEVEIVDEKMRKKIEPEKWPIPGPPPRSVPPTDFSQLIDCPEFVPGQAFCSHTESAPNSPRIGSPLSPKKNSETSILQAMSRGLSTSLPDLDSEPWIEVKKRHQPAPVKLRESVSVPEGSLNQLCSSEEPEQEELDFLFDEEIEQIGRKNTFTDWSDNDSDYEIDDQDLNKILIVTQTPPYVKKHPGGDRTGTHMSRAKITSELAKVINDGLYYYEQDLWMEEDENKHTAIKQEVENFKKLNLISKEQFENLTPELPFEPNQEVPVAPSQSRQGGVQGVLHIPKKDLTDELAQKLFDVSEITSAAMVHSLPTAVPESPRIHPTRTPKTPRTPRLQDPNKTPRFYPVVKEPKAIDVKSPRKRKTRHSTNPPLECHVGWVMDSRDRGPGTSSVSTSNASPSEGAPLAGSYGCTPHSFPKFQHPSHELLKENGFTQQVYHKYRRRCLSERKRLGIGQSQEMNTLFRFWSFFLRDHFNKKMYEEFRQLAWEDAKENYRYGLECLFRFYSYGLEKKFRREIFQDFQEETKKDYESGQLYGLEKFWAYLKYSQSKTQSIDPKLQEYLCSFKRLEDFRVDPPISDEFGRKRHSSTSGEESNRHRLPPNSSTKPPNAAKPTSTSELQVPINSPRRNISPESSDNSH
Protein: 3-oxoacyl-[acyl-carrier-protein] reductase MabA (EC 1.1.1.100) (3-ketoacyl reductase) (3-ketoacyl-acyl carrier protein reductase) (Acetoacetyl-CoA reductase) (EC 1.1.1.36) (Beta-ketoacyl-acyl carrier protein reductase) (Beta-ketoacyl-ACP reductase) (Mycolic acid biosynthesis A) (P9WGT3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:11932442}.
Interaction partners:
- Enoyl-[acyl-carrier-protein] reductase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Catalase-peroxidase
- DNA-directed RNA polymerase subunit beta
- Malonyl CoA-acyl carrier protein transacylase
- Coproporphyrin III ferrochelatase
- Mycobacterial beta-ketoacyl-[acyl-carrier-protein] synthase III
- Probable arabinosyltransferase B
- Probable fatty acid synthase Fas
Sequence:
MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH
Protein: CST complex subunit TEN1 (Protein telomeric pathways with STN1 homolog) (Telomere length regulation protein TEN1 homolog) (Q86WV5)
Organism: Homo sapiens (Human)
Function: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation. However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha. The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins.
Subcellular location: Nucleus {ECO:0000269|PubMed:19854130}. Chromosome, telomere {ECO:0000269|PubMed:19854130}.
Interaction partners:
- CST complex subunit CTC1
- CST complex subunit STN1
- DNA polymerase alpha subunit B
- DNA polymerase alpha catalytic subunit
- DNA primase large subunit
- DNA primase small subunit
- TERF1-interacting nuclear factor 2
- Adrenocortical dysplasia protein homolog
- Telomeric repeat-binding factor 1
- Telomeric repeat-binding factor 2
Sequence:
MMLPKPGTYYLPWEVSAGQVPDGSTLRTFGRLCLYDMIQSRVTLMAQHGSDQHQVLVCTKLVEPFHAQVGSLYIVLGELQHQQDRGSVVKARVLTCVEGMNLPLLEQAIREQRLYKQERGGSQ
Protein: Nitric oxide synthase (dNOS) (EC 1.14.13.39) (Q27571)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the conversion of L-arginine to L-citrulline producing nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. Truncated isoforms (isoform 3-isoform 6) are able to form intracellular complexes with the full-length protein and serve as dominant negative inhibitors of the enzyme activity.
Interaction partners:
- Arginase
- Argininosuccinate lyase, isoform B
- Argininosuccinate synthase
- Calcium-transporting ATPase
- Arginine kinase 1
- arginine kinase
- arginine kinase
- PAPS synthetase, isoform D
- Nitric oxide synthase-interacting protein homolog
- Anamorsin homolog
Sequence:
MSQHFTSIFENLRFVTIKRSTNAQQQQQQQQQQLQQQQQQLQQQKAQTQQQNSRKIKTQATPTLNGNGLLSGNPNGGGGDSSPSHEVDHPGGAQGAQAAGGLPSSSGTPLRHHKRASISTASPPIRERRGTNTSIVVELDGSGSGSGSGGGGVGVGQGAGCPPSGSCTASGKSSRELSPSPKNQQQPRKMSQDYRSRAGSFMHLDDEGRSLLMRKPMRLKNIEGRPEVYDTLHCKGREILSCSKATCTSSIMNIGNAAVEARKSDLILEHAKDFLEQYFTSIKRTSSTAHETRWKQVRQSIETTGHYQLTETELIYGAKLAWRNSSRCIGRIQWSKLQVFDCRYVTTTSGMFEAICNHIKYATNKGNLRSAITIFPQRTDAKHDYRIWNNQLISYAGYKQADGKIIGDPMNVEFTEVCTKLGWKSKGSEWDILPLVVSANGHDPDYFDYPPELILEVPLTHPKFEWFSDLGLRWYALPAVSSMLFDVGGIQFTATTFSGWYMSTEIGSRNLCDTNRRNMLETVALKMQLDTRTPTSLWKDKAVVEMNIAVLHSYQSRNVTIVDHHTASESFMKHFENESKLRNGCPADWIWIVPPLSGSITPVFHQEMALYYLKPSFEYQDPAWRTHVWKKGRGESKGKKPRRKFNFKQIARAVKFTSKLFGRALSKRIKATVLYATETGKSEQYAKQLCELLGHAFNAQIYCMSDYDISSIEHEALLIVVASTFGNGDPPENGELFSQELYAMRVQESSEHGLQDSSIGSSKSFMKASSRQEFMKLPLQQVKRIDRWDSLRGSTSDTFTEETFGPLSNVRFAVFALGSSAYPNFCAFGQYVDNILGELGGERLLRVAYGDEMCGQEQSFRKWAPEVFKLACETFCLDPEESLSDASLALQNDSLTVNTVRLVPSANKGSLDSSLSKYHNKKVHCCKAKAKPHNLTRLSEGAKTTMLLEICAPGLEYEPGDHVGIFPANRTELVDGLLNRLVGVDNPDEVLQLQLLKEKQTSNGIFKCWEPHDKIPPDTLRNLLARFFDLTTPPSRQLLTLLAGFCEDTADKERLELLVNDSSAYEDWRHWRLPHLLDVLEEFPSCRPPAPLLLAQLTPLQPRFYSISSSPRRVSDEIHLTVAIVKYRCEDGQGDERYGVCSNYLSGLRADDELFMFVRSALGFHLPSDRSRPIILIGPGTGIAPFRSFWQEFQVLSDLDPTAKLPKMWLFFGCRNRDVDLYAEEKAELQKDQILDRVFLALSREQAIPKTYVQDLIEQEFDSLYQLIVQERGHIYVCGDVTMAEHVYQTIRKCIAGKEQKSEAEVETFLLTLRDESRYHEDIFGITLRTAEIHTKSRATARIRMASQP
Protein: Nucleotide exchange factor SIL1 (Protein SLS1) (Q08199)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone KAR2.
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Heat shock protein 70 homolog LHS1
- Elongation factor Tu, mitochondrial
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
Sequence:
MVRILPIILSALSSKLVASTILHSSIHSVPSGGEIISAEDLKELEISGNSICVDNRCYPKIFEPRHDWQPILPGQELPGGLDIRINMDTGLKEAKLNDEKNVGDNGSHELIVSSEDMKASPGDYEFSSDFKEMRNIIDSNPTLSSQDIARLEDSFDRIMEFAHDYKHGYKIITHEFALLANLSLNENLPLTLRELSTRVITSCLRNNPPVVEFINESFPNFKSKIMAALSNLNDSNHRSSNILIKRYLSILNELPVTSEDLPIYSTVVLQNVYERNNKDKQLQIKVLELISKILKADMYENDDTNLILFKRNAENWSSNLQEWANEFQEMVQNKSIDELHTRTFFDTLYNLKKIFKSDITINKGFLNWLAQQCKARQSNLDNGLQERDTEQDSFDKKLIDSRHLIFGNPMAHRIKNFRDEL
Protein: Acetyl-CoA acetyltransferase 2 (EC 2.3.1.9) (Acetoacetyl-CoA thiolase 2) (Thiolase 2) (Protein EMBRYO DEFECTIVE 1276) (Q8S4Y1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17120136}. Peroxisome {ECO:0000269|PubMed:17120136}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- 3-hydroxyacyl-CoA dehydrogenase family protein
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
- Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
- Peroxisomal acyl-coenzyme A oxidase 1
- Acetyl-CoA carboxylase 2
- Acyl-coenzyme A oxidase 4, peroxisomal
- Acyl-coenzyme A oxidase 3, peroxisomal
- Acetyl-CoA carboxylase 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
Sequence:
MAHTSESVNPRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL