wanglab/gogpt-training-data huggingface dataset:
Protein: Olfactory receptor 52B6 (Olfactory receptor OR11-47) (Q8NGF0)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MAQVRALHKIMALFSANSIGAMNNSDTRIAGCFLTGIPGLEQLHIWLSIPFCIMYITALEGNGILICVILSQAILHEPMYIFLSMLASADVLLSTTTMPKALANLWLGYSLISFDGCLTQMFFIHFLFIHSAVLLAMAFDRYVAICSPLRYVTILTSKVIGKIVTAALSHSFIIMFPSIFLLEHLHYCQINIIAHTFCEHMGIAHLSCSDISINVWYGLAAALLSTGLDIMLITVSYIHILQAVFRLLSQDARSKALSTCGSHICVILLFYVPALFSVFAYRFGGRSVPCYVHILLASLYVVIPPMLNPVIYGVRTKPILEGAKQMFSNLAKGSK
Protein: Kinesin-related protein 11 (Kinesin family member 11) (Kinesin-7) (Q6S001)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Kinesin-related protein 2
- Microtubule-associated protein RP/EB family member 1
- Kinesin-related protein 12
Sequence:
MNENISVSVRARPFNEKEVKDKEHCLWQFGNNNTITSLPPPITQPVSSLPPISTPIKSSSSSSTSTSAGSLKTPLKTPLKTPLKTPLKTNSTTTNTTVPASPAPTSSLTSKFVSNSYTYDHLFPPTCDNYEVYDTVARELVKSAMEGYNASIMAYGITSSGKTFTMTGSGKKNPGIIPLSIQDIFTYIQECKEREFLLRVSYLEIYNETVNDLLGVNQENFNLKIHEHPVTGVYVAGLKEEIVLSVEHVLSLISAGEAHRHVGSTSYNLQSSRSHTIFKMIIESKEVLPEGSGSGGLESPVRYSTLNLIDLAGSEKASESTISAIRNKEGSYINKSLLTLGTVISKLSEKDTGYIPYRDSKLTRVLQNSLSGNSRVAIICTITLASNNFEESHNTLKFASRAKKISNNAKVNEILDDKALLKQYRNEIAELKSKLSDALSTEKELQETLTEKEKMKITNQELLHKLVDAEKHRSLLESKINNLNKLILVSTSVNNSASKGGSGSGNGNGSRSTFVSPSQNSHHHHGDLGSITPNSFSNLLLQSPSQNNNNNSHISPLSQSTSSLTIGGGSGNGFESNELIQIQSKMAKLELELEEKNKKIDFLTSFNQDSALEKIKQLEGELVQRDMDLGLYQRESTRLQTLLSHKDEKISSLESKLRDILLKFKQIDSENTSLKSKIQEYEVMY
Protein: Translationally-controlled tumor protein (E9PJF7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGSVYPADDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFF
Protein: Uncharacterized protein (Q38DJ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKHMLPISNLNKGVYDQGSKDPYNMTETLWLEMEKYETRRGSGTTALSRTNTAFSPLPTKPIPLFVIHQWRNYVSFCRWTIAQRIDWREVFSYLCNPKTESTMETNALHNSGDEGMNEVLYSRDGLFSLRGDCSSRGSKSSFSGYLDPVNLSFEKLKHELVMDCTSRFGTLPICVHQQRLLRWTKMLIQCVVWRLRYAFNVVTEGKGGVAVSDAELQSYRVVLTRGREVFGAGPYLRELCKLLDAHGGTLTDSLDLPTINKSPRAPPVNDDPVLNMTLTMVFDQTTACPGVSTYFIPSLAARSLDALWVDKLHIPWDILDPKDMPEKVRTRLLGPMTTNETAYIDFCPVKNRVQGQLHSTTFHLMFDAEDVREGVSEGEDTCRPRIVMAISSQRVELHQLISVVRLLEAGGYVMLTKIRHSTHLECYRVLPFLGDYITLRNIVNNAIPCTLGSVAVGGPAAAGAFPHSSNVLKMADLLLFGLSNATRNLYEHSIVCCLQKYRKRATDGRMTICMQPLSPGAETGVVSTTVSKPCISVLETVVEPTLGTLQLMLSNGSLKSSGGEDFGHFVLDMLVTAVNSAIARVSRQIKSNSGTGGQLRSDHALLRRYINMHPASTQLQESNIS
Protein: Polyubiquitin [Cleaved into: Ubiquitin] (P0CG72)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Ubiquitin-activating enzyme E1 1
- Ubiquitin-conjugating enzyme E2 13
- Ubiquitin carboxyl-terminal hydrolase 6
- Ubiquitin-conjugating enzyme E2 4
- 26S proteasome regulatory subunit rpn10
- 26S proteasome regulatory subunit rpn11
- Probable proteasome subunit beta type-4
- Ubiquitin-conjugating enzyme E2 1
- Ubiquitin-ribosomal protein eL40A fusion protein
- Ubiquitin-ribosomal protein eL40B fusion protein
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGLF
Protein: Coiled-coil domain-containing protein 66 (Q6NS45)
Organism: Mus musculus (Mouse)
Function: Microtubule-binding protein required for ciliogenesis. May function in ciliogenesis by mediating the transport of proteins like BBS4 to the cilium, but also through the organization of the centriolar satellites (By similarity). Plays a role in retina morphogenesis and/or homeostasis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:A2RUB6}. Cell projection, cilium {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A2RUB6}. Photoreceptor inner segment {ECO:0000269|PubMed:19777273}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:19777273}. Note=Restricted to the centrosomes and the spindle microtubules during mitosis (By similarity). Enriched in the inner segment of the photoreceptor (PubMed:19777273). {ECO:0000250|UniProtKB:A2RUB6, ECO:0000269|PubMed:19777273}.
Interaction partners:
- Coiled-coil domain-containing protein 14
Sequence:
MNLGDGLKLETELLDGKTKLILSPYEHKSKVSVKMGNKFKIAKCPLRTKQTGHTLKSTQNTYIGNENLSQKKISTLDTSQAKPENSRLTFSPSTDKQYSEKDSVRVQKEISPTTSNIRKIINTTGTCPVAKQKPCKKNPTAETMNSGLVCLTQDQLRQILMLSVNQGNGSVCLTETGEEEASQDSLHLINIPSQPKDVNDTGFLQNTEAASPVTSEHEHVHRRAQEAFQQCEQKAATENEWKPADIFSTLGERERDKSLLEARRAQWKKELDEQVALKKKEKEASQKWHNPWKPSDIECEKSQVHDQSKEARLLESPCSAIKQEQQRKWIEELNKQVEDDQQRKAEERMIYSKGEEHDRWAVHFDSLKSHPGSQSRLSSQLTHQHLESLCVSPDTQELADVNGVFTPPPGVQAEPSEKEQRARPVLEMAVSHGPKTNFLRSMTALLDPAQIEERERRRQKQLEHQKAIMAQVEENRRKKRLEEEQRKKEEQELELRLAREREEMQRQYEEDILKQRQREEIMTLKTNELFHTMQRAQELAQRLKQEQRIRELAQKGHDTSRLIQNLGAQVDYKAFTTISSSHSDPEETADTSTASPKKDTGVQTDDVNLGIFNDALPPCGSVTEKGIRNISSPEISAEFSGQTDIRKENQELSMNKGTNLDKENSWHNGQCNQYRRTEKQTKLMKKCPKKPAWNINKPLKKYVPASAKYPAHLQKEKEEKKVQRQMELLHLVERNNPENLSQNRGISPLATSHRETESESRLHLIKKVEEPLKTPSVSKERFQTSPAVKNRTQQTQSNVLHLPLKNNDYEKETLTLGDGHTKLSDEMSEPSHFIPYVRTNEIYYLDPDAPLSRPSTQDNQYQKSHDCAREQELFDSDHIRDPLLNPKLVKNRDRQQAILKGLSELRQGLLQKQKELETNLIPLTANQEDNFSSSF
Protein: Zinc finger FYVE domain-containing protein (Q960V6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR037289}. Early endosome membrane {ECO:0000256|PIRNR:PIRNR037289}.
Interaction partners:
Sequence:
MDLVDIDQVLDNLELSIAADEQLSRNAAAAAAAGANPGRFLGDGASASISGVGAGAGVSGAAGVTPTPASGKSFVGVSQVFNSLDDYRENVKSLQVDAQLPSYDWQTEAEHEDDIHKFSEQASKNNGQTIVSSSESLTTSSCSTFSSGPSPVSNGSHSEELATPPEDEKTSEVQVEPKEQDQQPEQVKHEDQHQDQAVPPPTQSKQTVEELAVGLSSISITASGTESQSLLPEEVTASSVLGQVLEELSEESSPSREPETEMTNGIDVPLANLPASVAEVPVPKEMEQPVQTEEEDVELPQEQHPRRSQPLTFCSTMDEISDTELDSMLQEMDADDNQADDQQMPDDEKSCSASPVTEEESVRILSDEQETTSNDQMNVDNFSQASTVEFADLKQPESTPVTAMGEDVASSFSSTESDSLSGRKLDGEVEVDREHEDASLATDALETQEQRPQRPQTLNLNGCQAESSTPSQDENPEIQQETLQPTEVREGAAGVGVIPGEDDEESPIYEAVGYSDPHANLGKVPPIWVPDNMAGQCMQCQQKFTMIKRRHHCRACGKVLCSVCCSQRFRLEFATEPESRVCVQCYMILSERQANGLNSESAPGSALPPTPIRSPNPNNPMEYCSTIPPHRQVANSPGAPPPSVIVPVGVLKKTDGSSSNSSSSDGQKGQRKRKSVMFSDGIAPGSELASTMEQQWGESKHSRRGLSRSGSGAGQKPPTPATEEPPRSIDTSSTLGLVAQLFRGSIPPSAAAATLSATETSAGRSSSQSQAQTSPRRKAESSRNRKLPPNGDAQGCYLPPEENGLPPICISSKEGGEVDYKVVRNDGSLLDRLQNETLKFIIKNNFFVLVKIVNMSCCMNRWVLNFTTSGLHHMGSDELIILLEIKQPKQEEYVKGEVAIPKDLFQHLYEIYVEAEHARSGTHELAFTSPRNANFLGSREHGGFIFIRPTYQCLQGVIVPDNPYLVGVLIHRHEVPWAKVLPLRLILRLGAQYRYYPCPLISVRGRESVYGEIAQTIINFLVDFRNYSYSLPAIRGLYIHMEDRQTTVIIPKYRQQDVIKAINNASDHILAFAGNFSKVADGHLVGMQNINDDRSEMYSYSTQAINIQGQPRKITGASFFVLNEALKSSSGLSGKCSIVEDGLMVQIMPAKMEEVRQALRNQNDIDIVCGPIDATDDQSEIVSIKWVDNNRDINVGVKSPIDDQPMDGISNMRVLKWASFNYSNTNYAIRLSDIYIIKCEDWYATNGGNCEEITRIAEQLARSASMALLPLLDLLAAAGINKLGLRATLDQDNVGYEAGARGSKLPPLYMNALDNHLIATLHGESSGIQEPIILELIFYILNA
Protein: Holliday junction branch migration complex subunit RuvA (P9WGW3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). Binds HJ DNA. RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00031}.
Interaction partners:
- Holliday junction branch migration complex subunit RuvB
- Crossover junction endodeoxyribonuclease RuvC
- Protein RecA
- LexA repressor
- UvrABC system protein A
- DNA repair protein RecN
- ATP-dependent DNA helicase RecG
- ATP-dependent DNA helicase UvrD1
- UvrABC system protein B
- UvrABC system protein C
Sequence:
MIASVRGEVLEVALDHVVIEAAGVGYRVNATPATLATLRQGTEARLITAMIVREDSMTLYGFPDGETRDLFLTLLSVSGVGPRLAMAALAVHDAPALRQVLADGNVAALTRVPGIGKRGAERMVLELRDKVGVAATGGALSTNGHAVRSPVVEALVGLGFAAKQAEEATDTVLAANHDATTSSALRSALSLLGKAR
Protein: Ift52 protein (Intraflagellar transport protein 52) (Q5PRA7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDKEQRNIVVFNASKRELFTSSSGYKSLQKKLRAQWKIQSIKEELTLEKLQGVKLWITAGPREKFTAAELEVLKQYLDSGGALLVMIGEGGELKYDTNINFLLEEFGIMVNNDAVIRNVYYKYFHPKEALVSNGVLNREISRAAGKVVTGVIDEENTGNNSQALTFVYPYGATLNVMKPAVAILSTGSVCFPLNRPVLAFHHSKNAGKLAVLGSCHMFSDQYLDKEENSRIMDVVFQWLTTDSIHLNQIDAEDPEITDYMMLPDTGSLSERLRVCLQEGDENPRDFTSLFDMSLLKLHTNTLPSVLDAYKQLNVKHEALQLITPQFETPLPPLQPAVFQPAFRDLPPPMLDLFDLDETFSSEKVRLAQLSNKCTDDDLEFYVRKCGDILGVTGNLDKDKRDAKHILEHVFFQVVEFKKLNEEHDVDTAEARFSMY
Protein: Probable cinnamyl alcohol dehydrogenase 9 (AtCAD9) (EC 1.1.1.195) (P42734)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in lignin biosynthesis. May catalyze the final step specific for the production of lignin monomers, like coniferyl alcohol, sinapyl alcohol and 4-coumaryl alcohol.
Interaction partners:
- Cinnamoyl-CoA reductase 2
- Cinnamoyl-CoA reductase 1
- Flavone 3'-O-methyltransferase 1
- Aldehyde dehydrogenase family 2 member C4
- F5F19.5 protein
- Cytochrome P450 84A1
- Trans-cinnamate 4-monooxygenase
- Peroxidase 17
- Caffeoyl-CoA O-methyltransferase 1
- Phenylalanine ammonia-lyase 1
Sequence:
MAKSPETEHPNKVFGWGARDKSGVLSPFHFSRRDNGENDVTVKILFCGVCHTDLHTIKNDWGYSYYPVVPGHEIVGIATKVGKNVTKFKEGDRVGVGVISGSCQSCESCDQDLENYCPQMSFTYNAIGSDGTKNYGGYSENIVVDQRFVLRFPENLPSDSGAPLLCAGITVYSPMKYYGMTEAGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSTKAEEAINHLGADSFLVTTDPQKMKAAIGTMDYIIDTISAVHALYPLLGLLKVNGKLIALGLPEKPLELPMFPLVLGRKMVGGSDVGGMKETQEMLDFCAKHNITADIELIKMDEINTAMERLAKSDVRYRFVIDVANSLSPP
Protein: Aldo-keto reductase AKR1C12 (Q9R0M7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSKQHYVKLNDGHLIPALGFGTYKPKEVPKSKSLEAACLALDVGYRHVDTAYAYQVEEEIGQAIQSKIKAGVVKREDLFVTTKLWCGCFRPELVKPALEKSLKSLQLDYVDLYLIHYPVPMKPGDNESPLDENGKFLLDTVDFCDTWERLEECKDAGLVKSIGVSNFNHRQLERILNNPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKEWVDQNSPVLLNDPVLCDVAKRNKRSPALIALRYLFQRGIVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRYLPAEFLADHPEYPFSEEY
Protein: StAR related lipid transfer domain containing 10 (F5H8H3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKLAASTEPQGPRPVLGRESVQVPDDQDFRSFRSECEAECRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACLKYPEWKQKHLPHFKPWLHPEQSPLPSLALSELSVQHADSLENIDESAVAESREERMGGAGGEGSDDDTSLT
Protein: Apoptotic chromatin condensation inducer 1 (E7EQT4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWRRKHPRTSGGTRGVLSGNRGVEYGSGRGHLGTFEGRWRKLPKMPEAVGTDPSTSRKMAELEEVTLDGKPLQALRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAAELEGKSSSISEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSPSPPRLTEDRKKASLVALPEQTASEEETPPPLLTKEASSPPPHPQLHSEEEIEPMEGPAPAVLIQLSPPNTDADTRELLVSQHTVQLVGGLSPLSSPSDTKAESPAEKVPEESVLPLVQKSTLADYSAQKDLEPESDRSAQPLPLKIEELALAKGITEECLKQPSLEQKEGRRASHTLLPSHRLKQSADSSSSRSSSSSSSSSRSRSRSPDSSGSRSHSPLRSKQRDVAQARTHANPRGRPKMGSRSTSESRSRSRSRSRSASSNSRKSLSPGVSRDSSTSYTETKDPSSGQEVATPPVPQLQVCEPKERTSTSSSSVQARRLSQPESAEKHVTQRLQPERGSPKKCEAEEAEPPAATQPQTSETQTSHLPESERIHHTVEEKEEVTMDTSENRPENDVPEPPMPIADQVSNDDRPEGSVEDEEKKESSLPKSFKRKISVVSATKGVPAGNSDTEGGQPGRKRRWGASTATTQKKPSISITTESLKSLIPDIKPLAGQEAVVDLHADDSRISEDETERNGDDGTHDKGLKICRTVTQVVPAEGQENGQREEEEEEKEPEAEPPVPPQVSVEVALPPPAEHEVKKVTLGDTLTRRSISQQKSGVSITIDDPVRTAQVPSPPRGKISNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQDELDYHRGLLVDRPSETKTEEQGIPRPLHPPPPPPVQPPQHPRAEQREQERAVREQWAEREREMERRERTRSEREWDRDKVREGPRSRSRSRDRRRKERAKSKEKKSEKKEKAQEEPPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQKEAERAERAKEREKRRKEQEEEEQKEREKEAERERNRQLEREKRREHSRERDRERERERERDRGDRDRDRERDRERGRERDRRDTKRHSRSRSRSTPVRDRGGRR
Protein: SD15071p (Q6AWS2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPFSDPFASATSKTVFFSDYVYVETTPNSPYLIRRIEELNKNQTGNVEAKVMCFYRRRDLPNPLVQLADKHQPALDEERTSPTQTSGGGGSATGNSGSNSSGTSNNNSSSTAIGGGAGGSGGAGGDAEKGEALTSKQRYQIKHRELFLSRQVESIPATQIRGKCSVTLLNETESLQSYLNKDDTFFYCLVFDPNQKTLLADKGEIRVGSRYQCDIPAKLKDTATDDRKLEELESLVWTPEHSLTDRKIDQFLVVSRSIGTFARALDCSSSVKQPSLHMSAAAASRDITLFHAMNILHKHEYSIEESMSSLVPSTGPVLCRDEIEDWSASEANLFEEALEKYGKDFNDIRQDFLPWKTLKQIIEYYYMWKTTDRYVQQKRVKAVEAELKLKQVYIPQYNNNGKGNGTSTKAGGGIYNGTTNGSTDLSSNGKPCESCGTTKSSQWNSVSSGHSTSRLCLSCWEYWRRYGSMKSATKGDAGEGDAKKKSSSAASTPTATLAGLATTPTAVVDLNDDEKISDLTNRQLHRCSIVNCGKEFKLKTHLARHYAQAHGIAISSGSPRPIMKTRTAFYLHTNPMTRVARAICRSIVKPKKAARQSAYAINAMLVKQEFTNRISGKSQAEIKKLLLLKPKDRGSVTTIANRLGAPGSGPHEWLVLTPKDKMPLPAVVSFPKPPKAPDGSLVYDRVPNKSPDVVAVPADKELTIIPTQATSTIRKRAHEDQQLNGTEVTIVPSGPPAKRPNKDPMPSHCPSPEQFAAMMAASGQPLSRHHLNGKQKIAQMARGGNGRKQVISWMDAPDDVYFRANDTHKPFYRKTRKILSAVDLRRAARKPWRTLPIKPAAPEPSSRPIESQIVILD
Protein: RE17477p (Senescence marker protein-30, isoform A (EC 3.1.1.17)) (Senescence marker protein-30, isoform B) (Senescence marker protein-30, isoform D) (Smp-30 protein) (Q9VFG5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSYKVEAVPDSYAALGEGPHWDVDRQSLYYVDLESAGINRYDFKQNKVYRAKIEGEIFASFILPVENKPQEFAVGCGLRTVIVQWDGVSAVAKVTRTLFEVQPDLKENRLNDAKTDPNGRFYGGTMADSGDIFTQWKGELYSWQAGGQPNAIRSKVGISNGLAWDVKAKKFYFIDTNNHEVLAYDYNQSTGAVSNPKVIFDLRKIRPEGPLFPDGMTVDTDGNIYVATFNGGTVFKVNPSTGKILLEIKIPTTQITSVAFGGPNLDILYVTTANKFDQPKPAGTTFQVTGLNAKGYAGVNLKI
Protein: Mediator of RNA polymerase II transcription subunit 11 (Mediator complex subunit 11) (Q9P086)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 22
Sequence:
MATYSLANERLRALEDIEREIGAILQNAGTVILELSKEKTNERLLDRQAAAFTASVQHVEAELSAQIRYLTQVATGQPHEGSSYSSRKDCQMALKRVDYARLKLSDVARTCEQMLEN
Protein: Macropin (MAC-1) (C0HL98)
Organism: Macropis fulvipes (Solitary bee) (Megilla fulvipes)
Function: Antimicrobial peptide active against Gram-positive bacteria like B.subtilis, S.aureus and L.monocytogenes as well as against Gram-negative bacteria like E.coli and P.aeruginosa with minimum inhibitory concentrations (MIC) between 1.3 uM and 35 uM. Active against fungus C.albicans (MIC=6.3 uM). Has little hemolytic activity. Acts by disrupting membranes and bacterial cell wall structures. Adopts an alpha-helical structure in a membrane mimic environment. Binds to peptidoglycan and lipopolysaccharide (LPS).
Subcellular location: Secreted {ECO:0000269|PubMed:24616110}. Target cell membrane {ECO:0000269|PubMed:24616110, ECO:0000269|PubMed:29185466}. Note=Adopts an alpha-helical structure in a membrane mimic environment. {ECO:0000269|PubMed:24616110, ECO:0000269|PubMed:29185466}.
Interaction partners:
Sequence:
GFGMALKLLKKVL
Protein: CRC domain-containing protein TSO1 (Q9LUI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable floral-specific cell division component, required for proper organ formation in flowers. Regulates the floral meristem cell division and the inflorescence meristem organization. Plays a role in development of both male and female reproductive tissues.
Subcellular location: Nucleus {ECO:0000269|PubMed:10769244, ECO:0000269|PubMed:10769245}.
Interaction partners:
- Retinoblastoma-related protein 1
- Transcription factor MYB3R-1
- Transcription factor E2FC
- F-box associated ubiquitination effector family protein
- Short integuments 2, mitochondrial
- Transcription factor MYB3R-4
- Histone-binding protein MSI1
- Transcription factor MYB3R-3
- Large ribosomal subunit protein uL14my
- Protein CHAPERONE-LIKE PROTEIN OF POR1, chloroplastic
Sequence:
MDKSQKNPTSQIGTSTPKSKFEDSPVFNYISNLSPIESVKSISTAQTFSSLSFTSPPPVFTSPHVISHRESRFFRCHNSVDRSKHLESLDGSAVKGEVVVPLVEDLNKEASLEDEEETSVETSSELPQIMKFDSQTSEHSDSPCTEDVVIEASSDPPRGDNGSSSEDVTMGLQNMLVVREGNDTPGCGRLISDATELLVFRSPNDSEAFRCLVDKISSSERRFCAGVKSTKRPDINKDIPANGSSNENQPLAVLPTNESVFNLHRGGMRRRCLDFEMPGKRKKDIVDDQQSVCDNNVAGESSSSCVVPGIGLHLNAVAMSAKDSNISVIHGYSISGEIQKSFSGSTTPIQSQDTVQETSDQAENEPVEEVPKALVFPELNLGSLKKKMRKSEQAGEGESCKRCNCKKSKCLKLYCECFAAGVYCIEPCSCIDCFNKPIHEETVLATRKQIESRNPLAFAPKVIRNADSIMEASDDASKTPASARHKRGCNCKKSNCMKKYCECYQGGVGCSMNCRCEGCTNVFGRKDGSLLVIMESKLEENQETYEKRIAKIQHNVEVSKEVEQNPSSDQPSTPLPPYRHLVVHQPFLSKNRLPPTQFFLGTGSSSFRKPNSDLAQSQNEKKPLETVTEDKTEIMPEILLNSPIANIKAISPNSKRVSPPQPGSSESGSILRRRGNGRKLILRSIPAFPSLNPNQ
Protein: Interferon regulatory factor 3 (B7SEE0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- Interferon
- TIR domain-containing adapter molecule 1
- Stimulator of interferon genes protein
- Inhibitor of nuclear factor kappa B kinase subunit epsilon
- histone acetyltransferase
- Mitochondrial antiviral-signaling protein
- Interferon regulatory factor 7
- E1A-binding protein p300 b.
- Cyclic GMP-AMP synthase
Sequence:
MTQAKPLFVPWLYEQIQSGRYPGVCWKNEDCTQFSIPWKHALRQDSNSDDVLIFKAWAQTSAAGDGRLNGDPSVWKRNFRSALRAKGFKMISDKKNDGADPHKVYQFPSDPHSAVHIILNPNDLYVDPGTQIYDFQAVVPIEAISSSDEGAVGGLGQISPTEGAMAVNHISREYQQTATQPHLGAVPDHTAIPEPNLATFFRIKVYYKGKMVMEQLVENDSGFRLMYHRNMDESGLQDGAGLPVVTLPPAEGMPDQMQTRLTNDILDNLGGLEIRRSDGVIHGHRWGSSRIYWGLCKHERSQTPRELSKNTPQPIYLMKDYISGGRPVNFLAEVDLNKHGCLMVYRSVGLMQFIQTGGESPSCTLYFFLGEKWPDPKMKPWEKKLIMIEVNLTALEFLKSMAVEQGASSLQSDELQLSLEQMMELC
Protein: CCCH-type zinc finger protein oma-1 (Maturation oocyte expansion protein 1) (Oocyte maturation defective protein 1) (G5EC86)
Organism: Caenorhabditis elegans
Function: Zinc-finger RNA-binding protein that binds to 5'-UA[AU]-3' motifs in the 3'-UTR of maternal mRNAs to suppress translation in oocytes and embryos. Acts as a ribonucleoprotein particle component that may exert part of its function within cytoplasmic foci of unfertilized oocytes. Acts redundantly with oma-2 to control the temporal expression and distribution of maternal proteins and thereby promote meiotic progression, oocyte maturation, fertilization and embryonic development. Recruits the translational repressor ifet-1 to the 3'-UTR of mei-1 and zif-1 to negatively regulate their translation. By suppressing the translation of the E3 ligase zif-1, may in turn play a role in the stabilization of zif-1 targets such as the maternal transcriptional repressor protein pie-1. Following fertilization, sequesters the transcription initiation factor, taf-4, in the cytoplasm, which prevents its nuclear localization and thus allows for transcriptional suppression in early embryos, but not in oocytes. Also, together with oma-2, is involved in P-granule distribution during embryonic development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:18854162}. Cytoplasmic granule {ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:25261697}. Nucleus {ECO:0000269|PubMed:18854162}. Note=Expressed in cytoplasmic P-granules in developing oocytes, and remains in P-granules following fertilization when cytoplasmic expression is abolished (PubMed:12296824, PubMed:12781695, PubMed:16611242, PubMed:25261697). When phosphorylated, increased levels in the cytoplasm of embryos after meiosis II and before anaphase of the first mitotic division (PubMed:16289132). {ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:18854162, ECO:0000269|PubMed:25261697}.
Interaction partners:
- PUM-HD domain-containing protein
- glutamine synthetase
- LDL receptor repeat-containing protein egg-1
- Zinc finger protein mex-5
- Chitin-binding domain protein cbd-1
- Pumilio domain-containing protein 7
- Chondroitin proteoglycan 4 domain-containing protein
- RNA-binding protein pos-1
- Inactive protein-tyrosine phosphatase egg-5
- Uncharacterized protein
Sequence:
MNVNGENNEKIDEHHLESSLAGVPTLPVSPLDHAKDLSQTNPNAQIGDLVTQTANLIAIKKQLLEDIAFNQHIQSMQVRAIQSFPQNNQVAPPFQQFDPRRRGLARMQKPESYKTVICQAWLESKTCSFADNCRFAHGEEELRPTFVEPLQNNKYKTKLCDKYTTTGLCPYGKRCLFIHPDHGPNAYIRADKLLEVSQRHALADIRDQMEQHIMTNGRIAAPPLSAIQHPLEMFARPSTPDEPAAKLPLGPTPVSTRGPRYELPTKELHDAEGAMTYPPSRWPLDPSMFALDAWNMAHRPASPLDSMVLGSAPNAGSFGMLGKQNTPGGVSGYSSAGSTPSQDLSSSSLNAASAAAAAAYFANSAVAQSLLMKSVATDPMMSCNGPFSPMPGFDQLAENMTKHLNLW