wanglab/gogpt-training-data huggingface dataset:
Protein: ORF7a protein (Accessory protein 7a) (Protein U122) (Protein X4) (P59635)
Organism: Severe acute respiratory syndrome coronavirus (SARS-CoV)
Function: Plays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect. Acts by binding to BST2 thereby interfering with its glycosylation. May suppress small interfering RNA (siRNA). May bind to host ITGAL, thereby playing a role in attachment or modulation of leukocytes.
Subcellular location: Virion. Host endoplasmic reticulum membrane; Single-pass membrane protein. Host endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass membrane protein.
Interaction partners:
Sequence:
MKIILFLTLIVFTSCELYHYQECVRGTTVLLKEPCPSGTYEGNSPFHPLADNKFALTCTSTHFAFACADGTRHTYQLRARSVSPKLFIRQEEVQQELYSPLFLIVAALVFLILCFTIKRKTE
Protein: Short transmembrane mitochondrial protein 1 (Mitochondrial micropeptide-47) (Mm47) (Protein mitolamban) (P0DP99)
Organism: Mus musculus (Mouse)
Function: Microprotein involved in mitochondrial respiratory chain complex III (ubiquinol-cytochrome c oxidoreductase) and complex IV (mitochondrial cytochrome c oxidase complex) assembly. Required for the formation of mitochondrial supercomplexes (SCs). Also required for the activation of the NLRP3 inflammasome.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:35101990}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:31836654}; Single-pass membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000269|PubMed:31836654}.
Interaction partners:
Sequence:
MLQFLLGFTLGNVVGMYLAQNYEMPNLAKKLEEIKKDLEAKKKPPSS
Protein: Replication protein A 70 kDa DNA-binding subunit (RP-A p70) (Replication factor A protein 1) (RF-A protein 1) (Single-stranded DNA-binding protein) (DmRPA1) (Q24492)
Organism: Drosophila melanogaster (Fruit fly)
Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage.
Subcellular location: Nucleus.
Interaction partners:
- GEO08380p1
- CG9273 protein
- RecQ-like DNA helicase Blm
- DNA topoisomerase 3-alpha
- DNA repair protein Rad51 homolog
- Timeout
- DNA polymerase delta catalytic subunit
- Protein TIPIN homolog
- DNA replication complex GINS protein SLD5
- Serine/threonine-protein kinase ATR
Sequence:
MVLASLSTGVIARIMHGEVVDAPVLQILAIKKINSAADSERYRILISDGKYFNSYAMLASQLNVMQHNGELEEFTIVQLDKYVTSLVGKDGAGKRVLIISELTVVNPGAEVKSKIGEPVTYENAAKQDLAPKPAVTSNSKPIAKKEPSHNNNNNIVMNSSINSGMTHPISSLSPYQNKWVIKARVTSKSGIRTWSNARGEGKLFSMDLMDESGEIRATAFKEQCDKFYDLIQVDSVYYISKCQLKPANKQYSSLNNAYEMTFSGETVVQLCEDTDDDPIPEIKYNLVPISDVSGMENKAAVDTIGICKEVGELQSFVARTTNKEFKKRDITLVDMSNSAISLTLWGDDAVNFDGHVQPVILVKGTRINEFNGGKSLSLGGGSIMKINPDIPEAHKLRGWFDNGGGDSVANMVSARTGGGSFSTEWMTLKDARARNLGSGDKPDYFQCKAVVHIVKQENAFYRACPQSDCNKKVVDEGNDQFRCEKCNALFPNFKYRLLINMSIGDWTSNRWVSSFNEVGEQLLGHTSQEVGEALENDPAKAEQIFSALNFTSHIFKLRCKNEVYGDMTRNKLTVQSVAPINHKEYNKHLLKELQELTGIGSSN
Protein: Pentatricopeptide repeat-containing protein At1g06580 (Q9SHK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein REDUCED CHLOROPLAST COVERAGE 1
- Pentatricopeptide repeat-containing protein At1g26460
- Pentatricopeptide repeat-containing protein At4g21190
- Transcription factor EMB1444
Sequence:
MRRSIVIVIALTAKGFLHRHLLEKGNLVTALSLRICNSRAFSGRSDYRERLRSGLHSIKFNDALTLFCDMAESHPLPSIVDFSRLLIAIAKLNKYEAVISLFRHLEMLGISHDLYSFTTLIDCFCRCARLSLALSCLGKMMKLGFEPSIVTFGSLVNGFCHVNRFYEAMSLVDQIVGLGYEPNVVIYNTIIDSLCEKGQVNTALDVLKHMKKMGIRPDVVTYNSLITRLFHSGTWGVSARILSDMMRMGISPDVITFSALIDVYGKEGQLLEAKKQYNEMIQRSVNPNIVTYNSLINGLCIHGLLDEAKKVLNVLVSKGFFPNAVTYNTLINGYCKAKRVDDGMKILCVMSRDGVDGDTFTYNTLYQGYCQAGKFSAAEKVLGRMVSCGVHPDMYTFNILLDGLCDHGKIGKALVRLEDLQKSKTVVGIITYNIIIKGLCKADKVEDAWYLFCSLALKGVSPDVITYITMMIGLRRKRLWREAHELYRKMQKEDGLMPIK
Protein: Homeobox protein Nkx-2.3 (Homeobox protein NK-2 homolog C) (Q8TAU0)
Organism: Homo sapiens (Human)
Function: Transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Mucosal addressin cell adhesion molecule 1
- Tyrosine-protein phosphatase non-receptor type 2
Sequence:
MMLPSPVTSTPFSVKDILNLEQQHQHFHGAHLQADLEHHFHSAPCMLAAAEGTQFSDGGEEDEEDEGEKLSYLNSLAAADGHGDSGLCPQGYVHTVLRDSCSEPKEHEEEPEVVRDRSQKSCQLKKSLETAGDCKAAEESERPKPRSRRKPRVLFSQAQVFELERRFKQQRYLSAPEREHLASSLKLTSTQVKIWFQNRRYKCKRQRQDKSLELGAHAPPPPPRRVAVPVLVRDGKPCVTPSAQAYGAPYSVGASAYSYNSFPAYGYGNSAAAAAAAAAAAAAAAAYSSSYGCAYPAGGGGGGGGTSAATTAMQPACSAAGGGPFVNVSNLGGFGSGGSAQPLHQGTAAGAACAQGTLQGIRAW
Protein: Nucleoplasmin-3 (O75607)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of diverse cellular processes such as ribosome biogenesis, chromatin remodeling or protein chaperoning. Modulates the histone chaperone function and the RNA-binding activity of nucleolar phosphoprotein B23/NPM. Efficiently mediates chromatin remodeling when included in a pentamer containing NPM3 and NPM.
Subcellular location: Nucleus {ECO:0000269|PubMed:11722795}. Nucleus, nucleolus {ECO:0000269|PubMed:15596447, ECO:0000269|PubMed:22362753}. Note=Mainly found in the granular component of the nucleolus. {ECO:0000269|PubMed:22362753}.
Interaction partners:
- Nucleophosmin
- Nucleoplasmin-2
- Protein O-GlcNAcase
- Fibroblast growth factor 8
- Nucleolin
Sequence:
MAAGTAAALAFLSQESRTRAGGVGGLRVPAPVTMDSFFFGCELSGHTRSFTFKVEEEDDAEHVLALTMLCLTEGAKDECNVVEVVARNHDHQEIAVPVANLKLSCQPMLSLDDFQLQPPVTFRLKSGSGPVRITGRHQIVTMSNDVSEEESEEEEEDSDEEEVELCPILPAKKQGGRP
Protein: Matrilin-3 (O35701)
Organism: Mus musculus (Mouse)
Function: Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.
Subcellular location: Secreted {ECO:0000269|PubMed:10660556, ECO:0000269|PubMed:23956175}.
Interaction partners:
- Cartilage oligomeric matrix protein
- Collagen, type IX, alpha 3
- Aggrecan core protein
- Collagen alpha-2
- Collagen alpha-1
- Sulfate transporter
Sequence:
MLLSAPLRHLPGLLLLLWPLLLLPSLAAPGRLARASVRRLGTRVPGGSPGHLSALATSTRAPYSGGRGAGVCKSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTMSGLAIQTAMEEAFTVEAGARGPMSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLEEHVFYVETYGVIEKLSARFQETFCALDQCMLGTHQCQHVCVSDGDGKHHCECSQGYTLNADGKTCSAIDKCALSTHGCEQICVNDRNGSYHCECYGGYALNADRRTCAALDKCASGTHGCQHICVNDGAGSHHCECFEGYTLNADKKTCSVRNKCALGTHGCQHICVSDGAVAYHCDCFPGYTLNDDKKTCSDIEEARSLISIEDACGCGATLAFQEKVSSHLQKLNTKLDNILKKLKVTEYGQVHR
Protein: Golgi phosphoprotein 3 homolog sauron (Protein rotini) (Q9VQ93)
Organism: Drosophila melanogaster (Fruit fly)
Function: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (By similarity). May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion (By similarity). Also involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part (By similarity). Functions in cytokinesis by regulating contractile ring formation and vesicle trafficking during cleavage furrow ingression. May also have a role in the intital steps of central spindle formation. Can also bind phosphatidylinositol-3-phosphate and phosphatidylinositol-5-phosphate in vitro.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:24786584, ECO:0000305|PubMed:23720043}; Peripheral membrane protein {ECO:0000305|PubMed:23720043}; Cytoplasmic side {ECO:0000305|PubMed:23720043}. Cytoplasmic vesicle {ECO:0000269|PubMed:24786584}. Cleavage furrow {ECO:0000269|PubMed:24786584}. Note=Phosphatidylinositol 4-phosphate-binding and oligomerization participate in the recruitment onto Golgi membranes (PubMed:23720043). In dividing cells associates with vesicles in polar regions of the cells during metaphase and anaphase, and localizes to the cleavage furrow during telophase (PubMed:24786584). {ECO:0000269|PubMed:24786584, ECO:0000305}.
Interaction partners:
- Phosphatidylinositol-3-phosphatase SAC1
- FI01544p
- Conserved oligomeric Golgi complex subunit 7
- Rab11
- Myosin regulatory light chain sqh
- Coatomer subunit alpha
- Signal recognition particle 54 kDa protein
- Phosphatidylinositol 4-kinase type 2
Sequence:
MNRSDGLVRRSVKPRENGGAEGGLNANTPDDNQDALDNLKDQEDNIDDGDSKETRLTLMEEVLLLGLKDKEGYTSFWNDCISSGLRGCILIELGLRGRVMIEKSGMRRRGLCTRKLILKSDQQTGDVLLDEALKHIKETDPPETVQSWIEYLSGETWNPLKLRYQLKNVRERLAKNLVEKGVLTTEKQNFLLFDMTTHPLSDNVVKCRLVKKIQDSVLSKWVNDPQRMDKRMLALIFLAHASDVIENAFAPLNDDDYEVAMKRVRELLDLDFEAESAKPNANEILWAVFMAFTK
Protein: Myozenin-1 (Calsarcin-2) (Filamin-, actinin- and telethonin-binding protein) (Protein FATZ) (Q9JK37)
Organism: Mus musculus (Mouse)
Function: Myozenins may serve as intracellular binding proteins involved in linking Z-disk proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis.
Subcellular location: Nucleus {ECO:0000250}. Cell projection, pseudopodium {ECO:0000250}. Note=Localized to the nucleus and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2, FLNC and MYOT at the Z-lines of skeletal muscle (By similarity). {ECO:0000250}.
Interaction partners:
- Alpha-actinin-2
- Alpha-actinin-3
- Myotilin
- Troponin T, fast skeletal muscle
- Troponin C, skeletal muscle
- Synaptopodin 2-like protein
- Telethonin
- Myosin regulatory light chain 11
- Myosin-4
- Troponin I, fast skeletal muscle
Sequence:
MPLSGTPAPNKRRKSSKLIMELTGGGRESSGLNLGKKISVPRDVMLEELSLLTNRGSKMFKLRQMRVEKFIYENHPDVFSDSSMDHFQKFLPTVGGQLETAGQGFSYGKGSSGGQAGSSGSAGQYGSDRHQQGSGFGAGGSGGPGGQAGGGGAPGTVGLGEPGSGDQAGGDGKHVTVFKTYISPWDRAMGVDPQQKVELGIDLLAYGAKAELPKYKSFNRTAMPYGGYEKASKRMTFQMPKFDLGPLLSEPLVLYNQNLSNRPSFNRTPIPWLSSGEHVDYNVDVGIPLDGETEEL
Protein: p-GlycoProtein related (Q20331)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- ABC transporter domain-containing protein
Sequence:
MPEATDALLEPVVPMKIASEHVELGSRPDKKKKKSRSSQGNSLSNLFRHSGCADYLLLLGGLVLSAANGALLPFNSLIFEGITNVLMKGEAQWQNGTFDYDTFSSGIQHYCLLYFLLGVLMFTCTYFSNACLFTMAERRLYCIRKHLLQSVLRQDAKWFDENTVGGLTQKMSSGIEKIKDGIGDKIGVLVSGIATFISGVALGFYMCWQLTLVMLVTVPLQLGSMYLSAKHLNRATKNEMSAYSSAGGMANEVIAGIRTVIAFNAQPFEIERYGAQLAKARKMGIRKAIVLALCSAMPLFLMFVLMAGAFWYGAILTSYGVATSGTTFGVFWAVILGTRRLGEAAPHMGAITGARLAVNDIFKVIDHEPEINCTKQEGRRPDKVNGKLVFDNIQFTYPTRPDVKILKGVSFEVNPGETIALVGHSGCGKSTSIGLLMRFYNQCAGSIKLDGIPIEDYNIQWLRSTIGIVQQEPIIFLATVAENVRMGDDSITDKDIENACRQANAHDFIGKLSEGYNTVIGAGAVQLSGGQKQRVAIARAIVRKPQILLLDEATSALDTESERMVQTALDKASEGRTTLCIAHRLSTIRNASKILVFDQGLIPERGIHDQLIRQNGIYANMVRAQEIEKAKDDTTQDDDELVEEDNYSISRRLSTSEEELRKSKSLLRDSTRFSQSMLSVTSQVPDWEMESAREEMIEEGAMEASMMDIFRFAKPEKMNIVIALIFTLIRGITWPAFSVVYGQLFKVFAEGGEDLPVNALISSLWFVLLAVTSAVTTFISGSLLGKTGETMSSRLRMDVFKNIMQQDATYFDDPKHNVGNLTSRLATDSQNVQAAIDHRLAEVLNGVVSLFTGIAVAFWFGWSMAPIGLITALLLVIAQSAVAQYLKYRGPKDMESAIEASRIVTESISNWKTVQALTKQEYMFHAFTAASKNPRKRAFTKGLWQSLSFALAGSFFLWNFAIAYMFGLWLISNNWTTPFAVFQVIEALNMASMSVMMAASYFPEYVRARISAGIMFTMIRQKAKIDNRGLTGETPDIRGDISMKGVYFAYPNRNRQLILNNFNMSAQFGETVALVGPSGCGKSTSIQLIERYYDAICGAVKIDDHDIRDISVKHLRHNIALVGQEPTLFNLTIRENITYGLENVSQEQVEKAATLANIHSFVENLPEGYDTSVGASGGRLSGGQKQRIAIARAIVRNPKILLLDEATSALDTESEKIVQEALDKARLGRTCVVIAHRLSTIQNADKIIVCRNGKAIEEGTHQTLLARRGLYYRLVEKQST
Protein: T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) (Q2NKZ1)
Organism: Bos taurus (Bovine)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P80313}.
Interaction partners:
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta-2
- Uncharacterized protein
- T-complex protein 1 subunit theta
Sequence:
MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKEDKVEQRKLLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFEMQPKKYHNPMIALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSSDVLGRCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINTEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRSTVDASPAAGRGRGRGRLH
Protein: Glucagon-like peptide 1 receptor (GLP-1 receptor) (GLP-1-R) (GLP-1R) (O35659)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for glucagon-like peptide 1 (GLP-1). Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels (By similarity). Plays a role in regulating insulin secretion in response to GLP-1.
Subcellular location: Cell membrane {ECO:0000305|PubMed:9568699}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P43220}.
Interaction partners:
- Pro-glucagon
- Gastric inhibitory polypeptide
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- VIP peptides
- Pituitary adenylate cyclase-activating polypeptide
- Natriuretic peptides A
- Dipeptidyl peptidase 4
- Glucagon-like peptide 2 receptor
- Insulin-1
Sequence:
MASTPSLLRLALLLLGAVGRAGPRPQGTTVSLSETVQKWREYRRQCQRFLTEAPLLATGLFCNRTFDDYACWPDGPPGSFVNVSCPWYLPWASSVLQGHVYRFCTAEGLWLHKDNSSLPWRDLSECEESKRGERNFPEEQLLSLYIIYTVGYALSFSALVIASAILVGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLGCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFKLYLSIGWGVPLLFVIPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFIRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFIKLFTELSFTSFQGLMVAILYCFVNNEVQMEFRKCWERWRLEHLNIQRDCSMKPLKCPTSSVSSGATVGSSVYAATCQSSYS
Protein: Carbon catabolite-derepressing protein kinase (EC 2.7.11.1) (Sucrose nonfermentating protein 1) (P06782)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine protein kinase essential for release from glucose repression. Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes. The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters. The complex also negatively regulates the HOG1 MAPK pathway in ER stress response including unfolded protein response (UPR). Under nutrient/energy depletion, the complex phosphorylates and activates PAS kinase PSK1 which in turn activates PBS1, leading to the inhibition of the TORC1 signaling pathway. SNF1 also interacts and phosphorylates adenylate cyclase CYR1 and negatively regulates the protein kinase A signaling pathway. Also phosphorylates and regulates the transcriptional activator CAT8.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25869125}. Nucleus {ECO:0000269|PubMed:25869125}. Nucleus membrane {ECO:0000269|PubMed:17237508}; Peripheral membrane protein {ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions (PubMed:25869125). {ECO:0000269|PubMed:25869125}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit gamma
- SNF1 protein kinase subunit beta-3
- SNF1 protein kinase subunit beta-1
- SNF1 protein kinase subunit beta-2
- Regulatory protein MIG1
- SNF1-activating kinase 1
- Low glucose sensor SNF3
- Serine/threonine-protein kinase ELM1
- Hexokinase-2
- High glucose sensor RGT2
Sequence:
MSSNNNTNTAPANANSSHHHHHHHHHHHHHGHGGSNSTLNNPKSSLADGAHIGNYQIVKTLGEGSFGKVKLAYHTTTGQKVALKIINKKVLAKSDMQGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRDKMSEQEARRFFQQIISAVEYCHRHKIVHRDLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYVMLCRRLPFDDESIPVLFKNISNGVYTLPKFLSPGAAGLIKRMLIVNPLNRISIHEIMQDDWFKVDLPEYLLPPDLKPHPEEENENNDSKKDGSSPDNDEIDDNLVNILSSTMGYEKDEIYESLESSEDTPAFNEIRDAYMLIKENKSLIKDMKANKSVSDELDTFLSQSPPTFQQQSKSHQKSQVDHETAKQHARRMASAITQQRTYHQSPFMDQYKEEDSTVSILPTSLPQIHRANMLAQGSPAASKISPLVTKKSKTRWHFGIRSRSYPLDVMGEIYIALKNLGAEWAKPSEEDLWTIKLRWKYDIGNKTNTNEKIPDLMKMVIQLFQIETNNYLVDFKFDGWESSYGDDTTVSNISEDEMSTFSAYPFLHLTTKLIMELAVNSQSN
Protein: histidine kinase (EC 2.7.13.3) (Q0PBM2)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Interaction partners:
- MCP-type signal transduction protein
- Chemotaxis protein
- protein-glutamate methylesterase
- Chemotaxis protein
- Methyl-accepting chemotaxis signal transduction protein
- Bipartate energy taxis response protein cetA
- Flagellar motor switch protein FliM
- Methyl-accepting chemotaxis signal transduction protein
- MCP-domain signal transduction protein
- Flagellar motor switch protein FliN
Sequence:
MEDMQEILEDFLVEAFELVEQIDHDLVELESNPEDLELLNRIFRVAHTVKGSSSFLNFDVLTKLTHHMEDVLNKARHGELKITPDIMDVVLESIDRMKTLLNSIRDNGNDTAIGMDIEPICARLTAISEGESPVVATDSNEKSIPQAELEAPKQEIATPEPEVDVNQLSDSEVEAEIERLLKVRKAEDQARRAQKKQTTNAAPKPTNNTANKPTESGEKKVPASGSNASSMDQTIRVEVKRLDHLMNLIGELVLGKNRLLKIYDDVEERYEGEKFLEELNQVVSQLSIIITDVQLAVMKTRMQPIAKVFNKFPRVVRDLSRELGKQIELEITGEETELDKSIVEEIGDPIMHMIRNSCDHGVEDPATRAANGKPEKGIVQLKAYNEGNHIVVEITDDGKGLDPNGLKAKAIEKNLITEREADQMTDKEAFALIFKPGFSTAAKVTNVSGRGVGMDVVKTNIEKLNGVIEIDSELGKGSSFKLKIPLTLAIIQSLLVGTQEEFYAIPLASVLETVRVPIDDIYTIEGKNVLRLRDEVLSLVRLSDVFGVKQVLESGDQTYVVVIGVAESKLGIIVDTLVGQEEIVIKSMGDYLQNIQGIAGATIRGDGRVTLIIDVGAMMDMAKEIKVDIKAQLESSAKKPKEQPSDYKVLIVDDSKMDRTLMQKALEPLGVSLIEATNGVEALNIIKSGEHDIDAMLIDIEMPRMDGYTLAGEIRKYSKYRNLPLIAVTSRTSKTDRLRGVEVGMTEYITKPYSPEYLENVVRKNLKLG
Protein: Osmotin-like protein OSM34 (P50700)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Basic endochitinase B
- At2g15220/F15A23.4
Sequence:
MANLLVSTFIFSALLLISTATAATFEILNQCSYTVWAAASPGGGRRLDAGQSWRLDVAAGTKMARIWGRTNCNFDSSGRGRCQTGDCSGGLQCTGWGQPPNTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPTSSNCHRILCTADINGQCPNVLRAPGGCNNPCTVFQTNQYCCTNGQGSCSDTEYSRFFKQRCPDAYSYPQDDPTSTFTCTNTNYRVVFCPRSRLGATGSHQLPIKMVTEEN
Protein: Transcription termination factor MTERF8, chloroplastic (Mitochondrial transcription termination factor 8) (Protein PLASTID TRANSCRIPTIONALLY ACTIVE 15) (Q9FK23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription termination factor that is transcriptionally active in chloroplasts.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16326926, ECO:0000269|PubMed:21464319}.
Interaction partners:
- Transcription termination factor MTEF18, mitochondrial
- Pentatricopeptide repeat-containing protein At1g74850, chloroplastic
- PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic
- Plastid transcriptionally active 3
- Mitochondrial transcription termination factor-related / mTERF-like protein
- Photosystem II reaction center protein J
- DNA-directed RNA polymerase subunit alpha
- Rho-N domain-containing protein 1
- Large ribosomal RNA subunit accumulation protein YCED homolog 1, chloroplastic
- Mitochondrial transcription termination factor family protein
Sequence:
MVILSLVSCSFSVFSPPISLRLHLPPVTSLCSHGTFPASSTFRSQLQPLLISCLNHREPALTFRCSCLSSPIESGSQIESLFSLFRDIGFIEEETEMILAKNPDIKSTSLDKIGARVASLQSLKINGFPLQGLIAKCPNLLTSEEFDLVISFLVDELEGRLDPELVERLLSVVDTSILLSFNQKVRLLLLHGIPKEKISHVLNKVYLNKLLYQKSVEDIERLISFLEPFGGIGIIARRPVILNSDLDSQLIPRVDFIRNLSGEDDFATGTVLRRLPAILSYSVEHMNGQVEFLKSFAGLTSEQVFKIVHVFPNVISTSKERKLRPRIEFLKECGFDSPGMFKFLSKAPLILALSENNLSHKLGFLVKIGYKHRTKELAFAMGAVTRTSSDNMQRVIGLYLSYGLSFEDILAMSTKHPQVLQYNYTSLEEKLEYLIEYMGREVEELLAFPAFLGYKLDSRIKHRYEEKLKSRGENMSLNKLLTVSAERFSKAADNIEMICL
Protein: Cell wall-binding protein Fur (Q7A2F4)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Interaction partners:
Sequence:
MTVYTNTSLKAELNERGWRLTPQRETILHIFQELPQGEHLSAEDLYHRLEADGEGISLSTIYRTLKLMARMGILRELELGEGHKHYEINQPYPHHHHHLICVKCNSTIEFKNDSILKIGAKTAQKEGFHLLDCQMTIHAVCPKCQRALMPL
Protein: Interleukin-15 (IL-15) (P40933)
Organism: Homo sapiens (Human)
Function: Cytokine that plays a major role in the development of inflammatory and protective immune responses to microbial invaders and parasites by modulating immune cells of both the innate and adaptive immune systems. Stimulates the proliferation of natural killer cells, T-cells and B-cells and promotes the secretion of several cytokines. In monocytes, induces the production of IL8 and monocyte chemotactic protein 1/CCL2, two chemokines that attract neutrophils and monocytes respectively to sites of infection. Unlike most cytokines, which are secreted in soluble form, IL15 is expressed in association with its high affinity IL15RA on the surface of IL15-producing cells and delivers signals to target cells that express IL2RB and IL2RG receptor subunits. Binding to its receptor triggers the phosphorylation of JAK1 and JAK3 and the recruitment and subsequent phosphorylation of signal transducer and activator of transcription-3/STAT3 and STAT5. In mast cells, induces the rapid tyrosine phosphorylation of STAT6 and thereby controls mast cell survival and release of cytokines such as IL4 (By similarity).
Subcellular location: [Isoform IL15-S48AA]: Secreted.; SUBCELLULAR LOCATION: [Isoform IL15-S21AA]: Cytoplasm. Nucleus. Note=IL15-S21AA is not secreted, but rather is stored intracellularly, appearing in the nucleus and cytoplasmic components.
Interaction partners:
- Interleukin-2 receptor subunit beta
- Interleukin-15 receptor subunit alpha
- Cytokine receptor common subunit gamma
- Tyrosine-protein kinase JAK3
- Interleukin-2 receptor subunit alpha
- Interleukin-7 receptor subunit alpha
- Interleukin-9
- Interleukin-7
- Interleukin-2
- Tyrosine-protein kinase JAK1
Sequence:
MRISKPHLRSISIQCYLCLLLNSHFLTEAGIHVFILGCFSAGLPKTEANWVNVISDLKKIEDLIQSMHIDATLYTESDVHPSCKVTAMKCFLLELQVISLESGDASIHDTVENLIILANNSLSSNGNVTESGCKECEELEEKNIKEFLQSFVHIVQMFINTS
Protein: FI01124p (Promyelocytic leukemia zinc finger, isoform A) (Promyelocytic leukemia zinc finger, isoform B) (Q9VKC4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLHSQTMQSIPTLHQPLHSKVSNYLNNQRRTGQFCDLLLELDSDDSLSLSVHFCVLAAQSQFINSNQKQQQFSIHNPLKITIRNFSCTQCLHTIVDFFYEDLVSVSKEHELHFRELAQILAVTELLNLYQLQPLGEAKEATEIPAPGEAQPNPDPEKKAEAVFENRQSYFKLKNPRAVKSSSKVNYCIGCDFKCYQVQKMIEHMGSCEPSHLICSLCEVGFLDWREYDTHLRRHSGDLRKPFFCLQCGIRFNTRAALLVHQPKHSTETPHICPHCGKGFKWKQGLSNHILVHNPEKQMLCDVCGYSTTHMKALKSHKLLHTGEFFACTVSGCKHRANRKENLKLHIETHKQGRDFICEVCGCKFSQSKNLKRHALKHTENGPNRYKCQLCGFSSHRSDKMKEHVQRVHTEKPVQLELSETVDSSFPDDFELPVIETSPKKKPKSVKSKTIRNVNPDKRLKTLLPKETVE
Protein: Exopolyphosphatase (EC 3.6.1.11) (Q93Q73)
Organism: Serratia marcescens
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
Interaction partners:
Sequence:
MPLKNTATNKPQEIAAIDLGSNSFHMVIARVVNGALQVLGRLKQRVHLADGLDSNNVLSEEAIERGLACLALFAERLQGFPADNVTIVGTHTLRQAVNAEVFLKRAAKVIPYPIEIIAGQEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGEDFEPLLAESRRMGCVSFAQLFFPGGEISKNNFRRARLAAAQKLETLAWQYRIQGWQYALGASGTIKAAHEVLVAMGEKDGLITLDRLEMLAEQVLQFKSFGSLSLPGLSEDRQSVFVPGLAILCGVFDALAIRDLRLSDGALREGVLYEMEGRFRHQDIRSRTAKSLADHYNIDREQAKRVLETTELLYSQWMAQNTKLVHPQLEALLKWAAMLHEVGLSINHSGMHRHSAYILQNSNLPGFNQEQQLLLAALVRFHRKAIKLQELLRLNLFKKKHYLPLIQLLRLSTLLNNQRQSTTTPKTLRLTTDDNHWTLRFPAGYLAQNNLVQLDFEREQAYWNDVVGWKLLIDEEGSQDEQRSA