wanglab/gogpt-training-data huggingface dataset:
Protein: Melanocortin receptor 4 (MC4-R) (P70596)
Organism: Rattus norvegicus (Rat)
Function: Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P32245}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-opiomelanocortin
- Agouti-related protein
- Leptin
- Pro-neuropeptide Y
- Guanine nucleotide-binding protein G
- Neutrophil gelatinase-associated lipocalin
- Hypocretin neuropeptide precursor
- Alpha-ketoglutarate-dependent dioxygenase FTO-)-demethylase FTO)
- Appetite-regulating hormone
- Leptin receptor
Sequence:
MNSTHHHGMYTSLHLWNRSSHGLHGNASESLGKGHSDGGCYEQLFVSPEVFVTLGVISLLENILVIVAIAKNKNLHSPMYFFICSLAVADMLVSVSNGSETIVITLLNSTDTDAQSFTVNIDNVIDSVICSSLLASICSLLSIAVDRYFTIFYALQYHNIMTVRRVGIIISCIWAACTVSGVLFIIYSDSSAVIICLITMFFTMLVLMASLYVHMFLMARLHIKRIAVLPGTGTIRQGANMKGAITLTILIGVFVVCWAPFFLHLLFYISCPQNPYCVCFMSHFNLYLILIMCNAVIDPLIYALRSQELRKTFKEIICFYPLGGICELPGRY
Protein: Ras-related protein Rab-3A (EC 3.6.5.2) (P20336)
Organism: Homo sapiens (Human)
Function: Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (By similarity). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (By similarity). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (By similarity). Stimulates insulin secretion through interaction with RIMS2 or RPH3AL effectors in pancreatic beta cells (By similarity). Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9. Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1. Also plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (By similarity). Interacts with MADD (via uDENN domain); the GTP-bound form is preferred for interaction (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P63012}. Lysosome {ECO:0000269|PubMed:27325790}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P63012}. Cell projection, axon {ECO:0000250|UniProtKB:P63011}. Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Presynapse {ECO:0000250|UniProtKB:P63011}. Postsynapse {ECO:0000250|UniProtKB:P63011}. Note=Cycles between a vesicle-associated GTP-bound form and a cytosolic GDP-bound form. {ECO:0000250|UniProtKB:P63012}.
Interaction partners:
- Rabphilin-3A
- Regulating synaptic membrane exocytosis protein 1
- Regulating synaptic membrane exocytosis protein 2
- Synaptophysin
- Synaptotagmin-1
- Vesicle-associated membrane protein 2
- Synapsin-1
- Synaptotagmin-like protein 4
- Rab GDP dissociation inhibitor alpha
- Rab proteins geranylgeranyltransferase component A 1
Sequence:
MASATDSRYGQKESSDQNFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEKMSESLDTADPAVTGAKQGPQLSDQQVPPHQDCAC
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (F1NIM4)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MTAEEMKADGAPLEGTDITPKRDEGVLKVVKREGTGTESPMIGDKVTVHYTGWLLDGTKFDSSLDRRDKFSFDLGKGEVIKAWDIAVATMKVGEICQITCKPEYAYGLAGSPPKIPPNATLIFEIELFEFKGEDLTDDEDGGIIRRIRKKGEGYLKPNEGALVEIQFEGRYRDRAFDKRELRFEIGEGDNYDLPHGLEKAIQKMEKSEESIFYLKPNYGFGSTGKEKFQIPPDAELQYEVKLKSFEKAKESWEMNTEEKLEQSCMVKERGTQYFKEGKYKRAALQYKKIVLWLEHESGLSDEEDTKAKSLRLAAHLNLAMCHLKLKEYSQALENCNKALELDSSNEKGLFRRGEAHLAVNDFELARGDFQKVIQLYPSNKAAKVQLVTCQQKIREQHEKEKKMYANMFQRLADKELKPATTLQTSHTEDAEMKDEQNGVDDK
Protein: Dichlorochromopyrrolate synthase (EC 1.21.98.2) (Catalase) (EC 1.11.1.6) (Q8KHV6)
Organism: Lentzea aerocolonigenes (Lechevalieria aerocolonigenes) (Saccharothrix aerocolonigenes)
Function: Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the hydrogen peroxide-dependent dimerization of two L-tryptophan-derived molecules (imine form of indole 3-pyruvate (IPA)), to form dichlorochromopyrrolic acid (CPA), the precursor for the six-ring bisindolopyrrolocarbazole scaffold of the rebeccamycin. The hydrogen peroxide is provided together with iminoindolpropanoate by RebO. Due to the instability of indole 3-pyruvate (IPA), which is hydrolyzed in solution and exits in equilibrium with the predominant ketone form of IPA, the concerted functioning of the RebO/RebD system appears to prevent the buildup of significant amounts of IPA and its imine in solution, effectively shepherding the imine further down the biosynthetic chain.
Interaction partners:
Sequence:
MSVFDLPRLHFAGTATTRLPTGPRNGLVDLSTHSVVMDGERFPASRPAAEYHAYLDRVGGKGTAFAGNGYFAIDAGITAVERAAGEVDTGDLLVGRAVDVWGHYNEYLATTFNRARIFDVDPSSSWTSTVMIGQFGFGRLGRSHDVGYVFTGGVHGMQPPRWHEDGRVLHQFTVPAGEDMTWFGSAADSPAAARLRELVESGEADGLVVQLALSDAGPAPMPHAQQWRLRGTIAPWHAGEPRTCPAGRLLTPHNLTADLRGDHVSLNLISFRPPTGISGLELRTADTDRFIARVPADDPHGVVTVPAAEGGDEALCVVGTTAAGERIVVSREREVTVHVDDASVFLEHPRGPGDSDQDAEIAVRTYVRGEPAAATIHIGQYFNPRAFPLDEHATAASATPEDLDVVALCVDGTRWSRHCVISTDENGDGRFLLRGARPGATRLLLSAEGATPFDGLTAAAAYDNDDSLGLWSGLASVAVRVLPDHWWMDDIPRDKVTFDLLYREVFAFYELLYSFMGEEVFSLADRFRVETHPRLIWQMCDPRNRAKTYYMPPTRDLTGPQARLLLAYLRAQNSDVVVPVIEPSHTRSGTPISTRTDLVRALRHGVAIELAVMLQYLYAAFSIPTHGAGQELVSRGDWTPEQLRLMCGDGGETTDGGVRGSLLGVAREEMIHFLVVNNVLMAVGEPFHVPDLDFGTINDTLMVPLDFSLEALGLGSVQRFIQIEQPEGLTGAVRLGDLPVPVREAEDFHYASLSELYGDIREGLQRVPGLFLVERGRGGGEHHLFLRESVNAVHPDYQLEVDDLSSALFAIDFVTEQGEGHVLTDEDTGEESHYDTFVRVADLLMKERLTAADTRRAQWSPAYPVARNPTVHGGGQSKELVTSPVARELMVLFNKSYFMMLQLMVQHFGGSPDASLRRSKLMNAAIDVMTGVMRPLAELLVTVPSGRHGRTAGPSFELDEKPAFIPRADVARRAISLRFRHLAESARTCALVPDKVVRNLDFLADQFATEGPR
Protein: ZAP3, isoform E (M9NGY4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWGQWQTAAAVAPTAALPPQPSVPPPLPDAPPPPPPSDATAGAGASSGASAPIVTTAAAVTTAPGFNPYSSGQATGAGNPYQQYTAAQYAAMTPEQQYALQHHWQQWQTYQEEYAKWHAQYGEQYKREMAAAAATTTAVQGVPAPVVATPAAAPVPVVAPPGPQAYPVAHNYYQGVSASPAQSTTPVAVAGAPPLPGKIMAQPQMYNQPPPPPQKGGYNQHPNDIQSMWSGPPPMQQPPPNRYGGGQMNQMNYNIAGQDNQGFPNLQQPPPSLQRPTPQQQQPHLNHMDHGQWGNNQHGVGNNNRPTWDTSGPPPDNTGQPNRWNGPPPANDVNNRWNGTSFNNNTNDGNRRWDGTSNQAPSGGDQQLNRWMSEPPPSLPNPNQQYQNQNSWMSGPPPSISDPPQDHQQQNNSSQNARSSRWQGINSDIDTPPMRTNNKPNSIQNSRNSWGDGGGDGNQSKNPFIKNPQSDFGNYGNSYNSQDQGSAGGGNFGGFGDDSGGKQSQDSFAGRGGGPGNNINNNFSNNRRQNNRRDNNRNQGFSDERGGGDSGPGGYNPNRGNYNQRNSFNQSNAPYKQSQQNRNQQQPPDLDEASFDLLFDQWEQQFEEWKLANANHPDRDEYRRYEEEFEKQRRRIAERREQMRRRRQLQMGGSAGGSTTDIRKEAAAGASTTAEQKPNKDPFEGQGRFADQGDQDHGSGPNFGNGNRQSGNAGHFGKENRPFESAGVPAFRGNQGPPPGMHNQYQTAQEAIQQILDEQPDESNQEIPTKPAASNENSSDVKKAKTTASPVAPPIAPVVPPEVKAPAAPVVPDPTVVPPTQPPPVSTNYGKRRQRAAPSQIPAKQVKEEEPIFTISLDDDDDDDEEKEVVQDAPNTPMGSIFKKNDGIPGLDLVDDGSNKNNSSSVFNVVLKDSSEKKAADETEKQPGDVSADKKGDESLSNALKDPNFINNLSQAVANVQEREQRDRHEQRDDQESGTDGRPLSFAEWQRKKNSGNENKSQDAGDSVSTNNGEKPDNNGPPGGFGPGNGPGGGPGSGPGQNDGSRFDVFGPNQVSGNNFIDLDNNGPPGFGPPGRNFGPNGPGPRGNFGPNFGHNFGPRGPGGPFIRPNGPLPGPGPNFGPHFRPNGPNFGPNFGPNFGPRPGSRNFGPRGPDGPFGPGRDDFGGPPFGGPRPHMGPNGPGHNMRGFNGGPISDNPFRRQGGPPGPGFGNDDLGAGPPRGPRNFGNRFGNPGGGGGGGGGGGNNNRKNWNDGPEQQQFHDRLNHNDAIYRPLKVFDYSNNPTAAKVIDYGHKSGDGNPIDGPSGSNPDDRIPEFKAMKTFEYGHSSYMGSNRLGMPGGMGGGGDHNQAMTGGRGMAAGPGRFGGPGGAGNKRKNKKKNKQQKNGELMTFNQNQQMQSNTVEERSITNPEQDEEQRAHNELRNQNQADEFQKNEERNDLEDISEGEDNLQSIVFDDDNEELPPPPSMKIWNQGNAQEQYNPFPVNPLRRQLGDYSDKLEAPSPAMSLFPSAANANDRTSDPMKASNLEMCVATSENRNTFSLDEVLLYPGRLNRPKRICIILRGPPGCGKSHVARLIKEKELEMGGANPRILSIDDYFLIENDYDEKCPKTGKKIPKKEILYEYDDTMEETYMQYLIKSFKKTLSDNLYDFVIVDCNNNSLRTLNEFYCHAKDSNFVPYIVDLHCDLETCLGRNSHQRSVNDIRVVLDNWCQTPTHYIKLDVSSLLENVVEMEDVEDMATDDNACADVGATVGESAALEDAAVEETDDSNSADASNYCGFLKSKWERDTTEDNLARLDGTKRLMQNRRTTSMADYLQLEDWKPPTTSDNGKKRVRWADIEEKRSQKKMRAIGFVVGQTDWNRMMDPNAGSRALNKTKFIERIKRR
Protein: Zinc finger X-chromosomal protein (P17010)
Organism: Homo sapiens (Human)
Function: Probable transcriptional activator.
Subcellular location: Nucleus.
Interaction partners:
- Small ribosomal subunit protein eS4, X isoform
- N-myc proto-oncogene protein
- Sex-determining region Y protein
- Lysine-specific demethylase 6A
- Myc proto-oncogene protein
- Ubiquitin carboxyl-terminal hydrolase 9X
- Ubiquitin-like modifier-activating enzyme 1
- Nuclear receptor subfamily 1 group I member 2
- Lysine-specific demethylase 5D
- Zinc finger Y-chromosomal protein
Sequence:
MDEDGLELQQEPNSFFDATGADGTHMDGDQIVVEVQETVFVSDVVDSDITVHNFVPDDPDSVVIQDVIEDVVIEDVQCPDIMEEADVSETVIIPEQVLDSDVTEEVSLAHCTVPDDVLASDITSASMSMPEHVLTGDSIHVSDVGHVGHVGHVEHVVHDSVVEAEIVTDPLTTDVVSEEVLVADCASEAVIDANGIPVDQQDDDKGNCEDYLMISLDDAGKIEHDGSSGMTMDTESEIDPCKVDGTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQPEDEDLNVAEIADEVYMEVIVGEEDAAAAAAAAAVHEQQMDDNEIKTFMPIAWAAAYGNNSDGIENRNGTASALLHIDESAGLGRLAKQKPKKRRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLAKKKYRCTDCDYTTNKKISLHNHLESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELKKHMRIHTGEKPYQCQYCEYRSADSSNLKTHVKTKHSKEMPFKCDICLLTFSDTKEVQQHALIHQESKTHQCLHCDHKSSNSSDLKRHIISVHTKDYPHKCDMCDKGFHRPSELKKHVAAHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCRKGFRQQSELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHIMRHHKEVGLP
Protein: E3 ubiquitin-protein ligase RHF2A (EC 2.3.2.27) (RING-H2 finger F2a) (RING-H2 zinc finger protein RHF2a) (RING-type E3 ubiquitin transferase RHF2A) (Q9ZT42)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase involved in the positive regulation of the gametogenesis progression. Required for the degradation of KRP6, a cyclin-dependent kinase inhibitor which accumulates during meiosis and blocks the progression of subsequent mitoses during gametophytes development. Functions in association with RHF1A.
Interaction partners:
- Cyclin-dependent kinase inhibitor 6
- F-box/LRR-repeat protein 17
- Cyclin family protein
- Homeodomain-like superfamily protein
- Ubiquitin-activating enzyme E1 1
- Cyclin-dependent kinase inhibitor 7
- Homeobox protein LUMINIDEPENDENS
Sequence:
MEGAGETTTSEGHLTSAAAFVEGGIQDACDDACSICLESFCESDPSTLTSCKHEYHLQCILEWCQRSSQCPMCWQSISLKDPTSQELLEAVEQERNFRFNPTRNATIFRHPTLGDFELQHLPVGVDNAEIEERIIQHLAAAAAMGRARHGVRREGHRSRSSSQGHQQFMVFSSQPNASSPPPHPPMPSSPSQRDESDTVSNLPHNALGEGSHQSNTQPPTSSHPRQVSPSASDSNSRPLNQSSPSEQDRAGPSELQSFSESLKSRLNAVSTRYKESISKNTRNWKDRLFSRNTSMADLGSEVKREVSAGIATVSRMMERLETRENSRPSTASVSDVSENHTPETNNEHNRAAAGDEHSVNERGVKETCATGSGSS
Protein: Transcription factor zip-4 (H2L0N3)
Organism: Caenorhabditis elegans
Function: Transcription factor that binds to the promoter and the enhancer regions of target genes (By similarity). Involved in responding to mitochondrial damage. Has a protective role in response to infection by the Gram-negative bacterium P.aeruginosa.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- CCAAT/enhancer-binding protein homolog 2
- Cytochrome c oxidase subunit 5A, mitochondrial
- COX5B-domain-containing protein
Sequence:
MYNYNYSRGNKSMGNPPRFHELTDMPDNGASTSAAAGMFTRQDSLALAASLQQRDRERNPVDFMETQLDLDNYLQCFTDLDVPADNVDLNDAELQKANILYDDDSYEQPQLNPYERHVAYGPGFRNPGEYEEQDGYKMNFEVKTEEEKKPETMKTSKTMTTRRAIKRPSCYDDYQEEGETSLSDNDESVDDSYYKPKSSKKTAAAVPNFVPKTKARKYNLKPDKEKVEPIYKLKRARNNDAVRKSRNKAKELQLQKDEEYDEMKKRITQLEAELQSEREGRERDQQLIKQLIREKESTSKGPRKSSRNALESFNKSNY
Protein: Peroxiredoxin (EC 1.11.1.24) (Thioredoxin peroxidase) (ApTPx) (Thioredoxin-dependent peroxiredoxin) (Q9Y9L0)
Organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12707274}.
Interaction partners:
- Thioredoxin
- Thioredoxin reductase
- Thioredoxin
- Thioredoxin
- Thioredoxin
- Thioredoxin
- Transcriptional regulator, Fur family
- Superoxide dismutase [Mn/Fe]
- DNA protection during starvation protein
- Protein-disulfide oxidoreductase
Sequence:
MPGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFSHPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYEEARTHLH
Protein: Signal transducer and activator of transcription (B9UYM8)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
- Tyrosine-protein kinase
- Tyrosine-protein kinase
- Tyrosine-protein kinase
- Tyrosine-protein kinase
- Signal transducer and activator of transcription 1
- Signal transducer and activator of transcription
- Interferon regulatory factor
- Interferon regulatory factor 9
- Tyrosine-protein kinase
- Interferon regulatory factor 3
Sequence:
MAQWEKLRQLDSVYLTQVDELYDGDAFPMDVRHYLAHWIEGQDWDRAARDHDVAMVLFQVLLENLDIQHSRFVQGGESFLLQHNIRRFKHSFQRYQEEPYNLANIIQWFLEKEKEILQNAELAEQVQLLQVQQNPMETDSQRNMSADGRRRISQCMTHSECLRHKMKVLHYTDSYMRDHHKRETEQMSAAGSTQQTDRFRKSMLSGMSVLLTLRDLLCVLVRGELVQWQRRQQKACIGAPDSTCLDQLEKWFTTEAECLFQVRKFLKKLEELMGKVTYEHDPVKKQKPALQKRVDSLLTSLLKSAFVVETQPSMPQGKGPLVLRTNVQFSVKTRFLVKFPELNHAMKVNVSMDREAPLVKGYRRFNVLGTNSKALNMAESMSGGMVADFRHLTLKEQKSGGGGKGIHDLSLSVTEELHIINFNTEFLLHDMSVSLETSSLPVVIISNSSQQQSAWASILWFNMLCLEPKNLLFFANCPAATWPQLGEMLSWQFLSSTTRGLEANQLDMIAHKLFGKQQSYDACKISWTKFSKENVPNTNFTFCVWFDGILFMVKTHLENLWKDGSIMGFVSKGKEKTLLKKKRRGTFLLRFSESIRDGGITFSWVDYSPTGEPDVRSVQPFTKVDLCQIPFHEIIRNFQILEEENVPENPLLFLYPDTPKVEAFALTEKSGADSQFFKYIRTKFVFVSKGNTLEAKSLMYSDTVEGEGSGPMNPRYGLGGEAVEPSTFLPLPPSPDPMLPDAMVNPGEDLNPTFQEFLDDQSIYDCGLRILLCVTERHQLHPTPGWYGGTHFNALLRRAGED
Protein: Cysteine-rich secretory protein LCCL domain-containing 1 (CocoaCrisp) (Cysteine-rich secretory protein 10) (CRISP-10) (LCCL domain-containing cysteine-rich secretory protein 1) (Trypsin inhibitor Hl) (Q9H336)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MKCTAREWLRVTTVLFMARAIPAMVVPNATLLEKLLEKYMDEDGEWWIAKQRGKRAITDNDMQSILDLHNKLRSQVYPTASNMEYMTWDVELERSAESWAESCLWEHGPASLLPSIGQNLGAHWGRYRPPTFHVQSWYDEVKDFSYPYEHECNPYCPFRCSGPVCTHYTQVVWATSNRIGCAINLCHNMNIWGQIWPKAVYLVCNYSPKGNWWGHAPYKHGRPCSACPPSFGGGCRENLCYKEGSDRYYPPREEETNEIERQQSQVHDTHVRTRSDDSSRNEVISAQQMSQIVSCEVRLRDQCKGTTCNRYECPAGCLDSKAKVIGSVHYEMQSSICRAAIHYGIIDNDGGWVDITRQGRKHYFIKSNRNGIQTIGKYQSANSFTVSKVTVQAVTCETTVEQLCPFHKPASHCPRVYCPRNCMQANPHYARVIGTRVYSDLSSICRAAVHAGVVRNHGGYVDVMPVDKRKTYIASFQNGIFSESLQNPPGGKAFRVFAVV
Protein: Zinc finger protein 502 (Q8TBZ5)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MLNMQGAEERDIRRETCPGWVNKNKPALEQDVCKIDSSGIVVKRFQEDEYQDSTFEEKYACEGMKENSPREIAESCLFQEGGFGRITFIHKEAPPEIISQGYNFEKSLLLTSSLVTRLRVSTEESLHQWETSNIQTNDISDQSKCPTLCTQKKSWKCNECGKTFTQSSSLTQHQRTHTGERPYTCEECGKAFSRSSFLVQHQRIHTGVKPYGCEQCGKTFRCRSFLTQHQRIHTGEKPYKCNECGNSFRNHSHLTEHQRIHTGEKPYKCNRCGKAFNQNTHLIHHQRIHTGEKPYICSECGSSFRKHSNLTQHQRIHTGEKPHKCDECGKTFQTKANLSQHQRIHSGEKPYKCKECGKAFCQSPSLIKHQRIHTGEKPYKCKECGKAFTQSTPLTKHQRIHTGERPYKCSECGKAFIQSICLIRHQRSHTGEKPYKCNECGKGFNQNTCLTQHMRIHTGEKPYKCKECGKAFAHSSSLTEHHRTHTGEKLYKCSECEKTFRKYAHLSEHYRIHTGEKPYECIECGKFFRHSSVLFRHQKLHSGD
Protein: Ras-related protein Rab (A0A0B4LEY0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU367128}; Lipid-anchor {ECO:0000256|RuleBase:RU367128}.
Interaction partners:
Sequence:
MTSTSDKREHLYKILVIGELGTGKTSFIKRYVHQFFSQNYRATIGVDFALKVLQWDANTIVRLQLWDIAGQERFGNMTRVYYKEAVGAFIVFDVTRSGTFDCVSKWKEDLDSKVQLPDGSPIPCILLANKCDQEKQGIITQPEKMDEYVRENGFAGWFETSAKENINIDEAARALVNKILINDKLISADLADGDKFNLSAADATGSDAKNKCSC
Protein: Uncharacterized GST-like protein YibF (P0ACA1)
Organism: Escherichia coli (strain K12)
Function: Glutathione (GSH) transferase homolog, that might be involved in selenium metabolism.
Interaction partners:
- L-seryl-tRNA
Sequence:
MKLVGSYTSPFVRKLSILLLEKGITFEFINELPYNADNGVAQFNPLGKVPVLVTEEGECWFDSPIIAEYIELMNVAPAMLPRDPLESLRVRKIEALADGIMDAGLVSVREQARPAAQQSEDELLRQREKINRSLDVLEGYLVDGTLKTDTVNLATIAIACAVGYLNFRRVAPGWCVDRPHLVKLVENLFSRESFARTEPPKA
Protein: Torsin-1A-interacting protein 2 (Q8BYU6)
Organism: Mus musculus (Mouse)
Function: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}.
Interaction partners:
- Torsin-1A
- Torsin-1B
- Torsin-3A
- Torsin-2A
Sequence:
MSQSLKSQNTNMSDSGCRDPVGDSQNVLENDPSINSQTQDTRVTPNNTAEAQPLQPTSDLKEDHHEIGARAQEHTDTGDRSESPEEPALEKPPLDKAELESSPSSQDTELGHHPHSEHGGGDALDLDPNCSQSDLGGRADAHLESSSVASPEGAGDRGEADEHLESSSAAPTEGAGDRGEAGQELLAEDSTDGQSLGHSNTGPGNQDSLRRRLPVPEAGSHEEETELVKEKQEVAQDTLRKTDKKSLWTYGSVFLGCLIVAVVLSSVNSYYSSPAQQVPQNPALEAFLAQFGQLKEKFPGQSSFLWQRGRKFLQKHLNASNPSEPATIIFTAAREGKETLKCLSYHVANAYTSSQKVTAVSIDGAERALQDSDTVKLLVDLELSDGFENGHKAAVVHHFESLPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVSPREIEEKVRDLLWAKFTNSESPTSYSHMDSDKLSGLWSRISHLVLPVQPVRNIEERGCLL
Protein: Facilitated trehalose transporter Tret1 (PvTret1) (A5LGM7)
Organism: Polypedilum vanderplanki (Sleeping chironomid midge)
Function: High-capacity facilitative transporter for trehalose, required to induce anhydrobiosis. Anhydrobiotic larvae can survive almost complete dehydration. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17606922, ECO:0000269|PubMed:20035867}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:17606922, ECO:0000269|PubMed:20035867}.
Interaction partners:
Sequence:
MELNNKEDSPRHTVPFVRQITEDGKAKLEIYRPTTNPIYIYTQILAAIAVSMGSMVVGFASAYTSPALVSMQNTTITSFKVTEQEASWVGGIMPLAGLAGGIAGGPFIEYLGRKNTILATAVPFIVAWLLIAFANSIWMVLAGRALSGFCVGIASLSLPVYLGETVQPEVRGTLGLLPTAFGNIGILICFVAGKYVNWSGLAFIGSILPIPFMVLTLLIPETPRWFVTRGREERARKALQWLRGKKADVEPELKGIVKSHCEAERHASQNAIFDLMKRSNLKPLLIALGLMFFQQLSGINAVIFYTVSIFKDAGSTIDENLCTIIVGVVNFGATFFATVLIDRLGRKILLYISEVAMVITLLTLGTFFYYKNSGNDVSNIGWLPLASFVIYVIGFSSGVGPIPWLMLGEILPGKIRGSAASVATGFNWTCTFIVTKTFADIVAAIGNHGAFWFFGVICLIGLFFVIFFVPETQGKSLEEIERKMMGRVRRMSSVANMKPLSFNM
Protein: Integrin subunit alpha 2b (A0A3B3IU79)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
XAGWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVGFFKRNRPPLEEDDEEGE
Protein: Homeobox protein OTX2 (zOTX2) (Orthodenticle homolog 2) (Q91981)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May play a role in very early embryogenesis, gastrulation, and the development and subdivision of the diencephalon and the midbrain.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Six3
- Sine oculis homeobox homolog 3a.
- Paired box protein Pax-2a
- Transcription factor Sox-2
- Fibroblast growth factor 8
- Sonic hedgehog protein
- Nuclear receptor subfamily 2, group E, member 3.
- Early growth response protein 2b
- E3 SUMO-protein ligase EGR2a isoform 1
- Chordin
Sequence:
MMSYLKQPPYTVNGLSLTTSGMDLLHPSVGYPATPRKQRRERTTFTRAQLDVLEALFAKTRYPDIFMREEVALKINLPESRVQVWFKNRRAKCRQQQQQQQNGGQNKVRPAKKKSSPAREASSESGASGQFTPPSSTSVPAISTTTAPVSIWSPASISPLSDPLSTSSSCMQRSYPMTYTQASGYSQGYAGSTSYFGGMDCGSYLTPMHHQLTGPGSTLSPMSSNAVTSHLNQSPASLPTQGYGASGLGFNSTADCLDYKDQASSWKLNFNADCLDYKDQTSSWKFQVL
Protein: Large ribosomal subunit protein eL30B (60S ribosomal protein L30-2) (Q9UTP0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL32A
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL22
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL2B
Sequence:
MSAAPTTAPVAAVSKKGKKSGDTINSKLALTMKSGKYVLGYKSTLKTLRSGKAKLILIAANAPPLRKSELEYYAMLSRCSVHHYSGNNIDLGTACGKLFRVGVLAVIDAGDSDILAA
Protein: Cell division protein FtsZ (P72079)
Organism: Neisseria gonorrhoeae
Function: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
Interaction partners:
Sequence:
MEFVYDVAESAVSPAVIKVIGLGGGGCNAINNMVANNVRSVEFISANTDAQSLAKNHAAKRIQLGTNLTRGLGAGANPDIGRAAAQEDREAIEEAIRGANMLFITTGMGGGTGTGSAPVVAEIAKSLGILTVAVVTRPFSYEGKRVHVAQAGLEQLKEHVDSLIIIPNDKLMTALGEDVTMREAFRAADNVLRDAVAGISEVVTCPSEIINLDFADVKTVMSNRGIAMMGSGYAQGIDRARMATDQAISSPLLDDVTLDGARGVLVNITTAPGCLKMSELSEVMKIVNQSAHPDLECKFGAAEDETMSEDAIRITIIATGLKEKGAVDPTPEREVEAVAPSKQEQSHIVEGMIRTNRGIRTMNLTAADFDNQSVLDDFEIPAILRRQHNSDK
Protein: Protein preli-like (Q9V579)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in maintaining the structural and functional integrity of mitochondria. Activity is required for maintaining the subcellular distribution, shape and activity of mitochondria in neurons and as a consequence has an important role in the development and maintenance of dendritic arbors. Function may be particularly important in class IV dendritic arborization (da) neurons.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15700158, ECO:0000269|PubMed:19855018}. Note=Detected at the mitochondria cristae. {ECO:0000269|PubMed:19855018}.
Interaction partners:
- AT19138p
- TP53-regulated inhibitor of apoptosis 1
- Protein real-time
- Protein slowmo
- Mitochondrial import inner membrane translocase subunit TIM50-C
- GH11727p
Sequence:
MVVAASTCRTETVFDYSWMNVVVAYWNRYPNPSSTHVLTEDTIQREVRDGKLFSRRLLSKTNPVPKWGARFYNNVPVKIVEDSVLDPVKKTFTTFTRNLGMTKIMKVDEIVVYSEQKDGSTLAVRRAYISSQVFGFSRAIRAFGIERFKANGNKASNGFNYVLRRMFPDSLVGGGHHQHAVTTTSPAGELPATTITVSTTNGSLNNQGALKSAAKVGYEFFKSHASKIAQLFSVKN
Protein: Uncharacterized protein (C6KSL9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MTDHLLDFNMYGSQLHNLLHNAFSTCLEESERTCKRTYVVAILLAFLVLHALLYMKYKKNFKLSGLFKKSKKRTKMSKHYEDDDDDDDYQPPRHSSLPNERKTSSSSRQAARSHSSSSSVYASANAEN