wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine-rich repeat, isoform G (E1JGZ7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSTRSQLTKDLNESVKSILGRHTKILVKYMVKLETKGDKTENRVLVFTPVRVYLLSAKVPTKIECHFHYLDIVGVESKKSTHFSIVTNDRPYSFVTTGDAGNFSSNADVILTDLASAIKQIFPTVPLKYIIRKIDIQPPERETIFSEEFRPSDPRNVGPCGGFSAQYACMCDFHGVPYREEVAWDVDTIYLSHDTRVLNLRDFDHLEPKDLMAIVSALEYNTFFRGLKAAHMRLSHETLERILHVLKRSMWLEELHLEALGLRWDFLNKLSISVITNSNPAIRTIDLSHNIIEDKGAIHLAGPIAKVSKGLCKLALAHCGLTSKGVNQMSHSLTLNQSISNSLTYLDLSGNSLKDDITNLHNFLAQPNVLEHLDLASTDITLENLFGALLRGCATHLAHLNVSHNSFSTKKGKEIPPSFKQFFTSTFSLKHLNIAGCKLPMEALKNLLLGLACNESTAGLYLDLSSNTLGAQGAHVLESCIHGVRVLQSLDISDNNLDAELAPVLTAISKNPSIRTLHLTRSLTGMKPKHIPPVMDALVNLIQKDDFPLVELVLSENKLKHDLHDFINALGSNQSLQKLDISGNFMGDVGARLLAKALQINNRLRTIYMDKNGVTLQGYADIVYALEHNHSMRTIPFPVFDIAPHLKSHPDKTDAVMRKMQELLQRNCNGLKRATGQGFRLQHGFMLSSTHQLVDKLVAETQDTISLAKGGSESASAVQRLITDAENCKQLMPKLQEAVRNESHPIEMKMTRVASELSYTIKSYLEETMETMMRTGIEQCPKTLGNQIVVQDLRKALAERLVVPEEFLQICLLNNAGSEIMNKVGEIEQSLAAAISDRATDEVLEALTRYRRGMGIAESPSVLLDEPQTPDIVRSRSSHDADGLIIRPGGRGSILPKLGLESPTATPHLPTKRRSLAKKVRPQSVVENLSLGHFPDLLESPSSHRSNSQLSARAAAGAAALVGAANMTDSIAVDDGGVDECCDSITELPSASFQLQHLVKGRPKRAKTRAPTRPLVTTECAGGSREIGEGLEHFFRPGSVTPTTLTPLVSPTSEECSSLSFVDSPTMSRDGNGHMTSEETTPILEERRPIKLERQSPLLKSASWATRSRSTDNLEKYSPLVGRKSPLVKMRTEGGPGSGSATGAEETSMPSSNLLKATAREDKTRSPSSDSIKSHAAGEGSVIVKTGNGILRTPIVLQKPRPWSVVGSEPKAGGDLITGNGNADSSKTTPDKLEEDDVEIVTFGNTCSGSIVGITPGIALSTSGGGSIVGITPGGALEKKSVRELAAGLNRMGDIS
Protein: Transcobalamin II (Transcobalamin-2 precursor) (F2Z4S3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Similar to Transcobalamin-1
- Transcobalamin beta b
- Lysosomal cobalamin transport escort protein LMBD1
- Cubilin.
- Amnion-associated transmembrane protein.
- Eukaryotic peptide chain release factor GTP-binding subunit ERF3A
- G1 to S phase transition 1
- Apolipoprotein E receptor 2
- Si:dkey-258f14.3.
- Low density lipoprotein receptor-related protein 2a.
Sequence:
MITLLIVSALLALAAGKPCASDHETLLQSLNKQLLRSVDTQDNLPNPSVHIALRLSTQHNLDKENQYLNRLKKEFHEDIEKSLRNGELVVGRLALYILALRSSCHDLSLHLNHNEKNEFLLTHLKKEMEEEKQNIAFSHRPKTNYYQYSLGILALCVSGVRVSTHVSHKLIHAVEHGQIKHGESLCIDSHAMAGMALQCLKNEGISVKDEAELDKALATIKQKLVDSKRADGHMGNEFSTGLAVQALLAMGVEMEECGTAIEALRGDIRKGTYHNPMAASQVLPALYQQSYLHLKSKECRSEDDTLTADVESASEVLPSLGQVAVQVEVIKSNGEASVFPINVPKGSSLFEALNLLQDKQTGFTFKTEDSLWGAFLSVLNDEQARQTDRRYWHVSSDGTSLTQGIKDYKIDSAQRITIKNTGY
Protein: Zinc finger protein 703 (NocA-like zinc finger protein 1) (NocA-related zinc finger protein 1) (Q90ZE2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional corepressor which does not bind directly to DNA and may regulate transcription through recruitment of histone deacetylases to gene promoters. Required for segmental gene expression during hindbrain development. May regulate cell adhesion, migration and proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:14550789, ECO:0000269|PubMed:14709556}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Transducin-like enhancer protein 3-A
- DDB1- and CUL4-associated factor 7
Sequence:
MSELPPGFAVSPRNQQTFKSHYITNDSSPTCLGLQVDSIASLPYRDPARQEKRLPIRILKMLTAHTSHILHPEYLQPLSSAPVSIELDAKKSPLALLAQTCSQIGKPDPPPSSKLGSLSSSSHGDKDSRSSSSSLKSGEHQNLDDKSSFKPYSKTGSECRKEGAGINSSADKAGFRVPNGSSSSVTCTSLPPHAPSPRASSPQQTSGQSHTHRQSQSPLSQKTAHLQTTHMDSKAAGSDPGNDSSSSGSDRNGKKDSDHNKSSLDVVQIANSSHARASVNSSSASSSSSPQPDSKTDSQPPQPSLGTGHIAPVSPFKPGHSVFPLPSSTMGYHGSIVGAYTGYPSQFVPGLDPAKSSLGMGVPGKHPSSSPLTGASPPSFMQGLCRDPYCLTYPNAPHLGGSNCSSCVHDPSSALKSGFPLMYPTHHLHSLHPSSLSSSATSSLSHPLYTYGFMLPNETLPHACNWVSVGGPCDKRFATSEELLAHLRTHTALPGVDGKLLSGYPSSVSSAASCHLHLPPPSSPGALPSSLSLRGSPGLGLARYHPYGKAHLPGAPSLPMHSLPATAPYYSPYALYSQRLGSASALGYQ
Protein: Protein RIC-3 (Resistant to inhibitor of cholinesterase 3) (Q7Z5B4)
Organism: Homo sapiens (Human)
Function: Molecular chaperone which facilitates proper subunit assembly and surface trafficking of alpha-7 (CHRNA7) and alpha-8 (CHRNA8) nicotinic acetylcholine receptors. May also promote functional expression of homomeric serotoninergic 5-HT3 receptors, and of heteromeric acetylcholine receptors alpha-3/beta-2, alpha-3/beta-4, alpha-4/beta-2 and alpha-4/beta-4.
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane; Single-pass membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein.
Interaction partners:
- 5-hydroxytryptamine receptor 3A
- Sphingolipid delta
- Protein unc-50 homolog
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit beta-4
Sequence:
MAYSTVQRVALASGLVLALSLLLPKAFLSRGKRQEPPPTPEGKLGRFPPMMHHHQAPSDGQTPGARFQRSHLAEAFAKAKGSGGGAGGGGSGRGLMGQIIPIYGFGIFLYILYILFKLSKGKTTAEDGKCYTAMPGNTHRKITSFELAQLQEKLKETEAAMEKLINRVGPNGESRAQTVTSDQEKRLLHQLREITRVMKEGKFIDRFSPEKEAEEAPYMEDWEGYPEETYPIYDLSDCIKRRQETILVDYPDPKELSAEEIAERMGMIEEEESDHLGWESLPTDPRAQEDNSVTSCDPKPETCSCCFHEDEDPAVLAENAGFSADSYPEQEETTKEEWSQDFKDEGLGISTDKAYTGSMLRKRNPQGLE
Protein: Cysteine protease ATG4 (EC 3.4.22.-) (Autophagy-related protein 4) (P53867)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cysteine protease that plays a key role in cytoplasm to vacuole transport (Cvt) and autophagy by mediating both proteolytic activation and delipidation of ATG8. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. The protease activity is required for proteolytic activation of ATG8: cleaves the C-terminal amino acid of ATG8 to reveal a C-terminal glycine. ATG8 ubiquitin-like activity requires the exposure of the glycine at the C-terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. In addition to the protease activity, also catalyzes deconjugation of PE-conjugated forms of ATG8 during macroautophagy: ATG8 delipidation is required to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11149920}. Nucleus {ECO:0000269|PubMed:14562095}. Preautophagosomal structure {ECO:0000269|PubMed:25483965, ECO:0000269|PubMed:28330855, ECO:0000269|PubMed:28821724}. Mitochondrion {ECO:0000269|PubMed:30510114}. Note=Associates with mitochondria following nitrogen starvation in a respiratory carbon source. {ECO:0000269|PubMed:30510114}.
Interaction partners:
- Autophagy-related protein 3
- Serine/threonine-protein kinase ATG1
- Putative lipase ATG15
- Autophagy-related protein 8
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy protein 5
- Ubiquitin-like protein ATG12
- Autophagy protein 16
- Ubiquitin-like-conjugating enzyme ATG10
- Vacuolar protein sorting-associated protein 30
Sequence:
MQRWLQLWKMDLVQKVSHGVFEGSSEEPAALMNHDYIVLGEVYPERDEESGAEQCEQDCRYRGEAVSDGFLSSLFGREISSYTKEFLLDVQSRVNFTYRTRFVPIARAPDGPSPLSLNLLVRTNPISTIEDYIANPDCFNTDIGWGCMIRTGQSLLGNALQILHLGRDFRVNGNESLERESKFVNWFNDTPEAPFSLHNFVSAGTELSDKRPGEWFGPAATARSIQSLIYGFPECGIDDCIVSVSSGDIYENEVEKVFAENPNSRILFLLGVKLGINAVNESYRESICGILSSTQSVGIAGGRPSSSLYFFGYQGNEFLHFDPHIPQPAVEDSFVESCHTSKFGKLQLSEMDPSMLIGILIKGEKDWQQWKLEVAESAIINVLAKRMDDFDVSCSMDDVESVSSNSMKKDASNNENLGVLEGDYVDIGAIFPHTTNTEDVDEYDCFQDIHCKKQKIVVMGNTHTVNANLTDYEVEGVLVEKETVGIHSPIDEKC
Protein: Angiopoietin-related protein 6 (Angiopoietin-like protein 6) (Angiopoietin-related growth factor) (Q8R0Z6)
Organism: Mus musculus (Mouse)
Function: May play a role in the wound healing process. May promote epidermal proliferation, remodeling and regeneration. May promote the chemotactic activity of endothelial cells and induce neovascularization. May counteract high-fat diet-induced obesity and related insulin resistance through increased energy expenditure.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cadherin-1
Sequence:
MGTARLRKLQLLLLLGAWRALGGAARCRVTLVLSPQKATSAVCRSSEATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAALGLLAERALDAEAEARRTTARLQQLDAQLREHAQLMSQHSSLLGRLQRACAGPERGQQQVLPLPLAPLVPLSLVGSASNTSRRLDQTPEHQREQSLRQQGPPSSLLPTGHLAVPTRPVGPWRDCAEAHGAGHWQSGVYDLRLGRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLEPVHQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCALYHRGGWWYHACAHSNLNGVWYHGGHYRSRYQDGVYWAEFRGGAYSLKKAVMLTRLVRL
Protein: Calcium release-activated calcium channel protein 1 (Protein orai-1) (Transmembrane protein 142A) (Q96D31)
Organism: Homo sapiens (Human)
Function: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1. CRAC channels are the main pathway for Ca(2+) influx in T-cells and promote the immune response to pathogens by activating the transcription factor NFAT. Plays a prominent role in Ca(2+) influx at the basolateral membrane of mammary epithelial cells independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May mediate transepithelial transport of large quantities of Ca(2+) for milk secretion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16582901, ECO:0000269|PubMed:16645049, ECO:0000269|PubMed:16921383, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19706554, ECO:0000269|PubMed:20887894, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:26956484, ECO:0000269|PubMed:27185316, ECO:0000269|PubMed:28058752, ECO:0000269|PubMed:28219928}; Multi-pass membrane protein {ECO:0000269|PubMed:16582901, ECO:0000269|PubMed:16645049, ECO:0000269|PubMed:16921383, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:22641696, ECO:0000269|PubMed:24351972}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8BWG9}; Multi-pass membrane protein {ECO:0000269|PubMed:19249086}. Note=Upon store depletion, colocalizes with STIM1 in membrane punctae at ER-PM junctions (PubMed:19182790, PubMed:19249086, PubMed:26221052, PubMed:27185316). {ECO:0000269|PubMed:19182790, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:26221052, ECO:0000269|PubMed:27185316}.; SUBCELLULAR LOCATION: [Isoform alpha]: Cell membrane {ECO:0000269|PubMed:22641696}.; SUBCELLULAR LOCATION: [Isoform beta]: Cell membrane {ECO:0000269|PubMed:22641696}.
Interaction partners:
- Stromal interaction molecule 1
- Stromal interaction molecule 2
- Protein orai-3
- Short transient receptor potential channel 1
- Protein orai-2
- Calmodulin-1
- Calmodulin-1
- Short transient receptor potential channel 3
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MHPEPAPPPSRSSPELPPSGGSTTSGSRRSRRRSGDGEPPGAPPPPPSAVTYPDWIGQSYSEVMSLNEHSMQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLDADHDYPPGLLIAFSACTTVLVAVHLFALMISTCILPNIEAVSNVHNLNSVKESPHERMHRHIELAWAFSTVIGTLLFLAEVVLLCWVKFLPLKKQPGQPRPTSKPPASGAAANVSTSGITPGQAAAIASTTIMVPFGLIFIVFAVHFYRSLVSHKTDRQFQELNELAEFARLQDQLDHRGDHPLTPGSHYA
Protein: Liquid facets-Related, isoform D (Q8IN05)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Telo2 interacting protein 1
- Serine/threonine-protein kinase mTor
- RuvB-like helicase 2
- Transcription-associated protein 1
- Serine/threonine-protein kinase ATM
- RuvB-like helicase 1
- LD27967p
- AP-1 complex subunit gamma
- Cyclin-G-associated kinase
- DNA repair endonuclease XPF
Sequence:
MVDKFISMWKVRELADKVTNVVMNYTETEGKVREATNDDPWGPTGPLMQELAYSTFSYETFPEVMSMLWKRMLQDNKTNWRRTYKSLLLLNYLVRNGSERVVTSSREHIYDLRSLENYTFTDEGGKDQGINVRHKVRELIDFIQDDDRLREERKKAKKNKDKYIGMSSDAMGMRSGGYSGYSGGSGGGGGGSGGYNDGDYRSSRGDNWYSDKSADKDRYEDDDTHYDGEREGSDSDSPSPRRNYRYNDRASPAEVASEAKPSSLNMNIRSKTVSSPVSKQPTSTASAKPALSQKKIDLGAAANFGKPAPGGAAGIHSPTHRDTPTSVDLMGGASPSPSTSKANNNTQSNNNDLLDDLFKTCSPPPGQEKTLNSAAVIVDDDDDFNPRASDASQQEFGDFASAFGQPSAGSTISEPPSTGLVPAANDEFADFAAFQGSTTSTSALDGNLLKTATPANDSFDLFNSAPTSTAAATTATDLLAGLGDLSIHQSMPMAVEEQLASSNDSMSSASPQPPSEAMRLAFSKAQKQLRDLMQVQSASAVAQVAAILGELHNSNALPGFTTPEQLVGLDRQTCDWTCLAHGEYAALLNQLTELFSQDWPEPSQDVEVVNIFKLDHSFDYVSVAFESLQTRLDKFPSTISSLLENMVKDESLISIALLHISRQRASLMQRFARTIKVMPERKVEELDAQVKAFFQLLISLPAQVANRLGRRLPETFAPVSYQKLLLRQWLKSLHFVLQCDDNREYFDLEPYSWLLSQAINLIYDVSTLESLLRVLKDYAVAPRGRKVVHTILKELDPAACLKTAQSALSAGLNLYVLIGAATLETPHWKHCLLQKLPLQRTPVDNKQLITLASYLNAVAPAQLQVLLNQLLGIWSKRISLQKLGSQEHLAISKLLVLAAKCLCGNLVMDLNIQRQLHDGLSNHLQSPDALQRHVGMKTVELIFNFIALPDAKEDDRLRFEYDSFKDTFHWHIFEEFDELGQFESPSKTKLDEKPCEDQLKQLELHLSDFMSTTEQKEPHKPNIEIQANPAPENQNVNMQLDSDDDEPLDEDDDELKPYDMSNDTTTTIDQRPKFVIDLLHLLREKVENYQVFEGALGTAEQLIRGQLAKHDTQLALDLLQLFLVMEMQFYYEQFERTQFKCCVAICVAHPGPCAEYLCRQFHTDNSFYSASVRILILQVLAATAKELSGDENMQNEMEIVDVIPPAAKHPRKFEFQQEEESPAARLAAAQRIIRDRLRAKTKRYFSKPKAGDQMEKANPFHPVAGTFFFSLVRGQRTRQMLYVKYENISHDIDTQLLVNLLNTMSVLVMCSQNCPLLPAMTREIFDLCAFVRFNAEARVRAATLQLIGIALVTTPAHVLAQHFAESLNELQRWLNDFIRSPLVGGETSEECRELAQSILDTCYKLFDTAAMEQAA
Protein: Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Bile acid-CoA thioesterase) (Choloyl-CoA hydrolase) (EC 3.1.2.27) (Glycine N-choloyltransferase) (Kan-1) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2) (Q63276)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More efficient at taurine conjugation of cholyl CoA than glycine conjugation. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (By similarity). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption (By similarity). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (By similarity). In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:12951368}. Cytoplasm, cytosol {ECO:0000269|PubMed:12951368}.
Interaction partners:
- Long-chain fatty acid transport protein 5
- Acyl-coenzyme A thioesterase 8
- Cysteine sulfinic acid decarboxylase
- Glutamate decarboxylase 1
- Acyl-coenzyme A amino acid N-acyltransferase 2
- Acyl-coenzyme A amino acid N-acyltransferase 1
- Glutamate decarboxylase 2
- Glutathione hydrolase 5 proenzyme
- Glutathione hydrolase 7
- Glutathione hydrolase 6
Sequence:
MAKLTAVPLSALVDEPVHIRVTGLTPFQVVCLQASLKDDKGNLFNSQAFYRASEVGEVDLERDSSLGGDYMGVHPMGLFWSMKPEKLLTRLVKRDVMNRPHKVHIKLCHPYFPVEGKVISSSLDSLILERWYVAPGVTRIHVKEGRIRGALFLPPGEGPFPGVIDLFGGAGGLFEFRASLLASHGFATLALAYWGYDDLPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQITATVLINGPNFVSSNPHVYRGKVFQPTPCSEEFVTTNALGLVEFYRTFEETADKDSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHAKQAIAQLMKSGKKNWTLLSYPGAGHLIEPPYSPLCSASRMPFVIPSINWGGEVIPHAAAQEHSWKEIQKFLKQHLNPGFNSQL
Protein: Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)] (P04202)
Organism: Mus musculus (Mouse)
Function: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-1
- TGF-beta receptor type-2
- Decorin
- Latent-transforming growth factor beta-binding protein 1
- Endoglin
- Latent-transforming growth factor beta-binding protein 4
- Integrin alpha-V
- Transforming growth factor beta receptor type 3
- Latent-transforming growth factor beta-binding protein 3
- Transforming growth factor beta activator LRRC32
Sequence:
MPPSGLRLLPLLLPLPWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESADPEPEPEADYYAKEVTRVLMVDRNNAIYEKTKDISHSIYMFFNTSDIREAVPEPPLLSRAELRLQRLKSSVEQHVELYQKYSNNSWRYLGNRLLTPTDTPEWLSFDVTGVVRQWLNQGDGIQGFRFSAHCSCDSKDNKLHVEINGISPKRRGDLGTIHDMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASASPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
Protein: Protease Do-like 9 (EC 3.4.21.-) (Q9FL12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protease that degrades the two-component response regulator ARR4. Regulates ARR4 stability by targeting ARR4 in the nucleus for degradation. Acts upstream of ARR4 and regulates the activity of ARR4 in cytokinin and light-signaling pathways. ARR4 mediates the cross-talk between light and cytokinin signaling through modulation of the activity of phytochrome B.
Subcellular location: Nucleus {ECO:0000269|PubMed:27274065}.
Interaction partners:
- Protease Do-like 5, chloroplastic
- Protease Do-like 7
- Glyoxysomal processing protease, glyoxysomal
- Carboxypeptidase SOL1
- WAT1-related protein At3g28050
- Wall-associated receptor kinase-like 14
Sequence:
MKNSEKRGRKHKRQDASSAENAGGEVKEASANEASLPQSPEPVSASEANPSPSRRSRGRGKKRRLNNESEAGNQRTSSPERSRSRLHHSDTKNGDCSNGMIVSTTTESIPAAPSWETVVKVVPSMDAVVKVFCVHTEPNFSLPWQRKRQYSSGSSGFIIGGRRVLTNAHSVEHHTQVKLKKRGSDTKYLATVLAIGTECDIALLTVTDDEFWEGVSPVEFGDLPALQDAVTVVGYPIGGDTISVTSGVVSRMEILSYVHGSTELLGLQIDAAINSGNSGGPAFNDKGKCVGIAFQSLKHEDAENIGYVIPTPVIVHFIQDYEKHDKYTGFPVLGIEWQKMENPDLRKSMGMESHQKGVRIRRIEPTAPESQVLKPSDIILSFDGVNIANDGTVPFRHGERIGFSYLISQKYTGDSALVKVLRNKEILEFNIKLAIHKRLIPAHISGKPPSYFIVAGFVFTTVSVPYLRSEYGKEYEFDAPVKLLEKHLHAMAQSVDEQLVVVSQVLVSDINIGYEEIVNTQVVAFNGKPVKNLKGLAGMVENCEDEYMKFNLDYDQIVVLDTKTAKEATLDILTTHCIPSAMSDDLKTEERN
Protein: Lipase 6 (EC 3.1.1.3) (Q9P4E8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Secreted {ECO:0000269|PubMed:11131027}.
Interaction partners:
Sequence:
MRDLILFLSLLHTIFASLFSLKPPSQDDFYKAPAGFKAAKPGDILKTRKSPNKPSSLYAPVDVQNSWQLLVRSEDSFGNPNAFVTTIIQPKNADPSKVVSYQNWEDASNINCSPSYGSQLGAPLSTILTQLDMTFIVPPLKSGYYVVLPDYEGPKSTFGVGRQSGKATLDSIKAVLKTKDFSGINDDAKVVLWGYSGGSFASGWAAVLQPEYAPELKDNLIGAALGGFAANLTGIAESVDGEVFSGFIPLALNGIANEYPDFKKRLYEEVKPGAKADLQKGAENCLAASLISYPMYQYFTGPRRVFEKGWSLLEDKTIGKTLEDNLLIALSKEHMPQIPIFVYHGTIDKIIPIKDSIKIYKNWCDWGIGSFEFSEDKSNGHTTETVVGAPAALTWIDARFAGKPAVEGCSFTTRASNFLYPNISESAASYFKGIYQTILRSKLGSGVTSDDVSVNGLRSLYHT
Protein: InTestinal NeureXin-like (H1ZUX6)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MWQLLVPLAVLLTVSGQSTDEISHERIFLKYPSSFVNFTSDNWKLTETDNQLIIAVKFQASSHIGQIFSVRFINPDGSLKALLTAGIAAGILQINLYDDKNTKILNKPMENSPINVHEHSLAVGLNTTARNLWYKLGADNDLNCEINQAIDISNTEVTVTIGGGSQSMIGCVSIVAVSAGESSPVSQGTPIAYQDIDECPKADACTTKDCNTGRCIQLEVPTCDCYGTEMAGPNCRLPAPTIQLRNNDENEESSAYLRYKPWEMDSHFSRLSMDFRFSDSDAKEGILVYGETSQGKIFKIYVVGTKGKVMLDTTNVADFELREDHSIFHSIIVKIVDGIFNMLVDDNVHRRAFNESDALVFDTIQFGAPIPTDVSEVGVTACVKNVYVDHVDIIELAVLTNDSRTTASRVRSCNNEDLTEFQGPSLFSADPLAEILVEDPSDIKSEFGESVIGADMFPVPSNKKPKTQPLSSCEKANAYMCQNGAGCKKESETEFTCFCKEGYIGKFCQFTTIPRSCAEAYDFLKLPNGATWVDVDGNRKLDPSVTMCTDGQTEIPHDMKPGYVVRDTTYQNHSLFVLSYRDFNSWQLAKYIKNSGSCSQTVNYRCNKAPLRFKEGKTWFKSVSNATEKIKQIGMLPNSCPCLDRGCQSGEKCNCDSGAISEDIGELTGRYSGICEVVTLFDEADVRAEMTISELKCSGYENEKPIRFTERTELKISDWTGESIDLQFRTTETPASLVTVQGNYGEKIISVSLTDGHTVQISNFEALKIIESQTKLNDSNWHHVLIELADGEIRVTVDATHVLMTIGDNAVLEGSVVLGGEGDGLIGCVRNVLINDEPVNLQEIVKTSEKTGITETCDTRCTADFCQNGAKCYEDFVSGMPFCQCAFPDVHSGVNCEIDINTNSSVSFHGGYLKFDDVKNVLNAPIYFSFRTDRTHALLFFAHDQNNNFLQVHLSEEVNVTLTLNNLDIVSQCTVRAQPGTEYGDMRWIQVAITHDSKSSQLQVDDAACTIRTSRVLSEIPITRLLDVYNSELVGMPVGLAAPVKPNPYTFTFIGNVNTGEKTNDGSFILAPKYESPIPRFYGCIRGFQINREMIDMREKTEHLATSEMYEAYGPALVKVGCEVGCSSITCLNGGHCSVAWANTDPSAATTTCDCSRTSYTGASCSLDEGVHMERSGFIEFDISKEMARYVFIEQNSKIPQLLKFAFSSSPEIVLKDKSMLALVVFREKQKLEIEINPNRTINVAITYENGKSDVLNFVGDFLDGYRHFVVVQTNQASATAVMIDSLRQDFEYRGKDKNIDLFNAERIRIGGGPRDRYTETDGYLKAGYTGCISNFIVDYQRGSSLTYKPITYFANPTHHLSKLIMTNRIVLGGCAAFEVPNSLPVYQNRVKFPVWDTEFRRFVYFRDVEPLNDNNDTEWTDEDSGSLMWVVFIIFVLGVIFLIIFCIFMKCCREKIHARDDEYLHDEDIPLHMAPTILRHPQPSPPPIKKSAASNYKIPNPNIDFNKENTFDYDDEDEFAGIADDNVTDDVTVRNEVDDSDNETIRHIDDEVQDEDGMVIVSRPTQVSHLPQRVSSFRTGDPTAPKDSPLYSNIRPPTSPIHASVPVPPPRMSNNSPFA
Protein: ADAM metallopeptidase with thrombospondin type 1 motif, 16 (D3ZLL7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MEPRGCFALWVLLLAQLSEQQTPACALGAAAAATERLGDPHPPSSSGSDWLETSEYDLVSAYEVDHSGDYVSYDIMHHQRRRRRAVTQSKGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPAEENCFYQGSLRSQGNSSVALSTCQGLLGMIRTKDADYFLKPLPPQLTSKLNRSAQGGSPSHILYKRSTEHQAPRENEVLMITRKRDLARTHLHHDNFHLGLSRKQHFCGRRKKYMPQPPDDNLYILPDEYKPSSRPKRSLLKSHRNEELNVETLVVVDRKMLQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADRTLTSFCQWQSGLMGKDGARHDHAILLTGLDICSWKNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGEGNMCKKSEGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQPKPVKEYKYPEKLPGQLYDANTQCKWQFGEKAKLCMLDFRKDICKALWCHRIGRKCETKFMPAAEGTLCGQDMWCRGGQCVKYGDEGPKPTHGHWSDWSPWSPCSRTCGGGVSHRDRLCTNPRPSHGGKFCQGSARTLKLCNSQKCPLDSVGFRAAQCAEYNSKRFRGWLYKWTPYTQVEDQDLCKLYCIAEGFDFFFSLSNKVKDGTPCSEDSRNVCIDGMCEKVGCDNVLGSDATEDSCGVCQGNNSDCVMHRGLYSKNHPTNQYYHVVTIPSGARSIHIYETNISTSYISVRNSVKKYYLNGHWSVDWPGRYKFSGTTFNYRRSYKEPESLTSTGPTNETLIVELLFQGRNPGVAWEFSVPRSGSKRTPPPQPSYSWAILRSECSVSCGGGKMSSKAGCYRDLKVLVNASFCNPKTRPVPALVPCKVSACPPSWSVGNWSTCSRTCGGGTQSRPVHCTRRAHYREESISASLCPQPAPPLHQACNSQSCPPAWSTGPWAECSRTCGKGWRKRTVACKSTNPSARAQLLHDTACTSEPKPRTHQVCLLKRCHKHKKLQWLVSAWSPCSATCQRGTQHRVLRCAEKYVSGKYRELASKKCLHLPKPDLELERACGLIPCPKHPPYAASGPPRGSWFASPWSLCTASCGGGVQRRTVQCLLGGQPASDCFLHEKPETSTACNTHFCPIAEKRDTFCRDLFHWCYLVPQHGMCSHRFYSKQCCNTCSKSNL
Protein: Kinetochore protein Cenp-F/LEK1 Rb protein-binding domain-containing protein (Q8BVF5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
ELQRELRDMLQKTTQLSEDYNKEKNRLTEEVEVLREELQNTKAAHLKSVNQLEKELQRAQGKIKLMLKSCRQLEGEKEMLQKELSQLEAAQQQRAGSLVDSNVDEVMTENKELKETLEEKVKEADKYLDKYCSLLISHEELEKAKEILEIEVARLKSRQSRQDLQSSPLLNSSIPGPSPNTSVSEMKSASGQNKASGKRQRSSGIWEHGKRAAPSTAETFSKKSRKSDSKSTRPAEHEQETEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSHRFATQKLVGSSPSLGKEKVVESSKPTAGGSRSQKVKVVQESSADSHTAFQELPAKSLTASNIPGRNSTESPREGLRAKRAYPASSPAAGPDPTNNENCRVQ
Protein: SKP1-like protein 20 (AtSK20) (A8MQG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- At1g30860
- RING-box protein 1a
- RING-H2 finger protein ATL57
- F-box protein 7
- RING-box protein 1b
- Putative E3 ubiquitin-protein ligase XBAT34
- F-box/kelch-repeat protein At1g80440
Sequence:
MSEGDLAVMKPETMKSYIWLQTADGSIQQVEQEVAMFCPMICQEVIQKGVGSSKNHAISLPQRVNPAMFSLILDYCRFHQLPGRSNKERKTYDERFIRMDTKRLCELTSAADSLQLKPLVDLTSRALARIIEGKNPEEIREIFHLPDDLTEEEKLEPLKNSMDDPRIRLLNRLYAKKRKELKERERLKNVEVEEHVDERSVDDLLSFINGRDHKAVKMSKGKKKKKKKKDQKIVSSNNIHDKESHDLRSKQQCVEEIGSSMREVPNLLSAEDDISTPNAGSEDEDIDDEIDPAMRELLDREVEDFAQRLNSNWVRSLGKERRPVHFSINGNGTTRRHTGMVSIWRPCMFTLF
Protein: Tachykinin-related peptide 6 (TKRP-6) (P86593)
Organism: Pyrrhocoris apterus (Sap sucking bug) (Cimex apterus)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
APSSMGFMGMR