lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex is a core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built.
Subcellular Localization:
Nucleus.
Sequence:
MEHSEMEFIAEKQKVKIVPNFSMSKIYFISGEVGPFQPGLPTEVPFWLAISLRQRQKCVIHPPDWLTIERLEEIKEAETTTELFTPLPNTHFREMCQLLLTHAKPNIQNADAVRTLVKDIWDIRAAKLRSSSDKFIRVQAGHARIDNLTLMEINIARPFLLASLDHLHTLRTSKQFTKKTRNKEY
The following text describes a protein:
Function:
Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MRVTIVLVAPARAENIGAAARAMKTMGFTDLRIVDSQAHLEPATRWVAHGSGDIIDNIEVFHTLADALHDVDFTVATTARSRAKFHYYASHAELVPLLQEKSRWMRHAALVFGREDSGLTNDELALADVLTGVPMAADYPSLNLGQAVMVYCYQLAGLMQQTTESVDIADESQLQALRARLLRLLTTLEAADDHKLTDWLQQRIGLLGQRDTVMLHRLVHDIEKKLTK
The following text describes a protein:
Function:
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Subcellular Localization:
Nucleus.
Sequence:
MQDEDHPASALVNRYLELSAGQITPSESQNITQELSSWVQKEPQTHLLLVIQASRLGLTSESDTTRAHANRLLARLVHALIDYKSLSKTQVNLLVEFFVEKLDDGPSIVVEALAALRSLSRSDNFQAEHAIKCCNAFVFSSTLPHAFLRVQLTPLPPNSLFQHLSIRDLEQPKRLAVLMLVDNLLAYHRDALQSMGSEFLSGYCTLVEGEKDPRNLVVAFKLAKVILTEFDLGDQAESLFDITFCYFPITFKPPPGNPDAYGGITAEELTQGLIDCLSATPQFGILVLPLLLEKFQAPGLGPKSQVLETVIQAFPIYGRAAVAEFASLFWESFLVEIFQPNTSPSQDFLRLLERACQTLFSTVFPAEVEFSPSGPLDFIKQALEVVMKELHSPEKSRAVPATRLVGWIVESGANVTDVILPTIDTSVGTLLHLWKATKTATGDDVLLKRTSILGHLSTIFSSIGAVTSKQATSVHLSISQWLTSSLRHDILSILIKEVLENASCTDPLLQVAALRTLVNFVGIPDTLEMHEANDVIGTVTRLLLSSDENEITNAVIENLSTIADSHPAAVASVTLPELFSKLPSANHLPSVEASPPIPPVTSAKYITILDGLASLCDRATLFDSFLVRLFDALESSCNAAFQVSVKEFLSLSDGNNRNQPFDYRAYSHHLLICLHTVIQAKINSFNATLKSPASDMEECAVTATQARGIIGRLFEILLCEGHALENLPAEGGGEASGVRRDVDLNAIREHCTIRNDKRIVINAGQIINSLMGQLDFHLGNVTEIVAESRNLSSASSATRSCKIERGFLPMSVDAPDPDKNMLALYVEALIAIRPGYYHFISQTGSPNPVALQASLRLLCSTLDQFWASEIEASRLTRPRSRKLAIMMWIWIIKGLVVRSDPRGYTMLDRICGLLKEDGELKGWIAKRLAVVVDHKDETISPKNFAVIKVEHSPPSSTVVCFRLDTNSIWDDAQFLSMQRACHYLIGRLVRDYAEANEDSRWVYLVGLATLLARVGSSVTSLQHEKIIPLLLEALKLPDVDVKLDSLVTIHDLIENDKRGTVFENHLSSLVSALLINCTFGRGSINGEDRSKTPNDSAPKTGGTSASVRLFALKILALLPSKAGHPSSSTPGPSPPPSGLPSNVAKGVLQGQRNKVLLALSSALDDPKRDVRKIAVDCRAYWFSLNLT
The following text describes a protein:
Function:
Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCPGPVYGFIFLFKWIEERRSRRKVSTLLDDTSVMEDEVVNNMFFAHQLIPNSCATHALLSVLLNCSGVHLGPTLSRIKEFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGISAVRTMEAFHFVSYVPIKGRLFELDGLKVYPIDHGPWAEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRLKYESKLNILKMNRQTVLEALQQLIRVTQPELIQAQKPTDSLNTEETKSPALKGPVSQESHRAHPASHRSATGTEPAGALLRGPVMSAYSKSNPLPQNGGNVPVPASRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRGVPPPAPDTDEEEEEETKNVRRTLTPPGFKRRSSESLPPPPGPEPGVLAEKLKETQRELCSPLSIKTGAPTAPHSQPSPTPSNESTDTASEIGSAFNSPLRSPLRSANPTRPSSPVTSHLSKVLFGEEEPLSRLDCVRYNRAVRELGPHISTGILHLSKDGYLCPLSRLGGKGPTDDTFTSANSDTGKVSPKNHKVEEPRESSEPDSERGRVTEAPQGEKFSPKELLALLKCVEAEISASEACLREELEKRKKFKIDDQRRTHNYDEFICAFISMLAQEGMLASLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ
The following text describes a protein:
Function:
Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893. MpaA is a Golgi apparatus-associated enzyme that catalyzes the prenylation of 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) to yield farnesyl-DHMP (FDHMP). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable).
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein. Note=Membrane association is functionally relevant because mpaA must ostensibly interact with its membrane-embedded substrate FPP.
Sequence:
MTNAVEDSGPRDLLFLLISTSRFNRYMPYYTMMAAESLSIEFILYKAGLCFVHCLLLCGAGNTWNDLVDRDIDARVARTKMRPLASGKVTLTEALLWMTGQYFLSVKMLDLILDGRNIWSLMLPLTASIMLYPYLKRPIFSKVFVYPQYILGLAIGYPAITGWASITGSEEPLGDIIKHCIPICLLVFFWCVYFNTAYSHQDSVDDRKMNINSAYVIAGQRIRLFLAFLSVLPLLTIPYIISTINSPWLWVSWMATWTVSIIMQIAQFDSQKLESGGRIHWDNFLLGLWTIAACMVEVGLQKVEFWKNVEGYIKL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
Sequence:
MISASSVLNDETLFLLKKFQKSNETTIIKTLDELKRNILLEPFISTKKEQQAFSLHFSNIFTTLSTHKSSNVRLNLFICLSDGILQSPQGKNMISFCISEIIPWWLLCCHDSVKEISEAAKKALNILSFEGRQKVITSNISQILRLVSSNEYDLISRMGCLATILPNINISKLSSYGKSHLENSIKSLIESYGSITNEVYFSSIDAALITCNFIVMERFESLKNIIVKTIDELQPFSKYSKQLFLCITSLLENGAIFNEEFYNKIIQYISTACLGSLYVFPTLKRLLPFIKEKELEKKYIEGVFKAIGDSHIRGPQRAVVILHYFESIKYFKYTNINELIEIMKLLLNDPGSIMIDSGYSSMGIFLTKLNETKEIQGVLSSAVTYLRRSEEKEYLIHLNCMKFIVDKCIKNEFTQGFSYDLLKTIIDKNENDHFFNDNEIDLIIFILQKYPATEEVHQMIVRQFQHIFMLSIEENINEFDIINDTVEINDEFLSYVIKMEDLLIQSISFEPSTSIGYLLNQMFFNLFPKHYALNHLNYLRLFINKLKEQQFIQTIVLQINPLIQLLLHSFKSSKDIVQSIISISPRLLTPQQLTELLFTNSINHLQVLLNVDLINYLIKSTINSKELLLHIIKSITSPDIFLPIHQPIRNVLLKLLPSLISYIGIEPIHEMLKSLLLSPNCTSFCISLTSEIPPLRNLLINDIKLLLPLSSFISLIPSYAQNIKSPLLIPMPFINSSEYPHYNNTLSLLVKLYHLNNEEIKEDNEYIEYWLFDSYQKLTNRISVEIPHLQQLILLQYLFKKNEIEQYLIFHIINQLSSWINLSKESIEYLAHLFDSSTSYSIRFFLSTYLSPLHIDWLEKKVNIIIKKFFMVNTQSDPQGLKELSILYPLIFFPTHLKMVFKYIFSLEITSELELPFLHILHYVFSSSCSLCFESLENEESLSLIYQFLLKILTSSVSSNLMKRGALQVSQILITHSLPPKLLTSESEGIQLSFKISLIDFIVNSIINKSNTQLISELLLQTDLLAEIDFMSDSMRKYIPELFKILKGKDSIIVKICTGYLIGASMNFKSDETFIDFDDNEQQKYHPLPPSLEEYLDKAIESFSQFNTLNKTTLIIFILGMLRKIKDSSTEYRSWIVAYLQAHHFELFINNLYTLLPDQHVPLTLSSVLSLLHSFINGEDEDENQLLTKQNENQILNILASYCMFVIVQSFPNVVRQWCLSLRKSAPKMVKKFFERNICPFILQEEVQKILSWKETDDFILRLQLDGKAVTVVYKNDELVFESQLIFPSTYPLDMITVNVASNKVSVSEAKSHLYKRMLTMNLMTRDLGIIDACLLWKQQLDRQFDNSDACPICYSLFYLRTTTIPNVACKCCRKKFHKQCIFGWFRSTGRHDCPLCTRNFYGENKN
The following text describes a protein:
Function:
Involved in the degradation of plant cell wall polysaccharides. Catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a large preference for the latter, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc).
Subcellular Localization:
Secreted.
Sequence:
MKPHALIGLLAGMLLSSSLYAADSTKPLPLHIGGRVLVESPANQPVSYTYSWPAVYFETAFKGQSLTLKFDDDQNIFRLIVDDKAPVVINKPGKVDYPVESLAPGKHRVRLEKLTETQSTSGRFLGFYTDPSAKPLALPKRKRQIEFIGDSFTVGYGNTSPSRECTDEELFKTTNSQMAFGPLTAKAFDADYQINASSGFGIVRNYNGTSPDKSLLSLYPYTLNNPDQLYHNKHWKPQVIVIGLGTNDFSTALNDNERWKTREALHADYVANYVKFVKQLHSNNARAQFILMNSDQSNGEIAEQVGKVVAQLKGGGLHQVEQIVFKGLDYSGCHWHPSANDDQLLANLLITHLQQKKGIW
The following text describes a protein:
Function:
Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system (Probable). Seems to be important for the virulence.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKHNGQLRIGYVPQKLYLDTTLPLTVNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAPEVVSMHPEFISMFGPRGAEQLGIYRHHHNHRHDLQGRIVLRRGNGHS
The following text describes a protein:
Function:
High-affinity manganese transporter involved in manganese uptake from the extracellular environment. Also contributes to cellular accumulation of other divalent metal ions such as cadmium, cobalt, copper, iron and nickel.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=In presence of excess manganese, targeted to the vacuolar lumen, where it is degraded.
Sequence:
MVNVGPSHAAVAVDASEARKRNISEEVFELRDKKDSTVVIEGEAPVRTFTSSSSNHEREDTYVSKRQVMRDIFAKYLKFIGPGLMVSVAYIDPGNYSTAVDAGASNQFSLLCIILLSNFIAIFLQCLCIKLGSVTGLDLSRACREYLPRWLNWTLYFFAECAVIATDIAEVIGTAIALNILIKVPLPAGVAITVVDVFLIMFTYKPGASSIRFIRIFECFVAVLVVGVCICFAIELAYIPKSTSVKQVFRGFVPSAQMFDHNGIYTAISILGATVMPHSLFLGSALVQPRLLDYDVKHGNYTVSEEQDKVKKSKSTEEIMEEKYFNYRPTNAAIKYCMKYSMVELSITLFTLALFVNCAILVVAGSTLYNSPEADGADLFTIHELLSRNLAPAAGTIFMLALLLSGQSAGVVCTMSGQIVSEGHINWKLQPWQRRLATRCISIIPCLVISICIGREALSKALNASQVVLSIVLPFLVAPLIFFTCKKSIMKTEITVDHTEEDSHNHQNNNDRSAGSVIEQDGSSGMEIENGKDVKIVYMANNWIITVIAIIVWLFLSLLNVYAIVQLGMSHGDIS
The following text describes a protein:
Function:
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
Subcellular Localization:
Nucleus.
Sequence:
MPKYYCEYCDIYLTHSSPVGRRQHIHGRKHISAKIEYFQNLLREEGITPQNFLGFLNNRNINNPLGNPMMNYMNPNMYMKYNPMKSYHSYSMRSSHPYRLNIHNNKYSRAGYVPPSHHKYSVNPMHNNYHQAHNNYSYPNSINPSNQINYSNNYGSNNFNNSNEFNKNMNEKDNINNNDIHDNKVKTDENDPINNDNLNNTRNFSYEENHYSTDHKKPSFLNPENSKEHIESDIS
The following text describes a protein:
Function:
Specifically promotes functional cell surface expression of olfactory receptors, but not of other GPCRs.
Subcellular Localization:
Cell membrane; Single-pass type III membrane protein. Note=Effective cell surface expression depends upon interaction with olfactory receptors.
Sequence:
MCTSLTTCEWKKVFYEKMEVAKPADSWELIIDPNLKPSELAPGWKQYLEQHASGRFHCSWCWHTWQSAHVVILFHMFLDRAQRAGSVRMRVFKQLCYECGTARLDESSMLEENIEGLVDNLITSLREQCYEEDGGQYRIHVASRPDSGPHRAEFCEACQEGIVHWKPSEKLLEEEVTTYTSEASKPRAQAGSGYNFLSLRWCLFWASLCLLVVYLQFSFLSPAFF
The following text describes a protein:
Function:
Essential for normal spermatogenesis and male fertility. Required for proper cell restructuring and DNA condensation during the elongation phase of spermiogenesis. Involved in the histone-protamine transition of sperm chromatin and the subsequent production of functional sperm. Binds both double-stranded and single-stranded DNA, ATP and protamine-1.
Subcellular Localization:
Nucleus. Chromosome. Note=In round and elongating spermatids, specifically localizes to a chromatin domain at the apical pole.
Sequence:
MAEAAQPTGESQGAELTIQIQQPVERALRTPVRRGAQSVLRVSQLLLRAIAGHQRLTLAALKKELGNAGYEVRRKISSHQAGDSTRSEKYTLLRVSGSDAAGYFRVWKISKPRRKAPRSRLTLGSHSHGKTVLKSPRPLRPRSRRKAAKKAREVWRRKARALKARSRRARSLARSMVRSRASSRASSRARSRARSRARSRARSRARSRASSRARSSARSSARSSARSSVRSSVRSSARSSARSSIRSRARSRARTRARSRAKDLVRSKAREQARTRAREQAHARARTHDCVRAKAQEYVRAKEQQYVSAKEQEYVRTKEQECAKAREQMRIGAMEEARIKAIDNRVQTTMEDTSPWSTDEMRSRTKPREEKRQEPERPVKQTNQKPAVVKVDNAPSRQGKTCTKSSTKSGHPGCSGTS
The following text describes a protein:
Function:
Probable oxidoreductase that may play a role as regulator of mitochondrial function.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MWRRSFSTLPKKKWDAVVIGGGHNGLTAAAYLARGGLSVAVLERRHVIGGAAVTEEIVPGFKFSRCSYLQGLLRPCIIRELELGRHGLKLLKRSPSSFTPCLDGRYLLLGPDQDLNHSEISKFSKHDADAYPRYEKQLERFCGFMDPLLDSTPPESLQSASSFNDKLSNKMYKSAFWARCLRQAVSLGHKDMVAFMDLLLAPASKVLNNWFESDVLKASLATDAVIGSTASVHTPGSGYVLLHHVMGETDGEKGIWSYVEGGMGSVSMAIANAAKEAGAEIFTNAEVSEILTEDSSIVKGVLLADGTRVESSAILSNATPYRTYVELVPTNVLPENFVSAIKNSDYSSATTKINLAVDKLPQFQCCNTNHSGPGPEHFGTIHIGAESMDEVHSACHDSENGLPSRRPVIEMTIPSTLDNTISPPGKHVINLFIQYTPYKPSDGSWEDPTYREAFAQRCFKLIDEYAPGFSSSIISYDMLTPPDLEREIGLTGGNIFHGAMGLDSLFLMRPVKGWSNYRSPLKGLYLCGSGAHPGGGVMGAPGRNAAHVVLQDLKRI
The following text describes a protein:
Function:
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Sequence:
MRCPKCGATKSSVIDSRQAEEGNTIRRRRECDECQHRFTTYERVEERTLVVVKKDGTREQFSRDKIFNGIIRSAQKRPVSSDEINMVVNRIEQKLRGRNENEIQSEDIGSLVMEELAELDEITYVRFASVYRSFKDVSELESLLQQITQSSKKKKER
The following text describes a protein:
Function:
Probable transcription factor. Involved in kidney development, acting synergistically with lhx1/lim-1 in pronephric morphogenesis during the tailbud stages.
Subcellular Localization:
Nucleus.
Sequence:
MDMHCKADPFSAMHRHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVDKIADYKRQNPTMFAWEIRDRLLAEGICDNDTVPSVSSINRIIRTKVQQPFHPTPDGTPVSTPGHTLVPSTASPPVSSASNDPVGSYSINGILGIPRSNGEKRKRDEDGSDGSGPNGDSQSSVESLRKHLRADNFTQQQLEALDRVFERPSYPDVFQSAEHIKSEQASEYSLPALTPGLDEVKSSLSASGNADLGSNVSGPQSYPVVTESFASHLYLKQEPHEASLTPFTPSSLASSGLADIQPFQMALTVDASTPTYSSFTHHGPPYGQFGSQPLIAGRDMSSTTLPGYPPHVPPTGQGSYPTSTLAGMVPGTNVSVHHSVQPVECCSCLSSSKPCLFHCRTGSGSEFSGNPYSHPQYTTYNEAWRFSNPALLSSPYYYSATSRGSAPPTAATAYDRH
The following text describes a protein:
Function:
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reduction of methionine sulfoxide in proteins to methionine. Does not catalyze the reverse reaction involving the oxidation of methionine residues.
Sequence:
MSLTITSSVTHPELKDLSTVRNEQKELNISPVHDVNVTKATATFGMGCFWGAESLYGATRGVLRTTVGYAGGSSDLPTYRKMGDHTEVLEIDYDPTVISFKELLDLFWNNHEYGLTTPIKRQYASLILYHDEEQKQVAHASKLEEQERRAPEIITTEIASKENFYPAEAYHQKYRLQGHKDLASSLNLSPKLLQTSYVATKLNGYLAGVGGIEQFKAEAETMGLTPTQRQYCYYHVEQNEGQGLYC
The following text describes a protein:
Function:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the first dolichyl beta-D-mannosyl phosphate derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-dolichol to produce Man(6)GlcNAc(2)-PP-dolichol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MPIVQESPKEVDTVLKNQSTNASTNTNTNKQQFRESPEFTLSNVLDDIKQGIIAFLINPKVTIIVYPIIICLSSILTKIVINKISYTEIDFITYMQQIKLINQGIIKYSEIEGDSGPIVYPGGFVQIYQFIQWLISSSSSSSSSTGEEILSYDVREAQYIFSYLFTTSIIFNCLIYINLINIPPWTIYLFLLSKRLVSIYVLRLFNDCWTTLAILGVILILQQASTNITEDWLVYLLVILASDLYSIAISIKMNALLYFPGFIIIVYFLLDESLIKSTSVLIVMIFIQIIMGWQFLLPLELFNNDVDVRRMASIIRWDYINQAFNFKRKFLYEWTVNWKFLSIETFTSDGFAKLLLLLHVFTLLVFIITRFLNSRITGKSITSLIYQIVLPFSSSSSSSKSSSSSNGNNSNLIKNPQSGPQLIFIIMSITNLIGILFARSLHYQFLSWYAWSLPGLLYLNFPIYFALPIWFVHEWCWNVFPSNSISSITLVSILSLIIGATWWNFDHWXPTISQFIIYF
The following text describes a protein:
Function:
Unknown. The enzyme has no activity toward sorbose.
Sequence:
MSKETTSYTNAKLGPLPTKAATIPDNILDAFSLKGKVASVTGSSGGIGWAVAEGYAQAGADVAIWYNSHPADDKAEYLTKTYGVKSKAYKCNVTDFQDVEKVVKQIESDFGTIDIFVANAGVAWTEGPEIDVKGVDKWNKVVDVDLNSVYYCAHVVGPIFRKKGKGSFIFTASMSASIVNVPQLQAAYNAAKAGVKHLSKSLSVEWAPFARVNSVSPGYIATHLSEFADPDVKSKWLQLTPLGREAKPRELVGAYLYLASDAASYTTGADLAVDGGYTVI
The following text describes a protein:
Function:
Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione conjugates.
Sequence:
MLHLSPLLCGLAVLGQLGSVVIAVPLEFKYQRVIQNISSEGHRGAVASESAICSQIGIDALRKGGSAADAMVATTLCVGTIGMYHSGIGGGGFMLVRDPDGNYHTVDYRETAPAAATQDMYNDDPNASVLGARSVAIPSELRGLEYVHSKYGRLPWHDLVMPSVKIAHDGFKVTEDLVRYMASASASDDFLTRDPVWAQDFAPNGTLLGLGDTITRKRYAKTLLKIALLGADAFYTGPIADSIIALLQPLGGILTHSDLANYEASIRPALNITYRDSFRIFATDAPSSGAVTLSILKTMEQFPSLNLSSNIPLTNHRFVEAMKFAYGARQSLGDPSFITNITSFQEAMLSPQSAKFISSKILPNSTLPLSEYDPVKNYAAASHGTSHIVTADRSGLTLSSTTTINLLFGSRLMTPDTGIILNDEMDDFSQPNKNNSFGFVPSPSNFIRAGKRPLSSICPLMVEHVSNGSLWFATGAAGGSRIISSTTQVAFNVLEGLAVHPNTTDLKVKGVGGEGSVMRAAVAAPRLHDQLMPEVLLVEKGYGQDVYDDLKRRGHNVTWQAPGLSAVQAVMRFGNGTFVAASETRQVNSGGFAV
The following text describes a protein:
Function:
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork.
Subcellular Localization:
Nucleus.
Sequence:
MSVSGDDFDDYFDDEIDDVIVPGTSDTVESVQTNNRPAKQSDISISQGNEEDEFQSPDRLSGNAVQFEDVERTSKYNVFIPKCKNVQENIFVTQLTQPPSPPEMIRGPRWKKPGPEPLAPEPATTRVGANHQSDQYHDEDKEMEAAIAASLRSFEEENGGDVPSTASGSTPARTAAAPCAAPKGTAADVPFDLDDIPDDAFDSDLSLSPPRSTSQATRGPPVQSQFRTNRPLGLRQSTLFDMAARNPDISSQRGEQIFSPPEKSEPPTHHKLNEEALNTWVYPTNLGKTRDYQFNIAQRGLFHNLLVALPTGLGKTFIAATIMLNWYRWTKSAQIIFVAPTKPLVAQQISACFQVAGIPRSETTMLTGEAAPGIRAEEWKSKRVFFMTPQTLVNDLKSGIADPKRIVLLVVDEAHRATGGYAYVEVVKFLKRYNKSFRVLALTATPGSTVESVQAIIDDLGIAKVEIRTEQSLDIREYVHARDTEVQTFQNSDEMVLCMELFTRTLQPLVDQLRNLNAYWGRDPMALTAFGLTKARQQWMGSDAGRNANLALKGKVNAIFTVLASLAHAIDLLKYHGITPFYRHLLHFQSNTDGQKGGKYQRQIVQDESFKKLMNHLQPWTKNPDFIGHPKLEYLKQVVLNHFMDRGEGTAANGDQSQSATRIMIFVHFRDSAEEVVRVLKRHEPLIRPHVFVGQSSAKGSEGMDQKTQLSIVQKFKKGTYNTIVATSIGEEGLDIGEVDLIVCYDSSASPIRMLQRMGRTGRKRAGNIVLLLMQGKEEESYIKAKDNYEKMQQMIASGTRFTFHDDKSPRILPPGVRPVAEKRQIDIPVENTQADLPEPRRRARPPKRPPKKFHMPDDVETGFAKASSLTGKVTKKAETKRAVRKPTPEPVEVPALEEVLLTPRQQQDLERRYCHIAGTSPEFIRNPRVDAYPRLQSVPRPTKAVKHGSLTSRMIGTLQKMGKVSVDCESRYRKVLALDSSKEIVDSVLSRDPWPPAKNSGRLGEKTHAFKRPSATPRPNNVHVREDENEDNCTPELVSPEKLMSSFLEPHTERPPYSSQRSQDAFELDFPDVETLLNRSAERHVSRKRNRFVLDDDSDE
The following text describes a protein:
Function:
Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1.
Sequence:
MASSSSSSSSSSSEKKIALKSSDGEALNVEKNVALEFEPVKGFLEDNSEGADDEAIVVPLPDVSAAVLSELIPYVKQRLELSAKPVQKKLIKAFDDQFTRHLSDDKLGELMLAANYLGVNYLLDVLCDVTADRIKNKSVKYVREFLGIQNDFTPEEEAELRAQCPWAFEGVDQD
The following text describes a protein:
Function:
Required for mobilization of iron from the bacterioferritin (BFR) complex, composed of BfrB and FtnA in varying proportions; mobilization requires the [2Fe-2S] cluster of this protein. Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR prior to its release as Fe(2+).
Domain:
The C-terminal 17 residues are not required for [2Fe-2S] cluster assembly, interaction with the BfrB bacterioferritin complex (BFR) or iron mobilization from the BfrB core.
Sequence:
MYVCLCQGVTDNQIRDAIYEGCCSYREVREATGVGTQCGKCACLAKQVVRETLNDLQSAQPVPAFGTTAFVAA
The following text describes a protein:
Function:
S-crystallins are structural components of squids and octopi eye lens. Contains relatively little if any GST activity.
Sequence:
MPTYKLVYFNGRARAETTRLAFAAAGIQYEDHRIERQQWPELKPKTFAGYLPYLEVDGKVLVESMAIARFVAREGKLAGGCSYEQAQIDSIVDILSSLLEKGFKVVYNSDPAEKVCKEFLEKTLPDVFKLLEKFLHDKHFFVHDKLSLADLHFYSVMESLAQVQKDWANVSPKLKALYDRVAAQPKIAEYLKKRPVTQF
The following text describes a protein:
Function:
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. In addition to the protease activity, also mediates delipidation of PE-conjugated ATG8 proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MRRIQERVLGYKTNVSNSISDIWLLGVCYKICLEDPSQEAVHSNGYAAFSEDFCSRILMTYRKGFVSIGDSKYSSDVHWGCMLRSSQMLVAQALLVHRLGRSWRKPLHQPFDRDYIEILHMFGDSEDSPFSIHNLVKAGESYALAPGSWVGPYAMCRRWETLIRSKIEKEGLQDKSFPMAIYVVSGDEDGERGGAPVLCIEDASRNCSEFQKNQTEWSPILLLVPLVLGLDKVNPRYLPLLAATFTFPQSLGILGGRPGASTYLVGAQDDKVFYLDPHEVQQAVNISKDDLEADTSSYHCNVIRQIPLESIDPSLAIGFYCRDKDDFDDFCSRASELAAESNGAPLFTVTQSRHSPKSSRSHEADFFDAADDAEGSAQDDWQLL
The following text describes a protein:
Function:
Component of the SKA complex, a microtubule plus end-binding complex of the outer kinetochore that stabilizes spindle microtubule-kinetochore attachments, promotes alignment of chromosomes at the mitotic spindle equator (chromosome congression) and assists suppression of the spindle assembly checkpoint. Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and spindle microtubules. The outer kinetochore is made up of the ten-subunit KMN network complex, comprising the MIS12, NDC80 and KNL1 complexes, and auxiliary microtubule-associated components such as the SKA complex; together they connect the outer kinetochore with the inner kinetochore, bind microtubules, and mediate interactions with mitotic checkpoint proteins that delay anaphase until chromosomes are bioriented on the spindle. The SKA complex is loaded onto bioriented kinetochores and it facilitates chromosome congression by stabilizing microtubules, and end-on attachment of the NDC80 complex to depolymerizing spindle microtubules, thereby assisting the poleward-moving kinetochore in withstanding microtubule pulling forces. The complex associates with dynamic microtubule plus-ends and can track both depolymerizing and elongating microtubules. The complex recruits protein phosphatase 1 (PP1) to the kinetochore in prometaphase and metaphase, to oppose spindle assembly checkpoint signaling and promote the onset of anaphase. Within the complex, binds microtubules but with a much lower affinity than SKA1 (By similarity). During meiosis the SKA complex stabilizes the meiotic spindle and is required for its migration to the cortex (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore.
Sequence:
MNPSERFFSKLRKLTVYLETESSSLLHTSQNLKEDEEDEETGAQALYQLHSEVRALKRQVRDQVATHDTSSADLRSFIRRCLVLKQRTTEDIDSLKKHYEKYGYRPRISRLGSTEVNCTKEAEERAERDAEKLDAAEEDEETERGDCDKVDQSVTPEKMPPPVDQLQTPKLSDFGLSALQFQRVLGEAEVPLSAAPESAIALSSPPILMNLQPPQPKTPKCSLSMEEDALTPRLEDFGISEYTMCWNNDFTMDLFNKKPPKNRSERNENVLKPHNVFSNTSSVLNKDVANKSLESPEPPEFCTPGFKIAKNHVPSTPLFNGKNDLNSPPRLNNNCPSTPELPAFETPFVSKLIKKEDREEESKIHSESQENSLRLPDLSTTNGTSWNDAPEMPKMLRYEEEALPEMPILQSNFGSSLAFKNTSGESLSRMKTGAGHMLEMKQTSVPVPEDGFNQDWCLSTPKVRVKFPAEPCTPEMPDMSSVTQDILKLVAQCKY