lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MTRALFSGRVFHGYRRLPCWRISSAYRVLNVYTARQASSTSTIGSANVSSLETGHITLEDNEGLVFVNNIFPRKLQWLLQLGPLNGTHSYEKALKRINRPQLAASDPLHIIRRVLPQDLDIDVKDVIPRFREGGAFVKYARKSEATDAEIEASIKEHLEKNPIRPWFNPFQQATVAHVQGRPWIEDLYRIPSPRIRVEFHPATPEGSATELTTEVLYSVFRRYGKLRYIEQQPPDSKVTPRYALVEFARPSNAVTAKNCVHGFTIPPEGGEGKSGTRVKIKYERKIRLSMIKDWLLSHPRLVIPAVAALIAAITVTIFDPIRTFFIKMKIKATLQIEENKFLQWVRYQVSKANIYFRQSKPDVRGLSAIWEDRHNDIEQLNSWLTESAETFIVIHGPRGSGKRELVLDRTLKDNKYKLIIDCKQIQDAKGDTAKIARAASQVGYRPVFSWMNSISSFIDLAAQGMIGTKAGFSETLDAQLSNIWQNTAVALKSITLEHRKKTDPDAQLSDEEYLEAHPEVRPVVVIDNYLHNNPEATSVVYDKITEWAAGLATGNIAHVIFLTTDVSFAKPLSKALPNTVFRTISLGDCSLEVGRKFVLNHLEHEARNKNKDTRHEEDLAELDSCIGVLGGRLTDLEFMAHRIEAGETPRGAVTRIVEQSASEILKMFILNPESESQKWTHQQAWHLIKTLARSKDGSVPYNHVIQSDLFKSNSQALRELEQAELISIVTVNGSPERVRAGRPVYQAVFKRLTENKALSSRLDMEVLSQLISKENKSIGKYEEELLLLGKLPKQPRELTGRIQWLLQKVYNSQNKIAKYEAESAALQKMLQSEH
The following text describes a protein:
Function:
Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate. Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.
Miscellaneous:
MISCELLANEOUS: Binds O(2) with a dissociation constant of about 74 uM.
Domain:
The EAL domain (residues 532 to 799) is a cyclic dinucleotide di-GMP (c-di-GMP) PDE hydrolyzing c-di-GMP to 5'pGpG; it has no activity on cAMP; Binding of an external ligand to the heme located in the N-terminal sensory domain displaces the distal heme ligand from Met-87 to the ligand and triggers a conformational change that regulates the activity of the C-terminal catalytic domain; The heme-PAS domain (residues 1-139) forms homodimers.
Sequence:
MKLTDADNAADGIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI
The following text describes a protein:
Function:
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular Localization:
Cytoplasm.
Sequence:
MPSHKSFRTKQKLAKAARQNRPIPQWIRLRTGNTVHYNMKRRHWRRTKLNI
The following text describes a protein:
Function:
Phytyl-phosphate kinase catalyzing the conversion of phytyl-monophosphate to phytyl-diphosphate. Involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol (vitamin E) biosynthesis. Involved in the biosynthesis of phylloquinone (vitamin K), which is required for the photosystem I (PSI) complex stability.
Miscellaneous:
MISCELLANEOUS: Overexpression of VTE6 results in increased phytyl-PP and tocopherol levels in seeds.
Subcellular Localization:
Plastid, chloroplast membrane; Multi-pass membrane protein.
Sequence:
MATISSTLLLNSSRSALPLRFPKFSGFSSSSPFARSYRFGRRNLEPLSNGMLSSGSRADGATAAAASMEGVMTEAMKLIQSASPTWKSAVANNLLIFVLGSPLLVTGLSASGIAAAFLLGTLTWRAYGSAGFLLVAAYFVIGTAATKVKMTQKEAQGVAEKRKGRRGPRSVIGSSAAGCVCAFLSIYQVGGAAFSQLFRLGFVSSFCTKVSDTVSSEIGKAYGKTTYLATTFKIVPRGTEGAMSLEGTLAGLLASFFLASVGCFLGQITPPEAAVCVLASQIANLGESIIGASFQDKEGFKWLNNDVVNVINISLGSIVAILMQQFILQNWVK
The following text describes a protein:
Function:
Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity.
Subcellular Localization:
Cell membrane. Cytoplasm. Endomembrane system; Peripheral membrane protein.
Sequence:
MSLNVTPDDAPVELTSGSFWEVNQYKRTVTRIDNGMKLCDDLMLFIKERATLEEQYSKLLKQWSSKFHKLVEKNSSYHTLQTTWLGMLNEADRTAQLHSTIKEQLMADPYEKVKQWKKENYHTLTLGGIKESKLLNEEFMRAQKQWAKYMKKVTDAKKTYFNVCKEERSAQTQESTAKSDTSLAPEKVKKLQELVEKKGAEKSKYREKYEQAVRALKDDTPRYMEDMEKVFVKCQEFEEKRLEKFKAIFHAVHGHLDLSTNVEHKAIFVDLKSNIDSANSQNDLQWWRSTHGPDMPMNWPEVEDYDPERILMQKSMSRKQGSKASKHVAGMDGLAGAQFTSTYPATAPVETKTSGNGSANRPNSWSDDEQNNPFQDSSSEGNPFGSVENTSGGVPVRALYNYDGQEEDELTFLSGETLYKLEDEDEQGWCKGRLSTGKVGLYPANYVETI
The following text describes a protein:
Function:
Involved in GM1/GD1B/GA1 ganglioside biosynthesis.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MQLRLFRRLLLAALLLVIVWTLFGPSGLGEELLSLSLASLLPAPASPGPPLALPRLLIPNQEACSGPGAPPFLLILVCTAPENLNQRNAIRASWGGLREARGLRVQTLFLLGEPNAQHPVWGSQGSDLASESAAQGDILQAAFQDSYRNLTLKTLSGLNWAEKHCPMARYVLKTDDDVYVNVPELVSELVLRGGRWGQWERSTEPQREAEQEGGQVLHSEEVPLLYLGRVHWRVNPSRTPGGRHRVSEEQWPHTWGPFPPYASGTGYVLSASAVQLILKVASRAPLLPLEDVFVGVSARRGGLAPTQCVKLAGATHYPLDRCCYGKFLLTSHRLDPWKMQEAWKLVGGSDGERTAPFCSWFQGVLGILRCRAIAWLQS
The following text describes a protein:
Function:
Endonuclease that is involved in the suppression of homologous recombination and thus may have a key role in the control of bacterial genetic diversity; Acts as a ribosome collision sensor, splitting the ribosome into its 2 subunits. Detects stalled/collided 70S ribosomes which it binds and splits by an ATP-hydrolysis driven conformational change. Acts upstream of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation. Probably generates substrates for RQC.
Sequence:
MREKDLIKLEFDKVKEVLASYAHSPATKEKIQNLKPYTNKEKVKEEIELSKAFFDIAENVRLFEFEDIRELLKKAKLQGAILGVEDILKILNVINLTKEIRRVLSSHVQRLEPLRKVYKKLYTFSPLENLIIGSIDPRGFVKDEASEELLRVRKSIRAVEEEIKKRLDNLINRPDSAKFLSDRIVTIRNGRYVIPVKTSHVKKIFGIVHGTSSSGYTTYVEPQFVIHLNNKLTELKQKEEEEVRKVLQRITEYIGDYAKELLESFEACVEVDFQQCKYRFSKLVEGSFPDFGEWVELYEARHPVLVLVKEDVVPVGILLKEKKGLILTGPNTGGKTVALKTLGLSVLMFQSAIPVPASPNSKLPLFEKVFTDIGDEQSIEQNLSTFSAHVKNMAEFLPKSDENTLVLIDELGAGTDPIEGSALGIGILEYLKKKKAWVFVTTHHTPIKLYSTNSDYYTPASVLFDRETLKPLYKIAYNTVGESMAFYIAQKYGIPSEVIEIAKRHVGEFGEQYIKAMEKLSDYVKKYEEEFRKLEELRKELQKEKEEVEKLRKEYEEAKRKGWKEAYKEAREYLRKLVQESEEIFKKAKEKKEIKEFVSKKREEIENLAPQKPQKLEVGDLVEFMGKKGKVLEVKGNKALVLVDHLRMWLDTRELQKVGKAEPQKETKVTVQTPVMEKRDTLNLIGKDVETAVRELEKFIEEAYSAGYKVVKVIHGIGSGKLKSAVREALSKNEKVKFFRDAYPKEGGSGVTVVYLEYGEET
The following text describes a protein:
Function:
Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation.
Sequence:
MATDRFIVEVEKGKEGVDGGSPSVGSVYRSIYAKDGFPEPADDLLSCWDIFRASASTPPEHHQRDPRSSELRSRQASNEPITRGALQASALRNQKPAKANLKETPFPETRAGDGGSEQASTSRKPPPLNMQAAPSPPVTSRRTRRCSTNRATVRDSGGTRGRTRRSMTGRRRRSDGKPLRRTKKGLRRRHGRSRADRTPVPKTDLTSLSFLSLSFKIDLSAEKSPDNPMLGRREIVDGKAGKYVWQTYKEVYDIVIKLGNSIRTIGVGKGEKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAIEFIICHAEVSLAFSEEKKISELLKTAPNSTKYLKNIVSFGEVSNVQRAEAERHGLSIYSWDQFLKLGEGKHYELPEKKRSDICTIMYTSGTTGDPKGVLLTNESIIYLLEGVKKLLKTINEELTSKDVYLSYLPLAHIFDRVIEELFIYEAASIGFWRGDVKILVEDIAALKPTIFCAVPRVLERIYNGLQQKLSDGGFLKKTLFNFAFNYKHNNMVKGKAHEQAAPIFDKIVFKKVKEGLGGRVRLILSGAAPLAAHIESFLRVVACAHVLQGYGLTESCGGTFVSIPNELQMLGTVGPPVPNVDIRLESVPEMGYDALASKPRGEICIRGKTLFSGYYKREDLTQEVFIDGWLHTGDVGEWQPDGAMKIIDRKKNIFKLSQGEYVAVENLENIYSHVAAIESIWVYGNSYESYLVAVVCPSKIQIEHWAKEHNVSGDFETICQNQKTKEFILGEFNRVAKDKKLKGFELIKGVHLDTVPFDMERDLITPSYKKKRPQLLKYYQKEIDEMYNKTKN
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Miscellaneous:
MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester formation; MISCELLANEOUS: Present with 7380 molecules/cell in log phase SD medium.
Sequence:
MSENNSHNLDEHESHSENSDYMMDTQVEDDYDEDGHVQGEYSYYPDEDEDEHMLSSVGSFEADDGEDDDNDYHHEDDSGLLYGYHRTQNGSDEDRNEEEDGLERSHDNNEFGSNPLHLPDILETFAQRLEQRRQTSEGLGQHPVGRTLPEILSMIGGRMERSAESSARNERISKLIENTGNASEDPYIAMESLKELSENILMMNQMVVDRIIPMETLIGNIAAILSDKILREELELQMQACRCMYNLFEVCPESISIAVDEHVIPILQGKLVEISYIDLAEQVLETVEYISRVHGRDILKTGQLSIYVQFFDFLTIHAQRKAIAIVSNACSSIRTDDFKTIVEVLPTLKPIFSNATDQPILTRLVNAMYGICGALHGVDKFETLFSLDLIERIVQLVSIQDTPLENKLKCLDILTVLAMSSDVLSRELREKTDIVDMATRSFQHYSKSPNAGLHETLIYVPNSLLISISRFIVVLFPPEDERILSADKYTGNSDRGVISNQEKFDSLVQCLIPILVEIYTNAADFDVRRYVLIALLRVVSCINNSTAKAINDQLIKLIGSILAQKETASNANGTYSSEAGTLLVGGLSLLDLICKKFSELFFPSIKREGIFDLVKDLSVDFNNIDLKEDGNENISLSDEEGDLHSSIEECDEGDEEYDYEFTDMEIPDSVKPKKISIHIFRTLSLAYIKNKGVNLVNRVLSQMNVEQEAITEELHQIEGVVSILENPSTPDKTEEDWKGIWSVLKKCIFHEDFDVSGFEFTSTGLASSITKRITSSTVSHFILAKSFLEVFEDCIDRFLEILQSALTRLENFSIVDCGLHDGGGVSSLAKEIKIKLVYDGDASKDNIGTDLSSTIVSVHCIASFTSLNEFLRHRMVRMRFLNSLIPNLTSSSTEADREEEENCLDHMRKKNFDFFYDNEKVDMESTVFGVIFNTFVRRNRDLKTLWDDTHTIKFCKSLEGNNRESEAAEEANEGKKLRDFYKKREFAQVDTGSSADILTLLDFLHSCGVKSDSFINSKLSAKLARQLDEPLVVASGALPDWSLFLTRRFPFLFPFDTRMLFLQCTSFGYGRLIQLWKNKSKGSKDLRNDEALQQLGRITRRKLRISRKTIFATGLKILSKYGSSPDVLEIEYQEEAGTGLGPTLEFYSVVSKYFARKSLNMWRCNSYSYRSEMDVDTTDDYITTLLFPEPLNPFSNNEKVIELFGYLGTFVARSLLDNRILDFRFSKVFFELLHRMSTPNVTTVPSDVETCLLMIELVDPLLAKSLKYIVANKDDNMTLESLSLTFTVPGNDDIELIPGGCNKSLNSSNVEEYIHGVIDQILGKGIEKQLKAFIEGFSKVFSYERMLILFPDELVDIFGRVEEDWSMATLYTNLNAEHGYTMDSSIIHDFISIISAFGKHERRLFLQFLTGSPKLPIGGFKSLNPKFTVVLKHAEDGLTADEYLPSVMTCANYLKLPKYTSKDIMRSRLCQAIEEGAGAFLLS
The following text describes a protein:
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MVTAVSPENLKEWHTPSTRPDVIHELIHGVDRYNPSNLPFMEDYLATELKEGQYDLFGNLAILKLYQFNPQHSNPDVIINILIKALAATVSGPDFNLCLEMLREPSAILHDIESADEALVIVMPYLQRLHELSRTCQFTKFWQEINSDSEAAKILRTRYLPQHASPLDDFRFIFSASIASCFRRISLSQLSRWLDIPSDKVGEWCSKVEWTVEGQDAVIPNNGQNDVKAGVVKENVQLGQLTKLVAAAGY
The following text describes a protein:
Function:
Enzyme with a broad specificity.
Subcellular Localization:
Membrane; Peripheral membrane protein.
Sequence:
MGPYLSQPNKNKTTTSGEGKSIIFAASEMQGWRNTMEDAHIHVCDLQQDLSIFGVFDGHGGKEVAQFVEKHFIEELQKNKNFKDQKFEDALRETFLKMDELLLTPEGQKEIIQIKGGDDEASYAGCTANVALFHKNVLYVANAGDSRSVLCRNNTNYDMSVDHKPDNYEEKSRIERAGGFVSDGRVNGNLNLSRALGDLEYKRDSKLRSNEQLIIALPDIKKVELNQTDKFLLMGCDGVFETLDHQDLLKFINQKLGNQQITPQLLGRVAEDLLDNLIAPDTSAGTGCDNMTTLIIYLKGK
The following text describes a protein:
Function:
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain.
Sequence:
MTSKTVEIVNETGLHTRPGNEFVSLAKTFSSQISVENEAGVKVNGTSLLKLLSLGIKKGSKITVYADGEDENEAVDKLSSLLENLKD
The following text describes a protein:
Function:
Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Sequence:
MKQTVYIASPESQQIHVWNLNHEGALTLTQVVDVPGQVQPMVVSPDKRYLYVGVRPEFRVLAYRIAPDDGALTFAAESALPGSPTHISTDHQGQFVFVGSYNAGNVSVTRLEDGLPVGVVDVVEGLDGCHSANISPDNRTLWVPALKQDRICLFTVSDDGHLVAQDPAEVTTVEGAGPRHMVFHPNEQYAYCVNELNSSVDVWELKDPHGNIECVQTLDMMPENFSDTRWAADIHITPDGRHLYACDRTASLITVFSVSEDGSVLSKEGFQPTETQPRGFNVDHSGKYLIAAGQKSHHISVYEIVGEQGLLHEKGRYAVGQGPMWVVVNAH
The following text describes a protein:
Function:
Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. It may be involved in the development of some ectoderm-derived structures. Acts as a negative regulator of type I interferon production via the complex formed with VCP and NPLOC4, which binds to RIGI and recruits RNF125 to promote ubiquitination and degradation of RIGI.
Sequence:
MFFSFNMFDHPIPRVFQNRFSTQYRCFSVSMLAGPNDRSDVEKGGKIIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKFQPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDFDAPLGYKEPERQVQHEESTEGEADHSGYAGELGFRAFSGSGNRLDGKKKGVEPSPSPIKPGDIKRGIPNYEFKLGKITFIRNSRPLVKKVEEDEAGGRFVAFSGEGQSLRKKGRKP
The following text describes a protein:
Function:
Thiol-dependent isopeptidase that specifically cleaves UFM1, a ubiquitin-like modifier protein, from conjugated proteins, such as CD274/PD-L1, CYB5R3, DDRGK1, MRE11, RPL26/uL24, TRIP4 and RPL26/uL24. While it is also able to mediate the processing of UFM1 precursors, a prerequisite for conjugation reactions, UFSP2 mainly acts as a protein deUFMylase that mediates deconjugation of UFM1 from target proteins. Mediates deUFMylation of RPL26/uL24, a critical step to release the UFM1 ribosome E3 ligase (UREL) complex during the recycling of 60S ribosome subunits from the endoplasmic reticulum. Catalyzes deUFMylation of TRIP4, regulating intracellular nuclear receptors transactivation and thereby regulate cell proliferation and differentiation.
Subcellular Localization:
Endoplasmic reticulum. Cytoplasm. Nucleus.
Sequence:
MVISESMDILFRIRGGLDLAFQLATPNEIFLKKALKHVLSDLSTKLSSNALVFRICHSSVYIWPSSDINTIPGELTDASACKNILRFIQFEPEEDIKRKFMRKKDKKLSDMHQIVNIDLMLEMSTSLAAVTPIVERESGGHHYVNMTLPVDAVISVAPEETWGKVRKLLVDAIHNQLTDMEKCILKYMKGTSIVVPEPLHFLLPGKKNLVTISYPSGIPDGQLQAYREELHDLFNLPHDRPYFKRSNAYHFPDEPYKDGYIRNPHTYLNPPNMETGMIYVVQGIYGYHHYMQDRIDDNGWGCAYRSLQTICSWFKHQGYTERSIPTHREIQQALVDAGDKPATFVGSRQWIGSIEVQLVLNQLIGITSKILFVSQGSEIASQGRELANHFQSEGTPVMIGGGVLAHTILGVAWNEITGQIKFLILDPHYTGAEDLQVILEKGWCGWKGPDFWNKDAYYNLCLPQRPNMI
The following text describes a protein:
Function:
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Sequence:
MEEQGNKIRILDRDTINKIAAGEVIERPASVVKELVDNSIDAGATEIRIEVEKGGKHSILIRDNGCGMSKADALLSYEKHATSKLTRIEDLDTVSTMGFRGEALASITAIAKVEILTRPPEELTGTKLVIHGGKVQETSDAGTAPGTSVYVKELFYNTPARRKYLKSDRTELAHITDTVTRLALANPGISFTLLSEGKPVIRSTGSSDLFKSLVNLLGPDTARSMLPLEYRTEDFEIRGYVSKPETNRGGSDQLYVFVNTRPVTSRAINMAVREGYYTKIPKGRYPVAVLALTLNPEEVDVNVHPRKAEVRFSREKEVGDAVIRAVEKVLSEHGLAPEVREKEGKRLQKTFEDPGLSEKIQPQETPATLPEKAAGKEIGVREEAKVSENSRLLKEKSEAYTYPIKDTERRLKKSERLLDSDGKAGIQDGLKKVEPASKKEEEKVNERIKAEEKQSQKLKPKANTDLLEDLRIIGQVSKMYILAEKGEDLVIIDQHAAHERVLYEQVLRTKKARVQELITPVMIELTPKERVLMEEYIPHLEEYGFGISEFGDNTYVVTFVPEVFGRLEDTGVIHDVISDLLAEGKVKKDTGISEKVSKTLACRAAIKGGAACNTRQMEELIEQLKAAESPYSCPHGRPTVITFTKGELDRMFARTQ
The following text describes a protein:
Function:
Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation.
Subcellular Localization:
Nucleus.
Sequence:
MASTPPSPLKQQENSANSLSSVHEKQSSLSLPPNVRHSPHNQDPVVSPPPPEDLWHLPGRLRINPSLWDKEDVALWLHWAHKEYSLQRAEKGRFEMNGRALCLLTKEDFRRRCPSSGDVLYEILQCVKQHRRGVVCETPIVSLGSSGNIQSEVSCPVPFGTVPEQQSVTISDNSVSTVATTAVSAALTATVSSRPETLLRNPLTLVSYPAYNNGSVVLSVAPNNQVACLPQTESIPQEPLNLSGREKPRSPVHKANGRIPRCRLLWDYVYQLLCDDRYRDYIRWEDEDSLIFRVVDPNGLARLWGNHKNRENMTYEKMSRALRHYYKLNIIKKERGQKLLFRFLKLPQDILEQQGDAPVSPDHTPPPDELSDDHFEVSPDRASPQPPTGAPVT
The following text describes a protein:
Function:
As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors.
Subcellular Localization:
Mitochondrion.
Sequence:
MGLPFLCHTRVCLFSNKIPFVLCGSRFAPATLHAHHTAAGGGETLNFPELSSPSTSKEPSVGSDSPQKKNKKQAFDALARWCGGHQQLLMRIQQSAEDTSAGVVFETPLTEVDSAAIRWLQGSTEQLTCGQSLLVCSFVCEVLYCQLNSASGGIGVEEAQRLQIHALTNRIAALLQRADESNKLESQPLSVLMSCAYVVQRLKYVDNPLFGETQRSLVKVPPSIMFALLHKLRGDGLGKLFQLDERTATDVCLSFLFIATEEHRQAFFSSGDAALVSNVLRRLVRYTASKTRRMRIQKEGDIIDLLTVDSPSDGGARQTPVCTSGTGFTSPSMRECAMIMQNVSFSSPSNRLELLLYLLCVRRNLAQCSLKDIELVPTVLSTVANIRSAEACSIRKKIISQLWLPENNPTLVAQLLVHSGESIPRYVTYLQGVPASKLSPRDAAQVILCAGTYLSYESLQLYIMAALRDIMPSSSLVTLGAETTSASVPATASVPTRVPACDSLETVLSVLLMRVEEKGGSLSEVEKDACMEYIRRLNELIDWCASAPTSSPKPALQRLTLLTKLFNRGLVVHAPETVVELAVQSLQLDPGNTMMNTLKCVSEALPLVSDDKKRSIIIEKMISYSGTRTTSSVIRFLLLLAPLVDADSPHSCELVEQLLKFHTLNPHKLRQASVEGVAKGIDVYTLLLINGIDFLLASGDWRSSPSQLQNVITTWVRDYTLYVMDPARKQKIDDGAAAHVAPATKGEKTDVVQHQQPSRLNEGGELPTLSGPNDEELEQVFTCLLRAGVKLPHAFSSELLSRIRRLQAKRNPADGTDQQVVFPLPAHFVFCCKLDVPVEVSVTPEMMKYHIDACDYRIIHCVITAFFSAAGTFKHNINDLLLCNMRLASRSFELFIQRLGEEASRSFRPATVSSVVANTLRFVVNHITKQERCQRVLRKLNEKGGIEAGEEELEGDRSLIAEHTRLGELLTRMIAYLSGAHVKNVGLSVLDRLSLLSPACGEYLMMRLSTQLSEFTQVELLYLVQKYPKSQDLVAELLGKSDLVSSMDFGDYMRVMRNLPMPINALVIGAHLPGLNFQWCTRILSSLSVRHESVPLHLLASVLRRLNDVTESATLTDRNIAFVVLQKYLQFDQTSGDGGDLEERQRLIKCSCDKLLVLSRINSLDTLKEFLVEFPEALSGVICESLSKHVVQHIVGGLLKDLDGLLTLCRLLHRHKLLTSDVKVAIVDGFFMKTLQSEVEGRANIEGESSQGLQPLNSVRGASLKTTHPVSNVLALALLLSDGPLHFPGASNSSSTICGDNERCAVSSMFQVVKESYTSPRDRLLIANTLVGQKGPNALTVVAKEICTELIENCESVTSNDFSRLLQCISRLKCWSELDLANSRFDEVFQRSCTQADAHSRCVAFRAVSFEADIFRRYESFMIPLLQETVDVMSNEDLETVLSSVLSLPFTEALESLIDAIGTRLLRMIDQCRRSALIRLLQCHAAFGIQDDALVSVCVATLTDQCGRDFRLDTAQVLALLQAAVDLDFFLPPKLVTSCFTWLEHHVENMTITQLGHAVRLAVDVEVGYTAAVHTLTLRALEQRDAIRSNASFREAVEMLCDEFSAEIPWHLRAPVLRRRYQSERLLEYLDKRRLAVDSTVA
The following text describes a protein:
Function:
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix, basement membrane.
Sequence:
MTGGERAARALRPRGRLWPLLAVLAAAAAGCARAAMDECADEGGRPQRCMPEFVNAAFNVTVVATNTCGAPPEEYCVQTGVTGVTKSCHLCDAGQPHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPNSINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGGDEQQALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGGRCKCNGHASECVKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPWRRATAESASECLPCDCNGRSQECYFDPELYRSTGHGGHCTNCQGNTDGANCERCRENFFRLVSHEACSPCHCSPVGSLSTQCDSYGRCSCKPGVMGEKCDRCQPGYHSLTEAGCRPCSCNPAGSIDECNVETGRCVCKDNVEGFNCERCKPGFFNLESSNPRGCTPCFCFGHSSVCTNAVGYSVYSITSTFQIDEDGWRVEQRDGSEASLEWSSERQDIAVISDSYFPRYFIAPAKFLGKQVWSYGQNLSFSFRVDRRDTRLSAEDLVLEGAGLRVSVPLIAQGNSYPSETTMKYVFRLHEATDYPWRPPLSPFEFQKLLNNLTSIKIRGTYSERSAGYLDDVTLTSARPGPGVPATWVESCTCPVGYGGQFCEMCLSGYRRETPSLGPYSPCVLCTCNGHSETCDPETGVCDCRDNTAGPHCEKCSDGYYGDSTTGSSSDCQPCPCPGGSSCAVVPKTQEVVCTNCPTGTTGKRCELCDDGYFGDPLGRNGPVRLCRLCQCNDNIDPNAVGNCNRLTGECLKCIYNTAGFYCDRCKDGFFGNPLAPNPADKCRACACNPYGTVKQQSSCNPVTGQCECLPHVTGRDCGACDPGFYNLQSGQGCERCDCHALGSTNGQCDIRTGQCECQPGITGQHCEHCEVNHFGFGPEGCKPCDCHPEGSVSLQCKDDGRCECKQGFVGNRCDQCEENYFYNRSWPGCQECPACYRLVKDKVADHRVKLQELENLIANLGTGEEVVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNSTLSSQISRLQNIRNTIEETGNLAEQARARVESTEQLIEIASRELEKAKIAVANVSITQPESTGDPNNMTLLAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLKTLAGENQTALEIEELNRKYEQAKNISEDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALENEANKIKKEAEDLDHLIDQKLKDYEDLREDMRGKELEVKKLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRNTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINQTIIEANEKTREAQLALGNAAADATEAKSKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKKKQDDADQDMMMAGMASQAAQEAEINARKAKNSVTSLLSLINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEARKQEAAIMDYNRDIEEIMKDIRNLEDIKKTLPTGCFNTPSIEKP
The following text describes a protein:
Function:
Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MEVPIAAMTFAHPANVMTLASRQPKSKRSHISPATTAHRNLQTRLAHHHHATPASLPMAICNTVDKVINRFIDLPEQRPTVDPRRVLSGNFAPVDELPPTSCHVIRGSIPSCLAGGVYIRNGPNPQHRLPQRTHHLFDGDGMLHSLLIPSASSTLLSEPVLCSRYVHTYKYLLERETGGPVLPNFFAGFHGVAGLARAVVMIARVLAGQINLNKGFGLANTSITLFADCLYALCESDLPYSMHINPANGEVTTLGRCDFGGDLSFRMTAHPKKDPVTMELFAFRYNVFQPFITYFWFDRAGSKVADVPILSLQKPSVMHDFAITERYAIFPESQLIVNPMDMVMRGSSLVGLDRTMVPRIGVLPRYAKDESDMRWFEVPRFNMLHTTNGWEEADGEEIVLVAPNILSIEHMLGNMELMRARVDMVRINLCTGDVSCTALSPESLEFGVIHQGYVGRKNRYGYFGVSGPLPKIKGIRKLDFDLVGSGDCTVGRRDFGLGCFAGEPFFVPDNIDGYGNEDSGYVVCYTHEEDTGESWFVVMDAKSPELDIVAEVQLPSRIPYGFHGIFVKQAELLAQQ
The following text describes a protein:
Function:
Synthesis and degradation of fructose 2,6-bisphosphate.
Sequence:
MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCALAALRDVKSYLTKEGGQIAVFDATNTTRERRHMILNFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRINCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEYNLQGKIGGDSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVSTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEERVASTSAALPSCLPPEVPTQLPGQPLLGKACLRSVCHIFSKFSPY
The following text describes a protein:
Function:
Inhibits osteoclast formation.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MNITRASLPMLNTTCSCRREKWNFLGRYEGTFDYWIGLHRASSKHPWMWTDNTEYNNMFVYHMNAQCLKKPEEGESSPGTGGVHSYKILQRNSLRAISPESSAKLYCCCGVIMVLTVAVVALSVALPATKTEQILINKTYAACPKNWIGVGNKCFYFSEYTSNWTFAQTFCMAQEAQLARFDNEKELNFLMRYKANFDSWIGLHRESSEHPWKWTDNTEYNNMIPIQGVETCAYLSGNGISSSRHYIPRIWICSKLNNYSLHCPTPVPV
The following text describes a protein:
Function:
Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins.
Miscellaneous:
MISCELLANEOUS: Target of the antifungal compound 1-[4-butylbenzyl]isoquinoline that inhibits cell wall localization of GPI-anchored mannoproteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSTLKQRKEDFVTGLNGGSITEINAVTSIALVTYISWNLLKNSNLMPPGISSVQYIIDFALNWVALLLSITIYASEPYLLNTLILLPCLLAFIYGKFTSSSKPSNPIYNKKKMITQRFQLEKKPYITAYRGGMLILTAIAILAVDFPIFPRRFAKVETWGTSLMDLGVGSFVFSNGIVSSRALLKNLSLKSKPSFLKNAFNALKSGGTLLFLGLLRLFFVKNLEYQEHVTEYGVHWNFFITLSLLPLVLTFIDPVTRMVPRCSIAIFISCIYEWLLLKDDRTLNFLILADRNCFFSANREGIFSFLGYCSIFLWGQNTGFYLLGNKPTLNNLYKPSTQDVVAASKKSSTWDYWTSVTPLSGLCIWSTIFLVISQLVFQYHPYSVSRRFANLPYTLWVITYNLLFLTGYCLTDKIFGNSSEYYKVAECLESINSNGLFLFLLANVSTGLVNMSMVTIDSSPLKSFLVLLAYCSFIAVISVFLYRKRIFIKL