wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane protein 106B (Q9NUM4)
Organism: Homo sapiens (Human)
Function: In neurons, involved in the transport of late endosomes/lysosomes. May be involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking. May act as a molecular brake for retrograde transport of late endosomes/lysosomes, possibly via its interaction with MAP6 (By similarity). In motoneurons, may mediate the axonal transport of lysosomes and axonal sorting at the initial segment (By similarity). It remains unclear whether TMEM106B affects the transport of moving lysosomes in the anterograde or retrograde direction in neurites and whether it is important in the sorting of lysosomes in axons or in dendrites (By similarity). In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress. Required for proper lysosomal acidification (By similarity).
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:22511793, ECO:0000269|PubMed:23136129, ECO:0000269|PubMed:25066864}; Single-pass type II membrane protein {ECO:0000269|PubMed:22511793, ECO:0000269|PubMed:23136129, ECO:0000269|PubMed:25066864}. Lysosome membrane {ECO:0000269|PubMed:22511793, ECO:0000269|PubMed:25066864, ECO:0000269|PubMed:37421949}; Single-pass type II membrane protein {ECO:0000269|PubMed:22511793, ECO:0000269|PubMed:23136129, ECO:0000269|PubMed:25066864}. Cell membrane {ECO:0000269|PubMed:37421949}; Single-pass type II membrane protein {ECO:0000255}. Note=Colocalizes with LAMP1. A small fraction resides on the cell surface (PubMed:37421949). {ECO:0000269|PubMed:22511793, ECO:0000269|PubMed:25066864, ECO:0000269|PubMed:37421949}.
Interaction partners:
- TAR DNA-binding protein 43
- Progranulin
- Charged multivesicular body protein 2b
- Microtubule-associated protein 6
- Guanine nucleotide exchange factor C9orf72
- Microtubule-associated protein tau
Sequence:
MGKSLSHLPLHSSKEDAYDGVTSENMRNGLVNSEVHNEDGRNGDVSQFPYVEFTGRDSVTCPTCQGTGRIPRGQENQLVALIPYSDQRLRPRRTKLYVMASVFVCLLLSGLAVFFLFPRSIDVKYIGVKSAYVSYDVQKRTIYLNITNTLNITNNNYYSVEVENITAQVQFSKTVIGKARLNNITIIGPLDMKQIDYTVPTVIAEEMSYMYDFCTLISIKVHNIVLMMQVTVTTTYFGHSEQISQERYQYVDCGRNTTYQLGQSEYLNVLQPQQ
Protein: ATP-dependent DNA helicase 2 subunit KU70 (OsKU70) (EC 3.6.4.12) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (Q7F1M0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair. When associated with KU70, binds to double-stranded telomeric and non-telomeric DNA sequences, but not to single-stranded DNA (By similarity). Required for the maintenance of chromosome stability and normal developmental growth. Plays a role in maintaining telomere length. Acts as a negative regulator in telomere homeostasis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Os01g0685500 protein
- ATP-dependent DNA helicase 2 subunit KU80
- Putative DNA ligase 4
- Double strand break repair protein, putative, expressed
- Telomerase reverse transcriptase
- ATP-dependent DNA helicase
- Os01g0660500 protein
- Chlorophyll a-b binding protein
- Double-strand break repair protein MRE11
- Double-strand break repair protein MRE11
Sequence:
MDLDPEGLFRDDSDEDDDNVQEREANKEMVVYLIDASPKMFTPATKADEKEETHFHTIVNCITHALKTQIIGRSYDEVAICFFNTKEKKNLQELAGVYVYNVTEREPLDRPDARLIKEFSCIEDSFMSNIGSRYGITSGSRENTLYNALWVAQALLRKGSVKTVSKRIVIFTNEDDPFGGLTGAVKTDMIRTTIQRARDAQDLGLSIELLPLSRPDEEFNMSLFYADLIGLEGDEIVDYLPSSGEKLEDMTNQLKKRMMKKRKVKTLAFAITNDVCIEVNTYALIRSTTPGAITWLDSISNLPLKAERSFICNDTGALIQDPQKRFQVYNDKIVKFSTRELSDVKRVSSHHLRLLGFKPLDYLKDYHNLRPSTFIYPSDEQIFGSTRVFVALHSSMRRLGRFALAFYGNPTRPQLVALIAQEEVTSAGGQIEPPGIHMIYLPYSDDVRYPEEVHLTSDDAPRATDEQIKKASNLLRRIDLKNFSVCQFSNPALQRHYGILEALALGEDEMPDVKDETLPDEEGLARPVVVKAVEEFKASVYGENYDQEEAEAAAAKAGASKKRKALTDAAAEKSAAHNWAELADTGKLKDMTVVDLKSYLSAHGLPVSGKKEALVSRILTHLGK
Protein: Dorsal-ventral patterning protein Sog (Short gastrulation protein) (Q24025)
Organism: Drosophila melanogaster (Fruit fly)
Function: Putative negative growth factor. Antagonist of dpp, a protein involved in patterning the dorsal region and in the development of the neuroectoderm; dpp inhibition is enhanced by tsg. Required for establishment of a narrow stripe of peak levels of BMP signaling in the dorsal midline of early embryos, that will give rise to the amnioserosa.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:20599894}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:20599894}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:20599894}.
Interaction partners:
- Protein decapentaplegic
- Protein twisted gastrulation
- Dorsal-ventral patterning protein tolloid
- Protein 60A
- Protein screw
- Crossveinless 2
- Protein tolkin
- Protein snail
- receptor protein serine/threonine kinase
- Mothers against decapentaplegic homolog
Sequence:
MANKLRKSNAIEWATATGTVPLLERSCCHSEDAALEPQASKTSHREQAPILRHLSQLSHLLIIAGLLIVCLAGVTEGRRHAPLMFEESDTGRRSNRPAVTECQFGKVLRELGSTWYADLGPPFGVMYCIKCECVAIPKKRRIVARVQCRNIKNECPPAKCDDPISLPGKCCKTCPGDRNDTDVALDVPVPNEEEERNMKHYAALLTGRTSYFLKGEEMKSMYTTYNPQNVVATARFLFHKKNLYYSFYTSSRIGRPRAIQFVDDAGVILEEHQLETTLAGTLSVYQNATGKICGVWRRVPRDYKRILRDDRLHVVLLWGNKQQAELALAGKVAKYTALQTELFSSLLEAPLPDGKTDPQLAGAGGTAIVSTSSGAASSMHLTLVFNGVFGAEEYADAALSVKIELAERKEVIFDEIPRVRKPSAEINVLELSSPISIQNLRLMSRGKLLLTVESKKYPHLRIQGHIVTRASCEIFQTLLAPHSAESSTKSSGLAWVYLNTDGSLAYNIETEHVNTRDRPNISLIEEQGKRKAKLEDLTPSFNFNQAIGSVEKLGPKVLESLYAGELGVNVATEHETSLIRGRLVPRPVADARDSAEPILLKRQEHTDAQNPHAVGMAWMSIDNECNLHYEVTLNGVPAQDLQLYLEEKPIEAIGAPVTRKLLEEFNGSYLEGFFLSMPSAELIKLEMSVCYLEVHSKHSKQLLLRGKLKSTKVPGHCFPVYTDNNVPVPGDHNDNHLVNGETKCFHSGRFYNESEQWRSAQDSCQMCACLRGQSSCEVIKCPALKCKSTEQLLQRDGECCPSCVPKKEAADYSAQSSPATNATDLLQQRRGCRLGEQFHPAGASWHPFLPPNGFDTCTTCSCDPLTLEIRCPRLVCPPLQCSEKLAYRPDKKACCKICPEGKQSSSNGHKTTPNNPNVLQDQAMQRSPSHSAEEVLANGGCKVVNKVYENGQEWHPILMSHGEQKCIKCRCKDSKVNCDRKRCSRSTCQQQTRVTSKRRLFEKPDAAAPAIDECCSTQCRRSRRHHKRQPHHQQRSSS
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (A0A0B4K669)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MIGGRRCSEAARRLRRRPDTLELSVLGGQPIETELQEDNERTPTKGAGNVDEPGIEAPEASCSAPSKRTRWFQFARSSKNRRKRLHCNEDEDVKQPERRNSDLEGSPRACLAQPEGMNIGSSTQTIATPLMIGDSFYSLAPGGGNPPPNKSDDQELYKQRDPSVTSESKSVPSLRRLSQIRRRRSSYYFSENERRIRANDKEFNAQFKYHNNYIKTSKYSLFTFLPFNLLEQFQRLANFYFLCLLVLQLIPAISSLTPVTTAIPLIGVLTLTAVKDAYDDIQRHISDSQVNNRKSKTLRNGKLVEAKWSEVQVGDVIRLDNNQFVAADTLLLSTSEPNGLCFIETAELDGETNLKAKQCLTETIELGDRHDSLWNFNGEIICERPNNLLNKFDGTLIWRGQRFALDNEKILLRGCVLRNTQWCYGVVVFAGVDTKLMQNSGKTQFKSTGVDRLLNFIIIGIVLFLVSICALFAIGCAIWEGLIGQHFQLYLPWEHIIPKDYIPTGATVIGLLVFFSYAIVLNTVVPISLYVSVEVIRFVQSFLINWDEEMYYPTTNTYAKARTTTLNEELGQIQYIFSDKTGTLTQNIMTFNKCSINGRSYGDVIDLRTGELVEITEALQSVDFSANPHHESDFRWYDRTLLDAVRSDEEHSHVFFRLLALCHTVMAETVDGKLEYQAQSPDEAALVSAARNFGFVFRTRTPNSITIEVMGQTEEYELLNILDFNNVRKRMSVILRRGDSMVLYCKGADNVIYDRLHGGQEDLKARTQDHLNKFAGEGLRTLALAERRLTEQYYNDWRSRQQEAALSMDSREQKLNAIYEEIESEMQLVGVTAIEDKLQDGVPKSIANLQNAGIKIWVLTGDKQETAINIGYSCQLLTDELADVFIVDGNSVEEVEKQLRQFKESIKIYNRFRPGGFDPFDRLNSDSNMDPLSVTMTQTSAFMQETNLPPTPPPPPAISVVTFRWDEKNKDNKGGPDSAECNNLFGDEKGSEDGGTASIVVDENTGFALVVNGHSLVHCLSPELENKFLDIASQCKAVICCRVTPLQKALVVELIKRAKNAVTLAIGDGANDVSMIKAAHIGVGISGQEGLQAVLSSDYSIAQFRYLERLLLVHGRWSYYRMCKFLRYFFYKNFAFTLCHCWYSLFCGFSAQTVFDPMFISVYNLFYTSLPVLALGVFEQDVSDKNSLEFPRLYTPGLKSELFNIREFIYSVLHGAFTSLVLFLIPYGVYKDGVSANGFVVSDHMTLGAVVATILIVDNTAQISLYTSYWTVVNHVTIWGSLVWYFVLDYFYNYVIGGPYVGSLTQAMKDLTFWVTMLITVMALVAPVLAYKFYLLDVHPSLSDKIRQKSLKKIHSRASSDVRRTASSRRGRRSVRSGYAFAHQEGFGRLITSGKIMHKLPQDFAFPLGLGTKKTQVLHNNLNSADGPNSKGNNVTGHHMVNNNTNMRHNQNQNHSSMADITADGRGNGGDDGRGSGGSDDMSPRAPCQDLDTINL
Protein: GDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) (Neurotic protein) (Peptide-O-fucosyltransferase 1) (O-FucT-1) (Q9V6X7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer (By similarity). Plays a crucial role in Notch signaling. Initial fucosylation of Notch/N by O-fut1 generates a substrate for Fringe/Fng, an acetylglucosaminyltransferase that can then extend the fucosylation on the Notch EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by Delta/Dl or Serrate/Ser. Also required for the transport of Notch/N to the early endosome.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6EV70}.
Interaction partners:
- GDP-fucose protein O-fucosyltransferase 2
- O-glucosyltransferase rumi
- Fringe glycosyltransferase
- EGF domain-specific O-linked N-acetylglucosamine transferase
- Neurogenic locus Notch protein
- GDP-mannose 4,6 dehydratase
Sequence:
MQWLKMKLRFVNLILLLISSTCAQLGGDPNGYLTYCPCMGRFGNQADHFLGSLAFAKALNRTLILPPWVEYRRGELRSRQVPFNTYFEVEPLKEYHRVITMADFMWHLADDIWPESERVSFCYKERYSLQQEKNDPDKPNCHAKDGNPFGPFWDTFHIDFVRSEFYAPLHFDVHHSNEAAKWQTKYPAESYPVLAFTGAPASFPVQLENCKLQRYLQWSQRYREASKDFIREQLPRGAFLGIHLRNGIDWVRACEHVKDSQHLFASPQCLGYKNERGALYPELCMPSKEAIIRQLKRTIKNVRQTQPDNEIKSVFVASDSNHMIGELNTALSRMGISVHKLPEDDPYLDLAILGQSNHFIGNCISSYSAFEKRERDVHGFPSYFWGFPKEKDRKHTNVHEEL
Protein: Cilia- and flagella-associated protein 263 (Q9H0I3)
Organism: Homo sapiens (Human)
Function: Component of centriolar satellites contributing to primary cilium formation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:25074808}. Cell projection, cilium {ECO:0000250|UniProtKB:Q22KK0}. Note=Colocalized with HAP1 at centriolar satellites. Centriolar satellite localization requires PCM1 (PubMed:25074808). Localizes at cilium but not at the ciliary tips (By similarity). {ECO:0000250|UniProtKB:Q22KK0, ECO:0000269|PubMed:25074808}.
Interaction partners:
- Cilia- and flagella-associated protein 206
Sequence:
MTDDESESVLSDSHEGSELELPVIQLCGLVEELSYVNSALKTETEMFEKYYAKLEPRDQRPPRLSEIKISAADYAQFRGRRRSKSRTGMDRGVGLTADQKLELVQKEVADMKDDLRHTRANAERDLQHHEAIIEEAEIRWSEVSREVHEFEKDILKAISKKKGSILATQKVMKYIEDMNRRRDNMKEKLRLKNVSLKVQRKKMLLQLRQKEEVSEALHDVDFQQLKIENAQFLETIEARNQELTQLKLSSGNTLQVLNAYKSKLHKAMEIYLNLDKEILLRKELLEKIEKETLQVEEDRAKAEAVNKRLRKQLAEFRAPQVMTYVREKILNADLEKSIRMWERKVEIAEMSLKGHRKAWNRMKITNEQLQADYLAGK
Protein: Interleukin enhancer-binding factor 3 (Double-stranded RNA-binding protein 76) (DRBP76) (M-phase phosphoprotein 4) (MPP4) (Nuclear factor associated with dsRNA) (NFAR) (Nuclear factor of activated T-cells 90 kDa) (NF-AT-90) (Translational control protein 80) (TCP80) (Q12906)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs. As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response. Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:26240280}. Cytoplasm {ECO:0000269|PubMed:28625552}. Nucleus {ECO:0000269|PubMed:10749851, ECO:0000269|PubMed:26240280, ECO:0000269|PubMed:28625552}. Note=Localizes in the cytoplasm in response to viral infection. The unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000269|PubMed:21123651}.
Interaction partners:
- Interleukin enhancer-binding factor 2
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoproteins C1/C2
- RNA-binding protein FUS
- ATP-dependent RNA helicase A
- Heterogeneous nuclear ribonucleoprotein H
- Interferon-induced, double-stranded RNA-activated protein kinase
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein A1
Sequence:
MRPMRIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGSSEQAESDNMDVPPEDDSKEGAGEQKTEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLAAVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKPKNENPVDYTVQIPPSTTYAITPMKRPMEEDGEEKSPSKKKKKIQKKEEKAEPPQAMNALMRLNQLKPGLQYKLVSQTGPVHAPIFTMSVEVDGNSFEASGPSKKTAKLHVAVKVLQDMGLPTGAEGRDSSKGEDSAEETEAKPAVVAPAPVVEAVSTPSAAFPSDATAEQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFPDTPLALDANKKKRAPVPVRGGPKFAAKPHNPGFGMGGPMHNEVPPPPNLRGRGRGGSIRGRGRGRGFGGANHGGYMNAGAGYGSYGYGGNSATAGYSQFYSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKHAGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPYSNYGPPQGKQKGYNHGQGSYSYSNSYNSPGGGGGSDYNYESKFNYSGSGGRSGGNSYGSGGASYNPGSHGGYGGGSGGGSSYQGKQGGYSQSNYNSPGSGQNYSGPPSSYQSSQGGYGRNADHSMNYQYR
Protein: Cytochrome c (Q08IR9)
Organism: Hydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila)
Interaction partners:
Sequence:
MKKVTFALAGVMGFSATLAWAGTADLDAKFKEMIDRSFKTTGIAQKERMIQLDFQKVCSALEAGEKVDPKTIEQLRQAQEQTVRWPSDGKFLGNWKEGEKIAQSGRGLTWIDKPDTVNGGGCYNCHQLDPKELSYGNIGPSLAGYGKLRGNSEEVLKYAWRQIWNSKSVNLCSSMPRFGDAGILTEQQIKDVMAYLFDPESPVNKNHK
Protein: IGL@ protein (Q6PIQ7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAWALLLLSLLTQGTGSWAQSALTQPRSVSGSPGQSVTIPCTGTSSDVGNYNYVSWYRQHPGKAPKLMIYDVNKRPSGVPDRFSGSKSGNTASLTISGLQAEDEADYYCCSYAGTYTFGVFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS
Protein: Resistance-Nodulation-Cell Division (RND) multidrug efflux membrane fusion protein (G3XD21)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004519}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004519}.
Interaction partners:
- Efflux pump membrane transporter
- Multidrug resistance protein MexB
- Outer membrane protein OprM
- Probable transcriptional regulator
- Multidrug resistance protein MexA
- Probable Resistance-Nodulation-Cell Division
- Probable Resistance-Nodulation-Cell Division
- Porin domain-containing protein
- Protein CyaE
- Probable outer membrane protein
Sequence:
MHIQWTGSLRGLLAALVALFLLGCEEAADAGKTAEAPAEVGVIVARPAPIGITSELPGRLEAYRQAEVRARVAGIVTRRLYEEGQDVRAGTVLFQIDPAPLKAALDISRGALARAEASHAAAADKLKRYADLIKDRAISEREYTEAQTDARQALAQIASAKAELEQARLRLGYATVTAPIDGRARRALVTEGALVGEDSPTPLTRVEQIDPIYVNFSQPAGEVAAMQRAIREGQVKGVADKDIAVRLVLADGSEYPLAGELLFSDLAVDPGTDTIAMRALFRNPHRELLPGGYVQVRLQRAVNPQAITVPRDALIRTAQSAVVKVVNPKGLVEDVEVRADTLQGRDWIISRGLKGGEWVIVENAAQHAAGSSVQAVVRQPASADAPSPLAASPAGQ
Protein: Myosin 2 (F4K7C5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFLDAAKSDSRFSVCVCDTVLLYVYHVNKTKSPQKVEESREARKGKNKIQKAEVFDLRNEMVANFNPSVGSFVWVEDPDEAWIDGEVVQVNGDEIKVLCTSGKHVVTKISNAYPKDVEAPASGVDDMTRLAYLHEPGVLQNLHSRYDINEIYTYTGSILIAVNPFRRLPHLYSSHMMAQYKGASLGELSPHPFAVADAAYRQMINDGVSQSILVSGESGAGKTESTKLLMRYLAYMGGRAAAEGRSVEQKVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDEKGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPQEDVKKFKLEEPKKYHYLNQSKCLELDSINDAEEYHATRRAMDVVGISTEEQDAIFSVVAAILHIGNIEFAKGEEIDSSIPKDDKSLFHLKTAAELLSCDEKALEDSLCKRIMVTRDETITKTLDPEAATLSRDALAKVMYSRLFDWLVDKINSSIGQDHDSKYLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYKKEEINWSYIEFVDNQDILDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTFKTHKRFTKPKLARSDFTICHYAGDVTYQTELFLDKNKDYVIAEHQALLNSSSCSFVASLFPPMSDDSKQSKFSSIGTRFKQQLVSLLEILNTTEPHYIRCIKPNNLLKPGIFENENILQQLRCGGVMEAIRISCAGYPTRKHFDEFLARFGILAPEVLVKNSDDPAACKKLLDKVGLEGYQIGKTKVFLRAGQMADLDTRRTEVLGRSASIIQRKVRSYLAKKSFIVLRNSAKQIQSVCRGYLARSVYEGMRREAAALKIQRDLRRFLARKAYTELYSAAVSVQAGMRGMVARKELCFRRQTKAAIIIQTWCRGYLARLHYRKLKKAAITTQCAWRSKVARGELRKLKMAARETGALQAAKNKLEKQVEELTWRLQLEKRIRTDLEEAKKQESAKAQSSLEELQLKCKETEALLIKEREAAKKIAETAPIIKEIPVVDQELMDKITNENEKLKSMVSSLEMKIGETEKKLQETTKISQDRLNQALEAESKLVKLKTAMQRLEEKILDMEAEKKIMHQQTISTPVRTNLGHPPTAPVKNLENGHQTNLEKEFNEAEFTTPVDGKAGKSAAERQIMNVDALIDCVKDNIGFSNGKPVAAFTIYKCLLHWKCFESEKTNVFDRLIQMIGSAIENEDDNSHLAYWLTSTSALLFLLQKSLKTNGSGATQSKKPPASTSLFGRMAMSFRSSPASGNLAAAAEAAALAVVRPVEAKYPALLFKQQLAAYVEKMFGMVRDNLKRELSTLLSLCIQAPRSSKGGMLRSGRSFGKDSPAVHWQSIIDGLNSLLVTLKENHVPLVLIQKIYSQTFSYINVQLFNSLLLRKECCTFSNGEFVKSGLAELELWCCQAKEYSGPSWEELKHIRQAVGFLVIHQKYRISYDEIANDLCPVLSVQQLYRICTLYWDDSYNTRSVSQEVISSMRTLMTEESNDADSDSFLLDDDSSIPFSIDDISSSMEEKDFVGIKPAEELLENPAFVFLH
Protein: Peptide transporter CstA (Carbon starvation protein A) (P15078)
Organism: Escherichia coli (strain K12)
Function: Involved in peptide utilization during carbon starvation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein YbdD
- Uncharacterized protein YjiX
- Sodium/proline symporter
- Sensor histidine kinase BtsS
Sequence:
MNKSGKYLVWTVLSVMGAFALGYIALNRGEQINALWIVVASVCIYLIAYRFYGLYIAKNVLAVDPTRMTPAVRHNDGLDYVPTDKKVLFGHHFAAIAGAGPLVGPVLAAQMGYLPGMIWLLAGVVLAGAVQDFMVLFVSTRRDGRSLGELVKEEMGPTAGVIALVACFMIMVIILAVLAMIVVKALTHSPWGTYTVAFTIPLALFMGIYLRYLRPGRIGEVSVIGLVFLIFAIISGGWVAESPTWAPYFDFTGVQLTWMLVGYGFVAAVLPVWLLLAPRDYLSTFLKIGTIVGLAVGILIMRPTLTMPALTKFVDGTGPVWTGNLFPFLFITIACGAVSGFHALISSGTTPKMLANEGQACFIGYGGMLMESFVAIMALVSACIIDPGVYFAMNSPMAVLAPAGTADVVASAAQVVSSWGFSITPDTLNQIASEVGEQSIISRAGGAPTLAVGMAYILHGALGGMMDVAFWYHFAILFEALFILTAVDAGTRAARFMLQDLLGVVSPGLKRTDSLPANLLATALCVLAWGYFLHQGVVDPLGGINTLWPLFGIANQMLAGMALMLCAVVLFKMKRQRYAWVALVPTAWLLICTLTAGWQKAFSPDAKVGFLAIANKFQAMIDSGNIPSQYTESQLAQLVFNNRLDAGLTIFFMVVVVVLALFSIKTALAALKDPKPTAKETPYEPMPENVEEIVAQAKGAH
Protein: Staphylococcal nuclease domain-containing protein 1 (EC 3.1.31.1) (100 kDa coactivator) (EBNA2 coactivator p100) (Tudor domain-containing protein 11) (p100 co-activator) (Q7KZF4)
Organism: Homo sapiens (Human)
Function: Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs. As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition. Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for STAT5 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:17081065}. Nucleus {ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:7651391}. Melanosome {ECO:0000269|PubMed:17081065}. Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus (PubMed:12234934). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:17081065}.
Interaction partners:
- Protein LYRIC
- Fragile X messenger ribonucleoprotein 1
- Piwi-like protein 1
- Protein argonaute-2
- Signal transducer and activator of transcription 6
- RNA-binding protein FXR1
- Ras GTPase-activating protein-binding protein 1
- Piwi-like protein 4
- Signal transducer and activator of transcription 5A
- Signal transducer and activator of transcription 5B
Sequence:
MASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTRVLPAQATEYAFAFIQVPQDDDARTDAVDSVVRDIQNTQCLLNVEHLSAGCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR
Protein: Somatic embryogenesis receptor kinase 2 (AtSERK2) (EC 2.7.11.1) (Somatic embryogenesis receptor-like kinase 2) (Q9XIC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-kinase involved in brassinosteroid-dependent and -independent signaling pathways. Acts redundantly with SERK1 as a control point for sporophytic development controlling male gametophyte production. Serves as coreceptor to small peptide (e.g. RGF1 and CLE44) signaling (Probable). Involved in the perception of phytosulfokine and subsequent signal transduction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16284305}; Single-pass type I membrane protein {ECO:0000269|PubMed:16284305}.
Interaction partners:
- Leucine-rich repeat receptor-like protein kinase TDR
- CLAVATA3/ESR
- CLAVATA3/ESR
- Probable inactive receptor kinase At1g27190
- Protein TAPETUM DETERMINANT 1
- Phytosulfokine receptor 1
Sequence:
MGRKKFEAFGFVCLISLLLLFNSLWLASSNMEGDALHSLRANLVDPNNVLQSWDPTLVNPCTWFHVTCNNENSVIRVDLGNADLSGQLVPQLGQLKNLQYLELYSNNITGPVPSDLGNLTNLVSLDLYLNSFTGPIPDSLGKLFKLRFLRLNNNSLTGPIPMSLTNIMTLQVLDLSNNRLSGSVPDNGSFSLFTPISFANNLDLCGPVTSRPCPGSPPFSPPPPFIPPPIVPTPGGYSATGAIAGGVAAGAALLFAAPALAFAWWRRRKPQEFFFDVPAEEDPEVHLGQLKRFSLRELQVATDSFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPPSQLPLAWSIRQQIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLARLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEMLVDPDLQSNYTEAEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAEKWDEWQKVEVLRQEVELSSHPTSDWILDSTDNLHAMELSGPR
Protein: Cysteine proteinase inhibitor 1 (KCPI1) (Phytocystatin) (allergen Act d 4) (Q6TPK4)
Organism: Actinidia deliciosa (Kiwi)
Function: Specific inhibitor of papain family cysteine proteinases. Inhibits papain, chymopapain, bromelain, ficin, human cathepsins B, H and L, actinidain and house dustmite endopeptidase 1, but does not inhibit human bleomycin hydrolase. Inhibits papain with an IC(50) of 2.47 nM. Does not inhibit cysteine proteinases belonging to other families including clostripain, streptopain and calpain.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01035}.
Interaction partners:
Sequence:
MVPKPLSLLLFLLLALSAAVVGGRKLVAAGGWRPIESLNSAEVQDVAQFAVSEHNKQANDELQYQSVVRGYTQVVAGTNYRLVIAAKDGAVVGNYEAVVWDKPWMHFRNLTSFRKV
Protein: Immediate early response 3-interacting protein 1 (Q9Y5U9)
Organism: Homo sapiens (Human)
Function: Regulator of endoplasmic reticulum secretion that acts as a key determinant of brain size. Required for secretion of extracellular matrix proteins. Required for correct brain development by depositing sufficient extracellular matrix proteins for tissue integrity and the proliferation of neural progenitors. Acts as a regulator of the unfolded protein response (UPR) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15276200, ECO:0000305|PubMed:33122427}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein YIPF5
- Protein YIPF6
Sequence:
MAFTLYSLLQAALLCVNAIAVLHEERFLKNIGWGTDQGIGGFGEEPGIKSQLMNLIRSVRTVMRVPLIIVNSIAIVLLLLFG