lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase. 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 microtubules. Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle. During spindle-kinetochore attachment, kinetochores first attach to the lateral surface of spindle microtubules, which supports the congression of chromosomes toward the middle of the dividing cell; they then slide along towards the spindle pole, a process independent of the DASH complex but requiring the NDC80 complex. When the end of a disassembling microtubule reaches the laterally attached kinetochore, the DASH complex together with the NDC80 complex and STU2 convert lateral attachment to end-on capture to produce a structure that can track with microtubule shortening and sustain attachment when tension is applied across sister kinetochores upon their biorientation. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached DASH complex to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids. Incorrect microtubule attachments are corrected by releasing microubules from the kinetochore through phosphorylation by IPL1 of kinetochore components. Links the microtubule cytoskeleton to chromosomes during interphase. Also contributes to the poleward transport of kinetochores on microtubules following centromeric DNA replication in S-phase.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Chromosome. Note=Associates with the mitotic spindle and the kinetochore. Associates with origin of replication (ORI) sites during interphase.
Sequence:
MGESLDRCIDDINRAVDSMSTLYFKPPGIFHNAILQGASNKASIRKDITRLIKDCNHDEAYLLFKVNPEKQSVSRRDGKEGVFDYVIKRDTDMKRNRRLGRPGEKPIIHVPKEVYLNKDRLDLNNKRRRTATTSGGGLNGFIFDTDLIGSSVISNSSSGTFKALSAVFKDDPQIQRLLYALENGSVLMEEESNNQRRKTIFVEDFPTDLILKVMAEVTDLWPLTEFKQDYDQLYHNYEQLSSKLRFIKKEVLLQDDRLKTMSQYHPSSSHDVAKIIRKEKDEIRRLEMEIANLQE
The following text describes a protein:
Function:
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MEGEFRENKKGQWSPYEMHGGTAIGICGDDYVVIGADTRLSVDYSIDSRHKARIFKMNSNCMISATGFDGDIDAFITRMRSILLNYENQHFHEMSVESVARCVSNTLYSKRFFPYYINILVGGINSEGKGKLYGYDPVGTIEDLHYDSNGSGSSLAAPLLDSAFGTIHHNTRPFPAVSLQDAKNIVRDAICSVTERDIYTGDALQLCVFTKDGFAQEEFPLPRH
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence:
MSRSGHRRGIFDGLPIPADKSYLKEGLSRIDEGWAAARFDSLPHVVHILTSKDRDGEIQFLKEQSDLIEDVVDEVVHAYHHGFNKAIQNYSQILRLFSESADSITGLKGEMAEAKKLLGRKNKHLGQLWYRSLTLRHVLSLLDQVEDVAKVPARIENLMAEKQLYAAVQLHVQSMLMLEREGLQAVGALQDVRSDLTKLRGVLFYKILEELHGHLYNNGEYSSVTLSMADSEDVPASTAAGRVLNSMQPLSRRTRSIKGDNHISGAVAADGFPKTSSIDGGSSFDGPDDDSSLDMRESDGRSRKDSKSISRQIPIFLSCAAPDEFIDSMIKADAPLNVKYLRTLVQCLSMLGKVAAAGAVICQRVRPTIHDVITSKIKAYSEEASKSSTDKAAKRTSDASHSDGPIPRFQMLKQKTKNGASVMAAQLVVSPISPAMAPTGDAQRAATQLLRSIFECLLDILENHIIVGDLLEQKSTSEVDNINTPHIVNGDASWNPDSESSQATGGFSVAFSLSVVQSECQQLLCEILRATPEAATADAAVQTARLANKDPVKEKRDGSEGLSFAFRITDSATSVPNEGQGWRRNSNVPQEGYGTASVIPDQGIFLAASVYRPVFEFMNKIGSMLPQKYSQLGSDGLLAFVDNFLKEHFLPAIFVDYRKCVQQAISSPAAFRPRVHATSVYDSLVELGRPVLQGLLAVDIIAKEVLGWVQLMPNYATELVEYVRTFLERTHERCRASYMEAVLEKQSYILLSRNDVESLMRLEPANIYLQNSTSQPDNNVTDAEAVEVEIELSDLLLDMCPIKQENLIHDDQKLILLASLSDSLEYLADSVERLGESFISPPTANHSQHGQHTRSSSAIPKGLASLANEYRRLAIDCVRVLRLEMQLEAVYHMQEMTKREYIEDQDAEDPDDFIISLTTQIARRDEEMAPYITESKRNYVFGGISSVAANASIKALAQMKSINLLGVQQICRNSIALEQALAAIPSIDSEAVQQRLDRVRTFYELLNLPFESLLGFIAEHEYLFSAKEYLSVLKVNVPGREIPMDAERRISQILGH
The following text describes a protein:
Function:
Cell surface receptor for IL3 expressed on hematopoietic progenitor cells, monocytes and B-lymphocytes that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Ligand stimulation rapidly induces hetrodimerization with IL3RB, phosphorylation and enzyme activity of effector proteins such as JAK2 and PI3K that play a role in signaling cell proliferation and differentiation. Activation of JAK2 leads to STAT5-mediated transcriptional program (By similarity).
Miscellaneous:
MISCELLANEOUS: The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Domain:
The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding; The box 1 motif is required for JAK interaction and/or activation.
Sequence:
MVLLWLTLLLIALPCLLQTKEDPNPPITNLRMKAKAQQLTWDLNRNVTDIECVKDADYSMPAVNNSYCQFGAISLCEVTNYTVRVANPPFSTWILFPENSGKPWAGAENLTCWIHDVDFLSCSWAVGPGAPADVQYDLYLNVANRRQQYECLHYKTDAQGTRIGCRFDDISRLSSGSQSSHILVRGRSAAFGIPCTDKFVVFSQIEILTPPNMTAKCNKTHSFMHWKMRSHFNRKFRYELQIQKRMQPVITEQVRDRTSFQLLNPGTYTVQIRARERVYEFLSAWSTPQRFECDQEEGANTRAWRTSLLIALGTLLALVCVFVICRRYLVMQRLFPRIPHMKDPIGDSFQNDKLVVWEAGKAGLEECLVTEVQVVQKT
The following text describes a protein:
Function:
May be involved in cell wall biosynthesis.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MMTPDFRSLPMLRNLRITRLVLGLTLSALATFVWVRADMPHFWPKLLDAVTHEPHPIIDHFPAFTPNVGCLSRSQQYKYRKQKNHFPISEPLTRALVKYTRMHSHCQLTKVGDVDSMQAACQYVVYYEGYEGLGNRLLSLVTAFSYALITNRALVIDERRGHLAQLLCQPFHNTSWLLPSHLALAVQKRAVKLQDMINNEVQNVTSVHVNLRHEQTLGDRTFFCSESQELLRKVTWVIWESNQYYVPRLFMIREFWPTLRLWFPNVSLVFTQLGRILSVPRNGVWETIERIQQAEMAWARVQVGIQVRRHGVSDNANFSETVYQRILKCVGEHAVLPNRTTAAVLVTSLRSVYWEKMRERWHGRDDEEGEVKFVMVSEEKEERYSYDQACKAMVEIWLLSFCDRLATSSWSTFGYVAQALAGIQPVIMNIRGEHPELDEQAQCWRGQSVEPCLHYPFIFRDDDSGTAYCISQAKPNLLPKRPQKEEEVETKQQEEHSAWIARHLVVCQDETRGLQLVS
The following text describes a protein:
Function:
Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Sequence:
MAEQAKLPDQAQPVPETQVPDNGKPEQQPTATESAPAPEPATTEPTTAATAPSAVDGTGETAPAAPEPAAAPVAAAAAAPAPEPTKSEPQPAVGEQSEPAKKDEPAKPEYFTKTPALEQFFDRLPTILSNTGHQEMWGVPLKHEVTDIPTINVLIKFLRANAGDLKAAEDQLSKALTWRKENDPIALADASKNSYDASKFKGLGYLTTYQREGKGDLVVTWNIYGAVKKFDETFGDITEFIKWRAALMELAVQELKLDQATSVIDYDGEDPYQMIQVHDYLNVSFLRMNPNVKAATKKTIDVFSTAYPELLREKFFVNVPAIMGWMFAVMKVFVNQNTARKFHPISNGANLAKEFPAGVAEKFPKAYGGSAPDLESSARTVALKEVKEEKKEEPKEGSKEEQKGEQKGE
The following text describes a protein:
Function:
Dual methyltransferase that catalyzes methylation of elongation factor 1-alpha (EEF1A1 and EEF1A2) at two different positions, and is therefore involved in the regulation of mRNA translation (By similarity). Via its C-terminus, methylates EEF1A1 and EEF1A2 at the N-terminal residue 'Gly-2' (By similarity). Via its N-terminus dimethylates EEF1A1 and EEF1A2 at residue 'Lys-55' (By similarity). Has no activity towards core histones H2A, H2B, H3 and H4 (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Mitochondrion.
Sequence:
MNLLPKSSKEFGSADYWEKFFQQRGKTAFEWYGTYLELCEVLHKYIKPKEKVLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLDAVLTDEEEVTLRQVDRMLAEVGRVLQVGGRYLCISLAQAHILKKAVGHFSREGWMVRAHQVASSQDRVSEAEPRFSLPVFAFVMTKFRPVPGSALQIFELCTQEQGKPVRLESADQLAEAVRERQYYAWLCSQLRRKAGLGSVSLDLCSGDTGEPRYTLHVVDNPAVKPSRDNHFAIFIIPQGRETEWLFGMEEGRKQLAASAGFRRLVTVALHRGQRYAGMESIQAELSARVMELAPAGLPPQQQVPFLSVGGDIGVRTVQHQDHSALSGDYVIEDVQGEDRWYFRRLIFLSNRNVVQSEARLLKDTSHRAQKKRKKDRKKQRPADTSEDFPPAPGQSIDKSYLCCEHHKAMVAGLALLRNPELLLETPLTLLVVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFSQSDRMKVHIADGLDYITSLAGEAPPHYDVIMFDVDSKDPTLGMSCPPPAFVDQVFLQKVKSILCHDGVFILNLVCRDVRLKDSVLAGLKAAFPLLYVRRIEGEVNEILFCQLHPEQKLATPELLEMAQVLERTLRKPGQGWDDTYVLSDMLKTVKIV
The following text describes a protein:
Function:
Transcription factor that is required for cell fate of coelomocytes which are non-muscle mesodermal cells. Acts in concert with, and by activating expression of, the homeodomain gene ceh-34. Binds to the sequence motif 5'-ATAAA[T/C]A-3'.
Subcellular Localization:
Nucleus.
Sequence:
MECSTAIYSLANALGPLKLDSTAPNNSHRTIKAENYFNEDEEDYNENSHEDSEDSKEDSDGQGCRSRKRKEKPPFSYIALIAMAISKRPDKKATLAEIYSYLQENFEFFRGEYAGWRNSIRHNLSLNECFVKLPKDTGESYRGRKGHKWTISDSCEFMLEENGFRRRPRGYKARKRTHFPGVTASNEMGIGGATFDYPSSTTELTDSGTSSLNTDVKNILLNGGEDFGPSISDQLVSSTTSAVLPSLNGPDQSPIYPNYFGYGTAEFPMQWASPTYDWPYYATPHIGLCSSDFPGISPSPTVTPQVSPYFYPPAITTASSFMDDWRFGVSSAAVGAYDSSASFLAAETTAGDVAIPQDLSDC
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates 60S ribosomal protein L1.
Sequence:
MLQLCPLDEDTLYTHVYERYVELDRHAETLAQDLGIHASDAETLVVDIAPAQPTKSSDTYSLTVSQSLASLRSSTVNNNSTTGYVLWSGTPFFLCWLLYAPSAAPLRDGGRVPVTDSAAQFLQLPPLFSAPARPVCVVELGSGAAGVAAIVLANYVDRYLVSDQKAILKPLRANLLANISEVSRRTVCSKQTPELSSNRRTPARCELELIALDWERIATVPAALRPTDAAHVHVLALDVVYNDFLIPPLLTAIKRLLRWYADEHAVKATAYVLVHLRAQDILQTFLEHAIIDLRLRCYYMDEERLRSSRFALYYVTL
The following text describes a protein:
Function:
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Sequence:
MQKIALCITGASGVIYGIKLLQVLEELDFSVDLVISRNAKVVLKEEHSLTFEEVLKGLKNVRIHEENDFTSPLASGSRLVHYRGVYVVPCSTNTLSCIANGINKNLIHRVGEVALKERVPLVLLVREAPYNEIHLENMLKITRMGGVVVPASPAFYHKPQSIDDMINFVVGKLLDVLRIEHNLYKRWRG
The following text describes a protein:
Function:
Toxic component of a toxin-antitoxin (TA) system. An RNase.
Sequence:
MLIVDTSVWIDFLRGEKTKACETLRELINSEEEIYITEIILTEILQGIKDDKLHHITKEYLLYFQILRPKGIETYIRASEIFRNCKKKGKTVRKTIDCIIASIAIENRATIIHKDHDYETIREFSELKTINMGNFC
The following text describes a protein:
Function:
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Sequence:
MKYVLVSGGVISGIGKGVIASSTGLLLKTLGLKVTSIKIDPYMNIDAGTMSPLEHGEVFVLNDGGEVDLDLGNYERYLNVTLTRDNNITTGKVYSRVIEKERRGDYLGKTVQIVPHVTNEIQDWIERVARIPVDETGEEPDVCIIELGGTVGDIESAPFVEAMRQFQFRVGHENFVSIHVSLVPVINGEQKTKPTQQAIRDLRSLGISPDLIACRSIRNNTARVQAGASMWASWKQLTSGHDRLFKKVSIVLVGKYTHLQDSYISVIKSLEHSAMRCGRKLDLQWVEAADLENETNNTDPLRYHKAWHLVCSADGILVPGGFGTRGIEGMIAAAKWARENNTPYLGICLGLQVAVIEYARNVCGIEEATSSEFDPDAKEPVVIYMPEISKDKLGGTMRLGLRPTVFQAGSEWSKLRKLYGNRAEVLERHRHRYEVNPEYIERIQTAGLTFIGKDDRGERMEIIEKKDHPYYVGVQYHPEYLSKPLNPSVPLFGLVAASAGVLDRFLESGEPVHWESSSIFNPDTPLSDFTDTVVVNSASA
The following text describes a protein:
Function:
Plays an important role in ciliogenesis. Required for apical targeting/anchoring of centrioles at the plasma membrane.
Subcellular Localization:
Cell projection, cilium. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Localized to basal bodies in multiciliated cells.
Sequence:
MSLRDRQFREEPSENALPLDRNHFRPSTEYDQSYEPLEASGQSGDSDLVSEYAQGNMSVTVSEEELRHELSLLGFSYVPRQRLLEFKKDLERLMNRGSAAASPETSRLENESLDDSTNTPPPLPIETSAWHQTSAWPTTTSTSSKEWDNQQRNQDSYTKHTVSLGGNVQATKKAPQITRKVLRRKSDGQTHVSDESFLYSETETEEEDTGSSIVDFRSESSGRSSASCAKSFIRPPLYSLLDQYRQRSDPVGRYQEYKQKWDALQGALERNRKELRWGIREQMMSAPPQPAARSVLLPNTYVIPTDKKRYALRWAVRRDLVNGVMPRGSYS
The following text describes a protein:
Function:
Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding (By similarity).
Subcellular Localization:
Cytoplasm. Secreted.
Sequence:
MAKLIFLTGLAFLLNAQLGSAYQLVCYFSNWAQYRPGLGSFKPDNIDPCLCTHLIYAFAGMSNSEITTIEWNDVALYSSFNDLKKKNSQLKILLAIGGWNFGTAPFTAMVATPENRKTFISSVIKFLHQYGFDGLDFDWEYPGFRGSPSQDKHLFTVLVQETREAFEQEAKQTNKPRLLVTAAVAAGISNIQAGYEIPQLSQYLDFIHVMTYDFHGSWEGYTGENSPLYKYPTDTGSNTYLNVEYAMNYWKKNGAPAEKLIIGFPAYGHNFILRDASNNGIGAPTSGAGPAGPYTREAGFWAYYEICAFLKDGATEAWDDSQNVPYAYKGTEWVGYDNVNSFRIKAQWLKENNFGGAMVWAIDLDDFTGTFCNQGKFPLINTLKDALGLKSATCNASTQSSEPNSSPGNESGSGNKSSSSEGRGYCAGKADGLYPVADNRNAFWNCVNGITYKQNCLTGLVFDTSCHCCNWA
The following text describes a protein:
Function:
Forms a tunnel that spans the entire periplasmic space. Is probably involved in the transport of lipids between the inner membrane and the outer membrane through the tunnel. Forms a dynamic tunnel sufficiently long to mediate lipid transport directly between the two membranes without the need for a shuttle protein. Binds phospholipids. Lipids bind inside the tunnel. Required for outer membrane homeostasis. Contributes to membrane integrity.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein; Periplasmic side.
Domain:
The seven MCE (Mammalian Cell Entry) domains of a single protomer of LetB resemble seven beads on a string. Six copies of this linearly configured protomer associate laterally to form a homohexameric assembly. The LetB hexamers form an elongated tube consisting of seven stacked MCE rings, each formed from the association of six identical MCE domains, with a central tunnel. Rings 1, 5, 6 and 7 are dynamic and adopt open and closed states. Studies with shorter mutant forms of LetB show that a five- or six-ring form of LetB is functional, but that the four-, three- and two-rings variants are stable and properly folded in vitro, but not functional. Mutants lacking ring 1, ring 2, ring 5 or ring 7 are non functional. Mutants lacking ring 6 or ring 3 are more resistant to lauryl sulfobetaine (LSB) and cholate.
Sequence:
MSQETPASTTEAQIKNKRRISPFWLLPFIALMIASWLIWDSYQDRGNTVTIDFMSADGIVPGRTPVRYQGVEVGTVQDISLSDDLRKIEVKVSIKSDMKDALREETQFWLVTPKASLAGVSGLDALVGGNYIGMMPGKGKEQDHFVALDTQPKYRLDNGDLMIHLQAPDLGSLNSGSLVYFRKIPVGKVYDYAINPNKQGVVIDVLIERRFTDLVKKGSRFWNVSGVDANVSISGAKVKLESLAALVNGAIAFDSPEESKPAEAEDTFGLYEDLAHSQRGVIIKLELPSGAGLTADSTPLMYQGLEVGQLTKLDLNPGGKVTGEMTVDPSVVTLLRENTRIELRNPKLSLSDANLSALLTGKTFELVPGDGEPRKEFVVVPGEKALLHEPDVLTLTLTAPESYGIDAGQPLILHGVQVGQVIDRKLTSKGVTFTVAIEPQHRELVKGDSKFVVNSRVDVKVGLDGVEFLGASASEWINGGIRILPGDKGEMKASYPLYANLEKALENSLSDLPTTTVSLSAETLPDVQAGSVVLYRKFEVGEVITVRPRANAFDIDLHIKPEYRNLLTSNSVFWAEGGAKVQLNGSGLTVQASPLSRALKGAISFDNLSGASASQRKGDKRILYASETAARAVGGQITLHAFDAGKLAVGMPIRYLGIDIGQIQTLDLITARNEVQAKAVLYPEYVQTFARGGTRFSVVTPQISAAGVEHLDTILQPYINVEPGRGNPRRDFELQEATITDSRYLDGLSIIVEAPEAGSLGIGTPVLFRGLEVGTVTGMTLGTLSDRVMIAMRISKRYQHLVRNNSVFWLASGYSLDFGLTGGVVKTGTFNQFIRGGIAFATPPGTPLAPKAQEGKHFLLQESEPKEWREWGTALPK
The following text describes a protein:
Function:
Nick-sensing 3'-phosphoesterase involved in a base excision repair pathway required for active DNA demethylation. The N-terminal DNA-binding domain binds specifically to gap sites and sharply bends the target DNA. Lacks 5'-kinase activity but is capable of 3'-phosphoglycolate end processing. Inactive on 3'-alpha,beta-unsaturated aldehyde (3'-dRP). Protects partially genes from transcriptional silencing by preventing promoter DNA hypermethylation.
Subcellular Localization:
Nucleus, nucleoplasm. Note=Not found in the nucleolus. Co-localizes in nucleoplasmic foci with APE1L and ROS1, two components of the DNA demethylase machinery.
Sequence:
MITVAPFVSLRFQFPLYIINRSTLFFRERTQYLVYNTCHILRTTAKTMPVVAEYAKSNRSSCRSCSNKIAVKSLRLGLISKGRGGVDMTRWHHFDCFPTDSESIASVDDIQGLSALEKEDQDALTKLVEQCGKVPAKKPDEKKGKAKKHIMGPKGLTKAATSSKVIADNAKSSRSSCNRCSQTIVSKDLRVGLVTEDSRGFDITRWHHLGCFPIDFHPIDSVEDIGGYSSLEKGDQMELKYLAEVNKKDKTLIDDVQKMDEGDDEAIADNELTEETKKGKHSPVAKLVEQPGEPAKEDEDEESKKPASDEISEQKTKDVKNSPDSSKVISEYAKSSRSTCKKCSQTIAAKELRLGLVTRNFRGFDMKQWHHLGCFPVDSDPIVSVEDIGGFSELQSGDQDALKELVQQCGKQTLVDKMDEDNDDTEAKIKLTEETNKRKHSEVGEMVEEDESLTKAKQQMAKTHKVNMSESTSQVEVEAEITLSASDVKDKYRDANLLPKWKAFETVIFLERDDGLNDSEKIAAFDFDGCLAKTSVKIVGADAWSLMYPSIPEKLQSLHDQGYKLVIFTNESNIDRWKNKRQAAVDSKIGRLNSFIERVKVPIQVFIACGVSSSGGKGGKDDLYRKPKAGMWQLMKKHFNSGIAIDMDKSFYVGDAAGRKMDHSDADIKFAQASGLKFFTPEEYFIPSSTSPGT
The following text describes a protein:
Function:
Transcriptional regulator that activates the expression of punC, which encodes a purine nucleoside transporter. In the presence of adenine, it binds to a conserved 23-bp palindromic motif in the intergenic region between punR and punC.
Subcellular Localization:
Cytoplasm.
Sequence:
MWSEYSLEVVDAVARNGSFSAAAQELHRVPSAVSYTVRQLEEWLAVPLFERRHRDVELTAAGAWFLKEGRSVVKKMQITRQQCQQIANGWRGQLAIAVDNIVRPERTRQMIVDFYRHFDDVELLVFQEVFNGVWDALSDGRVELAIGATRAIPVGGRYAFRDMGMLSWSCVVASHHPLALMDGPFSDDTLRNWPSLVREDTSRTLPKRITWLLDNQKRVVVPDWESSATCISAGLCIGMVPTHFAKPWLNEGKWVALELENPFPDSACCLTWQQNDMSPALTWLLEYLGDSETLNKEWLREPEETPATGD
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MEMQSYYAKLLGELNEQRKRDFFCDCSIIVEGRIFKAHRNILFANSGYFRALLIHYIQDSGRHSTASLDIVTSDAFSIILDFLYSGKLDLCGENVIEVMSAASYLQMNDVVNFCKTYIRSSLDICRKMEKEAAVAAAVAAAAAAAAAAAAAAAHQVDSGSPSSGREGTSCGTKSLVSSPAVGEKSVDCLRESPCGDCGDCHPLELVVKDSLGGGSADSDLSTPPKRIEPKVEFDADEVEVDVGEQLQQYAAPLNLAHVEEALPSGQTVDLAYSNYHVKQFLEALLRNSAAPSKDDADHHFSRSLEGRPEGAGVAMSSMMDVQADWYGEDSGDVLVVPIKLHKCPFCPYTAKQKGILKRHIRSHTGERPYPCETCGKRFTRQEHLRSHALSVHRSNRPIICKGCRRTFTSHLSQGLRRFGLCDSCTCVTDTPDDDDDLMPINLSLMEASSESQEKSDTDNDWPIYVESGEENDPAGDDSDDKPQIQPNLSDRETLT
The following text describes a protein:
Function:
Protects the cell against copper toxicity by tightly chelating copper ions. May also act as a depository for copper designated for the effective transfer into the apo forms of copper proteins.
Miscellaneous:
MISCELLANEOUS: There are 2 copies for copper thionein in yeast. The 2 identical copies CUP1-1 and CUP1-2 are arranged in tandem.
Domain:
Contains 1 metal-binding domain: 6 to 8 copper ions are chelated within a single copper-thiolate cluster and are coordinated via cysteinyl thiolate bridges to 10 cysteine ligands. 6 copper ions are trigonally coordinated, whereas the other 2 are only digonally coordinated.
Sequence:
MFSELINFQNEGHECQCQCGSCKNNEQCQKSCSCPTGCNSDDKCPCGNKSEETKKSCCSGK
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:
MKKKTADRKRFSRQLKDCPIDRPFEVKKTKNKRHILGTKTKNGRFAGYTNSKLALKRKDRLNTMIEQRTKRNKIVDHRLGEYDQSLSAEDKMIQRFAVEKKKHHEKAEAYQLEDYQLTHLGQSLAEVENFQEDEKFSSDEDNDNAQDDSDLYFGGFLKKKSESQSESTNQYERKREKERTENMMLNIDEEWKEMMPVLIQSSINAANTTRQENKVDSYDKSVRELAFDLKAKATSRLKSEEELIKEEKEKLEQLEADRLRRMKGLPDTSEKRPKHLSADAMETNIEEIRDKRIALRYMDGKAVIPEGYTEEELLPRSKATTVDDNELSDQEDVSDDDNDQNSDEAESAEEEGSEEEEEDLEEEEEISEEDSDSLEDLNSDEDVNSPQESENEDSAEEMNKQEEKNTVSLEMKAAAEELPYQFKAPASYNEFKSLVTKRSLQDQLTIIDRLRTHYHISLDSKNRGKLEVLLDCLLHHLENITQEFTEQMLNSNVLDGLIKHIFSLAQVSPQYTANCCLLFLNKYVNETKKKGKAAFPGIHQLIFFRVMAIIFPTTDYHHCISTPTMLYMGKLLIESNVESLTDITKGLFICNNILDYVSKSKRFVPEVVIFLTDIISAFSTFKDRKYENLLHIENLERLSLLALAIDLLDQFAKLYANAVAFPEIYHRTSEILNCIDIEGYPAEIKANYESIQMKISSSISEPRNYLILQKRKPQPLKLLEPRFEDRTQTNSERSYGNKKHLEKMKDRRQNKRDQKRLTRELRRDSRYVAMKQREDRRMRDTERKRKVKEIEHLLSNQQAEMKAYKKRK
The following text describes a protein:
Function:
Junctional adhesion protein that mediates heterotypic cell-cell interactions with its cognate receptor JAM3 to regulate different cellular processes. Plays a role in homing and mobilization of hematopoietic stem and progenitor cells within the bone marrow. At the surface of bone marrow stromal cells, it contributes to the retention of the hematopoietic stem and progenitor cells expressing JAM3. Plays a central role in leukocytes extravasation by facilitating not only transmigration but also tethering and rolling of leukocytes along the endothelium. Tethering and rolling of leukocytes are dependent on the binding by JAM2 of the integrin alpha-4/beta-1. Plays a role in spermatogenesis where JAM2 and JAM3, which are respectively expressed by Sertoli and germ cells, mediate an interaction between both cell types and play an essential role in the anchorage of germ cells onto Sertoli cells and the assembly of cell polarity complexes during spermatid differentiation (Probable). Also functions as an inhibitory somatodendritic cue that prevents the myelination of non-axonal parts of neurons. During myogenesis, it is involved in myocyte fusion (By similarity). May also play a role in angiogenesis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cell junction. Cell junction, tight junction. Note=Localized at tight junctions of both epithelial, endothelial cells and Sertoli cells. Specifically localized within the somatodendritic compartment of neurons and excluded from the axon.
Domain:
The Ig-like V-type domain is necessary and sufficient to mediate interaction with JAM3 and integrin alpha-4/beta-1.
Sequence:
MARSPQGLLMLLLLHYLIVALDYHKANGFSASKDHRQEVTVIEFQEAILACKTPKKTTSSRLEWKKVGQGVSLVYYQQALQGDFKDRAEMIDFNIRIKNVTRSDAGEYRCEVSAPTEQGQNLQEDKVMLEVLVAPAVPACEVPTSVMTGSVVELRCQDKEGNPAPEYIWFKDGTSLLGNPKGGTHNNSSYTMNTKSGILQFNMISKMDSGEYYCEARNSVGHRRCPGKRMQVDVLNISGIIATVVVVAFVISVCGLGTCYAQRKGYFSKETSFQKGSPASKVTTMSENDFKHTKSFII
The following text describes a protein:
Function:
Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Sequence:
MFGELVCGPPGSGKTTYCEGKRQFLSVYEPTRPVVLLNLDPANEDIFPYPCDVDIREVVSHVRVMETEELGPNGSYLFCAALMERRIDWIIQKVEEAVDRRLRDVVITGGGSVHPRPPYLIIDCPGQVEFYLGSPVMHTLFRALQKRLCCTLCTVHLVDASVSTRDISTYVSSCLLSITTMIDHELPHINVFSKWDTLSVEDSEEGEAYLRASSFMAEDFDRLWKKQLRQRRRNQRLAKLYPTGAEKLDARDEPSAAARDDMEVEAIDLEKDGGHLYRYSKAVMEVVDGYGLIGFLPLDVQSQDMMTRLTQQIDDCIGNFL
The following text describes a protein:
Function:
Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity. May target specifically CDKA-1.
Subcellular Localization:
Nucleus, nucleoplasm. Note=Homogeneously distributed. Accumulates strongly in vegetative cell nuclei immediately after asymmetric division and disappears later.
Sequence:
MSETKPKRDSEYEGSNIKRMRLDDDDDVLRSPTRTLSSSSSSSLAYSVSDSGGFCSVALSEEEDDHLSSSISSGCSSSETNEIATRLPFSDLEAHEISETEISTLLTNNFRKQGISSSENLGETAEMDSATTEMRDQRKTEKKKKMEKSPTQAELDDFFSAAERYEQKRFTEKYNYDIVNDTPLEGRYQWVSLKP
The following text describes a protein:
Function:
Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MKKKQTKVKQTVKLVLRNPLSISWPIVDANTQEKLAQTLVQWLPASHKDILDSKLTVGLNSVNELLERCCQNAKDVTQPAVVFILHDQDSMLVTHMPQLVANANFYGSSKCRLVPLGFSAQALIAKKLGLSRAGAIAVQDDSPLWKYLKDLVMNIEEPQARWLSENPEYEVTKVEKIITSQKENQGTKKEGKNEKGNEFKK