lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAAMAVGAAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFTQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENVPTTHTQEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPDEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL
The following text describes a protein:
Function:
Functions as a zinc transporter transporting Zn(2+) from the Golgi apparatus to the cytosol and thus influences the zinc level at least in areas of the cytosol. May regulate beige adipocyte differentiation.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MGRACRWLKGTQPAPHPVIKESLALGGQADTKSGTGSQGKKKVWSLEVGCGGAEPHCSVHPSQGSLEALGEAGRRAGAVAAGSAGRVQVPRFLSRCAAKGGRSRKRPLCVFSARGMPGCPCPGIGMAGQRLLFLAALALELLGGAGGSQQALRSRGVAAACRLDSKESESWGALLSGERLETWICSLLGSLMVGLSGVFPLLVIPLEMGTTLRSEAGARRLKQLLSFALGGLLGNVFLHLLPEAWAYTNSASSGGERQSLQQQQQLGLWVIAGFLTFLVLEKLFFDSKGKEETSQAPSKDPAAAAALNGGHYLAQPAAEPGPSAVVRNIKVSGYLNLLANTIDNFTHGLAVAASFLVSKKIGLLTTMAILLHEIPHEVGDFAILLRAGFDRWSAAKLQLSTALGGLLGACFAICAQSPKGVGTGVGVVAVRRGALAEGHGRPDPGIRARLCSGPPRGMGGGRYTWPPSPPQPVRAPPPATEETVAWILPFTSGGFLYIALVNVLPDLLEEDDPWRSLQQVLLLCAGIVVMVLFSVFVE
The following text describes a protein:
Function:
Component of the ESCRT-I complex (endosomal sorting complex required for transport I), a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs).
Subcellular Localization:
Endosome.
Sequence:
MFKFWGNQEQQEQARPQDVNPAQSWYPPSVVTSPSSSRPATPTSSSSSSHSLQRPTERPLSPSPAEAAAIITLLKDKSVDELRKLLSDKDAYHQFLLSLDQVKIQNNIRDELCKETLQLARENLEKEPRIMELRNQCRIIRTTELAAAQEKLNELEKQKEELLRSCSPASILQRLQEAMNKTEEESDAFHRQFLEKEMDLGAFVQKYKKLRTTYHKRALIHLAAKASPTG
The following text describes a protein:
Function:
Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Note=Associates loosely with the inner membrane.
Sequence:
MPNSQTSNSQPQVSEKDVDTGFRKGDDTFTHWRNVFNILTGRMTDEGIEQFRVARDLRNEAADCKRCEDQRDYLLQWSPIIRYMSDSIRQLGGDLSSHNIYCRRCTNRKAGGFDPEYGILICANEMKDQGHLEDTMAHEMVHAYDHLRFKVDWTNNLRHAACTEIRASSLSGECRWAREFFRRGQWKLTQQHQECVRRRAVLSVMARPGCQDKGHAEKVVNEVWDSCFRDTRPFDEIFR
The following text describes a protein:
Function:
Acts as a negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue. Dephosphorylates ZAP70 at its activating 'Tyr-493' residue. Dephosphorylates the immune system activator SKAP2. Positively regulates toll-like receptor (TLR)-induced type 1 interferon production. Promotes host antiviral responses mediated by type 1 interferon (By similarity). Regulates NOD2-induced pro-inflammatory cytokine secretion and autophagy. Acts as an activator of NLRP3 inflammasome assembly by mediating dephosphorylation of 'Tyr-861' of NLRP3. Dephosphorylates phospho-anandamide (p-AEA), an endocannabinoid to anandamide (also called N-arachidonoylethanolamide) (By similarity).
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Due to intron retention; MISCELLANEOUS: [Isoform 6]: Lacks most of the phosphatase domain and functions as a dominant negative isoform of the full length PTPN22.
Subcellular Localization:
Cytoplasm.
Sequence:
MDQREILQKFLDEAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFKRQMDVIRDKHSGTESQAKHCIPEKNHTLQADSYSPNLPKSTTKAAKMMNQQRTKMEIKESSSFDFRTSEISAKEELVLHPAKSSTSFDFLELNYSFDKNADTTMKWQTKAFPIVGEPLQKHQSLDLGSLLFEGCSNSKPVNAAGRYFNSKVPITRTKSTPFELIQQRETKEVDSKENFSYLESQPHDSCFVEMQAQKVMHVSSAELNYSLPYDSKHQIRNASNVKHHDSSALGVYSYIPLVENPYFSSWPPSGTSSKMSLDLPEKQDGTVFPSSLLPTSSTSLFSYYNSHDSLSLNSPTNISSLLNQESAVLATAPRIDDEIPPPLPVRTPESFIVVEEAGEFSPNVPKSLSSAVKVKIGTSLEWGGTSEPKKFDDSVILRPSKSVKLRSPKSELHQDRSSPPPPLPERTLESFFLADEDCMQAQSIETYSTSYPDTMENSTSSKQTLKTPGKSFTRSKSLKILRNMKKSICNSCPPNKPAESVQSNNSSSFLNFGFANRFSKPKGPRNPPPTWNI
The following text describes a protein:
Function:
Participates in iron-sulfur cluster formation (ISC) pathway for iron-sulfur (Fe-S) cluster biogenesis. Can bind iron and [4Fe-4S] clusters. May function as an iron chaperone.
Subcellular Localization:
Mitochondrion.
Sequence:
MLKFLSTKCKQFNSLNHIIKHKIYFPSKSNKSYFSSSVKDVEKKNKEPIIQLTNDAINKMKEINLKYKNSKALKVCVEAGGCSGFQYSFSLIDKNKIKDKEQIVYDKDCIVVIDKQVIDILKNSKIHYINNLISKKFTIENIQNISSKCSCGNSFDIDFV
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MAIKQNAKKGGKPGKPGGKPPGGGKPAGGKKVFRKIKNGFVEPRKAKAAKGTTVAAMDIVSAADLSASESEDENKLKDFAKFDDDEEEKEDKGGKAEKDVKKDVQKDVKKDVQKDVQKDVKKSVKKDVQKAGKKDTQKDVKKADAKTNSAIEGFAQATKGEEAEVSVPAKEVNKAAKKEDKDVKKDTKTKDTVKTKVKAAVLPESDAEMDNWSDAEFSDGGETIDLPAPGTKPLDINKMNWKKVELGDKKMDFEGFYGLEELDGVDIVVNNGLPTFVVGEKPEKKNSKKETKKAEVKKDKSGDASEPAKKKAKVAKDGKDGKEVAKTQPKQNSKKKAEGNAFEALNSVPDDIHLPDWTLNGEQLNYSLIQGLYALGYKSPTEIQKKSIPPILAGDDVIGKASTGSGKTLAYGLPILHRFLEAEKSDKKEEVEEEVPEKCTTKPRPKKVTKMTGQEEKKDDEEEEERFDMYDEAPEPRFDISDRPADLPVLDKEREDRENEVEMDEETEKVERDMSSVKPPQAIVFAPTRELAHQITDHLNAVSQFCPISGPRVMALTGGLSIMKQRRLMKWNPAIVVATPGRFHEFITDTDGMVDVFKRTKTVVMDEADRMLQDGHYEDLDKALDLIGRGKVAKRQTCVFSATFQKSLMFKLDKKRKQRTGLATDQETIRFLVSKMKFRQFHPTFVDANPAEVVARQVLESIVECGAMEKDQYLYYFLLTYPGKSIIFVNSIDSVKRLTPMLQNLELPAVQLHSNMIQKARMRSLERFRDNKNGILVATDVAARGLDIPNVHHVVHYHLPRTADVYVHRSGRTARAGNEGVSVLLCSPDEASGPLRKLRAALSRDNALAKLKPLSMNYDVLAQIKPRVELAKELADSVLDSTQVGKQDSWLKEAAEDLGVDFSDFENDTHDHKSHVRTKLGNNSKKGMKVMSKDQMARTRKELEKLLSKPLGRHSSKYITSTNGINLAKMVLDGKSHDKIMGVAPQTAGETLRKKRKN
The following text describes a protein:
Function:
Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions. In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MEESSLSRAPSRGGVNFLNVARTYIPNTKVECHYTLPPGTVPSASDWIGIFKVEAACVRDYHTFVWSLVPESVTDGSPIHASVQFQASYLPKPGAQLYQFRYVNRQGRVCGQSPPFQFREPRPMDELVTLEETDGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELKSQVQELEKALAAARQEHAELAEQYKGLSRSHGELTEERDILSRQQGDHVARILELEEDIQTISEKVLMKEVELDRVRDSVKALTREQEKLLGQLKEVQADKEQSEAELQMAQQENRRLNLELQEAKDRQEEQSAQAQRLKDKVAQMKDTLGQVQQRVAELEPLKEQLRGAQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAGVNGRLAELSLHLKEEKSQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEEKTQSQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWSEDPATEDEEAAVGLSCPAALTDSEDESPEDMRLPPYSLCESGDPGSSPATGPREASPLVVISQPAPIAPQLSGPAEDSSSDSEAEDEKSVLMAAVQSGGEEANLLLPELGSAFYDMASTVLCRAQIALHPPSPAPMPSPATSGFAVGPLTEASTGGPATPPWKECPICKERFPAESDKDAMEDHMDGHFFFSTQDPFTFE
The following text describes a protein:
Function:
Negative regulator of the innate immune response. Attenuates signaling pathways activated by Toll-like receptors (TLRs) and the DNA sensor STING/TMEM173 in response to pathogen-associated molecular patterns, such as intracellular poly(dA:dT), but not poly(I:C), or in response to DNA virus infection, including that of Herpes simplex virus 1 (HSV1). May affect TLR4 signaling by acting at the level of TRAF6 ubiquitination, decreasing the activating 'Lys-63'-linked ubiquitination and leaving unchanged the degradative 'Lys-48'-linked ubiquitination. Inhibits the PI3K-AKT-mTOR pathway possibly by directly interacting with the posphatidylinositol 3-kinase regulatory subunit p85 (PIK3R1/PIK3R2) and disrupting the association between PIK3R1/PIK3R2 and the catalytic subunit p110 (PIK3CA/PIK3CB/PIK3CD) and reducing PIK3R1/PIK3R2 activation. Via its regulation of the PI3K-AKT-mTOR pathway, controls cell proliferation, predominantly in intestinal epithelial cells. May also affect NOD1- or NOD2-mediated NF-kappa-B activation (By similarity). Might also affect the inflammatory response by preventing NLRP3 inflammasome formation, CASP1 cleavage and IL1B maturation (By similarity).
Subcellular Localization:
Cytoplasm.
Domain:
The leucine-rich repeat domain may reduce the interaction with TMEM173/STING.
Sequence:
MRRRYSHDPPGSFRETKVFGFRGEYGCKALVDLLAGKGSQLLQVRDKMPDSPLGSQSNESRIPKHSEALLSRVGNDPELGSPSHRLASLMLVEGLTDLQLKEHDFTQVEATRGVWHPARVITLDRLFLPLSRVSIPPRVSLTIGVAGVGKTTLVRHFVHCWARGQVGKGFSRVLPLTFRDLNTYEKLSADRLIQSIFSSIGEASLVATAPDRVLLVLDGLDECKTPLEFSNTMACSDPKKEIQVDHLITNIIRGNLFPEISVWITSRPSAAGQIPGGLVDRMTEIRGLTEEEIKVCLEQMFPEEQNLLGQVLSQVQANRALYLMCTVPAFCRLTGLALGHLYRTRLAVQDIELPLPQTLCELYSWYFRMALGGEGQDKEKVSPRIKQVTQGARKMVGTLGRLAFHGLVKKKYVFYEQDMKAFGVDLALLQNTLCSCLLQREETLASSVAYCFIHLSLQEFVAATYYYSASKRAIFDLFTESGMSWPRLGFLAHFRCAAQRATQAKDGRLDVFLRFLSGLLSPRVNTLLAGSLLSQGEHQSYRDQVAEVLQGFLHPDAAVCARAINVLYCLSELRHTELACSVEEAMRSGTLAGMTSPSHRTALAYLLQMSDICSPEADFSLCLSQHVLQSLLPQLLYCQSLRLDNNQFQDPVMELLGSVLSGKDCRIRKISLAENQIGNKGAKALARSLLVNRSLITLDLRSNSIGPPGAKALADALKINRTLTSLSLQSNVIKDDGVMCVAEALVSNQTISMLQLQKNLIGLIGAQQMADALKQNRSLKALMFSSNTIGDRGAIALAEALKVNQILENLDLQSNSISDMGVTVLMRALCSNQTLSSLNLRENSISPEGAQALTQALCRNNTLKHLDLTANLLHDRGAQAIAVAVGENHSLTHLHLQWNFIQAGAARALGQALQLNRTLTTLDLQENAIGDEGASSVAGALKVNTTLIALYLQVASIGSQGAQALGEALTVNRTLEILDLRGNDVGAAGAKALANALKLNSSLRRLNLQENSLGMDGAIFVASALSENHGLHHINLQGNPIGESAARMISEAIKTNAPTCTVEI
The following text describes a protein:
Function:
Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MTSQESIGIKFLFGGLSCMGAAVVSNPVDVLKTRFQIHGEGIDSKSLGLVNGTIKIIKNEGISAMYKGLTPSLLREATYSTLRMGGYDVIKNYFIDSNGKTNLLSKVTSGALSGALGACITSPTDLIKVRMQASSKGVKYDSISSAFKEIIAKEGIKGLWKGVGPTTQRAALLTASQIPSYDHIKHMILDHGIIQVDGLQVHIVSSIFAGLIASITTSPVDLVKTRIMNQPFDSNGVGLIYKSSYDCFKKTFQSEGISGLYKGFLPNWFRIGPHTIVTFILYEYLRKVSGIKPI
The following text describes a protein:
Function:
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MKNLQIGSVKTFENPEIAGADDFAVHPILQTIAVSTKNELLLLENNLISSTIKWAEQRRELEVISLSFRTDGNQIVVILADGRALIVEDGEVMDLEIAELTDTTVSAAEWTADEQTLALADNQTLYLADSSLVPFAERPLIFSENERKSAPVNVGWGSESTQFRGSAGKLKPGEKIEKEKEQIEQHSRKTSVHWRWDGEIVAVSFYSSQNDTRNLTVFDRNGEILNNMNIRNIYLSHCFAHKPNANLLCSAIQENGSDDRIVIYERNGETRNSYVVKWPANQIEDRRIIEKIEWNSTGTILSMQTSLGKKHQLEFWHLSNYEFTRKCYWKFSESIIWKWSTVECQNIEVLLESGQFFSVHITPTASFSDVISQNVVVATDELRMYSLCRRVVPPPMCDYSIQCLSDIVAYTTSTHHVHVITSDWKIISFSQDTDGYKFNSDRASIDEVLHTEVTEGIICGFVYDEPSESYIIWNVSHGKHQISRVGANPEKIFEGENIGWIGVNPSNKHVEIASNDGKFIDLNTKEELFKIDKFESTEVHFIQNHHVIQVDNSMLFLDSERVSQDAISILTRGSDILLIDFDNKLRFIDAESGKTLEDVRNVEAGCELVACDSQSANVILQAARGNLETIQPRRYVMAHTRDLLDRKEYIASFKWMKKHRVDMSFAMKYKGDDLEDDIPIWLKTSNDSQFLEQLLISCTEVFEDAGSSLCMTVARYVRDLSDAEKTKMFPLLLTALLRSKPSKVNDCLKEVQEHVEKIADRKDVFTRNSLHHISFFVPAKELFNCALSTYDLKLAQQVAEASNYDPKEYLPVLNKLNRVMCTLERQYRINVVREAWIDAVSSLFLLDSSKERGSEETWWNDIEDIIQREKLYQDALTLVKPGDRRYKQCCELYAAELERKVHWREAALFYELSGNSEKTLKCWEMSRDVDGLAASARRLAVDAGKLKIHAIKMSTTLREARQPKELAKALKLAGSSSTQIVHVLCDAFEWLDASREVEVGKEEALKKAALSRNDQVLMDLERRKTEFENYKKRLAVVRENKLKRVEQFAAGEVDDLRDDISVISSISSRSGSSKVSMASTVRRRKQIEKKKSSLKEGGEYEDSALLNVLSENYRWLENIGNELSQLILVLITVGNFPESLKLRSAYDEFATKLQKSKAAIWPESLSVQHLPGPLHALFDPNQEPSPIPMPPIFRLEPELVAPTSSFASVFP
The following text describes a protein:
Function:
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Also plays a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
WSEVQQILNGTPLYMYQDCPVQAGGDTDHWLRSNWIYRGEEASRVHVELQFTVRDCKSFPGGAGPLGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTRRGLYLAFHNPGACVALVSVRVFYQRCPEVVHSLARFPDTLPGPGGLVEVAGTCLPRAQASPGPSAAPRMHCSPDGEWLVPVGRCHCEPGYEEDGSGEACLACPSGSYRADTGAPHCLKCPGHSTTESEGATICTCESGHFRAPGEGPQVLCTRPPSVPRNLSFSILGTQLSLRWEPPADMGGRQDVRYIVGCSQCRGAVVDGGPCQPCGGSVRFSPGASGLIAPAVRVNGLEPYANYTFNVVAQNGVSGLGTSTHAGASLSISMGHAESLSGLSLRLVKKEPRQLELTWAGSRPRSPGGNLSYELHVLNQDEERHQMVLEPRVLLTELQPDTTYIVRVRMLTPLGPGPFSPDHEFRTSPPVSRRLTGGEIVAIIFGLLLAVALLLGMLFFRSRKAERRQQQRQRDRVTDVNREDKLWLKPYVDLQAYEDPAQGALDFTQELDPGWLIVDTVIGEGEFGEVYRGTLRIPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILHLEGVVTKRKPIMIITEFMQNGALDAFLREREDQLVPGQLVAMLQGIASGMNYLSDHNYVHRDLAARNILVSQNLCCKVSDFGLTRLLDNFDGTYETQGGKIPIRWTAPEAIAHRTFTTASDVWSFGIVMWEVLSFGDKPYGEMSNQEVMKSIEDGYRLPPPVDCPAPLYELMKNCWAYDRARRPSFHQLKAHLEQLLANPHSLRTIANFDPRVTLRLPSLSGSDGIPYRSVPEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLAQMGITLPGHQKRILCSIQGFKD
The following text describes a protein:
Function:
Acts as a regulator of the tubular endoplasmic reticulum (ER) network by modulating intracellular calcium homeostasis. Mechanistically, stimulates PKD2 calcium-dependent activity (By similarity). Suppresses the RTN3/4-induced formation of the ER tubules. Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling. Plays an essential role in VEGF-mediated release of Ca(2+) from ER stores during angiogenesis. Also plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. Participates in lipid metabolism by acting as a downstream effector of the pyruvate kinase/PKM. Forms a complex with RNF5 to facilitate polyubiquitination and subsequent degradation of SCAP on the ER membrane (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Melanosome. Nucleus envelope. Note=Co-localizes with RTN4 at the ER sheets.
Sequence:
MADTTPNGPQGAGAVQFMMTNKLDTAMWLSRLFTVYCSALFVLPLLGLHEAASFYQRALLANALTSALRLHQRLPHFQLSRAFLAQALLEDSCHYLLYSLIFVNSYPVTMSIFPVLLFSLLHAATYTKKVLDAKGSNSLPLLRSVLDKLSTNQQNILKFIACNEIFLMPATVFMLFSGQGSLLQPFIYYRFLTLRYSSRRNPYCRNLFNELRIVVEHIIMKPSCPLFVRRLCLQSIAFISRLAPTVA
The following text describes a protein:
Function:
Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces.
Subcellular Localization:
Secreted, extracellular space, surface film.
Sequence:
MDDKSKDEINAASEPPAYKFIPRVPKERTQMILISIVLVLLVTIIIGAILIGVHVTQEHTEKIIKTITKGANGEMVKQTVMVDTQENVAVFYIHSNTTSATVVYDYQQGLIAFRIHSRKQCSVVVMDLVDVPSLHEITELIDHSIDQVSEEDSLLYTFKQRGLADPNALGTTINVLCSDVPVYWAEKNHKKPRRRSVPCPDILILELCFAFL
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mL67/MHR1 also has extraribosomal functions, being involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells. mL67/MHR1 also acts as transcription factor involved in regulation of RNA polymerase II-dependent transcription.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
MAMRTRAEKRMRKFLIEQLKTRQQNGARIAQGKKSEHELIKNNLGPQVFVFRNLFSGQVLYSQVPAYHENQINQQFLSPNWQNRKPSRRQDLWKIMCVVNFNNYEYAIAAYKGLVDLRKTRDVVQKKEANEMRKKNDDGNIWYSGQFRPTYTQEAVADLTHVIDEFELEGTKIFWANEWHRGDDKHWRADLVEHDKLPVYDPRHQTVLLDIMREKAIEAFRENNTSEETIENATEPETA
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MHHMLVLMDILSNRAKADANANADSNKICSNDFECNICLEHVKDPVVTLCGHLYCWPCIYKWINSTSWEHNEKPECPICKSEISESTLVPLYGRGKTTSSSEGEAHQDGVVVPPRPLGPRSLDTATVSQPELEQAEAEAEAPPAQESSLHICLQYGPYKLDFRKFD
The following text describes a protein:
Function:
Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP. Is essential for chloroplast development.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice site.
Subcellular Localization:
Plastid, chloroplast stroma.
Sequence:
MATSSTQLLLSSSSLFHSQITKKPFLLPATKIGVWRPKKSLSLSCRPSASVSAASSAVDVNESVTSEKPTKTLPFRIGHGFDLHRLEPGYPLIIGGIVIPHDRGCEAHSDGDVLLHCVVDAILGALGLPDIGQIFPDSDPKWKGAASSVFIKEAVRLMDEAGYEIGNLDATLILQRPKISPHKETIRSNLSKLLGADPSVVNLKAKTHEKVDSLGENRSIAAHTVILLMKK
The following text describes a protein:
Function:
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MADNSKEKLGSGAAHTINLETFSRRLNVFYDHWNENKSDLWASSDAIAIATPPPSEDLRHLKSTALDVWFLGYDEFPETIIVFMQKQIHFLCSCFGSDIVLHVKSKNGDGIDLMDDNTAKVICWICVQLADVTHGFPEIFAVEGATKIICVKKTACLTSSLMKNFVVPTMEKVIDEERKVSHLSLMYDTEKVIIDPLKAKENGGKFDLRPGASSNDDYLYYDPASIIICATGSRYSNYCSNVARTFLTLLKAQEASLAACKPGNQMSAVFKAAVAVFDDKTAEILTNCSKAVKDVAYSFNDEEENVNDVPYSRELVIQVDQRNEGVLLPIYGSMIPFHVSTVKTTSNSERREYLACHSQMFDKAQGAIYLKMITLRSKDPRHSSEVVQQIKTLRRQVASREPERATLVTQEKLQQASTLQMRLNDVWIRPAFGGRGRKLTGTLQAHVNGFRCSTSRADETYVFFQPAEKEMITLLHIHCTIISWTGRTESTMEFQNYINKVNDHWSQPQFKGLDLEFHIPLRELGFHGVPYKASAFIIPTSTCLVELIETPFLVVTLGEIEIVNLERVGFGTKKFDMAIVFNDFKKDVLRIDSIQTTSLDAIKEWVDTTDLKYYESRLYLNWRPILKTIIDDPQKFVDDDKGYEPSAAEPESESEDEDSDSASLVESDEDEEED
The following text describes a protein:
Function:
Binds single-stranded (ss)DNA. At low concentrations (0.02 to 0.16 uM), stimulates the 5'-3' helicase activity of DnaB. At higher concentrtions eventually totally inhibits DnaB helicase.
Sequence:
MAGDTTITIVGNLTADPELRFTPSGAAVANFTVASTPRIYDRQTGEWKDGEALFLRCNIWREAAENVAESLTRGARVIVSGRLKQRSFETREGEKRTVIEVEVDEIGPSLRYATAKVNKASRSGGFGSGSRPAPAQTSSASGDDPWGSAPASGSFGGGDDEPPF
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization:
Cytoplasm.
Sequence:
MMSTDGSETVSFGSSISTAELPESNITDVTEPPAKLIKSKHEHCSQTDSSHTHSAGCSHTTSIAAQTEDIPSDALPRRAILTKEDLERFQTSPACQDFINFLTDLNQSVRNITLSTAVAESPNITKLLSVLETLDGWTVDLPPDEEGKSRFGNPAFQRWYDRLDSQAQTLLAPILSDHSSAIPELAVYLLHSFGNRKRIDYGTGHEAHFIAFLLCLEKLGIVQKEDYPALVLRVFWKYIKVMRTLQFNYWLEPAGSHGVWGLDDYHFLPFLFGSSQLADHKYFRPKSIHDPDIIAEFSKDYIYFACIQFINSVKTASLRWHSPMLDDISGVKKWDKVNQGMIKMYKAEVLAKLPIMQHFLFGSLLAFKGSAFSEGDATEDHGHDHIHAFGQEHPTCCGMRVPSAIAAGLAEHRALPRRPLPFD
The following text describes a protein:
Function:
Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing.
Miscellaneous:
MISCELLANEOUS: Ectopic expression of TMED2 alone does not result in its proper cis-Golgi network localization. Coexpression of TMED10 is necessary, and coexpression of TMED3 and/or TMED9 is facilitating localization. Down-regulation of TMED10 expression reduces TMED2 protein level.
Subcellular Localization:
Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Note=Cycles between compartments of the early secretatory pathway.
Sequence:
MVTLAELLVLLAALLATVSGYFVSIDAHAEECFFERVTSGTKMGLIFEVAEGGFLDIDVEITGPDNKGIYKGDRESSGKYTFAAHMDGTYKFCFSNRMSTMTPKIVMFTIDIGEAPKGQDMETEAHQNKLEEMINELAVAMTAVKHEQEYMEVRERIHRAINDNTNSRVVLWSFFEALVLVAMTLGQIYYLKRFFEVRRVV