wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 541 (Spermatogenic cell HDAC-interacting protein 1) (Q0GGX2)
Organism: Mus musculus (Mouse)
Function: Component of some chromatin remodeling multiprotein complex that plays a role during spermatogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:17662146, ECO:0000269|PubMed:18849567, ECO:0000269|PubMed:34075040, ECO:0000269|PubMed:35320728, ECO:0000269|PubMed:35341968}.
Interaction partners:
- Deoxynucleotidyltransferase terminal-interacting protein 1
- BTB/POZ domain-containing protein KCTD19
- Ribosomal protein S6 kinase-like 1
Sequence:
MEPYSLGEEGALPSEGHLPSFSESQVLNCSDTLNRDLGPSTRDLLYAGLSGLDLDPSLSTSDMPSEVLEDNLDTLSLYSGKDSDSVKLLEEYADSESQTSLQDLGLGALKVPKEADEGGRATGSTRKGKRQHSSPQNPLLDCSLCGKVFSSASSLSKHYLTHSQERKHVCKVCSKAFKRQDHLTGHMLTHQKTKPFVCIEQGCSKSYCDYRSLRRHYEVQHGVCILKETPPEEEAYGDPTHNHDVANQPPPSGLRSLGPPEARSPGSVLPNRDLLRCIVSSIVHQKIPSPGPAVGPSDTEARSSACACPTSLGSSSCTPASTPVALGTLGSEIPEETHPPRKEAATEVFTPVQSRAAENGVPDPPESELESESPRLQRPSSLEGWPEGSSLPACLPLFRGHSVPSGSQPSSHNFQWLRNLPGCPKNKGSNVFMVHKPPAVASREGSEGGGSGPSSTPTSVEPSPSLGTTQEELLPFPPALLKAPGEASSEVRQAAGEDETWAPKKCKPDCESFPWQSPTELGLQDAQNPGGLPSDATPLFRQLFMKSQESLVSHEQMQVLQMIAKSQRIFSHTQVATASAQRPGPEGKQSTLKPLQGPWPPQTLPPAPTVDSFQIGPGHSEPEGSPVRRRKTMPAVSRETSPGGPRRDTKGGPKVASAPPSLTGPGLLPSRNPDSSSLAKGTLDLGDIIPNAGSRQSQLGGDEPAGTQLVGKQGQGENGLASGAMRGEKGPACPRGGGYRLFSGHPRAQRFSGFRKEKVKMDVCCAASPSQVAMASFSSAGPLADPPRDMKSKLTIFNRIQGGNIYRLPHPVKEESLAGGCHQPNGGPTDWMESKSTFVCKNCSQMFYTEKGLSSHMCFHSDQWPSPRGKQEQQVKGQMVASVKRKAGREEGAVEDMKRHYDCSSSEPQDVTILSMLVSSGSCGVTPVVLSSLLQGQEKDGEERDSKESCQYRKRKKRPQPKALFAPPAPSALGEPGPGGCHQSCLHSPVFLVDHLLKGLFQCSPYTPPPMLSPIREGSGLYFNTLCSTSRAGPHLISPVLDQVDSSFGICVVKDDTKISIEPHINVGSRFQAEIPELQERLLARVDENVASLVWKPWGDVMTNPETQDRVMELCNVACSSVMPGGGTNLELALHCLHDAQGSVQVALETLLLRGPQKPRTHPLADYRYTGSDIWTPMEKRLFKKAFCAHKKDFYLIHKMIQTKSVAQCVEYYYIWKKMVKFDCGRAPGLEKRGRRELDEVERTEDKVTCSPRERPTHRPTPELKIKTKSYRRESILHSSPSAAPKRTPEPPGSVESQGVFPCRECERVFDKIKSRNAHMKRHRLQEHVEPVRVKWPVKPYPLKEEEEEEEEELGADMGPLQW
Protein: Epididymis secretory sperm binding protein (Myeloid cell nuclear differentiation antigen, isoform CRA_a) (cDNA FLJ78191, highly similar to Homo sapiens myeloid cell nuclear differentiation antigen, mRNA) (Q5VUU6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVNEYKKILLLKGFELMDDYHFTSIKSLLAYDLGLTTKMQEEYNRIKITDLMEKKFQGVACLDKLIELAKDMPSLKNLVNNLRKEKSKVAKKIKTQEKAPVKKINQEEVGLAAPAPTARNKLTSEARGRIPVAQKRKTPNKEKTEAKRNKVSQEQSKPPGPSGASTSAAVDHPPLPQTSSSTPSNTSFTPNQETQAQRQVDARRNVPQNDPVTVVVLKATAPFKYESPENGKSTMFHATVASKTQYFHVKVFDINLKEKFVRKKVITISDYSECKGVMEIKEASSVSDFNQNFEVPNRIIEIANKTPKISQLYKQASGTMVYGLFMLQKKSVHKKNTIYEIQDNTGSMDVVGSGKWHNIKCEKGDKLRLFCLQLRTVDRKLKLVCGSHSFIKVIKAKKNKEGPMNVN
Protein: Cyclin-dependent kinase 4 inhibitor C (Cyclin-dependent kinase 6 inhibitor) (p18-INK4c) (p18-INK6) (Q60772)
Organism: Mus musculus (Mouse)
Function: Interacts strongly with CDK6, weakly with CDK4. Inhibits cell growth and proliferation with a correlated dependence on endogenous retinoblastoma protein RB.
Interaction partners:
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase 4
- G1/S-specific cyclin-D3
- G1/S-specific cyclin-D1
- G1/S-specific cyclin-D2
- Cellular tumor antigen p53
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase inhibitor 1
- Menin
- Tumor suppressor ARF
Sequence:
MAEPWGNELASAAARGDLEQLTSLLQNNVNVNAQNGFGRTALQVMKLGNPEIARRLLLRGANPNLKDGTGFAVIHDAARAGFLDTVQALLEFQADVNIEDNEGNLPLHLAAKEGHLPVVEFLMKHTACNVGHRNHKGDTAFDLARFYGRNEVISLMEANGVGGATSLQ
Protein: Folate transporter 2 (PfFT2) (Q8IIK1)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell membrane {ECO:0000269|PubMed:21998306}; Multi-pass membrane protein {ECO:0000255}. Note=In intraerythrocytic stage parasites, localizes to the plasma membrane and some intracellular vesicular structures. {ECO:0000269|PubMed:21998306}.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1, putative
- GTP cyclohydrolase 1
- Protein YOP1, putative
Sequence:
MIEKSNNPFLSIDPIVERTKSNGEGLPLLSEKTKKGFDFTQIVVYLVGLSDGLTHLASLAIYYLFKDYFRLTPYQVSLILMYPYIPFILKPVIALITDSFSIFGMRRKPYLFLFSLFQSLNFLALAFLNLSVIQASLILFFISLCASFCTTVAEALVVESSMGQTYSQGTNKVTEFIASKAIGSLSVAYFSGYFLEKMPREYIFIATSIFPLIISLSCLFLKEKEYSTNRNIFNQLSDLIKFINTPIFLGPFLYIFVYMSGPDYDDAFFFFCTNKLGFRPSFMGTLRLTYGIASLIGIIIYRVFLKNCSLRKTLIITTLVSFPIYISPIILTEHINKFLGISNELFVLSGGFLIEAITEIQLLPLFILTANICQPGLEASVFATILSVKNLGSLTKKGTSSFITYLMKIDSYNFDNLSLYILTCGFFLLFSLTLVPLLPNEEHIEKLKNKETSKG
Protein: Adhesion G-protein coupled receptor D1 (G-protein coupled receptor 133) (G-protein coupled receptor PGR25) (Q6QNK2)
Organism: Homo sapiens (Human)
Function: Orphan receptor. Signals via G(s)-alpha family of G-proteins. Has protumorigenic function especially in glioblastoma.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22025619, ECO:0000269|PubMed:25533341}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- E3 SUMO-protein ligase RanBP2
- Ran GTPase-activating protein 1
- Exportin-1
- Exportin-T
- Exportin-2
- Importin subunit beta-1
- Guanine nucleotide-binding protein G
- Ran guanine nucleotide release factor
- Probable non-functional immunoglobulin heavy variable 3-16
Sequence:
MEKLLRLCCWYSWLLLFYYNFQVRGVYSRSQDHPGFQVLASASHYWPLENVDGIHELQDTTGDIVEGKVNKGIYLKEEKGVTLLYYGRYNSSCISKPEQCGPEGVTFSFFWKTQGEQSRPIPSAYGGQVISNGFKVCSSGGRGSVELYTRDNSMTWEASFSPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSRDYGESNVNLVIGSEQDQAKCYENGAFDEFIIWERALTPDEIAMYFTAAIGKHALLSSTLPSLFMTSTASPVMPTDAYHPIITNLTEERKTFQSPGVILSYLQNVSLSLPSKSLSEQTALNLTKTFLKAVGEILLLPGWIALSEDSAVVLSLIDTIDTVMGHVSSNLHGSTPQVTVEGSSAMAEFSVAKILPKTVNSSHYRFPAHGQSFIQIPHEAFHRHAWSTVVGLLYHSMHYYLNNIWPAHTKIAEAMHHQDCLLFATSHLISLEVSPPPTLSQNLSGSPLITVHLKHRLTRKQHSEATNSSNRVFVYCAFLDFSSGEGVWSNHGCALTRGNLTYSVCRCTHLTNFAILMQVVPLELARGHQVALSSISYVGCSLSVLCLVATLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQVLLLISFRLEPGTTPCQVMAVLLHYFFLSAFAWMLVEGLHLYSMVIKVFGSEDSKHRYYYGMGWGFPLLICIISLSFAMDSYGTSNNCWLSLASGAIWAFVAPALFVIVVNIGILIAVTRVISQISADNYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVNGCAVVFQYMFATLNSLQGLFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSARTSNAKPFHSDLMNGTRPGMASTKLSPWDKSSHSAHRVDLSAV
Protein: Serine/threonine-protein kinase STN7, chloroplastic (EC 2.7.11.1) (Protein STATE TRANSITION 7) (Stt7 homolog) (Q9S713)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine protein kinase required for state transition by phosphorylating light-harvesting complex II outer antennae (LCHII). State transition plays a central role in response to environmental changes and allows to adjust to changing light conditions via the redistribution of light excitation energy between photosystem II (PSII) and photosystem I (PSI). Phosphorylates the minor light harvesting protein LHCB4.2/CP29 and is involved in the light-dependent phosphorylation of TSP9. Acts as a key component of the long-term response (LTR) signaling pathway. Mediates phosphorylation-dependent PTAC16 subcellular localization to regulate plastid gene expression.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:15729347}.
Interaction partners:
- Protein phosphatase 2C 57
- Photosystem II 22 kDa protein, chloroplastic
- Probable protein phosphatase 2C 26
- Chlorophyll a-b binding protein 3, chloroplastic
- Protein PROTON GRADIENT REGULATION 5
- Chloroplast sensor kinase, chloroplastic
- 29 kDa ribonucleoprotein, chloroplastic
- Dual specificity phosphatase Cdc25
- Origin of replication complex subunit 2
- Chlorophyll a-b binding protein CP29.2, chloroplastic
Sequence:
MATISPGGAYIGTPSPFLGKKLKPFSLTSPILSFKPTVKLNSSCRAQLIDTVHNLFIGVGVGLPCTVMECGDMIYRSTLPKSNGLTITAPGVALALTALSYLWATPGVAPGFFDMFVLAFVERLFRPTFRKDDFVVGKKLGEGSFGVVYKVSLSKKRSNEEGEYVLKKATEYGAVEIWMNERVRRACGNSCADFVYGFLDKSSKKGPEYWLLWKYEGESTLAGLMQSKEFPYNVETIILGKVQDLPKGLERENKIIQTIMRQLLFALDGLHSTGIIHRDVKPQNIIFSEGSRSFKIIDLGAAADLRVGINYIPKEFLLDPRYAAPEQYIMSTQTPSAPSAPVAAALSPVLWQMNLPDRFDIYSIGLIFLQMAFPSLRSDSNLIQFNRQLKRCDYDLTAWRKLVEPRASADLRRGFELVDLDGGIGWELLTSMVRYKARQRISAKAALAHPYFDRQGLLALSVMQNLRMQYFRATQQDYSEAANWVIQLMAKNGTEKDGGFTETQLQELREKEPRKKANAQRNALASALRLQRKLVKTVTETIDEISDGRKTVWWNRWIPREE
Protein: Histone H3.1 (P68432)
Organism: Bos taurus (Bovine)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- DNA
- Bromodomain-containing protein 2
- WD repeat-containing protein 5
- Lysine-specific histone demethylase
- Histone H2B type 1
- Histone H2B
- Histone H3.2
- Histone deacetylase 1
- Histone acetyltransferase type B catalytic subunit
- Histone-lysine N-methyltransferase EZH2
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Nucleoprotein (Nucleocapsid protein) (Protein N) (Q5EP28)
Organism: Influenza A virus (strain A/Vietnam/1203/2004 H5N1)
Subcellular location: Virion {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}.
Interaction partners:
Sequence:
MASQGTKRSYEQMETGGERQNATEIRASVGRMVSGIGRFYIQMCTELKLSDYEGRLIQNSITIERMVLSAFDERRNRYLEEHPSAGKDPKKTGGPIYRRRDGKWVRELILYDKEEIRRIWRQANNGEDATAGLTHLMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQRAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGLAVASGYDFEREGYSLVGIDPFRLLQNSQVFSLIRPNENPAHKSQLVWMACHSAAFEDLRVSSFIRGTRVVPRGQLSTRGVQIASNENMEAMDSNTLELRSRYWAIRTRSGGNTNQQRASAGQISVQPTFSVQRNLPFERATIMAAFTGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKATNPIVPSFDMNNEGSYFFGDNAEEYDN
Protein: Citrate synthase, mitochondrial (EC 2.3.3.1) (Citrate (Si)-synthase) (P00889)
Organism: Sus scrofa (Pig)
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Aconitate hydratase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Cytoplasmic aconitate hydratase
- Malate dehydrogenase, cytoplasmic
- ATP-citrate synthase
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Acetyltransferase component of pyruvate dehydrogenase complex
- Propionate--CoA ligase
- Acetyl-coenzyme A synthetase
- Fumarate hydratase, mitochondrial
Sequence:
MALLTAAARLFGAKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK
Protein: Small ribosomal subunit protein uS8 (30S ribosomal protein S8) (P0A7W7)
Organism: Escherichia coli (strain K12)
Function: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Interaction partners:
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS2
- Elongation factor G
- Small ribosomal subunit protein bS18
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL18
- Elongation factor Tu 1
Sequence:
MSMQDPIADMLTRIRNGQAANKAAVTMPSSKLKVAIANVLKEEGFIEDFKVEGDTKPELELTLKYFQGKAVVESIQRVSRPGLRIYKRKDELPKVMAGLGIAVVSTSKGVMTDRAARQAGLGGEIICYVA
Protein: Apm4p (Q5A2L1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane, coated pit {ECO:0000256|ARBA:ARBA00037878}.
Interaction partners:
- AP complex subunit sigma
- AP-2 complex subunit alpha
- AP complex subunit beta
- AP complex subunit beta
- Helicase
- AP-1 complex subunit gamma
- AP-3 complex subunit delta
- Clathrin heavy chain
- Clathrin light chain
- Formin-binding protein
Sequence:
MITAIFIYDSKGDILISKLYKDGIKRNISDVFRIQVISQTSTNRAKEYRSPVLTLGSTSFIYIKSGKIWITAVTRSNQDCSLIMEFLYKLEALLRTVLGRDKKKQLMELTDNYIINNFALCYEILSEVCEFGFPINLDLNYLKKYIDDINVDDSIFKIAPLKRRSTINPLLGKSITSGNTNTTSNNNNSSNSSLKRSSAEENITWRSSGIKYRRNEIFLNVTERVNVLMNSQSDVLNAYVDGSIQMKTHLSGMPLCRFGFNDNTILLSNDEPRDGAVTLEDSKFHQCVQLNVFETERAIQFVPPDGEFQLMSYNCNSNINVPFKVYPQVQEIGRSKLMYKIRIKSFFPEKLPATNVSLKIPTPRGGTILSNLSSSIGKTKFHPEDNSISWKCNKFFGEQEHVLTAEIEVNSSSDELLYWTRPPIKLDFFLDMFSSSGLTVKFLRVQEKNNYRTVKWVKYGTQSGSYEIRY
Protein: Myrosinase 4 (EC 3.2.1.147) (Beta-glucosidase 34) (AtBGLU34) (EC 3.2.1.21) (Sinigrinase 4) (Thioglucosidase 4) (Q8GRX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl beta-D-glucoside.
Interaction partners:
- Nitrilase 1
- Nitrilase 2
- Nitrilase 3
- Cytosolic sulfotransferase 16
- Indoleacetaldoxime dehydratase
- Cytochrome P450 71A12
- Cytochrome P450 71A18
- Myrosinase 5
- Jacalin-related lectin 9
- Jacalin-related lectin 10
Sequence:
MAIPKAHYSLAVLVLLFVVVSSSQKVCNPECKAKEPFHCDNTHAFNRTGFPRNFTFGAATSAYQIEGAAHRALNGWDYFTHRYPEKVPDRSSGDLACDSYDLYKDDVKLLKRMNVQAYRLSIAWSRVLPKGRLTGGVDENGITYYNNLINELKANGIEPYVTIFHWDVPQTLEDEYGGFLSTRIVEDYTNYAELLFQRFGDRVKFWITLNQPFSLATKGYGDGSYPPGRCTGCELGGDSGVEPYTVAHNQLLAHAKTVSLYRKRYQKFQGGKIGTTLIGRWFAPLNEFSELDKAAAKRAFDFFVGWFLDPLVYGKYPTIMREMVGDRLPEFTPEQSALVKGSLDFLGLNYYVTQYATDAPPPTQLNAITDARVTLGFYRNGVPIGVVAPSFVYYPPGFRQILNYIKDNYKNPLTYITENGVADLDLGNVTLATALADNGRIQNHCSHLSCLKCAMKDGCNVAGYFAWSLMDNYEFGNGYTLRFGMNWVNFTNPADRKEKASGKWFSKFLAK
Protein: GH14288p1 (Peroxin 6, isoform C (EC 3.6.1.3)) (Q9V5R2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNENDDAKKVVGKRNSVSFDQQDPGQPRFSFSGRVQELVEGYNSAIQLLAPKWPWFLYPGYLTYAVYWRYAKYYKGKFLLTPIPNRLYDLLIKNEQIKSEHLVFASQEVYENYAESPDVNFVNLVIRGRRVRIGKPLASDEGNMTQTVIKQMLQEAPHTIVAQILPAAQCQPNCLYVQENFYGNILDRFQIRSNCWVQVEHFADEQTIPGIATKAHVYLVADPHELPAELTEVILSNYFNTPRLMHRGHTYRIEVNAELVGTATYAHYYLIFAHLRHVHLKCIHLETKGSEFELQAIVAKNFSNLVQVPASHSFLPRQVLDSMAIVENYPSGLRKPYKLLRSSVDAFLPKKSACLSSKHIFPVFLLQGERGSGKSKLVSAVAQELGMHIYGADCAEIVSQVPSHTEMKLKAVFAKSQVCEPLMICFHNFEIFGIDNEGNEDLRLLSAFHVQVQELFNRDRKHPIVVVALTSDRHLKPMIQGLFLEIINIDMPSKEERFEILRWMHVRETFNDIIYNQKAIEQLPLFSRENQSQFMPRISPSWRETLNVLQDVAAKSQGFLLGDLQLLYDNAVRMKIRNRLGRTTLDMSHFAKNLTDMQSSFADSLGAPKVPKVYWSDIGGLAKLKDEIQSSIGLPLKHVHLMGKNLRRSGILLYGPPGTGKTLVAKAVATECNLSFLSVQGPELLNMYVGQSEQNVREVFSRARSAAPCVLFLDELDSLAPNRGVAGDSGGVMDRVVSQLLAEMDGMSDGDTSKPIFILAATNRPDLIDPALLRPGRFDKLFYVGPCSTAEDKAAVLRAQTQRFALDAGVDMEQIAERLKSEMSGADLYSICSNAWLSAVRRTIDGHLSGTISEKELVPENVIVQEEDFTKSFNKFVPSISAKDLEYFNNLKASYSV
Protein: Lantibiotic lichenicidin A2 (LchA2) (BliA2) (P86720)
Organism: Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)
Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA2 exhibits activity towards L.lactis HP. When combined with LchA1, it displays activity towards a broad spectrum of non-pathogenic and pathogenic Gram-positive bacteria including strains of L.monocytogenes, methicillin-resistant S.aureus, S.pneumoniae and strains of vancomycin-resistant enterococci, but not towards E.faecium L4001 and BM4147-1. Combined LchA1 and LchA2 peptides also inhibit Bacillus sp. HIL-Y85/54728, L.lactis DPC3417 and B.halodurans C-125, which produce lantibiotics themselves. Inactivated by proteinase K and pronase E, but not by trypsin and chymotrypsin.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:19561184, ECO:0000269|PubMed:19707558}.
Interaction partners:
Sequence:
MKNSAAREAFKGANHPAGMVSEEELKALVGGNDVNPETTPATTSSWTCITAGVTVSASLCPTTKCTSRC
Protein: Probable pyridoxal 5'-phosphate synthase subunit PDX1 (PLP synthase subunit PDX1) (EC 4.3.3.6) (O14027)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers.
Interaction partners:
- Uncharacterized glutaminase C222.08c
- Probable pyridoxamine 5'-phosphate oxidase
- Putative pyridoxal kinase C6F6.11c
- Putative pyridoxal kinase C18.10
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
- Probable transketolase
- Transaldolase
- Ribokinase
- Ribose-phosphate pyrophosphokinase 2
- Ribose-5-phosphate isomerase
Sequence:
MSAEIKGSTQVKAGLAQMLKGGVIMDVVNAEQARIAEAAGACAVMALERVPADIRAQGGVARMSDPSMIKEIQAAVSIPVMAKVRIGHFVEAQILESIGVDYIDESEVLTPADDINHIEKSKFTVPFVCGSRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHTRQMQGELRRVKSMSPDELYTYAKEIAAPIDLVKECAQLGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFLSGDPAKRARAIVRAVTHYNDPKILAEVSENLGAAMVGRSVSSLEEKEKLATRGW
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 (BRG1-associated factor 47) (BAF47) (Integrase interactor 1 protein) (SNF5 homolog) (mSNF5) (Q9Z0H3)
Organism: Mus musculus (Mouse)
Function: Core component of the BAF (SWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth.
Subcellular location: Nucleus.
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- AT-rich interactive domain-containing protein 1B
- Actin-like protein 6A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Protein polybromo-1
- SWI/SNF complex subunit SMARCC2
- PHD finger protein 10
- AT-rich interactive domain-containing protein 2
- SWI/SNF complex subunit SMARCC1
Sequence:
MMMMALSKTFGQKPVKFQLEDDGEFYMIGSEVGNYLRMFRGSLYKRYPSLWRRLATVEERKKIVASSHGKKTKPNTKDHGYTTLATSVTLLKASEVEEILDGNDEKYKAVSISTEPPTYLREQKAKRNSQWVPTLPNSSHHLDAVPCSTTINRNRMGRDKKRTFPLCFDDHDPAVIHENASQPEVLVPIRLDMEIDGQKLRDAFTWNMNEKLMTPEMFSEILCDDLDLNPLTFVPAIASAIRQQIESYPTDSILEDQSDQRVIIKLNIHVGNISLVDQFEWDMSEKENSPEKFALKLCSELGLGGEFVTTIAYSIRGQLSWHQKTYAFSENPLPTVEIAIRNTGDADQWCPLLETLTDAEMEKKIRDQDRNTRRMRRLANTAPAW
Protein: Glycogenin-2 (EC 2.4.1.186) (Glycogen synthesis initiator protein 2) (Glycogenin glucosyltransferase 2) (P47011)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Self-glucosylating initiator of glycogen synthesis. Catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues. These chains act as primers for the elongation reaction catalyzed by glycogen synthase. Capable of transferring glucosyl residues to unbound acceptors such as free oligoglucans or oligoglucan derivatives.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:C4R941}. Vacuole {ECO:0000250|UniProtKB:C4R941}. Note=Localizes to glycogen granules (glycosomes) in the cytoplasm. Localizes to the vacuole during nitrogen starvation-induced glycophagy (autophagy of glycosomes). {ECO:0000250|UniProtKB:C4R941}.
Interaction partners:
- Glycogen [starch] synthase isoform 2
- Glycogen [starch] synthase isoform 1
- 1,4-alpha-glucan-branching enzyme
- Glycogen phosphorylase
- UTP--glucose-1-phosphate uridylyltransferase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Glycogenin-1
- Alpha,alpha-trehalose-phosphate synthase 56 kDa subunit
- Trehalose-phosphatase
- Trehalose synthase complex regulatory subunit TSL1
Sequence:
MAKKVAICTLLYSRDYLPGALTLAYQLQKLLKHAVVEDEITLCLLIEKKLFGDEFKPQEIALIRSLFKEIIIIEPLKDQEKSIEKNKANLELLKRPELSHTLLKARLWELVQFDQVLFLDADTLPLNKEFFEILRLYPEQTRFQIAAVPDIGWPDMFNTGVLLLIPDLDMATSLQDFLIKTVSIDGADQGIFNQFFNPICNYSKEVLHKVSPLMEWIRLPFTYNVTMPNYGYQSSPAMNFFQQHIRLIHFIGTFKPWSRNTTDYDDHYYQLWRSTQRELYSECHLSNYFTHLQLGNIETETNFYHEPPCLQDLLNHGKRENQKHVDLDITSVDRNASQKSTAEKHDIEKPTSKPQSAFKFDWESTDYLDRVQRAFPKPDT
Protein: Cell division cycle-related protein res2/pct1 (P41412)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the initiation of mitotic and premeiotic DNA synthesis. Has an additional role in meiotic division.
Interaction partners:
- Start control protein cdc10
- Cell division cycle-related protein res1/sct1
- Transcriptional activator protein rep2
- Transcription factor nrm1
- MBF complex negative regulatory component yox1
- G2/mitotic-specific cyclin cig2
- DSC E3 ubiquitin ligase complex subunit 1
- Cell division control protein 18
- Ribonucleoside-diphosphate reductase large chain
Sequence:
MAPRSSAVHVAVYSGVEVYECFIKGVSVMRRRRDSWLNATQILKVADFDKPQRTRVLERQVQIGAHEKVQGGYGKYQGTWVPFQRGVDLATKYKVDGIMSPILSLDIDEGKAIAPKKKQTKQKKPSVRGRRGRKPSSLSSSTLHSVNEKQPNSSISPTIESSMNKVNLPGAEEQVSATPLPASPNALLSPNDNTIKPVEELGMLEAPLDKYEESLLDFFLHPEEGRIPSFLYSPPPDFQVNSVIDDDGHTSLHWACSMGHIEMIKLLLRANADIGVCNRLSQTPLMRSVIFTNNYDCQTFGQVLELLQSTIYAVDTNGQSIFHHIVQSTSTPSKVAAAKYYLDCILEKLISIQPFENVVRLVNLQDSNGDTSLLIAARNGAMDCVNSLLSYNANPSIPNRQRRTASEYLLEADKKPHSLLQSNSNASHSAFSFSGISPAIISPSCSSHAFVKAIPSISSKFSQLAEEYESQLREKEEDLIRANRLKQDTLNEISRTYQELTFLQKNNPTYSQSMENLIREAQETYQQLSKRLLIWLEARQIFDLERSLKPHTSLSISFPSDFLKKEDGLSLNNDFKKPACNNVTNSDEYEQLINKLTSLQASRKKDTLYIRKLYEELGIDDTVNSYRRLIAMSCGINPEDLSLEILDAVEEALTREK