wanglab/gogpt-training-data huggingface dataset:
Protein: Histone H2A-Bbd type 2/3 (H2A Barr body-deficient) (H2A.Bbd) (P0C5Z0)
Organism: Homo sapiens (Human)
Function: Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo. They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase. They associate with spliceosome components and are required for mRNA splicing. May participate in spermatogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:20008104}. Chromosome {ECO:0000269|PubMed:20008104, ECO:0000269|PubMed:22795134}. Note=Associated with the active X chromosome and with autosomes, while it is absent from the inactive X chromosome and excluded from Barr bodies. {ECO:0000269|PubMed:20008104}.
Interaction partners:
- Histone H4
- Histone H2B type 2-E
- Histone H3.1
- Histone H4-like protein type G
- Histone deacetylase 1
- Histone H3-like centromeric protein A
- Histone deacetylase 2
Sequence:
MPRRRRRRGSSGAGGRGRTCSRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLSTLFNTTTISQVAPGED
Protein: Alpha-L-arabinofuranosidase B (ABF B) (Arabinosidase B) (EC 3.2.1.55) (Q2UIM2)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Probable alpha-L-arabinofuranosidase A
- non-reducing end alpha-L-arabinofuranosidase
- non-reducing end alpha-L-arabinofuranosidase
- galacturonan 1,4-alpha-galacturonidasegalacturonohydrolase)
- Xylanolytic transcriptional activator xlnR
- Endopolygalacturonase I
- Exo-1,4-beta-xylosidase xlnD
- galacturonan 1,4-alpha-galacturonidase
- Endopolygalacturonase B
- Gfo/Idh/MocA-like oxidoreductase N-terminal domain-containing protein
Sequence:
MSSGLSLERACAVALGIVASASLVAAGPCDIYSSGGTPCVAAHSTTRALYSAYTGALYQVKRGSDGSTTDIAPLSAGGVADAAIQDSFCANTTCLITIIYDQSGRGNHLTQAPPGGFNGPESNGYDNLASAVGAPVTLNGKKAYGVFMSPGTGYRNNAASGTATGDKAEGMYAVLDGTHYNSACCFDYGNAEVSNTDTGNGHMEAIYYGDNTVWGSGAGSGPWIMADLENGLFSGLSSTNNAGDPSISYRFVTAVVKGEANQWSIRGANAASGSLSTYYSGARPSASGYNPMSKEGAIILGIGGDNSNGAQGTFYEGVMTSGYPSDATENSVQADIVAAKYAIASLTSGPALTVGSSISLQVTTAGYTTRYLAHDGSTVNTQVVSSSSTTALRQQASWTVRTGLANSACLSFESVDTPGSYIRHYNFALLLNANDGTKQFYEDATFCPQAGLNGQGNSIRSWSYPTRYFRHYENVLYVASNGGVQTFDATTSFNDDVSWVVSTGFA
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit A, putative (EC 2.4.1.198) (Q8IJ83)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- N-acetylglucosaminylphosphatidylinositol deacetylase
- Phosphatidylinositol N-acetylglucosaminyltransferase, putative
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P, putative
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1
- GDP-L-fucose synthase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Lysine decarboxylase-like protein, putative
- Dolichol-phosphate mannosyltransferase subunit 1
- Glucose-6-phosphate isomerase
- Phosphomannomutase
Sequence:
MESAVSECNIYKKEKDKNIIYKQERKCCICMVSDFFYPNLGGIETHIFELSKNLIKKGFKVIVVTNFNNNRHGIRWMGNGIKVYYLPFQPFLDVVSFPNIIGTLPLCRNILYREKVDIVHGHQATSALAHQFILHAKTLGIKTIYTDHSLYSFSDKGCIHVNKLLKYCINDVDHSICVSHTNRENLVLRTESNPYKTSVIGNALDTTKFVPCISKRPKFPRINIIVISRLTYRKGIDLIVKVIPLVCQKYPFIKFIIGGEGPKRLLLEEMREKYHLHNSVVLLGKVKQENVKNILQTGHIFLNTSLTEAFCIAIIEAASCGLLVISTDVGGISEVLPHDMMILAKPNHIELCKAVDKALKIVQKVDSNLFHERLTKMYSWEKVAEKTEKVYMNVLNYANPSLFNRIRKIYEINTVFSIIYIFIIMISYIGCQILEWLMPRQNIEEVVSFPHFYDDENKNEK
Protein: Polyamine aminopropyltransferase (Putrescine aminopropyltransferase) (PAPT) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16) (Q9WZC2)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. It has lower affinity and lower activity towards 1,3-diaminopropane, cadaverine (1,5-diaminopentane), agmatine, norspermidine and spermidine (in vitro).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme
- Ornithine decarboxylase
- 5-methylthioadenosine/S-adenosylhomocysteine deaminase
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- Flagellar motor switch protein FliM
- Conserved hypothetical protein
Sequence:
MRTLKELERELQPRQHLWYFEYYTGNNVGLFMKMNRVIYSGQSDIQRIDIFENPDLGVVFALDGITMTTEKDEFMYHEMLAHVPMFLHPNPKKVLIIGGGDGGTLREVLKHDSVEKAILCEVDGLVIEAARKYLKQTSCGFDDPRAEIVIANGAEYVRKFKNEFDVIIIDSTDPTAGQGGHLFTEEFYQACYDALKEDGVFSAETEDPFYDIGWFKLAYRRISKVFPITRVYLGFMTTYPSGMWSYTFASKGIDPIKDFDPEKVRKFNKELKYYNEEVHVASFALPNFVKKELGLM
Protein: GATA-binding factor 1-A (Transcription factor xGATA-1A) (P23767)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that acts synergistically with tal1/scl and lmo2 to specify embryonic dorsal mesoderm to a hematopoietic fate.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P15976}.
Interaction partners:
Sequence:
MDYTTLTTQDPDPNYTESGLASTSEDSQFLYGLGGESSPGHYGGAVSSRAVGGFRHSPVFQTFPLHWPETSAGIPSNLTAYGRSTGTLSFYPSAASALGPITSPPLYSASSFLLGSAPPAEREGSPKFLETLKTERASPLTSDLLPLEPRSPSILQVGYIGGGGQEFSLFQSTEDRECVNCGATVTPLWRRDMSGHYLCNACGLYHKMNGQNRPLIRPKKRLIVSKRAGTQCSNCHTSTTTLWRRNASGDPVCNACGLYYKLHNVNRPLTMKKEGIQTRNRKVSSRSKKKKQLDNPFEPPKAGVEEPSPYPFGPLLFHGQMPPMGHMINPPHHFLQSPRISHSAPAVSYRQAASGVTPP
Protein: DNA-binding protein Ets97D (D-elg) (Q04688)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have a role in germline development.
Subcellular location: Nucleus.
Interaction partners:
- Ada2a-containing complex component 3, isoform D
- FI18188p1
Sequence:
MNSSNDLSDELIRRLSVGGALEEVIASEMFEDSIDVETEAEPDDIIIVHMDIREPLSMLKSLVEQKIGVCLNYYTFWLQDAQELESHKNLVDQCVKGEGLVQINVQIQTIRKRINIADVLKPTEAALAALAEEVVGQLSPPETASQKSSSSESPIKTPLKRMHKEDSEEESVEGKDVKPVLNWVLDSKFKREQIRLKIPEAANEWTHAHVTYWLEWAVKQFELVGINMSDWQMNGQELCAMTHEEFNQKLPRDPGNIFWTHLQLLKECNFVSVVHKRAEEQRKPKQPRIMSANSISTNSGGSLSLEQRIMRKSYQSVKSSDSVESTTSSMNPSNYTTIGSGNNGQVQLWQFLLEILTDCEHTDVIEWVGTEGEFKLTDPDRVARLWGEKKNKPAMNYEKLSRALRYYYDGDMISKVSGKRFAYKFDCDLKLLIGYDANELSTLVSEGKTAPERVAATETITEDT
Protein: Large ribosomal subunit protein eL30 (60S ribosomal protein L30) (P62889)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein eL22
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
Sequence:
MVAAKKTKKSLESINSRLQLVMKSGKYVLGYKQTLKMIRQGKAKLVILANNCPALRKSEIEYYAMLAKTGVHHYSGNNIELGTACGKYYRVCTLAIIDPGDSDIIRSMPEQTGEK
Protein: Myosin motor domain-containing protein (B6VQ62)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MENPLLARQIPRAYPYQNGNVVPPPPSSYRAPSPAPTSGDRRGLNRLPQESYTEPAVKNTKNNSEYLSPHRFNLDEQKAVIRHEKETAKNAINMLSDRLRKLPPPVDNVRLIRPITPAQPPITQSPVPSEPVVVRTPSPVPQPTPPPPPPPVREEWVIRDSVERDPVTQGRIRGSFRKEPLVPQPPRPPVVAEKPAVKFVKAPWKLTIRKEMFYPGEVLNDIQIIDQVFAQIVEDCKKSYPYRIREQDRKQVETVLRQYEIPPSDLNNQSNIHPDVKVAVIELARLWPLYFNQVYEVVEKRPDESVSTIFAISEHGIRLIVHTPHDLENPLKIQDFFPFETIADVSLEANDILSVHVRHEDEENAYSAVRIKTNQAPQIKKTLDRCLSGGVVPKRKFVRALEDYVTSEVNHLSFKQGDVIELLQEPEGETPPVGNWLYGKIENRFGFLLAQYVDSTDGDNVPPIRHETSEDRDERVRFFDDEVPFSSERYTMIDFATKYFRKPKDKKKQETWAWEDISQIVRFSEKPISQSLLADLGNEESKYAVETFHAIMKFMGDEPLKKSESMTDVVFKVLLICHRQPTLRDEVYCQLIKQTTSNISQKPNSALRAWRLLTIITAYFPSSLTLKPYVLQYLGDNADEWQRPFHGTARICQTNMIQTFKYGGRKVLLNALEVQQITDGCQLRRQAFYISKDHNVSQTLRPITVAEEMIQELCNLLNVRSLHEQQEFSLCYTVGKDKHLNYCKNDNYLMDIITESEHKKLPFQFYLKRTVWVHPLRYDNAAYIDSMFDQVIDDYLRGSLISTNSLGQLTAATTEEIIKLAAYLFLLLPDNPKGLNAKTLPQIVPKSVIEPKHRHQEEMVTRISRQLKMFGGRMRPAEAKSHFLELLSTWPTFGVLHYRLKSVVENGHQLPEVILTINKSGIQLLQPKSKEVFKERNYDQIVSVESIRKTAYKIVRLVINTMQGEETLDIKTDEADEISHLIGQYMFVTGGAEERGSTEL
Protein: Probable esterase afoC (EC 3.1.2.-) (Asperfuranone biosynthesis protein B) (Q5BEJ8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Probable esterase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent. The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation. AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2. After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination. AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone. Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood. Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency.
Interaction partners:
Sequence:
MPALDIASAPAAVYQQQLHLPRILCLHGGGTNARIFTAQCRALRRQLTDSYRLVFADAPFLSSAGPDVTSVYGEWGPFRSWVPVPAGVDISAWAAAGAASRIDIDVEAIDECIAAAIAQDDRAGATGDWVGLLGFSQGARVAASLLYRQQKQQRMGLTSWSRGRDRKRGATSSTNYRFAVLFAGRGPLLDLGFGSGSLAGSSAASSSASASVSGSESAGEEEEDGHLLSIPTIHVHGLRDPGLEMHRDLVRSCRPSSVRIVEWEGAHRMPITTKDVGAVVAELRHLAISRKYESLRC
Protein: Mce associated membrane protein (P71754)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Resuscitation-promoting factor RpfD
- Heme chaperone HemW
- Mycocerosic acid synthase-like polyketide synthase
- Phthioceranic/hydroxyphthioceranic acid synthase
- Mycoketide-CoA synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Conserved hypothetical Mce associated protein
- Putative peptidoglycan hydrolase Rv2525c
- Tetratrico peptide repeat group 5 domain-containing protein
Sequence:
MAIFGRGHGASEPGGTGEPAETPGRGRLTRSVIGWVGAVAVVVSLAGSGWCGWVLFEKHQTDVAAGQALQAARSYVVKLATMDCERIDHNMRDILEGSTGEFKDKYGKSSAHLRQLLADNRVATHGTVVAASVKSATTNKVVVLMFIDQSVSNRNSPTPQIDRSRIKVIMDKVNGRWLASKVELL
Protein: E3 ubiquitin-protein ligase BRE1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRE1) (Q5A4X0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q07457}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 2
- Cdc73p
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- RNA polymerase II-associated protein 1
- RNA polymerase-associated protein CTR9
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- RNA polymerase-associated protein LEO1
- Histone H2B.2
- Histone H2B.1
Sequence:
MAVDNEKKRSTPDSLNSPHAKKSKPMQELSESGPLTQADVVYFQKEAIWRQMIQYKQQMMSMRSELIRLQRESDASKHIVTVLTAWYEQILALFDELNSEETSDLLLAITKNDDEQLDLIRKKLSNLISSKVTFDSAKYEKVSGELALLSRQNEQMTEEKRSLGERIDELESKITELAKEHERAQSKTLKRLDSQRHIKTEEDEQSTTKEENPQPNGHHKENDKTAVVDSEELDNLKCELDKLKTANQLLVQQVEQLTKENQSLIQKSLNLENKLHNLEESDLEDNTYYKKIVKNNQSLQEQIGKLTKLNSSNVSRLNELERQQNDLKSVIEGEIIEENEKLKQQLQESENNLVRIRTTRDELLSKNNILTSQLQDQKTNESLVELNNVLSKRVESLTEERLEAIVGTPGTGKLEDLSQQELIHKISQLNNEIKEVELAFKQTREITLKKLTSSIDQENLTKKLTIEKNKADQKYFSAMRVKDSLTNENKLLKAQIAKSQDLIKNLNDLEKKYLNKIDLLSNQLVDFRIIKENSLAENSKLHDELKTLNIAQDALHQEVERVNAKLESTLKEHTDLQESNKKRELELAKLQKQLQSTENILQKYKTNNTNSLLQEDEQQLEALRSIAKCSVCSKNWKDTAITVCGHVFCSKCTQERLAARLRRCPSCNRGFSANDLLSIHL
Protein: Ras-related protein Rab-7b (Q96AH8)
Organism: Homo sapiens (Human)
Function: Controls vesicular trafficking from endosomes to the trans-Golgi network (TGN). Acts as a negative regulator of TLR9 signaling and can suppress TLR9-triggered TNFA, IL6, and IFNB production in macrophages by promoting TLR9 lysosomal degradation. Also negatively regulates TLR4 signaling in macrophages by promoting lysosomal degradation of TLR4. Promotes megakaryocytic differentiation by increasing NF-kappa-B-dependent IL6 production and subsequently enhancing the association of STAT3 with GATA1. Not involved in the regulation of the EGF- and EGFR degradation pathway.
Subcellular location: Late endosome {ECO:0000269|PubMed:20375062}. Lysosome {ECO:0000269|PubMed:15144907, ECO:0000269|PubMed:20375062}. Golgi apparatus {ECO:0000269|PubMed:20375062}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:20375062}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000269|PubMed:21255211}.
Interaction partners:
- Rab-interacting lysosomal protein
- TBC1 domain family member 15
- TBC1 domain family member 17
- Ras-related protein Rab-7a
- FYVE and coiled-coil domain-containing protein 1
- Geranylgeranyl transferase type-2 subunit alpha
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 16 homolog
Sequence:
MNPRKKVDLKLIIVGAIGVGKTSLLHQYVHKTFYEEYQTTLGASILSKIIILGDTTLKLQIWDTGGQERFRSMVSTFYKGSDGCILAFDVTDLESFEALDIWRGDVLAKIVPMEQSYPMVLLGNKIDLADRKVPQEVAQGWCREKDIPYFEVSAKNDINVVQAFEMLASRALSRYQSILENHLTESIKLSPDQSRSRCC
Protein: Asph protein (Q5U2Q8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004157}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004157}.
Interaction partners:
- Triadin
Sequence:
MAEDKEAKHGGHKNGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLEGPGGLAKRKTKAKVKEPTKEELKKEREKAVPSKTEEGRRGKKEREDGRKEKKKSDSDISQKASPGGKRDRAKEKASSDKSGKSKETVKKAAETKSVPSKVASTDKDRKGRGSSSHAPVTKENSQKRKN
Protein: Protocadherin alpha-4 (PCDH-alpha-4) (Q9UN74)
Organism: Homo sapiens (Human)
Function: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination. Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O88689}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O88689}. Note=Detected in dendrites and synapses. {ECO:0000250|UniProtKB:O88689}.
Interaction partners:
- Protocadherin alpha-7
- Protocadherin alpha-9
- Protocadherin alpha-11
Sequence:
MEFSWGSGQESRRLLLLLLLLAAWEAGNGQLHYSVSEEAKHGTFVGRIAQDLGLELAELVPRLFRVASKGRGGLLEVNLQNGILFVNSRIDREELCRRSAECSIHLEVIVDRPLQVFHVDVEVRDINDNPPVFPATQKNLSIAESRPLDSRFPLEGASDADIGENALLTYRLSPNEYFSLEKPPDDELVKGLGLILRKSLDREEAPEIFLVLTATDGGKPELTGTVQLLITVLDANDNAPAFDRTIYKVRLLENVPNGTLVIKLNASDLDEGLNGDIVYSFSNDISPNVKSKFHIDPITGQIIVKGYIDFEESKSYEIIVEGIDKGQLPLSGHCRVIVEVEDNNDNVPDLEFKSLSLPIREDAPLGTVIALISVSDKDMGVNGLVTCSLTSHVPFKLVSTFKNYYSLVLDSALDRESVSAYELVVTARDGGSPSLWATASVSVEVADVNDNAPAFAQPEYTVFVKENNPPGCHIFTVSAWDADAQENALVSYSLVERRVGERALSSYVSVHAESGKVYALQPLDHEELELLQFQVTARDAGVPPLGSNVTLQVFVLDENDNAPALLAPRAGGTGGAVSELVPWSVGVGHVVAKVRAVDADSGYNAWLSYELQPGTGGARIPFRVGLYTGEISTTRALDETDAPRHRLLVLVKDHGEPALTATATVLVSLVESGQAPKASSRALVGAVGPDAALVDVNVYLIIAICAVSSLLVLTLLLYTALRCSALPTEGACAPGKPTLVCSSAVGSWSYSQQRRPRVCSGEGPPKTDLMAFSPSLPDSRDREDQLQTTEESFAKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: Spn43Ac (Q6V6U8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FSSELFKEIIKSQSQQNVVFSPFSVHALLALIYGASDGKTFRELQKAGEFSKNAMAVAQDFESVIKYKKHLEGADLTLATKVYYNRELGGVNHSYDEYAKFYFSAGTEAVDMQNAKDTAAXINAWVMDTTRNKIRDLVTPTDVDPQTQALLVNAVYFQGRWEHEFATMDTSPYDFQHTNGRISKVAMMFNDXVYGLAXLPELGATALELAYKDSATSMLILLPNETTGLGKMLQQLSRPEFDLNRVAHRLRRQSVAVRLPKFQFEFEQDMTEPLKNLGVHQMFTPNSQVTKLMDQPVRVSKILQKAYINVGEAGTEASAASYAKFVPLSLPPKPTEFVANRPFVFAVRTPSSVLLI
Protein: Cytochrome c oxidase subunit 7C, mitochondrial (Cytochrome c oxidase polypeptide VIIc) (P15954)
Organism: Homo sapiens (Human)
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:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}.
Interaction partners:
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 6B1
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 6C
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MLGQSIRRFTTSVVRRSHYEEGPGKNLPFSVENKWSLLAKMCLYFGSAFATPFLVVRHQLLKT
Protein: BRCA1-associated RING domain protein 1 (BARD-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1) (O70445)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.
Subcellular location: Nucleus {ECO:0000269|PubMed:15077185}. Cytoplasm {ECO:0000269|PubMed:15077185}. Note=Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. {ECO:0000250|UniProtKB:Q99728}.
Interaction partners:
- BRCA1-A complex subunit Abraxas 1
- Breast cancer type 1 susceptibility protein homolog
- BRCA1-A complex subunit RAP80
- Fanconi anemia group J protein homolog
- DNA endonuclease RBBP8
- BRISC and BRCA1-A complex member 1
- Lys-63-specific deubiquitinase BRCC36
- Double-strand break repair protein MRE11
- Nibrin
- Breast cancer type 2 susceptibility protein homolog
Sequence:
MPRRPPRVCSGNQPAPVPAMEPATDGLWAHSRAALARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMIQLSSKLQNLLHDNKDSKDNTSRASLFGDAERKKNSIKMWFSPRSKKVRYVVTKVSVQTQPQKAKDDKAQEASMYEFVSATPPVAVPKSAKTASRTSAKKHPKKSVAKINREENLRPETKDSRFDSKEELKEEKVVSCSQIPVMERPRVNGEIDLLASGSVVEPECSGSLTEVSLPLAEHIVSPDTVSKNEETPEKKVCVKDLRSGGSNGNRKGCHRPTTSTSDSCGSNIPSTSRGIGEPALLAENVVLVDCSSLPSGQLQVDVTLRRKSNASDDPLSLSPGTPPPLLNNSTHRQMMSSPSTVKLSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHGASRNAVNIFGVRPVDYTDNENIRSLLLLPEENESFSTSQCSIVNTGQRKNGPLVFIGSGLSSQQQKMLSKLETVLKAKKCMEFDSTVTHVIVPDEEAQSTLKCMLGILSGCWILKFDWVKACLDSKVREQEEKYEVPGGPQRSRLNREQLLPKLFDGCYFFLGGNFKHHPRDDLLKLIAAAGGKVLSRKPKPDSDVTQTINTVAYHAKPESDQRFCTQYIVYEDLFNCHPERVRQGKVWMAPSTWLISCIMAFELLPLDS
Protein: ABC transporter B family member 25, mitochondrial (ABC transporter ABCB.25) (AtABCB25) (ABC transporter of the mitochondrion 3) (AtATM3) (Iron-sulfur clusters transporter ATM3) (Protein STARIK 1) (Q9LVM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins. Not required for mitochondrial and plastid Fe-S enzymes. Probably involved in the export of cyclic pyranopterin monophosphate (cPMP) from mitochondria into the cytosol. Mediates glutathione-dependent resistance to heavy metals such as cadmium and lead, as well as their transport from roots to leaves. Regulates nonprotein thiols (NPSH) and the cellular level of glutathione (GSH).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11158531, ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17517886}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:11158531, ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17517886}.
Interaction partners:
- Cytosolic Fe-S cluster assembly factor NBP35
- Protein NAR1
- MMS19 nucleotide excision repair protein homolog
- Protein AE7
- Iron-sulfur cluster assembly protein 1
- Cysteine desulfurase, mitochondrial
- Glutathione gamma-glutamylcysteinyltransferase 1
- Molybdopterin synthase catalytic subunit
- Cyclic pyranopterin monophosphate synthase, mitochondrial
- Iron-sulfur protein required for NADH dehydrogenase, mitochondrial
Sequence:
MSRGSRFVRAPGLLLCRVNLQPQPKIPSFSYSLRSDYRLHNGFSNYIRRNSIRTSPVINAFLSDNSPSPSPSPSPIRFVQRSSMLNGRLFSTSTPNPDQTTTKTKEIKTTSSDSDSAMADMKILRTLAGYLWMRDNPEFRFRVIAALGFLVGAKVLNVQVPFLFKLAVDWLASATGTGASLTTFAATNPTLLTVFATPAAVLIGYGIARTGSSAFNELRTAVFSKVALRTIRSVSRKVFSHLHDLDLRYHLSRETGGLNRIIDRGSRAINFILSAMVFNVVPTILEISMVSGILAYKFGAAFAWITSLSVGSYIVFTLAVTQWRTKFRKAMNKADNDASTRAIDSLINYETVKYFNNEGYEAEKYDQFLKKYEDAALQTQRSLAFLNFGQSIIFSTALSTAMVLCSQGIMNGQMTVGDLVMVNGLLFQLSLPLNFLGSVYRETIQSLVDMKSMFQLLEEKSDITNTSDAKPLVLKGGNIEFENVHFSYLPERKILDGISFVVPAGKSVAIVGTSGSGKSTILRMLFRFFDTDSGNIRIDGQDIKEVRLDSLRSSIGVVPQDTVLFNDTIFHNIHYGRLSATEEEVYEAARRAAIHETISNFPDKYSTIVGERGLKLSGGEKQRVALARTFLKSPAILLCDEATSALDSTTEAEILNALKALASNRTSIFIAHRLTTAMQCDEIVVLENGKVVEQGPHDELLGKSGRYAQLWTQQNSSVDMLDAAIKLE