wanglab/gogpt-training-data huggingface dataset:
Protein: Cysteine and glycine-rich protein 2 (Cysteine-rich protein 2) (CRP2) (Smooth muscle cell LIM protein) (SmLIM) (Q62908)
Organism: Rattus norvegicus (Rat)
Function: Drastically down-regulated in response to PDGF-BB or cell injury, that promote smooth muscle cell proliferation and dedifferentiation. Seems to play a role in the development of the embryonic vascular system.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MPVWGGGNKCGACGRTVYHAEEVQCDGRTFHRCCFLCMVCRKNLDSTTVAIHDEEIYCKSCYGKKYGPKGYGYGQGAGTLNMDRGERLGIKPESAQPHRPTTNPNTSKFAQKYGGAEKCSRCGDSVYAAEKIIGAGKPWHKNCFRCAKCGKSLESTTLTEKEGEIYCKGCYAKNFGPKGFGYGQGAGALVHAQ
Protein: Collagen type IV alpha 1 chain (A0A8I6AFK7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MGPRLSVWLLLPLAALLLHEERSRAAAKGDCGGSGCGKCDCHGVKGQKGERGFPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFSGNPGPPGLPGMKGDPGEILGHVPGTLLKGERGFPGIPGAPGSPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQAQVKEKGDFAPTGEKGQKGEPGFQGTPGYGEKGEPGKPGPRGKPGKDGEKGEKGSPGFPGESGYPGLPGRQGPQGEKGEPGLPGPPGTVVGTRPLGEKGERGYPGSPGLRGEPGPKGYPGSPGQPGPPGFAVPGQTGAPGFPGERGEKGERGSPGVSLPGPSGRDGAPGPPGPPGPPGQPGHTNGIVECQPGPPGDQGPPGIPGQPGLTGEVGQKGQKGESCLACDTEGLRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGLEGLPGPQGSPGLIGQPGAKGEPGEIFFDMRLKGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGERGPPGGVGFPGSRGDIGPPGPPGVGPIGPIGEKGQAGLPGGPGSPGLPGPKGEAGKVVPLPGPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGNPGEKGAVGQPGIGFPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPGIGLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGVQGPAGPPGVPGIGPPGAMGPPGGQGPPGSSGPPGVKGEKGFPGFPGLDMPGPKGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGAPGLPGEKGDHGFPGSSGPRGDPGFKGDKGDVGLPGMPGSMEHVDMGSMKGQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGIPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGLPGRGFPGFPGTKGDKGSKGEVGFPGLAGSPGIPGAKGEQGFMGPPGPQGQPGLPGTPGHPVEGPKGDRGPQGQPGLPGHPGPMGPPGFPGIDGPKGDKGNPGWPGAPGAPGPKGDPGFQGMPGIGGSPGITGSKGDMGPPGVPGFQGQKGLPGLQGVKGDQGDQGIPGPKGLQGPPGPPGPYDVIKGEPGLPGPEGPPGLKGLQGPPGPKGQQGVTGSVGLPGPPGVPGFDGAPGQKGETGPFGPPGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPISGDNIRPFISSFPWKTGVQFAKRPPW
Protein: RAD50 protein (Q5W4T6)
Organism: Gallus gallus (Chicken)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAKIEKMSILGVRSFGVEDKDKQIITFFNPLTILVGPNGAGKTTIIECLKYISTGDFPPGTKGNSFVHDPKVANETDVRAQIRLQFRDVSGELIAVQRSMVCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISALGVSKSVLNNVIFCHQEESNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRLKQGTKVKECQTELKYLKQNKEKAQEIQDNLANREAQLSASKENIKSIESQLDPLKSSLAAVEKNLMEVMSLDNNVKALESRRIQMEKDNQDLQRKMEKVFQGTDEQLKDRYHNHQRTVKEKEKRLSDCKRELDRASKECQRFNSEKSELLIERGRLQLQADRHQEHIKVRDSLIQALSAQLELDGFEQAPFNDRQIAVFHELLKERQKSDTEAANQLMREFTQKEAMKQEQIDKIRDRKTGLERSIDLKSDIQNKRLAELKNVKYELCQLEGSSDRIAELDREIVKMEHELEKAERNSNVETLEQEVQTLQNEKINLDKVLRRLDQEMEQLNLHTTTITQMEMLKKDKADKEEQIRKVKLRHFEELTLLLGYFPNKKQLEDWLHGKSTEINETRSRHALLNKQLASAEQQKNYISAELRKKEEQLSNYEAKLFDVCGSQDFDSNLNKLQDEIEKSSKQRAVLAGATAVYSQFITQLTEENQSCCPVCQRVFQTEAELQDVISDLQSKLRLAPDKLKSTESELKKREKKRDEMIGLKPIRQTVLELQERDIPDLRNRLQTVNRDFARLKGEIEEQETLLQTVLSEKEGANACLQDITLMERYQTDIRDVERKIAQQEAKLLGVDLNRTVLQVSQEKQAKKHLWDTVTSKIELNQKMKQDQQNQIQELKSTVNELRAEKLQISSSVQRRQQLEEQTVELTTEVQSLSREIKEEKEQVFPLDATLEKLQQDKEDLINKRTASNKEIQEKINAIKEKVKDINKYTKEIENYIQQGKEEYKKQKECELDEVNSQLVACEKQKEKISKEMEIIRQDIDTQKIQERWLEDNLTLRERNKELKGVEDNIKELVKKMGEMKVPQLKNEQKHLEEKIEALKRNHHVALGRQRGFEEEIVRFKKELRESQFKDAEEKHREMMIVMRTTELVNKDLDIYYKALDKAIMTFHSMKMQEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRSYNYRVVMIKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALV
Protein: Metastasis associated 1 (F8W9Y9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVLSSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGTYLGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED
Protein: Lysine (K)-specific demethylase 2Aa (EC 1.14.11.27) (A0A0R4IH56)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDVMSAGDATSRSKRSGTRRRYQDDGISDDEIDGRRTFDLEEKLHSSFFSSDRVKRMEGKDFSYEYVQRHGLRDPIIFEKPEGLGIKMPDPDFTVNDVKLFVGSRRIVDVMDVATQKGTEMSMAQWRRYYETPPSQREKLYNVISLEFSHTKLETLVKRPSTVDMIDWVDNMWPRHLKERQRDSTNSIMEMQYPKVQKYCLMSVQGCYTDFHIDFGGTSVWYHIHKGCKVFWLIPPTPQNLELYENWVLSGKQGDIFLGDRATDCQRIELKQGYTFIIPSGWIHAVYTPVDTLVFGGNFLHSFNVPMQLDISGIEDRTRVPVKFRYPFFFEMCWYVLERYLYSLTNKSHLIPEFQKHSLGIGLKRENSEVLNGHAKEERDEMDAPSPPSAPGLKTHLTAFELEGLWRLVGKLESLPSNKKCVPSGIHNAAALLLDIRALLKEHANDIPKLSYTGRPIVRWPKRPPWYQPPPPPPPVMRPKLATTPIVPRPVKPASNMSVLRRRRVRCKRCEACLRTECGDCNFCRDMKKFGGPGKLKQTCVLRQCLAPGLPLSAVCELCGEGNQETSEELMECSNCAQIAHPSCLKTSGEGVVNKDLPSCWECPKCVLGKDTDSESSGSGDDITAQDGSGGRGGEGGAWHGVGRPPSSLSHGSLQKRAAAPEQRLRKRIKLDGGKSHKRKSSSLDPRVAKIYRRHGMEHDDDSGSDDDGDGGRMSSVRSSVSSSRRGYGASRRGVWRGSSQRGPRGGGSLSSSSLKMRRGLGARGERGGRVRLRGGSQMRRRRYETDDDDDDDDDDDDDDDDDDDEDEDDEDDSEEDRHVSRSEKEHRSRRRRRRGDDYDDDEDEDDDDEEDSEEQDYEGEDDEMEDLDDGGDEDDEDGENQSDSDPDPPVLLVSDLNDDLLNDSYLTVTLHRPPKAKRDPGSIVPKLEAAMSPRTGGSSGFMQRKTLPKARPKTSSSTPAGNGLSQAKSGRPTRRSSNQDGRERDTASPSSMSSRSSVSPPPPPPAVTSSSPSLLSHPSFRDAGNELGCEKDIWVSVFRYLDRTDLAVCMRVCKAWFKWCCDKRLWTRIDLSRCRALSPQAVTAIIKLQPVTLDLSWTPVSKKQLAWLIHHLPSLKDLIMSGCSSLCVSALSSPSCPSLRTLDLCWAVGVKDSQIKDLIVQPGSESRSRLRSLVSLRLSGLELSDAVIKTMVRHMPSLRQLDLSYCQGLTDQSINLLTATGCNTRNTLRQLNLSGCNKLSDGCLSYMKRLSALALLDLRGCKNVTRHGCENFISDLSYCTVFCLTEDKLIQRVS
Protein: Voltage-dependent L-type calcium channel subunit beta-1 (CAB1) (Calcium channel voltage-dependent subunit beta 1) (Q02641)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of L-type calcium channels. Regulates the activity of L-type calcium channels that contain CACNA1A as pore-forming subunit (By similarity). Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit and increases the presence of the channel complex at the cell membrane. Required for functional expression L-type calcium channels that contain CACNA1D as pore-forming subunit. Regulates the activity of L-type calcium channels that contain CACNA1B as pore-forming subunit.
Subcellular location: Cell membrane, sarcolemma {ECO:0000305|PubMed:15615847}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19517}; Cytoplasmic side {ECO:0000250|UniProtKB:P19517}. Cell membrane {ECO:0000305|PubMed:1309651}; Peripheral membrane protein {ECO:0000305|PubMed:1309651}.
Interaction partners:
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent calcium channel subunit alpha-2/delta-4
Sequence:
MVQKTSMSRGPYPPSQEIPMEVFDPSPQGKYSKRKGRFKRSDGSTSSDTTSNSFVRQGSAESYTSRPSDSDVSLEEDREALRKEAERQALAQLEKAKTKPVAFAVRTNVGYNPSPGDEVPVQGVAITFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLDSLRLLQEQKLRQNRLGSSKSGDNSSSSLGDVVTGTRRPTPPASAKQKQKSTEHVPPYDVVPSMRPIILVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKHIIIERSNTRSSLAEVQSEIERIFELARTLQLVALDADTINHPAQLSKTSLAPIIVYIKITSPKVLQRLIKSRGKSQSKHLNVQIAASEKLAQCPPEMFDIILDENQLEDACEHLAEYLEAYWKATHPPSSTPPNPLLNRTMATAALAASPAPVSNLQGPYLASGDQPLERATGEHASMHEYPGELGQPPGLYPSSHPPGRAGTLRALSRQDTFDADTPGSRNSAYTELGDSCVDMETDPSEGPGLGDPAGGGTPPARQGSWEDEEEDYEEELTDNRNRGRNKARYCAEGGGPVLGRNKNELEGWGRGVYIR
Protein: DNA-binding protein SATB1 (Special AT-rich sequence-binding protein 1) (Q60611)
Organism: Mus musculus (Mouse)
Function: Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis (By similarity). Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma. Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone, possibly by positively regulating the expression of NEUROD1.
Subcellular location: Nucleus. Nucleus, PML body. Note=Organized into a cage-like network anchoring loops of heterochromatin and tethering specialized DNA sequences. When sumoylated, localized in promyelocytic leukemia nuclear bodies (PML NBs) (By similarity). {ECO:0000250}.
Interaction partners:
- Caspase-6
- Histone deacetylase 1
Sequence:
MDHLNEATQGKEHSEMSNNVSDPKGPPAKIARLEQNGSPLGRGRLGSTGGKMQGVPLKHSGHLMKTNLRKGTMLPVFCVVEHYENAIEYDCKEEHAEFVLVRKDMLFNQLIEMALLSLGYSHSSAAQAKGLIQVGKWNPVPLSYVTDAPDATVADMLQDVYHVVTLKIQLHSCPKLEDLPPEQWSHTTVRNALKDLLKDMNQSSLAKECPLSQSMISSIVNSTYYANVSAAKCQEFGRWYKHFKKTKDMMVEMDSLSELSQQGANHVNFGQQPVPGNTAEQPPSPAQLSHGSQPSVRTPLPNLHPGLVSTPISPQLVNQQLVMAQLLNQQYAVNRLLAQQSLNQQYLNHPPPVSRSMNKPLEQQVSTNTEVSSEIYQWVRDELKRAGISQAVFARVAFNRTQGLLSEILRKEEDPKTASQSLLVNLRAMQNFLQLPEAERDRIYQDERERSLNAASAMGPAPLLSTPPSRPPQVKTATLATERNGKPENNTMNINASIYDEIQQEMKRAKVSQALFAKVAATKSQGWLCELLRWKEDPSPENRTLWENLSMIRRFLSLPQPERDAIYEQESNAVHHHGDRPPHIIHVPAEQIQQQQQQQQQQQQQQQPPPPPPQPQPQPQAGPRLPPRQPTVASSAESDEENRQKTRPRTKISVEALGILQSFIQDVGLYPDEEAIQTLSAQLDLPKYTIIKFFQNQRYYLKHHGKLKDNSGLEVDVAEYKDEELLKDLEESVQDKNANTLFSVKLEEELSVEGSTDVNADLKD
Protein: Lactase/phlorizin hydrolase (Lactase/glycosylceramidase) [Includes: Lactase (EC 3.2.1.108); Glycosylceramidase (EC 3.2.1.62) (Phlorizin hydrolase)] (Q02401)
Organism: Rattus norvegicus (Rat)
Function: Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta-glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P09848}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09848}. Note=Brush border. {ECO:0000250|UniProtKB:P09849}.
Interaction partners:
- Beta-galactosidase
- Alpha-galactosidase
- Galactose mutarotase
- Glucose-6-phosphatase catalytic subunit 1
- Uncharacterized protein.
- Glucose-6-phosphatase 3
- Hexokinase-2
- Hexokinase-3
- aldose reductase
- Aldo-keto reductase family 1 member B7
Sequence:
MELPWTALFLSTVLLGLSCQGSDWESDRNFISAAGPLTNDLVLNLNYPPGKQGSDVVSGNTDHLLCQQPLPSFLSQYFSSLRASQVTHYKVLLSWAQLLPTGSSKNPDQEAVQCYRQLLQSLKDAQLEPMVVLCHQTPPTSSAIQREGAFADLFADYATLAFQSFGDLVEIWFTFSDLEKVIMDLPHKDLKASALQTLSNAHRRAFEIYHRKFSSQGGKLSVVLKAEDIPELLPDPALAALVQGSVDFLSLDLSYECQSVATLPQKLSELQNLEPKVKVFIYTLKLEDCPATGTSPSSLLISLLEAINKDQIQTVGFDVNAFLSCTSNSEESPSCSLTDSLALQTEQQQETAVPSSPGSAYQRVWAAFANQSREERDAFLQDVFPEGFLWGISTGAFNVEGGWAEGGRGPSIWDHYGNLNAAEGQATAKVASDSYHKPASDVALLRGIRAQVYKFSISWSGLFPLGQKSTPNRQGVAYYNKLIDRLLDSHIEPMATLFHWDLPQALQEQGGWQNESVVEAFLDYAAFCFSTFGDRVKLWVTFHEPWVMSYAGYGTGQHAPAISDPGMASFKVAHLILKAHARTWHLYDLHHRLQQQGRVGIVLNSDLAEPLDRKSPQDLAAAERFLHFMLGWFAHPIFVDGDYPTTSAQIQHINQQCGHPLAQLPEFTEAEKRLLKGSADFLGLSHYTSRLISKAGRQTCTSSYDNIGGFSQHVDPEWPQTASPWIRVVPWGIRRLLRFASMEYTKGKLPIFLAGNGMPVGEEADLFDDSVRVNYFNWYINEVLKAVKEDLVDVRSYIVRSLIDGYEGPLGFSQRFGLYHVNFNDSSRPRTPRKSAYLFTSIIEKNGFSAKKVKRNPLPVRADFTSRARVTDSLPSEVPSKAKISVEKFSKQPRFERDLFYDGRFRDDFLWGVSSSPYQIEGGWNADGKGPSIWDNFTHTPGNGVKDNATGDVACDSYHQLDADLNILRTLKVKSYRFSISWSRIFPTGRNSTINKQGVDYYNRLIDSLVDNNIFPMVTLFHWDLPQALQDIGGWENPSLIELFDSYADYCFKTFGDRVKFWMTFNEPWCHVVLGYSSGIFPPSVQEPGWLPYKVSHIVIKAHARVYHTYDEKYRSEQKGVISLSLNTHWAEPKDPGLQRDVEAADRMLQFTMGWFAHPIFKNGDYPDVMKWTVGNRSELQHLASSRLPTFTEEEKNYVRGTADVFCHNTYTSVFVQHSTPRLNPPSYDDDMELKLIEMNSSTGVMHQDVPWGTRRLLNWIKEEYGNIPIYITENGQGLENPTLDDTERIFYHKTYINEALKAYKLDGVDLRGYSAWTLMDDFEWLLGYTMRFGLYYVDFNHVSRPRTARASARYYPDLIANNGMPLAREDEFLYGEFPKGFIWSAASASYQVEGAWRADGKGLSIWDTFSHTPLRIGNDDNGDVACDSYHKIAEDVVALQNLGVSHYRFSIAWSRILPDGTTKFINEAGLSYYVRFIDALLAAGITPQVTIYHWDLPQALQDVGGWENETIVQRFKEYADVLFQRLGDRVKFWITLNEPFVIAAQGYGTGVSAPGISFRPGTAPYIAGHNLIKAHAEAWHLYNDVYRARQGGTISITISSDWGEPRDPTNREHVEAARSYVQFMGGWFAHPIFKNGDYPEVMKTRIRDRSLGAGLNKSRLPEFTESEKSRIKGTFDFFGFNHNTTVLAYNLDYPAAFSSFDADRGVASIADSSWPVSGSFWLKVTPFGFRRILNWLKEEYNNPPIYVTENGVSRRGEPELNDTDRIYYLRSYINEALKAVHDKVDLRGYTVWSIMDNFEWATGFAERFGVHFVNRSDPSLPRIPRASAKFYATIVRCNGFPDPAQGPHPCLQQPEDAAPTASPVQSEVPFLGLMLGIAEAQTALYVLFALLLLGACSLAFLTYNTGRRSKQGNAQPSQHQLSPISSF
Protein: Alpha-carbonic anhydrase domain-containing protein (Q21614)
Organism: Caenorhabditis elegans
Interaction partners:
- Carbonic anhydrase
- Beta carbonic anhydrase 1
- Ribosome production factor 2 homolog
- LIPaSe related
- Nematode Specific Peptide family, group E
Sequence:
MAPPQVRRSARLSKRCQEEKVKLQKKNVGFKAKSKSAKKSNKKFKKAAAQRQSPIDIVPQHVCCDTDVCKADALNIDYKSGDCCDVLVSEGGFLVNVKRNCGTFLTANHLPSSKFALAQFHAHWGSNSKEGSEHFLDGKQLSGEVHFVFWNTSYESFNVALSKPDGLAVVGVFLKEGKYNDNYHGLIDTVRKATGNATPIAMPKDFHIEHLLPSPDKREFVTYLGSLTTPPYNECVIWTLFTEPVEVSFGQLNVLRNIIPANHRACQDRCDREIRSSFNF
Protein: Myosin IXB (M0R0P8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSVKEAGSSGRREQAAYHLHIYPQLSTTESQASCRVTATKDSTTSDVIKDAIASLRLDGTKCYVLVEVKESGGEEWVLDANDSPVHRVLLWPRRAQDEHPQEDGYYFLLQERNADGTIKYVHMQLVAQATATRRLVERGLLPRQQADFDDLCNLPELTEGNLLKNLKHRFLQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKRVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVSYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPEDYFYLNQHNLKIEDGEDLKHDFERLKQAMEMVGFLPATKKQIFAVLSAILYLGNVTYKKRATGREEGLEVGPPEVLDTLSQLLKVKREILVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDVEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFNQHIFKLEQEEYQGEGITWHNIGYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSQTLLAKFKQQHEDNKYFLGTPVMEPAFIIQHFAGKVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRELIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAAGMSSPGAQSHPEELPRGASTPSEKLYRDLHNQMIKSIKGLPWQGEDPRSLLQSLSRLQKPRAFILKSKGIKQKQIIPKNLLDSKSLKLIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDAQPCREVISTLLEKMKIDKRNYQIGKTKVFLKETERQALQETLHREVVRKILLLQSWFRMVLERRHFLQMKRAAVTIQACWRSYRVRRALERTQAAVYLQASWRGYWQRKLYRHQKQSIIRLQSLCRGHLQRKSFSQMISEKQKAEEKEREALEAARAGAEEGGQGQAAGGQQVAEQGPEPAEDGGHLASEPEVQPSDRSPLEHSSPEKEAPSPEKTLPPQKTVAAESHEKVPSSREKRESRRQRGLEHVKFQNKHIQSCKEESALREPSRRVTQEQGVSLLEDKKESREDETLLVVETEAENTSQKQPTEQPQAMAVGKVSEETEKTLPSGSPRPGQLERPTSLALDSRVSPPAPGSAPETPEDKSKPCGSPRVQEKPDSPGGSTQIQRYLDAERLASAVELWRGKKLVAAASPSAMLSQSLDLSDRHRATGAALTPTEERRTSFSTSDVSKLLPSLAKAQPAAETTDGERSAKKPAVQKKKPGDASSLPDAGLSPGSQVDSKSTFKRLFLHKTKDKKYSLEGAEELENAVSGHVVLEATTMKKGLEAPSGQQHRHAAGEKRTKEPGGKGKKNRNVKIGKITVSEKWRESVFRQITNANELKYLDEFLLNKINDLRSQKTPIESLFIEATEKFRSNIKTMYSVPNGKIHVGYKDLMENYQIVVSNLATERGQKDTNLVLNLFQSLLDEFTRGYTKNDFEPVKQSKAQKKKRKQERAVQEHNGHVFASYQVSIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSHCSYTYGRKGEPGVEPGHFGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLENFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLEHLPEANHNSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPLTSMKDVLKITTCVEMLIKEQMRKYKVKMEEISQLEAAESIAFRRLSLLRQNAPWPLKLGFSSPYEGVLNKSPKTRDIQEEELEVLLEEEAAGGDEDREKEILIERIQSIKEEKQDITYRLPELDPRGSDEENLDSETSASTESLLEERAGRGASEGPPAPALPCPGAPTPSPLPTVAAPPRRRPSSFVTVRVKTPRRTPIMPTANIKLPPGLPSHLPRWAPGAREAAAPVRRREPPARRPDQIHSVYITPGADLPVQGALEPLEEDGQPPGAKRRYSDPPTYCLPPASGQTNG
Protein: Forkhead box P3 (Forkhead box protein) (Forkhead box protein P3a isoform X2) (Foxp3 protein) (A8WFW7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Interleukin family protein
- T-box 21 like
- Interleukin 17_5
- Interleukin 13
- Interleukin 17_1
- Interleukin 17_2
- CD28 molecule.
- Transcription factor GATA-3
- Tumor necrosis factor receptor superfamily member 18 isoform X1
- Indoleamine 2,3-dioxygenase 1.
Sequence:
MLLNATGTHRGDDNRSSHQHLYQDEDCATFSIIQMKSRISNSLLTSPKPMATKISVALESDLRGLGSSRNQNFTLQKQSASGSTTKYFKQHRPSVLRKGNQPFPQACSAHDWVVDTVCKTEPDSEPSDAIPLYTGQSESRIGAYASSPQPGSPEYTGKHPYSLSGDYLCVKGQCRWPGCSKSEDVFTEYGHFLRHLSTDHAPGDRSIGQLRMQKDRVQHMENQLTAERQKLQAMQLHLLDVKSTSEGGNIVEKPAHLSGLLQPASSNDHYDCERAATEALTQGYWQISTSQVIPGIIPSFEYYKFTNMRPPFTYASMIRWAILKSPEKQLTLKEIYQWFTSMFFYFRHNTATWKNAVRHNLSLHKCFVRVEGRKGSVWTVDEEEFLRRKGQKLHRDHDMDWMAPFQLFPLTPQGESYQM
Protein: GGDEF domain-containing protein (Q9I072)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Cyclic di-GMP phosphodiesterase RocR
- Sensory/regulatory protein RpfC
- cyclic-guanylate-specific phosphodiesterase
- histidine kinase
- histidine kinase
- histidine kinase
- cyclic-guanylate-specific phosphodiesterase
- Cyclic di-GMP phosphodiesterase PA4781
- GGDEF domain-containing protein
- EAL domain-containing protein
Sequence:
MLACPLPPDEALRQQALDDMALVDTPAEHYLDALVELARETFGVKTVLISLIDHDRQWFKARIGLDAEQTPRDLSFCGHAILASEPLMVTDASRDPRFHDNPLVTGPPFIRFYAGEPLHASNGQAIGTLCLIDPSPRLLDLREGRQLNRLSILAEGYLQLRSLTEHTRFLRQEIDREQRKSLLDPLTQLWNRAGFHALHQHELELARASDQRIGIIYSDIDHFKRINDTLGHRAGDSVLREAASRLRAALRPEDLLARFGGEEFVAMVRVRETTELTMIANRIRELMEATPIDCAGTSVPVTISAGCTLAGSGEEPERALARADAALYDAKRAGRNRVVSV
Protein: Telobox protein 1 (Meiotically up-regulated gene 152 protein) (Q10274)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: General transcription factor with prominent roles in controlling histone levels and stability. Binds and regulates the activities of many promoters, including those controlling the expression of all four types of canonical histones. Is also involved in the centromeric loading of cnp1 and maintenance of centromere identity. Moreover, regulates the expression of cdc2, a protease capable of histone clipping.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:23314747}.
Interaction partners:
- Elongation factor 3
- mRNA export factor elf1
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL6
Sequence:
MRSMKPPGFSSDLMDEHSVDLLNGSILAAENPSKREVAQDVPGFERKPTKVRKPRVKWTEKETNDLLRGCQIHGVGNWKKILLDERFHFTNRSPNDLKDRFRTILPEDYKKFYPNAKTHMGRPQKIPHTVGLSKSTRKERKQFTPEEDERLLEGFFLHGPCWTRISKDANLGLQNRRSTDLRDRFRNAFPERYAAAGFKLKNNPGNRSKYYQNNMVNDATTPNDSSTTEAAAAAVAAVAAVAASNPNASPQQTTEQPASDELLDWPHHNLPSQFFTSQRNPNYSTDSFLLGQSLSDPFNHTLQSFHPYESLFSAGQPPSLPISPSTSQNSVQPFPFSIQQPPLHLEPPLSSNTLNSSTLPQPNSTDFNTFPPLPSTPRISSEDIPWDNRG
Protein: Probable carboxylic ester hydrolase LipM (EC 3.1.1.-) (Q50681)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Esterase LipI
- Carboxylic ester hydrolase LipN
- Possible esterase LipW
- Probable conserved transmembrane protein
- Uncharacterized protein Rv2283
- Putative diacyglycerol O-acyltransferase Rv2285
- Esterase LipU
Sequence:
MGAPRLIHVIRQIGALVVAAVTAAATINAYRPLARNGFASLWSWFIGLVVTEFPLPTLASQLGGLVLTAQRLTRPVRAVSWLVAAFSALGLLNLSRAGRQADAQLTAALDSGLGPDRRTASAGLWRRPAGGGTAKTPGPLRMLRIYRDYAHDGDISYGEYGRANHLDIWRRPDLDLTGTAPVLFQIPGGAWTTGNKRGQAHPLMSHLAELGWICVAINYRHSPRNTWPDHIIDVKRALAWVKAHISEYGGDPDFIAITGGSAGGHLSSLAALTPNDPRFQPGFEEADTRVQAAVPFYGVYDFTRLQDAMHPMMLPLLERMVVKQPRTANMQSYLDASPVTHISADAPPFFVLHGRNDSLVPVQQARGFVDQLRQVSKQPVVYAELPFTQHAFDLLGSARAAHTAIAVEQFLAEVYATQHAGSEPGPAVAIP
Protein: t-SNARE coiled-coil homology domain-containing protein (Q57VM3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
Sequence:
MTSKVEELVGEVEEALEKLVNASDSIFNASTTLDKKQAELSAKPVMREARSKVEMLNDELRRTEDAAVRSHYEKVCRAAEEKIRVLDAEIKKHVYAKHTKVALEKTHAERREEELLGPGGADGSGFQDSQQVLEAAVNVQKDMLVSLQRTEKVMIMTEETGQETLQALQRQTEQMYQVDEGLEELQGQLDRAGRDVRWFFRQLAGDKCFLSLFGILVVAMAVLMGVMIYKKRQAKKNAEK
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5 (P63219)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- 5-hydroxytryptamine receptor 7
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Protein kinase C epsilon type
- Phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1
- C-X-C chemokine receptor type 4
- Apelin receptor
Sequence:
MSGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFRPQKVCSFL