wanglab/gogpt-training-data huggingface dataset:
Protein: Histone deacetylase (EC 3.5.1.98) (Q59E49)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MSSPDDRIPIHDLPSEAGSDERLLHITPATLTLDFKPHPAVDIDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQLEHKYQFAVNSHGAFQELRNESMVTAAAAAVAQEQHRQQLHQQQQQHQQQQQQQQHQQQQQQQQARGRDGMKLKQNCSANASPEVKQILNCFILSRKSQAAASNGTTTTSPYRNRGVVKSSSGESLPAGTVTSAHPYKIPQPPPSLLKYESDFPLRKTDCNSTPDSGPNSPPSAAALAVGVVGSRGSPTSAPIQEENEEGSQYQPGQRSSINDLPLFSSPSLPNISLGRPHLPNSAQAHAQVNAQVAAQAQAQAQAQAQAHAMFAALAAAQGGCGQPGYYNPLGMAFVGRQPAPLAMIPATGIAPQQPSPVVRSASATSTSSSQASLVGDVAPPQAHAASTILPSSSSYMQQLGSVAGSGVNLHAAAVAAAAAAAAAAGSLPPTNSHGHGHGSHAHPHPHAHGHGHGHGHGIYAGHQHNVPITDAQVAQVHLHKQGHRPLGRTQSAPLPLGHPMLTGAVQLNVVQTHYENSEAERQAYEHQVVNQKVRQTVLTRSGAAAAAAAAAGVSVVREAQLKEEDDDSAAEVMDLTDKKKPPKTVLTSTIATSTSQNLPEALAAAAAAAAYRAPHNASSNSASATKSGIKLRDQEYLQQQREQLLLLQQEEELAKSLMRPLSRTLSSPLVPLGPHGLSQIPDTGQQPAPIATSSSADHIPPVNLSLPHRQHRQLMSTLYASQLRNHQPSASGSPPHKVTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQCQLSRPKLENTLSASFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMPEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGFNVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHWPCVRMLEHTVGLSALETLKVEHDESETINAMAGLSMQSMHRTLSRDDSEEPMDQDETK
Protein: Pericentrin-like protein, isoform M (M9PCK2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MADQRTTTTTTTTATTATTPSSANILATTATTTTTTSSSIEEEIEEAIEISEVEEQLNTPLESLSEAAAYARPKDEQSSAKSLSSNPAEDEDADEFRIDDAQLSGGQLAQHFLVDEDESEEGSDLPAASKVEVSLSSNDDDFDISLPLEQRKPVHSLHEDDESVDQSLSNQSTTDDVSELVEEPVHEMDDKTDGSAAISASAPQETQVDESQITDEQDHSMEEIVATNESIEVTYEAEETVNTSQKQDLITDLDEESEDQVHVDNRPTSTLQALKLPALQQPQIVERKAATALTTLRLQADVLEPLELTILEMDDDENEEDDDDEESSLQLMKLRLMAMNQQMIVDNAPKLSPTEAEQTQVTSSSNNLEIKQMERVPLTEFSKDVLEDITEESERLLSMSTTMEEEQDPPSLSLDESKTLLQPGAHKTGGSSSSLVSLNMLKQLEAKVQELHTQLETKDNCLASLNLQLETARRESSAGPASARDSSSLMTNSTEYRTLQEELGGPTLDIYVEMSRRDELIAKLTDSLQQSLNVRDKLQVDADRLGGEVQNLRRQLQETLDAVKRSSAVWPDQECNPGQRISEISMDLISESDDDLDRHFLTDNEERGSRSSKERQLTQLQTNEELGLQASNPEWTPTFSKQIEQFHTYLLPTEQRIFQMVQRKFDDYLNQQITLCRDLGAQELKIARDQWESEKLTSEQNQQAAHAKQMEDLRKYFEHKCADLEKQFSDDVFSHKSQHQTGDSSSECSEVDQLPEEGAAAVSSKEPSPRKRKRAELLLSPSHRQMTPCGLDSLGENTGKTEKDNTADIADLKIFYQTHIKELKRAHEDQVRKLSDRIKFYERQQGDDDYKSLLSENTVDDQHWPKELILLREKFTAKSQLEITQLNIKHAEEMSRLKLEFEKQLNRKNKRHLTFDAARDLEQVICERDGLRELSKSFRSVLCRLAKCVAHCEEDLNATLSEEVQRLLFHSRSQDGGDDLEATISSSLNNTKHMLRVPDVHSLLEVVEDPSLVQFIDSKSNEEPSEDFDLNDCLERLKSEASYLLHLSEDLHKQRTHDESSEHLDEPEKQEHELCCEAEDGLKTTGAVNQQVLSKFLRTNSLNDQQMGVANQRKNSNPEAGKTHSSLPPDLQEHAGNASELSFQLVQLKNRLIKSEADRQNLQQQLSRTIDRNAELGQELQALRDQLSQLNSLNHTDYNEGYGLGTMKSLQEQGLDQSSASFLALQERARHLLSSSPVKEQPSRDHGNSTVILLQMIEDFCREGDKVVEFSKKDREDLQSQYAQLESQFREVNQQLCESNAKRDKFEVELKASIDKIFVLREIISELETQVQTKALNEEVLAEKAQQLEEYVSLQMRDNDILQQEVHSLKTDIGEGYQSRIRVLEEKLKQSGPTAEQGVVLSQVAEKLRDIETTLDQKTKALESLHNSNATSNSASLSVTEDVSIHGSKEPTAVGSPSHPSLTVEGVQRVTEKLDRHTRVEEAAIKRIRDLEMQVHQMRAGCVELQHERDTLQGRMEEQTQRISTLQNRLEEQRQRAEQLHRTGTSDLNTRVHELQGEVQNLYEQLAARDKQMANMRQQLQRSKEEITRLETEVEVRTQPDRSLVNKLQAEVQQKGAEIVKLKDKIRTEMINRLAIPDLMETMLADKNDEIDHLRDQLEAKEKELQASQQEASQISSPSGAAGKQEGSGGKLSARTLSDIGSITEFPEPDVERRAAMRSLTALQMSEGAGGFLHQTMETSKEAVANLTHKRTDDLSGFIVPYPVNTFEHPHYFQALGVTAQSTDGLTPGLVPRQINFSNLTEDSKLKTTSLLMHTPELPRPTTPPEIHQLRVKLSDLQTEKQRQQSELEKKLQDLQKELEQEKEKLSRQAQTLQSYEESEAKYRLRIENLESKVLETAAQAASDRENLRKELNCVSAAHEQCENAAAARKRELEKLNSEVKVKADQLHAALRRCADLELQVLTLERDLERLKNSDNSSKQYSVDEIAQQVEKELNYSAQLDSNILKAIESEEENNLDKKLQKGVQTEEETLPGTGNGTDDENFTGERELLNQLEALRAQLAVEREQCEAMSKELLGEKQHSQDIQEQDVIIIEAMRKRLETALDAEDELHKQLDQERERCERLQTQLTSLQRAESRRNSSLLLKSPGDSPRKSPRADFESELGDRLRSEIKLLVAQNERERERSADAQRSSERERQRYEKELQERVAYCERLKQEMEKLSRDKESAETELEHFNERLTLQASEIESLEARLVTLQEAETRRANTRTRQHQENVKLQAEIHELKSKLLAAEAARDCLDQKVTQLRFDVSRSGQREAKLAEALAQANDRLAHSTDDNVPAQFMQKMKEINALLAENTQENRQMAETVQFLVGERIALQKKCEELGGAGNTNVTELEERCRQLIGRYLRVESHRKALVYQKRYLKLTLEGYQASEQLALQNLRGGAEQPPQRNIKKKFKTVALAIIAIQRIKYIGRIWHTGKRIVSKSVFTITQQRSPGLNLNVAPPQSPLPGPNSNLPTNNNNLMGRLSYAPLSPPMVNFSTVQPIMLPSDFTLQAPTTSLQTTIANNNSENTLPSLARLDWPTMQKPKRAHARHH
Protein: Membrane protein MLC1 (Q8VHK5)
Organism: Mus musculus (Mouse)
Function: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q15049}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15049}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q15049}.
Interaction partners:
Sequence:
MTREGQFREELGYDRMPTLERGRQDAGRQDPGSYTPDSKPKDLQLSKRLPPCFSYKTWVFSVLMGSCLLVTSGFSLYLGNVFPSEMDYLRCAAGSCIPSAIVSFAVGRRNVSAIPNFQILFVSTFAVTTTCLIWFGCKLILNPSAININFNLILLLLLELLMAATVIISARSSEEPCKKKKGSISDGSNILDEVTFPARVLKSYSVVEVIAGVSAVLGGVIALNVEEAVSGPHLSVTFFWILVACFPSAIASHVTAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSVMRVVEIFKDYPPAIKSYDVLLLLLLLLLLLQGGLNTGTAIQCVSFKVSARLQAASWDPQSCPQERPAGEVVRGPLKEFDKEKAWRAVVVQMAQ
Protein: coproporphyrinogen oxidase (EC 1.3.3.3) (Q8IHU1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen oxidase
- hydroxymethylbilane synthase
- ATP synthase-associated protein, putative
- Methyltransferase, putative
- Delta-aminolevulinic acid dehydratase
Sequence:
MKDEIAPNEYFRNLWENLLKSEQNNICSLIESLDNKKFQEEVWYRKSGKNKNLGGGITRILEDGNIFEKCAVNYSCIYGAIDKESAKQMCVNHYNKEFINTTKICHSDDINILISRVLNSHNIRIINEKYKFYASGISIIAHPVNPNVPTVHMNFRFFQIFIKTGKKKKKYNNLNNVNNNNLNNNLNNNFVKNKIDNNYKSIKHWFGGGCDLSPCYIFPDLFTEFHNSFKLVCDKYNHLFYRHFKIWCDLYFRIKHRNINRGIGGIFFDNLLNNIIKNKKVIRSGKLKDINKKNGNDPTINNNNNNNKDCKCYSCNNIMDKSYRMIYFFIQECIINFRKSYLHILLETVNFKYDDNMLKWQRVCRGRYVEFNLLYDRGTKFGIELNRYKIYRRKKKQKKLENYSSTNFIKDEIFDEQVSDYLSDEHEKIDNVFSSLPLKCDFQYKYKIEKYSREYETLEILKYPKKWVDY
Protein: Polymeric immunoglobulin receptor (PIgR) (Poly-Ig receptor) (Hepatocellular carcinoma-associated protein TB6) [Cleaved into: Secretory component] (P01833)
Organism: Homo sapiens (Human)
Function: Mediates selective transcytosis of polymeric IgA and IgM across mucosal epithelial cells. Binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment.
Subcellular location: [Polymeric immunoglobulin receptor]: Cell membrane {ECO:0000269|PubMed:9379029}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secretory component]: Secreted {ECO:0000269|PubMed:16543244, ECO:0000269|PubMed:19079336, ECO:0000269|PubMed:8292260}.
Interaction partners:
- Immunoglobulin J chain
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Immunoglobulin heavy variable 4-38-2
- Ras-related protein Rab-3B
- Interleukin-2
- Surfactant protein C
- Immunoglobulin alpha Fc receptor
- Lactotransferrin
- High affinity immunoglobulin gamma Fc receptor I
- B-cell antigen receptor complex-associated protein alpha chain
Sequence:
MLLFVLTCLLAVFPAISTKSPIFGPEEVNSVEGNSVSITCYYPPTSVNRHTRKYWCRQGARGGCITLISSEGYVSSKYAGRANLTNFPENGTFVVNIAQLSQDDSGRYKCGLGINSRGLSFDVSLEVSQGPGLLNDTKVYTVDLGRTVTINCPFKTENAQKRKSLYKQIGLYPVLVIDSSGYVNPNYTGRIRLDIQGTGQLLFSVVINQLRLSDAGQYLCQAGDDSNSNKKNADLQVLKPEPELVYEDLRGSVTFHCALGPEVANVAKFLCRQSSGENCDVVVNTLGKRAPAFEGRILLNPQDKDGSFSVVITGLRKEDAGRYLCGAHSDGQLQEGSPIQAWQLFVNEESTIPRSPTVVKGVAGGSVAVLCPYNRKESKSIKYWCLWEGAQNGRCPLLVDSEGWVKAQYEGRLSLLEEPGNGTFTVILNQLTSRDAGFYWCLTNGDTLWRTTVEIKIIEGEPNLKVPGNVTAVLGETLKVPCHFPCKFSSYEKYWCKWNNTGCQALPSQDEGPSKAFVNCDENSRLVSLTLNLVTRADEGWYWCGVKQGHFYGETAAVYVAVEERKAAGSRDVSLAKADAAPDEKVLDSGFREIENKAIQDPRLFAEEKAVADTRDQADGSRASVDSGSSEEQGGSSRALVSTLVPLGLVLAVGAVAVGVARARHRKNVDRVSIRSYRTDISMSDFENSREFGANDNMGASSITQETSLGGKEEFVATTESTTETKEPKKAKRSSKEEAEMAYKDFLLQSSTVAAEAQDGPQEA
Protein: Ribonuclease 3 (EC 3.1.26.3) (Ribonuclease III) (RNase III) (P0A7Y0)
Organism: Escherichia coli (strain K12)
Function: Digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs; cleavage can occur in assembled 30S, 50S and even 70S subunits and is influenced by the presence of ribosomal proteins. The E.coli enzyme does not cleave R.capsulatus rRNA precursor, although R.capsulatus will complement an E.coli disruption, showing substrate recognition is different. Removes the intervening sequences from Salmonella typhimurium rRNA precursor. Complements the pre-crRNA processing defect in an rnc deletion in S.pyogenes strain 370, although this E.coli strain does not have the corresponding CRISPR locus (strain TOP10).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:4865702}. Note=Loosely associated with ribosomes.
Interaction partners:
- GTPase Era
- Signal peptidase I
- Small ribosomal subunit protein uS15
- Signal recognition particle receptor FtsY
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease E
- 5'-3' exoribonuclease Rnm
- DNA repair protein RecO
- Ribonuclease R
- Ribonuclease G
Sequence:
MNPIVINRLQRKLGYTFNHQELLQQALTHRSASSKHNERLEFLGDSILSYVIANALYHRFPRVDEGDMSRMRATLVRGNTLAELAREFELGECLRLGPGELKSGGFRRESILADTVEALIGGVFLDSDIQTVEKLILNWYQTRLDEISPGDKQKDPKTRLQEYLQGRHLPLPTYLVVQVRGEAHDQEFTIHCQVSGLSEPVVGTGSSRRKAEQAAAEQALKKLELE
Protein: Protein EARLY HEADING DATE 2 (Ehd2) (Protein RICE INDETERMINATE 1) (OsID) (OsID1) (B1B534)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription activator that acts as a flowering master switch in both long and short days, independently of the circadian clock. Promotes flowering upstream of HD1 by up-regulating FTL1, FTL4, FTL5, FTL6, EHD1, HD3A and RFT1. Seems to repress FTL11 expression. May recognize the consensus motif 5'-TTTGTCGTAAT-3' in target gene promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:18725639, ECO:0000269|PubMed:18774969, ECO:0000269|PubMed:24280027}.
Interaction partners:
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- protein-serine/threonine phosphatase
- Os04g0589400 protein
- Small ribosomal subunit protein uS2c
- Os01g0220300 protein
- Os06g0255200 protein
- Os02g0102400 protein
- Small ribosomal subunit protein uS14c
Sequence:
MLLSDLSSDQEATGSNSHGGGGGDRMVVGSHGAAHVVLSNLFLPPAAAAAATMLLPAAPVMVRPAAMAAAQEPRAKKKRSLPGNPDPEAEVIALSPRALVATNRFVCEVCNKGFQRDQNLQLHRRGHNLPWKLRHRAAAVSAVTTAAPAPRKRVYVCPEPTCVHHDPARALGDLTGIKKHFSRKHGEKRWRCERCGKRYAVHSDWKAHVKNCGTREYRCDCGILFSRKDSLLTHRAFCDALAEESARLLAAANNSSSITTTTCNNSNISSNNNNNNINSISNSNNLLITSSSSSPPLFLPFSTTPAENPNPNQLLFLQQHQAAHHQLLLPQFQQPPSSPPAYFDHLAFGGGGGVITGSSCNDDNSSIAGDVMVAAGGDSVSFGLTSEGSVTMHAGDVGRRRLTRDFLGVDHDAGEVDELELDELPADLSTTAAACQGCNFAAATTAACCATDFTTGSRQYLGRLPPVNETWSHNF
Protein: Histone H1.10 (Histone H1x) (Q92522)
Organism: Homo sapiens (Human)
Function: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H1.8
- Testis-specific H1 histone
- Histone H4
- Histone H1t
- Histone H2A type 1-B/E
- Histone H3.1
- Histone H2B type 1-J
- Ribosomal L1 domain-containing protein 1
- Histone H1.0
Sequence:
MSVELEEALPVTTAEGMAKKVTKAGGSAALSPSKKRKNSKKKNQPGKYSQLVVETIRRLGERNGSSLAKIYTEAKKVPWFDQQNGRTYLKYSIKALVQNDTLLQVKGTGANGSFKLNRKKLEGGGERRGAPAAATAPAPTAHKAKKAAPGAAGSRRADKKPARGQKPEQRSHKKGAGAKKDKGGKAKKTAAAGGKKVKKAAKPSVPKVPKGRK
Protein: S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) (Q9CQ65)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Subcellular location: Cytoplasm. Nucleus {ECO:0000255|HAMAP-Rule:MF_03155}.
Interaction partners:
- Spermidine synthase
- Spermine synthase
- Methylthioribose-1-phosphate isomerase
- Adenine phosphoribosyltransferase
- Protein arginine N-methyltransferase 5
- GMP synthase
- Serine/threonine-protein kinase RIO1
- Cyclin-dependent kinase 4 inhibitor B
- Tumor suppressor ARF
Sequence:
MASGSACTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDMVIIDQFIDRTSLRPQTFYDGSHCSARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTIVTIEGPRFSSRAESLIFRTWGADVVNMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDGVLKTMKENANKAKSLLLTTIPQIGSMEWSETLRNLKNMAQFSVLPPRH
Protein: WASP like actin nucleation promoting factor b (Wiskott-Aldrich syndrome, like) (Q6NYX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGPPSNRRPALNVGSILLTHQENEVLFNHLGKKCISLSSAVVQVYAADRNSSWVKKCCGVACLVKDNTQRSYYIRVIDMKDGKTLFEQEMYNNFSINCSRPYFITFSGDNCQIGLNFANEEEAKRFRSAIGELVGRKSRRTEKRREPPNGPSVSSGPSGPALPMATVDIKNPEITNQRYHNNTQMNNLQSNFNRAKDKSKGKNNNKKKKISKAEIGTPSNFRHVGHVGWDPNTGFDLNNLDPDLKKLFDMCGISEDELKDKETSKVIYDLIEKQGGVEAVKNEMRRQAPPPPPPSRGGAPPPPPPHNSAPPPPPPSRGRGAPPPPPPSRAPTSAPPPPPPSRPGMGAPPPPPPPSRGPTQAPPPPPPPHSASISPPAPPSIGGAPPPPPPPPPPPGPPPPGPPPAQDVDSGDSPGGRSAFLDQIREGAQLKKVDQNNKPPVSTGGRGALLDQIRQGIQLKTVTDAPESPPPSLAPSDGIVGALMEAMKNRSKVIHCSDDDDDDDDVDDFEDDEDWED
Protein: DNA-binding protein (Q6VQX1)
Organism: Yersinia pseudotuberculosis
Subcellular location: Cytoplasm, nucleoid {ECO:0000256|ARBA:ARBA00004453}.
Interaction partners:
Sequence:
MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESQSQAEIEERARKLQQYREMLIADGIDPNELLQASAAAKAAGKAKRAARPAKYQYKDENGELKTWTGQGRTPAVIKKAIEEQGKSLDDFLL
Protein: RNase L inhibitor (Q6SSD8)
Organism: Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Interaction partners:
Sequence:
MADKLTRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSNLEKETTHRYCANAFKLHRLPIPRPGEVLGLAGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLKAIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAVVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYVPTENLRFRDASLVFKVAETANEEEVKKMCMYKYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQKISPKSTGSVRQLLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEITFRRDPNNYRPRINKLNSIKDVEQKKSGNYFFLDD
Protein: Zinc finger protein 768 (Q9H5H4)
Organism: Homo sapiens (Human)
Function: Binds to mammalian-wide interspersed repeat (MIRs) sequences in euchromatin and promoter regions of genes at the consensus sequence 5'-GCTGTGTG-[N20]-CCTCTCTG-3', consisting of two anchor regions connected by a linker region; the linker region probably does not contribute to the binding specificity. Required for cell homeostasis. May be involved in transcriptional regulation (Probable).
Subcellular location: Nucleus {ECO:0000305|PubMed:30476274}. Chromosome {ECO:0000269|PubMed:30476274}. Note=Localizes to euchromatin. {ECO:0000269|PubMed:30476274}.
Interaction partners:
Sequence:
MEREALPWGLEPQDVQSSDEMRSPEGYLRGNMSENEEEEISQQEGSGDYEVEEIPFGLEPQSPGFEPQSPEFEPQSPRFEPESPGFESRSPGLVPPSPEFAPRSPESDSQSPEFESQSPRYEPQSPGYEPRSPGYEPRSPGYESESSRYESQNTELKTQSPEFEAQSSKFQEGAEMLLNPEEKSPLNISVGVHPLDSFTQGFGEQPTGDLPIGPPFEMPTGALLSTPQFEMLQNPLGLTGALRGPGRRGGRARGGQGPRPNICGICGKSFGRGSTLIQHQRIHTGEKPYKCEVCSKAFSQSSDLIKHQRTHTGERPYKCPRCGKAFADSSYLLRHQRTHSGQKPYKCPHCGKAFGDSSYLLRHQRTHSHERPYSCTECGKCYSQNSSLRSHQRVHTGQRPFSCGICGKSFSQRSALIPHARSHAREKPFKCPECGKRFGQSSVLAIHARTHLPGRTYSCPDCGKTFNRSSTLIQHQRSHTGERPYRCAVCGKGFCRSSTLLQHHRVHSGERPYKCDDCGKAFSQSSDLIRHQRTHAAGRR
Protein: Curculin-like (Mannose-binding) lectin family protein (Q94K76)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ribosomal RNA-processing protein 42
- Ribosomal RNA-processing protein 43
- Nuclear nucleic acid-binding protein C1D
- Ribosomal RNA-processing protein 40
- Ribosomal RNA-processing protein 40
- Exosome complex exonuclease RRP46-like protein
- Exosome complex exonuclease RRP46 homolog
- Exosome complex component RRP45A
- Exosome complex component RRP45B
- DExH-box ATP-dependent RNA helicase DExH9
Sequence:
MALSIVLLPFILILIPTFLSSVFAVSPLKTDTLKPGQQLRDWEQLISADGIFTLGFFTPKDSSTSELGSAGLRYLGIWPQSIPINLVWVGNPTESVSDSSGSLSIDTNGVLKITQANAIPILVNQRPAAQLSLVGNVSAILLDTGNFVVREIRPGGVPGRVLWQSFDHPTNTLLPGMKIGFNLRTKKEVSVTSWITDQVPVPGAFRLGLDPSGANQLLVWRRGEIYWSSGILTNNGSSHLNLEVSRHYIDYEFKFDSNKYMKYFSYSIKKANSSVFSSWFLDTLGQITVTFSLSSNNSSTWISESSEPCKTDLKNSSAICITEKPTACRKGSEYFEPRRGYMMENNTGYYPFYYDDSLSAGLSDCHGTCWRNCSCIAFQAFPDGCQYWEKGSKFVPYDSFNSNLVTYVLDSVK
Protein: Nucleus accumbens-associated protein 1 (NAC-1) (BTB/POZ domain-containing protein 14B) (Q96RE7)
Organism: Homo sapiens (Human)
Function: Functions as a transcriptional repressor. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines.
Subcellular location: Nucleus. Cytoplasm. Note=Distribution in the cytoplasm is dependent on phosphorylation. {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein mL64
- Histone deacetylase 4
- Splicing factor, arginine/serine-rich 19
- F-box/LRR-repeat protein 19
- Homeobox protein NANOG
- POU domain, class 5, transcription factor 1
- Transcription factor SOX-2
Sequence:
MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNNSRSAVVELPAAVQPQSFQQILSFCYTGRLSMNVGDQFLLMYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHAEEAPSSEPQSPVAQTSGWPACSTPLPLVSRVKTEQQESDSVQCMPVAKRLWDSGQKEAGGGGNGSRKMAKFSTPDLAANRPHQPPPPQQAPVVAAAQPAVAAGAGQPAGGVAAAGGVVSGPSTSERTSPGTSSAYTSDSPGSYHNEEDEEEDGGEEGMDEQYRQICNMYTMYSMMNVGQTAEKVEALPEQVAPESRNRIRVRQDLASLPAELINQIGNRCHPKLYDEGDPSEKLELVTGTNVYITRAQLMNCHVSAGTRHKVLLRRLLASFFDRNTLANSCGTGIRSSTNDPRRKPLDSRVLHAVKYYCQNFAPNFKESEMNAIAADMCTNARRVVRKSWMPKVKVLKAEDDAYTTFISETGKIEPDMMGVEHGFETASHEGEAGPSAEALQ
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (EC 7.1.1.2) (E5KNH5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU364066}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364066}; Matrix side {ECO:0000256|RuleBase:RU364066}.
Interaction partners:
Sequence:
MLATRRLLGWSLPARVSVRFSGDTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGSLSRGDWYKTKEILLKGPDWILGEIKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEGEPGTCKDREILRHDPHKLLEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELIEKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALVQAQTGLGTAAVIVMDRSTDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIEGHTICALGDGAAWPVQGLIRHFRPELEERMQRFAQQHQARQAAS
Protein: Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylglucosaminidase) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) (Q2CEE3)
Organism: Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516)
Function: Cleaves GlcNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrate (in vitro).
Interaction partners:
- Putative acetyltransferase OgpAT
- Probable N-acetylglucosamine kinase
- Sugar ABC transporter substrate-binding protein
- ABC transmembrane type-1 domain-containing protein
- Sugar ABC transporter permease
- Histidine ammonia-lyase
Sequence:
MLTGVIEGFYGRDWRRDERATVMDWIAAAGMNTYIYGPKDDVHVRARWRVPYDAAGLARLTELRDAAAARGMVFYVSLAPCLDVTYSDPQDRAALLARVDQLARAGLRNLVLLFDDIPSVLPEADRHRFDSFAEAQADLSNMVLRHLRGAGHVVFCPTEYCGRMAGGDPRGSAYLQRLGSTLDPAIDIFWTGPEIVSEEIVAAHLAAVGEVLRRRPVIWDNFHANDYDIRRVFAGPLGGRSRDILPLVAGWITNPNNEAEANFPAIHTTGAYLADPDYAPERAIAAAVAAWQPRFRLAFGDGAVPSDLVALLCDLFWQPFALGPETTRILSALRAALTVPRPDPSDPAWRAALEDLRDLKRRINKLFTLMTEIENRDLFHTFHNYLWEAQEEVGHLVAYCDWLDEAPPPGAVFPATDRIHNFYRRGFGVAVQDILQRDRQGRYHHGV
Protein: Uncharacterized protein (Q582B7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- C2 domain-containing protein
- EF-hand domain-containing protein
- Uncharacterized protein
Sequence:
MSRRVLWESVRQEARSRVEGVNASPISTNGIIEARDKSDGLITYEEGGGVSGVANDNEGGSHGKIGNMATVSQENRDTQNHATGSHDSIIASCDISCIPKDKHELHGPPSHLSRCGSSPEAEGNCSATADPTQSHLTDLAISVLLETGGDTHQDKGYNTGLDVNNSRFNSSATNNIHRELAQEKQKNIAAEQRLLTLEKKIRALREENQHLLLSSATNATDRKMMKGATSAYAEGEVVGHGVQRDFADEVTDTAGEELLALKRRCDELEVRLGELTAQVRQKDQELEQKENRIRQLEHIIANDLIRRSADVNKEENTQGRSEGVGRSSPKVEFSVKKDVPGKKNSSTQGTNGVVSRESPTTAAARETASSTAAAPPGLNLGDLRSVEALQRLLLSSIEATNLLVDSSRVSKGKEMDTLSVPSSLTHGSSHLAEGYTRVSTSDVKQRPLRVVRQGEIVSHSATSRASSAAGVRASPSRHGARHRASSVPGRCSESRASSVRAIRQRGPSSDSPMREAAMFARISSAPGCSKATSSLSSRRPPTQKLLSGRIPLRSTELFSNVTHMNRFSQYQNARRTSRPDACASAASPKSSCSTNKSNGRAPNVKKYVTPRARARPRIGVEATARSLKCSPPQKPSTTVITRVEKQRERTPPTPVRRAEYVKEVLSQDPFVSEMFKTTYRPNRLVRCSKEEGESV
Protein: Beta-toxin Cb1 (C0HLR3)
Organism: Centruroides baergi (Scorpion) (Centruroides nigrovariatus baergi)
Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and reduces peak current and shifts the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. Has an inhibitory effect on voltage-gated sodium channel hNav1.6/SCN8A, affecting both the activation and inactivation processes. This toxin is active against mammals and lethal to mice.
Subcellular location: Secreted {ECO:0000269|PubMed:32479835}.
Interaction partners:
Sequence:
KEGYIVNHSTGCKYECYKLGDNDYCLRECKAQYGKGAGGYCYAFGCWCTHLYEQAVVWPLPKKTCN
Protein: 3-hydroxyisobutyrate dehydrogenase, mitochondrial (HIBADH) (EC 1.1.1.31) (P31937)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion.
Interaction partners:
- 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Peroxisomal bifunctional enzyme
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Aldehyde dehydrogenase X, mitochondrial
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase, mitochondrial
- 4-aminobutyrate aminotransferase, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- Alpha-aminoadipic semialdehyde dehydrogenase
Sequence:
MAASLRLLGAASGLRYWSRRLRPAAGSFAAVCSRSVASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVFPDACKEFQDAGEQVVSSPADVAEKADRIITMLPTSINAIEAYSGANGILKKVKKGSLLIDSSTIDPAVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLGCMGSNVVYCGAVGTGQAAKICNNMLLAISMIGTAEAMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSANNYQGGFGTTLMAKDLGLAQDSATSTKSPILLGSLAHQIYRMMCAKGYSKKDFSSVFQFLREEETF