wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear pore complex protein An-Nup133 (Eurofung) (Q5B587)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}.
Interaction partners:
- Nucleoporin NSP1
- Protein transport protein sec13
- Peptidase S59 domain-containing protein
- Nuclear pore complex protein
- WD40 protein related to S. cerevisiae SEH1
- Nuclear pore complex protein An-Nup159
- Nuclear pore complex protein An-Nup170
- Nuclear pore complex protein AN-Nup192
- Nuclear pore complex protein An-Nic96
- Nuclear pore complex protein An-Nup57
Sequence:
MFVPKAGSATTLRNPRRRQRTSSGESIKAPSAKRQRSILSQDDNPDTGIPTYGAPNHRSSIPTATTEVDSTPAPGGENQKNIPIRTFNATEKRKSDVLGPIILYLNCHVYLTKSETSVQKIADVLSPPAMGMGLLSLNSRPSFGRIPPWSHRPYLPMDASDVSPLGVILSTATSSTPGLMILMPHNGRIIYWETVSCAASLSLPRQKQTGLQGYVPGMLSGECATDIVNAEPSGVIVTFSTGRVAHITLRDSQGKPAVTVNFLKNPHSTGGIGFLDGIKNVFGAGYWRKKVAAVRAGESFQRGQRDIIIATSAGLVEVWDTHWNNGSILKNQYDVKEDLLAATRKDEASDYEVKIWDLAVVTSSCEDSSNPWEISVLVGLFSGVTIQGVFVTRLRLTDGARVLSTNPISLHTFPTDSLHLEPRLFIPKPHETAFIVIGQSIILLSLTDAEGTSSSQLLIDNGQPRTFHDSINFRSGQAYEILGSGFEDQSEEYANPSCLLMIREFGVVRITALPRQETAETARISAQHKLEQAVFYGTMLGNPLNLSSKGDLDFPVPEIEQATLAICQGLLRSTSKFIPSAAISIDQNLKLRSKALDDLSRILLDQNKIIDRRIWWELLWGAEKLAAQRAIWRLEASARKRNSSGATFLAHVLGLMNEKFKTKLDDTDDPIRQWFLFDSYRMEHIVPWIFHAIKPQKGNTSKQMRRMSEQILEAGELSLAVLETAFRYRDEHASQFGIGDGYLEEGVLTTNYEGLPEFWTSQSISYSEIGHLLDLELDSCRAIQQTSTSSDGGDQQISAKIARNSARHLRIMGQMYSERIRWLSAQEDQKLIDEASATKQSHIKQRRWQLFKLAGIGQLNEAIELAESFQDMSALVELIIELQDQNKVVFTNVDTPDGIELDRKISLYFEKFGDAWADAFFGRQISMGQPGILFSAKKFQSFVTRFLHKHQPYARLSWINDVIGEADYECAAKTLEHLALEQEQDVWGHRVKLALAKLSHLARWEKDAPSDTRALQNDIKRLEGLAEMGAVQEVIYSYVSPVLRDAIDQKAEIDLAIDHFAKSTAQKLPSLHELLKEALTGVVTRKMLSLDQLVDVLTLIDPSQDPDIGQNDFSGDEFHLALRVIRLGHNAQGDPNYSLALQKLVWRRCIIRDKWDATGGTAEQMGSETESPLTATALSRTLALCLNDRTDPSKPPLYRPTRPQDVLLNDSDSALISSRFRPEQRARIIRDLERENSTLLRYIEKSELECWFKSLLSSAEKERTSDDALQTPCSMDAESSLSQTNRKERLSWL
Protein: Forkhead box protein J1-A (F1QDF8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Key transcription factor required for motile ciliogenesis. Activates genes essential for motile cilia formation and function. Its activity is sufficient for ectopic development of cilia that resemble motile cilia.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Multicilin
- DNA-binding protein RFX2
- Transcription factor RFX3
- CYCLIN domain-containing protein
- Sperm-associated antigen 6
- Transcription factor RFX4
- Geminin coiled-coil domain-containing
- ADP-ribosylation factor-like protein 13B
- Dynein, axonemal, heavy chain 9.
- Intraflagellar transport 88 homolog.
Sequence:
MLSMSSMDPWPEGSVGLEEEVVTAAAQAERLDTSTPLQCNTSLDSDNLDDSLTSLQWLQEFSILNASTGQHTSPSSHSHLMGSDAPSSPLAGDPASIGMPLTPGKPTAASFCRVPMFSALPSLVAHGHCPDEVDYKSNPHIKPPYSYATLICMAMQASKKTKITLSCIYKWITDNFCYFRHADPTWQNSIRHNLSLNKCFIKVPRQKDEPGKGGFWKIDPQYAERLLNGAYKKRRLPPVQINPALQHRLRMNAQATGVISRNLSVSPESQQLLKDFEEATSADQNWDPRLAEATMLSCWISGKGTNKRKQPYNHRTGKTPRRSSSPLLVMDEQEDLSSLRGNFDWDALLDSALNGELSLNEGSPLSPTPQDEELMIRGTHISPQEAPVENHVLMETQRSGDEDFDEETFLATAFLQSPWSEVDESNRSDFLGSSTVSIDQLFDLSFGGDLSSKIETLL
Protein: Aminotransferase-like, plant mobile domain family protein (Q8RXC3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- WPP domain-interacting tail-anchored protein 2
- AT4G31340 protein
- Golgin family A protein
- AT2G24420 protein
Sequence:
MDSTFRDEDLVEEREELMVSYSENNSRPIMKKAHFLKPFVTSSIDGFQGMLRPSPSPELKASSLSVSFRGWRLPNKKFQFWVKKMVALHKPTWLKSGIFEAIKASTYRIHKNPSLILSLAQNWCPETNTFVFPWGEATITLEDVNVLLGFSISGSSVFASLQSSEMKEAVEKLQKRCQGSMKQESWISSFVDDEMEHEAFLVLWLSKFVFPDKFCSSISSDVFPLAVRLARGERIAFAPAVLANLYNDLGHICVLASIQNVLASSLFKLVQVWIWERFKSIRPEAKVIPRGQPRIAQWSGLKQRFKNVGLIIFHGNFDWRPYSEPLENWNPPRFYVEEAKWVRIDESLDGDYDDDDEFVSFARCVRVSKLVGIGVVENYYPNRVAMQFGLAQDVPVLGTNHRRNFTEEEAWDDYNKPLVGLKLYFPSRVATASVTTRYRDWWAKSVSEMRKESMETFNVSSTVDHYDDSDDDIPLKIVPLSQVYQKLDDEMKKAKHSTNKRRKRAREDDESAAETEDDESADTEDDESADTEDDESAETEDDDNMTIAQRINSRKKSDDIENTEGERSRLVADNNVSGLPQKLAYGDETVATTQEETEQKNNENKSSNGVAAEKEEDDERLKQRKLAIKELALKTEARMLKVENTLAKIKQWKLTRLHTKKPLVSS
Protein: N-alpha-acetyltransferase 40 (EC 2.3.1.257) (N-acetyltransferase 11) (N-alpha-acetyltransferase D) (NatD) (Protein acetyltransferase 1) (Q8VE10)
Organism: Mus musculus (Mouse)
Function: N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A (By similarity). In contrast to other N-alpha-acetyltransferase, has a very specific selectivity for histones H4 and H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg-Gly sequence' (By similarity). Acts as a negative regulator of apoptosis (By similarity). May play a role in hepatic lipid metabolism.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86UY6}. Nucleus {ECO:0000250|UniProtKB:Q86UY6}.
Interaction partners:
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 60
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 80
- N-alpha-acetyltransferase 25, NatB auxiliary subunit
Sequence:
MGRKSSKAKEKKQKRLEERAAMDAVCAKVDAANRLGDPLEAFPVFKKYDRNGLNVSIECKRVSGLEPATVDWAFDLTKTNMQTMYEQSEWGWKDREKREEMTDDRAWYLIAWENSSIPVAFSHFRFDVECGDEVLYCYEVQLESKVRRKGLGKFLIQILQLMANSTQMKKVMLTVFKHNHGAYQFFREALQFEIDDSSPSMSGCCGEDCSYEILSRRTKFGDSQHSHTGGHCGGCCH
Protein: J domain-containing protein (Q384H7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MAGINTVVSATPSLYAVLGVAPTVSQAELTRQFKRLSLQLHPDRAAYRTGENETEVQRQYQSIVEAYEVLSNPDHRRSYDTKCGVNFSARVAALRQTLAQNEVMPVVNCPTEPTSAETVQVTEDEDDEEYTP
Protein: Gap junction gamma-3 protein (Connexin-30.2) (Cx30.2) (Connexin-31.3) (Cx31.3) (Gap junction epsilon-1 protein) (Q8NFK1)
Organism: Homo sapiens (Human)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 2
- AP-1 complex subunit sigma-1A
Sequence:
MCGRFLRRLLAEESRRSTPVGRLLLPVLLGFRLVLLAASGPGVYGDEQSEFVCHTQQPGCKAACFDAFHPLSPLRFWVFQVILVAVPSALYMGFTLYHVIWHWELSGKGKEEETLIQGREGNTDVPGAGSLRLLWAYVAQLGARLVLEGAALGLQYHLYGFQMPSSFACRREPCLGSITCNLSRPSEKTIFLKTMFGVSGFCLLFTFLELVLLGLGRWWRTWKHKSSSSKYFLTSESTRRHKKATDSLPVVETKEQFQEAVPGRSLAQEKQRPVGPRDA
Protein: Cytochrome c oxidase subunit 2 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide II) (P18944)
Organism: Gallus gallus (Chicken)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P68530}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P68530}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 1
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- ATP synthase F
- NADH-ubiquinone oxidoreductase chain 5
- Cytochrome c oxidase subunit 4
- Cytochrome c oxidase subunit 5B.
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5A.
Sequence:
MANHSQLGFQDASSPIMEELVEFHDHALMVALAICSLVLYLLTLMLMEKLSSNTVDAQEVELIWTILPAIVLVLLALPSLQILYMMDEIDEPDLTLKAIGHQWYWTYEYTDFKDLSFDSYMTPTTDLPLGHFRLLEVDHRIVIPMESPIRVIITADDVLHSWAVPALGVKTDAIPGRLNQTSFITTRPGVFYGQCSEICGANHSYMPIVVESTPLKHFEAWSSLLSS
Protein: Slr2004 protein (P73837)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Plastocyanin
Sequence:
MHQISMKQTRFVQVLIVSIFLVFGMAIGLQQLSAQPKMTLSRIPLEDKLYEPAGMAFRPNQSNQLWVVNHGNDSIATLTNLGESNLEVSVKSDAYAEHFLAKPTGIAFGYDDTFAVSNDSINELRGMNFIKNPERNKNFVNNHFMGPTLFSASTYALAGQTKKYLEDWPQPGNGHDPDRDLTLSQGCPLTYWNSSVQQCYWPREGSHLDMLHESPLAMGIAHDKGNAYFLLDGCGSRDSNKQCLGNGHLMRYDFNRDHQEGNGFHGDGIVWRYPEIDFKRDKDIPSGMLVLDDWLYFSNTGMGKVERIATTEGNVQTIVKSWSDQYDKEQVGTGIISWEDVKSVSMDGDEPEAISNWVRTHGDLAKIAELGQAWIPPMEVLAEYSYVYNVPQETFISENWLDKPSGLASDGKSLFVADYSSGWIAAFDLKTAKLEWRYQSKLNSISGLAFNPNKSHELYISDRDTNSLYQLKWN
Protein: Tastin (Trophinin-assisting protein) (Trophinin-associated protein) (Q12815)
Organism: Homo sapiens (Human)
Function: Could be involved with bystin and trophinin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation.
Subcellular location: Cytoplasm.
Interaction partners:
- Trophinin
- Bystin
- Holliday junction recognition protein
- Kinesin-like protein KIF18B
- Cell division cycle-associated protein 3
- Separin
- Chromosome-associated kinesin KIF4A
- Aurora kinase B
- Kinesin-like protein KIF2C
- Kinesin-like protein KIF20A
Sequence:
MTTRQATKDPLLRGVSPTPSKIPVRSQKRTPFPTVTSCAVDQENQDPRRWVQKPPLNIQRPLVDSAGPRPKARHQAETSQRLVGISQPRNPLEELRPSPRGQNVGPGPPAQTEAPGTIEFVADPAALATILSGEGVKSCHLGRQPSLAKRVLVRGSQGGTTQRVQGVRASAYLAPRTPTHRLDPARASCFSRLEGPGPRGRTLCPQRLQALISPSGPSFHPSTRPSFQELRRETAGSSRTSVSQASGLLLETPVQPAFSLPKGEREVVTHSDEGGVASLGLAQRVPLRENREMSHTRDSHDSHLMPSPAPVAQPLPGHVVPCPSPFGRAQRVPSPGPPTLTSYSVLRRLTVQPKTRFTPMPSTPRVQQAQWLRGVSPQSCSEDPALPWEQVAVRLFDQESCIRSLEGSGKPPVATPSGPHSNRTPSLQEVKIQRIGILQQLLRQEVEGLVGGQCVPLNGGSSLDMVELQPLLTEISRTLNATEHNSGTSHLPGLLKHSGLPKPCLPEECGEPQPCPPAEPGPPEAFCRSEPEIPEPSLQEQLEVPEPYPPAEPRPLESCCRSEPEIPESSRQEQLEVPEPCPPAEPRPLESYCRIEPEIPESSRQEQLEVPEPCPPAEPGPLQPSTQGQSGPPGPCPRVELGASEPCTLEHRSLESSLPPCCSQWAPATTSLIFSSQHPLCASPPICSLQSLRPPAGQAGLSNLAPRTLALRERLKSCLTAIHCFHEARLDDECAFYTSRAPPSGPTRVCTNPVATLLEWQDALCFIPVGSAAPQGSP
Protein: Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase (EC 2.4.1.258) (Alpha-1,3-mannosyltransferase ALG3) (Asparagine-linked glycosylation protein 3) (AtALG3) (Not56-like protein) (O82244)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for N-linked oligosaccharide assembly. Adds the sixth mannose residue in an alpha-1,3 linkage onto the dolichol-PP-oligosaccharide precursor dolichol-PP-Man(5)GlcNAc(2).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18567790, ECO:0000269|PubMed:20356820}; Multi-pass membrane protein {ECO:0000269|PubMed:18567790, ECO:0000269|PubMed:20356820}.
Interaction partners:
- Dol-P-Man:Man
- Alpha-1,2-mannosyltransferase ALG9
- Dol-P-Glc:Glc
- dolichyl-phosphate beta-glucosyltransferase
- GDP-Man:Man
- Dolichol-phosphate mannosyltransferase subunit 1
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichol-phosphate mannose synthase subunit 2
- Dolichol-phosphate mannose synthase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Sequence:
MAGASSPASLRASRSRRLGKETNRSDLFKKPAVPFAFALILADAILVALIIAYVPYTKIDWDAYMSQVSGFLGGERDYGNLKGDTGPLVYPAGFLYVYSAVQNLTGGEVYPAQILFGVLYIVNLGIVLIIYVKTDVVPWWALSLLCLSKRIHSIFVLRLFNDCFAMTLLHASMALFLYRKWHLGMLVFSGAVSVKMNVLLYAPTLLLLLLKAMNIIGVVSALAGAALVQILVGLPFLITYPVSYIANAFDLGRVFIHFWSVNFKFVPERVFVSKEFAVCLLIAHLFLLVAFANYKWCKHEGGIIGFMRSRHFFLTLPSSLSFSDVSASRIITKEHVVTAMFVGNFIGIVFARSLHYQFYSWYFYSLPYLLWRTPFPTWLRLIMFLGIELCWNVYPSTPSSSGLLLCLHLIILVGLWLAPSVDPYQLKEHPKSQIHKKA
Protein: Calpain, putative cysteine peptidase, Clan CA, family C2, putative (Q4GZ09)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGCGASSTQSEDGMHEPIPPMEMVRKQIAAAQPEQNGVKEGQSSKKKRSGDDPPDEFEELTVTALPQRWQRDSTYKCGYPMITGDEVKPCFEKGLLYRIVKGDTWAFYNDTRTYEMCVSFTFGRDSTVRGMGNTVITNLEGGEILAEASIYPCETAIFVRGRFSGFRSKIKAQPLSDEILKAKVKQYDKYIQEDLARVNAMINENDTDDAILAKCVEGPTPFIDIRFPPNQTSIERGAVLPIMTIPWARPDMYLPLGFPPQVRLFRSAISTVNIEQGDLGDYWIMCAIASLEDDTERLRGMFRHPVSCEKTAKERAVGAYRVTLNKSGWWHSVIVDDYLPVVGNRPKFAQSLSDPCEVWVSILQKAYAKVHGSYVNIVAGDPLHALQDFTGYISSRYDYILDPEPGLEENEILERLEKYDQQGFKIILSTHNAKTDNPNVDETYREVGLLAGHAYPVKAVRYFASENIALLQIRNPWCRETEWKGEWANGNAEWKSHPEIAKACEINAQDGSSFWMSWGDVQKYFNGCGVLFRYPRSVDYRVRGVFRGDIPSVSILISVNKTISLVCSLTQEDRRGTKMADDYPPIMLSLCGGDRLSDDMEVEKSTTTEADYPGEDLTFVHSRDVGMMCTLTPFKSPYLLVPRIITGRDEEHPYVIGLLSEAEFGADLKAEFFSVPANCEVFRNAKSFAFQGDVVEAKFQVRTPDCRFPTEYNSTVIVKAKKGDWYVENKKK
Protein: PDZ domain-containing protein (Q4GYE7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Dynein heavy chain, putative
- Flagellum-adhesion glycoprotein, putative
- Uncharacterized protein
- Flagellar attachment zone protein 1 conserved domain-containing protein
- Cofilin/actin depolymerizing factor, putative
- Uncharacterized protein
Sequence:
MENDYPVNLRVDIAPEDGTVMLPGSITITRTTVSVFKLRESTDEEPLFIGVCSVPLIKFSRCPSTVFPRTDALLLTSVSGHLFINAALTAGVVPPEESGLGTPSSSASDIARSHASGTRRDSVDERRKKIDNPGLWTRLRLEFRDNDDCDRCVEALLARHAEELNSRGTSSTSSLSKSHSQNDVTGASRSRRDSSMRTHSGPRRSTHSESTRSTESSMRSTQEDLVRSSRGGESRNSRGDASRSGGTPLRSAPDDSRRSRGPESHSVRSDTTRTGGTPSRGGPDDVRHSRGPDSHSSRSDTTRTGATPLRSAPDDSRRSRGPESHVTRSETSRSAGTPLRSAHNETARNSRSEASRSGGTPLRSAPDDSRRSRGPESHSVRSDTTRTGGTPSRGGPDDVRHSRGPDSHSSHSELSRSGGTPPRSAPDAMFRHSRGPDSQTTRSEASRSVRSSSKHSPAGAGRSTGTTRSSGTALPAGAGVSEMMHTCRSGPTYMEGSCTSSNARRNGGIHHGSDRTPIRAGRGPADGDSESDAASSAVDIRRHGRSSVTSSASRGSGLDSQPLTPSGSEVGGQKRRSGSPADFHTPNSKRRDSQSEYSQDSQLTPRGLPNRSRGDGSYREADSVSELRTPRSSLREGSRDGYGTRAPGTARDAPNAAQSPYNIRRHSLNSTGTSTMQTSVIDSIVGGGHDRGRAHSQATSARTTPYNSRSPPGHPSTGKKRTELQYFLRCILKFMHHRLHFMQYLHKEVVFEAYLHEEARLLGGRPRSRSMRRSSRATSASHNASRMSASPRRSLIPPGLEEAHRLREIEDRLREVENLHRTTELERAELERRQREFEEERRDFERRRQELAHQRLEVQDLLREVGDRWRDGDRMGGMGSGINRFDYLSDQRPRDSYGYGEGIGSRHSSHHSRQRDSDTLSVPTGEAKLLLSSQKPPALEEALDEADYPTAFVDRYVYGDEWRMLLPKREMEVRFNALVDTCIALKLPRRLVTILTVSVEQPGLRVTAEVRHNPETLSRDVLTRRFTTQPLRFLQRLYDLRHYYAMDDTVANAPQRSLPRGSRGTSRGTPLQGSRVLPGVIPRVNENSGIYDESSDDDLMGDNAMVDPMARMREFQRGAERRRLQRELESANMREKKQATQQKQRRFQQLEQLEQEESMGRSSIVLAELQTRRSMFASAVFRQRPSAITLRRQLEEKEQVERSLLEVGYVRQTQVLMQAHRRNLNFVRLLMHEAERRLRHVELEREARMELDIMMNPTRWVKSVSLPEVNERTRRQRLVAAEMKQRMHIYANIRSFVADAVQSEIDTLISDEMAARLVLGADEMKSRIDLYSWSQAPGSIYTPRSAAIAAAGRQGIPPQALHALFAEESVERVHLGNDELRRRHLYQREYIITTEDAARNDIELEELDEHVTMLDGLVQKNRKMLERRRQEQQRSIKLLSEEQYYRKSIINDEQDEFEEFMEQFDAEINDMIMTEASQLGPAHDIDSPSRRRRVPSTPRQAKLFHYMSFVPEDMDHVPTANLAIEGMLGCSINKNLEVTCIARPLPKAEAEELQFQAGDMILDVAGYSLHSLSHLREVLANRAMQIQHEAREEFDDVPEDELLTNPALQKYIEVLCEHHNFLVQVLRGCDIFQIIVKS
Protein: Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2) (Nucleosome-remodeling factor subunit RBAP46) (Retinoblastoma-binding protein 7) (RBBP-7) (Retinoblastoma-binding protein p46) (Q16576)
Organism: Homo sapiens (Human)
Function: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- Transcriptional repressor p66-alpha
- Histone deacetylase complex subunit SAP18
- Sin3 histone deacetylase corepressor complex component SDS3
- Metastasis-associated protein MTA3
- Histone deacetylase 2
- Zinc finger protein AEBP2
- Histone-lysine N-methyltransferase EZH1
- Metastasis-associated protein MTA1
- Chromodomain-helicase-DNA-binding protein 4
Sequence:
MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSDKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTTSELEGQGS
Protein: Ribosomal RNA-processing protein 17 (O14012)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in ribosomal RNA processing.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribosome biogenesis protein brx1
- Probable rRNA-processing protein ebp2
- Uncharacterized RNA-binding protein C1827.05c
- ATP-dependent RNA helicase has1
- AdoMet-dependent rRNA methyltransferase spb1
- 25S rRNA
- Ribosome biogenesis protein erb1
- Probable nucleolar GTP-binding protein 1
- Ribosome biogenesis protein ytm1
- ATP-dependent rRNA helicase spb4
Sequence:
MDNTSLLTRGGEIYSRKKGKKQRLEEIVFDKEKRKEYLTGFHKRKVERRKHAQVQLEQQKREERLALRKSLREQRKRELAERLAFSKELNSSLENDEESSQQEDSSSKSDSEEESSMEPKTTEYDEDDKHVTVEIVEDDDDEEIAYPKEGFVTPRISPPPDVPLRPHKPKNAAKKKFRYESKFERTQDRRKEKIRRLKKKIRR
Protein: Methylosome subunit pICln (Chloride channel, nucleotide sensitive 1A) (Chloride conductance regulatory protein ICln) (E9PMI6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFLKSFPPPGPAEGLLRQQPDTEAVLNGKGLGTGTLYIAESRLSWLDGSGLGFSLEYPTISLHALSRDRSDCLGEHLYVMVNAKFEEQGQGDIPTFYTYEEGLSHLTAEGQATLERLEGMLSQSVSSQYNMAGVRTEDSIRDYEDGMEVDTTPTVAGQFEDADVDH
Protein: Small ribosomal subunit protein eS6y (40S ribosomal protein S6-2) (Protein EMBRYO DEFECTIVE 3010) (P51430)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the 40S small ribosomal subunit (By similarity). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (By similarity).
Interaction partners:
- Small ribosomal subunit protein uS17z
- Large ribosomal subunit protein uL4y
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS12z
- Small ribosomal subunit protein eS26x
- Small ribosomal subunit protein eS28z/eS28y
- Large ribosomal subunit protein eL8z
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein uS17x
Sequence:
MKFNVANPTTGCQKKLEIDDDQKLRAFFDKRLSQEVSGDALGEEFKGYVFKIMGGCDKQGFPMKQGVLTPGRVRLLLHRGTPCFRGHGRRTGERRRKSVRGCIVSPDLSVLNLVIVKKGVSDLPGLTDTEKPRMRGPKRASKIRKLFNLGKEDDVRKYVNTYRRTFTNKKGKKVSKAPKIQRLVTPLTLQRKRARIADKKKRIAKANSDAADYQKLLASRLKEQRDRRSESLAKKRSRLSSAPAKPVAA
Protein: Calmodulin-3 (CaM-3) (P0DH98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Activates MPK8 in vitro.
Interaction partners:
- Calcium/calmodulin-regulated receptor-like kinase 1
- CDPK-related kinase 1
- Mitogen-activated protein kinase 8
Sequence:
MADQLTDDQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVDEMIKEADVDGDGQINYEEFVKVMMAK
Protein: Aloesone synthase (EC 2.3.1.-) (Polyketide synthase 3) (C4MBZ5)
Organism: Aloe arborescens (Kidachi aloe)
Function: Catalyzes the iterative condensations of 6, 7 or 8 molecules of malonyl-CoA to produce various aromatic polyketides. Produces the heptaketide aloesone, the aglycone of aloesin, from 7 molecules of malonyl-CoA as a major product. Also able to produce a hexaketide pyrone, a heptaketide 6-(2-acetyl-3,5-dihydroxybenzyl)-4-hydroxy-2-pyrone, a novel heptaketide 6-(2-(2,4-dihydroxy-6-methylphenyl)-2-oxoethyl)-4-hydroxy-2-pyrone and octaketides SEK4/SEK4b.
Interaction partners:
Sequence:
MGSLSDSTPLMKDVQGIRKAQKADGTATVMAIGTAHPPHIISQDSYADFYFRVTNSEHKVELKKKFDRICKKTMIGKRYFNFDEEFLKKYPNITSFDKPSLNDRHDICIPGVPALGAEAAVKAIEEWGRPKSEITHLVFCTSGGVDMPSADFQCAKLLGLRTNVNKYCIYMQGCYAGGTVMRYAKDLAENNRGARVLMVCAELTIIALRGPNDSHIDNAIGNSLFGDGAAALIVGSDPIIGVEKPMFEIVCAKQTVIPNSEEVIHLHLRESGLMFYMTKDSAATISNNIEACLVDVFKSVGMTPPEDWNSLFWIPHPGGRAILDQVEAKLKLRPEKFSATRTVLWDYGNMISACVLYILDEMRRKSAAEGLETYGEGLEWGVLLGFGPGMTIETILLHSLPPV
Protein: Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) (Q27820)
Organism: Trichomonas vaginalis
Interaction partners:
Sequence:
RIGRLVFRACRKLYPKDIQVVAIHDLGDIKTNVYLLKYDTAHRAFPEPVTVDEAKQEFTVGEGADKWVVKSIGGRLGPSQLPWKELGIDVVLESTGIFRTKAEKDAEGKIKKDGYDGHLVSGAKKVVLSVPSADEIECTLVLGVNDEDLKPETKCISNASCTTNCLGPVAKTLNNAFGIRNGFMTTVHSYTNDQVVADTMHKDLRRARAAGMNIIPTSTGAAIALPKVCHGLPPKSLDGFALRVPTITGSLVDLTVNVNAKVTKEEVNAALKKATEEGSLKGIMTYVTDPIVSSDIIGCQYSSIVDALSTKVLPNPEGQGTLVKVLSWYDNEWMYSCRCADIFHRLEKYL
Protein: C-type (Calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 5 (C-type lectin domain family 5, member A, isoform CRA_b) (cDNA FLJ78045, highly similar to Homo sapiens C-type lectin domain family 5, member A (CLEC5A), mRNA) (A4D1U7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MNWHMIISGLIVVVLKVVGMTLFLLYFPQIFNKSNDGFTTTRSYGTVSQIFGSSSPSPNGFITTRSYGTVCPKDWEFYQARCFFLSTSESSWNESRDFCKGKGSTLAIVNTPEKLKFLQDITDAEKYFIGLIYHREEKRWRWINNSVFNGNVTNQNQNFNCATIGLTKTFDAASCDISYRRICEKNAK
Protein: Beta-mammal toxin Co1 (C0HLF2)
Organism: Centruroides ornatus (Scorpion) (Centruroides infamatus ornatus)
Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin acts on human Nav1.6/SCN8A voltage-gated sodium channels. In vivo, is lethal to mice 40 minutes after intraperitoneal injection at a dose of 5ug. No activity is observed when injected into crickets or woodlice.
Subcellular location: Secreted {ECO:0000269|PubMed:31734253}.
Interaction partners:
Sequence:
KEGYLVNHSTGCKYECFKLGDNDYCLRECKQQYGKGAGGYCYAFGCWCTHLYEQAVVWPLPKKTCN