lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-118' (By similarity). Regulates the cell-cycle checkpoint activation in response to DNA damage (By similarity). Positive regulator of amino acid starvation-induced autophagy. Also acts as a negative regulator of basal autophagy. Positively regulates mTor activity. Promotes, in an energy-dependent manner, the assembly of the TTT complex and the RUVBL complex composed of pont and rept into the TTT-RUVBL complex (By similarity). This leads to dimerization of the mTORC1 complex and its subsequent activation (By similarity). May negatively regulate the ubiquitin proteasome pathway (By similarity). Required for habituation, a form of non-associative learning.
Subcellular Localization:
Nucleus. Lysosome.
Sequence:
MVMHARKPQRMNDGYFEKHTSHTSYQSSKYSSSKRDYERDRSSNYRDRDLSPGAGGGGGGGSAGGGGGGSGNGGGPLNNGNSYRSQSPDIDSPSSRSHDLRDRSDHRGGGGGNGRGGSGERYSFMQKMRDRDRDVYKKDKYSDKRDRRGNDRDSESSYRTNHDRDRRGGGGSGGGSGKLCSSRENDKRSGSDDRDRDRDRDLRDLRDKRDRGSDRDRDMYKKDKYADKRERSDRGERTARYGDWSEHVSSSGKMYYYNCKTEISQWEKPKEWVDRERNLPRDQHREKDYRDKDRDRDRDDRFSRSTYKHSNSSRDNSRLRWNYDNDGGPPSHRRRLDGRHNDNADMDISGDSTPTSEASYSLSGTPTTHGGGPGGGGPGGGGGSNSDQPMGNALPRLSSHPTANSSASVATGTGATGGLHYGSGTGGGPVTGATMLPTMSGMLNSNSSNSAGGSSSNASSSSLRNSVVGHIGSTSGTTVPTLGSQDPHQHHLNSNAPLPPGAKGKDQALLMRQKMHLGLGVLDVQSHHGVNSVGSVSDGTNHAYNSVNNSVSGSLRDNSVNSPLYMHHSMSPSLNFTKSPIPTIVGHTNNMSIAYTCNPPFGLKATLDGGVMVANASPATPGGNASSGSSGANSSQSIVPGMGPVCGISVITSMGSNSGTLCEGPPTPTQELDLSGSALEQQQLAAAAAAATASSLQLQAAQQAQQQRKLDGTSSATLSSLQSCVSSSGQAANLRGPEISPKLAKYFRADLIAHVTNWHAEVLERQAQKCCEDTHLFGDITCTRICAELKCARSLVRSTEINATLQEQKIMYLRHQIRRIEESKTQNAFMSDDT
The following text describes a protein:
Function:
Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B.
Sequence:
MFQKSIKKNELIMLLLFLLVLSAHADLPVHCVRHQIVGKWQLQFTEPQIKGSGPLTCGHNVPDNERTSQFAGQNTFQQAFTHEVVLTAKNNVVLKKKLQGKWTMVYDEGFEVDFMHYKCFAFSKYKTNYSGAYSYCGETLVGWYQNTKTNERGCYRAQKIEKTHKVSEGANNGHVVQPQFFQYQNTGMNKVWSRIDALNFVEQINRAQLQWKAKAYGEIIGLTTKQLNKYAGRKKHSSTILLEKQKKKQQILEYDLNHLPKEFSWEKYLGKKIYEQKGCGSCYTISTMTMLSARLKIKGLKADLSPQQSIDCNYYNQGCDGGYPFLVEKYLTELDGLIYEEKEYPYKGQVGECKAIEKKKKYRVLNYRFVGGAYGKSNELNIMEEIYNNGPVVLNFEPSFDFMFYVGGIFHSTTPDWIINGLAKPEWEKVDHSVLCYGWGEENGVKYWLLQNSWGKQWGENGRFRMKRGQDESSIESMAEAADVEIIEDS
The following text describes a protein:
Function:
Lignin degradation and detoxification of lignin-derived products (Probable). Oxidation of a broad range of substrates including mono-, di- and polyphenols, aromatic amines and methoxy-substituted phenols accompanied by reduction of oxygen to water.
Miscellaneous:
MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 3.85, its MW is: 67 kDa.
Subcellular Localization:
Secreted.
Sequence:
AIGPVADLDIVNDQLTDASMIKWDCLPYDVRSPNPLGTTGFAGGNYRSVPADLHLTTLADPR
The following text describes a protein:
Function:
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MKASEMARPPMRPGNPHAFASPATTPSRTASPNNAQGANVRTTQGGNQAGASEQQQPLDCFVVYELFASAVTALVSFFLVKDCGAVALNYRTFVSKVEPQQEEGKIVTDLDRLYWLTSVHVHWFSSGTLLVSTSTERTLALQCLGDLSEDEQQKLVDRCIRVAPNAMLASISSFDDPRQLSADDSNRRTSKKKAKMDSLEQNIEKWRMSVQRWLSRRGYSLPNLDKNSAWVTIRVGQLAQFPAMSPHLPTSARDVLWPRSLCFMQSLVPDDLKWFEVPGSAGFRDPIDAAQDWFTGQLERDKILDMQRKAKKAEEDAMRRKDEAPGLYPSSPFTARTGVYGDLQPVSGVYPTPPDGIVPGTGISSTDTPSVSGTASNVVLVPGGNTPAINLSAPQDYTTTDNQQHASTSPTFPAPLEPFQTSGEDDDLFEDMEGDGFGGPDVEEADFDFFDGPDGDDVNMADAPALPETTNKPHKQLNNDVAMAHEEEHSVKEEMSDPLAALESALAAPYRPINDGMPEEKVSEKEAKAVVPVEALATSPAQIKQNPPAKKEATPPLSPSAIAKTLQPSPPKKQSSFPASLQRTNSAFHSLDFSRRLSLVDAKYQDGRFAARIEKTEDDESAVNPGRLKSLKDLPLLNKLRYAVASASTAKSTEALSLARAVSDDSASDSESETSDMSEGSPEDPVDTHPLPYLGRLIIPAKRKLPTEGHGTPLSVTSFAESLAGDWQDSNSLLLDESSLTFFEPNTWDWSIPDLSMEPPEEKPLNGKESIAVTQILTDQIVSATLDLLDENALVESTSSIEPSSETRWQICIKELFPKAAECTLSALIAIHDVFPDLSAQAKGQQRPPPRKPNESNAIPSNHMYPMNPPFIRVRRAETHWDLLPPSIAFWEPLGLAPASPPKNVVAFCIYPHSASLRPILDRFMLNLQLAYDTCKLGSHARVETVIEYEGGLVPVKANSQTSAKEAFRALKDTCIQLGKLLAIQYAQLGEQQDTKIDAFVVYMVDPFGNPAALWELCSAFWSLFQAYGQGPPGRSDPTPKPDLVLQIIPIKYLASFDVPVILDAATYVSLAREVYDRCPPSVASTDKTPLSIYKAPAFQLEESLPRNVQFKLLSEPPQDLLRENSYMHIAYAISLDGNWLTAAWSDSCGKSQAVVSYHLGTRVFGDIAKEIWQTTIEILQARRVQWRVCIAKSGPLDREELETWVLLITCPTQVNLFLTILTVIEDPPYKFTPTTPAPSNSSAQANTNTPGSTPQTGVSPDPTIGLTPAATPSADPAPDPAADPEARLIDVTDETWGIILAHRLHNSNSTNQFSPALISGLLVKRGITHATSNSIHHPIPDPLPGPITVAVNILWIGAVGSTWKRAAESRGTQY
The following text describes a protein:
Function:
Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy-D-galactonate.
Miscellaneous:
MISCELLANEOUS: Reaction proceeds via an anti dehydration.
Sequence:
MKITKITTYRLPPRWMFLKIETDEGVVGWGEPVIEGRARTVEAAVHELGDYLIGQDPSRINDLWQVMYRAGFYRGGPILMSAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAYSWVGGDRPADVIDGIKTLREIGFDTFKLNGCEELGLIDNSRAVDAAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPLGPIALAACLHIDFVSYNAVLQEQSMGIHYNKGAELLDFVKNKEDFSMVGGFFKPLTKPGLGVEIDEAKVIEFSKNAPDWRNPLWRHEDNSVAEW
The following text describes a protein:
Function:
Probable transcription factor, involved in regulation of sexually dimorphic synaptic connectivity and behavior. Promotes pruning of phasmid neuron synaptic connections in hermaphrodite animals during sexual maturation.
Subcellular Localization:
Nucleus.
Domain:
DMA domain may interact with ubiquitin.
Sequence:
MMIGNLHVFPNGRIERERKPKCARCRNHGLVSWLKGHKRHCKYKECACEKCNLIAERQRVMAAQVALKRRQATEDAIALGLRVVAGQAIDRLPQGPVWNTAGGEDEDMDYLDEEIEEKPPTPVSEELVPLKRKKVEETYELSSFSPIELLMTLFCEHEKHVLELVLEACHGNVLQAIEHFANVRRVKNINQMKLFAAATRMDHVFPNMTNFILPKQSFLIDSLLEQPTFPVSSQASTSTKTCDSSSVDSISPNSSTFESS
The following text describes a protein:
Function:
Slow, weak voltage-dependent S-type anion efflux channel involved in maintenance of anion homeostasis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNNPRSVSPLVSPANHSDLLENQRQSGSGDFSRLEKRIGARKMKFHSKSMPRGAMFLDQEASRNFHDKRYDLFRTMSGKLERQISNLRGKPTESSLQDHKEITESLTADRYFDALQGPELETLKEKEKIVLPEDKTWPFLLRFPITSYGMCLGVSSQAIMWKTLATTEAEKFLHVTQVINHVLWWISLLLLLAVSITYLFKTILFFEAVRREFRHPIRVNFFFAPLISILFLALGIPHSIISHLPSTLWYFLMAPILFLEMKIYGQWMSGGQRRLSKVANPTNHLSIVGNFAGALLGASMGLKEGPIFFFAIGLAYYLVLFVTLYQRLPTNETLPKELHPVFFLFVAAPAVASMAWTKISASFDLGSRLAYFISLFLYFSLVCRINLFRGFKFSLAWWAYTFPMTAVASATIKYSDEVTGVATKILSVVMSGAATLTVIAVLGLTVMHAFVQRDLFPNDVVIAISAEQPKQKRWFKHLTKESYGNNERCPKILDPEDNQIDLESPPLVNVDSSTVQNSN
The following text describes a protein:
Function:
Binds to the 23S rRNA.
Sequence:
MVKGTTSMGGFTKKKVHIRCRRCGKNSLHKRHHQCASCGFPEAKRRKYSWIKWYT
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAASKRNAQNGKGALKGGTPNQRSKGDTAVSGQKANPFERMWNRRKFDVLGKKTKGEQRKVGQSRSRAVEMRKDTLLHEYRQSKKANAFIDRRFGESDASLAEDDKAIMRYQKERLAQLNKRSRFNLKDDDVSDGEEDLLMHRGVAAGVDDFDEGDVPGEEDENNPELDAEIVDKLHFGGFERASGGESLDIGKPKTRKEVMEELIAKSKFYKAQKAKEKEEADDLLGTLDEQFRELTQKGLLASKPSKKDDMSALMAKYGVAATASEEKGRKADTALTGGKQDLAGKKKEPKAEESAGGMEAKRAGAKDSGKLVPGKEGKKSGTAETEPEKDDYEKLAREMASDLRARASDRTKDPEEAAKEERERLEKLEKKRRQRMEGLDEETEGEESEDETGGRRARKRRKRAETSGDDLGENFVLEGEEFQQEGWATDIMKQGEDEDEDDEESGEEDELEGSADEDDDVSEDEDDDVTADGDDEGSQDDADVSGGEGPEDDVSGGEEESGSGSDGDLDDFLGAVQREKEMRELEKREKGGQEVLKRKKNGNRDAASDAASLEKPDPHTKTGKGGRTAGKVKEGARKKDGGKRPRGELPYVIDAPQTLELFRAIVDGRSDAELALAIERIRACNSVKLAADNRRKMQIFYSVLVQYFSALAGDSPLPLGRIDVLVKPLLEMSQDTPLIAAVNARERILKMQQQLSAKLRDPDGSSCWPSARTLLLLRLWTLTFPPSDFRHPVTTPLAILVGEYLARCHVAGPRDAAVGAFLSAFALQFHSQAKRFCPEAVTFLHALLLTALPPSSQKTHPSLWGAVPAYLREQVGSQLWLHVPSKTSSKKDSEKHPSETAKKAKAKASNGVSENGVGKTHGDHTETASPSSESESLDLVSLLSGGADLREYETDQWKQSLLAAVLETLGGFVRLYKGLPSFSELFRPLGGTLEALLKEGLRSETLQAAAARLREDITTTSADVISTRQPVRMRTKRAEPIKQYNPRFEEDGYVAGRDYDPDRERAEKKKLKKQLKKETKGAARELRKDNYFLAEEKRRDQLVAEEERHDKYRSAMAFLQQQEGAFKSGQLGGGKRKRK
The following text describes a protein:
Function:
Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease (By similarity). Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with NCOA1 and/or NCOA2. Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Note=Colocalizes with HIF3A in the nucleus and speckles (By similarity). Cytoplasmic in normoxia, nuclear translocation in response to hypoxia (By similarity).
Domain:
Contains two independent C-terminal transactivation domains, NTAD and CTAD, which function synergistically. Their transcriptional activity is repressed by an intervening inhibitory domain (ID) (By similarity).
Sequence:
MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDEMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQSQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWIETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSSNEKLQNINLAMSPLPASETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQPASPSDGSTRQSSPEPNSPSEYCFDVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLENSSTSPQSASTNTVFQPTQMQKPPIATVTTTATSDELKTVTKDGMEDIKILIAFPSPPHVPKEPPCATTSPYSDTGSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTAPEEELNPKILALQNAQRKRKIEHDGSLFQAVGIGTLLQQPDDRATTTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
The following text describes a protein:
Function:
Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells; Expression of the Bil system in E.coli (strain MG1655) confers about 100-fold resistance to phage SECphi27, SECphi18, SECphi6, SECphi4 and T5, but not to SECphi17. When cells expressing the Bil system are infected by phage SECphi27 at low multiplicity of infection (0.03 MOI) the culture survives, at 3.0 MOI the culture collapses at the same time as cells without the Bil system.
Sequence:
MTTLVVFIQVQGRPGIIETKLGPATTIGELKAALAAVGVNIDVETFIYVEDAENHLHGEHHEPAYGVKHGCRIHVSRCKRIRATVHYLDKTETRDFAPGARIRAVKAHAVDVFHIPPKDAGEHVLQLCNSLERPASDTPLHTLADHNTCAVCFDLVPEKRIEG
The following text describes a protein:
Function:
Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA.
Sequence:
MAPQNVGILAMEIYFPPTCIQQDILEDFDGVSKGKYTIGLGQDCMAFCSEVEDVISMGLTAVTSLLEKYEVDPRQIGRLEVGSETVIDKSKSIKTYLMKVFEDCGNTDIEGVDSTNACYGGTAALFNCVNWVESNSWDGRYGLVVCTDSAVYAEGPARPTGGAAAIAMLIGPDAPIAFESKFRASHMSHVYDFYKPDLASEYPVVDGKLSQTCYLMALDSCYNGYCHKYEKLEGKQFSIVDADYFVFHSPYNKLVQKSFARLVFSDVVRNASSVDESVKEKLGQFTPLTGDESYQNRDLEKASQQAAKSYYDKKVQPGTLINKQVGNMYTASIYAAFASLIHNKYSSLDGNRVMMFSYGSGSSATMFSLHLSKGKSPFSLSNIAKVMNVDEKLKRRTELAPEKFVELMKVMEHRYGGKDFVTSKDASLLAPGTYYLTEVDSKYRRFYAKKTSEES
The following text describes a protein:
Function:
Probably involved in the defense reaction of plants against pathogens.
Sequence:
MNTFKTPFLIIVAISFLVLATNAQNAQQDYLNTHNTARAQVGVANVVWDTVVAAYATNYANARKVDCSLTPSTGGSYGENLANGNNALFTGVAAVNLWVNEKPYYNYTANACIGAQQCKHYTQVVWSNSVKIGCARVLCNNGGYFVGCNYDASAALKSRKITASVRQTRGLGASAACGQLRNKFQKSPSLATAEGEVIEARLRSEDFDNSCIGFAFTYICDACVGL
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MGGGHHEPFKIPNYSIYSNFRDFPQLAQHEKRLAQIGLKDPWIRNYVYLYDRKYPHVVGQWAHFKKLILPGWKAGVAFTAALIFVEEAYQYKTHGTTSWDGHH
The following text describes a protein:
Function:
Has nicotinamidemononucleotide (NMN) aminohydrolase activity, not active on other substrates.
Sequence:
MTDSELMQLSEQVGQALKARGATVTTAESCTGGWVAKVITDIAGSSAWFERGFVTYSNEAKAQMIGVREETLAQHGAVSEPVVVEMAIGALKAARADYAVSISGIAGPDGGSEEKPVGTVWFAFATARGEGITRRECFSGDRDAVRRQATAYALQTLWQQFLQNT
The following text describes a protein:
Function:
Catalyzes the hydrolysis of L-arginine to urea and L-ornithine. The latter can be utilized in the urea cycle or as a precursor for the synthesis of both polyamines and proline.
Sequence:
MHLVYCAECFAISEHLKGHMNLLVEKQVSCTSLAWHFVTSLPSFLSSPQPLRSLAFSRRLRLLLQSSVPPLDDSSAMGGAAAATGAARWIQRLSAARISTEALERGQSRVIDASLTLIRERAKLKGELLRAMGGVKASATLLGVPLGHNSSFLQGPAFAPPRIREAIWCGSTNSSTEEGKELNDPRVLTDVGDVPIQEIRDCGVEDDRLMHVISESVKTVMDEDPLRPLVLGGDHSISYPVVRAVSEKLGGPVDILHLDAHPDIYDCFEGNTYSHASSFARIMEGGYARRLLQVGLRSITKEGREQGKRFGVEQYEMRTFSRDREKLENLKLGEGVKGVYVSVDVDCLDPAFAPGVSHIEPGGLSFRDVLNILQNLQGDVVAGDVVEFNPQRDTVDGMTAMVAAKLVRELSAKISK
The following text describes a protein:
Function:
Molecular adapter which is involved in cilium biogenesis. Part of a functional complex including OFD1 a centriolar protein involved in cilium assembly. Could regulate the cAMP-dependent phosphorylation of OFD1, and its subsequent ubiquitination by PJA2 which ultimately leads to its proteasomal degradation.
Subcellular Localization:
Cell projection, cilium. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.
Sequence:
MTELVDLQGLADRSTLPFDIGLLPPAESGRLFTITHRRRGKVPSDTFATYRVAQASHQADASAMIETCRHAMHQMAVPPSFVISEAMFGIYTLLLEDRCTCLAEVHDPTHVVHHLSADYTGKRILPSVAVANVRHLLAFVLIFTLFMFLTSAAEALLLDAETLDSLRALHGAEGIGLRTAFFNNARGEVVTCFRNDVIMTWTADRLEYQLELRVPSSLLSSLQSSTDGPERHAPTHQLRCFALSADGTTLAAAGKGAHTYLWNLGTQQLERAISLPEAKSVIGLSFVADQSRRELLAILAQDGILSLCAPDTGAIYAQLGPPHDVFIDAISGNPRSRYLLATLISGQLGVYDVDACLRVTGSGASRAAAVQANHMEARLGASRREGMARATTLPTQAFTPVTSTSLKASRDDSTTTNSTTARQWREYMPKVSFAQLRDVLHGLGEYPAQYRQTYRVLMNNVFSRRIIWRIVLQTPSNAEAFGRLLELGTHPAHLQLHRKYPIKSRKLLRVLQRTLSCLSHWSPVFAEADFIAAAVFPFVKLFQNSPALNAIENMLALHDEALLRALIRLEATADLYAWPLLYTVLSEVFYEKDWLVVWDNILSNHPAYLFAVVVSFLMELRVKLMQCRSCDELYQLLHHKHSLNVAQLVQRAYTILQTPNQEVDLRRIFDGFAPLSRQDYPLFEEYPAFVVNYQGSSYCQKTLMHVACSTLLVKLKEKERIRREEMRLLKERTALMAEGRQLGLVAAQRAGQARRQELLEAAMRAQEDEIKADELRLDAQRAELQALRRQQELKMLQPAVQPDETADGASQPSTSFSDLYRQTHALEEWIEELDQRIDQQQHADSLRFDSYRQRVDVAMESDAQQGAADQLTSSLRDQRNSLERQQQRLLADVQQLRREPALMNDCLTGALRSLTLGVEA
The following text describes a protein:
Function:
Metalloprotease. Was previously shown to degrade COMP. However, a later study found no activity against COMP.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Note=Also found associated with the external cell surface.
Domain:
The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix; The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme (By similarity).
Sequence:
MHRGLNLLLILCALAPHVLGPASGLPTEGRAGLDIVHPVRVDAGGSFLSYELWPRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQTSVPTCHLLGDVQDPELEGGFAAISACDGLRGVFQLSNEDYFIEPLDEVPAQPGHAQPHMVYKHKRSGQQDDSRTSGTCGVQGSPELKHQREHWEQRQQKRRQQRSISKEKWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQKNVNMKGDDHPQHHDTAILLTRKDLCATMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGTGNDCESIGKRPFIMSPQLLYDRGIPLTWSRCSREYITRFLDRGWGLCLDDRPSKGVINFPSVLPGVLYDVNHQCRLQYGPSSAYCEDVDNVCYTLWCSVGTTCHSKMDAAVDGTSCGKNKWCLNGECVPEGFQPETVDGGWSGWSAWSVCSRSCGVGVRSSERQCTQPVPKNKGKYCVGERKRYRLCNLQACPPDRPSFRHTQCSQFDSMLYKGKLHKWVPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRDICIDGICKKVGCDFELDSGAEEDRCGVCRGDGSTCHTVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSEDPDKYFLNGGWTIQWNGDYQVAGTTFTYTRKGNWETLTSPGPTTEPVWIQLLFQERNPGVHYKYTIQRASHSEAQPPEFSWHYGPWSKCPVTCGTGVQRQSLYCMEKQAGIVDEGHCDHLSRPRDRKRKCNEEPCPARWWVGDWQPCSRSCGPGGFFRRAVFCTRSVGLDEQRALEPSACGHLPRPLAEIPCYHYVACPSSWGVGNWSQCSVTCGAGIRQRSVLCINNTGVPCDGAERPITETFCFLQPCQYSTYIVDTGASGSGSSSPELFNEVDFDPHQPVPRPSPASSPKPVSISNAIDEEDPELDPPGPVFVDDFYYDYNFINFHEDLSYGSFEESHSDLVDIGGQTVPPHIRPTEPPSDSPVPTAGAPGAEEEGIQGSWSPSPLLSEASHSPPVLLENTPVNPLANFLTEEESPIGAPELGLPSVSWPPASVDGMVTSVAPGNPDELLVREDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPFPTQPSSPSNSTTQASLSPDAVEVSTGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSPGLLPRPAQETQTNSSKDPAVQPLQPSLVEDGAPTDLLPAKNASWQVGNWSQCSTTCGLGAIWRLVRCSSGNDEDCTLSSRPQPARHCHLRPCAAWRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCQPGPTKPPTRQLCGTQPCLPWYTSSWRECSEACGGGEQQRLVTCPEPGLCEESLRPNNTRPCNTHPCTQWVVGPWGQCSAPCGGGVQRRLVKCVNTQTGLAEEDSDLCSHEAWPESSRPCATEDCELVEPSRCERDRLPFNFCETLRLLGRCQLPTIRAQCCRSCPPLSRGVPSRGHQRVARR
The following text describes a protein:
Function:
Directs RNA polymerase II nuclear import.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MATNDGNSSCQSQSLPTSVLIRIKRKISDLSDESAAIDQPASKHSKNKNNPRGDKGASLLFKEPTLNQHKLFQFIGTVNSTEDKLVKTTVVDQLNNSQGKRSFSKHHKVDIATIKSKLKKEQLLHREKQRFKIVSHRIAKLKEIAIQEQSIEDIVSNGGNIDQGCGNCEIVDVEELQSEVEGRDYAMQSGITCNGVEMTIQQSEESSQSNAKYTYDLYWCRNSAYRTNDEFTSLGNTIEFESFDEQLLTLDHWQQDKEYNEHYYDEDDSNDESNWRNDYPDEDDLNLWEESSDGGNSSDDSEDNYCNIGNYEEENYGYFEEGLRLSDAD
The following text describes a protein:
Function:
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Sequence:
MSTEQTFIAVKPDAVQRGLIGYIISKFELKGYKLRALKFLVPSRDLVEEHYAEHKGKPFYEKLVGFMASGPVCAMIWEGKQAVKTGRLMLGASNPLDSAPGTIRGDYGIDLGRNVCHGSDSIESANREIKLWFQPSEIQVYDRTIEPWIYE
The following text describes a protein:
Function:
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Sequence:
MTKLFIPYIMGNKDLIENATLLSENGADIIEIGVPFSDPVADGPVIMEAGQQAIKQGITIDYIFNQLEKHGDQIKCNYVLMTYYNIICHYGEQAFFEKCRDTGVYGLIIPDLPYELSQRLKQQFSHYGVKIISLVAMTTDDKRIKDIVSHAEGFIYTVTMNATTGQNGAFHPELKRKIESIKAIANVPVVAGFGIRTPQHVADIKEVADGIVIGSEIVKRFKSNTREEIIKYLQSIQQTLNN
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MDPSILATMDRDALKKQIENMKYQASMERWPLSKSIAAMREYVEENEKNDPLIHAPDKKNNPWAEKGKCVIM
The following text describes a protein:
Function:
May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSNLKSDLDEYLLLQSDQKKPSFNVKLPQLKVPFFSSSDPEANSFLKDSDSCFPKLSRLQRIVGFVACLGMGALCMTLSTFYIPFLILKARKFALLYTLGSLFFILSFCFLSGFGSFLKQMFSKPRLLTSLSYSSCLILTLYCALVAKSTAFTVLFAVAQIIALLFMVLGTVPGGATGLKFFGQLFKNTVSASTSVLPV
The following text describes a protein:
Function:
Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development.
Subcellular Localization:
Chromosome.
Sequence:
MMETQPASVPCVLPQDVYEFSEDRESLGRLRVSEMPAELNGGGDGSKGDGAAVVATEVSQQSNKKRKRCGVCVPCLRKEPCGTCYNCVNRSTSHQICKMRKCEQLKKKRVVPMKGVEAVDKDDAKNQAKEQVPSVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKQECDSTLPSKGSEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPIIPNHIAANNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSISMQLYEKFNYETNQDNSGHSEGNAPSCPEDLNTLKEALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSTGKGSQESPFPSLGQVSKKLVQKSYHKEQVLNLENTNVTCPSGNLPFSQNALSLAKEKNISLQTAIAIEALTQLSSALPQTNNEYPNAPSQPLINHNDQLTHFPTAKGNQLPMLPLSCNELFQNQQAQLYTGKNALPVPQSPRQASWEQNKKPGYQESEYIPENLSQSSSVLPSDASTPQKKEFLQQWVQNADLLKSPSDPMTGLKQLLGNTDEYIKSAFKGPEGLSKKIKNVKSKHTIKSIKKESADFTKMSPDQQLSQLLQGNDFHRNTQAALQQHLHHKRNLFVDSNTMEACTQEQQNWWVPNSQQAPVSKTTEKPVKERKKRRQSPSQKQVEPKPKPPRKQVQIKKPRVKEGNAVFMPVSQISLDSFRRVEKEENQVKELDLENSLPINVQPDLLGSQSIQLTGSQANLENQKTVNTQETCNENQTSIGKANNFALCVNKTNSLVAKGRCPTPSTGDSSSGQGDSANQHTNLTDVPGQNDLSCIDDKFEDLIKQFAAEFGEDFSLPGSEVPSQNGERPPKQQTSGVPQFKMPFPSQLPSENATHSNPALSNNLLTHNASHKFDSLFSSKSPKQIKIESSGAITVVSTTCSYSEENQHLDGTPTKSELPFNPTLSGFLESPLKYLTSPTKSLIDTPAKMAQAEFPTCDCVEQINEKDEGPYYTHLGSGPTVASIRELMEERFGEKGEAIRIEKVIYTGKEGKSSRGCPIAKWVIRRQSEDEKLMCLVRQRAGHHCENAVIIILIMAWEGIPRALGDSLYDDISGTITKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGDNPKEEEFLKDSFQDLATKVAPVYKMLAPQAYQNQANNEDVAIDCRLGLEEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRMIGKIAEDEQLHVLPLYKVSTTDEFGSEERQLEKIRKGGIQVLSSFPREVRKLSEPAKSCRQRQLDAKKAAAEKKKLQKEKLVSPDKTKQEPSDTKTCQQNPGVPQQQTKPCVKVEPSNHYNTFKYNGNGVVESYSVLGSCRPSDPYSMNSVYSYHSFYAQPNLPSVNGFHSKFALPPFGFYSFPNNPVVPNQFMNYGTGDARNSGWMNNSFEKKPELQSLADGMNQSYGSELPEQNYRRSSEVPHHYSLQNSNSQKSVGVPHRTTPAPMETTPFSNVPCYNKVIKKEPVCDPLVDPFQRSNSVHSQSPGVNHSLQTNDLSYKANGALPSSGRTNKEGPCSMFLPSDKNGLEKRDYFGVHSNVPGLKEKQWTPYGIDVPVGQRDSLDSQCSGKVWSSCKLSDSPAVMPSTVQDKNWTGRQASLNQGVKEPMPFQEKLWNSVAASGRCSTTPNDRSSVTPCAELQDKNWMSFPNPAVNSLKTDSSQNHWDPYSLDDNMDDGQSKSVKEEEDEEEIWSDSEHNFLDGNIGGVAVAPGHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARVKEEEAAKLGIKQEVKSLGKKRKWGGAATTETPPVEKKDFIPTRQAATSLTDSTTTAFSYAYTKVTGPYSRFI