wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66) (Jumanjic domain protein 1) (O01658)
Organism: Caenorhabditis elegans
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Mediates response to multiple stress stimuli, including heat shock and osmotic, oxidative, and ethanol stress.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL2
Sequence:
MGKKKNSNKSAAAAPAVKHNDRWSSIELGEAKSAAVSHYKEPSKEPKFVHPAKLEKVKRIHDGLNIDRVLSHGPVPKQNGGTKRKHVEVTTQKLENKKPKVEVKKEDEKSKNKKMKNQNKHTALVQNETSTRSTYFVEEPDNENKVTLISNGREIAFKKTEVVESDDEQMIGLDSDEELEDEDETDIDEDEMMIDPKDIERYINFESVEDEEDMEDEEIEDEEFEDEEFEDEEEEADEQEEEEEDVSDEESVVSEMDADSDDEGFIAGKDREAHVISKDKFTRNAPAVDFDKFPFTDEDSVVTSSRAFGFMISPCDVQTFFDKFYQSNVLVVRRKQPTYFGNLFSTARLGELLEKNHLEYGRNINIAQYKNGVRTTLNGQGRAYPQIVKQHLHNMCSVQLVNPQTYDDRIWYLCEVIQEQFGCFVGANTYLTPAGSSGFAPHWDEIDAFLLQVEGRKYWRVWAPESAEEELPLESSDNFTEDDMKGREPVFEGWIEKGDMIYIPRGYIHQARTDSKVHSLHVTVSTGRQWSFANLMEKVVPEAIGVLTDTRHKLRRGLPTGLFDMGGVIDLDYSQEDHFVEKFKMVVDRHMSMLRNLVADQLLESSVDSLAKEFMKQALPPRLTEQEKKLSVLGSSTNLLGDDLVDFTARTKVRLIRRHTQRLLMESEDACFISHRINNSRLFEGRPEQIVEYPISGIDAYRVLSNSYPEWRTLYEIFSLRETKTKSRKENLAAIQLLFQIGVLLVKN
Protein: Alpha-1,3-mannosyltransferase MNT3 (EC 2.4.1.-) (P40549)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mannosyltransferase involved in adding the 4th and 5th mannose residues of O-linked glycans.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLKSLKSRRLILKRLVTLLLSLFFSYLIFSASRNVTSSNKLNNHASERTAVESSAFNWIEKRQHQVRSENLMNRLSAYFLPFLSRSSHKERVLLRQLGNNEIAKSDKCRYIFEVLYKIDPDWDNAQTAKFYNVDGVDNTLASLLGERLRSYDYCFLSGQLDPTAIFANSTVNPHDLQNRMFPFLKKINEESKTVMWPIITDMTTGEAVPAPEVDMESSNFNGNFWSNWNRLSKGRGFVLTIAEKDVPLFLKQLKVMEFSKNELPFQIVSTGNELSAESIAKISETAKETEQRVYLVDCSTVLDTNFANTYISFFQNKWVATLFNTFEEYILLDADVVPFVGSDYFFDSPSYRESGILLFKDRVMENEQTFQYCIEMLNEVEPSAQERRFIGSRLVFDSSLPFSSETSEEASVYYNFFKKLRLHHVDSGLVVVNKLEKLNGLLMSFMLNLDGKLQRCVYGDKEIFWLGQLYAGQDYSINPVDGSIIGPVNEEPENDDGHKSGMYYICSTQIAHSDSKNRLLWVNGGLKTCKISNSAEDDFGREPEYFKSRYGDISKLKRIYDASLNVEGLIVPDVSVHPWMQIKECSNYMYCAYATGDGHTNSELDEGRLITFTEKELRYINDISRTWNAN
Protein: Phosphatidylinositol:ceramide inositolphosphotransferase 1 (EC 2.7.8.-) (Inositol-phosphorylceramide synthase 1) (AtIPCS1) (IPC synthase 1) (Protein ERH1-like2) (Sphingolipid synthase 1) (Q9M325)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of the phosphorylinositol group from phosphatidylinositol (PI) to phytoceramide, an essential step in sphingolipid biosynthesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Uncharacterized CRM domain-containing protein At3g25440
- Ceramide synthase LOH2
- Proline-rich extensin-like protein EPR1
- Long chain base biosynthesis protein 2b
- Sphingosine-1-phosphate lyase
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Phosphoinositide phospholipase C 1
- Long chain base biosynthesis protein 2a
- Phosphoinositide phospholipase C 3
Sequence:
MTLYIRREASKLWRRFCSEITTEIGLLAENWKYLLAGLLCQYIHGLAARGVHYIHRPGPTLQDSGFFVLPELGQDKGFISETVFTCVFLSFFLWTFHPFIVKSKKIYTVLIWCRVLAFLVACQFLRVITFYSTQLPGPNYHCREGSELARLPRPHNVLEVLLLNFPRGVIYGCGDLIFSSHMIFTLVFVRTYQKYGSKRFIKLLGWVIAILQSLLIIASRKHYTVDVVVAWYTVNLVVFFLDKKLPELPDRTTALLPVISKDRTKEESHKLLNGNGVDPADRRPRAQVNGKDSNGGHTDNATNGT
Protein: Forkhead box protein C2 (Brain factor 3) (BF-3) (Forkhead-related protein FKHL14) (Mesenchyme fork head protein 1) (MFH-1 protein) (Transcription factor FKH-14) (Q61850)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator. Might be involved in the formation of special mesenchymal tissues.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99958}.
Interaction partners:
- Zinc finger protein SNAI1
- Zinc finger E-box-binding homeobox 1
- Forkhead box protein D1
- Twist-related protein 1
- Integrin alpha-9
- Lymphatic vessel endothelial hyaluronic acid receptor 1
- Zinc finger protein SNAI2
- Recombining binding protein suppressor of hairless
Sequence:
MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYGAGMGRSYAPYHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVPKDKEERAHLKEPPSTTAKGAPTGTPVADGPKEAEKKVVVKSEAASPALPVITKVETLSPEGALQASPRSASSTPAGSPDGSLPEHHAAAPNGLPGFSVETIMTLRTSPPGGDLSPAAARAGLVVPPLALPYAAAPPAAYTQPCAQGLEAAGSAGYQCSMRAMSLYTGAERPAHVCVPPALDEALSDHPSGPGSPLGALNLAAGQEGALGASGHHHQHHGHLHPQAPPPAPQPPPAPQPATQATSWYLNHGGDLSHLPGHTFATQQQTFPNVREMFNSHRLGLDNSSLGESQVSNASCQLPYRATPSLYRHAAPYSYDCTKY
Protein: Alpha-tubulin N-acetyltransferase 2 (Alpha-TAT 2) (TAT 2) (EC 2.3.1.108) (Mec-17-like protein) (Q23192)
Organism: Caenorhabditis elegans
Function: Specifically acetylates 'Lys-40' in alpha-tubulin/mec-12 on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for the maintenance of touch receptor neurons and possibly other type of neurons involved in locomotion.
Interaction partners:
- Methyltransferase domain-containing protein
- Tubulin alpha-3 chain
- Tubulin beta-1 chain
- Tubulin-specific chaperone cofactor E-like protein
Sequence:
MEIAFDLSTIFTDNIQRLTRTDLLKYGPKRYWAVAQSIDCLGEMSSKFHGWKRVITMYDKIVDHDEEQTTYIMWEKVNGSKSILKGLLRVGYKTLYLTDNEQNQYMEKAMCILDFFVVPTEQRSGNGFKMFDEMLKAENVTVDQCAFDKPSAALQQFLEKYYDRKDLVWQSNKYALCSNFFIGRHPTVPFTPRQTKRASRASSAVSSHASSRNTSPIGRNRPRHDSVADLMRQDMLAGVRAEVDPNSPTGLKNARDFGHRRIW
Protein: Gap junction alpha-1 protein (Connexin-43) (Cx43) (Gap junction 43 kDa heart protein) (P23242)
Organism: Mus musculus (Mouse)
Function: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26403541, ECO:0000269|PubMed:28507509}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum {ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20940304}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD is dependent on TMEM65. {ECO:0000269|PubMed:26403541}.
Interaction partners:
- Tight junction protein 1
- Gap junction alpha-5 protein
- Proto-oncogene tyrosine-protein kinase Src
- Gap junction gamma-1 protein
- Mitogen-activated protein kinase 3
- Tubulin beta-3 chain
- Plakophilin-2
- Tubulin beta-4A chain
- E3 ubiquitin-protein ligase NEDD4
- Cadherin-2
Sequence:
MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDSQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI
Protein: Fibroblast growth factor 13 (FGF-13) (xFGF13) (A6P7H6)
Organism: Xenopus laevis (African clawed frog)
Function: Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules (By similarity). Through its action on microtubules, may participate in the refinement of axons by negatively regulating axonal and leading processes branching (By similarity). Plays a crucial role in neuron polarization and migration (By similarity). Regulates voltage-gated sodium channels transport and function (By similarity). Required for proper head development, it is involved in neural differentiation through regulation of the mek5-erk5 pathway.
Subcellular location: Cell projection, filopodium {ECO:0000250|UniProtKB:P70377}. Cell projection, growth cone {ECO:0000250|UniProtKB:P70377}. Cell projection, dendrite {ECO:0000250|UniProtKB:P70377}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P70377}. Cytoplasm {ECO:0000250|UniProtKB:P70377}. Note=Not secreted. Localizes to the lateral membrane and intercalated disks of myocytes. {ECO:0000250|UniProtKB:P70377}.
Interaction partners:
Sequence:
MAAAIASSLIRQKRQAREREKSNACKCVSSPSKSKGNCEKNKLNVFSRVKLFGSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQPDGTIDGAKEEESSATVFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSEHFTPECKFKESVFENYYVTYSSMIYRQQHSGRSWFLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSQNDST
Protein: Candida glabrata strain CBS138 chromosome A complete sequence (Q6FY51)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MVEWCVIVYDKPGSDRSTCRPQHLAGIPPLVEAGKLVCAGAIYNEPAQAGGERTFAGSHLQIVADTKEEALELVHNDVFAKNGIWDLENIIIYQFGCAVRQPKA
Protein: Transposon Tn7 transposition protein TnsA (Restriction enzyme-like endonuclease TnsA) (EC 3.1.21.-) (P13988)
Organism: Escherichia coli
Function: Required for Tn7 transposition. Forms the transposase, together with TnsB. TnsA executes the 5'-DNA strand breakage reaction. TnsABC and TnsD promote high-frequency insertion of Tn7 into a specific target site known as ATT-Tn7 whereas TnsABC and TnsD promote low-frequency insertion into many different sites.
Interaction partners:
Sequence:
MAKANSSFSEVQIARRIKEGRGQGHGKDYIPWLTVQEVPSSGRSHRIYSHKTGRVHHLLSDLELAVFLSLEWESSVLDIREQFPLLPSDTRQIAIDSGIKHPVIRGVDQVMSTDFLVDCKDGPFEQFAIQVKPAAALQDERTLEKLELERRYWQQKQIPWFIFTDKEINPVVKENIEWLYSVKTEEVSAELLAQLSPLAHILQEKGDENIINVCKQVDIAYDLELGKTLSEIRALTANGFIKFNIYKSFRANKCADLCISQVVNMEELRYVAN
Protein: Tryptophan synthase alpha chain (EC 4.2.1.20) (P07344)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Interaction partners:
- Indole-3-glycerol phosphate synthase
- Tryptophan synthase beta chain
- N-
- Anthranilate phosphoribosyltransferase
- Anthranilate synthase component 1
- anthranilate synthase
- aminodeoxychorismate synthase
- Anthranilate synthase component 2
- L-threonine dehydratase
- L-threonine dehydratase
Sequence:
MSRLQTRFAQLKQENRAALVTFVTAGDPDYASSLEILKGLPAAGADVIELGMPFTDPMADGPAIQLANIRALDGGQTLARTLQMVREFRSGDSETPLVLMGYFNPIHHYGVERFIAEAKEVGVDGLIVVDLPPEHNEDLCHPAQAAGIDFIRLTTPTTGDQRLPTVLEGSSGFVYYVSVAGVTGANAATLEHVEEAVARLRRHTDLPIGIGFGIRSAEHAAAVARLADGVVVGSALIDRIAKARDNAQAVKDVLALCGELAEGVRNAR
Protein: Splicing factor-like protein 1 (AtSF1) (SF1 homolog protein) (Q9LU44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for the splicing of pre-mRNA. Required during development and for abscisic acid (ABA) responses.
Subcellular location: Nucleus {ECO:0000269|PubMed:24580679}. Nucleus speckle {ECO:0000269|PubMed:32123040}. Note=Colocalizes in nuclear speckles with SF1. {ECO:0000269|PubMed:32123040}.
Interaction partners:
- Nuclear protein-like
- At2g32600/T26B15.16
- Cell division cycle 5-like protein
- Splicing factor SF3a60 homolog
- DEAD-box ATP-dependent RNA helicase 42
- RNA-binding
- RNA-binding
- DEAD-box ATP-dependent RNA helicase 45
- Serine/arginine-rich-splicing factor SR34
- Splicing factor U2af large subunit A
Sequence:
MESVEMNNPNSQTLDQPPPSSNGDTAPLALDHMNPQNSESVALNGSSTPIPDTNGSSAKPELLRPLLSENGVSKTLSGNDKDQSGGEEETTSRRKRRSRWDPPPSESINNPSAEGGTDSGTGTRKRKSRWADDEPRTQIQLPDFMKDFTGGIEFDPEIQALNSRLLEISRMLQSGMPLDDRPEGQRSPSPEPVYDNMGIRINTREYRARERLNRERQEIIAQIIKKNPAFKPPADYRPPKLHKKLFIPMKEFPGYNFIGLIIGPRGNTQKRMERETGAKIVIRGKGSVKEGRHQQKKDLKYDPSENEDLHVLVEAETQEALEAAAGMVEKLLQPVDEVLNEHKRQQLRELATLNGTIRDEEFCRLCGEPGHRQYACPSRTNTFKSDVLCKICGDGGHPTIDCPVKGTTGKKMDDEYQNFLAELGGTVPESSLKQSATLALGPGSSGSNPPWANNAGNGASAHPGLGSTPTKPPSKEYDETNLYIGFLPPMLEDDGLINLFSSFGEIVMAKVIKDRVTGLSKGYGFVKYADVQMANTAVQAMNGYRFEGRTLAVRIAGKSPPPIAPPGPPAPQPPTQGYPPSNQPPGAYPSQQYATGGYSTAPVPWGPPVPSYSPYALPPPPPGSYHPVHGQHMPPYGMQYPPPPPHVTQAPPPGTTQNPSSSEPQQSFPPGVQADSGAATSSIPPNVYGSSVTAMPGQPPYMSYPSYYNAVPPPTPPAPASSTDHSQNMGNMPWANNPSVSTPDHSQGLVNAPWAPNPPMPPTVGYSQSMGNVPWAPKPPVQPPAENPSSVGESEYEKFMAEMK
Protein: Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (PEPCK-C) (EC 4.1.1.32) (Serine-protein kinase PCK1) (EC 2.7.11.-) (P05153)
Organism: Gallus gallus (Chicken)
Function: Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle. At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate. In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P35558}.
Interaction partners:
- Lipoyl-binding domain-containing protein.
- Citrate synthase, mitochondrial
- ATP-citrate synthase
- Alpha-enolase
- Malate dehydrogenase
- Pyruvate kinase PKM
- Enolase 4
- Gamma-enolase
- Malate dehydrogenase, cytoplasmic
- Phosphoenolpyruvate carboxykinase, mitochondrial
Sequence:
MAPELKTEVNIISKVIQGDLESLPPQVREFIESNAKLCQPESIHICDGSEEENKKILDIMVEQGMIKKLSKYENCWLALTNPRDVARIESKTVIITQEQRDTIPIPKTGSSQLGRWMSEEDFEKAFNTRFPGCMQGRTMYVIPFSMGPIGSPLAKIGIELTDSPYVVASMRMMTRMGTAALKALGNGEFVKCLHSVGCPLPLKEPLINNWPCNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRIASRIAKEEGWLAEHMLILGITNPEGEKKYFAAAFPSACGKTNLAMMNPSRPGWKIECVGDDIAWMKFDELGNLRAINPENGFFGVAPGTSIKTNPNAIKTIFKNTIFTNVAETSDGGVYWEGIDEPLPPGVTLTSWKNKDWTPDNGEPCAHPNSRFCTPASQCPIMDPAWESPEGVPIEGIIFGGRRPAGVPLVYEAFNWQHGVFIGAAMRSEATAAAEHKGKIIMHDPFAMRPFFGYNFGKYLAHWLSMAHRPAAKLPRIFHVNWFRKDSQGKFLWPGYGENSRVLEWMFNRIQGKASAKSTAIGYIPADTALNLKGLEDINLTELFNISKEFWEKEVEEIKQYFEGQVNADLPYEIERELLALEMRIKQL
Protein: GID complex subunit 1 (Glucose-induced degradation protein 1) (Vacuolar import and degradation protein 30) (O94712)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P53076}. Cytoplasm {ECO:0000250|UniProtKB:P53076}.
Interaction partners:
- GID complex subunit 8
- GID complex substrate-recognition subunit 4
- GID complex subunit 7
- GID complex substrate-recognition subunit 10
- GID complex subunit 9
- E3 ubiquitin-protein ligase gid2
- Protein yippee-like PJ691.02
- Fructose-1,6-bisphosphatase
- ATP-dependent RNA helicase ded1
- Mei4-dependent protein 6
Sequence:
MTSTPKNLEKQPINFDNLPLYLQGTNYGENVLRSDPRWLKWEKYLREFDMTREGNVTNTPKAIPSSWNPNDKSDSLELMNNNMGVYFFGPEAGTEHDAASVKADHAIPSNTSIYYYEIQILSRGKEGKMGVGFCRKSMQTNRLPGCTAESWGYHGNSGEKFNCSKTGEAYGPEFTTGDIIGCGVNFINRTIFYTKNGAYLGVAFKKVSDVLYPVIGLKSHGEHVEVNFGQNPFLYDIDYAIQMEKNKLFEQATKSPKQEELKQRQEFLNELISSFLLNNGFVETAKKFCPENTEVSDASIRKEISSMLANGQLDLAMTKIDCQYPVAIQECPDLIMSLRFLRFLQLVKVTHDQRLTKSKGTKQISQEEDLRILQPLMNYAQELSNDYEHTKSSNLQAMIKLSMGLLAYFDPFSSPLSFFMSSDFHKYMAEQINCLLLELTGHSPDSELRRFLQHTVCLNDLLCRNGCRSNTLFNVQSDFLSPY
Protein: Kelch-like protein 18 (O94889)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL18) E3 ubiquitin ligase complex mediates the ubiquitination of AURKA leading to its activation at the centrosome which is required for initiating mitotic entry. Regulates light-and dark-dependent alpha-transducin localization changes in rod photoreceptors through UNC119 ubiquitination and degradation (By similarity). Preferentially ubiquitinates the unphosphorylated form of UNC119 over the phosphorylated form (By similarity). In the presence of UNC119, under dark-adapted conditions alpha-transducin mislocalizes from the outer segment to the inner part of rod photoreceptors which leads to decreased photoreceptor damage caused by light (By similarity).
Interaction partners:
- Cullin-3
Sequence:
MVEDGAEELEDLVHFSVSELPSRGYGVMEEIRRQGKLCDVTLKIGDHKFSAHRIVLAASIPYFHAMFTNDMMECKQDEIVMQGMDPSALEALINFAYNGNLAIDQQNVQSLLMGASFLQLQSIKDACCTFLRERLHPKNCLGVRQFAETMMCAVLYDAANSFIHQHFVEVSMSEEFLALPLEDVLELVSRDELNVKSEEQVFEAALAWVRYDREQRGPYLPELLSNIRLPLCRPQFLSDRVQQDDLVRCCHKCRDLVDEAKDYHLMPERRPHLPAFRTRPRCCTSIAGLIYAVGGLNSAGDSLNVVEVFDPIANCWERCRPMTTARSRVGVAVVNGLLYAIGGYDGQLRLSTVEAYNPETDTWTRVGSMNSKRSAMGTVVLDGQIYVCGGYDGNSSLSSVETYSPETDKWTVVTSMSSNRSAAGVTVFEGRIYVSGGHDGLQIFSSVEHYNHHTATWHPAAGMLNKRCRHGAASLGSKMFVCGGYDGSGFLSIAEMYSSVADQWCLIVPMHTRRSRVSLVASCGRLYAVGGYDGQSNLSSVEMYDPETDCWTFMAPMACHEGGVGVGCIPLLTI
Protein: Factor of DNA methylation 3 (Q9LHB1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in association with FDM4 and FDM5 for RNA-directed DNA methylation (RdDM).
Interaction partners:
- Protein SUPPRESSOR OF GENE SILENCING 3
- Glyoxylate/hydroxypyruvate reductase HPR3
- Protein IDA-LIKE 2
Sequence:
MNNKLSDFEKNLYKKLKSGKLEVKVSYRTFLCPYCPDNKKKVGLYVDILQHASGVGNSQSKKRSLTEKASHRALAKYLIKDLAHYATSTISKRLKARTSFIPAETGDAPIIYDDAQFEKLVWPWKGVLVNIPTTSTEDGRSCTGESGPKLKDELIRRGFNPIRVRTVWDRFGHSGTGIVEFNRDWNGLQDALVFKKAYEGDGHGKKDWLCGATDSSLYAWLANADDYYRANILGENLRKMGDLKSIYRFAEEEARKDQKLLQRLNFMVENKQYRLKKLQIKYSQDSVKLKYETEEKEKILRAYSEDLTGRQQKSTDHFNRIFADHEKQKVQLESQIKELEIRKLELAKREAENETQRKIVAKELEQNAAINSYVQLSALEQQKTREKAQRLAVDHKMQKEKLHKRIAALERQLDQKQELELEVQQLKSQLSVMRLVELDSGSEIVNKVETFLRDLSETEGELAHLNQFNQDLVVQERKSNDELQEARRALISNLRDMGLHIGVKRMGELDTKPFMKAMRIKYCQEDLEDWAVEVIQLWEEYLKDPDWHPFKRIKLETAETIVEVIDEDDEKLRTLKNELGDDAYQAVANALLEINEYNPSGRYISSELWNFREDRKATLEEGVNSLLEQWNQAKHLKS
Protein: 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (A0A8I6A4A3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
RSSRITAVVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATPGTEGERDSDDALLKMTISQQEFGRAGLPDLSSMTEEEQIAYAMQMSLQGAEFGQAESGDIDASSAMDTSEPVKEEDDYDVMQDPEFLQSVLENLPGVDPNNEAIRNAMGSLASQATKDGKKDKKEEEKK
Protein: Gamma-crystallin B (Gamma-B-crystallin) (Gamma-crystallin 3) (P04344)
Organism: Mus musculus (Mouse)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A chain
- Gamma-crystallin F
- Lens fiber major intrinsic protein
- Gamma-crystallin C
- Beta-crystallin A1
Sequence:
MGKITFFEDRSFQGRCYECSSDCPNLQTYFSRCNSVRVDSGCWMLYERPNYQGHQYFLRRGEYPDYQQWMGFSDSIRSCCLIPQHSGTYRMRIYEKDDFRGQMSEITDDCLSLQDRFHFSEIHSLNVMEGCWVLYEMPSYRGRQYLLRPGEYRRYLDWGAANAKVGSFRRVMDFY
Protein: DUF38 domain-containing protein (G5EDX9)
Organism: Caenorhabditis elegans
Interaction partners:
- Skp1-related protein
Sequence:
MTSQRAEIGETTDKQNSMKLSKTSSPTLFDLPLNIMKKIVKKLHPYDWISVRNSNGNLRSFIDTLKLDLDIDIFIEGHRYTIVLNGKSFRYRYRFVPYDEISNARNEPFHPVVADDERRTIYNKGLQFALRKLFNVMKLPKAQIEKFSLDFDSIGGYEDYVHNERLRSSLRTIDMEFGDAHCFRAKSVSLSGFKKPRAALILSSFDAGTLVKFEIMRCIFNDIRPLTCLEQFKNAKQLRTDLNICSVFGFTVSDLLGFSSIEFTSPEVSPNDLKELVNSSTKLETCVVSKQLDDSESIAEEMLQEFDPTFAGKTGTINYKANGFEYVIEVTEERVKIEKKLG
Protein: Exported protein family 4 (Q8IIY2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNFFHVIILDVGIVICLYLIIYKNSDIKWKKHINCCKYHFYFFSSKRCLLQHMVEEPFEKKDKSGVLLKDKNTEEGRKKERQKPMCIKSINKKKKKNNNNNNNNVLKNLNNEEINKQRNMTNERIRNKNKNDKGVENISSNTQMEEKNIICKDINSNVILNQNEINDDQMVQKIKENFVKDLMKNENKEIFKQIETINSVGTMAKIKNSLYSIIFKGSNFWKGLGIYLGTLSGAVLGQLILAGILQFGTFSVMNFSIYFSAVPSFIAFSSFVGIILLSIIIVICLLVWLWPSRGKLMGKDKTENKSDT
Protein: Acidic amino acid decarboxylase GADL1 (Aspartate 1-decarboxylase) (ADC) (HuADC) (EC 4.1.1.11) (Cysteine sulfinic acid decarboxylase) (CSADC) (HuCSADC) (EC 4.1.1.29) (Glutamate decarboxylase-like protein 1) (Q6ZQY3)
Organism: Homo sapiens (Human)
Function: May catalyze the decarboxylation of L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. Does not exhibit any decarboxylation activity toward glutamate.
Interaction partners:
- Cysteine dioxygenase type 1
- 4-aminobutyrate aminotransferase, mitochondrial
- 2-aminoethanethiol dioxygenase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- Alpha-aminoadipic semialdehyde dehydrogenase
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase family 3 member B1
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Aldehyde dehydrogenase family 3 member B2
Sequence:
MSSDSDRQCPVDGDIDQQEMIPSKKNAVLVDGVVLNGPTTDAKAGEKFVEEACRLIMEEVVLKATDVNEKVCEWRPPEQLKQLLDLEMRDSGEPPHKLLELCRDVIHYSVKTNHPRFFNQLYAGLDYYSLVARFMTEALNPSVYTYEVSPVFLLVEEAVLKKMIEFIGWKEGDGIFNPGGSVSNMYAMNLARYKYCPDIKEKGLSGSPRLILFTSAECHYSMKKAASFLGIGTENVCFVETDGRGKMIPEELEKQVWQARKEGAAPFLVCATSGTTVLGAFDPLDEIADICERHSLWLHVDASWGGSALMSRKHRKLLHGIHRADSVAWNPHKMLMAGIQCCALLVKDKSDLLKKCYSAKASYLFQQDKFYDVSYDTGDKSIQCSRRPDAFKFWMTWKALGTLGLEERVNRALALSRYLVDEIKKREGFKLLMEPEYANICFWYIPPSLREMEEGPEFWAKLNLVAPAIKERMMKKGSLMLGYQPHRGKVNFFRQVVISPQVSREDMDFLLDEIDLLGKDM
Protein: PDZ domain-containing protein GIPC2 (SemaF cytoplasmic domain-associated protein 2) (SEMCAP-2) (Q9Z2H7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Unconventional myosin-VI
Sequence:
MPLGLRGKKKAAKSKEAARLVEGERSSGSQGVPGPPAPARKLVFHAQLAHGSATGRVEDFSSISELYAKIAGVFEIAPSEILFCTLNTPKIDMGKLLGGQLGLEDFIFAHVKGTKKEVNVYKSEDSLGLTITDNGVGYAFIKRIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVAKKLKELKKEELFTLQLIEPKKAFEIGPRSKAGKTSTEKIGTSRGTLRLRSKGPATVEELPSEAKAKAIGKVDDLLELYMGIRDIDLATTMFEAGKDKSNPDEFAVALDETLGDFAFPDEFLFDVWGAISDMKQGR
Protein: Dual specificity protein phosphatase 19 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase TS-DSP1) (Low molecular weight dual specificity phosphatase 3) (LMW-DSP3) (Protein phosphatase SKRP1) (Stress-activated protein kinase pathway-regulating phosphatase 1) (SAPK pathway-regulating phosphatase 1) (Q8WTR2)
Organism: Homo sapiens (Human)
Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
- Mitogen-activated protein kinase kinase kinase 5
- Mitogen-activated protein kinase 9
- 5-aminolevulinate synthase, non-specific, mitochondrial
Sequence:
MYSLNQEIKAFSRNNLRKQCTRVTTLTGKKIIETWKDARIHVVEEVEPSSGGGCGYVQDLSSDLQVGVIKPWLLLGSQDAAHDLDTLKKNKVTHILNVAYGVENAFLSDFTYKSISILDLPETNILSYFPECFEFIEEAKRKDGVVLVHCNAGVSRAAAIVIGFLMNSEQTSFTSAFSLVKNARPSICPNSGFMEQLRTYQEGKESNKCDRIQENSS