wanglab/gogpt-training-data huggingface dataset:
Protein: Augmin-like complex subunit 3-like protein alpha (HAUS augmin-like complex subunit 3) (HAUS augmin-like complex, subunit 3) (Zgc:153228) (Q08CD9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
MLDGAQFIEALSRLGYPRASMLKCSEFDWLFDTAPDNLHLLRIVCNRLKRCNVLAPEELQAYKSLQESGKPILDEATLAELLKTCLPADGGFGSQSCSSLGGEGTVTIEELETELQALRKEKQLKQRRLNKLQMQAASWGANSSLSQMLLQEGDNKVKDANSALAAENAYTNSALDNLSKETTKLAGFFQSDLSNSLRSKDGASPSLGLQSGSPVLFSQCPLEPFLHQQEQFTKTLASYTQRQFFQGISDLMETSTFSRSQMTNLSCCSENGKEVDEELVELRKKEMAQLQWAFIVAQYQVVKEKAEENGDKTAKEWLIQRLNSSSEAVHYSPMSRLEPDLRSEITSVQFEIQSLLLDPVRSALRDCARLLNIPVVRGDLALQVARQNYLASRQTEVRDQLLHQKAFFELLRLAQDAELLRGKRVMGQINDIVERLEGATQDATQRENTLTQSHLTEDPFLGANANQQVISSKDTAFTRLLQMLELGKASTNREDPFQTYSKLETAASKLQEDLITVQEALDGARQEQAYTGARLERDRDALDQVAYSDIVQPLLRPQELTIVVDELEVKQKTLYMLLQEIVGDLKTKRGRLERSATLRRERELYVYFHLDPRLLNRAVRDIEAQAGVM
Protein: Berberine bridge enzyme-like 12 (AtBBE-like 12) (EC 1.1.1.-) (Q9SA89)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:O64743}.
Interaction partners:
Sequence:
MYLIFLLFFAASYSMSLSSADSVTIYEDFVQCFKNVTTISDIDLSDVVLPRTSISFTPTLRAYIRNARFNTSSMPKPSIIIVPRVDSHVQAAVICAKTLNLQLKIRSGGHDYDGLSYVSAVTFLVLDLSNFRNITVDLNDGGGSAWVQTGATLGELYYRIWEKSEVHAFPAGVCPTVGVGGHVSGGGYGHMIRKFGLTIDHVVDATIVDANGQIHDRKSMEEDLFWAIRGGGGGSFGVVLAFKVKLVTVPKTVTVFRVDKSVDENALDMVYKWQFVAPRTDPGLFMRVLLSSPTQNKTSTVNTKLRALYLGKADDVVLKMAEEFPELGLKKEDCKEMTWIQSLLWWMNHVDVDKVKPEILLEREPDSAKFLKRKSDYVEKEMTKPELNRLFQKLATLDRTGLVLNPYGGSLNVTAVNATAFPHRHKLYKIQHSVTWPDAGPEAERLYIGNLRTTYNIMTPFVSKNPRSSYLNYRDIDIGVNDHGADGYRKGEIYGRKYFGENFDRLVRVKTAVDPDNFFRNEQSIPTLPPNRR
Protein: TFIIS N-terminal domain-containing protein (Q8SUS7)
Organism: Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00649}.
Interaction partners:
- CHROMATIN STRUCTURE MODULATOR
- TRANSCRIPTION ELONGATION FACTOR SII
- RNA polymerase II subunit A C-terminal domain phosphatase
- FACT complex subunit POB3
- Chromatin elongation factor SPT5
- FACT complex subunit
- Transcription elongation factor SPT4
- DNA-directed RNA polymerase II subunit RPB1
- DNA-DIRECTED RNA POLYMERASE II THIRD CHAIN
- Tetratricopeptide repeat protein
Sequence:
MDRDSGQDFPEAQSGEFGDTGGRQKKAKAASRAERKGDLDPGTVLEISRSLKKRMQDILKKDNANNLEGRPATGKIENVEEISDILMSKALQESLLDEGILDEIKGWLEPLPDKSMPNIKIRKRLLDVLKTMKIHKEHLVTSGVGKIVYFYSINPKESKEVRASAKALVQKWTNEVFKPEGGD
Protein: Protein diaphanous (P48608)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for cytokinesis in both mitosis and meiosis. Has a role in actin cytoskeleton organization and is essential for many, if not all, actin-mediated events involving membrane invagination. May serve as a mediator between signaling molecules and actin organizers at specific phases of the cell cycle. Possible component of the contractile ring or may control its function.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7821209}. Cleavage furrow {ECO:0000269|PubMed:7821209}. Apical cell membrane {ECO:0000269|PubMed:23853710}. Note=Localizes to the site where the metaphase furrow is anticipated to form, to the growing tip of cellularization furrows, and to contractile rings (PubMed:7821209). Recruited to the apical cell membrane of epithelial cells in a Rho1 dependent manner, enhanced by phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) enrichment established by sktl/skittles and Pten (PubMed:23853710). {ECO:0000269|PubMed:23853710, ECO:0000269|PubMed:7821209}.
Interaction partners:
- Ras-like GTP-binding protein Rho1
- Profilin
- Cdc42 homolog
- Anillin
- Rho-associated protein kinase
- Pebble, isoform B
- Rho-related BTB domain containing, isoform B
- Cofilin/actin-depolymerizing factor homolog
- Cdc42-interacting protein 4, isoform B
- LD12055p
Sequence:
MSRHEKTKSTGGGLLDSLFGRPSKSKGGTISSGTLAHGGRPVSADNYVVPGVEDFEQYIQQLSVAELDAKFLEIIEDMNIPKDKREPLLAKSKEERQKMIMWHLKGKNSLERSANSRFEKPIDYVEYLQNGEHSTHKVYQCVESLRVALTSNPISWIKEFGVAGIGTIEKLLARSKNNASYEKIEFEAIRCLKAIMNNTWGLNVVLNPDQHSVVLLLAQSLDPRKPQTMCEALKLLASFCIVYERNGYEKVLRAITTIAATSFKASERFRPIVDALFASDQQDPKRDLACHSLIFINTLTNTPTDLNFRLHLRCEIMRMGLYDRLDEFTKIVEASNNENLQQHFKIFNEIREDDFEEFVQRFDNVTFNMDDATDCFDVLKNLVTDTTSEPYFLSILQHLLYIRDDFYFRPAYYQLIEECISQIVFHKGYCDPNFENRNFNIDTSLLLDDIVEKAKAKESKRSEEYEKKIEQLESAKQEAEAKAAHLEEKVKLMEANGVAAPSPNKLPKVNIPMPPPPPGGGGAPPPPPPPMPGRAGGGPPPPPPPPMPGRAGGPPPPPPPPGMGGPPPPPMPGMMRPGGGPPPPPMMMGPMVPVLPHGLKPKKKWDVKNPMKRANWKAIVPAKMSDKAFWVKCQEDKLAQDDFLAELAVKFSSKPVKKEQKDAVDKPTTLTKKNVDLRVLDSKTAQNLAIMLGGSLKHLSYEQIKICLLRCDTDILSSNILQQLIQYLPPPEHLKRLQEIKAKGEPLPPIEQFAATIGEIKRLSPRLHNLNFKLTYADMVQDIKPDIVAGTAACEEIRNSKKFSKILELILLLGNYMNSGSKNEAAFGFEISYLTKLSNTKDADNKQTLLHYLADLVEKKFPDALNFYDDLSHVNKASRVNMDAIQKAMRQMNSAVKNLETDLQNNKVPQCDDDKFSEVMGKFAEECRQQVDVLGKMQLQMEKLYKDLSEYYAFDPSKYTMEEFFADIKTFKDAFQAAHNDNVRVREELEKKRRLQEAREQSAREQQERQQRKKAVVDMDAPQTQEGVMDSLLEALQTGSAFGQRNRQARRQRPAGAERRAQLSRSRSRTRVTNGQLMTREMILNEVLGSA
Protein: Acyl-coenzyme A diphosphatase FITM2 (EC 3.6.1.-) (Fat storage-inducing transmembrane protein 2) (Fat-inducing protein 2) (P59266)
Organism: Mus musculus (Mouse)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates such as oleoyl-CoA/(9Z)-octadecenoyl-CoA and arachidonoyl-CoA/(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). Directly binds to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18160536, ECO:0000269|PubMed:22106267}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03230}.
Interaction partners:
- Seipin
Sequence:
MEHLERCAWFLRGTLVRATVRRHLPWALVAAMLAGSVVKELSPLPESYLSNKRNVLNVYFVKLAWAWTVCLLLPFIALTNYHLTGKTSLVLRRLSTLLVGTAIWYICTALFSNIEHYTGSCYQSPALEGIRQEHRSKQQCHREGGFWHGFDISGHSFLLTFCALMIVEEMAVLHEVKTDRGHHLHAAITTLVVALGFLTFIWVWMFLCTAVYFHDLTQKVFGTMFGLLGWYGTYGYWYLKSFSPGLPPQSCSLTLKRDTYKK
Protein: Solute carrier family 37 (glucose-6-phosphate transporter), member 4 (A0A1L1SV42)
Organism: Mus musculus (Mouse)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MAAQGYGYYRTVIFAAMFGGYSLYYFNRKTFSFVMPSLVDEIALDKDDLGVLLPAPLRCRAHHKQPVGSLRHQQVCERGSVRSDERPLALLLWAAP
Protein: Protein LIKE EARLY STARVATION, chloroplastic (Q5EAH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds preferentially to highly ordered alpha-glucans, such as starch and crystalline maltodextrins. Involved in the organization of the starch granule matrix, thus influencing starch turnover by modulating the accessibility of starch polymers to modifying and degrading enzymes involved in phosphorylation, hydrolyzes and synthesis, including starch synthases (SSI and SSIII), starch phosphorylases (PHS1), isoamylase, beta-amylase, glucan water dikinase (GWD) and phosphoglucan water dikinase (PWD).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:17631522, ECO:0000269|PubMed:27207856}. Note=Binds to starch granules in chloroplasts. {ECO:0000269|PubMed:17631522, ECO:0000269|PubMed:27207856}.
Interaction partners:
- Rhodanese-like domain-containing protein 7
- Ethylene-responsive transcription factor ERF008
- Arginine-specific demethylase JMJ22
Sequence:
MALRLGVSIGAALGSSHWDDGQRVRQRDFSASVNFTAPVTSRRSLRGSRTGVRILRVSNEGRESYLDMWKNAVDREKKEKAFEKIAENVVAVDGEKEKGGDLEKKSDEFQKILEVSVEERDRIQRMQVVDRAAAAISAARAILASNNSGDGKEGFPNEDNTVTSEVTETPKNAKLGMWSRTVYVPRSETSGTETPGPDFWSWTPPQGSEISSVDLQAVEKPAEFPTLPNPVLEKDKSADSLSIPYESMLSSERHSFTIPPFESLIEVRKEAETKPSSETLSTEHDLDLISSANAEEVARVLDSLDESSTHGVSEDGLKWWKQTGVEKRPDGVVCRWTMIRGVTADGVVEWQDKYWEASDDFGFKELGSEKSGRDATGNVWREFWRESMSQENGVVHMEKTADKWGKSGQGDEWQEKWWEHYDATGKSEKWAHKWCSIDRNTPLDAGHAHVWHERWGEKYDGQGGSTKYTDKWAERWVGDGWDKWGDKWDENFNPSAQGVKQGETWWEGKHGDRWNRSWGEGHNGSGWVHKYGKSSSGEHWDTHVPQETWYEKFPHFGFFHCFDNSVQLRAVKKPSDMS
Protein: Phosphatidylinositol transfer protein beta isoform (PI-TP-beta) (PtdIns transfer protein beta) (PtdInsTP beta) (P48739)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes. Also catalyzes the transfer of sphingomyelin (By similarity). Required for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum; phosphatidylinositol and phosphatidylcholine transfer activity is essential for this function.
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:P53811}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P53812}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53812}.
Interaction partners:
- Membrane-associated phosphatidylinositol transfer protein 3
Sequence:
MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHKIYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLGTLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKELANSPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTMEDIRRMEDETQKELETMRKRGSVRGTSAADV
Protein: Glutathione peroxidase 7 (GPx-7) (GSHPx-7) (EC 1.11.1.9) (CL683) (Q96SL4)
Organism: Homo sapiens (Human)
Function: It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Glutathione reductase, mitochondrial
- Peroxiredoxin-6
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Glutathione synthetase
- Polyunsaturated fatty acid 5-lipoxygenase
- Glutathione peroxidase 2
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Glutathione peroxidase 3
- Epididymal secretory glutathione peroxidase
- Phospholipid hydroperoxide glutathione peroxidase GPX4
Sequence:
MVAATVAAAWLLLWAAACAQQEQDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALVRKLILLKREDL
Protein: Vitronectin (VN) (S-protein) (Serum-spreading factor) (V75) [Cleaved into: Vitronectin V65 subunit; Vitronectin V10 subunit; Somatomedin-B] (P04004)
Organism: Homo sapiens (Human)
Function: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:2448300, ECO:0000269|PubMed:29567995}.; SUBCELLULAR LOCATION: Parasitophorous vacuole {ECO:0000269|PubMed:29567995}. Note=(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage (PubMed:29567995). Colocalizes with SERA5 at the schizont stage and with SERA5 P47 at the merozoite surface (PubMed:29567995). {ECO:0000269|PubMed:29567995}.
Interaction partners:
- Plasminogen activator inhibitor 1
- Integrin beta-3
- Urokinase plasminogen activator surface receptor
- Integrin alpha-V
- Integrin alpha-IIb
- Fibronectin
- Urokinase-type plasminogen activator
- Nidogen-1
- Plasminogen
- Integrin beta-5
Sequence:
MAPLRPLLILALLAWVALADQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTMPEDEYTVYDDGEEKNNATVHEQVGGPSLTSDLQAQSKGNPEQTPVLKPEEEAPAPEVGASKPEGIDSRPETLHPGRPQPPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDEKAVRPGYPKLIRDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISDGFDGIPDNVDAALALPAHSYSGRERVYFFKGKQYWEYQFQHQPSQEECEGSSLSAVFEHFAMMQRDSWEDIFELLFWGRTSAGTRQPQFISRDWHGVPGQVDAAMAGRIYISGMAPRPSLAKKQRFRHRNRKGYRSQRGHSRGRNQNSRRPSRATWLSLFSSEESNLGANNYDDYRMDWLVPATCEPIQSVFFFSGDKYYRVNLRTRRVDTVDPPYPRSIAQYWLGCPAPGHL
Protein: Aryl hydrocarbon receptor nuclear translocator 2 (ARNT protein 2) (zfARNT2) (Q9DG12)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that plays a role in the development of the hypothalamo-pituitary axis. Specifically recognizes the xenobiotic response element (XRE) (By similarity). Isoform 1 acts as a transcriptional activator. Isoform 3 acts as a transcriptional repressor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Neuronal PAS domain-containing protein 4A
- Aryl hydrocarbon receptor 1a.
- Single-minded homolog 1-A
- Aryl hydrocarbon receptor 2.
- SIM bHLH transcription factor 1b
- Aryl hydrocarbon receptor
- Aryl-hydrocarbon receptor repressor a.
- Cytochrome P450 1A
- Cytochrome P450 1A
- Aryl-hydrocarbon receptor repressor b.
Sequence:
MATPAAVNPSEMGTDLPGPVSMPGAVVGAGQVRMTGAMPGRGGKRRSAGMDFDDEDGEGPSKFSRYDDDQIPGDKERYARENHSEIERRRRNKMTQYITELSDMVPTCSALARKPDKLTILRMAVSHMKSMRGTGNTSTDGAYKPSFLTEQELKHLILEAADGFLFVVAAETGRVIYVSDSVTPVLNHPQSEWFGSTLFEQVHPDDVDKLREQLSTSENSMTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGSAPLDHISLNRLSSMRKRYRNGLGPSKEGEAQYSVVHCTGYIKAWPPAGMTIPDEDTEAGQTSKYCLVAIGRLQVTSSPVSMDMNGLSVPTEFLSRHNSDGIITFVDPRCINVIGYQPQDLLGKDILEFCHPEDQSHLRESFQQVVKLKGQVLSVMYRFRMKNREWMLIRTSSFTFQNPYSDEIEYIICTNTNVKQLQQQQQAELEVHQRDGLTAYDLSQVPVSGVSAGVHESGKTIDKTESLFSQERDPRFSDIYTGISTSEKKMMVPSSTSGGQQLYSQGSPFQPGHSGKSFSSSVIHVPGVNDIQSTAGSAGQNLSQISRQINTGQVSWSGNRPPFSGQQIPAQSNKAQSSPFGIGSSHSYQADPSSYSPLSSPATSSPSGNAYSNLANRNTAFDVSGESSQSGGQFQGRPSEVWSQWQSQHHSQQAGDPHPHTQASQTEVFQDMLPMPGDPTQGTTNYNIEDFADLGMFPPFSE
Protein: MICAL-like protein 2 (Junctional Rab13-binding protein) (Molecule interacting with CasL-like 2) (MICAL-L2) (Q8IY33)
Organism: Homo sapiens (Human)
Function: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q3TN34}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q3TN34}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q3TN34}. Recycling endosome {ECO:0000250|UniProtKB:Q3TN34}. Cell projection {ECO:0000250|UniProtKB:Q3TN34}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q3TN34}.
Interaction partners:
- Ras-related protein Rab-13
- Ras-related protein Rab-8A
- Alpha-actinin-4
- Ras-related protein Rab-8B
- Alpha-actinin-1
- Enhancer of filamentation 1
Sequence:
MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVALKVPDRLSILTYVSQYYNYFHGRSPIGGMAGVKRASEDSEEEPSGKKAPVQAAKLPSPAPARKPPLSPAQTNPVVQRRNEGAGGPPPKTDQALAGSLVSSTCGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGEPGTFVCTSHLPAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQASALPPAGRRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQDMSTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRALAEPRAGEAPRKVSGSFAGSVHITLTPVRPDRTPRPASPGPSLPARSPSPPRRRRLAVPASLDVCDNWLRPEPPGQEARVQSWKEEEKKPHLQGKPGRPLSPANVPALPGETVTSPVRLHPDYLSPEEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEGELRRLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKIWSPKSKSSPSQ
Protein: Protein RCR1 (Resistance to Congo red protein 1) (P38212)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates chitin deposition in the cell wall.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15590673}; Single-pass type I membrane protein {ECO:0000269|PubMed:15590673}.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
Sequence:
MGLISYENEAINEVKKADNHHVSKFVTSYYGPSSSSWQSGIWILFVLFVAAVILIILFTFVANRRRRRMGRAPIRGTAWLTPPSYRQSQQQYTGTVQQRTDDYVPEYTETANEHDLGYYDQRGEFHPNDKAAYVAPPPLVQECSSESVNSLERPPAAVVHQANSLDTDYGLTRPSNGRVPAVSDTVEQLERLPGGTTTQEINPPERAKVNARS
Protein: Putative Xaa-Pro aminopeptidase FRA1 (EC 3.4.11.9) (Fe repressor of activation 1) (Q07825)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the regulation of the iron regulon in responss to decreased mitochondrial iron-sulfur cluster synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- BolA-like protein 2
- Monothiol glutaredoxin-3
- Uncharacterized peptidase YFR006W
- Uncharacterized protein YJL132W
- Iron-regulated transcriptional activator AFT1
- Iron-regulated transcriptional activator AFT2
- Monothiol glutaredoxin-4
Sequence:
MTSKPSTSDGRAHSISHVPGTHMRGTSASHSPRPFRPCADCTCSPGLLSRQGRRASLFLRQLENSRRSSSMLLNELKGAGGGSSAGNGSVYSCDSLCAVNREVNTTDRLLKLRQEMKKHDLCCYIVPSCDEHQSEYVSLRDQRRAFISGFSGSAGVACITRDLLNFNDDHPDGKSILSTDGRYFNQARQELDYNWTLLRQNEDPITWQEWCVREALEMAKGLGNKEGMVLKIGIDPKLITFNDYVSFRKMIDTKYDAKGKVELVPVEENLVDSIWPDFETLPERPCNDLLLLKYEFHGEEFKDKKEKLLKKLNDKASSATTGRNTFIVVALDEICWLLNLRGSDIDYNPVFFSYVAINEDETILFTNNPFNDDISEYFKINGIEVRPYEQIWEHLTKITSQASSAEHEFLIPDSASWQMVRCLNTSTNANGAIAKKMTAQNFAIIHSPIDVLKSIKNDIEIKNAHKAQVKDAVCLVQYFAWLEQQLVGREALIDEYRAAEKLTEIRKTQRNFMGNSFETISSTGSNAAIIHYSPPVENSSMIDPTKIYLCDSGSQFLEGTTDITRTIHLTKPTKEEMDNYTLVLKGGLALERLIFPENTPGFNIDAIARQFLWSRGLDYKHGTGHGIGSFLNVHEGPMGVGFRPHLMNFPLRAGNIISNEPGYYKDGEYGIRIESDMLIKKATEKGNFLKFENMTVVPYCRKLINTKLLNEEEKTQINEYHARVWRTIVHFLQPQSISYKWLKRETSPL
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FTY9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome J complete sequence
- E3 ubiquitin ligase complex SCF subunit
- Histone H3-like centromeric protein CSE4
- Candida glabrata strain CBS138 chromosome I complete sequence
Sequence:
MFQRPLPTKSNRPCSVCSKRKVKCDRLVPCGHCRKRGTESECVQSAISANKGNHESEKGYLSGLLRFWQSYEYWIPNIGLFKSQKLKYENNEVLDYLNVEAQFWESSITETGSYKLLNYTIENLGTLYFGCIGDVTELYKILEQYWDIKEDQSSKLPFSDSDKCYSRALLWSIFTMGVYYCPKELLDGIISIDKVRDFTKKQTLTEEQIRCKIYEGFITTTIDSLYRCNFMAQPDIRFIQTYIILSTTLYSFQFPIQANMILTNAMYVTKLLSATVISASNSEDIIGSIANESLNRLWYRICACDYIQEGPNKSIDFNRELGSLLKHAAYLEDLPSTDVYKEEDNYEILFWKLLSLDRDIDQYLNNGLKPPPKTLDAVQREVDIYTQKVSNLEEDQKSINSKFEKFLGHFILYTVSWKIQKLQIIFYDNKVSLNKLIRITKNIIKLLVKNFEHGHDTFNKHPLVIYYLSRVATFTNFYHIFENSVEIHEIVLDINELIVNLPPIFGNHLENLKYIIFRFTLLRKEFGKTDVVDTGGEFQHPVFKVLQNDVATISKSNNKLNYLLKGLGSLIPGKSIGEGIYEEDEDSMLDPTILEIVSEFEEKYPIDRVID
Protein: Hexosyltransferase (EC 2.4.1.-) (Q584H9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
Sequence:
MSPLKMRPTQARRRPRTADIAVILLLVMSLLIICCNLHRIHEVSTFLDENQAGVSQPIDEGEYLMFVPSNVAAVWKAQRFLAVLGIPSVDNSERSRRRDLQRQTCWKYSGVATRSNNFSGSLLPLCLLAPHQSNSYLISHSLKEEAARTHDIITLPTNDVSPSTRKKIGENGNWGIEAEVAMSRKTYLWLRFALHMFPNVSYIVKGDDDIFIRVPKYLADLRVMPRHGLYMGRYNYYNRIWRRNQLTYVNGYCITLSRDTAQAIISYKPLERLVNMPFSMWDYFDFLDLGMFYEDVMVGMILREKVVYRNLISVEMGRCHFHNAGKFGVKKSVRNMSVVIHHIQEADYEMLMDYFPEGVIPPAPSKLMWLNSNWAAMQCEFRLGRKREILPSFPFWRKRA
Protein: Translocon EspA (B7UM94)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Interaction partners:
Sequence:
MDTSTTASVASANASTSTSMAYDLGSMSKDDVIDLFNKLGVFQAAILMFAYMYQAQSDLSIAKFADMNEASKESTTAQKMANLVDAKIADVQSSSDKNAKAQLPDEVISYINDPRNDITISGIDNINAQLGAGDLQTVKAAISAKANNLTTTVNNSQLEIQQMSNTLNLLTSARSDMQSLQYRTISGISLGK
Protein: Lysine-specific demethylase 7A (JmjC domain-containing histone demethylation protein 1D) (Lysine-specific demethylase 7) ([histone H3]-dimethyl-L-lysine9 demethylase 7A) (EC 1.14.11.65) (Q6ZMT4)
Organism: Homo sapiens (Human)
Function: Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9', 'Lys-27' and 'Lys-36' (H3K9me2, H3K27me2, H3K36me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate.
Subcellular location: Nucleus.
Interaction partners:
- Lysine-specific demethylase 6B
- Lysine-specific demethylase 3A demethylase 3A)
- Lysine-specific demethylase 4A demethylase 4A) demethylase 4A)
- F-box/LRR-repeat protein 19
- Lysine-specific demethylase 3B
- Histone H3.1
- Histone H3.2
- Lysine-specific demethylase 6A
Sequence:
MAGAAAAVAAGAAAGAAAAAVSVAAPGRASAPPPPPPVYCVCRQPYDVNRFMIECDICKDWFHGSCVGVEEHHAVDIDLYHCPNCAVLHGSSLMKKRRNWHRHDYTEIDDGSKPVQAGTRTFIKELRSRVFPSADEIIIKMHGSQLTQRYLEKHGFDVPIMVPKLDDLGLRLPSPTFSVMDVERYVGGDKVIDVIDVARQADSKMTLHNYVKYFMNPNRPKVLNVISLEFSDTKMSELVEVPDIAKKLSWVENYWPDDSVFPKPFVQKYCLMGVQDSYTDFHIDFGGTSVWYHVLWGEKIFYLIKPTDENLARYESWSSSVTQSEVFFGDKVDKCYKCVVKQGHTLFVPTGWIHAVLTSQDCMAFGGNFLHNLNIGMQLRCYEMEKRLKTPDLFKFPFFEAICWFVAKNLLETLKELREDGFQPQTYLVQGVKALHTALKLWMKKELVSEHAFEIPDNVRPGHLIKELSKVIRAIEEENGKPVKSQGIPIVCPVSRSSNEATSPYHSRRKMRKLRDHNVRTPSNLDILELHTREVLKRLEMCPWEEDILSSKLNGKFNKHLQPSSTVPEWRAKDNDLRLLLTNGRIIKDERQPFADQSLYTADSENEEDKRRTKKAKMKIEESSGVEGVEHEESQKPLNGFFTRVKSELRSRSSGYSDISESEDSGPECTALKSIFTTEESESSGDEKKQEITSNFKEESNVMRNFLQKSQKPSRSEIPIKRECPTSTSTEEEAIQGMLSMAGLHYSTCLQRQIQSTDCSGERNSLQDPSSCHGSNHEVRQLYRYDKPVECGYHVKTEDPDLRTSSWIKQFDTSRFHPQDLSRSQKCIRKEGSSEISQRVQSRNYVDSSGSSLQNGKYMQNSNLTSGACQISNGSLSPERPVGETSFSVPLHPTKRPASNPPPISNQATKGKRPKKGMATAKQRLGKILKLNRNGHARFFV
Protein: TIP41-like protein (Q8VXY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the regulation of the TOR signaling pathway. Indirectly activates the PP2A phosphatase via interaction with its suppressor TAP46. Could play a role in cytoskeleton functions.
Interaction partners:
- Aquaporin TIP4-1
- RGS1-HXK1-interacting protein 1
- Vacuolar fusion protein MON1 homolog
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
- PP2A regulatory subunit TAP46
- AT4g33380/F17M5_140
- AP-2 complex subunit mu
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- F-box/kelch-repeat protein At5g15710
- non-specific serine/threonine protein kinase
Sequence:
METVVDKDVLKSSGAELLPDGRRGLRIHDWEIETLRGTILTSLAVEEWEKKLKTSHLPEMVFGENALVLKHLGSNTKIHFNAFDALAGWKQEGLPPVEVPAAAQWKFRSKPSQQVILDYDYTFTTPYCGSEVVEKDKETVEAKANPKGEATLQWENCEDQIDLAALSLKEPILFYDEVVLYEDELADNGVSLLTVKVRVMPSSWFLLLRFWLRVDGVLMRLRETRMHYRFGEDEAPTVLRENCWREATFQSLSAKGYPVDLAVWSDPSSISQRLPVIKHTTQKLKIPSKV