wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclic nucleotide gated channel subunit alpha 2a isoform X1 (Cyclic nucleotide-gated channel CNGA5) (Cyclic nucleotide-gated channel subunit alpha 2a) (Q0GFG2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Cyclic nucleotide-gated channel subunit beta 3, tandem duplicate 1.
- Cyclic nucleotide-gated channel subunit beta 3, tandem duplicate 2.
- Cyclic nucleotide-gated channel subunit beta 1a.
- Solute carrier family 12 member 8
- Dynein light chain Tctex-type 5
- Adenylate kinase isoenzyme 5
- Cyclic nucleotide-gated channel subunit alpha 2b.
Sequence:
MTCQLLLESMDLSPHRLSVKTSIEDESEPADCTFSRDQSICDDTSSELQRVATLEQQRLNSFRDRGALSRLVNMVVTLREWAHKSLQEEEERPDSFLERFRGPELQIATSRLSISRHDIQDGNTSAKTKKKSDVFILSPADDLYYRWLFVIASAVLYNWCFVVARACFNELQTRNFILWLFLDYLSDVIYILDTCVRLRTGFLEQGLLVKDLIKLRESYFHTLQFKLDLLSIIPTDLGYIVIGIHVPELRLNRLMRFSRLFEFFDRTETRTSYPNLFRICNLVLYILVIIHWNACIYFAISKSLGFGSDQWVYPNISDPKFGTLTRGYVYCLYWSTLTLTTIGEMPAPVQDEEYLFVVFDFLVGVLIFATIVGNVGAMISNMNATRAEFQGQIDAIKHYMKFRKVSKELEARVIKWFDYLWTNKKTIDEQDVLKNLPNKLRAEIAINVHLETLKKVRIFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGCLAVVADDGVTQYAHLTAGSCFGEISILNIRGSKMGNRRTANIRSIGYSDLFCLSKGDLMEAVMEYPDAKKVLEEKGRQILIKEGLLEEVEADGIGVEDIEKRVERMEDTIEILQTRFARLLAQYTATQQHLKQRLTTLECRTNHSGSGFLSDGNESTIDGDGTNSEVNIHL
Protein: GPI mannosyltransferase 4 (EC 2.4.1.-) (GPI mannosyltransferase IV) (GPI-MT-IV) (Q04174)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alpha-1,2-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is essential in fungi. Involved in plasmid maintenance with SMP2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- GPI mannosyltransferase 2
- GPI mannosyltransferase 3
- Glycosylphosphatidylinositol anchor biosynthesis protein 11
- GPI ethanolamine phosphate transferase 3
- GPI mannosyltransferase 1
- GPI-anchor transamidase
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19
- GPI transamidase component GAA1
- GPI ethanolamine phosphate transferase 2
Sequence:
MMRYQWWLYLVYAIGLMLCLGPSYIHPDEHFQCIEILAMQFMKVKGTIPWEFKSKFAARSYGPLLLVYGPLFTILESFPEIQDNPALILYSMRLQNYVMYLLCYHFLIPKLIRDERKAVQFIKKSLLLTSYVTWTYQTHTFSNSIETLALISTLTVMEDMVNEKNIQRSNFKNSVILGLIFSFGVFNRVTFPAFIFLPCLILFWKFYRVHWKSFSLLLLSFSFSSCLFVLIDTNIYNNGKGFVITPLNNLKYNLNVQNLQVHGLHPRYTHLLVNLPQIVGPVLLLAIFSGYKLDKLSTYAIISGLLFLSFFQHQELRFLVPLVPLLVTNLNWTPLSSTLVNKKIFKGTWLLFNIIMAFIMGISHQAGIIQFLGDYFHFRTEQMGVHIWWKTYSPPTWMYMSNNLTVSSLINTQDGIESIDEVAFSVGNHHVIDLKGCDLPLLTETIRRLRLNGSITPLTLVTPNSMTSELKKLKRDGTINLIPKRNYLFHLDLDHLDFNDFTTFKPGLTVYSIELL
Protein: LDL receptor related protein 8 (A0A8I6GFL9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046288}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00046288}.
Interaction partners:
Sequence:
MGRPERGALRPLALLLLLLLLLLQLQHLSTADPLPGGQGPVKECEEDQFRCRNERCIPSVWRCDEDNDCSDNSDEDDCPKRTCTDSDFTCDNGHCIPERWKCDGEEECPDGSDESKATCSSEECPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCPTLCAPHEFQCSNRSCLASVFVCDGDDDCGDGSDERGCSDPACPPREFRCGGGGTCIPERWVCDGQFDCEDRSDEAAELCGRAGQGTTATPAACAPTTQFTCRSGECIHLGWRCDGDRDCKDKSDEADCSAPGPCRENDFQCGDGTCILAIKRCNQERDCLDGSDEAGCLQVAPIFQGNRRRPRGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECQDPDACSQICVNYKGYFKCECHPGYEMDTLTKNCKAVAGRSPSLIFTNRHEVRRIDLVKRDYSRLIPMLKNVVALDVEVDTNRIYWCDLSYRKIYSAHMDKASIPDEQVVLIGEQLHSPEGLAVDWVHKHIYWTDSGNKTVSVATTDGRRRCTLFNRDLSEPRAIAVDPLRGFMYWSDWGFQAKIEKAGLNGADRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFNGGNRKMLIFSTDFLSHPFGVAVFEDKVFWTDLENEAIFSANRLNGLEISILAENLNNPHDIVIFHELKQPKAADACELSAQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPPSTSTTTLASAMTRTVPATTGAPGTTIHDSTYQNHSTEMPSQTAAVPHSVNIPKAHSTSPSTLSPATSNHSQHYGNEGSQMGSTVTAAVIGIIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEEEDELHIGRTAQIGHVYPARVALSLEDDGLP
Protein: Heat shock protein 88 (Heat shock 70-related protein) (Q6TMK3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May function in protein folding and assembly, and disassembly of protein complexes.
Interaction partners:
- Small ribosomal subunit protein uS9
- DNA primase large subunit
- GrpE protein homolog, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- J domain-containing protein
- Uncharacterized protein
- Endoplasmin homolog
- J domain-containing protein
- J domain-containing protein
- J domain-containing protein
Sequence:
MSFVVGFDFGTKNCTIAVAQKGGVDVIANEVSNRLTPSMVSFGEKERYLGESALTNQLRNIRNTITNIKRFIGQEFKTDTVQEELKHEMFQSYEMDNGFVGYNVTYAGEQCSFSSEAILGMLFGKLKKTTEAFVNNPVRDVVISVPVFWNDYQRRAILNAGSIAGLNIIRLINETTATALSYGIYKEWSETDPTNVLFVDVGDSATSVSAVQYKKGQLKVLGTASNPNIGSRVFDETLVKHFAKEFQTKYKINVFENKKALIRLRQACEKVKKILSSNNEAPVSIDSLMDDKDVKGMIDRATFEELANDDMNTIVEPLQRLLSELQMTPDQFQSIEITGGGTRSTSLQKKLSEVLGRDLSKTINSEESVCRGAALQCAMLSPVFRVRPFAVNDVASYPVSVHFKSVSGVEQKLDLFNLKSAIPTPKPLRISFPVTKAEGFEIVVNSTFGTIATVKVDNIPAFTNKSSIKAKVWLDIHGIFHIDEVKLVEQIPEEETAAPAETPAETPANGEAAKPAEEKKVKVKETSLVFTTSRKGLTNELLKAAIEEEGRMQASDLLAIETAEKKNALESYIYDMRSKLQSSLKEYVTPADAETFMTQLNKQMDWLESEEGEDQTKSVYAGKLEELRRLGNPIQKRKQDLEDYPDAVQTLKNIASYVKNEAMIPGERYDHIEKEEKEKLCKDCDDAVEWIDALVAKQQATPKTQPCIINTTEVLAKKTQLEVTAKMILGKPKPKPVEVPKEEPKDTPMESKDAPAEEPVATKDQKMDDILD
Protein: N-terminal amino-acid N(alpha)-acetyltransferase NatA (EC 2.3.1.255) (Q9VT75)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- N
- Probable N-acetyltransferase san
- N-alpha-acetyltransferase 20
- GEO07882p1
- N-alpha-acetyltransferase 35, NatC auxiliary subunit homolog
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 30A
- Phagocyte signaling-impaired protein
- N-alpha-acetyltransferase 40
- N-acetyltransferase eco
Sequence:
MNIRCAKPEDLMTMQHCNLLCLPENYQMKYYFYHGLTWPQLSYVAVDDKGAIVGYVLAKMEEPEPNEESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVECFNAQYVSLHVRKSNRAALNLYTNALKFKIIEVEPKYYADGEDAYAMRRDLSEFADEDQAKAAKQSGEEEEKAVHRSGGHGHSHNHSGHDGHCC
Protein: U6 snRNA phosphodiesterase 1 (3'-5' RNA exonuclease USB1) (H3BN52)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAAPLVGYSSSGSEDESEDGMRTRPGDGSHRRGQSPLPRQRFPVPDSVLNMFPGTEEGPEDDSTKHGGRVRTFPHERGNWATHVYVPYEAKEEFLDLLDVLLPHAQTYVPRLVRMKVFHLSLSQSVVLRHHWILPFVQALKARMTSFHRCQKPMPEAQPKVA
Protein: Somatostatin receptor type 4 (SS-4-R) (SS4-R) (SS4R) (P30937)
Organism: Rattus norvegicus (Rat)
Function: Receptor for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. It is functionally coupled not only to inhibition of adenylate cyclase, but also to activation of both arachidonate release and mitogen-activated protein (MAP) kinase cascade.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Somatostatin
Sequence:
MNTPATLPLGGEDTTWTPGINASWAPDEEEDAVRSDGTGTAGMVTIQCIYALVCLVGLVGNALVIFVILRYAKMKTATNIYLLNLAVADELFMLSVPFVASAAALRHWPFGAVLCRAVLSVDGLNMFTSVFCLTVLSVDRYVAVVHPLRAATYRRPSVAKLINLGVWLASLLVTLPIAVFADTRPARGGEAVACNLHWPHPAWSAVFVIYTFLLGFLLPVLAIGLCYLLIVGKMRAVALRAGWQQRRRSEKKITRLVLMVVTVFVLCWMPFYVVQLLNLFVTSLDATVNHVSLILSYANSCANPILYGFLSDNFRRSFQRVLCLRCCLLETTGGAEEEPLDYYATALKSRGGPGCICPPLPCQQEPMQAEPACKRVPFTKTTTF
Protein: Tail sheath protein (TSP) (Gene product 39) (gp39) (Gene product L) (gpL) (P79678)
Organism: Escherichia phage Mu (Bacteriophage Mu)
Function: Polymerizes as an extended helical structure around the baseplate-tail tube complex. During ejection, the sheath shifts to a contracted form, thereby making the inner tail tube protrude through the host cell envelope.
Subcellular location: Virion {ECO:0000269|PubMed:8599204}. Host cytoplasm {ECO:0000305|PubMed:8599204}. Note=Tail. {ECO:0000305}.
Interaction partners:
Sequence:
MSDISFNAIPSDVRVPLTYIEFDNSNAVSGTPAPRQRVLMFGQSGSKASAAPNVPVRIRSGSQASAAFGQGSMLALMADAFLNANRVAELWCIPQGNGTGNAAVGEISLSGTAGENGSLVTYIAGQRLAVSVAAGATGAALADLLVARIKGQPDLPVTAEVRADSGDDDTHADVVLSAKFTGALSAVDVRWNYYAGETTPYGIITAFKAASGKNGNPDISASIAGMGDLQYKYIVMPYTDEPNLNLLRTELQERWGPVNQADGFAVTVLSGTYGDISTFGVSRNDHLISCMGIAGAPEPSYLYAATLCAVASQALSIDPARPLQTLTLPGRMPPAVGDRFTWSERNALLFDGISTFNVNDGGEMQIERMITMYRTNKYGDSDPSYLNVNTIATLSYLRYSLRTRITQKFPNYKLASDGTRFATGQAVVTPSVIKTELLALFEEWENAGLVEDFDTFKEELYVARNKDDKDRLDVLCGPNLINQFRIFAAQVQFIL
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A0A0B4JCW5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MAESVKSQSLSALTEGQHDDGGSTATSATLANKTSGTNTTSASNHSSQRRRNNNTNSNRNKSHHKNEKRNAPATSGPAVSSSVDVVPATSTASATSTRRSRSQGRHSSAAALSSKESQIPKRSVGAIRSPSSPAFNSIPVVSDQSLSPGSRKRQLNQHNNSNNKASSSHQSAPGGDQLVCAPLKKRRLQQSLGSGICEGAVEINLGAASFDHTPRQASGDCVAQRTRSKTISPEELPSTSSAAAARHHQIRPSASSTSFSSSHRNKRKASIGGSIAAVETTPHRGTAAARAGRSGNLLNYYRKTRKVSHTRSSQKSEKQSIPAEDTTANRNGSAGSGSSSKSGVIPKNRKSLRHSQQNLLDTEAAEVESAAAETGGEQQSEHGNLDVIDQLPTPEAGPNQSEASGIHNQSQLEADRQPVVQDEDDEEDDEEEEEEEEEEVGFYGIVNSAGSSYEEDTQIVAEEDEITTEEEVDDEDDDEIEEEDLSESEFAQQLIGELGGAGPPPALFQQQAPPQLTRYTPATATTAATFVPPQQQQVVYNPQQQQHSSLRRSSRGKTGSCVSSAAAAQQQQHHQQQQHSSAAAAVQQQLLPPPGTYQYQQVGGNTVVVAVRHQQQLQQQQQQQQQLALHHQHQQQQHQQQQQQHQQQQHQQQQRATLVQPGFLFSYRSNQPQQQQQPAQQIHQGPKVTHSSASDALTYSLMAQQPPSGPPHAGGQQITPGANSANLSIVAAALSAARDVGGGSDGGGSAGGATPATGASASSVGNTSAVGASSSSNSSAGQAASSNSNNVTATGSGSAPGGGPTSTGTTSGTQHGSGSGAAAAVDSESDDSEVGRLQALLEARGLPPHLFGALGPRVTHILHRTIGNSSSSKANQLLQGLQSHDESQQLQAAIEMCQMLVMGNEDTLAGFPIKQVVPALIQLLRMEHNFDIMNNACRALAYMLEALPRSSGTVVEAVPVFLEKLQVIQCMDVAEQSLSALEILSRRHNKAILQANGISACLTYLDFFSIVAQRAALAIAANCCLNMHPEEFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASPDLLKNCQQLLLVTPAILNTGTFTAVVRMLSLMCCSCPDLAISLLRNDIAATLLYLLTGNAEPAAASATHVELISRSPSELYELTCLIGELMPRLPLDGIFAVDSLLDRPTLNTQDQVHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVAPMSAGQDLTTTSAGSAAAGGASTSAAAAAASSNNNNNNNNNPPGNSVNLNQVKRRPSLDARIACLKEERGLAADFIKHIFNVLYEVYSSSAGPNVRYKCLRALLRMVYYATPELLRQVLKYQLVSSHIAGMLGSNDLRIVVGALQMAEILMRQLPDVFGTHFRREGVIYQFTQLTDPNNPICANPSPKPLSATATPTANAGGSQSAPASANSLQVNPFFMDSAPGLSSASTTPSSSKHQSYSVKSFSHAMNALTASAKGTPSGALDATSSSTTAGGYNYSSSAPSSSSGAPAAYFVTQQGDPRQYVHFQQPAVPAPPPQQELLPSGVQQQGQQVPQVIYQPHHQQPAHLVLASTSSGAASSSSSSSSSSSASALQHKMTDMLKRKAPPKRKSQSGGRAKSRQEDAAVAPAGSGPGGAPPSSSGSAMHELLSRATSLGSGNGGRSTPNSGGGSGSSKSRFNAGNSSNAGSSKSSFLASLNPARWGRQTHQNHHHHHQQSQQQHHGLSKDSGNSNSTGSGSGAGLAYTVSQHGAGSGAGGLNAAAVAASISKSISHANLLAAANRERARQWVREQAVDFVKRYTEQEAKRSKAASESGATQSGSSGVGLSSTGNTPLSTAGSTNVLERLSSILFKLNGSYHDCLDALLELKTILLESDISPFEVNHSGLIKAMLNYMTSETGLVERDARLRSFMHVFAGLPLEPLLQNVGQMPTIEPIAFGAFVAKLNGCVTQLEQFPVKVHDFPAGPGGRSNQSALRFFNTHQLKCNLQRHPQCNNLRQWKGGTVKIDPLAMVQAIERYLVVRGYGGIRADSDDDSEEDMDDNVAAVVLSQASFRHKLQFTIGDHVLPYNMTVYQAVKQFSPLVSEQPETDNESETLLGNASIWVQQHTIHYRPVEEEVTSGAAAGAASSSSSCSSGVQKQQSSSSSASSCVNATSSCSSSSGVASGGGSLTKKAHKSSSKFMRKKTELWHEGIAPVVISALKPFLSSSLPADVVTVQDASLDALCMLRVIHALNRHWDHLYGCVVRQNIIPQSDFIHPKIMAKANRQLQDPLVIMTGNLPQWLPQIGMACPFLFPFETRHLLFYATSFDRDRALQRLLDTTPDLNAAESSERVAPRLDRRKRAISRTEILKQAEHILQDFGHSKALLEIQYENEVGTGLGPTLEFYALVSAELQRTDLGLWNGSDSYKQNSVTIVDVVKANSAVLHIEDALEATTTDQNTPAVAGASLVSSSTTTTTTTAQQHQHPPTRSSSRSHVLRSGAGQQPVEHSSSSAGANENALNMVIAQQFSDTNSANPAAIDNPSSTTTATTVVQHNTTTNNSSIITTTTTTSYVHAVHGLFPLPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEHSIGLADLMRVAPEVQNTLVRLQDLVRQREYILSDPNIDAMEKTEKIEQLDLDGCPIADLGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSEQQHSRWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHLS
Protein: Beta-defensin 2 (Defensin beta 2) (Q32ZI5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Beta-defensin 5
Sequence:
MRTLCSLLLIGCLLFSYATPVAGILGPLRIQTDYHRCLREKGFCLNAVCPRSTLFVGTCFPYKFYCCKFKR
Protein: Periostin, osteoblast-specific factor b (A0A0R4INY2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MKLLFAATFALFVLSAFDQADSSAYDKIVAHSRIRAKKQGPNMCALQQVVGTKKKYFSTCRNWYQGAICGKTATVLYECCPGYMELAGQRGCPAVAPIDNVFGTLGLVKAKTTQDYSDISKLRQEIEGAGSYTFFAPSNDAWDLLEAEVRNALVSNVNIELYNALHYHMVNKRLLTKDLKNGMTATSMYNDLSLHINHYSNGVVTVNCARIIHGNQVATNGVVHVIDRVITAVGSTIQDMIEVEDDLSTLSTVATDSGLIDKLGEPGHFTLFAPTNAAFDKLGREVLDRLMKDKKSLQALLNYHLLNSVQCSEAIMAGTSHETLEGSNIEIGCDGDSLTVNGIKMVLKKDIVATNGVIHLIDEVLMPDSAKQVMELVGQSQATFSDMLTELGLSAAMRPQAEYTLLAPVNAAFNDEVMSMDQSFLKIILENHILKNKIVLSQLYNGQRLETLSGKFLRVFVYRTALCIENACLIRGSKEGSNGALHLMKTLISPAESSMFQILVKNGAFKIFLSLMEAAGLTDLLKQEGDFTLFAPTDEAFAGLSERDLTLLKSNGNALKAILLYHFSNGVFIGGGLETGVTNLLKTLQGSNLRVLYANASMLVNTVKVPEPDIMATNGVVHFVRTLLYPEDIPVGSQDLLSLLRRIIRYIQFKFVPGYRYQEIPLTFMRRVITVPGDVTKVTRVIQGEPTITKVTRVIEGAPSVTKVTRVIEGQPSITKVTRVIEGQPSLTKVTRVIEGDPSMTRVIEGGVRRRT
Protein: Cyclin-dependent kinase inhibitor 1C (Cyclin-dependent kinase inhibitor p57) (p57Kip2) (P49918)
Organism: Homo sapiens (Human)
Function: Potent tight-binding inhibitor of several G1 cyclin/CDK complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to lesser extent, of the mitotic cyclin B-CDC2. Negative regulator of cell proliferation. May play a role in maintenance of the non-proliferative state throughout life.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cyclin-dependent kinase 2
- Cyclin-A2
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase 4
- G1/S-specific cyclin-D2
- G1/S-specific cyclin-D1
- G1/S-specific cyclin-D3
- Cyclin-A1
- G1/S-specific cyclin-E2
- S-phase kinase-associated protein 2
Sequence:
MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR
Protein: Histone chaperone RTT106 (Regulator of Ty1 transposition protein 106) (P40161)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition.
Subcellular location: Nucleus {ECO:0000269|PubMed:19683497}. Chromosome {ECO:0000269|PubMed:19683497}. Note=Localizes to the promoter region of histones HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2,. {ECO:0000269|PubMed:19683497}.
Interaction partners:
- Histone H3
- Histone chaperone ASF1
- Chromatin assembly factor 1 subunit B
- Chromatin assembly factor 1 subunit A
- Histone-binding protein MSI1
- Box C/D snoRNA protein 1
- Histone H4
- Protein HIR2
- Histone acetyltransferase RTT109
- ATPase histone chaperone YTA7
Sequence:
MSKLFLDELPESLSRKIGTVVRVLPSSLEIFEELYKYALNENSNDRSGRHKKPRIDVSSDLLKTDEISETNTIFKLEGVSVLSPLRKKLDLVFYLSNVDGSPVITLLKGNDRELSIYQLNKNIKMASFLPVPEKPNLIYLFMTYTSCEDNKFSEPVVMTLNKENTLNQFKNLGLLDSNVTDFEKCVEYIRKQAILTGFKISNPFVNSTLVDTDAEKINSFHLQCHRGTKEGTLYFLPDHIIFGFKKPILLFDASDIESITYSSITRLTFNASLVTKDGEKYEFSMIDQTEYAKIDDYVKRKQMKDKSMSEELKAKSKSKGQATDGTADQPSILQEATRQMQDEKKAGVFSDDDEENDQNFEAESDLSDGSGQESSDGAEDGEEAEEDDEEDDEEEDKKGQSALNRDNSFASINGQPEQELQYKEFKEPLELEDIPIEIDNDDDEDDEDGSGVEYD
Protein: Killer cell lectin-like receptor subfamily B member 1F (CD161 antigen-like family member F) (Natural killer cell surface protein NKR-P1F) (CD antigen CD161f) (Q8VD98)
Organism: Mus musculus (Mouse)
Function: Binds CLEC2I/Clr-g leading to activation of natural killer cells or costimulation of IL-2 production and proliferation of T-cells in response to antigen stimulation. May contribute to the formation of the immunological synapse between T-cells and antigen-presenting dendritic cells.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- C-type lectin domain family 2 member I
Sequence:
MDTSKVHGNVKPFRCPGYKQASSPSFSPDACRCPHWHHLALKSGCAGLILLLLSLIGLSVLVRFLVQKPPIEKCSVAAQENRTELTGRSAILECPRYWHPHWNKCLFVSQISRPWAEGRDACSMEDAILLLIENKEELRFVQNLIKGKEQLFFIGLKYVQKEKIWKWIDGSILNPNLLRITGKDKENSCAIISHTEVFSDSCSSDNHWICQKTLIHV
Protein: Desmoglein-2 (O55111)
Organism: Mus musculus (Mouse)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14126}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14126}. Cell junction, desmosome {ECO:0000269|PubMed:12494996, ECO:0000269|PubMed:38395410}. Cytoplasm {ECO:0000250|UniProtKB:Q14126}.
Interaction partners:
- Desmocollin-2
- Junction plakoglobin
- Plakophilin-2
- Desmoplakin
- Plakophilin-1
- Plakophilin-3
- Desmocollin-1
- Plakophilin-4
- Transmembrane protein 43
- Caspase-3
Sequence:
MARSPGDRCALLLLVQLLAVVCLDFGNGLHLEVFSPRNEGKPFPKHTHLVRQKRAWITAPVALREGEDLSRKNPIAKIHSDLAEEKGIKITYKYTGKGITEPPFGIFVFDRNTGELNITSILDREETPYFLLTGYALDSRGNNLEKPLELRIKVLDINDNEPVFTQEVFVGSIEELSAAHTLVMKITATDADDPETLNAKVSYRIVSQEPANSHMFYLNKDTGEIYTTSFTLDREEHSSYSLTVEARDGNGQITDKPVQQAQVQIRILDVNDNIPVVENKMYEGTVEENQVNVEVMRIKVTDADEVGSDNWLANFTFASGNEGGYFHIETDTQTNEGIVTLVKEVDYEEMKKLDLSIIVTNKAAFHKSILSKYKATPIPITVKVKNVVEGIHFKSSVVSFRASEAMDRSSLSRSIGNFQVFDEDTGQAAKVTYVKVQDTDNWVSVDSVTSEIKLVKIPDFESRYVQNGTYTAKVVAISKEHPQKTITGTIVITVEDVNDNCPVLVDSVRSVCEDEPYVNVTAEDLDGAQNSAPFSFSIIDQPPGTAQKWKITHQESTSVLLQQSERKRGRSEIPFLISDSQGFSCPERQVLQLTVCECLKGGGCVAAQYDNYVGLGPAAIALMILALLLLLLVPLLLLICHCGGGAKGFTPIPGTIEMLHPWNNEGAPPEDKVVPSLLVADHAESSAVRGGVGGAMLKEGMMKGSSSASVTKGQHELSEVDGRWEEHRSLLTAGATHHVRTAGTIAANEAVRTRATGSSRDMSGARGAVAVNEEFLRSYFTEKAASYNGEDDLHMAKDCLLVYSQEDTASLRGSVGCCSFIEGELDDLFLDDLGLKFKTLAEVCLGRKIDLDVDIEQRQKPVREASVSAASGSHYEQAVTSSESAYSSNTGFPAPKPLHEVHTEKVTQEIVTESSVSSRQSQKVVPPPDPVASGNIIVTETSYAKGSAVPPSTVLLAPRQPQSLIVTERVYAPTSTLVDQHYANEEKVLVTERVIQPNGGIPKPLEVTQHLKDAQYVMVRERESILAPSSGVQPTLAMPSVAAGGQNVTVTERILTPASTLQSSYQIPSETSITARNTVLSSVGSIGPLPNLDLEESDRPNSTITTSSTRVTKHSTMQHSYS
Protein: Moira (Q7KPY3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MALSGGEKKTIYSQPYLLQYLAHSSEPITKESLAQLFIHFLQYVEAKLGKNSADPPATRIPMRCFLDFKSGGGLCIIFSTMFRFRAEQRGKKFDFSIGKNPTRKDPNIQLLIEIEQALVEADLYRIPYIYIRPEIEKGFEGKLREILDNRRVEIVSDEEDATHIVYPVVDPHPDEYARPIFKRGGHVMLHWYYFPESYDSWAVNNFDLPDHIPENPESPAERWRVSASWIVDLEQYNEWMAEEDYEVDEQGKKKTHKQRMSIDDIMSFGDEKKKPAASSGGGKQKRRRSPSPASSASTSKPGKRKRSPAVVHKKSRNDDDDEDLTRDLDDPPAEPNVQEVHKANAALQSTASPAPGGKSRGDNDMMPIKGGTMTDLDDEMTGGSAAQAMSTGDGENSQTGKTSDNSNTQEFSSSAKEDMEDNVTEQTHHIIVPSYSAWFDYNSIHVIEKRAMPEFFNSKNKSKTPEIYMAYRNFMIDTYRLNPTEYLTTTACRRNLAGDVCAIMRVHAFLEQWGLINYQIDADVRPTPMGPPPTSHFHILSDTPSGLQSINPQKTQQPSAAKTLLDLDKKPLGKDGGLELGDKSGLTGIKTEALENGAAGGLSSGVSQFGLKLDQYAKKPAAMRNRTAASMAREWTDQETLLLLEGLEMHKDDWNKVCEHVGSRTQDECILHFLRLPIEDPYLEDDGGFLGPLACQPIPFSKSGNPIMSTVAFLASVVDPRVAAAAAKAAMEEFAAIKDEVPATIMDNHLKNVEKASAGGKFNPNFGLANSGIAGTGNDKDDEEGKEGGASASAGGSDEEMKDLSKKDDDAKSKDNTKSDKTNTNTDSSSTSSSATGNTNNTDKKPKESSGSSPSGDKSAIKSDKSNKSSPTETAAAASGGEVDIKTEDSSGDGETKDGTEAKEGTGTGTGPLAVPKEGTFSENNMQTAAAAALASAAVKAKHLAALEERKIKSLVALLVETQMKKLEIKLRHFEELEATMEREREGLEYQRQQLITERQQFHLEQLKAAEFRARQQAHHRLQQELQGQAAAGSMILPQQQQLPQAQQPQQQQQTLPPHPHLAQQQQLPPHPHQLPPQSQPLAGPTAQHQPLPPHVVSSPNGAPFAAPPISLTGGLPPGAPTAIVTNPSDQTGPVAAGAAQSQAPTPMDTTPPSSGPVSDANAPPGSAMPPGGIPPANTAPIAGVAPSS
Protein: Adrenodoxin-like protein 2, mitochondrial (Mitochondrial ferredoxin 2) (AtMFDX2) (Q8S904)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Associates with the adrenodoxin reductase MFDR to form an efficient low potential electron transfer chain that is able to reduce cytochrome C.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9M0V0}.
Interaction partners:
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Frataxin, mitochondrial
- Iron-sulfur cluster assembly protein 1
- Cysteine desulfurase, mitochondrial
- Iron-sulfur cluster assembly protein 2
- Iron-sulfur cluster assembly protein 3
- Protein CIA1
- Iron-sulfur protein required for NADH dehydrogenase, mitochondrial
- SufE-like protein 2, chloroplastic
- FAD-linked sulfhydryl oxidase ERV1
Sequence:
MVFHRLSRLGSRIVKELPRERHLSMCGKRILQRSYGQYLQSSPMLQRQTRSFKEALFSNNHKFCTSFSTTSEKGGEKTEKINVTFVDKDGEEIHIKVPVGMNILEAAHENDIELEGACEGSLACSTCHVIVMDTKYYNKLEEPTDEENDMLDLAFGLTATSRLGCQVIAKPELDGVRLAIPSATRNFAVDGFVPKPH
Protein: GrpE protein homolog (Q9C8X4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion matrix {ECO:0000256|RuleBase:RU000640}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM17-2
- Mitochondrial import inner membrane translocase subunit TIM44-1
- Mitochondrial import inner membrane translocase subunit TIM44-2
- Thylakoid lumenal 16.5 kDa protein
- Heat shock 70 kDa protein 6, chloroplastic
- Mitochondrial import inner membrane translocase subunit PAM16 like 2
- Small ribosomal subunit protein bTHXc
- GrpE protein homolog 1
- Heat shock 70 kDa protein 7, chloroplastic
- SPFH/Band 7/PHB domain-containing membrane-associated protein family
Sequence:
MAISFAIDPSISPCFSFSSPSSSSKTLPLRNNLHFHGRPSPISPLISKPSRKFPIFSAHQTNNSEEANSKQQADVKTLIRSYKQALLNGDETSVTEIETMFCKIEKEKNKMDQKVLSLSMKIASEKEMKIRLQADFDNTRKKLDKDRLSTESNAKVQILKSLLPIIDSFEKAKLQVRVDTDKEKKIDTSYQGIYRQFVEVLRYLRVSVIATVGKPFDPLLHEAISREESEAVKAGIITEELNKGFVLGDRVLRPAKVKVSLGPVNKKTPSAAEEITPSA
Protein: AP-2 complex subunit mu-A (AP-2 mu-A chain) (Clathrin assembly protein complex 2 mu-A medium chain) (Clathrin coat assembly protein AP50-A) (Clathrin coat-associated protein AP50-A) (Mu2-adaptin-A) (Plasma membrane adaptor AP-2 50 kDa protein A) (Q6NWK2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP50 is a subunit of the plasma membrane adaptor. The complex binds polyphosphoinositide-containing lipids (By similarity).
Subcellular location: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. {ECO:0000250}.
Interaction partners:
Sequence:
MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKRSNIWLAAVTKQNVNAAMVFEFLYKMCDVMTAYFGKISEENIKNNFVLIYELLDEILDFGYPQNSETGALKTFITQQGIKGQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIDKQGKGGTTDDAGKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEYELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFESKLNYSDHDVIKWVRYIGRSGIYETRC
Protein: Putative lipoprotein LppW (P9WK67)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
Sequence:
MRARPLTLLTALAAVTLVVVAGCEARVEAEAYSAADRISSRPQARPQPQPVELLLRAITPPRAPAASPNVGFGELPTRVRQATDEAAAMGATLSVAVLDRATGQLVSNGNTQIIATASVAKLFIADDLLLAEAEGKVTLSPEDHHALDVMLQSSDDGAAERFWSQDGGNAVVTQVARRYGLRSTAPPSDGRWWNTISSAPDLIRYYDMLLDGSGGLPLDRAAVIIADLAQSTPTGIDGYPQRFGIPDGLYAEPVAVKQGWMCCIGSSWMHLSTGVIGPERRYIMVIESLQPADDATARATITQAVRTMFPNGRI
Protein: Ring finger protein 8 (C9J858)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISRNHCVLKQNPEGQWTIMDNKSLNGVWLNRARLEPLRVYSIHQGDYIQLGVPLENKENAEYEYEVTEEDWETIYPCLSPKNDQMIEKNKELRTKRKFSLDELAGPGAEGPSNLKSKINKVSCESGQPVKSQGKGEVASTPSDNLDPKLTALEPSKTTGAPIYPGFPKVTEVHHEQKASNSSASQRSLQMFKVTMSRILRLKIQ