wanglab/gogpt-training-data huggingface dataset:
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 (BRG1-associated factor 57) (BAF57) (Q56A18)
Organism: Rattus norvegicus (Rat)
Function: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Required for the coactivation of estrogen responsive promoters by SWI/SNF complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1
- PHD finger protein 10
- AT-rich interaction domain 1A
- AT-rich interactive domain-containing protein 2
- Bromodomain containing 7
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
- AT-rich interaction domain 1B
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1
- Protein polybromo-1
Sequence:
MSKRPSYAPPPTPAPATASSGITIPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQGSIAPEEEQVANKAEEKKDEENIPMETEETHLEDTAENQQNGEEGTSTPEDKESGQEGVDSMEVEGTSDSNTGSESNSATVEEPPTDPVPEDEKKE
Protein: Uncharacterized protein (Q83ED7)
Organism: Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Interaction partners:
- Hypothetical cytosolic protein
- Uncharacterized protein
- Hypothetical cytosolic protein
- Hypothetical cytosolic protein
- Putative ankyrin repeat protein CBU_0781
Sequence:
MRSWLSLQAIEKLDKKQAGEVVFSGIIEQLKKLEEFSGTKVIRFEDRERGKNKNQAEIQTKTDFAEKMGDLVRCCALAADFLYNPDQLKVVTHQAKLCLMTFVEVDKDKLKTQRLNEVKASINEIVETHFDPQSPPLIYWAIRLGDADFFLYLLNNFSPALSSKDLNFEIPEGLYFDIITEIFRYSSVDFYNAVKETIEEEQRKKTYLWKGTGVPFINALQMQNVELAFHLINELSSDDYQRHLSYPGIYPVVSLFVGKKTSLYHHRGKRRFSAMMTTLMQSIDLESGLSRIEVVNRILIKNLKTMTIIGIEPKAKDAIHPFIQWLKFLEKNKSLPLCRIYIIDLYYLSSESKDNAVAKPLDSYLEMIIFFDQLIAQKTVSKFEASVLERLRGFFINQLKSIIETNNQLAHLQLYCKLRGYDSYPIIQSLFQNEAGIEIQRPIIFNYQEEFEIDFTNPVNFIRSLHQLVQNRQFEENDKKEKRCSKDEMAFEILEQLKKYRLLNEGRGLRELEDNINLVCYPENHLEETQPKLLIFLAIDLQSVELFKFLLEFNPCLKNITSYFLERCDSIETYRKFSEIFNELSNQHGNDYCLDECNLEDGRIPLTVLLSRPTVNIPLLKYYINHLDSGYYESQLHLQGRDYAHPPLMLALCHLKTISLVDLVSEKYSLSAIFNMAIEFVLKEDSNRDLVQLLQKMLSRAQLSTLISNSFEAGIEHYYNLERKKDPEKFFQYKEKILGSKATLIMQNGSRSFALLSIEETALQFIQYFYSAQNEISFGKKKSSIKKSIFQKVKGGVKSTIATLIDQLATPGTVETAELRLRHILEFYFVLCTFADNTGDHAPRESEKEICTQMSQGYLYFFDDLSPQQSQRLYELLNDNGYLLLAGADVLLDRLKPPALYEEKESDVELKTIKMQEKVEEKKPSKKVKIKKSKPKKKKITKNNQSENLVNLPLCSTVPEKQAYEEEQKQEAIGQQGFIHKLRNIERELHQLRSFENNEFLEKQIVLFKSIIERVKALVSVDKDENDNKASPTSRNFSTNLWDQLVHQWNCAVSTFAEEIKSTDVKLCEELCCCHMPNEINFEADYHNRQAIFELFSEIKKVEIAEVGSRIFTRKFPPLKKADNDYVLYLDPNLMKNFDEKVTEIANQLKAKNIKHTVKRGQLLAQNGKPFMYAKICVHFDQGNAETLEVDLTITTAAPQQDLKPRWLNLGAERISDKGGWALPPNGYNEIFASEPVKIRFTVPFGDIVAAPLFMTLNRLGYCFRMFAKVFSLPIEVELPPEWLAYQNDEKNRETVSKAIRAALCKVNCSSMGMLNYLRQTGFCDLSTLTVEEEADSEALRKALCELFRPSACSTVACSTVSFFGSKEHSYSSDTNSENERKIERKVNFEKS
Protein: LexA repressor (EC 3.4.21.88) (P0DN68)
Organism: Fibrobacter succinogenes (strain ATCC 19169 / S85)
Function: Probably represses a number of genes involved in the response to DNA damage (SOS response), including itself, recA, uvrA, ruvAB and ssb. The probable consensus LexA box is 5'-TGCAC-N4-GTGCA-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair (Probable).
Interaction partners:
Sequence:
MENTNEKRKEMTARQEEIYEYIKKYSKENHMPPTVREIGNHFDISSTNGVRSILAALIKKGYINRSPRLSRGIEILSDDKESSKEVASNTIEIPIVGRVAAGTPILAVQNLEGTVTIDRDFLACRSDVFALRVKGDSMINAGIFDGDLIFARQQKTADLGEIVVAQIDNEATVKYYHPSADHVELRPANPKYKPIIVNNRKDFSIAGRVIGVMRKVN
Protein: Complex I assembly factor TIMMDC1, mitochondrial (Translocase of inner mitochondrial membrane domain-containing protein 1) (TIMM domain containing-protein 1) (Q8BUY5)
Organism: Mus musculus (Mouse)
Function: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex assembly factor 4
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- Complex I assembly factor TMEM126B, mitochondrial
- Complex I intermediate-associated protein 30, mitochondrial
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Complex I assembly factor ACAD9, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
Sequence:
MGAPPPAPRSRLCGAWGPFPRVFAAGAVAADSPGFVEDREQRSGVSDPGSLESGWDRLRQLFAKDEQQRFSKEIDYIYRAAVSAGIIGWAYGGIPAFIYAKKRYIEQSQAEIYHNRFDAVQSAHRAATRGFIRYGWRWSWRTAVFVTIFNTVNTGLTVYRNKDAMSHFAIAGAVTGGLFRINLGVRGLVAGSIIGALLGAPMGSLLMALEKYSGETVQERRQKEWKALHEQRLEEWRSSLQVTELLPMEIESGLEKIQPEGDAQRIEELLSLPRNPSSPHQQSKH
Protein: Adenosine receptor A2b (P29276)
Organism: Rattus norvegicus (Rat)
Function: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Adenosine receptor A2a
- Neuroendocrine secretory protein 55
- Guanine nucleotide-binding protein G
- Adora3 protein
- Guanine nucleotide-binding protein G
- Ectonucleoside triphosphate diphosphohydrolase 1
- 5'-nucleotidase
- Ectonucleoside triphosphate diphosphohydrolase 1
- Adenosine deaminase
Sequence:
MQLETQDALYVALELVIAALAVAGNVLVCAAVGASSALQTPTNYFLVSLATADVAVGLFAIPFAITISLGFCTDFHSCLFLACFVLVLTQSSIFSLLAVAVDRYLAIRVPLRYKGLVTGTRARGIIAVLWVLAFGIGLTPFLGWNSKDRATSNCTEPGDGITNKSCCPVKCLFENVVPMSYMVYFNFFGCVLPPLLIMMVIYIKIFMVACKQLQHMELMEHSRTTLQREIHAAKSLAMIVGIFALCWLPVHAINCITLFHPALAKDKPKWVMNVAILLSHANSVVNPIVYAYRNRDFRYSFHRIISRYVLCQTDTKGGSGQAGGQSTFSLSL
Protein: Amastin (Q585J8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Trypanosoma glutamic acid/alanine-rich protein domain-containing protein
Sequence:
MLCCGCLTILMTLLGASTSVCTIIFPVFRMKNETKEAIQTLWYYMEKTASTESKTSVRESECYEYSVYFQVSMGAVAAAAAVGLISLLFLCGVVACGKKMKHLKAVSLSLVFFSLLGAITCIGLVTLGYLRGYCQGDPKLRDKYAPFKERGFKIDVGSYLLCAAVALYLLTTITHCCL
Protein: Glycine cleavage system H protein (P0A6T9)
Organism: Escherichia coli (strain K12)
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Interaction partners:
- Aminomethyltransferase
- Glycine dehydrogenase
- Lipoate-protein ligase A
- Dihydrolipoyl dehydrogenase
- Serine hydroxymethyltransferase
- Lipoyl synthase
- Octanoyltransferase
- Bifunctional protein FolD
- Bifunctional protein PutA
- Glutamate synthase large chain
Sequence:
MSNVPAELKYSKEHEWLRKEADGTYTVGITEHAQELLGDMVFVDLPEVGATVSAGDDCAVAESVKAASDIYAPVSGEIVAVNDALSDSPELVNSEPYAGGWIFKIKASDESELESLLDATAYEALLEDE
Protein: Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin) (Q8BG40)
Organism: Mus musculus (Mouse)
Function: Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. The function in regulating microtubule dynamics at spindle poles seems to depend on the association of the katanin KATNA1:KATNB1 complex with ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM blocking activity on microtubule minus-end growth. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BVA0}. Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9BVA0, ECO:0000255|HAMAP-Rule:MF_03022}.
Interaction partners:
- Katanin p60 ATPase-containing subunit A1
- Katanin p60 ATPase-containing subunit A-like 1
- KATNB1-like protein 1
- Katanin p60 ATPase-containing subunit A-like 2
- Abnormal spindle-like microcephaly-associated protein homolog
- Gamma-tubulin complex component 2
Sequence:
MATPVVTKTAWKLQEIVAHASNVSSLVLGKASGRLLATGGDDCRVNLWSINKPNCIMSLTGHTSPVESVRLNTPEELIVAGSQSGSIRVWDLEAAKILRTLMGHKANICSLDFHPYGEFVASGSQDTNIKLWDIRRKGCVFRYRGHSQAVRCLRFSPDGKWLASAADDHTVKLWDLTAGKMMSEFPGHTGPVNVVEFHPNEYLLASGSSDRTIRFWDLEKFQVVSCIEGEPGPVRSVLFNPDGCCLYSGCQDSLRVYGWEPERCFDVVLVNWGKVADLAICNDQLIGVAFSQSNVSSYVVDLTRVTRTGTVTQDPVQANQPLTQQTPNPGVSLRRIYERPSTTCSKPQRVKHNSESERRSPSSEDDRDERESRAEIQNAEDYNEIFQPKNSISRTPPRRSEPFPAPPEDDAATVKEVSKPSPAMDVQLPQLPVPNLEVPARPSVMTSTPAPKGEPDIIPATRNEPIGLKASDFLPAVKVPQQAELVDEDAMSQIRKGHDTMFVVLTSRHKNLDTVRAVWTTGDIKTSVDSAVAINDLSVVVDLLNIVNQKASLWKLDLCTTVLPQIEKLLQSKYESYVQTGCTSLKLILQRFLPLITDILAAPPSVGVDISREERLHKCRLCFKQLKSISGLVKSKSGLSGRHGSAFRELHLLMASLD
Protein: Beta-elicitin cinnamomin (P15569)
Organism: Phytophthora cinnamomi (Cinnamon fungus)
Function: Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane. Elicitins are able to load, carry, and transfer sterols between membranes.
Subcellular location: Secreted.
Interaction partners:
Sequence:
TACTATQQTAAYKTLVSILSESSFSQCSKDSGYSMLTATALPTNAQYKLMCASTACNTMIKKIVALNPPDCDLTVPTSGLVLDVYTYANGFSSKCASL
Protein: Crooked legs, isoform D (GH27971p) (Q8MRK4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQHVSAASSVPSVVTPVVTTGGTTITLGGPPPLPKSEHKEDGKPPHGIEMYKVNIEDISQLFTYHEVFGKIHGDVVNHQLAAAHGGQLPPPPPLPPQVTSHAASAAAAAAAASTNNAAVAAVMASANAAAAAAAAASAGGGLPPATSGNGGQQVTVTTTSSSTSSGGSTTSGGTTTTAGELLMPKMEGGIHGVDGSGNGGNGGGQNVALAPDGTPIATGTHVCDICGKMFQFRYQLIVHRRYHSERKPFMCQVCGQGFTTSQDLTRHGKIHIGGPMFTCIVCFNVFANNTSLERHMKRHSTDKPFACTICQKTFARKEHLDNHFRSHTGETPFRCQYCAKTFTRKEHMVNHVRKHTGETPHRCDICKKSFTRKEHYVNHYMWHTGETPHRCDFCSKTFTRKEHLLNHVRQHTGESPHRCSYCMKTFTRKEHLVNHIRQHTGESPHKCTYCTKTFTRKEHLTNHVRQHTGDSPHRCSYCKKTFTRKEHLTNHVRLHTGDSPHKCEYCQKTFTRKEHLNNHMRQHSSDNPHCCNVCNKPFTRKEHLINHMSRCHTGDRPFTCETCGKSFPLKGNLLFHQRSHTKGQEMERPFACEKCPKNFICKGHLVSHMRSHSGEKPHACTLCSKAFVERGNLKRHMKMNHPDAMMPPPPVHPHPQIPAGVLTQVKQEVKPIIIPHHSATTTMHTIQQITAGAAGGAGAVQLTPGLVPLVTSTLISHNAAAQQQSQKQQAAAAAAAQQQAAAAAAAQQQAAQQQAAAAHQQHQQQVAAQHQQQAAVAAHQQQQQQLQQQQQLLQLSIQQAAHHHQQEQHRQQQQQQHQQQQQQQHHQQQQQGHPQAPPPQQQQQPPPIALISDPSALARAAIQLQHLPANVEQHPVVY
Protein: Retinoid isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl-palmitate hydrolase) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein) (Retinol isomerase) (Q9YGX2)
Organism: Gallus gallus (Chicken)
Function: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. Essential for the production of 11-cis retinal for both rod and cone photoreceptors (By similarity). Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}. Cell membrane {ECO:0000250|UniProtKB:Q28175}; Lipid-anchor {ECO:0000250|UniProtKB:Q28175}. Microsome membrane {ECO:0000250|UniProtKB:Q28175}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. {ECO:0000250|UniProtKB:Q28175}.
Interaction partners:
- Uncharacterized protein
- Lecithin retinol acyltransferase
- Uncharacterized protein
- Patatin like phospholipase domain containing 4
- Rhodopsin
- Green-sensitive opsin
- Bestrophin 1.
- NADP-retinol dehydrogenase
- ATP binding cassette subfamily A member 4.
- CRAL-TRIO domain-containing protein.
Sequence:
MYSQVEHPAGGYKKLFETVEELSSPVTAHVTGRIPTWLRGSLLRCGPGLFEVGAEPFYHLFDGQALLHKFDFKEGHVTYHRRFVRTDAYVRAMTEKRIVITEFGTYAYPDPCKNIFSRFFSYFKGVEVTDNALVNVYPVGEDYYACTETNFITKINPDTLETIKQVDLCKYVSVNGATAHPHVENDGTVYNIGNCFGKNFSLAYNIIRIPPLQADKEDPMNKSEVVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLLKFLSSWSLWGANYMDCFESNETMGVWLHVAEKKKGRLLNIKYRTSAFNLFHHINTFEDNGFLIVDLCTWKGFEFVYNYLYLANLRANWDEVKKQAEKAPQPEARRYVLPLRIDKADTGKNLVTLPYTTATATLRSDETVWLEPEVIFSGPRHAFEFPQINYKKYGGKPYTYTYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALEEDDGVVLSIVISPGSGPKPAYLLILNAKDMSEVARAEVEVNIPVTFHGLFKRA
Protein: DUF3263 domain-containing protein (P96276)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Vesiculogenesis and immune response regulator
- Putative glutamate--cysteine ligase 2
- Superoxide dismutase
- Lon N-terminal domain-containing protein
- Peptide deformylase
Sequence:
MDSAMARAIRSGDDAEVADGLTRREHDILAFERQWWKFAGVKEEAIKELFSMSATRYYQVLNALVDRPEALAADPMLVKRLRRLRASRQKARAARRLGFEVT
Protein: Putative nucleosome assembly protein C2D10.11C (P78920)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone H2A.Z-specific chaperone chz1
- Histone H2A.Z
- Histone H2B-alpha
- Importin subunit beta-5
- Protein sda1
- Uncharacterized threonine-rich GPI-anchored glycoprotein PJ4664.02
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein eS6B
Sequence:
MSKGPGDFKKSWNGFAAQTPQNTPSSDVHLSKAALEKARQTLQSQLEDKSAHDEVSGLLRNNPAMLSMIEGRLSSLVGKSSGYIESLAPAVQNRITALKGLQKDCDAIQYEFRQKMLDLETKYEKKYQPIFSRRAEIIKGVSEPVDDELDHEEEIFQNNLPDPKGIPEFWLTCLHNVFLVGEMITPEDENVLRSLSDIRFTNLSGDVHGYKLEFEFDSNDYFTNKILTKTYYYKDDLSPSGEFLYDHAEGDKINWIKPEKNLTVRVETKKQRNRKTNQTRLVRTTVPNDSFFNFFSPPQLDDDESDDGLDDKTELLELDYQLGEVFKDQIIPLAIDCFLEEGDLSDFNQMDEEDSEDAYTDEEDLSSDDEEILSSEISD
Protein: Single-strand-selective monofunctional uracil-DNA glycosylase 1 (D6RAI1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVKGLASPVGGVGGSRWMLGWVCCGEGACAWL
Protein: Cadherin-related neural recepter 6 (O88193)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
FSSKHGTFVGRIAQDLGLELTELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVKDINDNPPKFSRPEQRLFILESRMPDSRFPVEGASDLDIGANAALSYKINPNEYFDLDVKRNEEETSVLQLVLKKPLDREETQEHRLLLIAIDGGKPELTGTVQLLIDVLDANDNAPEFDKSIYNVRLLENTPNGTLVIKLNASDADEGINKEILYFFSNLVLDDVKSKFTIDSSSGEIKVKGELDYEDCKVYEINIDAVDRSAFPLAGHCKIIVKLVDVNDNVPEMAITSIFLPIKEDAPLATVIALISVSDRDSGANGQVTCSLTPHIPFKLVSTFKNYYSLVLDRALDRETIANYDVVVTARDGGSPSLWATASVSVEVADVNDNVPAFAQPEYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLQYQVSARDAGVPALGSNVTLQVFVLDENDNAPTLLGPQGSGGTIELLSRSVSSGHVVAKVRAVDADSGYNAWLSYELQPATGAVRSPFRVGLYTGEISTTRVLDEADMPRQRLLVLVKDHGEPPLTATATFLVSLVENSQTPKVSSRVLVGTSGSDSTLIDVNVYLIIAICAVSSLLVLTLLLYTAIRCSATPTDGACAPGKPVLVCSSAVGTWSYSQQRRQRVCSGEGPPKTDLMAFSPSLPQGPSSTENPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: Proteasome subunit alpha type-6-B (20S proteasome subunit alpha A-2) (Proteasome subunit alpha type-1) (O81147)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-3-A
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- Proteasome subunit beta type-1
- Proteasome subunit beta type-7-B
- Proteasome subunit beta type-7-A
- Proteasome subunit beta type-2-B
- Proteasome subunit alpha type-1-B
- Proteasome subunit beta type-3-B
Sequence:
MSRGSGAGYDRHITIFSPEGRLFQVEYAFKAVKAAGITSIGVRGKDSVCVVTQKKVPDKLLDQSSVSHLFPVTKYLGLLATGMTADSRSLVQQARNEAAEFRFQYGYEMPADILAKWIADKSQVYTQHAYMRPLGVVAMVLGIDEERGPLLYKCDPAGHFYGHKATSAGMKEQEAVNFLEKKMKENPAFTYDETVQTAISALQSVLQEDFKATEIEVGVVRADDPLFRSLRTEEIDEHLTAISERD
Protein: Villin-like protein ABP41 (Calcium-dependent actin-binding protein ABP41) (P84994)
Organism: Lilium davidii (David's lily)
Function: Ca(2+)-dependent actin filament-severing protein that is required for pollen tube growth. Probably regulates the dynamics of the actin cytoskeleton. It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
Sequence:
PAFQGVGQRLGTEIESSKDEAATAALKTVELDAVLGGRTPEEETFETRLYQFNGANSNLQERALEVLQYLKVMGDPTVTLETTPGKSAEEFLLDENRPKDVALLDDGRVVEEETMETRLYQFNGANSNLGAERSAEEMLLNENRPK
Protein: Pleckstrin homology-like domain family B member 2 (Protein LL5-beta) (Q86SQ0)
Organism: Homo sapiens (Human)
Function: Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12376540}. Cytoplasm, cell cortex {ECO:0000269|PubMed:24120883}. Membrane {ECO:0000269|PubMed:12376540}; Peripheral membrane protein {ECO:0000269|PubMed:12376540}. Cell projection, podosome {ECO:0000250|UniProtKB:Q8K1N2}. Note=Translocates to the plasma membrane at high levels of PtdIns(3,4,5)P3. At low levels of PtdIns(3,4,5)P3 is translocated to vesicular compartments. Localized to the myotube podosome cortex that surrounds the core (By similarity). {ECO:0000250|UniProtKB:Q8K1N2}.
Interaction partners:
- CLK4-associating serine/arginine rich protein
- ELKS/Rab6-interacting/CAST family member 1
- Liprin-alpha-1
- KN motif and ankyrin repeat domain-containing protein 1
- CLIP-associating protein 2
- Filamin-C
- Prickle-like protein 1
- Filamin-A
- CLIP-associating protein 1
Sequence:
MEEHSYIQKELDLQNGSLEEDSVVHSVENDSQNMMESLSPKKYSSSLRFKANGDYSGSYLTLSQPVPAKRSPSPLGTSVRSSPSLAKIQGSKQFSYDGTDKNIPMKPPTPLLNTTSSLSGYPLGRADFDHYTGRDSERALRLSEKPPYSKYSSRHKSHDNVYSLGGLEGRKASGSLLAMWNGSSLSDAGPPPISRSGAASMPSSPKQARKMSIQDSLALQPKLTRHKELASENINLRTRKYSSSSLSHMGAYSRSLPRLYRATENQLTPLSLPPRNSLGNSKRTKLGEKDLPHSVIDNDNYLNFSSLSSGALPYKTSASEGNPYVSSTLSVPASPRVARKMLLASTSSCASDDFDQASYVGTNPSHSLLAGESDRVFATRRNFSCGSVEFDEADLESLRQASGTPQPALRERKSSISSISGRDDLMDYHRRQREERLREQEMERLERQRLETILSLCAEYTKPDSRLSTGTTVEDVQKINKELEKLQLSDEESVFEEALMSPDTRYRCHRKDSLPDADLASCGSLSQSSASFFTPRSTRNDELLSDLTRTPPPPSSTFPKASSESSYLSILPKTPEGISEEQRSQELAAMEETRIVILNNLEELKQKIKDINDQMDESFRELDMECALLDGEQKSETTELMKEKEILDHLNRKIAELEKNIVGEKTKEKVKLDAEREKLERLQELYSEQKTQLDNCPESMREQLQQQLKRDADLLDVESKHFEDLEFQQLEHESRLDEEKENLTQQLLREVAEYQRNIVSRKEKISALKKQANHIVQQAQREQDHFVKEKNNLIMMLQREKENLCNLEKKYSSLSGGKGFPVNPNTLKEGYISVNEINEPCGNSTNLSPSTQFPADADAVATEPATAVLASQPQSKEHFRSLEERKKQHKEGLYLSDTLPRKKTTSSISPHFSSATMGRSITPKAHLPLGQSNSCGSVLPPSLAAMAKDSESRRMLRGYNHQQMSEGHRQKSEFYNRTASESNVYLNSFHYPDHSYKDQAFDTLSLDSSDSMETSISACSPDNISSASTSNIARIEEMERLLKQAHAEKTRLLESREREMEAKKRALEEEKRRREILEKRLQEETSQRQKLIEKEVKIRERQRAQARPLTRYLPVRKEDFDLRSHVETAGHNIDTCYHVSITEKTCRGFLIKMGGKIKTWKKRWFVFDRNKRTFSYYADKHETKLKGVIYFQAIEEVYYDHLKNANKSPNPLLTFSVKTHDRIYYMVAPSPEAMRIWMDVIVTGAEGYTHFLL
Protein: Nonsense-mediated mRNA decay factor SMG9 (Q9DB90)
Organism: Mus musculus (Mouse)
Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between SMG1 and SMG8 (By similarity). Plays a role in brain, heart, and eye development.
Interaction partners:
- Serine/threonine-protein kinase SMG1
- Nonsense-mediated mRNA decay factor SMG8
- Nonsense-mediated mRNA decay factor SMG7
- Telomerase-binding protein EST1A
- Nonsense-mediated mRNA decay factor SMG5
- Regulator of nonsense transcripts 2
- Regulator of nonsense transcripts 1
- UPF3 regulator of nonsense transcripts homolog A
- Probable ATP-dependent RNA helicase DHX34
- Eukaryotic peptide chain release factor subunit 1
Sequence:
MSESGHSQPGLYGIERRRRWKEPGSSGPQNLSGPGGRERDYIAPWERERRDGSEDPSTNVMQKTPIILSKPPAERSKQPPPSTAPAAPPAPAPLEKPIVLMKPREEGKGPVAGTGASTPEGTAPPPPTAPAPPKGEKEGQRPTQPVYQIQNRGMGTAAPTAMDPVVGQAKLLPPERMKHSIKLVDDQMNWCDSAIEYLLDQTDVLVVGVLGLQGTGKSMVMSLLSANTPEEDQRAYVFRAQSAEMKERGGNQTSGIDFFITQERIVFLDTQPILSPSILDHLINNDRKLPPEYNLPHTYVEMQSLQIAAFLFTVCHVVIVVQDWFTDLSLYRFLQTAEMVKPSTPSPSHESSSSAGSDEGTEYYPHLVFLQNKARREDFCPRKLRQMHLMIDQLMAHSHLRYKGTLSMLQCNVFPGLPPDFLDAEVNLFLVPFMDSEAENENPPRAGPGSSPLFSLLPGYRGHPSFQSLVSKLRSQVMSMARPQLSHTILTEKNWFHYAARIWDGVKKSSALAEYSRLLA