wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (eIF-3-beta) (eIF3 p36) (B0BNA7)
Organism: Rattus norvegicus (Rat)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit L
Sequence:
MKPILLQGHERSITQIKYNREGDLLFTVAKDPIVNVWYSVNGERLGTYMGHTGAVWCVDADWDTKHVLTGSADNSCRLWDCETGKQLALLKTNSAVRTCGFDFGGNIIMFSTDKQMGYQCFVSFFDLRDPSQIDSNEPYMKIPCNDSKITSAVWGPLGECIIAGHESGELNQYSAKSGEVLVNVKEHSRQINDIQLSRDMTMFVTASKDNTAKLFDSTSLEHQKTFRTERPVNSAALSPNYDHVVLGGGQEAMDVTTTSTRIGKFEARFFHLAFEEEFGRVKGHFGPINSVAFHPDGKSYSSGGEDGYVRIHYFDPQYFEFEFEA
Protein: WD repeat-containing protein 11 (Bromodomain and WD repeat-containing protein 2) (WD repeat-containing protein 15) (Q9BZH6)
Organism: Homo sapiens (Human)
Function: Involved in the Hedgehog (Hh) signaling pathway, is essential for normal ciliogenesis. Regulates the proteolytic processing of GLI3 and cooperates with the transcription factor EMX1 in the induction of downstream Hh pathway gene expression and gonadotropin-releasing hormone production. WDR11 complex facilitates the tethering of Adaptor protein-1 complex (AP-1)-derived vesicles. WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29263200}. Cytoplasm {ECO:0000269|PubMed:20887964}. Nucleus {ECO:0000269|PubMed:20887964, ECO:0000269|PubMed:29263200}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29263200}. Cytoplasmic vesicle {ECO:0000269|PubMed:29426865}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:29426865, ECO:0000269|PubMed:34413497}. Note=Shuttles from the cilium to the nucleus in response to Hh signaling (PubMed:29263200). Might be shuttling between the nucleus and the cytoplasm (PubMed:20887964). {ECO:0000269|PubMed:20887964, ECO:0000269|PubMed:29263200}.
Interaction partners:
- Protein Njmu-R1
- N-alpha-acetyltransferase 40
- Torsin-1A
- Tumor necrosis factor receptor superfamily member 25
- Tumor necrosis factor receptor superfamily member 10A
- Exportin-T
Sequence:
MLPYTVNFKVSARTLTGALNAHNKAAVDWGWQGLIAYGCHSLVVVIDSITAQTLQVLEKHKADVVKVKWARENYHHNIGSPYCLRLASADVNGKIIVWDVAAGVAQCEIQEHAKPIQDVQWLWNQDASRDLLLAIHPPNYIVLWNADTGTKLWKKSYADNILSFSFDPFDPSHLTLLTSEGIVFISDFSPSKPPSGPGKKVYISSPHSSPAHNKLATATGAKKALNKVKILITQEKPSAEFITLNDCLQLAYLPSKRNHMLLLYPREILILDLEVNQTVGVIAIERTGVPFLQVIPCFQRDGLFCLHENGCITLRVRRSYNNIFTTSNEEPDPDPVQELTYDLRSQCDAIRVTKTVRPFSMVCCPVNENAAALVVSDGRVMIWELKSAVCNRNSRNSSSGVSPLYSPVSFCGIPVGVLQNKLPDLSLDNMIGQSAIAGEEHPRGSILREVHLKFLLTGLLSGLPAPQFAIRMCPPLTTKNIKMYQPLLAVGTSNGSVLVYHLTSGLLHKELSIHSCEVKGIEWTSLTSFLSFATSTPNNMGLVRNELQLVDLPTGRSIAFRGERGNDESAIEMIKVSHLKQYLAVVFRDKPLELWDVRTCTLLREMSKNFPTITALEWSPSHNLKSLRKKQLATREAMARQTVVSDTELSIVESSVISLLQEAESKSELSQNISAREHFVFTDIDGQVYHLTVEGNSVKDSARIPPDGSMGSITCIAWKGDTLVLGDMDGNLNFWDLKGRVSRGIPTHRSWVRKIRFAPGKGNQKLIAMYNDGAEVWDTKEVQMVSSLRSGRNVTFRILDVDWCTSDKVILASDDGCIRVLEMSMKSACFRMDEQELTEPVWCPYLLVPRASLALKAFLLHQPWNGQYSLDISHVDYPENEEIKNLLQEQLNSLSNDIKKLLLDPEFTLLQRCLLVSRLYGDESELHFWTVAAHYLHSLSQEKSASTTAPKEAAPRDKLSNPLDICYDVLCENAYFQKFQLERVNLQEVKRSTYDHTRKCTDQLLLLGQTDRAVQLLLETSADNQHYYCDSLKACLVTTVTSSGPSQSTIKLVATNMIANGKLAEGVQLLCLIDKAADACRYLQTYGEWNRAAWLAKVRLNPEECADVLRRWVDHLCSPQVNQKSKALLVLLSLGCFFSVAETLHSMRYFDRAALFVEACLKYGAFEVTEDTEKLITAIYADYARSLKNLGFKQGAVLFASKAGAAGKDLLNELESPKEEPIEE
Protein: Gastrin-releasing peptide (GRP) [Cleaved into: Neuromedin-C (GRP-10) (GRP18-27)] (P07492)
Organism: Homo sapiens (Human)
Function: Stimulates the release of gastrin and other gastrointestinal hormones (By similarity). Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior (By similarity). Contributes primarily to nonhistaminergic itch sensation (By similarity). In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear (By similarity). In another study, shown to act on vasoactive intestinal peptide (VIP)-expressing cells in the auditory cortex, most likely via extrasynaptic diffusion from local and long-range sources, to mediate disinhibition of glutamatergic cells via VIP cell-specific GRPR signaling which leads to enhanced auditory fear memories (By similarity). Contributes to the regulation of food intake (By similarity). Inhibits voltage-gated sodium channels but enhances voltage-gated potassium channels in hippocampal neurons (By similarity). Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:3211139}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q863C3}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q8R1I2}. Note=In neurons of the retrotrapezoid nucleus/parafacial respiratory group, expressed on neuron projections which project into the pre-Botzinger complex. {ECO:0000250|UniProtKB:Q8R1I2}.
Interaction partners:
- Gastrin-releasing peptide receptor
- Neuromedin-B
- Neuromedin-B receptor
- Bombesin receptor subtype-3
- Protachykinin-1
- Angiotensinogen
- Neurotensin/neuromedin N
- Cholecystokinin
- Gastrin
- Pro-glucagon
Sequence:
MRGRELPLVLLALVLCLAPRGRAVPLPAGGGTVLTKMYPRGNHWAVGHLMGKKSTGESSSVSERGSLKQQLREYIRWEEAARNLLGLIEAKENRNHQPPQPKALGNQQPSWDSEDSSNFKDVGSKGKVGRLSAPGSQREGRNPQLNQQ
Protein: Cytochrome b-245 light chain (Cytochrome b(558) alpha chain) (Cytochrome b558 subunit alpha) (Neutrophil cytochrome b 22 kDa polypeptide) (Superoxide-generating NADPH oxidase light chain subunit) (p22 phagocyte B-cytochrome) (p22-phox) (Q6PH62)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236, ECO:0000256|PIRNR:PIRNR019635}.
Interaction partners:
- Neutrophil cytosol factor 4
- Neutrophil cytosolic factor 1.
- Neutrophil cytosol factor 2
- Cytochrome b-245, beta polypeptide
- NADPH oxidase 4.
- NADPH oxidase activator 1.
- Dual oxidase.
- NADPH oxidase 1
- NADPH oxidase organizer 1a.
- NADPH oxidase organizer 1b
Sequence:
MAKIEWAMWANEQALAAGLIYLTGGIVGVAGQFRGWQFAAFGIAAGVFVCLLEYPRSKRGKGTSIERSGQYCFTVCVKSFGPLTRNYYVRAFLHAALCVPGGFMLATVLGCVCLGMASLIYLSAAIHGEHWEPILHIETKKRLGESIKEPPQNPPPRPPPELRRKKADNLDAAAYDNPMSVTINE
Protein: FAD-linked sulfhydryl oxidase ERV2 (EC 1.8.3.2) (Q12284)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen in parallel to ERO1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11313344, ECO:0000269|PubMed:11584268}; Single-pass type III membrane protein {ECO:0000269|PubMed:11313344, ECO:0000269|PubMed:11584268}; Lumenal side {ECO:0000269|PubMed:11313344, ECO:0000269|PubMed:11584268}.
Interaction partners:
- Endoplasmic oxidoreductin-1
- Mitochondrial intermembrane space import and assembly protein 40
Sequence:
MKQIVKRSHAIRIVAALGIIGLWMFFSSNELSIATPGLIKAKSGIDEVQGAAAEKNDARLKEIEKQTIMPLMGDDKVKKEVGRASWKYFHTLLARFPDEPTPEEREKLHTFIGLYAELYPCGECSYHFVKLIEKYPVQTSSRTAAAMWGCHIHNKVNEYLKKDIYDCATILEDYDCGCSDSDGKRVSLEKEAKQHG
Protein: Interleukin-13 (Q4VB50)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MALLLTTVIALTCLGGFASPGPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAIEKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGQFNRNFESIIICRDRT
Protein: Focal adhesion kinase 1 (EC 2.7.10.2) (Protein-tyrosine kinase 2) (pp125FAK) (E7ESA6)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
Sequence:
MLLELAGQEALKPAGAIYMEKSGCSPFPVCWAKEYDRYLASSKIMAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
Protein: Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12 (NCp12); Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4] (P03354)
Organism: Rous sarcoma virus subgroup C (strain Prague) (RSV-Pr-C)
Function: Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. Binds to inositol hexakisphosphate (IP6), which allows the assembly of the polyhedral capsid.
Subcellular location: [Matrix protein p19]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMILGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGPALTDWARVREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLNRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADIMQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRTAPSTLTTPGEIIKYVLDRQKTAPLTDQGIAAAMSSAIQPLIMAVVNRERDGQTGSGGRARGLCYTCGSPGHYQAQCPKKRKSGNSRERCQLCNGMGHNAKQCRKRDGNQGQRPGKGLSSGPWPGPEPPAVSLAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVMEAANPQIHGIGGGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNLIGRATVLTVALHLAIPLKWKPDHTPVWIDQWPLPEGKLVALTQLVEKELQLGHIEPSLSCWNTPVFVIRKASGSYRLLHDLRAVNAKLVPFGAVQQGAPVLSALPRGWPLMVLDLKDCFFSIPLAEQDREAFAFTLPSVNNQAPARRFQWKVLPQGMTCSPTICQLVVGQVLEPLRLKHPSLCMLHYMDDLLLAASSHDGLEAAGEEVISTLERAGFTISPDKVQREPGVQYLGYKLGSTYVAPVGLVAEPRIATLWDVQKLVGSLQWLRPALGIPPRLMGPFYEQLRGSDPNEAREWNLDMKMAWREIVRLSTTAALERWDPALPLEGAVARCEQGAIGVLGQGLSTHPRPCLWLFSTQPTKAFTAWLEVLTLLITKLRASAVRTFGKEVDILLLPACFREDLPLPEGILLALKGFAGKIRSSDTPSIFDIARPLHVSLKVRVTDHPVPGPTVFTDASSSTHKGVVVWREGPRWEIKEIADLGASVQQLEARAVAMALLLWPTTPTNVVTDSAFVAKMLLKMGQEGVPSTAAAFILEDALSQRSAMAAVLHVRSHSEVPGFFTEGNDVADSQATFQAYPLREAKDLHTALHIGPRALSKACNISMQQAREVVQTCPHCNSAPALEAGVNPRGLGPLQIWQTDFTLEPRMAPRSWLAVTVDTASSAIVVTQHGRVTSVAVQHHWATAIAVLGRPKAIKTDNGSCFTSKSTREWLARWGIAHTTGIPGNSQGQAMVERANRLLKDRIRVLAEGDGFMKRIPTSKQGELLAKAMYALNHFERGENTKTPIQKHWRPTVLTEGPPVKIRIETGEWEKGWNVLVWGRGYAAVKNRDTDKVIWVPSRKVKPDITQKDEVTKKDEASPLFAGISDWIPWEDEQEGLQGETASNKQERPGEDTLAANES
Protein: Glutamine synthetase (EC 6.3.1.2) (O04998)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- glutamate synthase
- glutamate synthase
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
- Ferredoxin--nitrite reductase, chloroplastic
- glutamine--fructose-6-phosphate transaminase
- Glutamate-glyoxylate aminotransferase
- Amidophosphoribosyltransferase
- amidophosphoribosyltransferase
- glutamate dehydrogenase
Sequence:
MSLLSDLINLNLSESSEKIIAEYIWVGGSGMDLRSKARTLPGPVSDPSKLPKWNYDGSSTNQAPGQDSEVILYPQAIFKDPFRQGNNILVICDVYTPAGEPLPTNKRYNAAKIFSHPDVAAEVPWYGIEQEYTLLQKDTNWPLGWPIGGYPGPQGPYYCGIGADKAYGRDIVDAHYKACLYAGINISGINGEVMPGQWEFQVGPSVGISAGDEIWAARYILERITEIAGVVVSFDPKPIPGDWNGAGAHTNYSTKSMRENGGYEIIKKAIEKLGLRHKEHIAAYGEGNERRLTGKHETADINTFSWGVANRGASVRVGRDTEKDGKGYFEDRRPSSNMDPYVVTSMIAETTLLWKP
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q75GN8)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MANARNAAAASPPPPSSSSSYSSSASDGEILRSLHRLARDLAAAEAPAPFLETVFAAVSRRAKLLAAVFDDLLRCGRLPRSASLCLREVLLVLQRFKAVVADCSARSRMRLLLQADEVAARVRELQHDLATLLDLLPVPELGLADDVVDLLALASRQCRRSSPSADAAEHELKTGVLALIQEVEREIVPERERLEGILEEVGINDPACCSDEIETLEREIGDRVAERWTSAMIALVGLLRYAKCVLFTAATPRPMDTKVDVDDDDDDDDAEPPSPPPDFRCPISLDLMRDPVVSASGQTYDRESITRWFGSGKSTCPKTGQVLANLELVPNKALKNLISRWCRENGVAMESSEPSKPEPAPVVTANKAALEAARMTASFLVKKLSVSFSPAAANRVVHEIRQLARSGNDTRAFIGEAGAVPLLVPLLHSDDTATQLNAVTALLNLSILDANKKRIMHAEGAVEAICHAMGSGATWRAKENAAATVLSLASVHSYRRRLGRNPRVVERVVHLVRTGPSSTKKDAIAALLCLSGERENVGKLVEAGAAEAALSAISEEETAVAVLASLAKRGGAEAIVNIDGAVVRLVAELRRGTEWSRECAAAALVLLCRRVGAAVVAQVMSVSGVEWAIWELMATGTERARRKAASLGRACRRWAAAEQTAEYPATSDVTTTAITAS
Protein: phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (Formylglycinamide ribotide amidotransferase) (D4AB17)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAPVLHFYVRPSGHEGAASGHVLRRLQEKLPTLQNVETELCYNVHWAAETLPWAEEMKKLLWLFGCPLLQDDVARESWLVPGSNDLLLEVGPRLNFSTPASTNIVSVCQAAGLRAVDRVETTRRYRLSFAKQPTAEMEAISLAALHDRMTEQHYPDPIQSFSPQSIPAPLKDSINILAEGRPALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEVFDLAQSNSEHSRHWFFKGQLHVDGKKLARSLFESIMSTQSSSNPNNVLKFCDNSSAIQGKEVRFLRPEDSTRPSCFRQQRGLRHVVFTAETHNFPTGVAPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGYNLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREWIKPIMFSGGIGSMEAKHVGKEPPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPGGNPICSLHDQGAGGNGNVLKELSEPAGAVIYTSRFQLGDPTLNALEIWGAEYQESNALLLRPSDRDFLSRASARERCPACFVGTITGDKRIVLVDDRECLMGKSGQGDAPPTPPTPVDLDLDWVLGKMPQKEFFLQRKPPVLQPLALPPDLSVGQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHQELVGAATALGEQPVKSLLDPKAAARLAVSEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAGLADACEAMVTVMAALGVAVDGGKDSLSMAARVGTETVPAPGSLVISAYAVCPDITATVTPDLKHPGGKGHLLYVPLSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFHITQGLLKDRRLCSGHDVSDGGLVTCLLEMAFAGNCGIEVDVPAPGIHALPVLFAEEPGLVLEVQEADVAGVLQRYQSAGLHCLELGHTGEAGPQAMVRVSVNGTVVVEEPVGQLRALWEETSFQLDLLQAEPRCVTEEKQGLKERIGPSYCLPPTFPVASVPCKPGGPIPRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAVRLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFNPQAREELGRFRRRPDTFSLGVCNGCQLLALLGWVGSDPNEDQVEPDHDSQPAQPGLLLRHNLSGRFESRWATVRVEPGPALMLRGMEGSVLPVWSAHGEGYMAFSSPELQAKIKAKGLVPLHWADDDGNPTEQYPLNPNGSPGGIAGICSPDGRHLALMPHPERAVRLWQWAWRPSPFDGLSTSPWLQLFINARNWTQEDSC
Protein: Maternal effect protein staufen (P25159)
Organism: Drosophila melanogaster (Fruit fly)
Function: RNA-binding protein which forms ribonucleoprotein complexes (RNPs) that play critical roles in the localization, translational repression and turnover of RNAs during embryogenesis, neurotransmission and neurogenesis. In the oocyte, essential for the localization of both the osk/oskar mRNA to the posterior pole and bcd/bicoid RNA to the anterior pole, and is therefore required for the correct anterior-posterior patterning of the developing embryo. Association with osk or bcd at their respective poles, appears to promote the formation and stabilization of the ribonucleoprotein complexes. Integral component of diverse neuritic ribonucleoprotein complexes (RNPs) that mediate the transport, translation and turnover of neuronal RNAs during neuorgenesis and the translation repression of synaptic transcripts in preparation for their dendritic targeting.
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:17178403}. Note=Detected within ribonucleoprotein granules in pherpiheral nerves that are exiting the larval central nervous system, and cell bodies within the ventral ganglion. {ECO:0000269|PubMed:17178403}.
Interaction partners:
- Miranda, isoform A
- Maternal effect protein oskar
- Regulator of nonsense transcripts 1 homolog
- Fragile X messenger ribonucleoprotein 1 homolog
- Homeotic protein bicoid
- ATP-dependent RNA helicase me31b
- Maternal protein pumilio
- Protein CASC3
- 5'-3' exoribonuclease 1
- Protein cup
Sequence:
MQHNVHAARPAPHIRAAHHHSHSHAHMHLHPGMEQHLGPSLQQQQQPPPPPQQPPHRDLHARLNHHHLHAQQQQQQQTSSNQAGAVAAAGAAYHHGNINSNSGSNISSNSNQMQKIRQQHQHLSSSNGLLGNQPPGPPPQAFNPLAGNPAALAYNQLPPHPPHHMAAHLGSYAAPPPHYYMSQAKPAKYNHYGSNANSNSGSNNSNSNYAPKAILQNTYRNQKVVVPPVVQEVTPVPEPPVTTNNATTNSTSNSTVIASEPVTQEDTSQKPETRQEPASADDHVSTGNIDATGALSNEDTSSSGRGGKDKTPMCLVNELARYNKITHQYRLTEERGPAHCKTFTVTLMLGDEEYSADGFKIKKAQHLAASKAIEETMYKHPPPKIRRSEEGGPMRTHITPTVELNALAMKLGQRTFYLLDPTQIPPTDSIVPPEFAGGHLLTAPGPGMPQPPPPPAYALRQRLGNGFVPIPSQPMHPHFFHGPGQRPFPPKFPSRFALPPPLGAHVHHGPNGPFPSVPTPPSKITLFVGKQKFVGIGRTLQQAKHDAAARALQVLKTQAISASEEALEDSMDEGDKKSPISQVHEIGIKRNMTVHFKVLREEGPAHMKNFITACIVGSIVTEGEGNGKKVSKKRAAEKMLVELQKLPPLTPTKQTPLKRIKVKTPGKSGAAAREGSVVSGTDGPTQTGKPERRKRLNPPKDKLIDMDDADNPITKLIQLQQTRKEKEPIFELIAKNGNETARRREFVMEVSASGSTARGTGNSKKLAKRNAAQALFELLEAVQVTPTNETQSSEECSTSATMSAVTAPAVEATAEGKVPMVATPVGPMPGILILRQNKKPAKKRDQIVIVKSNVESKEEEANKEVAVAAEENSNNSANSGDSSNSSSGDSQATEAASESALNTSTGSNTSGVSSNSSNVGANTDGNNHAESKNNTESSSNSTSNTQSAGVHMKEQLLYLSKLLDFEVNFSDYPKGNHNEFLTIVTLSTHPPQICHGVGKSSEESQNDAASNALKILSKLGLNNAMK
Protein: Isopentenyl-diphosphate delta-isomerase (Q9FM77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- UBQ, helicase-c and DEAD-like helicase domain-containing protein
- Phenylalanine--tRNA ligase beta subunit, cytoplasmic
- Nucleic acid-binding, OB-fold-like protein
Sequence:
MAGIALVLDLLKKSQSKNTLHSSSFYSASAAAVSAAASAPFASRFLFGSFEPRVAYCDAAAAIDDDYLGAIRKMSADVLQRQPLAYISRSKEYNIQPKPVLSAFEFRALAMTTVRSLLMFYLPLLEPKTASEDDDDFLNNAAEENRHTDLIVPLKKSAKQIARETTVVTTRRVLERLALSYVSQRMAWKLLKDVPQSALRKAQRGLPTHVYIFKVSQTTLRGHFLGIAASWVVQVGIEIYRCVFPNVKPEEEEEEEKVEISQQAKDLGNKVVGITVRCGASLVFAAIGAGICSCLIRPSTGQWIGCALGDLAGPMVVSVCLQKTLQADY
Protein: MIP05121p (Q9VDX4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH17939p
- AT16150p
- FI08029p
- IP07030p
- J domain-containing protein
- AT25465p
- Cytochrome c oxidase subunit 6A-like 2, isoform B
- IP08114p
- FI09606p
- AT08308p
Sequence:
MHNNSCLEPMDRTKTTKLPQLKSSVTPYRPKPNLIRSDSPKLENDKRNGLDLELLDNPEIPSVKRVRWAPMYGERSPSKTGFTSVPLSSKKAQFDHDTTDELILANELRLAVHRGGGSIDPDKNYELRARLSPLQLPYSRVQRILKECELSERNHHTYSIPMDYGRQLVAMVCKIRTDNLPELKLRLASLLRQNKARFFNRHLFNETGLIEATLPSVTPLSFEEFNQTLRIDALWCKATDSTITDLAKGSVLFKCRPLDLQEVAYKLRQCNYKIVHKEVGHCPNKPLVELNDRQMARYQEFRKNLLQDIDVVKIYDNVRVQ
Protein: Uncharacterized protein AzuC (C1P605)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19121005, ECO:0000305|PubMed:21778229}; Peripheral membrane protein {ECO:0000305|PubMed:19121005, ECO:0000305|PubMed:21778229}.
Interaction partners:
- Aerobic glycerol-3-phosphate dehydrogenase
- Uncharacterized membrane protein YkgR
Sequence:
MKLRKILKSMFNNYCKTFKDVPPGNMFR
Protein: Uncharacterized serine-rich protein C1E8.05 (O42970)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable zinc transporter cis4
- Uncharacterized membrane protein C1322.03
- Uncharacterized WD repeat-containing protein C17D11.16
- Cell wall protein ecm33
Sequence:
MKLSFILSTLVAGALAYNEFSAPGPNAVLQEGGGVNTVSWSNLTSSTVTLTLYRGGNSALTPIETIASDIDNTGTYLWNIATYYEAADDYLLGLSFDGGETYSQYFTLQACSTCTISTSSLSYSGTISSTSIAPSMIGTRTSSSYFITSSSSTPSSSSSSSSSSPSSSSSKSSSSSKSSSSSSSSSKSSSSSSSSSKSSSSSSSSSKSSASPSSSKSSSKFSSSSFITSTTPASSSSSGAIVSNAKTASTDDSSSASSATSSVSSVVSSASSALSASASSASASVSSSASSDASPALKTGINALVAVGVVSAIALFL
Protein: Uroplakin-2 (UP2) (Uroplakin II) (UPII) (Q08537)
Organism: Bos taurus (Bovine)
Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in regulating the assembly of the AUM.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1A is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000269|PubMed:12475947}.
Interaction partners:
- Uroplakin-1a
- Uroplakin-1b
- Uroplakin-3a
- Uroplakin-3b
- Keratin, type I cytoskeletal 20
- Forkhead box R1
Sequence:
MASPWPVWTLSWILILLAVLVPGAAADFNISSLSGLLSPVMTESLLVALPPCHLTGGNATLTVRRANDSKVVRSSFVVPPCRGRRELVSVVDSGSGFTVTRLSAYQVTNLAPGTKYYISYLVTKGASTESSREIPMSTFPRRKAESIGLAMARTGGMVVITVLLSVAMFLLVLGLIIALALGARK
Protein: Pre-mRNA cleavage factor Im 25 kDa subunit 2 (Q8GXS3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O43809}. Note=In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles. {ECO:0000250|UniProtKB:O43809}.
Interaction partners:
- FIP1[V]-like protein
- 30-kDa cleavage and polyadenylation specificity factor 30
- Cleavage stimulation factor subunit 50
- Flowering time control protein FY
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 3-I
- Cleavage stimulation factor subunit 77
- Cleavage stimulating factor 64
- Pre-mRNA cleavage complex 2 Pcf11-like protein
- HEAT repeat-containing protein
Sequence:
MAMSQVVNTYPLSNYSFGTKEPKLEKDTSVADRLARMKINYMKEGMRTSVEGILLVQEHNHPHILLLQIGNTFCKLPGGRLKPGENEADGLKRKLTSKLGGNSAALVPDWTVGECVATWWRPNFETMMYPYCPPHITKPKECKRLYIVHLSEKEYFAVPKNLKLLAVPLFELYDNVQRYGPVISTIPQQLSRFHFNMISS