wanglab/gogpt-training-data huggingface dataset:
Protein: Protein SEY1 (EC 3.6.5.-) (Q9C0L9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization (By similarity). Required for virulence and resistance to cycloheximide.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER. Concentrated in punctae along the ER tubules. {ECO:0000255|HAMAP-Rule:MF_03109}.
Interaction partners:
- ADP-ribosylation factor GTPase-activating protein
- Protein YOP1
- Guanine nucleotide-exchange factor SEC12
- N-acetylglucosamine kinase 1
Sequence:
MELSEGELSHTSSSSSFVPVDQRQLQDAIQIIDENKHFNTGILDYINKTSPADVGNNYHIISVFGSQSTGKSTLLNRLFNTNFDVMDESNRQQTTKGIWLAYSPVVSTTLGHTTSKSNILVMDVEGTDGRERGEDQDFERKAALFALSTSEVLIINIWETQVGLYQGANMGLLKTVFEVNLSLFGKSKLETHNDHKVLLLIVIRDHVGVTPVESLAKTFTSDLQNMWSSLAKPAELEHLQFADFFDVTFHALNHKVLQPKEFGEGINRLDDRLVVSNELFKPEYHHDVPIDGWTMYAERCWEQIETNKDLDLPTQQILVAQFKCDEIVESVFQEFLAKYQHHFKEVDAAPDFEELGALFADLRQDAFEDYDASASRYNKAVYEQKRKKLRWLINDKLKEVFDVHAKNLCNTLLEKFEKDLVALKGKDFAVNVKTLSTKLVEDVNFQVSLMSLQGDLSLDEIILALTKDIDAIVAKQQVIELNSIVNKSVKKLSASLSKSIQFELGDPNEETWDNVLQQFKGVYEKFGGDFGLGTSSTQNQQAIEKFKFKSWCQFYDVTHKLISREKLLALLQDRFDDKFRYDENGLPKLYLNEQDLEKTFAVAKQHALQVLPILTFAKLADGSEIVPDYDIFDSKLREQFLGGYDDSDDEEDHCFAEIITEQEKSEVLAKFKKEVDAKYIETKRSIVQHITQIPYYIYLIILVLGWNEFMAIIRNPLFFSLSIVLGATVYVLYYLGLLRPALVVAQRTMDEVIVMAKTKLREVLIDDHEVTGRQLNKMAGSKENIELDDM
Protein: Histone H3.1 (P59226)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000269|PubMed:17439305, ECO:0000269|PubMed:25086063}. Chromosome {ECO:0000269|PubMed:17439305, ECO:0000269|PubMed:25086063}. Note=Localized at chromocenters. {ECO:0000269|PubMed:25086063}.
Interaction partners:
- Histone H4
- Protein TONSOKU
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4
- Histone H2B.6
- Protein SAWADEE HOMEODOMAIN HOMOLOG 1
- Chromo domain-containing protein LHP1
- Lysine-specific demethylase ELF6
- DNA
- Chromatin remodeling protein EBS
- Histone-lysine N-methyltransferase CLF
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVAALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Beta-D-xylosidase 4 (AtBXL4) (EC 3.2.1.37) (Q9FLG1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-D-xylosidase showing an optimal efficiency with the natural substrate xylobiose.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cellulose synthase-like protein D5
- Putative alpha-xylosidase 2
- Probable glucuronokinase 2
- Glucuronokinase 1
- Aldo-keto reductase family 4 member C10
- UDP-glucuronic acid decarboxylase 4
- Uncharacterized protein At2g41810
- Alpha-L-arabinofuranosidase 1
Sequence:
MGSSSPLTRRNRAPPSSVSSVYLIFLCFFLYFLNFSNAQSSPVFACDVAANPSLAAYGFCNTVLKIEYRVADLVARLTLQEKIGFLVSKANGVTRLGIPTYEWWSEALHGVSYIGPGTHFSSQVPGATSFPQVILTAASFNVSLFQAIGKVVSTEARAMYNVGLAGLTYWSPNVNIFRDPRWGRGQETPGEDPLLASKYASGYVKGLQETDGGDSNRLKVAACCKHYTAYDVDNWKGVERYSFNAVVTQQDMDDTYQPPFKSCVVDGNVASVMCSYNQVNGKPTCADPDLLSGVIRGEWKLNGYIVSDCDSVDVLYKNQHYTKTPAEAAAISILAGLDLNCGSFLGQHTEEAVKSGLVNEAAIDKAISNNFLTLMRLGFFDGNPKNQIYGGLGPTDVCTSANQELAADAARQGIVLLKNTGCLPLSPKSIKTLAVIGPNANVTKTMIGNYEGTPCKYTTPLQGLAGTVSTTYLPGCSNVACAVADVAGATKLAATADVSVLVIGADQSIEAESRDRVDLHLPGQQQELVIQVAKAAKGPVLLVIMSGGGFDITFAKNDPKIAGILWVGYPGEAGGIAIADIIFGRYNPSGKLPMTWYPQSYVEKVPMTIMNMRPDKASGYPGRTYRFYTGETVYAFGDGLSYTKFSHTLVKAPSLVSLGLEENHVCRSSECQSLDAIGPHCENAVSGGGSAFEVHIKVRNGGDREGIHTVFLFTTPPAIHGSPRKHLVGFEKIRLGKREEAVVRFKVEICKDLSVVDEIGKRKIGLGKHLLHVGDLKHSLSIRI
Protein: Non-specific serine/threonine protein kinase (H2KYA9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPVGNSGSRSGRLARISQSNIRPFGSNGGGATNSYGPGTHPMSGAEPCSPTKKEKHRFEITKKLGSGTYGKVSLAYDHKFDREVAVKLIKKSAIESKADLVRIRREIRIMSALNHPNIIQIYEVFENKDKIILVMEYSSGGELYDYVSRCGSLPEAEARRIFRQITSAVLYCHKHRVAHRDLKLENILLDQNNNAKIADFGLSNYFADKNLLTTFCGSPLYASPEIINGTPYKGPEVDCWSLGILLYTLVYGSMPFDGRDFNRMVRQIKRGAYFEPETPSTASMLIRNMLRVNPERRATIFDIASHWWLNLEENMPVIQELPENQIIDHTPLTEREETMIVQDLADEQDVFMEFGHLSSETRRKIEDFRIRRKEAEEFNDNSPVKPPKARKTDELTGKISKEQPEEMKSAEKSLRGVKEEKEKPKVVDPNDPLERLRQIENRLGQNKKDKEAAKTSARVETVKLKEVKKEKSPEQQPEDPKTARGTSKPADSRAPSFVPVKDRPETSEPERPRTRPHLTASAYRIETDSLNMLMNQVLEQMEKGPVNLNIIARIKAHPLYDTRPMVKELLESIIAAQPEPVQKQTSKVVEQQTFSRQNTLTRKKKEDPLEEEIPEVPSPSRKMKERPWHSVEVGFDPDEEPEHDRMQESIASNATEVTVQDTSFEDDSSDEEERKKTPVASTPKTPVLIVEKQESSTNAEDEESDEGDDYSDAEMEELADEVDKKGPSDSKLAPVVENLEANPPPDPSSSPQFLDAFDRGLIKRQSKGKYQHTLINNYGRGVSTECESPTQQRKFFGGPQPSAELSPFLFDKAKEILQTYPNNKLDARGIDVELRRKLRMEKVKADLLKQPKDGDKPRNSYVGSVPPRSPPPIVVKSDGEELDDEEEEEEDEEEIEETDSEEGSDFENFKPKRPIIAAVRRDDGAVVPVIHQTTRPAVVSPNSQNPRYQVASPKTSTVIQATPEKVPVAGTSAKYLVTVAELKLKPTDKKEEAQLKEQLKDSEINSERKTSQTNLLFRPSAYRESDLYRRINAALERPSVDPYDDRAFSPLSTDPFYSHHSSGSAAPSALGYVRPRYHDDSYRTHRDSDYRPMSPTSRYTAAVTRDDRGKSTSYDPHETTRPSYDRGYITSSNASPSYTRKFEHEQPTLNSWANDRKFEVYKTRAERDAERNTYHPTGTTGASSYRPSSYYTSASDRPVTGLRRPEESYTSSTNYGRYDGRSTTPSNDQYAISTALAENQASSMNNRFRPTARRVASAMTDADRRNYHRSRSMDRNKVDYEYGSNLLNRLTTPDSHGDYSYVNYHDSSNGRSNITLEKDGQPRSILKNKQSADIEPRVESSYEPSNGVRSHEFLDQLLSMRFILQVFERLRRHLSLEKSVSPQRQNTSFYGRQLRVASVGPHSRNIDSTSSALDNPKKKRSLLSFNRRKTSEVRMGADGKLVTNGYDSTPSSRDFKRPSSPIDRIKSLFRKNESSGTGHSDYYNSSRNYTSSNPVSTTREPYVAQYRKYPGSTSRDTSSALNRYSYTPGLTDQRRHWYDDPNIY
Protein: Glycoprotein (Q4VCP5)
Organism: Nipah virus
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004336}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004336}. Virion membrane {ECO:0000256|ARBA:ARBA00004208}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004208}.
Interaction partners:
Sequence:
MPTESKKVRFENTASDKGKNPSKVIKSYYGTMDIKKINEGLLDSKILSAFNTVIALLGSIVIIVMNIMIIQNYTRSTDNQAMIKDALQSIQQQIKGLADKIGTEIGPKVSLIDTSSTITIPANIGLLGSKISQSTASINENVNEKCKFTLPPLKIHECNISCPNPLPFREYKPQTEGVSNLVGLPNNICLQKTSNQILKPKLISYTLPVVGQSGTCITDPLLAMDEGYFAYSHLEKIGSCSRGVSKQRIIGVGEVLDRGDEVPSLFMTNVWTPSNPNTVYHCSAVYNNEFYYVLCAVSVVGDPILNSTYWSGSLMMTRLAVKPKNNGESYNQHQFALRNIEKGKYDKVMPYGPSGIKQGDTLYFPAVGFLVRTEFKYNDSNCPIAECQYSKPENCRLSMGIRPNSHYILRSGLLKYNLSDEENSKIVFIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWDTMIKFGDVQTVNPLVVNWRDNTVISRPGQSQCPRFNKCPEVCWEGVYNDAFLIDRINWISAGVFLDSNQTAENPVFTVFKDNEVLYRAQLASEDTNAQKTITNCFLLKNKIWCISLVEIYDTGDNVIRPKLFAVKIPEQCT
Protein: Aconitate hydratase A (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (Iron-responsive protein-like) (IRP-like) (Probable 2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (RNA-binding protein) (Q8NQ98)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein (By similarity).
Interaction partners:
- Citrate synthase
- Isocitrate dehydrogenase
- Isocitrate lyase
- acetolactate synthase
- 2-methylcitrate synthase 1
- 2-methylcitrate synthase 2
- Succinate dehydrogenase/fumarate reductase, flavoprotein subunits
- 2-oxoglutarate dehydrogenase E1/E2 component
- Superoxide dismutase
- 3-hydroxyisobutyryl-CoA hydrolase
Sequence:
MTESKNSFNAKSTLEVGDKSYDYFALSAVPGMEKLPYSLKVLGENLLRTEDGANITNEHIEAIANWDASSDPSIEIQFTPARVLMQDFTGVPCVVDLATMREAVAALGGDPNDVNPLNPAEMVIDHSVIVEAFGRPDALAKNVEIEYERNEERYQFLRWGSESFSNFRVVPPGTGIVHQVNIEYLARVVFDNEGLAYPDTCIGTDSHTTMENGLGILGWGVGGIEAEAAMLGQPVSMLIPRVVGFKLTGEIPVGVTATDVVLTITEMLRDHGVVQKFVEFYGSGVKAVPLANRATIGNMSPEFGSTCAMFPIDEETTKYLRLTGRPEEQVALVEAYAKAQGMWLDEDTVEAEYSEYLELDLSTVVPSIAGPKRPQDRILLSEAKEQFRKDLPTYTDDAVSVDTSIPATRMVNEGGGQPEGGVEADNYNASWAGSGESLATGAEGRPSKPVTVASPQGGEYTIDHGMVAIASITSCTNTSNPSVMIGAGLIARKAAEKGLKSKPWVKTICAPGSQVVDGYYQRADLWKDLEAMGFYLSGFGCTTCIGNSGPLPEEISAAINEHDLTATAVLSGNRNFEGRISPDVKMNYLASPIMVIAYAIAGTMDFDFENEALGQDQDGNDVFLKDIWPSTEEIEDTIQQAISRELYEADYADVFKGDKQWQELDVPTGDTFEWDENSTYIRKAPYFDGMPVEPVAVTDIQGARVLAKLGDSVTTDHISPASSIKPGTPAAQYLDEHGVERHDYNSLGSRRGNHEVMMRGTFANIRLQNQLVDIAGGYTRDFTQEGAPQAFIYDASVNYKAAGIPLVVLGGKEYGTGSSRDWAAKGTNLLGIRAVITESFERIHRSNLIGMGVVPLQFPAGESHESLGLDGTETFDITGLTALNEGETPKTVKVTATKENGDVVEFDAVVRIDTPGEADYYRHGGILQYVLRQMAASSK
Protein: Uncharacterized protein (Q83A08)
Organism: Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Interaction partners:
Sequence:
MNDDEKKKLLEAYQNAVLIEPPKELPPIFVTPQTSDEPLQNLAITLSAFPIENRGGVQVFEVPKIADDCRSYVGRGYDAYEDTAAKGPQGPAWKPDSTWVKLESIEDFACRKGFEKVYVYEGHHYARQWGDGTILEKLGSTHWGATPVVRLIDPHALIVKKYYGEVKEIWIRPYLHGSVPIPYLRAQSSYRRGPFGNYHLFKSVYKKEIVIQKMTKDDWEPHYQWAKKEQQRQQQATAQFFKPQEEKQQESKKFINSFLVRLCEVLRIFISDENREPRKIDPS
Protein: Plantazolicin (PZN) (Plantazolicin A) (Plantazolicin B) (cpd1335) (D3VML5)
Organism: Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum)
Function: Peptide antibiotic inhibiting growth of Gram-positive bacteria in the dimethylated form plantazolicin A. The desmethyl form plantazolicin B has no antibiotic activity. The mode of action appears to be disruption of cell walls and lysis of cells. Inhibits B.subtilis strain HB0042, B.megaterium strain 7A1 and B.anthracis (MIC=2-4 ug/ml). Weakly inhibits Gram-positive bacteria B.brevis strain ATCC 8246, B.subtilis strain 168, B.cereus strain ATCC 14579 and strain CU1065, B.licheniformis strain ATCC 9789, M.luteus, B.sphaericus, P.granivorans and S.pyogenes (MIC=128 ug/ml). Does not inhibit B.pumilus, P.polymyxa, Arthrobacter sp., S.aureus, vancomycin-resistant E.faecalis, L.monocytogenes, methicillin-resistant S.aureus or Gram-negative bacteria E.coli strain K12, K.terrigena, Pseudomonas sp. and E.carotovora.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:20971906, ECO:0000269|PubMed:21950656}.
Interaction partners:
Sequence:
MTQIKVPTALIASVHGEGQHLFEPMAARCTCTTIISSSSTF
Protein: Topoisomerase 1-associated factor 1 (P53840)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms a fork protection complex (FPC) with CSM3 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors and protects stalled replication forks against the fork-releasing activity of RRM3 helicase.
Subcellular location: Nucleus {ECO:0000269|PubMed:12944972, ECO:0000269|PubMed:14562095}. Note=Associated with chromatin during S phase.
Interaction partners:
- Chromosome segregation in meiosis protein 3
- DNA replication licensing factor MCM4
- Cell division control protein 45
- DNA polymerase alpha-binding protein
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM3
- Mediator of replication checkpoint protein 1
- Minichromosome maintenance protein 5
- DNA replication complex GINS protein SLD5
Sequence:
MSADLQQGTTNAADFSLTVLRARIALLATAIGGPDYTSQIDPPPYKLGDDCLACLKDLKRWFKLVDDQQKRWDVAMAVAEYRILTDDLLPILIDWENKCSLAAKLAKNNPDHEEFRNKAYYDKIALNCLQLLVLMTWPLIVTEQSSSNQITLYGELKKHQLVYKKTILSMESGKVLRAAIRLALDVIKIDRLSRTPRDNMVLKLVLNFFRNVIAIEPGEFTINTKKSMPKKGITSIDTLPPNVSMDDISLNTVISSFHKNKVFGFLLTLTSSLSKEFDQDFINIPLLEIMFYFTKDVNQELLFPRQFETGTHSKVVNKNESSSANNIVTSAGFELSKLLQKEHQMRKNVIKHTSARHSRFGGLLSIQTPDKTRLTVSGSQALVDEKIALQKLDDSKKWNKRIIKKHQSVAAEGLPNSLLNSQTGKAIFFTESNGKHFKEFINNFIDSGFNILLHSVTNYFTTEQDRMVTLEQVEYLLFFAWFVKYQLLRSKIDNSADIKQVSEALKEVTFILVSSLLRSAYDLKNWTVTHAGMIAFNELLNLVSRTKAAQEEDSTDIEFIVSRLFSDERIQLLSNLPKIGSKYSLQFMKSCIELTHSVLKVLEQYSDDKTLVIEGKSRRQKKFNISEGDITKLIEEENVDRDEALDILTSSLRSIEVNFQKVQANYMTEPVIETYINFLERFRELEDDSIKKVFSFFHRVFVQAKEQALLFRFDLIILLREMLSPDGLDRMSRSRKYVSQFSDYFLARLKKRLKKSPAWFVGLLFPPLHNSEVGFYQRYGEYNVLNNESMYAAPASQFKPIPDEEALPPSILLDMKYGVLVSTLLDDGKTELLDQLLKHITHTLDIFKSWLTVNVNAGKETVNPPNEYFTLTGVLNNDPIFKDKDYRALLLLIGYSIPRKINEPCFLPGTVEVSDLTVSCELVKKYLSTPFETPNGLPSSSYLLRVRSEKDSFSHNEQDGWEGDDDYDYNDPYIVPDDQILSKSDAAYFKDLDNNASDKLKGTKFSKGIARSKKKDKRKRRKGEAKTNLPMFGDQDDERPQTVRERHGVFSKEFISDSEDDEDLMNPIFFENETYMRWLLDKNNGQLTEDRYIQFAKFAAERMNNGGVVTGDYTSLFGGSIPSIESIRATESSSFAPDKSLISLASHVASEMSIFDVNNNNNNQLSDDDVNSESRNSLGSSQPSNSQNMFQSEVYSRKESTKRSLEASAADESDEDEEAIRLFGKKSRVVLSQGDSDD
Protein: Protein SMAX1-LIKE 2 (AtSMXL2) (Q9M0C5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of a transcriptional corepressor complex that acts specifically in the karrikin pathway. Controls seedling growth redundantly with SMAX1, but is not involved in leaf morphology, shoot branching or germination control.
Interaction partners:
- F-box protein MAX2
- Probable esterase KAI2
- F-box/kelch-repeat protein SKIP25
- Strigolactone esterase D14
- Alpha/beta-Hydrolases superfamily protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- RNA polymerase II C-terminal domain phosphatase-like 5
- ATP-dependent Clp protease adapter protein CLPS1
- 2-oxoglutarate
- Carotenoid cleavage dioxygenase 8, chloroplastic
Sequence:
MRADLITIQQTLTPEAATVLNQSIAEATRRNHGHTTPLHVAATLLSSSSGYLRQACIKSHPNSSHPLQCRALELCFSVALERLPTTSTTTTTTSSSSSSSPSQTQEPLLSNALTAALKRAQAHQRRGCPEQQQQPLLAVKVELEQLIISILDDPSVSRVMREASFSSPAVKSAIEQSLIGNSVSNSRQTGSPGIINPSAIGFGYRSVPAPVNRNLYLNPRLQQPGVGMQSGMMIQRTDEAKRVIEIMIRTRKRNPVLVGDSEPHILVKEILEKIENGEFSDGALRNFQVIRLEKELVSQLATRLGEISGLVETRIGGGGVVLDLGDLKWLVEHPAANGGAVVEMRKLLERYKGRLCFIGTATCETYLRCQVYYPSMENDWDLQAIPIAAKSSLPAIFPRLGSNNNNNAMLLSNNIISIESISPTRSFQIPMSKMSCCSRCLQSYENDVAKVEKDLTGDNRSVLPQWLQNAKANDDGDKKLTKDQQIVELQKKWNDLCLRLHPNQSVSERIAPSTLSMMKINTRSDITPPGSPVGTDLVLGRPNRGLSSPEKKTREARFGKLGDSFDIDLFKKLLKGLAKSVWWQHDAASSVAAAITECKHGNGKSKGDIWLMFTGPDRAGKSKMASALSDLVSGSQPITISLGSSSRMDDGLNIRGKTALDRFAEAVRRNPFAVIVLEDIDEADILLRNNVKIAIERGRICDSYGREVSLGNVIIILTANSSLGSAKNVASIDETRLESLVNKGWELRLSVCNSSKTRKRKPNWLYSDNDQTKQRKEICFDLNEAAEFDSSSDVTVEHDQEDNGNLVHKLVGLVDDAILFRPVDFDSIKSKTAESLKKRFSNGLADGLTVEIEDDALERIAGAIWLSKISLEEWLEEAMGSSLNSVKSRVSSSEDSVIRIELEDDLNDRISGGYLPSSIRTVVV
Protein: Coronin-6 (Coronin-like protein E) (Clipin-E) (Q6QEF8)
Organism: Homo sapiens (Human)
Interaction partners:
- Coronin-1B
Sequence:
MSRRVVRQSKFRHVFGQAAKADQAYEDIRVSKVTWDSSFCAVNPKFLAIIVEAGGGGAFIVLPLAKTGRVDKNYPLVTGHTAPVLDIDWCPHNDNVIASASDDTTIMVWQIPDYTPMRNITEPIITLEGHSKRVGILSWHPTARNVLLSAGGDNVIIIWNVGTGEVLLSLDDMHPDVIHSVCWNSNGSLLATTCKDKTLRIIDPRKGQVVAEQARPHEGARPLRAVFTADGKLLSTGFSRMSERQLALWDPNNFEEPVALQEMDTSNGVLLPFYDPDSSIVYLCGKGDSSIRYFEITDEPPFVHYLNTFSSKEPQRGMGFMPKRGLDVSKCEIARFYKLHERKCEPIIMTVPRKSDLFQDDLYPDTPGPEPALEADEWLSGQDAEPVLISLRDGYVPPKHRELRVTKRNILDVRPPSGPRRSQSASDAPLSQQHTLETLLEEIKALRERVQAQEQRITALENMLCELVDGTD
Protein: Protein phosphatase PP2A regulatory subunit B (Cell division control protein 55) (PR55) (Q00362)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates.
Interaction partners:
- Separin
- Nucleolar protein NET1
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Kinetochore protein SLK19
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Cyclin-dependent kinase 1
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
- Protein phosphatase PP2A regulatory subunit A
- Mitosis inhibitor protein kinase SWE1
- Securin
Sequence:
MAQNNFDFKFSQCFGDKADIVVTEADLITAVEFDYTGNYLATGDKGGRVVLFERSNSRHCEYKFLTEFQSHDAEFDYLKSLEIEEKINEIKWLRPTQRSHFLLSTNDKTIKLWKVYEKNIKLVSQNNLTEGVTFAKKGKPDNHNSRGGSVRAVLSLQSLKLPQLSQHDKIIAATPKRIYSNAHTYHINSISLNSDQETFLSADDLRINLWNLDIPDQSFNIVDIKPTNMEELTEVITSAEFHPQECNLFMYSSSKGTIKLCDMRQNSLCDNKTKTFEEYLDPINHNFFTEITSSISDIKFSPNGRYIASRDYLTVKIWDVNMDNKPLKTINIHEQLKERLSDTYENDAIFDKFEVNFSGDSSSVMTGSYNNNFMIYPNVVTSGDNDNGIVKTFDEHNAPNSNSNKNIHNSIQNKDSSSSGNSHKRRSNGRNTGMVGSSNSSRSSIAGGEGANSEDSGTEMNEIVLQADKTAFRNKRYGSLAQRSARNKDWGDDIDFKKNILHFSWHPRENSIAVAATNNLFIFSAL
Protein: Probable cytochrome P450 508B1 (EC 1.14.-.-) (Q54SK0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLFNIFLYLFIFCIVSSGIKKYKKIHKNELSGPFPIPLLGNLHQLGKEPHYTLTKMHNVYGEIFRLHFGDVYTVVVSDPILIREMFVDNHENFKYRPLLPTFKFGAGGDHGLSLSNERWERTRELVQNAMKRTSIKKIYDMLDSQVYELIKSMKQYQVTGNPFEIHLYAQRFTLSIMFKYIFNEDISYDEDITKGKIAELVQPMDQIFKSLGSGKLGDFISIAQPFYYQWLKFSDKQFNGPFSTVKKFIYKRYLEHINTIDHDNPRDLMDLLINEFSNDKNLIPTILQTSLDMFLAGNDTTAASIIWFVLRMQEHPEIQLKAYNEIKDAVGDRDRVLLSDRPKTPYLNAIIKEILRLNPVGPFGLPHRSSNDIVIGNGKYFIPKDSQILVNYRGLGFNEKYFENPSQFDPSRFLNKNNDAYMPFGVGDRKCVGLQLAGDEQYLSFSNILLNFNLKNIGTPVSDYEEFGLTLKPNKFKVLLESRK
Protein: AP-2 complex subunit alpha (Alpha-adaptin) (Clathrin assembly protein complex 2 alpha large chain) (Clathrin assembly protein large alpha chain) (Q9C0W7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Alpha adaptin is a subunit of the plasma membrane adaptor (By similarity).
Subcellular location: Cell membrane {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- AP-2 complex subunit beta
- Probable clathrin heavy chain
- Uncharacterized calcium-binding protein C800.10c
- AP-1 complex subunit beta-1
- Clathrin light chain
- AP-3 complex subunit beta
- AP-1 complex subunit sigma-1
- AP-3 complex subunit mu
Sequence:
MVASNNMKGLRAFISDLRSLEHDDEEKRVNVELAKIRAKFQSSTLSAYDRKKYVSKLLYIYMLGYPITFGHMEAAKLLSGTKYSEKLIGYLAVALLLNENHELMKLVINSIKKDLLSHDSLQNSLALHTIANIGGRELCETVYYDIYKLLMSASNENIVRQKSALALLHIYRKFPDLINPEWFEPIVMILGDDDLNVSLAVSNFVNLIVIREPKYQKFAYGKAVGKLKNIVFEHGYSSDYLYYSVPCPWLQVNLCRILLACERPSDNPTRATLIRVLDRILSLPNDNSNVQQVNAVNAILFEAIKLAFLVDESHSLYEKCMDRLADMIADKESNIRYLAFETTAYLISCGHSITSLKHYKELILSSLRYKDVSLRKKSLELLYMMCDEENAKLIVADLLQYLPHLDSVTQEDLISKVAIISETFATDYEWYVDVTIQLLRIAGKSADDGVWHQLVHVIVNNEEIQEYATKRLFSLLQSETIHECLVKAGGYVLGEFGHLITDYPDSQPVHQFSTIYRKLNVSSPSTRVLLLTTLIKLANLQPELNDRIAKVFQEYSTIINPEVQQRACEYLQLLKMPRDFLQLVCDEVPPFLDGNRDGVHPKSRPSSKVNLVDTYPQTIPNVSKPSTPIDVPEYDISACLPGFYRLCWKDKGILYQDSQIQIGVRSEYHNSEGAIYLYYENRQSNTLKSLSSTLIRTFSTFHLATTFQDTNLPSGVQLQQKYVMSGVNEIFEPPIIHVSYVTGVIRSIDLQLPVLLSKFMKPTIFDSYDFFNHWGQMGVEREAQLTFGLNSKDRKLDAKRLTKIVSGFHWGICQNVDSIALNIVGAGIIRFGTQNVGCLLRIEPNYEQNLIRLSIRSTNTSIANTLAKEMQEILRNSF
Protein: Tyrosine-protein phosphatase Lar (EC 3.1.3.48) (Protein-tyrosine-phosphate phosphohydrolase) (dLAR) (P16621)
Organism: Drosophila melanogaster (Fruit fly)
Function: Possible cell adhesion receptor (Probable). It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). It controls motor axon guidance. In the developing eye, has a role in normal axonal targeting of the R7 photoreceptor, where it negatively regulates bdl. Inhibits bdl cell adhesion activity in vitro; this effect is independent of its PTPase function.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Dally-like, isoform A
- Liprin-alpha, isoform E
- Syndecan
- Insulin-like receptor
- Tyrosine-protein kinase Abl
- Kekkon 5, isoform A
- FI03228p
- Neural-cadherin
Sequence:
MGLQMTAARPIAALSLLVLSLLTWTHPTIVDAAHPPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEPVRAGRDDAPYECVAENGVGDAVSADATLTIYEGDKTPAGFPVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSKATNLYVKVRRVPPTFSRPPETISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNVLQLINIQESANYTCIAASTLGQIDSVSVVKVQSLPTAPTDVQISEVTATSVRLEWSYKGPEDLQYYVIQYKPKNANQAFSEISGIITMYYVVRALSPYTEYEFYVIAVNNIGRGPPSAPATCTTGETKMESAPRNVQVRTLSSSTMVITWEPPETPNGQVTGYKVYYTTNSNQPEASWNSQMVDNSELTTVSELTPHAIYTVRVQAYTSMGAGPMSTPVQVKAQQGVPSQPSNFRATDIGETAVTLQWTKPTHSSENIVHYELYWNDTYANQAHHKRISNSEAYTLDGLYPDTLYYIWLAARSQRGEGATTPPIPVRTKQYVPGAPPRNITAIATSSTTISLSWLPPPVERSNGRIIYYKVFFVEVGREDDEATTMTLNMTSIVLDELKRWTEYKIWVLAGTSVGDGPRSHPIILRTQEDVPGDPQDVKATPLNSTSIHVSWKPPLEKDRNGIIRGYHIHAQELRDEGKGFLNEPFKFDVVDTLEFNVTGLQPDTKYSIQVAALTRKGDGDRSAAIVVKTPGGVPVRPTVSLKIMEREPIVSIELEWERPAQTYGELRGYRLRWGVKDQALKEEMLSGPQMTKKRFDNLERGVEYEFRVAGSNHIGIGQETVKIFQTPEGTPGGPPSNITIRFQTPDVLCVTWDPPTREHRNGIITRYDVQFHKKIDHGLGSERNMTLRKAVFTNLEENTEYIFRVRAYTKQGAGPFSDKLIVETERDMGRAPMSLQAEATSEQTAEIWWEPVTSRGKLLGYKIFYTMTAVEDLDDWQTKTVGLTESADLVNLEKFAQYAVAIAARFKNGLGRLSEKVTVRIKPEDVPLNLRAHDVSTHSMTLSWSPPIRLTPVNYKISFDAMKVFVDSQGFSQTQIVPKREIILKHYVKTHTINELSPFTTYNVNVSAIPSDYSYRPPTKITVTTQMAAPQPMVKPDFYGVVNGEEILVILPQASEEYGPISHYYLVVVPEDKSNLHKIPDQFLTDDLLPGRNKPERPNAPYIAAKFPQRSIPFTFHLGSGDDYHNFTNRKLEREKRYRIFVRAVVDTPQKHLYTSSPFSEFLSLDMREAPPGERPHRPDPNWPAEPEVSVNRNKDEPEILWVVLPLMVSTFIVSTALIVLCVVKRRRQPCKTPDQAAVTRPLMAADLGAGPTPSDPVDMRRLNFQTPGMISHPPIPISEFANHIERLKSNDNQKFSQEYESIEPGQQFTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIICGVTEVPARNLHTHLQKLLITEPGETISGMEVEFKKLSNVKMDSSKFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYLGSFDNYTN
Protein: GH08630p (Kctd12-like, isoform A) (Kctd12-like, isoform B) (Q9VDH3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Calbindin-32
Sequence:
MPEIIELNVGGVSYTTTLATLLQDKSTLLAELFGEGRDSLAKDSKGRYFLDRDGVLFRYILDFLRDKALHLPEGFRERQRLLREAEHFKLTAMLECIRSERDARPPGCITIGYRGSFQFGKDGLADVKFRKLSRILVCGRVAQCREVFGDTLNESRDPDHGGTDRYTSRFFLKHCYIEQAFDNLHDHGYRMAGSCGSGTAGSAAEPKPGVDTEENRWNHYNEFVFIRD
Protein: Non-specific lipid-transfer protein EPAD1 (Protein EXINE PATTERN DESIGNER 1) (Q75GY0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Plant non-specific lipid-transfer protein that binds phospholipids in vitro. Required for correct pollen exine patterning by controlling the continuity and homogeneity of the primexine distribution.
Subcellular location: Cell membrane {ECO:0000269|PubMed:33093144}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:33093144}. Note=Localizes to the microspore plasma membrane. {ECO:0000269|PubMed:33093144}.
Interaction partners:
Sequence:
MERSHLAVLLGLLAFAAGVPAAAAATAVEGAQAATAEASCEPSILATQVSLFCAPDMPTAQCCEPVVASVDLGGGVPCLCRVAAEPQLIISGLNATHLLTLYAACGGLRPGGARLAAACEGPAPPASIVTAPPPPVAFRRKPPAREAPPPPPAAEKLSPPPQQHDDSDHNKRVGPLPRGSPPPYAQSVPVGPAAAPPPPRSGASSSLQAPLAATTTIVAITLIAAAQY