lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Central component of a redox-sensitive mitochondrial intermembrane space import machinery which is required for the biogenesis of respiratory chain complexes. Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17, COX19, MICU1 and COA7. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Required for the import of COA7 in the IMS. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay system. Mediates formation of disulfide bond in MICU1 in the IMS, promoting formation of the MICU1-MICU2 heterodimer that regulates mitochondrial calcium uptake.
Subcellular Localization:
Mitochondrion intermembrane space.
Domain:
The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria.
Sequence:
MSYCRQEGKDRIIFVTKEDHETPSSAELVADDPNDPYEEHGLILPNGDINWNCPCLGGMASGPCGEQFKSAFSCFHYSTEDIKGSDCIDQFRAMQECMQKYPDLYPQDEEEEEEAKPVEPVEETADTKVSAAKEQGTSS
The following text describes a protein:
Function:
Negatively regulates the expression of the aliphatic amidase operon. AmiC functions by inhibiting the action of AmiR at the protein level. It exhibits protein kinase activity.
Domain:
Consists of two beta-alpha-beta domains with a central cleft in which the amide binds.
Sequence:
MGSHQERPLIGLLFSETGVTADIERSQRYGALLAVEQLNREGGVGGRPIETLSQDPGGDPDRYRLCAEDFIRNRGVRFLVGCYMSHTRKAVMPVVERADALLCYPTPYEGFEYSPNIVYGGPAPNQNSAPLAAYLIRHYGERVVFIGSDYIYPRESNHVMRHLYRQHGGTVLEEIYIPLYPSDDDVQRAVERIYQARADVVFSTVVGTGTAELYRAIARRYGDGRRPPIASLTTSEAEVAKMESDVAEGQVVVAPYFSSIDTAASRAFVQACHGFFPENATITAWAEAAYWQTLLLGRAAQAAGSWRVEDVQRHLYDICIDAPQGPVRVERQNNHSRLSSRIAEIDARGVFQVRWQSPEPIRPDPYVVVHNLDDWSASMGGGALP
The following text describes a protein:
Function:
Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton.
Sequence:
MNSVAGNKERLAVSTRGKKYGVNEMCSPTKPSAPCSPESWYRKAYEESRAGSRPTPEGAGSALGSSGTPSPGSGTSSPSSFTGSPGPASPGIGTSSPGSLGGSPGFGTGSPGSGSGGGSSPGSDRGVWCENCNARLVELKRQALKLLLPGPLPGKDPAFSAVIHDKLQVPNTIRKSWNDRDNRCDICATHLNQLKQEAIQMVLTLEQAAGSEHYDTSLGSPPPISSIPTLVGSRHMGGLQQPREWAFVPAPYATSTYTGLVNKHSGKPNSLGVSNGAEKKSGSPTHQAKVSLQMATSPSNGNILNSVAIQAHQYLDGTWSLSRTNGVTLYPYQISQLMTETGREGLTESALNRYNADKPAASSVPAPQGSCVASETSTGTSVAASFFARAAQKLNLSSKKKKHRPSTPSVAEAPLFATSFSGILQTSPPPAPPCLLRAVNKVKDTPGMGKVKVMLRICSTSARDTSESSSFLKVDPRKKQITLYDPLTCGGQNAFQKRSSQVPPKMFAFDAVFPQDASQAEVCAGTVAEVIQSVVNGADGCVFCFGHAKLGKSYTMIGRDDSMQNLGIIPCAISWLFKLINERKEKTGARFSVRISAVEVWGKEENLRDLLSEVATGSLQDGQSPGVYLCEDPICGTQLQNQSELRAPTAEKAAFFLDAAIASRRSNQQDCDEDDHRNSHMLFTLHIYQYRMEKSGKGGMSGGRSRLHLIDLGSCVKALSKNREGGSGLCLSLSALGNVILALVNGSKHIPYKESKLTMLLRESLGNVNCRTTMIAHISAAASSYAETLSTIQIASRVLRMKKKKTKYTSSSSGGESSCEEGRMRRPTQLRPFHARAPVDPEFPLAPLSSDPDYSSSSEQSCDTVIYIGPNGTALSDKELTDNEGPPDFVPIVPALQKTRGDSRPGEAAEAAASKSERDCLKCNTFAELQERLDCIDGSEEPSKFPFEELPIQFGPEQAGRCAPLSQAVGPDTPSESEKEDNGSDNGQLTEREGTELPASKAQRNRSPAPTVTRSSSPSPASPRSIPGSSSQHSTSQLTQSPSLQSSRESLNSCGFVEGKPRPMGSPRLGIASLSKTSEYKPPSSPSQRCKVYTQKGVLPSSAPPPSLSKDSGMVSSESLLQPDVRTPPVGMSPQVLKKSMSAGSEGFPGTLVDGEDQEGPPADSKKEILSTTMVTVQQPLELNGEDELVFTLVEELTISGVLDSGRPTSIISFNSDCSVQALASGSRPVSIISSISEDLECYSSMAPVSEVSITQFLPLPKLGLDEKARDAGSRRSSISSWLSEMSAGSDGEQSCHSFIAQTCFGHGEAMAEPPASEFVSSIQNTAVVCREKPEVGPDNLLILSEMGEESGNKAAPIKGCKISTVGKAMVTISNTASLSSCEGYIPMKTNITVYPCIAMSPRNVQEPESSTATPKVSPKASQAQESKEPSTRREMKFEDPWLKREEEVKRENAYSSEEGVKCEPLPSSLKTEGKSEQELDGRPSSGNRLSSSSSEAAAFQGTDNVRRVVDGCEMALPGLVAQSPLHVNRNLKSSSLPRAFQKADRHEELDSFYHCLADSNGFSAASGIPSSKTTLERKVASPKHCVLARPKGTPPLPPVRKSSLDQKNRASPQHGGGSSNTSSPLNQPATFLACFPDESNGKTKDVSSSSKLFSAKLEQLASRSNSLGRTTVSHYECLSLERAESLSSVSSRMHAGKDSTMPRTGRSLGRSTGASPPSCGITQSTGASPKASQSKISAVSKLLLASPKSRSSLSTSTTKTLSFSTKSLPQSVGQSSNLPPSGKHMSWSTQSLSRNRGSGLASKLPLRAVNGRISELLQGSAGPRSAQLRAEAEERSGAPSEDKPAAAHLLPSPYSKITPPRKPHRCSSGHGSDNSSVLSGELPPAMGKTALFYHSGGSSGYESMMRDSEATGSASSAQDSMSENSSSVGGRCRSLKNQKKRSNSGSQRRRLIPALSLDTPSPVRKTASSTGVRWVDGPLRSTQRSLGEPFEIKVYEIDDVERLQRRRGATSKEVMCFNAKLKILEHRQQRIAEVRAKYEWLMKELEATKQYLMLDPNKWLREFDLEQVLQLDSLEYLEALEGVTERLESRVNFCKAHLMMITCFDITSRRR
The following text describes a protein:
Function:
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Subcellular Localization:
Cytoplasm.
Sequence:
MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAEQLPALFNGMPMGTRILA
The following text describes a protein:
Function:
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Subcellular Localization:
Mitochondrion.
Sequence:
MIRSLNFALRNCNKNILINSNKITINNGLLLKKNNFCTQSTSEVKVPTELVVQLRKKTQSPVQECKKALQASNNDMDGAIKWLLEKGKATAEKLKSRVSAEGIISVLVDSGSGKAVILEMNSETDFVSRGDIFRNLARDISKATLSNPISGGKLAENGILELDPTQVENIYPIKINITNEDGVAEEMTIKDSIVRIVSKLRENIVIRRASFIQPLNNNNNNSKSYISSYAHDSTSEKKDVGRLGSIVQFEYQGDCNNMNSLKEFANQLAIHIVSNSPSVVTVNDIPSSVLEECKNNNKNPESLYDDMVLYEQSYMYSPDHSVKQYLEILSEKLGIKNLSVKTFRRYAIGETAERV
The following text describes a protein:
Function:
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Miscellaneous:
MISCELLANEOUS: The porphobilinogen subunits are added to the dipyrromethane group.
Sequence:
MRMSAPELIRIVSRDSPMALAQVERVRAELAALHPGVRTEVVPVRTTGDKWLGDLSQVEGKGAFTKEVDAALLSGEADLAVHCVKDVPADRPLPAGTVFAAFLKRDDVRDALVHPDGLTLDELPDGTRVGTSSVRRVAQLAATHPHLRCVPFRGNANRRLAKLAAGEADALLLAVSGLERIGRTDVISEVLSTETMMPPIGAGILALQCREGDRALIEAVSALGDPRTHREATAERMFLHVLQGHCNSPIAGHAQVDRSGELSLRACVFTPDGKVRLNAHEWAGRLDPATLGTSVAVALLRQGAREIIDGIAH
The following text describes a protein:
Function:
Part of the ferric enterobactin transport system.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSSLNIKQGSDAHFPDYPLASPSNNEIDLLNLISVLWRAKKTVMAVVFAFACAGLLISFILPQKWTSAAVVTPPEPVQWQELEKSFTKLRVLDLDIKIDRTEAFNLFIKKFQSVSLLEEYLRSSPYVMDQLKEAKIDELDLHRAIVALSEKMKAVDDNASKKKDEPSLYTSWTLSFTAPTSEEAQTVLSGYIDYISTLVVKESLENVRNKLEIKTQFEKEKLAQDRIKTKNQLDANIQRLNYSLDIANAAGIKKPVYSNGQAVKDDPDFSISLGADGIERKLEIEKAVTDVAELNGELRNRQYLVEQLTKAHVNDVNFTPFKYQLSPSLPVKKDGPGKAIIVILSALIGGMVACGGVLLRYAMASRKQDAMMADHLV
The following text describes a protein:
Function:
The H4 subclass of histamine receptors could mediate the histamine signals in peripheral tissues. Displays a significant level of constitutive activity (spontaneous activity in the absence of agonist).
Miscellaneous:
MISCELLANEOUS: Does not bind diphenhydramine, loratadine, ranitidine, cimetidine and chlorpheniramine. Shows modest affinity for dimaprit, impromidine, clobenpropit, thioperamide, burimamide clozapine, immepip and imetit. The order of inhibitory activity was imetit > clobenpropit > burimamide > thioperamide. Clobenpropit behaves as a partial agonist, dimaprit and impromidine show some agonist activity while clozapine behaves as a full agonist. Thioperamide shows inverse agonism (enhances cAMP activity). The order of inhibitory activity of histamine derivatives was Histamine > N-alpha-methylhistamine > R(-)-alpha-methylhistamine > S(+)-alpha-methylhistamine. Both N-alpha-methylhistamine > R(-)-alpha-methylhistamine behave as full agonists.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPDTNSTINLSLSTRVTLAFFMSLVAFAIMLGNALVILAFVVDKNLRHRSSYFFLNLAISDFFVGVISIPLYIPHTLFEWDFGKEICVFWLTTDYLLCTASVYNIVLISYDRYLSVSNAVSYRTQHTGVLKIVTLMVAVWVLAFLVNGPMILVSESWKDEGSECEPGFFSEWYILAITSFLEFVIPVILVAYFNMNIYWSLWKRDHLSRCQSHPGLTAVSSNICGHSFRGRLSSRRSLSASTEVPASFHSERQRRKSSLMFSSRTKMNSNTIASKMGSFSQSDSVALHQREHVELLRARRLAKSLAILLGVFAVCWAPYSLFTIVLSFYSSATGPKSVWYRIAFWLQWFNSFVNPLLYPLCHKRFQKAFLKIFCIKKQPLPSQHSRSVSS
The following text describes a protein:
Function:
Regulator of microtubule dynamic that has microtubule bundling activity. Required for embryo implantation; possibly by regulating beta-catenin (By similarity). Also required for decidualization via regulation of beta-catenin.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton.
Sequence:
MAASTDMAGLEESFRKFAIHGDPKASGQEMNGKNWAKLCKDCKVADGKSVTGTDVDIVFSKVKGKSARVINYEEFKKALEELATKRFKGKSKEEAFDAICQLVAGKEPANVGVTKAKTGGAVDRLTDTSRYTGSHKERFDESGKGKGIAGRQDILDDSGYVSAYKNAGTYDAKVKK
The following text describes a protein:
Function:
Cell surface receptor that regulates diverse cellular processes including cell proliferation, differentiation, migration, and apoptosis. Initiates BMP, inhibin, and TGF-beta signaling pathways by interacting with different ligands including TGFB1, BMP2, BMP5, BMP7 or GDF5. Alternatively, acts as a cell surface coreceptor for BMP ligands, serving to enhance ligand binding by differentially regulating BMPR1A/ALK3 and BMPR1B/ALK6 receptor trafficking. Promotes epithelial cell adhesion, focal adhesion formation and integrin signaling during epithelial cell spreading on fibronectin. By interacting with the scaffolding protein beta-arrestin2/ARRB2, regulates migration or actin cytoskeleton and promotes the activation of CDC42 as well as the inhibition of NF-kappa-B (By similarity). In gonadotrope cells, acts as an inhibin A coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility. Plays a role in the inhibition of directed and random cell migration in epithelial cells by altering the actin cytoskeletal organization (By similarity). Participates in epithelial-mesenchymal transformation (EMT) upon binding to BMP2 or TGFB2, by activating the PAR6/SMURF1/RHOA pathway (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Secreted. Secreted, extracellular space, extracellular matrix. Note=Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix.
Sequence:
MAVTSHHMVPVFVLMSACLATAGPEPSTRCELSPISASHPVQALMESFTVLSGCASRGTTGLPREVHILNLRSTDQGLGQPQREVTLHLNPIASVHTHHKPVVFLLNSPQPLVWHVKTERLAAGVPRLFLVSEGSVVQFSSGNFSLTAETEERSFPQENEHLLHWAQKEYGAVTSFTELKIARNIYIKVGEDQVFPPTCNIGKNFLSLNYLAEYLQPKAAEGCVLASQPHEKEVHIIELISPNSNPYSTFQVDIIIDIRPAREDPEVVKNLVLILKCKKSVNWVIKSFDVKGNLKVIAPDSIGFGKESERSMTVTKLVRNDYPSTQENLMKWALDNGYSPVTSYTIAPVANRFHLRLENNEEMRDEEVHTIPPELRILLGPDHLPALDSPPFQGEIPNGGFPFPFPDIPRRGWKEGEDRIPRPKEPIIPRVQLLPDHREPEEVQGGVNIALSVKCDNEKMVVAVDKDSFQTNGYSGMELTLLDPSCKAKMNGTHFVLESPLNGCGTRHRRSAPDGVVYYNSIVVQAPSPGDSSGWPDGYEDLESGDNGFPGDTDEGETAPLSRAGVVVFNCSLRQLRSPSGFQDQLDGNATFNMELYNTDLFLVPSPGVFSVAENEHVYVEVSVTKADQDLGFAIQTCFISPYSNPDRMSDYTIIENICPKDDSVKFYSSKRVHFPIPHAEVDKKRFSFVFKSVFNTSLLFLHCELTLCSRNKGSQKLPKCVTPDDACTSLDATMIWTMMQNKKTFTKPLAVVLQVDYKENVPNMKESSPVPPPPQIFHGLDTLTVMGIAFAAFVIGALLTGALWYIYSHTGETARRQQVPTSPPASENSSAAHSIGSTQSTPCSSSSTA
The following text describes a protein:
Function:
Binds to the peptide-binding site of MHC class II alpha/beta heterodimers forming an alpha-beta-CLIP complex, thereby preventing the loading of antigenic peptides to the MHC class II complex until its release by HLA-DM in the endosome.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane. Golgi apparatus, trans-Golgi network. Late endosome. Lysosome. Secreted.
Sequence:
MHRRSSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTEAPPKVLTKCQEEVSHIPAVYPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLSPVPM
The following text describes a protein:
Function:
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
MSGAGRGAVTRSRSRRPGRVEDAGSRPAAGSRLQPSPSEVNLEKGRQTPPDTSPFAVVPAGEAQVRPLKRQRRRPKAGSLEVCYEPLAGSGGEAAGLGPSGSSPWEPPAWRQHLDNIRDMRESRDAPVDQLGVEQCFDRDAPPEVQRYQVLLSLMLSSQTKDQVTAGAMRRLQAHGLSVDGVLRMDDATLGRLIYPVGFWKSKVRFIKQTTAILKDRYRGDIPATVAGLLQLPGVGPKMAHLAMAIAWGAVSGIAVDTHVHRIANRLQWTQTETKSPEQTRAALEDWLPRELWSEINWLLVGFGQQVCLPRHPRCASCLNRTLCPAARES
The following text describes a protein:
Function:
In embryogenesis, has a role in somatic muscle attachment and in the development of axonal pathways probably by stabilizing cell-matrix adhesion and/or by acting as a competitive antagonist of serine proteases.
Subcellular Localization:
Secreted. Cell projection, axon. Note=Localizes to vesicle-like structures in epidermal cells.
Domain:
The CLIP domain consists of 37-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence:
MPRHSSTMSRLVLPLIFSILLVSKPSPSQAQDESLAGSFLSGLLDTITSTADSKDCPGVCVHTLATLICYEVLDDVACPSPSMKCCIENAPAGKNATAVRATTTPKTTTTASTTTTQRTTTTVATTSTTKRTTTTSTTPKPKPKPQTKRPATSSTTKATVATTKKPSTTKKVATAKPKDKEEATKADDANKDCTGVCVADRIAEYCEAYLTSDGLCKEGTKCCVSLDEYSNGKLPKDIYIPAKHMSNLKPNQTLSEKSAPAKSSSTSTTSTTTTTSTTTTPEPARINNSSPKPTKHKKHPTTTTTEAAEEEEEQETEEDGEEEEPPLSNKLKSGQGQGQVLKECEGECMNGIFAIFCDDIDSDAFCPGEESCCVTGGASEATPSSKAPPTKPAIKHAPKPAAKPARPASPPPAPPSSTSGGGGGGDFLSQIISFAESTLNSPSPPPPPPQAPIQVPRCPGFCLLNIMAAFCERPSVLVSTPTTCAKGSVCCDNSRAGAPKPKLPPPTPSPTASPTAPPYVLPNTPSPDPREECPGSCIVSLLSFTCFKNAEMTDLFRCKRSGQICCAPKSKILEKQQFQTRNDTAYYPAPPPPPIGPPQAYPPQTPPYSYMNNPPPQGPPPQMAPHHPNPYQPPPPAPNYADYYPVSGPGLPPQPQPPMTTPPTTTTTTTTPRPHVYSKYVCGVKGTLRTGRSQALSFVSYARAKYGVQRTARQMTSAAGYSPNFNKSNERLVLGSAIVPIQIHNDKLGDLVESSSLQSNQLRSYHNHQAQADQPDLVYPEYYQQRSLYGLQSNFSGRRRARVVGGEDGENGEWCWQVALINSLNQYLCGAALIGTQWVLTAAHCVTNIVRSGDAIYVRVGDYDLTRKYGSPGAQTLRVATTYIHHNHNSQTLDNDIALLKLHGQAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGEAGPIPLRVREAEIPIVSDTECIRKVNAVTEKIFILPASSFCAGGEEGHDACQGDGGGPLVCQDDGFYELAGLVSWGFGCGRQDVPGVYVKTSSFIGWINQIISVNNL
The following text describes a protein:
Function:
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFPIYEVTFFIFAAVLIAAAAMVIISRNPVHAVLFLVLAFFASAVLWMMMQAEFLALVLIFVYVGAVMTLFLFVVMMLNIDLSDLQQKFVRFLPFGLIAMALLIGMMVVIVSPRHFTVATAHLPHVASNFSNVKAMGSLLYVDYFYPFEIAAVILLVAIIAAITLAFHGRKPNTKSQRVREQLEAKKENRLRVIKMKTENS
The following text describes a protein:
Function:
Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.
Subcellular Localization:
Cytoplasm, perinuclear region. Membrane; Lipid-anchor.
Sequence:
MGHALCICSRGTVTIDNKRYLFIQKLGEGGFSFVDLVEGLQDGRFYALKRIVCHERQDREDAQHEADMHRLFQHPNILPLEAYCLVERGPKHEAWLLLPFLKGGTLWSEVEGLRDRGSFLSEERILFLLLGICRGLEAIHAQGYAHRDLKPTNILLGETGQPVLMDLGSMNRARIQVDDSRQALALQDWAAQRCTISYRAPELFCVQSRRVVDERADVWSLGCVLYAMMFGEGPFDAVFQKGDSVALAVQSPLDVPRTPRYSPPLRRLLSSMMTVDPQARPHVPPLLAQLEALRPPAPGQLTTPI
The following text describes a protein:
Function:
Transcription factor. Binds to GC-rich DNA motifs, such as 5'-GGGCGGGG-3'. Involved in cell autonomous neuroblast asymmetric divisions that generate one precursor cell and one apoptotic cell, by transcriptionally activating target genes, such as cell death activator egl-1 and leucine zipper kinase pig-1, in caspase-dependent and -independent apoptotic pathways. Plays a role in the regulation of apoptosis, cell lineage, cell differentiation, embryonic morphogenesis, vulval development, and oocyte production.
Subcellular Localization:
Nucleus.
Sequence:
MSKSGQQQQPHQQMQQQQQQQGKMMVVHHQRTTTPDGSQVYLLQPSQSHPQQRQVQFIPIQVAQGEKKPQTVMMNQMMGQQQQQQPSSSNQQSQQQVQQQQQQVHQVQQVQQHQMQQQNQTVQQQHLMMETIDQVGSGIIGNSNGNNQQQQQQQQQQQQRRDPIPIAPAGMVSGQRMQQQQQQPQQQQQHNNNNTGASTSNGGVNAAPVMPVMGGQQRITLGNLHFQQDPNDPQKWIITNEGPPVAGPSAPARKPNQIQHRQMIPQMNEDGMMNMGNDYGDINGQGLGEAPKRCACTCPNCLQQNNRQGDGKSRIHICHLCNKTYGKTSHLRAHLRGHAGNKPFACDWQHCNKKFTRSDELQRHRRTHTGEKRFACNHCGKKFMRSDHLTKHERTHQSNRINNINQQTLRLS
The following text describes a protein:
Function:
Involved in a signal transduction pathway that play a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act on the BCK1 kinase that then phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.
Miscellaneous:
MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
Sequence:
MASLFRPPESAKCNPNSPRLKLPLLRNNQVDENNIYLTSNGSSTTAYSSHTPEPLTSSTSTLFSQTRLHPSDSSMTLNTMKKRPAPPSLPSLSINSQSKCKTLPELVPIADVSDGKHDLGLKQRVIAENELSGNSDLTPSSMASPFSHTNTSSPYLRNDLSNSVGSDFSNLISAYEQSSSPIKSSSQPKSSSESYIDLNSVRDVDQLDENGWKYANLKDRIETLGILGEGAGGSVSKCKLKNGSKIFALKVINTLNTDPEYQKQIFRELQFNRSFQSEYIVRYYGMFTDDENSSIYIAMEYMGGRSLDAIYKNLLERGGRISEKVLGKIAEAVLRGLSYLHEKKVIHRDIKPQNILLNENGQVKLCDFGVSGEAVNSLATTFTGTSFYMAPERIQGQPYSVTSDVWSLGLTILEVANGKFPCSSEKMAANIAPFELLMWILTFTPELKDEPESNIIWSPSFKSFIDYCLKKDSRERPSPRQMINHPWIKGQMKKNVNMEKFVRKCWKD
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular Localization:
Nucleus.
Sequence:
MHLMRWSNVCKDENMEVWKLEDTRPLIGHYKANGCGGMSRSQGSSLKRKRPDTNTASQPLLDAERVLYDLIRSKEDMGIWTRDMKRETNLPDNVVTKSLKALQVKKLIKEVVNIQSKGRKHYMAVEFEPSKELTGGAWYVEGNLDTEYIKILKKTCVRVLSKLKVATAEGISESINKTGLCATECSTQQIAEILRALVLDNEIMEVRSSGSGEFSSIPIGAVCYRCTNKGGLGGGGPTIGAMASIPCGVCPRITQCTPDGIISPKTCAYYTKWLDF
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Sequence:
MHDFVSHILRQYFHATNWNEYNSYLHLTSCSSAILDFCVPTGLSLSISASPTPPFFTTYRLGALPNLRAGIGYIYASTDSKIDFGGSSKDVRLKEIIERFRIVEARAPAAFKSKEKEKEYYWLAGDRYPEQEALGDLGKKERGGGEYLVYGCMHVPSARLDALWTKRISPTWQLIVTAVSSPPRYPLNALQNAAIASRSAYSTGAKSTSSSMDRLDSSNPSLSSSTSLSNTGASTAATTAAAAAAAAAAQDTYGLGPPGSTNLQFTLQRDTGRWFTEYSYSIDDALWGFRVLHNFGTPADTASTTLAALSEGAVETSSSASYPQRNGSVLHTGSSSSSEDTEAGGGLRGRFSAGAEVFISTVEKSAGLSTGIRFSTLPDTPQQPLMIAPSFDSSPSPHQASTLASAPSQPPTVITATLNPMMGHLSTAYAARMARDVVVCSRFDFNVYSYESEWTMGAEYWLRKSGGGGGVESVEASDADVPAPMNRIGSTSSIGGLRGHDETRQARFQEEHAMSLREASEAVSQVDGNTGDGGTSVFGLLRDPPALAPSAPSPRATCANSTLSHLLSPITGVLKARISSTSDIRLLWQGRLSHCLVSLGVKADLSGTHGASYSVGGAPASPKMGIVKSIGLEVMYFSQAEDESVE
The following text describes a protein:
Function:
Ca(2+)-dependent modulation of synaptic efficacy. Also plays a role in axon terminal morphology.
Miscellaneous:
MISCELLANEOUS: Binds 3 calcium ions via the second, third and fourth EF-hands.
Subcellular Localization:
Cytoplasm.
Sequence:
MGKKSSKLKQDTIDRLTTDTYFTEKEIRQWHKGFLKDCPNGLLTEQGFIKIYKQFFPQGDPSKFASLVFRVFDENNDGSIEFEEFIRALSVTSKGNLDEKLQWAFRLYDVDNDGYITREEMYNIVDAIYQMVGQQPQSEDENTPQKRVDKIFDQMDKNHDGKLTLEEFREGSKADPRIVQALSLGGG
The following text describes a protein:
Function:
Converts protoheme IX and farnesyl diphosphate to heme O.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MMLSKIINNISKSGLRNTTNSKNGGLLYFQNYYMKSSTTITRLNSGNNNYSNNNNNNNNIILNDKFLNKQQNDKKIIYNNIFEEKNQFLKRIYSTSTTTTSTTTTTNINENNIKNENNNENNNENSNNNNEQSIKSNQTKSKGFLRGPYMTLIKLPITVYVTLTAIAGYVAACPIGAFDWVVLSQVSIGTFLASCSANIHNQEIEVQHDRKMPRTKDRPLVIGTINRGKAWVGSIALLTLGFGTMAVTPSLFVPGTLAACNVILYCWYTDLKRVTPLNTWIGAFVGAIPPLIGSVAATGEFEAIGMLLATFMYIWQIPHFLALSQVLREQYRGAGYKMLSVTHEKKTVDRVSLAHALFGIPLPFIFDYFFNFNVHPITLTCMALSSASLALPFITKISPKRLYIISLISLPITLFLSCLLRQPFAYYTDDDDEDKDKDNQNQIENQDKK
The following text describes a protein:
Function:
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Sequence:
MGKNGKVPQKEKRGKNKRFDRVGQPSAHDHPEFPVRLAMWDFGQCDPKRCSGIKLKRLGYVRVLNLRDTFHGLVLSPIGTQIISPEDKELALSSGLAVVDCSWKQLDHTDVTQLKARHHRVLPYLVAANTVNFGKPWRLNCAEALAACLAIFGMQDAADELLNQFKWGHSFFEQNGDYIDAYKTARSAQEMTDMQNFFLNELKEEAEQMQDENYDPIIDGNPNRRPVKRHIYIPKEYPEEPKSNPDAPVDPNAPAQPAPEAPKPVVNVLSPKDLGSDYSDNGYCTEDEDD
The following text describes a protein:
Function:
Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron.
Subcellular Localization:
Nucleus, PML body. Cytoplasm. Note=The sumoylated form locates to the nuclear bodies PML oncogenic domains (PODs). Translocated to the cytoplasm through interaction with ITCH (By similarity).
Domain:
The PXY motifs are required for binding WW domains. PXY1 is required to promote transactivation of beta-globin and for hyperacetylation of histone H3, but not for binding to the HS2 promoter site.
Sequence:
MPPCPPQQNRNRLSQLPVGELGEMELTWQEIMSITELQGLNVPSETSFEPQAPTPYPGPLPPPTYCPCSIHPDAGFSLPPPSYELPASTPHVPELPYSYGNVAIPVSKPLTLSGLLNEPLPDHLALLDIGLPVGQPKPQEDPESDSGLSLNYSDAESLELEGMEAGRRRSEYVDMYPVEYPYSLMPNSLAHPNYTLPPTETPLALESSSGPVRAKPAVRGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLAQYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLSSERERLLRARGEADRTLEVMRQQLAELYHDIFQHLRDESGNSYSPEEYVLQQAADGAIFLVPRGTKMEATD