wanglab/gogpt-training-data huggingface dataset:
Protein: CREB-regulated transcription coactivator 1 homolog (Q95XA8)
Organism: Caenorhabditis elegans
Function: Transcriptional coactivator for crh-1, the homolog of vertebrate transcription factor CREB1. Regulates the transcription of metabolic genes and may have a role in mitochondrial dynamics and metabolism. Involved in modulation of lifespan. Through crh-1, counteracts the pro-lifespan-extension signals of AMPK both cell autonomously and, when expressed in neurons, at a systemic level, possibly using the catecholamine analog, octopamine, as a messenger.
Subcellular location: Nucleus {ECO:0000269|PubMed:21331044, ECO:0000269|PubMed:26232604, ECO:0000269|PubMed:28560849}. Cytoplasm, cytosol {ECO:0000269|PubMed:21331044, ECO:0000269|PubMed:28560849}. Note=Localization is phosphorylation-dependent with the phosphorylated form translocating to the cytosol (PubMed:21331044). Cytosolic sequestration requires 14-3-3 proteins fft-1 and fft-2 (PubMed:21331044). Cytosolic sequestration is partially dependent upon mitochondrial electron transport complex III component isp-1, perhaps as a result of a retrograde signaling pathway relaying signals from mitochondria to the nucleus (PubMed:28560849). Nuclear localization may in part depend on activity of the calcineurin subunit tax-6 and its regulator rcan-1 in response to changes in intracellular calcium levels (PubMed:26232604). {ECO:0000269|PubMed:21331044, ECO:0000269|PubMed:26232604}.
Interaction partners:
- BZIP domain-containing protein.
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Serine/threonine-protein phosphatase 2B catalytic subunit
Sequence:
MSNSNTPRKFSEKIAILERKQNEENTTFEDIMRQVQSITHHPTDSSGSSTATAPMPIPQQGLLPPQQPWGHNLGGSLPNVHQMPSYSPPQWPPNWQHEIQHRPIQGHRSRSPEDHMIGSASGSPSHHYHPYGMRSNGLSRSPDRTPPQHPQYTPYGPPYNQPGQLVPPESWNQINRARSDPAIHNMGGMVPMHPHHHQQQQMAFHQMPHYLQNSMPGPSGMMAPNSQSQQHSPQLTPQGSQQGSPVQMHHQIPPPLQMGNNQQMGGGNNGMSPLQSPNHMMTPMYGYHNGSPLHSPMDSPHASTLMLDGSGTPSPYMEVSPPGMHDFNQDAGSLPNLQNVQQQQQQQQEIYTNGGAPGGGYYHAPIGPRHSTGACGPRLVPGPALTPESQSAPTSPHNQLDPNQPPMWPTRTFSNSPEALDIPKLTITNAEGAPGHHVDSYNDFNDLGLDSLDSVLCNGAPPQTISNHQTPNNSFHDPGGTQMLQN
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q8IPS6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.
Interaction partners:
Sequence:
MLRARRTISIFIEEQTGLTLTPEMLLSTSESSTHSASEVAGRLQVDVRTGLKWTEAKYRAKIIGHNELLLVAEDPTWKKYIEQFRNPLILLLLGSALVSVIMKQFDDAVSITIAILIVVTVAFIQEYRSEKSLEELKKLVPPECHCLREGRLDTFLARELVPGDIVHLNVGDRVPADVRLFEAVDLSIDESSFTGETEPARKITDVLLNNTNVKDHSNMKNIAFMGTLVRCGNGKGIVVSTGERSEFGEVFKMMQAEEAPKTPLQKSMDILGAQLSFYSFLIIGVIMLLGWLQGKPLSEMFNISVSLAVAAIPEGLPIVVTVTLALGVMRMAKRNSIVKKLPTVETLGCVNVICSDKTGTLTKNEMTATIIITSDGYMADVTGAGYNDQGEIHIRHCNNVEMAKTNITNLLEIGAVCNNAYIQNGTLLGQPTEGALVAVAMKNGMYATAENYVRIQEYPFSSEQKMMAVKCIHKYNNNKEEIFFAKGALETLLPQCTKYQFGTQTVPLTKQNEAEFLAEAYEIGRKGLRVLALAKGRSMQDLIYCGLVGITDPPRPLVRESIEMLMQSGVRVKMVTGDAQETALAIANLIGIDTIHHQTLSGQEMDQMNEHQLDKVANNVSVFYRVSPRHKLEIVKSLQRSGNIVGMTGDGVNDGVALKKADIGIAMGKNGTDVCKEAADMILVNDDFHTIIAAIEEGKGIFYNIRNFVRFQLSTSIAALALIALATLMDIANPLNAMQILWINIIMDGPPAQSLGVEPVDHDVLKQKPRNVKQPMITKSVVVNVLLSASIIVLGTLWVFQREMADGTLGKTKRDTTMTFTCFVFFDMFNALSCRSQTKSVFTIGLTTNRMFLLAVAFSIIGQMLVVYFPPLQMVFQTEALTPYDIFFLVSLTSSVLVVSEIKKWFERTMERKMYSTRSELDFV
Protein: Arogenate dehydratase/prephenate dehydratase 1, chloroplastic (AtADT1) (AtPDT1) (EC 4.2.1.51) (EC 4.2.1.91) (Q9SA96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine. Dehydratase that uses arogenate and prephenate as substrates. Utilzes more efficiently arogenate than prephenate.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19136569}.
Interaction partners:
- Arogenate dehydrogenase 2, chloroplastic
- Chorismate mutase 1, chloroplastic
- Arogenate dehydrogenase 1, chloroplastic
- Chorismate mutase 2
- Chorismate mutase 3, chloroplastic
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
- Tyrosine aminotransferase
- Probable aminotransferase TAT1
- Probable aminotransferase TAT4
Sequence:
MALRCFPIWVCPQTTHHRSPLMGLAEFDADKRRRFCLWECSSSASQRAVTAIEGEIPFSRELKKSSDELGLTQETQSLSFHRDLSMLPKPLTANSLYSSDGDDSKVRISFQGIPGAYSETAALKAFPNCETVPCEQFEAAFQAVELWLVDKAVLPIENSVGGSIHRNYDLLLRHRLHIVQEVHLPVNHCLLGVPGVKKEDIKCVLSHPQALDQCVNSLNNLGIQRISAKDTATAAQTVSSSGKIDVGAIASVRAANIYGLDILAENIQDDVNNVTRFLILAREPMIPRTDRPYKTSIVFSLEEGPGVLFKALAVFALRSINLSKIESRPQRRRPLRVVDGSNNGSAKYFDYLFYIDFEASMADTRAQHALGHLQEFASFIRILGCYPMDLVR
Protein: Abhydrolase domain-containing protein C57A10.08c (EC 3.-.-.-) (P87056)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255, ECO:0000269|PubMed:16823372}.
Interaction partners:
- mRNA-capping enzyme subunit beta
- DNA-directed RNA polymerase II subunit rpb1
Sequence:
MYFFTISRLTSFISYGILGALGILTFLYLYDAYLAKSFQRLVIERRSKRESLSKNLSPNDNSHNSKIDISSDYQLLNEYKVAYYLRPGIIPLNHNLAKQEVFVFLHGLGGQMSQFQKVMSYFPPTACLFSFDYWGCGLSRQAFPNQRIGSVDQLTTKGLSKLTYKVLEKLFPENTQFILIGHSMGATIASRVSKMLQTRCTALLLLNPKIRFTSKEISMIVRLRKTPNAFISLYRLLDRFHGLRSSSVTRSLSKNIKGDGDAVRAQLWLWNRQSNTKIWKTMLMGLEELLEPGFHFPKCPILILFGEFDPVSSLKDKVFFQDYPGNYTFKEIDTGHCSMLEQPSEVYNCIDSFLDKFSTTDHNI
Protein: Amine oxidase domain-containing protein (O53734)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Tuberculostearic acid methyltransferase UfaA1
- DUF1365 domain-containing protein
- Possible conserved transmembrane protein
- ECF RNA polymerase sigma factor SigK
- Cyclopropane mycolic acid synthase 1
- Possible transcriptional regulatory protein
- Anti-sigma-K factor RskA
Sequence:
MQQSLRRSVAVVGSGVAGLTAAYILSGRDRVTLYEADGRLGGHAHTHYLDNGGGPRGTDVVGVDSAFLVHNDRTYPTLCRLFAELGVATQESEMSMSVRADDIGLEYAGALGARGLFACRQSLRPRYLCMLAEILRFHRAAARLLREETDNAEDKPETLEAFLSRHHFSQYFVDYFITPLVAAVWSCGGADALRYPARYLFVFLDHHGMLSVFGSPTWRTVTGGSANYVQAIAAQLDEVSTRTPVHSLRRLPDGVLVGAGDGPSRRFDAAVVAVHPDQALLLLDEPTPAERAVLGAIAYSTNSAQLHTDESVLPRHHRARASWNYLVTPGQHQVVVSYDISRLMRLDGGRRYLVTLGGHDRVDPSSVIAEMTYSHPLYTPESVAAQRLLPTLGDNRVVFAGAYHGWGFHEDGAASGLRAARRLGADWPAAIPQEAMVAC
Protein: Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (COX-1) (Prostaglandin H2 synthase 1) (PGH synthase 1) (PGHS-1) (PHS 1) (Prostaglandin-endoperoxide synthase 1) (Q63921)
Organism: Rattus norvegicus (Rat)
Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells.
Subcellular location: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Interaction partners:
- Prostaglandin E synthase
- Prostacyclin synthase
- Thromboxane-A synthase
- Prostaglandin E synthase 3
- Polyunsaturated fatty acid 5-lipoxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Prostaglandin G/H synthase 2
- Prostaglandin E synthase 2
- Hematopoietic prostaglandin D synthase
- Prostaglandin-H2 D-isomerase
Sequence:
MSRRSLSLQFPLLLLLLLLPPPPVLLTDAGVPSPVNPCCYYPCQNQGVCVRFGLDHYQCDCTRTGYSGPNCTIPEIWTWLRSSLRPSPSFTHFLLTHGYWIWEFVNATFIREVLMRLVITVRSNLIPSPPTYNTAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDIHLLAQRLLLRREFIPGPQGTNVLFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDSLERQYHLRLFKDGKLKYQVLDGEVYPPSVEQASVLMRYPPGVPPEKQMAVGQEVFGLLPGLMLFSTIWLREHNRVCDLLKEEHPTWDDEQLFQTTRLILIGETIKIIIEEYVQHLSGYFLQLKFDPELLFRAQFQYRNRIALEFNHLYHWHPLMPDSFQVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQRAGRIGGGRNFDYHVLHVAEDVIKESREMRLQSFNEYRKRFGLKPYTSFQEFTGEKEMAAELEELYGDIDALEFYPGLMLEKCQPNSLFGESMIEMGAPFSLKGLLGNPICSPEYWKPSTFGGDVGFNIVNTASLKKLVCLNTKTCPYVSFRVPDYPGDDGSVFVRPSTEL
Protein: Tail sheath protein (TSP) (Gene product 18) (gp18) (P13332)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Structural component of the bacteriophage tail which consists of a contractile sheath, a tube and a baseplate. The central cylindrical segment of the tail consists of a rigid tube, composed of multiple copies of gp19, surrounded by the outer contractile sheath assembled from gp18 subunits. A total of 138 copies of gp18 arranged into 23 hexameric rings constitutes the sheath. During infection, contraction of the sheath drives the central tube through the host outer membrane, creating a channel for DNA ejection from the capsid into the host cell.
Subcellular location: Virion {ECO:0000269|PubMed:15315755}.
Interaction partners:
Sequence:
MTLLSPGIELKETTVQSTVVNNSTGTAALAGKFQWGPAFQIKQVTNEVDLVNTFGQPTAETADYFMSAMNFLQYGNDLRVVRAVDRDTAKNSSPIAGNIDYTISTPGSNYAVGDKITVKYVSDDIETEGKITEVDADGKIKKINIPTGKNYAKAKEVGEYPTLGSNWTAEISSSSSGLAAVITLGKIITDSGILLAEIENAEAAMTAVDFQANLKKYGIPGVVALYPGELGDKIEIEIVSKADYAKGASALLPIYPGGGTRASTAKAVFGYGPQTDSQYAIIVRRNDAIVQSVVLSTKRGEKDIYDSNIYIDDFFAKGGSEYIFATAQNWPEGFSGILTLSGGLSSNAEVTAGDLMEAWDFFADRESVDVQLFIAGSCAGESLETASTVQKHVVSIGDARQDCLVLCSPPRETVVGIPVTRAVDNLVNWRTAAGSYTDNNFNISSTYAAIDGNHKYQYDKYNDVNRWVPLAADIAGLCARTDNVSQTWMSPAGYNRGQILNVIKLAIETRQAQRDRLYQEAINPVTGTGGDGYVLYGDKTATSVPSPFDRINVRRLFNMLKTNIGRSSKYRLFELNNAFTRSSFRTETAQYLQGNKALGGIYEYRVVCDTTNNTPSVIDRNEFVATFYIQPARSINYITLNFVATATGADFDELTGLAG
Protein: Protein FAM135B (Q49AJ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSEIQGTVEFSVELHKFYNVDLFQRGYYQIRVTLKVSSRIPHRLSASIAGQTESSSLHSACVHDSTVHSRVFQILYRNEEVPINDAVVFRVHLLLGGERMEDALSEVDFQLKVDLHFTDSEQQLRDVAGAPMVSSRTLGLHFHPRNGLHHQVPVMFDYFHLSVISVTVHAALVALQQPLISFTRPGRGSWLGKGGPDTGQEQSIISLENLVFGAGYCKPTSSEGSFYITSENCMQHAHKWHRDLCLLLLHAYRGLRLHFLVIMRDIPELPHTELEALAVEETLSQLCSELQMLNNPEKIAEQISKDLAWLTSHMMTLWTQFLDTVTLHSQVTTYLTQEHHTLRVRRFSEAFFYMEHQKLAVLTFQENLIQTHSQLSLDIRNSEYLTSMPPLPAECLDIDGDWNTLPVIFEDRYVDCPATGHNLSVYPNFDVPVTSPTIMNLKDKEDNCMVNSNLSFREDLVLSTIKPSQMDSDEEVIRCPEPGENVATQNHMDMCSESQVYISIGEFQNKAGVPEDECWTGQTSDAGTYPVADVDTSRRSPGPEDGQAPVLTYIDVKSSNKNPSRAEPLVAFNAQHESRSSRDKYGLDRTGLSKVVVGGSHQNAISSDKTTLHELSTLGKGIDQEGKMVLLSLKLTPSEPCDPLSSTLREPLDIRSSLKDSHTEEQEELSVLSGVIKRSSSIISDSGIESEPSSVAWSEARSRALELPSDREVLHPFVRRHALHRNSLEGGHTESNTSLPSGIQASLTSISSLPFEEDEREVALTKLTKSVSAPHISSPEEAAEDADTKQQDGGFAEPSDMHSKSQGSPGSCSQLCGDSGTDAGADHPLVEIVLDADNQQGPGYIDIPKGKGKQFDAQGHCLPDGRTENTPGVETKGLNLKIPRVIALENPRTRSLHRALEETPKGMPKDLNVGQQALSNSGISEVEGLSQHQVPELSCTSAADAINRNSTGQQSQSGSPCIMDDTAFNRGVNAFPEAKHKAGTVCPTVTHSVHSQVLKNQELKAGTSIMGSHLTSAETFTLDSLKAVEVVNLSVSCTATCLPFSSVPKETPARAGFSSKQTLFPITHQPLGSFGVVSTHSSTLDEEVSERMFSFYQAKEKFKKELKIEGFLYSDLTVLASDIPYFPPEEEEENLEDGIHLVVCVHGLDGNSADLRLVKTFIELGLPGGKLDFLMSEKNQMDTFADFDTMTDRLLDEIIQHIQLYNLSISRISFIGHSLGNIIIRSVLTRPRFRYYLNKLHTFLSLSGPHLGTLYNNSTLVSTGLWLMQKLKKSGSLLQLTFRDNADLRKCFLYQLSQKTGLQYFKNVVLVASPQDRYVPFHSARIEMCKTALKDRHTGPVYAEMINNLLGPLVEAKDCTLIRHNVFHALPNTANTLIGRAAHIAVLDSELFLEKFFLVAGLNYFK
Protein: BAR/IMD domain-containing adapter protein 2 (Brain-specific angiogenesis inhibitor 1-associated protein 2) (I3L4C2)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MSLSRSEEMHRLTENVYKRVEEKYQRNLFPIFSPSALKPESRNFRGESWQGTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSSADVEVARF
Protein: Fibronectin (Q6JAN2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTRESVKRLLLLLCIGGSVHCMPQSAGKSKRQAQQQQIHLDTVYEEARSLAIHESGCNDNGRVYRMNDEWERPYMDSTLKCTCEGASGVKCRSKPAAEESCYDKFNARSYRVGETYERPKDNMIWDCTCIGSGKGKISCTIANRCHEGGNSYRIGDTWTRPHDTGDYMLECVCLGNGKGEWTCKPVAERCYDDSLGSSYVVGQTWQKPYQGWMIVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGETWSKIDSSGHTLQCLCTGNGRGEWKCDRHAASHVIPAIGTGSAVTRRVTPVMNQVNVLNELIEEGNCKTDSGVSYYNGMSWIRTQGTKEMLCTCVGGGISCEEQDGQSQVYGGNSGGQPCVFPFVFSGNTHYSCISEGRSDGQLWCSTTSDYDSDGLYSFCTQKNLLVATRGGNSNGALCQFPFKYNGRNYTDCTAEGRRDGMKWCGTTADYDREQKYGFCPMAAHEEVCTVNDVMYRVGDEWDKRHDTLGHMMRCTCQGNGRGEWNCISHTQLKDQCVVNGQTYDVNETFDKRHDQGYMMNCTCFGQGRGRWKCDAIDQCQEPETKVFYQIGQTWNKVIQGTPYRCSCYGNGIGEMACEPLQSTAPGRVIITEAGNQPNSHPIQWNAPPSAHITQYILKWRVKNTRTPWKEVTIPGHINSYTISGLKAGLTYEGQLISILRYGPREVTRFDFTTTYGSLAKAEGETTQPRQVVDTSESVTEITSNSFVISWVSASDTVSGFRVEYELSEEGARKRVLDLPRTTTSVNIQDLLPGRRYNVDVYEVNPEGDTKLILTTTQTTAPDAPTNHEVSNVQETSIVIRWSKPKAPITGYRVVYTPSVEGSSTELILPGTQTSVTLGDLRPGLSYNISIYSVEDNLESEPLVLQASTAGEQQPEEIQAPTDPQFYEVTDVKITITWTGPPNEVSGYCVTFAPVSTDGQAQRPLQLPVTHNAYAELMRLQPGTLYRFHIYAVSGGVESEPLIGEKSTKPDAPTDLRFTDITDDSALVIWSFPRAQVTGYRLFISIGSSSPKQLRIPGHKSQYKLPNLQPGTEYRVTLHSEQGNTLSEGITDTFRTTQPTGNAPRFNTEVTDTAIIVTWIPVAKFSYRMSVKPSQSGETPREETSGSGRIYISGLTPGLEYIYSLQPLFSGRKHGSPITNKVVTSLSPPTDLNVEPNSVNGELNVRWRGTKSPDITGYRVTGTPINGQRGVSLEESVRGEETSCILENLSPGVDYNISVYTVKNHLESEPISTSVTQDAVPAPTNLYISEVGADSMHVSWTAPSVQPSEISRFVIRYHPTNNDDDTQEVNVGGGTTSFVLQNLLPNTEYLVKVVCVYDDRESEPVTGIQKTKLDSPTNLDFSDVSTNSFTVHWMAPRAVITGYRLRYQPTSGGRAKDERLPPTRNYFTLVNLAPETEYTVHIYAVSSNIESLPLTGTQATVSDAPTDLAVTSSTPTSITISWDAPAVTVRYYKITHGETGERDAPREFTVPGTQSSATIQGLRPDTDYTITLYAVTGRGDSPASSTPVIITHRTAGGSIASPSDLDVTDIQDNTLTVRWTPARGPITGYRVTGTPKGGQGPTFSELVGPERTEMTIHGLVPTVEYTINVVALSQKGESTPVVQKATTTYEQKPKDLTLTDVDSNSMLVKWNGPRVPGVTSYRVLYSSPEEGEKEYQPALSGRDNSVLLQGLNPGTMYIIKVIPMKGRNPLQTLEGIQQTIQEDTQRIAVPAPTDIQFFDISPSSFIVSWQAPNSRLSGYRVVVTPRNQLATSKEMTVSPDSTQVLVPGLVVATPYNVHVYALRGSDSSPPLTGEITTADNITPPRRVRISDVKDTSFTLAWRAVNNEPMTGFLIEATPKNGGYPTFRQTIPSDRRTYVVTGLHPGVMYVVNMYTVNGNMRSPPFTMTVNTARPAVQSPTNLQFTSLTPNSISFTWQAPPTHITGYYITYEESGGSPRELFPRNNVGQNYATIAGLKPGTEYIIKIIALLNNQRSAPLVGTATTQLISGLPSLPSHGGRDKLDVPEPDNRINTVGPTGHDSTDAHGQHVEYTEYNNQPKQPNIGYQPQNRQPISQPNQPRPQPYVPQVGETLVYVPQVGPDGGRVPQIIQVSERPGDGHTFGFPEDRTGRPQEAQTQTTISWQPVQQSPAYPASGQPITHPDEKMFQMRVPGTSTTATLIGLTSGASYNVIVEALKGALKHKILEEVVTAGNTVPGDATSSKDSCYDTFTATHHDVGAEWERMSDTGFKLWCRCLGLGSGHFRCDSSKWCHDSGNNYRIGEKWERRAENGHLMSCTCLGNGKGEFKCEPHDSIWYDDGKMYQMGNQWQKEYLRAICTCTCYGGQQGWRCENCRRPGAEINADLLRPVRLNNGQRVNIQCPIECLRPELLADAVVNPKTQE
Protein: Dynactin subunit 4 (Q18194)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000256|ARBA:ARBA00004529}. Cytoplasm, myofibril {ECO:0000256|ARBA:ARBA00004657}.
Interaction partners:
- Dynactin subunit 5
- Dynactin subunit 6
- Actin-related protein 10
- Probable dynactin subunit 2
- Dynactin subunit 1
- Actin
- F-actin-capping protein subunit beta
- DyNactin Complex component
- F-actin-capping protein subunit alpha
- ER membrane protein complex subunit 1
Sequence:
MSELLQYSRIKYECTCGKFRTLPDLVFCRYCFKIKCDDCSLGEVDNIFCPRCLEPSSVPEARLKKHKCASCNDCPKCANVLSARTENDNVYLVCQYCRWSSREANQEDQENTKSWPTKENPLVNQLGEVTAYMKRLELIENAPKDLKKGKSGKAWTAFHLKDKFGFQQMVDKRKKALAPEMNPVDAHAPTEAPTLEDEIKERTDDLRTLDQIIMQPLINISEPLLPVQVPLAGRVQVRCDECERTLIKRDFGVTTFKFKISSFARQFVPDIRMSRPVDDLKVGETSHVFLSITNLSSSAMDLTIAPQSGNGFIQCSSDPIQLLLPSSRASDTAAPGVHADQSDVIVFRQHNRVGLRLDVIPTEMDLSSPCLNLLITYCQDGSFRLSSASDKILKPEETCPDPILSANLKVDLR
Protein: Dahlein-5.5 (P84271)
Organism: Ranoidea dahlii (Dahl's aquatic frog) (Litoria dahlii)
Function: Has no antimicrobial activity. Strongly inhibits the formation of NO by neuronal nitric oxide synthase at micromolar concentrations.
Subcellular location: Secreted {ECO:0000269|PubMed:11555873}.
Interaction partners:
Sequence:
GLLASLGKVLGGYLAEKLKPK
Protein: L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase (L-Cys:GlcN-Ins ligase) (EC 6.3.1.13) (Mycothiol ligase) (MSH ligase) (P9WJM9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
Interaction partners:
- Mycothiol acetyltransferase
- 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase
- D-inositol 3-phosphate glycosyltransferase
- Mycothiol S-conjugate amidase
- 3'-phosphoadenosine 5'-phosphate phosphatase
- Serine acetyltransferase
- DNA-directed RNA polymerase subunit omega
- Phosphoglucosamine mutase
- Glucosyl-3-phosphoglycerate synthase
- Protein Rv2133c
Sequence:
MQSWYCPPVPVLPGRGPQLRLYDSADRQVRPVAPGSKATMYVCGITPYDATHLGHAATYVTFDLIHRLWLDLGHELHYVQNITDIDDPLFERADRDGVDWRDLAQAEVALFCEDMAALRVLPPQDYVGATEAIAEMVELIEKMLACGAAYVIDREMGEYQDIYFRADATLQFGYESGYDRDTMLRLCEERGGDPRRPGKSDELDALLWRAARPGEPSWPSPFGPGRPGWHVECAAIALSRIGSGLDIQGGGSDLIFPHHEFTAAHAECVSGERRFARHYVHAGMIGWDGHKMSKSRGNLVLVSALRAQDVEPSAVRLGLLAGHYRADRFWSQQVLDEATARLHRWRTATALPAGPAAVDVVARVRRYLADDLDTPKAIAALDGWVTDAVEYGGHDAGAPKLVATAIDALLGVDL
Protein: rRNA 2'-O-methyltransferase fibrillarin (EC 2.1.1.-) (Histone-glutamine methyltransferase) (Q9W1V3)
Organism: Drosophila melanogaster (Fruit fly)
Function: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Note=Fibrillar region of the nucleolus. {ECO:0000250}.
Interaction partners:
- Nucleolar protein 58
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex subunit 4
- H/ACA ribonucleoprotein complex subunit 2
- LD17611p
- NHP2-like protein 1 homolog
- Small ribosomal subunit protein uS9
- Nopp140, isoform E
- H/ACA ribonucleoprotein complex subunit 1
- LD10780p
Sequence:
MGKPGFSPRGGGGGGGGGGGGFRGRGGGGGGGGGGFGGGRGRGGGGDRGGRGGFGGGRGGGGRGGGGGGGRGAFGGRGGGGGRGGGGRGGGGRGGGGRGGGAGGFKGGKTVTIEPHRHEGVFIARGKEDALVTRNFVPGSEVYGEKRISVETNGEKIEYRVWNPFRSKLAAAVLGGVEQIHMPPGSKVLYLGAASGTTVSHVSDVVGPEGLVYAVEFSHRSGRDLINVAKKRTNIIPIIEDARHPHKYRMLVGMVDTIFADVAQPDQGRIVALNAQHFLKNGGHFVISIKASCIDSTAQPEAVFAAEVKKMQADKLKPQEQLTLEPYERDHAVVVGVYRPPPKQ
Protein: Protein KINASE OF THE OUTER CHLOROPLAST MEMBRANE 1 (EC 2.7.11.1) (Q8RWX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:28283569}; Single-pass membrane protein {ECO:0000269|PubMed:28283569}; Cytoplasmic side {ECO:0000269|PubMed:28283569}.
Interaction partners:
- non-specific serine/threonine protein kinase
- At3g08760
- Kinase with adenine nucleotide alpha hydrolases-like domain-containing protein
- Expressed protein
- Early endosome antigen
- Uncharacterized aarF domain-containing protein kinase At1g71810, chloroplastic
- AT3g52230/F4F15_340
- Receptor protein kinase-like protein ZAR1
- At1g68680
- Sequence-specific DNA binding transcription factor
Sequence:
MASKIIAGKPDDTEYEIIEGESESALAAGTSPWMNSSTLKLRHRIGRGPFGDVWLATHHQSTEDYDEHHEVAIKMLYPIKEDQRRVVVDKFEDLFSKCQGLENVCLLRGVSSINGKICVVMKFYEGSLGDKMARLKGGKLSLPDVLRYGVDLATGILELHSKGFLILNLKPSNFLLSDNDKAILGDVGIPYLLLSIPLPSSDMTERLGTPNYMAPEQWQPDVRGPMSFETDSWGFGCSIVEMLTGVQPWSGRSADEIYDLVVRKQEKLSIPSSIPPPLENLLRGCFMYDLRSRPSMTDILLVLKSLQNSEEEQVRRGIDSREIRKSSATLGYTEWFLSKDHLQVRDTVRSRKPANSCKHENMDVPEGMVVGLERDSTDPDGFVLVKVHGVHDPLRVHVSVLERVTNGLASGDWVRLKVRKDKRHSPVGVLHSIDREGNVAVGFIGLPTLWKGTSSQLQMAKVYSVGQFVKLKANVVIPRFKWMRKGRGIWATGRISQVLPNGCLEVDFPGMLPFGEEHGSYLADPAEVEIVNFNTCQGAVEKYQHLEDFHWAVRPLLIAMGLLTAMKLGICVRKKIGRSKDGKQRDGSTGQGDCKIPDGKGSDKSKWLVFF
Protein: cDNA FLJ13861 fis, clone THYRO1001100, moderately similar to ZINC FINGER X-LINKED PROTEIN ZXDA (Q9H891)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKAHMVRQHSRRQDLLPQLEAPSSLTPSSELSSPGQSELTNMDLAALFSDTPANASGSAGGSDEALNSGILTIDVTSVSSSLGGNLPANNSSLGPMEPLVLVAHSDIPPSLDSPLVLGTAATVLQQGSFSVDDVQTVSAGALGCLVALPMKNLSDDPLALTSNSNLAAHITTPTSSSTPRENASVPELLAPIKVEPDSPSRPGAVGQQEGSHGLPQSTLPSPAEQHGAQDTELSAGTGNFYLESGGSARTDYRAIQLAKEKKQRGAGSNAGASQSTQRKIKEGKMSPPHFHASQNSWLCGSLVVPSGGRPGPAPAAGVQCGAQGVQVQLVQDDPSGEGVLPSARGPATFLPFLTVDLPVYVLQEVLPSSGGPAGPEATQFPGSTINLQDLQ