wanglab/gogpt-training-data huggingface dataset:
Protein: 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58) (O43242)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Interaction partners:
- Proteasomal ubiquitin receptor ADRM1
- Proteasome subunit beta type-7
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 7
- Proteasome subunit alpha type-2
- Ubiquitin carboxyl-terminal hydrolase 14
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit 6B
Sequence:
MKQEGSARRRGADKAKPPPGGGEQEPPPPPAPQDVEMKEEAATGGGSTGEADGKTAAAAAEHSQRELDTVTLEDIKEHVKQLEKAVSGKEPRFVLRALRMLPSTSRRLNHYVLYKAVQGFFTSNNATRDFLLPFLEEPMDTEADLQFRPRTGKAASTPLLPEVEAYLQLLVVIFMMNSKRYKEAQKISDDLMQKISTQNRRALDLVAAKCYYYHARVYEFLDKLDVVRSFLHARLRTATLRHDADGQATLLNLLLRNYLHYSLYDQAEKLVSKSVFPEQANNNEWARYLYYTGRIKAIQLEYSEARRTMTNALRKAPQHTAVGFKQTVHKLLIVVELLLGEIPDRLQFRQPSLKRSLMPYFLLTQAVRTGNLAKFNQVLDQFGEKFQADGTYTLIIRLRHNVIKTGVRMISLSYSRISLADIAQKLQLDSPEDAEFIVAKAIRDGVIEASINHEKGYVQSKEMIDIYSTREPQLAFHQRISFCLDIHNMSVKAMRFPPKSYNKDLESAEERREREQQDLEFAKEMAEDDDDSFP
Protein: APO RNA-binding protein (DUF794) (F4I896)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLQESGKVIVFGLILIWVLTYIVNMLLVSPACRGVYLQTIDPKPIDFSARASYALCFQIPTSIPKRECLMRLGTVFCFNQKHREQTSFKKRYVSTQNVDLPPILPKNKKKPYPIPFKQIQEEARKDKKLAQMGIEKQLDPPKNGLLVPNLVPVADQVIDNWKLLIKGLAQLLHVVPVFACSECGAVHVANVGHNIRDCNGPTNSQRRGSHSWVKGTINDVLIPVESYHMYDPFGRRIKHETRFEYERIPALVELCIQAGVEIPEYPCRRRTQPIRMMGKRVIDRGGYHKEPEKPQTSSSLSSPLAELDTLGVFERYPPPTPEDIPKIAQETMDAYEKVRLGVTKLMRKFTVKACGYCSEVHVGPWGHSVKLCGEFKHQWRDGKHGWQDALVDEVFPPNYVWHVRDLKGNPLTGNLRRFYGKAPALVEICMHSGARVPQRYKAMMRLDIIVPDSQEADMVA
Protein: Hydroxycarboxylic acid receptor 2 (G-protein coupled receptor 109) (G-protein coupled receptor 109A) (G-protein coupled receptor HM74) (Niacin receptor 1) (Nicotinic acid receptor) (Protein PUMA-G) (Q9EP66)
Organism: Mus musculus (Mouse)
Function: Acts as a high affinity receptor for both nicotinic acid (also known as niacin) and (D)-beta-hydroxybutyrate and mediates increased adiponectin secretion and decreased lipolysis through G(i)-protein-mediated inhibition of adenylyl cyclase. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. Mediates nicotinic acid-induced apoptosis in mature neutrophils. Receptor activation by nicotinic acid results in reduced cAMP levels which may affect activity of cAMP-dependent protein kinase A and phosphorylation of target proteins, leading to neutrophil apoptosis.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Olfactory receptor 51E2
- Pro-neuropeptide Y
- Sodium-coupled monocarboxylate transporter 1
- Hydroxycarboxylic acid receptor 1
- Endothelin-1
- Appetite-regulating hormone
- Succinate receptor 1
- Oxytocin-neurophysin 1
Sequence:
MSKSDHFLVINGKNCCVFRDENIAKVLPPVLGLEFVFGLLGNGLALWIFCFHLKSWKSSRIFLFNLAVADFLLIICLPFLTDNYVHNWDWRFGGIPCRVMLFMLAMNRQGSIIFLTVVAVDRYFRVVHPHHFLNKISNRTAAIISCFLWGLTIGLTVHLLYTNMMTKNGEAYLCSSFSICYNFRWHDAMFLLEFFLPLAIILFCSGRIIWSLRQRQMDRHAKIKRAINFIMVVAIVFIICFLPSVAVRIRIFWLLYKYNVRNCDIYSSVDLAFFTTLSFTYMNSMLDPVVYYFSSPSFPNFFSTCINRCLRKKTLGEPDNNRSTSVELTGDPSTTRSIPGALMADPSEPGSPPYLASTSR
Protein: Troponin I, slow skeletal muscle (Troponin I, slow-twitch isoform) (P13413)
Organism: Rattus norvegicus (Rat)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin T, slow skeletal muscle
- Troponin T, cardiac muscle
- Troponin T, fast skeletal muscle
- Troponin C, slow skeletal and cardiac muscles
- Troponin C, skeletal muscle
- Myosin light chain 3
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin I, fast skeletal muscle
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin-6
Sequence:
MPEVERKSKITASRKLMLKSLMLAKAKECWEQEHEEREAEKVRYLSERIPTLQTRGLSLSALQDLCRELHAKVEVVDEERYDIEAKCLHNTREIKDLKLKVLDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVKKEDTEKERPVEVGDWRKNVEAMSGMEGRKKMFDAAKSPTLQ
Protein: Myofilin, isoform H (E1JIK6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFKNHLEMIGRNESPSKKAKFWQSYIRSLKGSEDIRAHEAPRASRPYSSYLDSPSYRSIYDEPATANERVQSSGYRYLPVSRDTYGYSPRAIYDHHYSRTIPANYDAEKAWNDHLKRMQEIERRYPSRYGLYLRDKPLTPNSLVPLEYEPEDKLLAELNKARRSASPFRPARTTRAGSEPYVPPPSYWNREGSVPRGGPSVFDRATSLAPFTRPSFRASSLEPLDELFEPEEEDLF
Protein: Glycosylphosphatidylinositol anchor attachment 1 protein, putative (C0H5L4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- GPI transamidase component GPI16, putative
- GPI-anchor transamidase
- GPI transamidase subunit PIG-U, putative
Sequence:
MGFSENPKFCLLINKLIKKSKVIGVFLSIIGVIFFLVFNKFNKNAELDARTFTQFVGNSVLNKKNEKFYNDTNSYFMNYTYEGKEDIIKLIYDYIRKNILVNVENEMVKIKLTDRIEQNILISNVGCKYCNNMESLVVVINFDFKERKYFHSVIIGLTLMEHFSKCNYMSKDVTFLFTNKELLYSLGVQEFIQKYFYNNTNRIGKKIIRSSTIIEFDSIYPSYIKINYEGLNGMLPNQDLILLLTNELHFYSIPIKMELTHGSIFDMALEKNYENGHIYFLRENIPAFTATGGSKVPIRNKMINLFNLTKALQSYLRSQSNTHEGFCHSSNFYFFNTFRRHIPISIYCYSVYLICAYSIMKLFKSTIFRSYINFLTGFYTYLITILIISLPIYLISTNKKFYELLNFEENYIPSCYEWHPDNFDKYIKIANIWWNVLFFSIFGAFFFNLFISFLVNKKRKVIPKKNDQNESFDGYKKVEKVERILILEKIKELQNEIMKRKGITNNHNNIKNYNIYTNENIYNNNINNINNNNNIYENLYDNGEVKKNILVKPKIINSDDEDFLLEKKNSEFIKKIEKQIEILEEKLEFLSNDENVKYIFYNNSIAPFNTMMIYMNIFYFILVALLSSLYNWSYSVLFSLLFVIPISILHNLKTKPVRIFKKIILSLFILCMFIYMYPNDNHLWNIRQKLTNLFRNNISKCCKYLDKHKILQSKYFPESLQFICSNRLFDSFYSNKYFLDNLNIKFSYVLDIQNGFLLTLYNLARNHFCIGTATYPLICFTLFPIVFYIVFLFFC
Protein: Calcium channel flower homolog (Calcium channel flower domain-containing protein 1) (Q9UGQ2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:D4A9I3}. Golgi apparatus {ECO:0000250|UniProtKB:D4A9I3}. Vesicle {ECO:0000250|UniProtKB:Q8BG21}. Note=In cytotoxic T-lymphoocytes, localizes to intracellular vesicles that move to the immuno synapse (By similarity). Enriched in synaptic vesicles at the presynpatic vesicles (By similarity). Detected in the Golgi apparatus of cultured hippocampal neurons (By similarity). {ECO:0000250|UniProtKB:D4A9I3, ECO:0000250|UniProtKB:Q8BG21}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:37348560}; Multi-pass membrane protein {ECO:0000269|PubMed:37348560}. Early endosome {ECO:0000269|PubMed:37348560}. Recycling endosome {ECO:0000269|PubMed:37348560}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:37348560}; Multi-pass membrane protein {ECO:0000269|PubMed:37348560}.
Interaction partners:
Sequence:
MSSSGGAPGASASSAPPAQEEGMTWWYRWLCRLSGVLGAVSCAISGLFNCITIHPLNIAAGVWMIMNAFILLLCEAPFCCQFIEFANTVAEKVDRLRSWQKAVFYCGMAVVPIVISLTLTTLLGNAIAFATGVLYGLSALGKKGDAISYARIQQQRQQADEEKLAETLEGEL
Protein: Enoyl-CoA hydratase (EC 4.2.1.17) (Enoyl-CoA hydratase EchA3 (Enoyl hydrase) (Unsaturated acyl-CoA hydratase) (Crotonase)) (Enoyl-CoA hydratase echA17) (Enoyl-coA hydratase homolog) (P96907)
Organism: Mycobacterium tuberculosis
Interaction partners:
- Acyl-CoA dehydrogenase
- Glutaryl-CoA dehydrogenase
- Acyl-CoA dehydrogenase)
- (R)-benzylsuccinyl-CoA dehydrogenase (Acyl-CoA dehydrogenase) (Acyl-CoA dehydrogenase family protein)
- Acyl-CoA dehydrogenase
- Acyl-CoA dehydrogenase
- Acyl-CoA dehydrogenase FadE23
- Putative acyl-CoA dehydrogenase FadE35
- 3-hydroxybutyryl-CoA dehydrogenase
- Acetyl-/propionyl-CoA carboxylase, AccD1
Sequence:
MSDPVSYTRKDSIAVISMDDGKVNALGPAMQQALNAAIDNADRDDVGALVITGNGRVFSGGFDLKILTSGEVQPAIDMLRGGFELAYRLLSYPKPVVMACTGHAIAMGAFLLSCGDHRVAAHAYNIQANEVAIGMTIPYAALEIMKLRLTRSAYQQATGLAKTFFGETALAAGFIDEIALPEVVVSRAEEAAREFAGLNQHAHAATKLRSRADALTAIRAGIDGIAAEFGL
Protein: F-box and WD repeat domain containing 8 (A0A499FIY5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKNEMNDVPFFDIQLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLCQQEGHLPDSSISDYSCWKLIFQECRAKEHMLRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIAGYTSGDVRVWDTRTWDYVAPFLESEDEEDEPGMQPNVSFVRINSSLAVAAYEDGFLNIWDLRTGKYPVHRFEHDARIQALALSQDDATVATASAFDVVMLSPNEEGYWQIAAEFEVPKLVQYLEIVPETRRYPVAVAAAGDLMYLLKAEDSARTLLYAHGPPVTCLDVSANQVAFGVQGLGWVYEGSKILVYSLEAGRRLLKLGNVLRDFTCVNLSDSPPNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVQMDDWKIVSGGEEGLVSVWDYRMNQKLWEVYSGHPVQHISFSSHSLITANVPYQTVMRNADLDSFTTHRRHRGLIRAYEFAVDQLAFQSPLPVCRSSCDAMATHYYDLALAFPYNHV
Protein: Protein phosphatase 1 regulatory subunit 16A (Myosin phosphatase-targeting subunit 3) (Q96I34)
Organism: Homo sapiens (Human)
Function: Inhibits protein phosphatase 1 activity toward phosphorylase, myosin light chain and myosin substrates.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Alanine aminotransferase 1
- demerged
Sequence:
MAEHLELLAEMPMVGRMSTQERLKHAQKRRAQQVKMWAQAEKEAQGKKGPGERPRKEAASQGLLKQVLFPPSVVLLEAAARNDLEEVRQFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINACDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDLCDDEQTLDCLETAMADRGITQDSIEAARAVPELRMLDDIRSRLQAGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQDGWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVCGDEEVRAKLLELKHKHDALLRAQSRQRSLLRRRTSSAGSRGKVVRRVSLTQRTDLYRKQHAQEAIVWQQPPPTSPEPPEDNDDRQTGAELRPPPPEEDNPEVVRPHNGRVGGSPVRHLYSKRLDRSVSYQLSPLDSTTPHTLVHDKAHHTLADLKRQRAAAKLQRPPPEGPESPETAEPGLPGDTVTPQPDCGFRAGGDPPLLKLTAPAVEAPVERRPCCLLM
Protein: Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (Q700Q7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAEDSESAASQLSLELDDQDTCGIDGDNEEETEHAKGSPGRDLGAKKKKKKQKRKKEKPNSGGTKSDSASDSQEIKIQQSSKHNAIWQQISAGAAMGGDTMEGEWIDLRMYHKNPTIPIQKLQDIQRAMELLSACQGPARNIDEATKRRYQFWDTQPVPKLNEVITSHGAIEPDKDNIRQEPYSLPQGFMWDTLDLSNAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLEGFISAIPANIRIYDSVKRMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPVATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIRAVRELINVYLKQFHLAPVMGDEEVAHWFLPREHIIDTFVVESPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMNDALIIAKLKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ
Protein: MICOS complex subunit MIC13 (A0A140TA86)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU363009}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU363009}.
Interaction partners:
Sequence:
MRSECVLGAASDSGQEAPRDTWFLQGWKASRRFLIKGSVAGGAVYLVYDQELLGPSDKSQAALQKAGEVVPPAMYQFSQYVCQQTGLQIPQLPAPPKIYFPIRDSWNAGIMTVMSALSVAPSKAREYSKEGWEYVKARTK
Protein: KIF-binding protein (KIF1-binding protein) (Kinesin family binding protein) (Q96EK5)
Organism: Homo sapiens (Human)
Function: Required for organization of axonal microtubules, and axonal outgrowth and maintenance during peripheral and central nervous system development.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16225668, ECO:0000269|PubMed:20621975, ECO:0000269|PubMed:23427148}.
Interaction partners:
- Kinesin-like protein KIF15
- Kinesin-like protein KIF18A
- Kinesin-like protein KIF1C
- Kinesin-like protein KIF1B
Sequence:
MANVPWAEVCEKFQAALALSRVELHKNPEKEPYKSKYSARALLEEVKALLGPAPEDEDERPEAEDGPGAGDHALGLPAEVVEPEGPVAQRAVRLAVIEFHLGVNHIDTEELSAGEEHLVKCLRLLRRYRLSHDCISLCIQAQNNLGILWSEREEIETAQAYLESSEALYNQYMKEVGSPPLDPTERFLPEEEKLTEQERSKRFEKVYTHNLYYLAQVYQHLEMFEKAAHYCHSTLKRQLEHNAYHPIEWAINAATLSQFYINKLCFMEARHCLSAANVIFGQTGKISATEDTPEAEGEVPELYHQRKGEIARCWIKYCLTLMQNAQLSMQDNIGELDLDKQSELRALRKKELDEEESIRKKAVQFGTGELCDAISAVEEKVSYLRPLDFEEARELFLLGQHYVFEAKEFFQIDGYVTDHIEVVQDHSALFKVLAFFETDMERRCKMHKRRIAMLEPLTVDLNPQYYLLVNRQIQFEIAHAYYDMMDLKVAIADRLRDPDSHIVKKINNLNKSALKYYQLFLDSLRDPNKVFPEHIGEDVLRPAMLAKFRVARLYGKIITADPKKELENLATSLEHYKFIVDYCEKHPEAAQEIEVELELSKEMVSLLPTKMERFRTKMALT
Protein: Basonuclin 2 (Zinc finger protein basonuclin-2 isoform 1) (A0A0R4IKC9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MRCDVTWAKVRRTRKRVRLGFQMMGCVPLPPLSRDRRDRLEQKSAQSEETELDVRGGVVWRERDRERARESTARASSRSSSSSSGAGGGGGEEGESSMQFSTRPASAEPGFMGTWTQQSTDSNLLFRMSQQAIRCTLVNCTCECFQPGKIHLRTCDQCKHGWVAHALDKLSTQHLYHPTQVEIVQSNVVFDISSLMLYGTQAVPVRLKILLDRLFSVLKQEEVLHILHGLGWTLRDYVRGYILQDAAGKVLDRWTIMSREEEIITLQQFLRFGETKSIVELMAIQEKEGQAVTVPSSKTDSGIRTFIESNNRTRSPGLLSHLENNSPSSIHHFENIPNSLAFLLPFQYINPMSAPMLGLPPNGLSIEQSGLRMREPNLPNQSDPVEASESEVSLSPFHSGQSPSRGVMGTLPNAIEPKTEPNRASPISPTPSTLQSQQPQTPTQQTQGQQQSSSLNNHQIHHHFEKNEQSKTITHSSFSSKMHRIRRMGATSRKGRVCCNSCGKTFYDKGTLKIHYNAVHLKIKHRCTIEGCNMVFSSLRSRNRHSANPNPRLHMPMLRNNRDKDLIRSSSGTATPVISSTKSGFNLTSPGRPPLSFATPPLEPMIQSPLQSPLVFPSLKSVQPVQPVPPFYRTLLSPADLVSPPVSLPTSPILPTTANSTSLTDQQQMLAVSSLSMHVSETSPFSHRLPTNHSTQDSIILDPMPKKKPRKSSMPVKIEKEVIDVADDYDDKDEDDDDGDSCHHHHHQPSSIHNVNGNCNNNNNGSSSSSHHCGGSGHESPSHDEMSPSQALRGMLHPEQEECTGSHGGRGHGDLRCIDSFTSEDQDHERDFENESETSESKMLYRDELMDTDINQTALGKNMDKEHQGTEDDQHLRKDLDEHSHSPPSQHQPVIKIKEEINDPTYDMFCMGQYSLYNGGMAAAAAAAASMAALHESFISSMSYGTSTPKFPSQSPEGDLCSSPDPKICYVCKKSFKSSYSVKLHYKNVHLKEMHVCTVSGCNAAFPSRRSRDRHSSNINLHRKLLTKELDDIVLDPQLTTLPKQLRAEFLSKIYADHHTGLEGVGGFDNGPPQSRGHEGMRSQVAREYSHSNGYCHGPNDDYVVLDLSTASSVQSSGSVQSSHESDEGSDEGILLDDLEDASDTEDCTPSTGAQRLSMEGKNREEAGKEEREGETDERILHYDPSVSPSILASSGGNGTGGILCTICHKLYSNKGTLRVHYKTVHLREMHKCKIPGCNMMFSSVRSRNRHSQNPNLHKKAPYTTMID
Protein: Radical SAM domain protein (Q726V2)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- NeuB family protein
- WbqC-like family protein
- Aminotransferase, DegT/DnrJ/EryC1/StrS family
- Radical SAM domain protein
- Aminotransferase, DegT/DnrJ/EryC1/StrS family
- Flagellar basal-body rod protein FlgC
- Polysaccharide biosynthesis protein/methyltransferase, putative
- Tetratricopeptide TPR_2 repeat protein
- Pyruvate:ferredoxin oxidoreductase
- Radical SAM domain protein
Sequence:
MRANSLSRSTIRANMPTRRVWGRPRWPAYCLRQGGSHTSSVEPRKPASRAMNASRSLPPVIIQATNIAPLRGKHLLPLVEGRTVIEVLIGRLRGIWHDDICVATSDLPDDDALCAHVAALGAQVVRGPHRDLVKRLILAAEAMHCDHFVRVMGAAPFVCIPRLADLAAEHAERGVEFSYNEHRMGVPRGLGGQVVSVDMLKRLDAADISAEVRQEFAYSVLQNAEHFAVHRQDSDLPRLALDFHLETTKDLSLLREIAVNVPDVTIEAIIDYAAQHPALHTLSRAFPPKEVGLEKLFLHPEKILALTSQNGLPDASFPVSVELSLTNRCNLACVWCSDKDLRGRQGVKATLSLDTVRRLTHELREGGTKGIVIEGGGEPTLHPDFAAIVACITDAGMGAGLITNGVVTLPPDVLRRLDWVRVSLDSSTRAEFQNAKGRDAFETVMGNIAHFARHCPTVGIGYVVTRHNTEHLESLVLRARQAKASYIQFRPVIDAPDIAPEDFNLDYLKLFETDGFCVNTDAMRDNQVRGNSNLPCRAHPLTSVIGADGSVHLCGRLNIFDWFEPIGNINEQSFGDIWRGAKRKSAAKALADPGFCGQWCPECRITKFNQLLWRLSQSRTRNFI
Protein: UNC-45 (G5EG62)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
- Heat shock protein 90
- Ubiquitin conjugation factor E4 ufd-2
- Myosin-4
- Myosin motor domain-containing protein
- Heat shock protein 70
- Myosin-11
- Paramyosin
- Unconventional myosin-Ie
- Myosin-3
- VWFA domain-containing protein
Sequence:
MVARVQTAEEIRDEGNAAVKDQDYIKADELYTEALQLTTDEDKALRPVLYRNRAMARLKRDDFEGAQSDCTKALEFDGADVKALFRRSLAREQLGNVGPAFQDAKEALRLSPNDKGIVEVLQRLVKANNDKIKQTTSLANKVTDMEKLAFRGEAKDTEQKMTALNNLLVLCRESESGATGVWNQGALVPFVLNLINDASENEEVTVTAIRILDETIKNSVRCMKFLAMHDPDGPKSVRFVCRLMCKKSTKDFVDATGILVQRVFNAMAKMDRQKEMKPDPEVAEANKIWIIRVLLELQEMLQDPKVGAVQRETCIDLFLKNLMHMDGGIPRGWSWKFVEERGLLALLDVASQIPELCEYPVSAETRQHVAICLQRLEEDMVFDTKRTIFKEKVDMFFNALISRCTNDDEGHKYRIKLSCFLITMLQGPVDIGINLITNDQLTPIMLEMAASQDHLMQGIAAELIVATVSKHERAINMLKVGIPVLRALYDSEDPTVKVRALVGLCKIGAAGGDDISKATMKEEAVISLAKTCKKFLLETEKYSVDIRRYACEGLSYLSLDADVKEWIVDDSLLLKALVLLAKKAGALCVYTLATIYANLSNAFEKPKVDEEMVKLAQFAKHHVPETHPKDTEEYVEKRVRALVEEGAVPACVAVSKTESKNALELIARSLLAFAEYEDLRGRIIAEGGTVLCLRLTKEASGEGKIKAGHAIAKLGAKADPMISFPGQRAYEVVKPLCDLLHPDVEGKANYDSLLTLTNLASVSDSIRGRILKEKAIPKIEEFWFMTDHEHLRAAAAELLLNLLFFEKFYEETVAPGTDRLKLWVLYSAEVEEERLSRASAAGFAILTEDENACARIMDEIKSWPEVFKDIAMHEDAETQRRGLMGIANIMHSSNKLCSEIVSSEVFRVLVAVTKLGTINQERAGSTEQAKRGLEAAEKFGLIKATDREIYERENQMSTIQE
Protein: Guanine nucleotide exchange factor for Rab-3A (Rab-3A-interacting-like protein 1) (Rab3A-interacting-like protein 1) (Rabin3-like 1) (Q99NH3)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide exchange factor (GEF) which may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May also activate RAB8A and RAB8B (By similarity).
Interaction partners:
- Ras-related protein Rab-8A
- Ras-related protein Rab-8B
- Ras-related protein Rab-11A
- Ras-related protein Rab-3A
- Ras-related protein Rab-11B
Sequence:
MWSGPPQQDEGLPVGLSAISVPWKNLGPSKGNRKSPGGLVEASASWEEAGGEEHPAAAPLDVSRLRSSSMEIREKGSEFLKEELYKAQKELKLKDEECERLCKVRAQLEQELEELTASLFEEAHKMVREANMKQAASEKQLKEAWGKIDMLQAEVTALKTLVITSTPASPNRELHPQLLSPTKAGPRKGHSRQKSTSSLCPVVCPTAGHIPTPDKEGKEVDTTLFAEFQAWRASPTLDKNCPFLERVYREDVGPCLDFTVQELSALVRTAVEDNTLTIEPVASQTLPNVECNNTNTCALSGLARTCHHRIRLGDSDGHYYISPSSRARITAVCNFFTYVRYIQQGLVRQDAEPMFWEIMRLRKGMSLAKLGFFPQEA
Protein: F-box protein SKP2A (FBL5-like protein) (AtFBL5) (SKP2-like protein 1) (AtSKP2;1) (Q9LPL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(SKP2A) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (including cell cycle repressors). Acts as an auxin receptor; one active auxin is indole-3-acetate. Regulates the stability of the transcription factors E2FC and DPB, repressors of cell proliferation. Confers increase tolerance to osmotic stress by promoting cell division, especially in meristems. Promotes the formation of lateral root primordia.
Subcellular location: Nucleus {ECO:0000269|PubMed:18036202}.
Interaction partners:
- Transcription factor-like protein DPB
- F-box protein SKP2B
- Auxin-binding protein 1
- Transcription factor E2FC
- Cullin-1
- SKP1-like protein 1A
- Protein-tyrosine-phosphatase IBR5
Sequence:
MVMGGEASMELDQCFQKMKMEGISIKEWKDIPVELLMRILSLVDDRNVIVASGVCTGWRDAISFGLTRLRLSWCNNNMNSLVLSLVPKFVKLQTLNLRQDKPQLEDNAVEAIANHCHELQELDLSKSLKITDRSLYALAHGCPDLTKLNLSGCTSFSDTAIAYLTRFCRKLKVLNLCGCVKAVTDNALEAIGNNCNQMQSLNLGWCENISDDGVMSLAYGCPDLRTLDLCGCVLITDESVVALADWCVHLRSLGLYYCRNITDRAMYSLAQSGVKNKPGSWKSVKKGKYDEEGLRSLNISQCTALTPSAVQAVCDSFPALHTCSGRHSLVMSGCLNLTTVHCACILQAHRAHNAVPHPAH
Protein: Cuticle collagen bli-1 (Blistered cuticle protein 1) (Q09457)
Organism: Caenorhabditis elegans
Function: Probable cuticular collagen-like protein (Probable). Nematode cuticles are composed largely of collagen-like proteins (Probable). The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment (Probable). Acts downstream of the Wnt signaling pathway; perhaps in the formation of the adult cuticle. Required for proper strut formation within the unique medial layer of the adult cuticle (Ref.2).
Subcellular location: Nucleus {ECO:0000269|PubMed:24569038}.
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
- CPG4 domain-containing protein
Sequence:
MVKSYTLAGLAAIACLLLAIGAVISTVYILNDISDFYSEAQEELVEFKDIANNIWEEMVFELTPEEMREAEDNDREKRSYEPEGPYQSETTTPSTTTSTAATTTEAAEDESGYDFVNDNGPPSSRPRKPEPPTMPRTIQGFRAPPPAATSTYRPPHGSNYDNYGREPASSRRPYPPQQPPSTSAPHSSPNNRTSLYNPQPPPKTGYPTNPRVPYNPPQPNYTRQPTYPEDNRAPYKPTRSPNTPPPRQPSGGYDSDGQTPPSSPRIYNTRRPNNHGPGYPEDQVPTAPPVPGQQRVPPTQTRNPPNPTNTRQPSRPVPPTSDGHIEATTPYNPSAQYPTGKRGSHPGFGPQRPRPGTRPRGNPCDQCSAQPNHCPSGPPGPRGRPGPPGFPGQDGPRGLRGLNGGYSGVQPSSYDPVIGCVQCPIGPPGERGPDGTPGVPGEDGIDGEQGVNGQDGQPGAPGAPGYHGMNGSPGTPGKPGLPGRNGQSCKSIPGPPGQPGVMGVPGRDGDPGTDGEHGQDGSPGIQGPPGRDGTSGPDGQPGVSAPGAPGTDGGYCPCPKRSSKFDFNDAYNDDEKRGLEEHRPRGYDSERAEEPRPRQTVRTNTYDENSGAEHQRRPNYEPSAEVAPPRQDRYEDEERVREPPPKRPPPPHRQTPHELYPEEQPYVRRPPPPQNRGNYEVERSREYVPEAPRPRQGYEHSSGYGGDDRKEQPKYMESRPVDEPRYETDAPSRSRPLKKVEIIRHPERGYDRRQPSYEDSKPRQEEPRRYETEAEPRYEEVPRKETHPPGFGRPKSEENPRETGRTYSEEAMPPVQQTEKYNGDKRKKNQPEYEDISKPEEDKERAMEKHHKKPNKFQEKQWEEHRKSQELRNSREHGGQVPVETSVPMQQVKPESSAEEKPVPPVHDNFQSSEKRAFSNENPLPSEQIPYRRRNRFYRNHYYEKFLV
Protein: Heat shock protein cognate 20 (MIP14027p) (A8JNT7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Iron-sulfur cluster assembly enzyme IscU
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Heat shock 70 kDa protein cognate 5
- Glutaredoxin-related protein 5, mitochondrial
Sequence:
MSRVINGFKSAVKATNYTPLVRNAAQFNQFQLPEIRKFSVESSPACWNCQKKSELKQNMICSDCGHLQDVNSGINYFKLLSFPIQFSLESQKLTRSFRQLQTIVHPDKYSNKTSREQTNSSDWSSLINKAYKTLSTPIDRGQYLLQLEGEQMPQDNSALNKEFLMAMMERNEEVEDAEDTQTLENLNIQLIKELEEMARKLNALFDSKDLSGVKETLVEMKYLLSIQNSIKQKQQSLLGS
Protein: Angiopoietin-1 (ANG-1) (O08538)
Organism: Mus musculus (Mouse)
Function: Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:8980223}.
Interaction partners:
- Angiopoietin-1 receptor
- Tyrosine-protein kinase receptor Tie-1
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 1
- Angiopoietin-2
- Platelet-derived growth factor receptor beta
- Vascular endothelial growth factor receptor 3
- Angiopoietin-4
- Epidermal growth factor receptor
- Macrophage colony-stimulating factor 1 receptor
Sequence:
MTVFLSFAFFAAILTHIGCSNQRRNPENGGRRYNRIQHGQCAYTFILPEHDGNCRESATEQYNTNALQRDAPHVEPDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTVHNLISLCTKEGVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF