lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Bifunctional axonal guidance cue regulated by sulfated proteoglycans; attractive effects result from interactions with heparan sulfate proteoglycans (HSPGs), while the inhibitory effects depend on interactions with chondroitin sulfate proteoglycans (CSPGs). Ligand for receptor PLXNB3. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. May promote angiogenesis by increasing endothelial cell proliferation and migration and inhibiting apoptosis.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MKGPCVIAWLFSSLGWWRLAQLETDASLCQRAEHPVISYKEIGPWLREFRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQAAEWECDEATKKACYSKGKSQEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNRTLSNLTEIHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYHELQGTFFLPELDLIYGIFTTNVNSIAASAVCIFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTVDQGVYMNLTERNLQDAQKFILMHEVVQPVSPVPAFMEDSSRFSHVAVDVVQARDALVHVIYLATDYGTIKKVRAPLTQTSGGCVLEEMELFPERRPEPVRSLRILHSQSVLFAGLREHVAKIPLKRCQFYRSRSACIGAQDPYCGWDLVMKKCTSLEESLSMTQWEQSIATCPVRNLTVDGHFGAWSPWTPCTHMDGSAVGSCLCRTRSCDSPAPQCGGWQCQGPRMEIANCSRNGGWTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERYCNEHLLCPPHVFWTGWGPWERCTAQCGGGIQARRRTCENGPDCAGCNVEYQPCNTNPCPELKKTTPWTPWTPVNISDNGGHYEQRFRYTCKARLPDPNLLEVGRQRIEMRYCSSDGTSGCSTDGLSGDFLRAGRYSAHTVNGAWSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKFGGMPCLGPSLEYQECNILPCPVDGMWSCWSSWSTCSATCGGGHYMRTRSCTNPAPAYGGDICLGLHTEEALCNTQPCPESWSEWSEWSECDVAGVQVRVRQCVLLFPVGSQCSGNTTESRPCIFDSNFIPEVSVARSSSIEEKRCGEFNLFHMIAVGLSSSILGCLLTLLVYTYCQRYQQQSHDATVIHPVAPAPLNTSITNHINKLDKYDSVEAIKAFNKNNLILEERNKYFNPHLTGKTYSNAYFTDLNNYDEY
The following text describes a protein:
Function:
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Sequence:
MNRATATINVTALKHNLSQIKALAPKSLAWAMIKSNGYGHGLVRVAKALSDANAFGVACIDEALTLREVGIKSPIIVMKGFYNEAELSQFARHRLGAVIHCSDQVSLLEKTNLTSSLSVWLKIDTGMNRLGFSVEQSPAVYNQLKTSSSIQKPIGLMTHLADADNENKTFTELQIKRFFSVTEKMIGPKSIVNSAGFFAYPNALVDWIRPGIILYGISPFGINYNSFKEKIEKKFRPVMTLSAKIIAIKNRRQNDSVGYGCTWSCPEDMPIAIVSIGYGDGYPRHAPSGTPVLLNGKICPLIGRVSMDMIAIDLRSQPNAQVGDDVILWGEGLPVEIIAEKAGTIAYELLCKITQRVQFIEIEK
The following text describes a protein:
Function:
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Subcellular Localization:
Plastid, chloroplast. Mitochondrion.
Sequence:
MEALKVWSLTATPLKQLLRLSSSSTRLATTIYGRRSYHLSPALRCASAASSSSSSATTAETSKPSGRNRRSASSSNSTSDREAIRSIRLKKVEELRGQGLEPYAYKWEKSHSANQLQEIYKHLANGEESDNEIDCVSIAGRVVARRAFGKLAFLTLRDDSGTIQLYCEKERLSDDQFEQLKQFIDIGDILGASGSMKRTEKGELSICVNSFSILTKSLLPLPDKYHGLTDIDKRYRQRYVDMIANPEVADVFRRRAKIVSEIRKTVESFGYLEVETPVLQGAAGGAEARPFVTFHNSLGRDLYLRIATELHLKRMLVGGFEKVYEIGRIFRNEGISTRHNPEFTTIEMYEAYSDYHSMMDMAELIVTQCSMAVNGKLTIDYQGTEICLERPWRRETMHNLVKEITGINFSELGEDLGNAKDTVLLALQDVLEPKDKSGIRACSSLGHLLNEIFEVVVEPKLVQPTFVLDYPIEISPLAKPHRGNAGLTERFELFICGREMANAFSELTDPVDQRTRLEEQVRQHNAKRAEAVRESPEPNAKKDDDDDESYEVTLDEDFLTALEYGMPPASGMGLGIDRLVMLLTNSASIRDVIAFPVLKLQQ
The following text describes a protein:
Function:
Involved in triacylglycerol (TAG) synthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA. Can use oleoyl-CoA and linoleoyl-CoA as substrates. May play a role in TAG biosynthesis in different tissues in responses to environmental and hormonal cues.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Lipid droplet.
Sequence:
MAAEPVSDGGAAAEKLISGREEFGDSSNLFSAILAMVLWLGAIHFNIALILLAVFFLPLSKSLLVFGFLFGFMVLPINEKSRFGRRLSRFICKHACNYFPITLHVEDMKAFDPNRAYVFGYEPHSVLPIGIVALADHTGFMPLPKVKVLASSTVFYTPFLRHLWTWLGLTPATKKNFISLLASGHSCILIPGGVQEAFHMQHGTEIAFLKARRGFVRVAMVKGKPLVPVFCFGQSNVYKWWKPGGKLFLKFARAIKFTPICFWGIFGSPLPFRHPMHVVVGRPIEVDKNREPTTEEVAKIHGLFVEALQDLFERHKARAGYPNLELRIV
The following text describes a protein:
Function:
Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation; Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt) and autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system is essential for its function. ATG12/ATG5 conjugate has an essential role in plant nutrient recycling.
Sequence:
MAASEAEQKVVVHVRSAGNAPILKQDKFKISGRDKFLRVIEFLRRQLHQDTLFVYVNSSFSPSPDELIIDLYNNFAIDGKLVVNYALSAAWG
The following text describes a protein:
Function:
D-proline reductase catalyzes the reductive cleavage of a C-N bond in D-proline resulting in the formation of 5-aminovalerate. The alpha subunit has been shown to bind D-proline, presumably via the pyruvoyl group.
Miscellaneous:
MISCELLANEOUS: The reaction mechanism first involves the formation of an adduct (and not a Schiff base) between the nitrogen of proline and the pyruvoyl group of the alpha subunit. The selenol anion of selenocysteine in PrdB nucleophilically attacks the alpha-carbon, resulting in cleavage of the N-C bond of the proline ring. This intermediate is then transformed to the oxidized gamma subunit containing a mixed selenide/sulfide group and to the 5-aminovalerate adduct of the alpha subunit. The final product, 5-aminovalerate, is formed by hydrolysis. Subsequently, the selenide-sulfide group of PrdB is reduced, but the natural electron donating system for D-proline reductase is unknown.
Subcellular Localization:
Cytoplasm.
Sequence:
MSITLESAKEHANDLAVLCCRAEEGTVIGPSNLEDPAIFGDLEDSGLLTIPANCLKIGEVLGAKLVKTADSLTPLTPELLEGVNSISEEAPKQEASAPVEAPVAEVAPAAMPVANVTGSMLKIHIGEGKDINLEIPLTIAGQMGVVAPTAAAPAGVAMPVASATEQVVAPAGEPKLVRTLQKKHFKIEKVEFGPETKIENNTIYIRENICEDAVKVSNLVTDIKVEIITPADYGKYSETIMDVQPIATKEGDGKIGQGVTRVIDGAIIMVTGTDEDGVQIGEFGSSEGELDANIMWGRPGAPDKGEILIKTQVTIKAGTNMERPGPLAAHKATDFITQEIREALKKLDDSEVVETEELAQYRRPGKKKVVIIKEIMGQGAMHDNLILPVEPVGVIGAKPNVDLGNVPVVLSPLEVLDGGIHALTCIGPASKENSRHYWREPLVIEVMNDEEFDLAGVVFVGSPQVNAEKFYVSERLGMLVETMDVEGAFITTEGFGNNHIDFASHHEQVGMRGIPVVGMSFCAVQGALVVGNKYMKYMVDNNKSEQGIENEILSNNTLCPEDAIRAVAMLKAAIAEEEVKVAERKFNKNVKENNVDLIEEQAGKEITLLPNEQVLPMSKKRKEIYEADK
The following text describes a protein:
Function:
Acyltransferase involved in taxol biosynthesis. Catalyzes the selective 13-O-acylation of baccatin III with (3R)-3-amino-3-phenylpropanoyl-CoA as the acyl donor to form 3'-N-debenzoyl-2'-deoxytaxol.
Sequence:
MKKTGSFAEFHVNMIERVMVRPCLPSPKTILPLSAIDNMARAFSNVLLVYAANMDRVSADPAKVIREALSKVLVYYYPFAGRLRNKENGELEVECTGQGVLFLEAMADSDLSVLTDLDNYNPSFQQLIFSLPQDTDIEDLHLLIVQVTRFTCGGFVVGANVYGSACDAKGFGQFLQSMAEMARGEVKPSIEPIWNRELVKLEHCMPFRMSHLQIIHAPVIEEKFVQTSLVINFEIINHIRRRIMEERKESLSSFEIVAALVWLAKIKAFQIPHSENVKLLFAMDLRRSFNPPLPHGYYGNAFGIACAMDNVHDLLSGSLLRTIMIIKKSKFSLHKELNSKTVMSSSVVDVNTKFEDVVSISDWRHSIYYEVDFGWGDAMNVSTMLQQQEHEKSLPTYFSFLQSTKNMPDGIKMLMFMPPSKLKKFKIEIEAMIKKYVTKVCPSKL
The following text describes a protein:
Function:
Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis (By similarity). Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+) (By similarity). Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 (By similarity). Plays a role in central nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Glutamatergic synaptic vesicles.
Sequence:
MTDSSSASDPTAGPVDPGPAPSAPDPALEDPASTPANGHHPNQADSFNMEQQMKIGEPEDNAGLLESSMRLKPHEAQSYRKKALWVSWVSIVVTMILAIAAFTVSIMRHSASAFGFAFDATLDVLSSIIVLWRYSNAAAVHSAHREYIACVILGVVFILSAITILVKAIHDLATKLEPEVDDFLYSVSVISGVVCTVLCVCKFMLGKVLTSRALITDGFNSLVGGVMGFSILISAEVFKHEPSVWFLDGTIGILIGLIILAYGVKLLKDMVPRIRQTRHYERFE
The following text describes a protein:
Function:
DNA repair protein involved in DNA non-homologous end joining (NHEJ); it is required for double-strand break (DSB) repair and V(D)J recombination and is also involved in telomere maintenance. Plays a key role in NHEJ by promoting the ligation of various mismatched and non-cohesive ends. Together with PAXX, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends. May act in concert with XRCC5-XRCC6 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are non-complementary or partially complementary. In some studies, has been shown to associate with XRCC4 to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired. Alternatively, it has also been shown that rather than forming filaments, a single NHEJ1 dimer interacts through both head domains with XRCC4 to promote the close alignment of DNA ends (By similarity). The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other. The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors. Binds DNA in a length-dependent manner.
Miscellaneous:
MISCELLANEOUS: Was named 'Cernunnos' after the enigmatic Celtic god of hunting, the underworld and fertility.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to site of double-strand breaks; recruitment is dependent on XRCC5-XRCC6 (Ku) heterodimer.
Domain:
The coiled-coil region mediates homodimerization; The Leu-lock (Leu-115) site inserts into a hydrophobic pocket in XRCC4; The XLM motif (also called the KBM motif or KBMX motif) and the interior region of the C-terminal tail preceding the XLM motif are essential for DNA end joining. The sequence of the C-terminal tail is not critical for its role in end joining but it must be sufficiently long to interact with XRCC4 and to stabilize the interaction of XRCC4 with LIG4 (By similarity). A single XLM motif and C-terminal tail is sufficient to promote end joining (By similarity).
Sequence:
MEELEQGLLMQPWAWLQLAENSLLAKVFITKQGYALLVSDLQQVWHEQVDTSVVSQRAKELNKRLTAPPAAFLCHLDNLLRPLLKDAAHPSEATFSCDCVADALILRVRSELSGLPFYWNFHCMLASPSLVSQHLIRPLMGMSLALQCQVRELATLLHMKDLEIQDYQESGATLIRDRLKTEPFEENSFLEQFMIEKLPEACSIGDGKPFVMNLQDLYMAVTTQEVQVGQKHQGAGDPHTSNSASLQGIDSQCVNQPEQLVSSAPTLSAPEKESTGTSGPLQRPQLSKVKRKKPRGLFS
The following text describes a protein:
Function:
Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Sequence:
METSTQQKNVANRTKRAALKRNASGDGDDIPVKSPYFKDLSQSEPSETDVPDAVQIPAAQSQLADKMPSAGPRLGPSFFQQPCTQLARQLLGQVLVRVIGDQRLIGRIVETEAYLGVEDSACHTYMGRKSVANKSMFLSPGHAYVYMTYGMYHCINITSQGEGQAVLIRGLFPLEGKYTMATLRQKASKKSNRTFKTKDLCNGPGKLCLSLDIDRQLDGIDLTQSDSSMWVESGDHISDGDIVSCPRIGIDSATKEWVQKPLRFYVKGNSCVSKRNKAREAEMNYST
The following text describes a protein:
Function:
Catalyzes the transamination reaction between 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) and alanine to produce pyruvate and 5-(aminomethyl)-3-furanmethanol phosphate (F1-P), the precursor for the furan moiety in methanofuran.
Subcellular Localization:
Cytoplasm.
Sequence:
MLSKRLLNFESFEVMDILALAQKLESEGKKVIHLEIGEPDFNTPKPIVDEGIKSLKEGKTHYTDSRGILELREKISELYKDKYKADIIPDNIIITGGSSLGLFFALSSIIDDGDEVLIQNPCYPCYKNFIRFLGAKPVFCDFTVESLEEALSDKTKAIIINSPSNPLGEVIDREIYEFAYENIPYIISDEIYNGLVYEGKCYSAIEFDENLEKTILINGFSKLYAMTGWRIGYVISNDEIIEAILKLQQNLFISAPTISQYAALKAFEKETEREINSMIKEFDRRRRLVLKYVKDFGWEVNNPIGAYYVFPNIGEDGREFAYKLLKEKFVALTPGIGFGSKGKNYIRISYANSYENIKEGLERIKEFLNK
The following text describes a protein:
Function:
Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control.
Sequence:
MNPPMSIEPVIIPRANHPISRSLVSPNALRVLYRLRDNGFIAYLVGGCVRDLLLGREPKDFDVATDATPNQIKRIFRNCRLVGRRFRLAHIHFTDEIIEVATFRALSPPEQGEGEPVADETGQRGGDEAERLRPPRHLVSDEGMVLRDNVFGTPGEDALRRDFTVNALAYCIADFSIIDYAGGMEDLQRGMIRTIGDPRVRFTEDPVRMLRAVRFAAVLGFAVEEETWQAMLDLAPAITRATAPRLYEEMLKLFLSGEGERAYQLLRQTGLFAHLFPGFEAWLGEETDGFPHARTGSALEWVDSQVGSGEPVSPPLLLALLFGGYLEEQSERFMGQGASPLDAVSAAVAAFLGEQAPLVAVPHRIGLAMREILALQQRLHRIPGKRPQAVLARASFAEAMAYLRCRCAMNGEDSPVLAWWERYARDSVMPPVEPCSAGGETKKPRRRRRRRGVRKAAPQ
The following text describes a protein:
Function:
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes; Regulates also the sphingolipid metabolism.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MPVCTACACPADYIYTTYKTKSNIRLAVCPRCNQFVDPLIEHPSLLLLLDLVLLKPRVFLHLLFNRGSLPFSAVSEPASEIERETARRKQLWEDFSTLALLSVGAETAVRLLPTLSGSEDSSDIQLSKIFWTISAVLLEGAAQHLTTLGLSILVLKLRGQNCSVSPSDDMHPARQDGRRKFFAPILIPLTLLYTSLLPLLFQLFLFPWYSTQPTIHEQPPSPSLSLSLLSSLPLPSSFTIPPSWLETERLLSEAWARGDRIWAGTRLLGGMSAGYGLRVLLPTKPWETTLIVLAGWMAAAFVGKVVAELPSRS
The following text describes a protein:
Function:
mRNA-binding protein which interacts with a range of target mRNAs including SERPINE1, ACTA2, CCN2 and COL4A1 and may promote extracellular matrix production. Binds to the 3'-UTR of SERPINE1 mRNA and stabilizes the mRNA, possibly by competing for binding with SERBP1 and preventing SERBP1-mediated mRNA degradation. Also binds to the 3'-UTR of ACTA2. Testis-derived lumicrine factor that triggers epididymal differentiation and sperm maturation.
Miscellaneous:
MISCELLANEOUS: Up-regulated in the kidneys and serum of patients with diabetic nephropathy and enhances renal fibrosis so may have promise as a biomarker of renal fibrosis and as a therapeutic agent for chronic kidney disease.
Subcellular Localization:
Secreted. Cytoplasm, perinuclear region. Note=Detected in the perinuclear region of fibroblasts.
Sequence:
MAPPPACRSPMSPPPPPLLLLLLSLALLGARARAEPAGSAVPAQSRPCVDCHAFEFMQRALQDLRKTACSLDARTETLLLQAERRALCACWPAGH
The following text describes a protein:
Function:
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity); The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Sequence:
MGARKKISAEKRKEALKTMYFAKLQNVPTSPRKMRLVADMIRGMEVNRALGVLKFSSKEAAARVEKLLRSAIANWEQKNERKAESGELFVTQIFVDGGATLKRMRPAPQGRGYRIRKRSNHVTLFVGAKSNNEDQN
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport. The non-phosphorylated EIII-Glc is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, and glycerol. Phosphorylated EIII-Glc, however, may be an activator for adenylate cyclase. It is an important regulatory protein for cell metabolism.
Subcellular Localization:
Cytoplasm.
Domain:
The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
Sequence:
MGLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMVAPVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVIEFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK
The following text describes a protein:
Function:
Toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is PhoAT; expression in M.smegmatis (strain mc(2)155) requires the cognate M.tuberculosis antitoxin gene. Expression in M.smegmatis strain mc(2)155 of the toxin alone slows growth and reduces cell viability, effects which are abrogated when cognate antitoxin PhoAT is coexpressed. Unwinds and/or cleaves 5'-tailed RNA in vitro that starts with 5'-AC, the reaction requires hydrolyzable ATP; double-stranded (ds)RNA and dsDNA are not unwound or cleaved. Can be expressed in the absence of its antitoxin gene in E.coli. In vitro has both ATPase and GTPase activity which are the best in vitro substrates; also hydrolyzes ADP>UDP/GDP>CDP>UTP>CTP.
Domain:
Has an N-terminal PINc domain and a C-terminal PhoH domain, suggesting it has RNase and nucleotide hydrolysis activities.
Sequence:
MTDTRTYVLDTSVLLSDPWACSRFAEHDVVVPLVVISELEAKRHHHELGWFARQALRLFDDLRLEHGRLDQPIPVGTQGGTLHVELNHTDPAVLPAGFRTDSNDSRILSCAANLAAEGKRVTLVSKDIPLRVKAAAVGLAADEYHAQDVVVSGWSGMHELETASADIDALFADGEIDLVEARDLPCHTGIRLLGGGSHALGRVNAHKRVQLVRGDREAFGLRGRSAEQRVALDLLLDESVGIVSLGGKAGTGKSALALCAGLEAVLERRTHRKVVVFRPLYAVGGQELGYLPGSESEKMGPWAQAVFDTLEGLASPAVLEEVLSRGMLEVLPLTHIRGRSLHDSFVIVDEAQSLERNVLLTVLSRLGTGSRVVLTHDIAQRDNLRVGRHDGVAAVIEKLKGHPLFAHITLLRSERSPIAALVTEMLEEITGPR
The following text describes a protein:
Function:
May play a role in the negative regulation of cell cycle progression.
Subcellular Localization:
Cytoplasm.
Sequence:
MEPPAEREDGAQLVQEARESIEAAQSYGRELGQRLQGLQEARRQIKESASQTRVALKKHFSDLKGTLQKLLDERLGSLLHQVDTIELDNIKPLDECQKLIEHGVSTAEDLVREGEIAVLGGVGEKNEKLWSFTQKASHIQLDSLPEVPSLVDVPCLSAQLDDSILTIVKDQILKHGTVASRPPVQIEELLEKPGGIIVRWCKVDDEFTAQDYRLQFRKSTSNHFEDVYVGSETEFIVLHIDPNVDYQFRVCARGDGRQEWSPWSVPQIGHSTLVPHEWTAGFEGYSLSSRRNMALRNDSQASGVLYSSAPTYFWGQTLTFRVETVGQPDRRDSIGVCVEQQNGHDSLQRDQAVCVGTNGAVFVNGKEMTNQLPAVTCGTTVTFDMEAVTLGLPNNDGGNFKLRVTISSNNREVVFDWLLDQSCDSLYFGCSFSYPGWKVLVF
The following text describes a protein:
Function:
May play a role in MAPK signaling.
Subcellular Localization:
Cytoplasm. Cytoplasm, perinuclear region.
Domain:
All members of the FAM83 family of proteins share a conserved N-terminal DUF1669 (domain of unknown function 1669) domain of about 300 amino acids. This domain mediates the interaction with casein kinase 1 (CK1) isoforms. Therefore, it has been proposed to rename DUF1669 the polypeptide anchor of CK1 domain.
Sequence:
MAASQLAALEGVDSGPRVPGASPGFLYSEGQRLALEALLSKGAEAFQTCVQREELWPFLSADEVQGLAAAAEDWTVAKQEPSGMAEGATTTDVDAGSLSYWPGQSEQPAPVLRLGWPVDSAWKGITRAQLYTQPPGEGQPPLKELVRLEIQAAHKLVAVVMDVFTDPDLLLDLVDAATRRWVPVYLLLDRQQLPAFLELAQQLGVNPWNTENVDVRVVRGCSFQSRWRRQVSGTVREKFVLLDGERVISGSYSFTWSDARLHRGLVTLLTGEIVDAFSLEFRTLYAASCPLPPAPPQKPSVIGGLQRGRSPHRVSRRRSVAPASPPPPDGPLAHRLAACRVSPATPGPALSDILRSVQRARTPSGPPARPSRSMWDLSRLSQLSGSSDGDNELKKSWGSKDTPAKALMRQRGTGGGPWGEVDSRPPWGGALPLPPAHRLRYLSPARRRFGGDATFKLQEPRGVRPSDWAPRAGLGGQP
The following text describes a protein:
Function:
Required for assembly of the mitotic spindle. Interacts with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly, CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediate by KAR3.
Miscellaneous:
MISCELLANEOUS: Present with 56 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Note=Spindle microtubules that lie between the poles.
Sequence:
MARSSLPNRRTAQFEANKRRTIAHAPSPSLSNGMHTLTPPTCNNGAATSDSNIHVYVRCRSRNKREIEEKSSVVISTLGPQGKEIILSNGSHQSYSSSKKTYQFDQVFGAESDQETVFNATAKNYIKEMLHGYNCTIFAYGQTGTGKTYTMSGDINILGDVQSTDNLLLGEHAGIIPRVLVDLFKELSSLNKEYSVKISFLELYNENLKDLLSDSEDDDPAVNDPKRQIRIFDNNNNNSSIMVKGMQEIFINSAHEGLNLLMQGSLKRKVAATKCNDLSSRSHTVFTITTNIVEQDSKDHGQNKNFVKIGKLNLVDLAGSENINRSGAENKRAQEAGLINKSLLTLGRVINALVDHSNHIPYRESKLTRLLQDSLGGMTKTCIIATISPAKISMEETASTLEYATRAKSIKNTPQVNQSLSKDTCLKDYIQEIEKLRNDLKNSRNKQGIFITQDQLDLYESNSILIDEQNLKIHNLREQIKKFKENYLNQLDINNLLQSEKEKLIAIIQNFNVDFSNFYSEIQKIHHTNLELMNEVIQQRDFSLENSQKQYNTNQNMQLKISQQVLQTLNTLQGSLNNYNSKCSEVIKGVTEELTRNVNTHKAKHDSTLKSLLNITTNLLMNQMNELVRSISTSLEIFQSDSTSHYRKDLNEIYQSHQQFLKNLQNDIKSCLDSIGSSILTSINEISQNCTTNLNSMNVLIENQQSGSSKLIKEQDLEIKKLKNDLINERRISNQFNQQLAEMKRYFQDHVSRTRSEFHDELNKCIDNLKDKQSKLDQDIWQKTASIFNETDIVVNKIHSDSIASLAHNAENTLKTVSQNNESFTNDLISLSRGMNMDISSKLRSLPINEFLNKISQTICETCGDDNTIASNPVLTSIKKFQNIICSDIALTNEKIMSLIDEIQSQIETISNENNINLIAINENFNSLCNFILTDYDENIMQISKTQDEVLSEHCEKLQSLKILGMDIFTAHSIEKPLHEHTRPEASVIKALPLLDYPKQFQIYRDAENKSKDDTSNSRTCIPNLSTNENFPLSQFSPKTPVPVPDQPLPKVLIPKSINSAKSNRSKTLPNTEGTGRESQNNLKRRFTTEPILKGEETENNDILQNKKLHQ
The following text describes a protein:
Function:
Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity. Stabilizes AZIN2 by interfering with its ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MKKKRKKQATLPSSPLSWLDHKATIRRRPSLGSAPDVLNNKHSNSSSLKFANQLLKSVSNQGHEIKLKSFIRNITEKTVVCWDTVAIGERLYVHVPINVNRDSFVALLDYAEEELEVSQVVVCIDANSQDLPNMVKAFRFMGFEHIHPDDPSMKVLKQSSDLQGFRYLGYDLD
The following text describes a protein:
Function:
Has phosphatase activity toward PtdIns(4,5)P2 and at a lower extent toward PtdIns(3,4,5)P3 but not toward Ins(1,4,5)P3. Acts redundantly with CVP2 for maintaining vascular continuity. Regulates phosphoinositide-dependent VAN3 localization. Functions in salt stress response by regulating reactive oxygen species (ROS) production and stress-responsive genes expression.
Miscellaneous:
MISCELLANEOUS: Cvp1 and cvp2 double mutant displays high PtdIns(4,5)P2 levels.
Subcellular Localization:
Nucleus. Cell membrane; Peripheral membrane protein.
Sequence:
MRDDKTKKSKLSWSKKMVRKWFNIKSKTEKFQADVSLPQGVEVEHRNSFSEREPCTIKKSKTEKLNKNWEQQARQRKMNYENPRIIDVQNHSIFVATWNVAGRSPPEDLNLDEWLHSSAPADIYVLGFQEIVPLNAGNVLGAEDNGPAKKWHSLIRKTLNNLPGASSACHTPSPIPVPIAEIDADFSGSSRQKNETFFNRRSFQTPSVWSMEENDPSISQPRLDRRFSVCDRVFFSHRPSDFDPSFRCGHRPSDYSRRPSDYSRPSDYYSRPSNYSRPSDVSRWGSSDDDNGPGDSPSTFLNSPGSFLGSAANENGYRTPWNSSQYCLVASKQMVGIFLTIWVKSELREHVKNMKVSCVGRGLMGYLGNKGSISISMLLHQTSFCFVCTHLTSGQKEGDELRRNSDVMEILKKTRFPRVQSSADEKSPENILQHDRVIWLGDLNYRIALSYRSAKALVEMQNWRALLENDQLRIEQKRGHVFKGWNEGKIYFPPTYKYSNNSDRYAGGDLHPKEKRRTPAWCDRILWHGEGLHQLSYVRGESRFSDHRPVYGIFSAEVESNHKRSKRTNSHSTARVEAEELLPYARGYTELTFF