wanglab/gogpt-training-data huggingface dataset:
Protein: Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (ACAT-related gene product 1) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase) (O75907)
Organism: Homo sapiens (Human)
Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats. In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage. Also present in female mammary glands, where it produces fat in the milk (By similarity). May be involved in VLDL (very low density lipoprotein) assembly. In contrast to DGAT2 it is not essential for survival (By similarity). Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders. Exhibits additional acyltransferase activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z2A7}; Multi-pass membrane protein {ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611}.
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- 2-acylglycerol O-acyltransferase 1
- 2-acylglycerol O-acyltransferase 2
- 2-acylglycerol O-acyltransferase 3
- Phospholipid phosphatase 2
- Phospholipid phosphatase 3
- Phospholipid phosphatase 4
- Acyl-CoA wax alcohol acyltransferase 2
- Phospholipid phosphatase 5
- Retinoid isomerohydrolase
Sequence:
MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVGSGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPAAVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVSVPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLNYEAPAAEA
Protein: Polybromo 1 (C9JPI5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSKRRRATSPSSSVSGDFDDGHHSVSTPGPSRKRRRLSNLPTVDPIAVCHELYNTIRDYKDEQGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDVNLLTADFQLLFNNAKSYYKPDSPEYKAACKLWDLYLRTRNEFVQKGEADDEDDDEDGQDNQGTVTEGSSPAYLKEILEQLLEAIVVATNPSGRLISELFQKLPSKVQYPDYYAIIKEPIDL
Protein: Sorbitol-6-phosphate 2-dehydrogenase (EC 1.1.1.140) (Glucitol-6-phosphate dehydrogenase) (Ketosephosphate reductase) (P05707)
Organism: Escherichia coli (strain K12)
Interaction partners:
- PTS system glucitol/sorbitol-specific EIIC component
- PTS system glucitol/sorbitol-specific EIIB component
- PTS system glucitol/sorbitol-specific EIIA component
- Glucitol operon activator protein
- Mannitol-1-phosphate 5-dehydrogenase
- ATP-dependent 6-phosphofructokinase isozyme 2
- Uncharacterized protein YggP
- D-allulose-6-phosphate 3-epimerase
- ATP-dependent 6-phosphofructokinase isozyme 1
- Mannose-6-phosphate isomerase
Sequence:
MNQVAVVIGGGQTLGAFLCHGLAAEGYRVAVVDIQSDKAANVAQEINAEYGESMAYGFGADATSEQSVLALSRGVDEIFGRVDLLVYSAGIAKAAFISDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLLKSPMFQSLLPQYATKLGIKPDQVEQYYIDKVPLKRGCDYQDVLNMLLFYASPKASYCTGQSINVTGGQVMF
Protein: Pentatricopeptide repeat-containing protein 2, mitochondrial (B3KPU6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKDQHLRGFFSDSTSFNILMDMLFIKGKYKSALQVLIEMKNQDVKFTKDTYVLAFAICYKLNSPESFKICTTLREEALLKGEILSRRASCFAVALALNQNEMAKAVSIFSQIMNPESIACINLNIIIHIQSNMLENLIKTLKNAAEGNLSKFVKRHVFSEEVLAKVREKVKDVPALVAKFDEIYGTLHITGQVTTDSLDAVLCHTPRDRKSHTLLLNKRMVSRRTFQPLSQSLLAE
Protein: ATPase family AAA domain-containing protein FIGL1 (AAA-ATPase FIDGETIN-LIKE 1) (EC 3.6.4.-) (F4JEX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Limits class II meiotic crossover (CO) formation by regulating the invasion step of meiotic HR. May counteract DMC1 and RAD51-mediated inter-homolog strand invasion to limit CO formation. Functions independently of FANCM.
Subcellular location: Nucleus {ECO:0000269|PubMed:26161528}.
Interaction partners:
- Holliday junction resolvase
- DEAD-box ATP-dependent RNA helicase FANCM
- ATP-dependent DNA helicase Q-like 4A
- ATP-dependent DNA helicase Q-like 4B
- Protein MHF1 homolog
- E3 ubiquitin-protein ligase CCNB1IP1 homolog
- Crossover junction endonuclease MUS81
- Protein MHF2 homolog
- DNA mismatch repair protein MSH4
- Meiotic recombination protein DMC1 homolog
Sequence:
MCGSVVSDSEREFEFHFWGFGHLGKEEERIMAGKRSSPFSSPLLRPPPEFLNVKEEGETETPCWRKEVDENLKRLQSLLFGADKFLEKSDFSSAQILGLRLLGFLDSRSVTDADRDFIGPIRREVASKIDLALEGLVSDSDRKAFELANTAPGAIFGSKGGFDVEKIKQSKYFGFHVSQSNGKGVKEMEERHDTDKLIPKAPKSMMQAKLTSLYGNSIGKPDNQRKTSVNNQDRASDECVIVERSHGFGFGTKRPHAETSSLANDGEVKEDGAPNGFVSAKIKLEMDVRQKRGSTESPSSCLSPQSDKNALGRGYGSRSGGLRRGYRSNFVPPVKTNGNNVGNLTSRIGGKTDDALDDSTRTCLEMLCGPDGELPEKLRNLEPRLIEHVSNEIMDRDPNVRWDDIAGLEHAKKCVTEMVIWPLLRPDIFKGCRSPGKGLLLFGPPGTGKTMIGKAIAGEAKATFFYISASSLTSKWIGEGEKLVRALFGVASCRQPAVIFVDEIDSLLSQRKSDGEHESSRRLKTQFLIEMEGFDSGSEQILLIGATNRPQELDEAARRRLTKRLYIPLPSSEARAWIIQNLLKKDGLFTLSDDDMNIICNLTEGYSGSDMKNLVKDATMGPLREALKRGIDITNLTKDDMRLVTLQDFKDALQEVRPSVSQNELGIYENWNNQFGSLSL
Protein: N6-succino-2-amino-2'-deoxyadenylate synthase (EC 6.3.4.25) (2-amino-2'-deoxyadenylo-succinate synthase) (PurZ) (A0A7U3TBV6)
Organism: Cyanophage S-2L (Cyanobacteria phage S-2L)
Function: Involved in the synthesis of the atypical nucleotide dZTP (2-amino-2'-deoxyadenosine-5'-triphosphate). Catalyzes the condensation of aspartate with deoxyguanylate into dSMP (N6-succino-2-amino-2'-deoxyadenylate), which undergoes defumarylation and phosphorylation respectively by host PurB and guanylate/nucleoside diphosphate kinases to give dZTP. dZTP is integrated into the viral genome instead of adenine by the viral DNA polymerase. This Z-base probably completely replaces adenosine and forms a triple bond to the opposite T-base. The resulting non-standard viral DNA is called Z-genome. The chemically modified DNA is probably harder for the host bacteria to digest with nucleases or restriction enzymes (Probable).
Interaction partners:
Sequence:
MLSIPPYYRVKNCNLIVDCQYGSTGKGLLAGYLGALEAPQVLCMAPSPNAGHTLVEEDGTARVHKMLPLGITSPSLERIYLGPGSVIDMDRLLEEYLALPRQVELWVHQNAAVVLQEHRDEEAAGGLAPGSTRSGAGSAFIAKIRRRPGTLLFGEAVRDHPLHGVVRVVDTRTAQDMLFRTRSIQAEGCQGYSLSVHHGAYPYCTARDVTTAQLIADCGLPYDVARIARVVGSMRTYPIRVANRPEAGEWSGPCYPDSVECQFADLGLEQEYTTVTKLPRRIFTFSAIQAHEAIAQNGVDEVFLNFAQYPPSLGALEDILDAIEARAEVTYVGFGPKVTDVYHTPTRAELEGLYARYRR
Protein: Signal peptide, CUB and EGF-like domain-containing protein 3 (Q8IX30)
Organism: Homo sapiens (Human)
Function: Is a positive regulator of the BMP signaling pathway, required for proper chondrogenesis, osteogenesis and skeletal development. It acts as coreceptor for BMP ligands, particularly BMP2 and BMP4, facilitating their interactions with BMP type I receptors. It is required for ligand-induced recruitment of BMP receptors to lipid rafts (By similarity). Binds to TGFBR2 and activates TGFB signaling. In lung cancer cells, could serve as an endogenous autocrine and paracrine ligand of TGFBR2, which could regulate TGFBR2 signaling and hence modulate epithelial-mesenchymal transition and cancer progression.
Subcellular location: Secreted {ECO:0000269|PubMed:15234972, ECO:0000269|PubMed:33308444}. Cell surface {ECO:0000269|PubMed:15234972, ECO:0000269|PubMed:33308444}.
Interaction partners:
- TGF-beta receptor type-2
- Matrix metalloproteinase-9
- 72 kDa type IV collagenase
- Signal peptide, CUB and EGF-like domain-containing protein 1
Sequence:
MGSGRVPGLCLLVLLVHARAAQYSKAAQDVDECVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHCKDVDECEREDNAGCVHDCVNIPGNYRCTCYDGFHLAHDGHNCLDVDECAEGNGGCQQSCVNMMGSYECHCREGFFLSDNQHTCIQRPEEGMNCMNKNHGCAHICRETPKGGIACECRPGFELTKNQRDCKLTCNYGNGGCQHTCDDTEQGPRCGCHIKFVLHTDGKTCIETCAVNNGGCDSKCHDAATGVHCTCPVGFMLQPDRKTCKDIDECRLNNGGCDHICRNTVGSFECSCKKGYKLLINERNCQDIDECSFDRTCDHICVNTPGSFQCLCHRGYLLYGITHCGDVDECSINRGGCRFGCINTPGSYQCTCPAGQGRLHWNGKDCTEPLKCQGSPGASKAMLSCNRSGKKDTCALTCPSRARFLPESENGFTVSCGTPSPRAAPARAGHNGNSTNSNHCHEAAVLSIKQRASFKIKDAKCRLHLRNKGKTEEAGRITGPGGAPCSECQVTFIHLKCDSSRKGKGRRARTPPGKEVTRLTLELEAEVRAEETTASCGLPCLRQRMERRLKGSLKMLRKSINQDRFLLRLAGLDYELAHKPGLVAGERAEPMESCRPGQHRAGTKCVSCPQGTYYHGQTEQCVPCPAGTFQEREGQLSCDLCPGSDAHGPLGATNVTTCAGQCPPGQHSVDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAISFQDCDTKVQCSPGHYYNTSIHRCIRCAMGSYQPDFRQNFCSRCPGNTSTDFDGSTSVAQCKNRQCGGELGEFTGYIESPNYPGNYPAGVECIWNINPPPKRKILIVVPEIFLPSEDECGDVLVMRKNSSPSSITTYETCQTYERPIAFTARSRKLWINFKTSEANSARGFQIPYVTYDEDYEQLVEDIVRDGRLYASENHQEILKDKKLIKAFFEVLAHPQNYFKYTEKHKEMLPKSFIKLLRSKVSSFLRPYK
Protein: Keratin-associated protein 2-3 (High sulfur keratin-associated protein 2.4) (Keratin-associated protein 2.3) (P0C7H8)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity).
Interaction partners:
Sequence:
MTGSCCGSTLSSLSYGGGCCQPCCCRDPCCCRPVTCQTTVCRPVTCVPRCTRPICEPCRRPVCCDPCSLQEGCCRPITCCPSSCTAVVCRPCCWATTCCQPVSVQSPCCRPPCGQPTPCSTTCRTSSC
Protein: Sterile alpha motif domain-containing protein 11 (SAM domain-containing protein 11) (Major retinal SAM domain-containing protein) (Mr-s) (Q1RNF8)
Organism: Mus musculus (Mouse)
Function: May play a role in photoreceptor development.
Subcellular location: Nucleus {ECO:0000269|PubMed:16539743}.
Interaction partners:
Sequence:
MPEHPRHCDFQRGNVEIGLGPGGDLLGKRLSCPCITSHCSSEKKARSKDPQATSLLPELESTMAPEDHYHQLMSALSEASSFEETQRLYHLGIPSHDLLRVRQEVATATLRGPSGLEVHLPSSTADHRRKQGLVQRREGAVPAAATSFSEREMSQPPPLLSPQNAAHITMSSHLRPPFLGMPTAVCQTPGFSFLPSAQAEMLARQQELLRKQSLARLEMSELLRQKELGSVHRPLLPAPEVALHIPEGPDELQRRGSMLVLKHSSAPLLALPPQGPPGPGPPIPPKESARSRSEKGSLGVQPSQPKETTGAGLWAQEVSEEPSKDSDGEDPETAAAREGTSTPSQVPAGGTRAEGRGLLSGSTLPPPLPLGFPCGAVSPYFHTGTMGGLFTDEETTTLEDVNKWTVDDVCNFVGGLSGCGEYARVFGEQGIDGETLPLLTEEHLLNTMGLKLGPALKIRAQVAKRLGRVFYMASFPVALPLQPPSLQAPELSPGHQPLSPATTTSPYEGTHLPTGQASPKQENGSGTIALLSGAPDPSQLLQ
Protein: Hexokinase-3 (EC 2.7.1.1) (Hexokinase type III) (HK III) (Hexokinase-C) (Q3TRM8)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate.
Interaction partners:
- GDH/6PGL endoplasmic bifunctional protein
- ATP-dependent 6-phosphofructokinase, liver type
- Glucose-6-phosphate isomerase
- Glucose-6-phosphatase 3
- Glucose-6-phosphatase catalytic subunit 1
- Glucose-6-phosphatase 2
- Non-selective voltage-gated ion channel VDAC1
- Phosphoglucomutase-1
- ATP-dependent 6-phosphofructokinase, platelet type
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Sequence:
MATIGPSGLHPGERASVCPHEGVPRPSGSLELECLQQFKVTRTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATGASLRVLWVTLTGTKECRVEPRSREFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYRIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEDALGPVLTTFDSALDRESLTPGAQRFEKMIGGLYLGELVRLVLVHLTQHGVLFDGCASPALLSQGCILLDHVAEMEDTATGTARVHTILQDLGLSPRASDAELVQYVCVAVCTRAAQLCAAALAAVLSRLQHSREQQTLQVAVATGGRVFERHPRFLRILKETVTLLAPNCDVSFIPSVDGGGRGVAMVTAVAARLAAHRRILEETLAPFQLTLEQMTVVQAQMREAMIRGLQGEASSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQIINQVYSIPECRAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPRCEMGLIVGTGTNACYMEELRNVASVPGDSGLMCINMEWGAFGDDGSLGTLSTRFDTSVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTNLGVLFRGQKTQCLQARDIFKTKFLSEIESDSLALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSKLVSATVRKLAPQCTVTFLQSEDGSGKGAALVTAVACRLTQMAHV
Protein: Probable respiratory burst oxidase homolog protein I (EC 1.11.1.-) (EC 1.6.3.-) (NADPH oxidase RBOHI) (AtRBOHI) (Q9SUT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-dependent NADPH oxidase that generates superoxide.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- AICARFT/IMPCHase bienzyme family protein
- Tetratricopeptide repeat
- Calcium-dependent protein kinase 30
- Calcium-dependent protein kinase 10
- Nucleobase-ascorbate transporter 2
Sequence:
MSMSFSGGTHNDRWGSDLASAGEFTQSFPSLPATYSPSPSSSSSSGEELLEVTIEFPSGVIINIDSVTGTGTDISGTDLEITSCSDSGSGSRSLSLGWSASSERLTAGTNSKQQIQKISRRGYGYSSRSAPEPVVPHRGEITDSVNLPRALSQRPTRPNRDGSGTERAIHGLKFISSKENGIVDWNDVQNNFAHLSKDGYLFKSDFAHCIGLENENSKEFADELFDALCRRRRIMVDKINLQELYEFWYQITDESFDSRLQIFFNMVKNGDGRITENEVKEIIILSASANNLSRLRERAEEYAALIMEELAPDGLYSQYIELKDLEILLLEKDISHSYSLPFSQTSRALSQNLKDRRWRMSRNLLYSLQDNWKRIWVLTLWFVIMAWLFMWKCYQYKHKDAFHVMGYCLVMAKGAAETLKFNMALILLPVCRNTITYLRSTALSHSVPFDDCINFHKTISVAIISAMLLHATSHLACDFPRILASTDTDYKRYLVKYFGVTRPTYFGLVNTPVGITGIIMVAFMLIAFTLASRRCRRNLTKLPKPFDKLTGYNAFWYSHHLLLTVYVLLVIHGVSLYLEHKWYRKTVWMYLAVPVLLYVGERIFRFFRSRLYTVEICKVVIYPGNVVVLRMSKPTSFDYKSGQYVFVQCPSVSKFEWHPFSITSSPGDDYLSIHIRQRGDWTEGIKKAFSVVCHAPEAGKSGLLRADVPNQRSFPELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLNNIIKQQEQAECISGSCSNSNISSDHSFSCLNSEAASRIPQTQRKTLNTKNAYFYWVTREQGSFDWFKEIMNEIADSDRKGVIEMHNYLTSVYEEGDTRSNLLTMIQTLNHAKNGVDIFSGTKVRTHFGRPKWKKVLSKISTKHRNARIGVFYCGVPSLGKELSTLCHEFNQTGITRFDFHKEQF
Protein: rRNA N(6)-adenosine-methyltransferase Mettl5 (EC 2.1.1.-) (Methyltransferase-like protein 5) (Q8MSW4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic subunit of a heterodimer with Trmt112, which specifically methylates the 6th position of adenine in 18S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32350990}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- Methyltransferase N6AMT1
- 18S rRNA
Sequence:
MARLKLRKLEEYLQGVDGFEQPKILLEQYPTPPHIAACMAHHMQSQHEDIEGKLVGDLGCGCGMLSIASTLLGAQLTVGFELDGDAVDTFRGNVVEMELPNVDCVRADVLQLIGSKWEKSFDTVLMNPPFGTKHNAGMDMRFLEVALRLANRAVYSLHKTSTRSYIQKKALEWGARGSVVAELRYNIDASYKFHKQKSKDIEVDFWRFEIGTE
Protein: Cytochrome b-c1 complex subunit 9 (Complex III subunit 9) (Complex III subunit X) (Cytochrome c1 non-heme 7 kDa protein) (Ubiquinol-cytochrome c reductase complex 7.2 kDa protein) (Q8R1I1)
Organism: Mus musculus (Mouse)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 6B1
- Cytochrome b-c1 complex subunit 10
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
Sequence:
MSSPTIPSRLYSLLFRRTSTFALTIAVGALFFERAFDQGADAIYEHINEGKLWKHIKHKYENKE
Protein: Reduction in Cnn dots 1, isoform E (EC 3.-.-.-) (A0A0B4KF25)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- KAT8 regulatory NSL complex subunit 2
- GH01794p
- Protein MBD-R2
- Protein will die slowly
- Histone acetyltransferase MOF
- Non-specific lethal 1, isoform M
- Protein male-specific lethal-1
- Protein male-specific lethal-3
- Dosage compensation regulator mle
- Histone acetyltransferase Tip60
Sequence:
MKESGSVSKNQPQTSEARGSIITYSPSKFLTSVGTGRTTYSTHTHTTTATSAATTATKTNNLPMGGSSAAYYVVKAGSLGSAASMSGCIKVSSPPKGPPMAKSPALVVTSPCTPTESSSTISAPSESSFSEKMEHSYMRDTPVRSDVHNGLTPARNILVRHPPQCPSCHTYPPQHEELSEIQQAHVPPYDEVVAKEAMNECARIAKYVKNNNSDEQDWVARVNKFNWTPMQEMVFEKVCSILDQDQLARLANDKRQHEPIHRRISSDKSASRFRKLLASVAWESRITQWIHALLMEHLSPSYMASYLEILQTLKTKLPTLVDKMLFGRPLNNSQELLAPVMKKRWEPNIMPKSRQLTHNAIMVVLPNMPTTGTVSDRMQKWYQALSTITQVVQISLPNTNNRIGNQNLDHVAETIVSITRVKINELRTENPSRGIILVGFNAGAALALQVALSESVACVVCMGFAYNTIRGPRGTPDDRMLDIKAPILFVIGQNSARTSQEEMEGLRERMQSESSLVVVGSADDALRVPKSKRRIEGVTQSMVDYMVVEEIFEFVNRTLSNPPGPRMPTCLMHQQGYQRLPKQSPHILADGNANKAVQQMRKRKMDGGLDDSMGQPSKTKFVPHNRVHKPKPPRLIDPFAVKRKVGRPRTRPLPNVGGSARSVSQKGAPHPDQPKLSGEEPNQSIEFILDDAQDYGDAQTTAGGSASLPKVITPGVLGKQLPPVNLAAGTKIKMIPSSQFVQIKSLPSQSKLINYTLNKPSVGTSSTANIGSVVKTLPCSSVSGQQIITLKTPSGQTQQFATAATSTGAAGSSTSTGTGQKKYTVFKNANGMTMLHLTKSVPTTGSSSGSANMDLSNIIDMPIVFADNEGNIPEHQQADKDIKPAPIRSANKSPLIISQKIIKEANKPSGMVTSGSITAVSKPGNIVLNKGLQQLLNSSPGGTLATQNKVVYLNRSTIKPMGNVAPGTHRVPIRIVSTPNTGGAVTTTASSSPIMVDPATGSKVAKTVNVQTIKPTGSVLAQGTIRQAGNVGTKSYLQMINTAPGASKTVAGDGKGSVRNIYFKSATGLKQLPVQMLGNRIPGGAVISSTASASSGSPGLRRVVNIGPVSKVTATSTTSSSIAATLTHNKM
Protein: Mitochondrial RNA binding protein (Q57WL3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Guide RNA binding protein
- HTH OST-type domain-containing protein
- Uncharacterized protein
- Treble clef zinc finger domain-containing protein
Sequence:
MRRLSLLPRRSAAVVGSAYARFATPAAPTNLKASTLELNNPVVTHTAHTPVTLTATTDAASGNIYSSKEVEAEVAVPAAGAKEKIQASRRKHVNTVELLISMAVTLQKKSSGAAAAAVTDSACGDEKKEATDGDATVGIAPRPVDPLQLLKALRAYIRSEDILAELCRSKVQAVRQRYVAIRARRQRVPAFHRDILLSEVTRVVERREVPYIEVARLLRPHWPAQLMDASGGRYHSFLQRSLLAWIAELLREGKLSPEEARSVLSQCPRLFHGHLSLMSSIVECALLDINTIQSPDPIIGLMWSVNEAGTHAPSHFWQRTVGRLAQLNRSLRDTLGDAMQLGKCGNGPKDGTTIHSGPGGREKKGEKGNIKSNNDNKGGNINDTKQNYTVGHVFSGLTTRQLFRVLRVLRKECWCNDVSTVYDFVDKALKNIAFEVEAIGSCEATSQKRPMSRQTITQRVKKSADLTPKELLSLLSIAGELGVDFHASLARTSDFLLAPMVHYLDREELLQLSLFVRKTRCDSLTLVQSIADEIVRRGVNYPLSVSLSKAALRTALQKPVLLSQLTLTPLVDHVISLCRTYGWYMRASQLLGWAEVLYDLSRRYAPSSSVGVNVRSCVEALAAPLRAMLEAGVVPMPVVSRFIELTVILGMRAKPHQYTQSIKLWEERNAAANARITFAKSVLNKESDMLIPMSELLYDAAELEDSGEVGEVTSRPTAELCRAARQVYDELIYLFEMQMIMRSPITQKEEDRLNDTFSHVGLYNIVVGARAMWRVHLQPSSFPSANASCVEGVVPLSSPHRISSTPPRALPVWVERRINATIEGRIRRANISPTSTDEDVLRLFGQRHCNAAKVRHFMQLLMEESSLVLVKQQRFVWIFTAELARRFGGGQEQQMAQKMLAKVFC
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q9VKZ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH11341p
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory complex subunit p50
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 11
Sequence:
MPAFKVKVKWGRELYTDIVVNTDEEPILFKAQLFALTGVQPDRQKVMCKGGILKDDQWNLQIKDGAVVLLLGSKESVPEVPATPVKFIEDMNEAEAATAMRLPAGLTNLGNTCYMNATVQCLNAVPELRTALSTFSNDGTDTMSTAFSISSAMKSIFAQMEKGTTVTPIVLLQALHRASPQFAQTGENGTYRQQDANECWAEILKMLQQKLRPKNQEPSNTVQKRHSSFIDQFFGGTFEVKMSSEEDPDEPSTVTSENFLQLSCFISMDVKYMQSGLKSKMKEQLVKKSETLGRDAKYIRTYLVSRLPAYLTVQFVRFQYKGKEGINAKVLKDIKFPIDFDAFELCTPELQNKLCPMRSKFKDLEDKKMEVDVVKRNEPNEEKKDVKYEQFWFDDDLGSNNSGYYTLQAVLTHKGRSSSSGHYVAWVRSSGDVWFKFDDDEVSAVATDEILRLSGGGDWHCAYVLLYAPRRLEKL
Protein: Forkhead box P, isoform E (A0A126GUS5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MHRIHDDEYSEDAKESDFKSSIQKEISVKSRHQISIPDICSDAVKNNCFPPTGFLNNSITFASHVVKCSSPASSIDESSTAAQQHESNPHMHIQGQHMMAPVPDLGFYNVPEFISEQEKLMFSDAERFLRSKDNEVCNNDFSYMHDEFAMRKYYHPLFAHGICRWPGCEMDLEDITSFVKHLNTEHGLDDRSTAQARVQMQVVSQLESHLQKERDRLQAMMHHLYLSKQLLSPTKIDRKDVPGREGKFCRSPLTVNSIGRPIRQTNSPSPLNLPMVNSTNLCSIKKRNHDKNTFSINGGLPYMLERAGLDVQQEIHRNREFYKNADVRPPFTYASLIRQAIIDSPDKQLTLNEIYNWFQNTFCYFRRNAATWKVKCPIYVNLLSSILSIYYAT
Protein: DIS3-like exonuclease 2 (EC 3.1.13.-) (Q09568)
Organism: Caenorhabditis elegans
Function: 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03045}. Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03045}.
Interaction partners:
- Exosome complex component 10 homolog
- Exosome complex component RRP4 homolog
- Exosome complex component CSL4 homolog
- Exosome complex component RRP40
- Putative exosome complex component RRP41
- Exosome complex component RRP46 homolog
- Exoribonuclease phosphorolytic domain-containing protein
- Exosome complex component RRP45
- Ribosomal RNA-processing protein 42
- Nuclear nucleic acid-binding protein C1D
Sequence:
MSAVESPVIVTEPGSLKPQGLTQTATGGKFGAAATVKTTPTKAKPYVKPQNANNLQNNFNPRKIFTEYISKEETDAGIEDGSMFKGVLRINPKNYQECFLDHPKGTNHPDVLVLGQDRNRAMQGDVVAVKIKPKEDWLVNYVEYVKWWAEHKKGDRNSGKTDNNSPNKTEKRCLRNEIQDNGVTSDEVPDSCLITIGAIVHILEKKHFRVAAGKLQLMPNSANPNVLFVATDSRVPRILIPKSDVDKEFFSRPKDFERFLYTAKITDWRAESVYADGRLVKLLGMSGEIDTETERIVYEHQIDHREFSDECLESLPITTAENWKVPDAEFEYRRDFRSDIVFTIDPKTARDLDDALHAKHIDDCDGKGTPGLEIGVHIADVTFFLKEGTELDKWASERGNSTYLSQTVIPMLPRILCEQLCSLNPGVDRLSFSTVFKMSYEAELYDVWFGRSVIRSRVKLAYEHAQDFIENPEKDFTCDELPDISDGNTPFEIKEKTLMLHRIAQVLRQKREDSGALRIELPRLKFALDEDKKPQGVSIYEIKDSNKLVEEFMLLANMEVAKKIAENFPEHALLRNHPPPKEKMIKDVAEQCARIGFPLDGRTSGLLSTSLRKYQGKSRLDMCIRQVISSLTIKPMQQAKYFCTFEMPLSFYHHFALNVDHYTHFTSPIRRYPDVIVHRQLAAALGYNERSERVPEEIQEICTRCNDTKLASKEASDESAMLYFGVFIHQTGPMKCQAVVLGVMDLSFDVLIVEYGVVKRVYVDKMKRDFNKSTEKLTIYWPADPNAESGNREEFSSSIQMCNVVYVILVPYKSIEVSATIVRPSLEQRNILKSTLKDMKETGSTILQ