wanglab/gogpt-training-data huggingface dataset:
Protein: Cardiolipin-specific deacylase 1, mitochondrial (EC 3.5.1.-) (P53264)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin (CL). Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin. Has a strong substrate preference for palmitic acid residues and generates monolysocardiolipin (MLCL) for TAZ1-dependent reacylation with unsaturated fatty acids. The hydrolytic selectivity of the enzyme toward C16-CL substrates contributes to the preservation of C18:1-containing CL species. Has high specificity towards peroxidized cardiolipids CL(OX). Required to mitigate oxidative stress by removing CL(OX).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19244244}. Mitochondrion inner membrane {ECO:0000269|PubMed:23637464}; Peripheral membrane protein {ECO:0000269|PubMed:23637464}; Matrix side {ECO:0000269|PubMed:23637464}.
Interaction partners:
- Cardiolipin synthase
- Tafazzin
- Phosphatidylglycerophosphatase GEP4, mitochondrial
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidate cytidylyltransferase, mitochondrial
- Protein UPS1, mitochondrial
Sequence:
MFKSTLNSIIRRPLKGFQLLRGADSSNTRPQSPRASARDVTEKQILRTPSAPTAIPLREIIYRVPSLFPRPLEDSVKDFRDFIKNEDAFQTELLKTLPFYPTPSESKTARLIRTVVDDEGNYINEFCIRPRKTSVPEADLKHLVFIHGYGAGLGFFIKNFEDIPLLDNEWCIHAIDLPGYGFSSRPKFPFEYPRDNIHSVQDWFHERIHTWFSKRNLLNRPEKNIVMAHSLGSYLMALYLQKYKESPSFKKLILCSPAGVSYRDFNNTASEVEKWKPPPWWYVKLWDRNISPFTLVRNFRQLGSKITSGWSYRRFKHILNGDPEQSKRFEALHRYAYAIFNKRGSGEYLLSFALKCGGEPRLSLEQQLFDGKKSDILKNSNCDWLWLYGDDDWMDVNGGLRVSRFLKEKLKQKSNVIIVPHSGHHLYLDNYKFFNNILTKEMQKI
Protein: Aminopyrrolnitrin oxidase PrnD (Q4KAM4)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Interaction partners:
- Halogenase PrnC
- Halogenase PltM
- Putative halogenase PltD
- Flavin reductase-like protein
- Tryptophan halogenase PrnA
- Pyrrolnitrin biosynthesis enzyme PrnB
Sequence:
MNNIQLDQANVKKHPPGAYDATTRVAASWYVAMRSNGLRDKPKELTLFGRPYVAWRAATGQAVVMDRHCSHLGANLADGRIKDGCIQCPFHHWRYDEQGKCVHIPGHSEVVRQLEPVPRAARQPTLVTTERYGYVWVWYGSPQPLHPLPEITAADVDNGDFMHLHFAFETTTAVLRIVENFYDAQHATPVHALPISAFELKLFDDWSRWPEVESLARAGAWFGAGIDFHVNRYFGPLGMLSRALGLNMSQMNLHFDGYPGGCVMTVALDADVKYKLLQCVTPVSDGKNIMHMLISIKKVGGVLRRATDFVLFGLQTRQAAGYDVKIWNGMKPDGGGAYSKYDKLVLKYRAFYRGWVDRVASEQ
Protein: Interleukin-1 beta (Q9YGD3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P01584}. Secreted {ECO:0000250|UniProtKB:P01584}. Lysosome {ECO:0000250|UniProtKB:P01584}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10749}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. {ECO:0000250|UniProtKB:P01584}.
Interaction partners:
Sequence:
MDFESNYSLIKNTSESAAWSSKLPQGLDLEVSHHPITMRHIANLIIAMERLKGGEGVTMGTEFKDKDLLNFLLESAVEEHIVLELESAPPASRRAAGFSSTSQYECSVTDSENKCWVLMNEAMELHAMMLQGGSSYHKVHLNLSSYVTPVPIETEARPVALGIKGSNLYLSCSKSGGRPTLHLEEVADKDQLKSISQQSDMVRFLFYRRNTGVDISTLESASFRNWFISTDMQQDYTKPVDMCQKAAPNRLTTFTIQRHN
Protein: Chromatin modification-related protein (A0A1D8PIP3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU361213}.
Interaction partners:
- Ume1p
- Chromatin modification-related protein EAF3
- Chromatin modification-related protein EAF6
- Enhancer of polycomb-like protein 1
- Histone acetyltransferase
- SWR1-complex protein 4
- Histone acetyltransferase ESA1
- Actin-related protein 4
- Protein AF-9 homolog
- Chromatin modification-related protein EAF1
Sequence:
MRTKQQQQQQQQSNSSSGVANNQKSYGYTTRIKSNSSVTNGGNVGATLTESRIITNINELLPGLNDISDAFEALPIDLIRYFTLLKEIDAKCINTIPQINHLINQYITNLHQDKNVTTTTTTTTNDDNTIDLNKKLETRRLNLIKNKINEVIPCLEEKMHVTSVASDLLKKHMYRINQDYKLILLNNEIPQSIRIGPLNHPAMINDTHTTSSSSTTSTGNGTGGGGGTNNNHGGNNSVQSQRSESRREALAARKANKEDDRENNTATGGSGRKKKKEQNNNNNSTASGADGNNGSNGKKRNRDDKSNNTGSGNDLKKKKKSNNNDQSDNRRRGEDENGKGDGETSFNSGNAKNDPHGKLKTTTTGNLVGGSSTTTTVSSSSTTSSSATTTTTSSTTTTKNSGSTGASTATATGASGAKGSSSSSSGNNEPTYCYCNQVSFGEMVGCDGDDCKREWFHLPCIGFKNPPKGKWYCDDCLKKLK
Protein: Phosphorylated adapter RNA export protein (26 kDa resiniferatoxin-binding protein) (RBP-26) (RNA U small nuclear RNA export adapter protein) (RTX-42) (Resiniferatoxin-binding protein 2) (RBP-2) (Q63068)
Organism: Rattus norvegicus (Rat)
Function: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner. Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H814}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H814}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9H814}. Cytoplasm {ECO:0000250|UniProtKB:Q9H814}. Note=Shuttles between the nucleus and the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies. {ECO:0000250|UniProtKB:Q9H814}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran, testis-specific isoform
- Nuclear cap-binding protein subunit 1
- Exportin-1
- Arsenite-resistance protein 2
- Nucleolar and coiled-body phosphoprotein 1
Sequence:
MALEAGDMEEGQLSDSDSDMTVVPSDRPLQMAKVLGGGGAACAPVSNYRTVKHVDSSEESLDSDDDCSLWKRKRQKCHSPPPKPEPFPFGQSGQKPALNGGKKVNNIWGAVLQEQNQDAVATELGILGMEGTIDRSRQSETYNYLLAKKLAKKESQEYTKELDKDLDEYMHGDKKPGSKEEENGQGHLKRKRPVRDRLGNRVEMNYKGRYDITEEDSPEKVADEIAFRLQEPKKDLIARVVTILGNKKAIELLMETAEVEQNGGLFIMNGSRRRTPGGVFLNLLKNTPSISEEQIKDIFYIENQKEYENKKAARKRRTQLLGKKMKEAIKSLNFQEDDDTSRETFASDTNEALASLDEAQEGPGETKLDAEDAIEVDHPQDLDIF
Protein: Zinc finger protein 138 (P52744)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation as a repressor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MKRHEMVVAKHSALCSRFAQDLWLEQNIKDSFQKVTLSRYGKYGHKNLQLRKGCKSVDECKGHQGGFNGLNQCLKITTSKIFQCNKYVKVMHKFSNSNRHKIRHTENKHFRCKECDKSLCMLSRLTQHKKIHTRENFYKCEECGKTFNWSTNLSKPKKIHTGEKPYKCEVCGKAFHQSSILTKHKIIRTGEKPYKCAHCGKAFKQSSHLTRHKIIHTEEKPYKCEQCGKVFKQSPTLTKHQIIYTGEEPYKCEECGKAFNLS
Protein: Mitogen-activated protein kinase FUS3 (MAP kinase FUS3) (EC 2.7.11.24) (P16892)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Together with closely related KSS1, FUS3 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12.
Subcellular location: Nucleus {ECO:0000269|PubMed:11781566}. Cytoplasm {ECO:0000269|PubMed:11781566}. Periplasm {ECO:0000269|PubMed:11781566}. Note=FUS3 shuttles rapidly between the cytoplasm and the nucleus independent of pheromone treatment or FUS3 phosphorylation level. Activated FUS3 translocates rapidly to the nucleus.
Interaction partners:
- Cyclin-dependent kinase inhibitor FAR1
- Tyrosine-protein phosphatase MSG5
- Protein STE5
- Serine/threonine-protein kinase STE7
- Protein STE12
- Down-regulator of invasive growth 1
- Guanine nucleotide-binding protein alpha-1 subunit
- Down-regulator of invasive growth 2
- Guanine nucleotide-binding protein subunit beta
- Mitochondrial import inner membrane translocase subunit TIM12
Sequence:
MPKRIVYNISSDFQLKSLLGEGAYGVVCSATHKPTGEIVAIKKIEPFDKPLFALRTLREIKILKHFKHENIITIFNIQRPDSFENFNEVYIIQELMQTDLHRVISTQMLSDDHIQYFIYQTLRAVKVLHGSNVIHRDLKPSNLLINSNCDLKVCDFGLARIIDESAADNSEPTGQQSGMTEYVATRWYRAPEVMLTSAKYSRAMDVWSCGCILAELFLRRPIFPGRDYRHQLLLIFGIIGTPHSDNDLRCIESPRAREYIKSLPMYPAAPLEKMFPRVNPKGIDLLQRMLVFDPAKRITAKEALEHPYLQTYHDPNDEPEGEPIPPSFFEFDHYKEALTTKDLKKLIWNEIFS
Protein: PDZ domain containing 7 (A0A2R8YFN1)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MAQGFAVGFDPLGLGDLSSGSLSSLSSRGHLGSDSGSTATRYLLRKQQRLLNGPPRGIRASSPMGRVILINSPIEANSDESDIIHSVRVEKSPAGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVKVLTSSSRLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCGSTPSDTSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSCASSAPYSSGSLPSDRMDICLGQEEPGSRGPGWGRADTAMQTEPDAGGRVETWCSVRPTVILRDTAIRSDGPHPGRRLDSALSESPKTALLLALSRPRPPITRSQSYLTLWEEKQQRKKEKSGSPGEKGALQRSKTLMNLFFKGGRQGRLARDGRREAWTLDSGSLAKTYPRLDIEKDGVLLLLPRRECNGTISAHCDLRLPRSSDPPTSASQSAGMTRVHHHAQLIFLHLFVEMGVSPCCPG
Protein: Enoyl-CoA hydratase/isomerase family protein (P71851)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MPITSTTPEPGIVAVTVDYPPVNAIPSKAWFDLADAVTAAGANSDTRAVILRAEGRGFNAGVDIKEMQRTEGFTALIDANRGCFAAFRAVYECAVPVIAAVNGFCVGGGIGLVGNSDVIVASEDATFGLPEVERGALGAATHLSRLVPQHLMRRLFFTAATVDAATLQHFGSVHEVVSRDQLDEAALRVARDIAAKDTRVIRAAKEALNFIDVQRVNASYRMEQGFTFELNLAGVADEHRDAFVKKS
Protein: SH3 and multiple ankyrin repeat domains 1 (H9KV90)
Organism: Homo sapiens (Human)
Subcellular location: Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MTHSPATSEDEERHSASECPEGGSESDSSPDGPGRGPRGTRGQGSGAPGSLASVRGLQGRSMSVPDDAHFSMMVFRIGIPDLHQTKCLRFNPDATIWTAKQQVLCALSESLQDVLNYGLFQPATSGRDANFLEEERLLREYPQSFEKGVPYLEFRYKTRVYKQTNLDEKQLAKLHTKTGLKKFLEYVQLGTSDKVARLLDKGLDPNYHDSDSGETPLTLAAQTEGSVEVIRTLCLGGAHIDFRARDGMTALHKAACARHCLALTALLDLGGSPNYKDRRGLTPLFHTAMVGGDPRCCELLLFNRAQLGIADENGWQEIHQACQRGHSQHLEHLLFYGAEPGAQNASGNTALHICALYNKETCARILLYRGADKDVKNNNGQTPFQVAVIAGNFELGELIRNHREQDVVPFQESPKYAARRRGPPGTGLTVPPALLRANSDTSMALPDWMVFSAPGAASSGAPGPTSGSQGQSQPSAPTTKLSSGTLRSASSPRGARARSPSRGRHPEDAKRQPRGRPSSSGTPREGPAGGTGGSGGPGGSLGSRGRRRKLYSAVPGRSFMAVKSYQAQAEGEISLSKGEKIKVLSIGEGGFWEGQVKGRVGWFPSDCLEEVANRSQESKQESRSDKAKRLFRHYTVGSYDSFDAPSLMDGIGPGSDYIIKEKTVLLQKKDSEGFGFVLRGAKAQTPIEEFTPTPAFPALQYLESVDEGGVAWRAGLRMGDFLIEVNGQNVVKVGHRQVVNMIRQGGNTLMVKVVMVTRHPDMDEAVHKKAPQQAKRLPPPTISLRSKSMTSELEEMVSPWKKKSEYEQQPAPVPSMEKKRTVYQMALNKLDEILAAAQQTISASESPGPGGLASLGKHRPKGFFATESSFDPHHRAQPSYERPSFLPPGPGLMLRQKSIGAAEDDRPYLAPPAMKFSRSLSVPGSEDIPPPPTTSPPEPPYSTPPVPSSSGRLTPSPRGGPFNPGSGGPLPASSPASFDGPSPPDTRVGSREKSLYHSGPLPPAHHHPPHHHHHHAPPPQPHHHHAHPPHPPEMETGGSPDDPPPRLALGPQPSLRGWRGGGPSPTPGAPSPSHHGSAGGGGGSSQGPALRYFQLPPRAASAAMYVPARSGRGRKGPLVKQTKVEGEPQKGGGLPPAPSPTSPASPQPPPAVAAPSEKNSIPIPTIIIKAPSTSSSGRSSQGSSTEAEPPTQPEPTGGGGGGGSSPSPAPAMSPVPPSPSPVPTPASPSGPATLDFTSQFGAALVGAARREGGWQNEARRRSTLFLSTDAGDEDGGDGGLGTGAAPGPRLRHSKSIDEGMFSAEPYLRLESAGSGAGYGGYGAGSRAYGGGGGSSAFTSFLPPRPLVHPLTGKALDPASPLGLALAARERALKESSEGGGAPQPPPRPPSPRYEAPPPTPHHHSPHAHHEPVLRLWGASPPDPARRELGYRAGLGSQEKSLPASPPAARRSLLHRLPPTAPGVGPLLLQLGTEPPAPHPGVSKPWRSAAPEEPERLPLHVRFLENCQPRAPVTSGRGPPSEDGPGVPPPSPRRSVPPSPTSPRASEENGLPLLVLPPPAPSVDVEDGEFLFVEPLPPPLEFSNSFEKPESPLTPGPPHPLPDTPAPATPLPPVPPPAVAAAPPTLDSTASSLTSYDSEVATLTQGASAAPGDPHPPGPPAPAAPAPAAPQPGPDPPPGTDSGIEEVDSRSSSDHPLETISSASTLSSLSAEGGGSAGGGGGAGAGVASGPELLDTYVAYLDGQAFGGSSTPGPPYPPQLMTPSKLRGRALGASGGLRPGPSGGLRDPVTPTSPTVSVTGAGTDGLLALRACSGPPTAGVAGGPVAVEPEVPPVPLPTASSLPRKLLPWEEGPGPPPPPLPGPLAQPQASALATVKASIISELSSKLQQFGGSSAAGGALPWARGGSGGGGDSHHGGASYVPERTSSLQRQRLSDDSQSSLLSKPVSSLFQNWPKPPLPPLPTGTGVSPTAAAAPGATSPSASSSSTSTRHLQGVEFEMRPPLLRRAPSPSLLPASEHKVSPAPRPSSLPILPSGPLYPGLFDIRGSPTGGAGGSADPFAPVFVPPHPGISGGLGGALSGASRSLSPTRLLSLPPDKPFGAKPLGFWTKFDVADWLEWLGLAEHRAQFLDHEIDGSHLPALTKEDYVDLGVTRVGHRMNIDRALKFFLER
Protein: Wilms tumor protein homolog B (XWT1b) (XeWT1) (P79958)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor required for development of the vascular component of the pronephric kidney, the glomus; may repress tubule-specific gene expression in the portion of the pronephros fated to form the glomus. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' (By similarity). Inhibits Wnt-signaling during embryonic development (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P22561}. Cytoplasm {ECO:0000250|UniProtKB:P22561}. Nucleus speckle {ECO:0000250|UniProtKB:P22561}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250|UniProtKB:P22561}.
Interaction partners:
Sequence:
MGSDVRDMNLLPPVSSLSGNSSCNMPVSNSSQWAPVLDFPPGAPYSSLTPHSFIKQEPTWNPDPHEDQCLSAFTVHFSGQFTGTAGACRYGPFGAPTPSQATTGQARMFPNAPYLSNCLDNQQSMRNQGYSAVAFDGTPSYGHTPSHHTAQFTNHSFKHEDPISQQTSLGEQQYSVPPPVYGCHTPTDTCTGSQALLLRTPYNSDNLYQMECMTWNQMNLGSSLKSHGTTYENDSHSAPMLYSCGGQYRIHTHGVFRGIQDVRRVPGVTPAIVRSTEANEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL
Protein: Olfactory receptor 2AG1 (HT3) (Olfactory receptor 2AG3) (Olfactory receptor OR11-79) (Q9H205)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Olfactory receptor 6A2
- Activin receptor type-1-like
- Olfactory receptor 2D2
- Endoglin
Sequence:
MELWNFTLGSGFILVGILNDSGSPELLCATITILYLLALISNGLLLLAITMEARLHMPMYLLLGQLSLMDLLFTSVVTPKALADFLRRENTISFGGCALQMFLALTMGGAEDLLLAFMAYDRYVAICHPLTYMTLMSSRACWLMVATSWILASLSALIYTVYTMHYPFCRAQEIRHLLCEIPHLLKVACADTSRYELMVYVMGVTFLIPSLAAILASYTQILLTVLHMPSNEGRKKALVTCSSHLTVVGMFYGAATFMYVLPSSFHSTRQDNIISVFYTIVTPALNPLIYSLRNKEVMRALRRVLGKYMLPAHSTL
Protein: Myelin P2 protein (P24526)
Organism: Mus musculus (Mouse)
Function: May play a role in lipid transport protein in Schwann cells. May bind cholesterol (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Myelin protein P0
Sequence:
MSNKFLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAKSIVTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEKV
Protein: Serine/arginine-rich splicing factor RS40 (At-RSp40) (AtRS40) (P92965)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for constitutive and alternative pre-mRNA splicing (Probable). Involved in primary miRNA processing and pri-miRNA biogenesis. Binds both intronless and intron-containing pri-miRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:24146632, ECO:0000269|PubMed:26227967}. Nucleus speckle {ECO:0000269|PubMed:15133128, ECO:0000269|PubMed:19245862, ECO:0000269|PubMed:24146632, ECO:0000269|PubMed:26227967}.
Interaction partners:
- Serine/arginine-rich splicing factor SC35
- Serine/arginine-rich SC35-like splicing factor SCL30A
- RNA-binding motif protein 25
- Nuclear protein-like
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 1
- Serine/arginine-rich splicing factor RSZ22A
- Splicing factor U2af large subunit A
- RNA-binding KH domain-containing protein RCF3
- RNA polymerase II C-terminal domain phosphatase-like 1
Sequence:
MKPVFCGNFEYDAREGDLERLFRKYGKVERVDMKAGFAFVYMEDERDAEDAIRALDRFEFGRKGRRLRVEWTKSERGGDKRSGGGSRRSSSSMRPSKTLFVINFDADNTRTRDLEKHFEPYGKIVNVRIRRNFAFIQYEAQEDATRALDASNNSKLMDKVISVEYAVKDDDARGNGHSPERRRDRSPERRRRSPSPYKRERGSPDYGRGASPVAAYRKERTSPDYGRRRSPSPYKKSRRGSPEYGRDRRGNDSPRRRERVASPTKYSRSPNNKRERMSPNHSPFKKESPRNGVGEVESPIERRERSRSSPENGQVESPGSIGRRDSDGGYDGAESPMQKSRSPRSPPADE
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (B3IWJ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MALCGTTASNAAKMMAAYNGGTAAVAAHHPHHHHQLPHLPPPAHLHHHHHHQHSHHLQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGARAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCYTTSSGRVYTSDFEPVTNPKFDDGFEKNLTSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE
Protein: Transcription factor-like protein DPB (DP-like protein B) (AtDPbB) (E2F dimerization partner protein B) (Q9FNY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of the G1/S transition. Increases the DNA binding activity of E2F proteins after heterodimerization. The complex DPB/E2FC restricts cell division and lateral root initiation and may function as a negative regulator of E2F-regulated genes. The interaction with SKP2A is controlled by auxin.
Subcellular location: Nucleus {ECO:0000269|PubMed:11891240}. Cytoplasm {ECO:0000269|PubMed:11891240}.
Interaction partners:
- Transcription factor E2FC
- Transcription factor E2FB
- Retinoblastoma-related protein 1
- Transcription factor E2FA
- Protein ALWAYS EARLY 1
- Protein ALWAYS EARLY 3
- Protein ALWAYS EARLY 2
- Histone-binding protein MSI1
- F-box protein SKP2A
- At2g40630/T2P4.2
Sequence:
MTTTGSNSNHNHHESNNNNNNPSTRSWGTAVSGQSVSTSGSMGSPSSRSEQTITVVTSTSDTTFQRLNNLDIQGDDAGSQGASGVKKKKRGQRAAGPDKTGRGLRQFSMKVCEKVESKGRTTYNEVADELVAEFALPNNDGTSPDQQQYDEKNIRRRVYDALNVLMAMDIISKDKKEIQWRGLPRTSLSDIEELKNERLSLRNRIEKKTAYSQELEEQYVGLQNLIQRNEHLYSSGNAPSGGVALPFILVQTRPHATVEVEISEDMQLVHFDFNSTPFELHDDNFVLKTMKFCDQPPQQPNGRNNSQLVCHNFTPENPNKGPSTGPTPQLDMYETHLQSQQHQQHSQLQIIPMPETNNVTSSADTAPVKSPSLPGIMNSSMKPEN
Protein: Protein-glutamine deamidase Cif (EC 3.5.1.44) (Cycle-inhibiting factor homolog) (CHYP) (A0A0H3B1Q8)
Organism: Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
Function: Protein-glutamine deamidase effector that inhibits the host cell cycle and other key cellular processes such as the actin network and programmed-cell death. Acts by mediating the side chain deamidation of 'Gln-40' of host NEDD8, converting it to glutamate, thereby abolishing the activity of cullin-RING-based E3 ubiquitin-protein ligase complexes (CRL complexes). Inactivation of CRL complexes prevents ubiquitination and subsequent degradation of the cyclin-dependent kinase inhibitors CDKN1A/p21 and CDKN1B/p27, leading to G1 and G2 cell cycle arrests in host cells. Also able to catalyze deamidation of 'Gln-40' of host ubiquitin in vitro; however, NEDD8 constitutes the preferred substrate in vivo (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0DUW5}. Host nucleus {ECO:0000250|UniProtKB:P0DUW5}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:P0DUW5}.
Interaction partners:
Sequence:
MKISPNTISPSQSDPRMSTNVSQRSRVSGIGVPVSHSINNPSIQHVQDFATLSARSLRANVLLNSDDHSVPIHAKNPSELLEAIDNNISQTAQDWGVSIQEVEVILGSSKRIIEPVCGVTANTIMKLFLDNDIFSYSFEKGQSLSLSQLQERLASLPAHKNFILRVNDGGLGHAYVIDFPATTNPSRDAFLYQSDLGEGVTREVRFEDWMTQKASHPISLDDINTHFIGIAQDQIDLAHIAKLFDVDGNVKMLRADHLISHKTSEFNFQLFEYDLKNLENNMSIIKTHCN
Protein: Calcium release-activated calcium channel protein 1 (Protein orai) (Q9U6B8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores. Regulates transcription factor NFAT nuclear import.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Stromal interaction molecule homolog
- Inositol 1,4,5-trisphosphate receptor
- Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type
- Nuclear factor of activated T-cells 5
- Tropomyosin-1, isoforms 9A/A/B
- Calmodulin
- Tropomyosin-2
- GEO12020p1
- EF-hand domain-containing protein
- Calmodulin-related protein 97A
Sequence:
MSVWTTANNSGLETPTKSPITSSVPRAARSSAVITTGNHQQHHFQHVVAAAVAAATSVATGHQFQQQFPLHAHPHPQHHSNSPTGSGSNSNNSAGFQRTSISNSLLQFPPPPPPSSQNQAKPRGHHRTASSSMSQSGEDLHSPTYLSWRKLQLSRAKLKASSKTSALLSGFAMVAMVEVQLDHDTNVPPGMLIAFAICTTLLVAVHMLALMISTCILPNIETVCNLHSISLVHESPHERLHWYIETAWAFSTLLGLILFLLEIAILCWVKFYDLSPPAAWSACVVLIPVMIIFMAFAIHFYRSLVSHKYEVTVSGIRELEMLKEQMEQDHLEHHNNIRNNGMNYGASGDIV
Protein: Caveolae-associated protein 2 (Cavin-2) (PS-p68) (Phosphatidylserine-binding protein) (Serum deprivation-response protein) (O95810)
Organism: Homo sapiens (Human)
Function: Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae. Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10191091, ECO:0000269|PubMed:2390065}. Membrane, caveola {ECO:0000269|PubMed:19262564, ECO:0000269|PubMed:19525939}. Note=Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000269|PubMed:19262564}.
Interaction partners:
- Caveolin-1
- Caveolae-associated protein 4
- Caveolae-associated protein 3
- Caveolae-associated protein 1
Sequence:
MGEDAAQAEKFQHPGSDMRQEKPSSPSPMPSSTPSPSLNLGNTEEAIRDNSQVNAVTVLTLLDKLVNMLDAVQENQHKMEQRQISLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRKVSAHTRAVKERMDRQCAQVKRLENNHAQLLRRNHFKVLIFQEENEIPASVFVKQPVSGAVEGKEELPDENKSLEETLHTVDLSSDDDLPHDEEALEDSAEEKVEESRAEKIKRSSLKKVDSLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTSNHQKISSGKSSPFKVSPLTFGRKKVREGESHAENETKSEDLPSSEQMPNDQEEESFAEGHSEASLASALVEGEIAEEAAEKATSRGSNSGMDSNIDLTIVEDEEEESVALEQAQKVRYEGSYALTSEEAERSDGDPVQPAVLQVHQTS
Protein: Non-specific lipid-transfer protein (Q9FVA5)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MASSMSLKLACVVVLCMVVGAPLAQGAVTCGQVTNSLAPCINYLRGSGAGAVPPGCCSGIKSLNSAAQTTPDRQAACRCIKSAAAGITGINFGLASGLPGKCGVNIPYKISPSTDCNSVK