wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane protease serine 6 (EC 3.4.21.-) (Matriptase-2) (Q8IU80)
Organism: Homo sapiens (Human)
Function: Membrane-bound serine protease. Through the cleavage of cell surface HJV, a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18976966, ECO:0000269|PubMed:20518742, ECO:0000269|PubMed:25588876}; Single-pass type II membrane protein {ECO:0000269|PubMed:20518742}. Note=The processed, activated two-chains form is released in the extracellular space. {ECO:0000269|PubMed:25156943}.
Interaction partners:
- Hemojuvelin
- Hepcidin
- Neogenin
- Hereditary hemochromatosis protein
- Transferrin receptor protein 2
- Bone morphogenetic protein 6
- Transferrin receptor protein 1
- Decorin
- Erythropoietin
- Cyclic AMP-responsive element-binding protein 3-like protein 3
Sequence:
MLLLFHSKRMPVAEAPQVAGGQGDGGDGEEAEPEGMFKACEDSKRKARGYLRLVPLFVLLALLVLASAGVLLWYFLGYKAEVMVSQVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELITSTRLGTYYNSSSVYSFGEGPLTCFFWFILQIPEHRRLMLSPEVVQALLVEELLSTVNSSAAVPYRAEYEVDPEGLVILEASVKDIAALNSTLGCYRYSYVGQGQVLRLKGPDHLASSCLWHLQGPKDLMLKLRLEWTLAECRDRLAMYDVAGPLEKRLITSVYGCSRQEPVVEVLASGAIMAVVWKKGLHSYYDPFVLSVQPVVFQACEVNLTLDNRLDSQGVLSTPYFPSYYSPQTHCSWHLTVPSLDYGLALWFDAYALRRQKYDLPCTQGQWTIQNRRLCGLRILQPYAERIPVVATAGITINFTSQISLTGPGVRVHYGLYNQSDPCPGEFLCSVNGLCVPACDGVKDCPNGLDERNCVCRATFQCKEDSTCISLPKVCDGQPDCLNGSDEEQCQEGVPCGTFTFQCEDRSCVKKPNPQCDGRPDCRDGSDEEHCDCGLQGPSSRIVGGAVSSEGEWPWQASLQVRGRHICGGALIADRWVITAAHCFQEDSMASTVLWTVFLGKVWQNSRWPGEVSFKVSRLLLHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPISNALQKVDVQLIPQDLCSEVYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVCKALSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVISWIQQVVT
Protein: Chaperonin (Q877H2)
Organism: Acidianus tengchongensis
Interaction partners:
Sequence:
MASTATVATTPEGIPVIILKEGSSRTYGKEAVRANIAAVKAVEEALKSTYGPRGMDKMLVDSLGDITITNDGATILDKMDLQHPAAKLLVQIAKGQDEETADGTKTAVIFSGELVKKAEDLLYKDVHPTIIISGYKKAEEVALQTIQELAQTVSINDTDLLRKIAMTSLSSKAVAGAREYIADIVVKAVTQVAELRGDKWYVDLDNIQIVKKAGGSINDTQLVYGIVVDKEVVHPGMPKRLENAKIALIDASLEVEKPELDAEIRINDPTQMQKFLDEEENLIKEKVDKILATGANVIICQKGIDEVAQSYLAKKGVLAVRRAKKSDLEKLARATGGRVVSNIDEISEQDLGYASLIEERKVGEDKMVFVEGAKNPKSISILIRGGLERLVDETERALRDALGTVADVIKDGRAIAGGGAVEIEIAKKLRKYAPQVGGKEQLAVEAYANALESLVSILIENAGFDPIDLLMKLRSTHENENNKWYGIDLYAGQPVDMWQKGVIEPALVKMNAIKAATEAATLVLRIDDVVSAGKKSGGESKTPGGANKPSEED
Protein: D-allulose-6-phosphate 3-epimerase (EC 5.1.3.-) (P32719)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible epimerization of D-allulose 6-phosphate to D-fructose 6-phosphate. Can also catalyze with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Interaction partners:
- D-allose kinase
- D-allose transport system permease protein AlsC
- D-allose import ATP-binding protein AlsA
- Ribose-5-phosphate isomerase B
- D-allose-binding periplasmic protein
- Mannose-6-phosphate isomerase
- Fructose-1,6-bisphosphatase class 1
- Sorbitol-6-phosphate 2-dehydrogenase
- ATP-dependent 6-phosphofructokinase isozyme 1
- Fructose-1,6-bisphosphatase 2 class 2
Sequence:
MKISPSLMCMDLLKFKEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAGADFITLHPETINGQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAWREREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGTSGLFNHAENIDEAWRIMTAQILAAKSEVQPHAKTA
Protein: Zinc metalloproteinase-disintegrin-like uracoina-1 (EC 3.4.24.-) (Snake venom metalloprotease) (SVMP) (C0HL97)
Organism: Crotalus vegrandis (Uracoan rattlesnake) (Crotalus durissus vegrandis)
Function: Snake venom zinc metalloprotease that possesses hemorrhagic activity (minimum hemorrhagic dose, MHD=4.7 ug) when injected intradermally into mice. Degrades the alpha-chain of fibrinogen (FGA).
Subcellular location: Secreted {ECO:0000269|PubMed:11451438}.
Interaction partners:
Sequence:
HQKYNPFRFVELVLVVDKAM
Protein: 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 (AtHMGR2) (HMG-CoA reductase 2) (EC 1.1.1.34) (P43256)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of mevalonate. The specific precursor of all isoprenoid compounds present in plants.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8302869}; Multi-pass membrane protein {ECO:0000269|PubMed:8302869}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- Mevalonate kinase
- 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
- Phosphomevalonate kinase, peroxisomal
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Acetyl-CoA acetyltransferase 2
- Acetyl-CoA acetyltransferase 1
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase, chloroplastic
Sequence:
MEDLRRRFPTKKNGEEISNVAVDPPLRKASDALPLPLYLTNTFFLSLFFATVYFLLSRWREKIRNSTPLHVVDLSEICALIGFVASFIYLLGFCGIDLIFRSSSDDDVWVNDGMIPCNQSLDCREVLPIKPNSVDPPRESELDSVEDEEIVKLVIDGTIPSYSLETKLGDCKRAAAIRREAVQRITGKSLTGLPLEGFDYNSILGQCCEMPVGYVQIPVGIAGPLLLDGVEYSVPMATTEGCLVASTNRGFKAIHLSGGAFSVLVKDAMTRAPVVRFPSARRAALVMFYLQDPSNFERLSLIFNKSSRFARLQSITCTIAGRNLYPRFACSTGDAMGMNMVSKGVQNVLDFVKSEFPDMDVIGISGNYCSDKKASAVNWIEGRGKHVVCEAFIKAEIVEKVLKTSVEALVELNTLKNLVGSAMAGSLGGFNAHSSNIVSAVFIATGQDPAQNVESSHCMTMILPDGDDLHISVSMPCIEVGTVGGGTQLASQAACLNLLGVKGSNNEKPGSNAQQLARIVAGSVLAGELSLMSAIAAGQLVKSHMKYNRSSRDIGPSSQVNR
Protein: Zinc finger protein 84 (Zinc finger protein HPF2) (P51523)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MTMLQESFSFDDLSVDFTQKEWQLLDPSQKNLYKDVMLENYSSLVSLGYEVMKPDVIFKLEQGEEPWVGDGEIPSSDSPEVWKVDGNMMWHQDNQDKLKIIKRGHECDAFGKNFNLNMNFVPLRKSNSEGDLDGLILKHHLDLLIPKGDYGKAESDDFNVFDNFFLHSKPEDTDTWLKYYDCDKYKESYKKSQIIIYHRNRLGEKLYECSECRKRFSKKPSLIKHQSRHIRDIAFGCGNCGKTFPQKSQFITHHRTHTGEKPYNCSQCGKAFSQKSQLTSHQRTHTGEKPYECGECGKAFSRKSHLISHWRTHTGEKPYGCNECGRAFSEKSNLINHQRIHTGEKPFECRECGKAFSRKSQLVTHHRTHTGTKPFGCSDCRKAFFEKSELIRHQTIHTGEKPYECSECRKAFRERSSLINHQRTHTGEKPHGCIQCGKAFSQKSHLISHQMTHTGEKPFICSKCGKAFSRKSQLVRHQRTHTGEKPYECSECGKAFSEKLSLTNHQRIHTGEKPYVCSECGKAFCQKSHLISHQRTHTGEKPYECSECGKAFGEKSSLATHQRTHTGEKPYECRDCEKAFSQKSQLNTHQRIHTGEKPYECSLCRKAFFEKSELIRHLRTHTGEKPYECNECRKAFREKSSLINHQRIHTGEKPFECSECGKAFSRKSHLIPHQRTHTGEKPYGCSECRKAFSQKSQLVNHQRIHTGEKPYRCIECGKAFSQKSQLINHQRTHTVKKS
Protein: Glutamate-gated chloride channel subunit (Ig-like domain-containing protein) (G5EEZ3)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Probable vesicular glutamate transporter eat-4
Sequence:
MSLRSLLNILLIVAFWIVGGNCDASSDTEIIKKLLGKGYDWRVRPPGINLTIPGTHGAVIVYVNMLIRSISKIDDVNMEYSVQLTFREEWVDGRLAYGFPGDSTPDFLILTAGQQIWMPDSFFQNEKQAHKHDIDKPNVLIRIHRDGRILYSVRISMVLSCPMHLQYYPMDVQTCLIDLASYAYTENDIEYRWKKTDPVQLKKGLHSSLPSFELNNVDTTLCTSKTNTGTYSCLRTVLELRRQFSYYLLQLYIPSTMLVIVSWVSFWLDRGAVPARVTLGVTTLLTMTTQASGINAKLPPVSYTKAIDVWIGACLTFIFGALLEFAWVTYISSRSFYKRNKNCSSRNSLLIETKQALIIPNTVVAQFPEHPEEVEMGLAQAPDVWIRQSGNGKTVSRVNGHINHNNDEAAELIIFDAKHKNRRFVWWTNFRNIRLIRWIRNRLNVDDNAKRADLISRVLFPTLFVCFNFVYWTKYSQYHAPEAK
Protein: Nuclear pore complex protein NUP50A (Nucleoporin 50A) (Q9C829)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in nucleocytoplasmic transport via its interactions with importins and Ran, rather than by forming part of the nuclear pore complex (NPC) scaffolding.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Protein SEH1
- Nuclear pore complex protein NUP155
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP93A
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP205
- GTP-binding nuclear protein Ran-1
- RAN GTPase-activating protein 1
Sequence:
MGDSENVQQPSKKRGALKQLSRDNPGLDDDDDSAELESGTFKKASDEVLASRRIVRVKRKEPSAAPVAASNPFAGIQLVPTTAPASTPVGTNAPLAESKLAPAEAVVEDNQKASDIEEGDEVDSKKVDVKDAVGEETEKTKDKDDNHCGKSADVQVAATEVAQMVSCDTNVCNNAVEGTDQTDFPLEKDSGGDQAEKKEKEGNGIEEADKNGDNGAFSSFQQHSSNKNAFTGLASTEASGSSFSFGLVSQDGSTGTGSLFGFGLPSSNSSSIFGATGSSIIKKSEGSGFPPKQEVSTETGEENEKVAFSADSIMFEYLDGGWKERGKGELKVNVSSNDGKARLVMRAKGNYRLILNASLYPEMKLANMDKKGITFACVNSVSEGKEGLSTFALKFKDPTIVEEFRVAIDKHKDSKPMEKAAEKSALPLKTPENSPTATDT
Protein: Transcription factor bHLH71 (Basic helix-loop-helix protein 71) (AtbHLH71) (bHLH 71) (Transcription factor EN 17) (bHLH transcription factor bHLH071) (Q56XR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. May be involved in the differentiation of stomatal guard cells.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor bHLH168
- Transcription factor bHLH110
- Receptor-like protein 35
Sequence:
MTLEALSSNGLLNFLLSETLSPTPFKSLVDLEPLPENDVIISKNTISEISNQEPPPQRQPPATNRGKKRRRRKPRVCKNEEEAENQRMTHIAVERNRRRQMNQHLSVLRSLMPQPFAHKGDQASIVGGAIDFIKELEHKLLSLEAQKHHNAKLNQSVTSSTSQDSNGEQENPHQPSSLSLSQFFLHSYDPSQENRNGSTSSVKTPMEDLEVTLIETHANIRILSRRRGFRWSTLATTKPPQLSKLVASLQSLSLSILHLSVTTLDNYAIYSISAKVEESCQLSSVDDIAGAVHHMLSIIEEEPFCCSSMSELPFDFSLNHSNVTHSL
Protein: Bifunctional coenzyme A synthase (CoA synthase) (NBP) (POV-2) [Includes: Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT); Dephospho-CoA kinase (DPCK) (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (DPCOAK)] (Q8MIR4)
Organism: Sus scrofa (Pig)
Function: Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13057}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q13057}. Note=The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but this protein is also present in cell lysate. {ECO:0000250|UniProtKB:Q13057}.
Interaction partners:
- Phosphopantothenate--cysteine ligase
- Phosphopantothenoylcysteine decarboxylase.
- Coiled-coil domain containing 30
- Cytochrome c oxidase assembly protein COX19
- Dephospho-CoA kinase domain-containing protein
- Adenylosuccinate lyase
- 4'-phosphopantetheine phosphatase
- Ribonucleoside-diphosphate reductase
- Pantothenate kinase 3
- MAX dimerization protein MLX.
Sequence:
MAVFRSGLLVLTTPLASLVPRLAPILTSAARLVNHTLYVHLQPGMNLGGPAQPQSSPVQATFEVIDFITHLYAGADLHRHLDVRILLTNIRTKSFLPPLPSSVQNLAHPPEVVLTDFQTLDGSQYNPVKQQLERYATSCYSCCPQLSSVLLYPDYGPGMLPVQPLDVPLPSTIRPASPVARSAKQPVRGHQRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLSFDLIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAVNRFRLENGLEELTLYQIQLLKDLNPKENEEDKVSSSSFRQQMLGNLLRPPHKRPELPPGCYVIGLTGISGSGKSSVAQRLKGLGAYVIDSDQLGHRSYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQLKILTDIVWPVIAKLAREEVDQAVAEGKRVCVIDAAVLLEAGWQNMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQMSGQQLVDQSHVVLSTLWEPHVTQRQVEKAWALLQKRISEAPSDP
Protein: FI04035p (Rho GTPase activating protein at 93B) (Q9VDE9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Roundabout 1, isoform A
- LP22668p
- FI17823p1
- Roundabout 2, isoform B
- Rho GTPase activating protein at 71E, isoform D
- Rho GTPase activating protein at 16F, isoform E
Sequence:
MSSSCERIEWVEIIEPRTKEHMYANLTTGECVWDPPEDVPIKRTDSSQWWELFDTNTQRFYYYNAATQKTVWHRPSKCDIIPLAKLQTLKQNTDPSERREQTTPQKQQQQQVQHASQQQQHPSPMSGPNKKGRGQQRISGGNGTVASSEEKLTSSEVISSPRGRQSFRVSTGDSSRSMDMQQQHPQGYASRRSQDSCNQYKESGKSSDSSLSSAHGYRRFNDSGVPVSGHPDNLRLGSLQKQQRGGGKDNGAFEMLQESTSSHNLPHGSTSTSSSYAGGSGYGDKYFDHQLLPNHLQGYSSKSSDIASPTHSIHTPQSQKKKMSPDAAPAAQYNYAQQQHQQRSAQRSGGGAAGTGAPAGKSYGGDREYKVSLARSGSFMSSSINPAAAGHHSKSYRKSSAEAANGGAASDDSMHEKYFKSVENTPLSRRRHTTNATKSGGGASGSNTATSTAGSGSSSHKKHSSDSSPQSPISPQTKSSRQAKTSATSTVPQLQHSPRLQEPSHSLDLLSLERISLGKSGPISPGGGTENLGLLTHSSRGSNDSARQRQKSNNSSANRSQSHHYPGQSSLRHSASSSLDKRGYHVGGGSGDGRGVTGGEKRRSKQHHYQQQADNSDVEYDNGNTSPLYTNWDQEMPHLLPLKHYIIEQAKLSGRYEYRGGDGGDSDSYHSDSQSEHSLSGHEPDNEDSDGGSDTHGGYLEHNYGMIDDYANMGDSVSYYAYMYPPHDPAGREDISENVEAVLEGIGGNATEPSAPTATAPKPKPRYQISYYDTVSHSPSAGSGYHGQQLYSNTPPYSGHGHGHHVPPPSLPHQQQLHLEPSDTKQKQSQTLPSPNRQISRLAGAGHQGSGPAASSKEETGHSTVAGQQQVTVGTVTPASLSRPGHKMAPPSLKPTIQQIFPPSERAPGMGNLGLGGPTLACMKECDIEKFAADNLNLHSKGIFRKKASVRDMLSWTAEAISRPMLALSRDKADKKTAIELFKLVQIYMADRKARIGMTLNSVAIEIISASLPQQQLRDELYVQLCRQTTENPKRDSLIRGWELMAICLSYVPPSPTFQPTLLNYVNRHRDPSFATCFMEVSKWPIHVQISHYATVCCRRLDRIGSSGRRMAKKPTVDEVEQARQQILRNSMFGNTLSEVMDLQKEKFPFRKLPWIQTTLSEHVLLLNGKQTEGIFRVSADVDEVGCMKNRLDRWDVPDYKNTLVDAHTPASLLKLWYRELYDPLIPDAYYEDCVNTEDPDKAKEIVNKLPEINQLVLTYLIHFLQQFAIPEVVSCTKMDSSNLAMVFAPNCLRCTSEDPKVILENARKEMSFMRTLIQHMDTTHVANLV
Protein: RNA-binding protein FXR1 (FMR1 autosomal homolog 1) (hFXR1p) (P51114)
Organism: Homo sapiens (Human)
Function: RNA-binding protein required for embryonic and postnatal development of muscle tissue. May regulate intracellular transport and local translation of certain mRNAs (By similarity).
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:32706158, ECO:0000269|PubMed:39106863}. Cytoplasm, Stress granule {ECO:0000269|PubMed:20417602}. Cytoplasm {ECO:0000269|PubMed:30770808, ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:9259278}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61584}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q61584}. Cell projection, axon {ECO:0000250|UniProtKB:Q61584}. Nucleus envelope {ECO:0000269|PubMed:32706158}. Postsynapse {ECO:0000250|UniProtKB:Q61584}. Note=Specifically localizes to cytoplasmic ribonucleoprotein membraneless compartments (By similarity). Localizes to stress granules following phosphorylation at Ser-420 by PAK1 (PubMed:20417602). Adjacent to Z-lines in muscles (By similarity). {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:20417602}.
Interaction partners:
- Cytoplasmic FMR1-interacting protein 1
- Cytoplasmic FMR1-interacting protein 2
- RNA-binding protein FXR2
- Protein argonaute-2
- Fragile X messenger ribonucleoprotein 1
- FMR1-interacting protein NUFIP1
- Endoribonuclease Dicer
- Ras GTPase-activating protein-binding protein 1
- Plakophilin-3
- Heterogeneous nuclear ribonucleoprotein K
Sequence:
MAELTVEVRGSNGAFYKGFIKDVHEDSLTVVFENNWQPERQVPFNEVRLPPPPDIKKEISEGDEVEVYSRANDQEPCGWWLAKVRMMKGEFYVIEYAACDATYNEIVTFERLRPVNQNKTVKKNTFFKCTVDVPEDLREACANENAHKDFKKAVGACRIFYHPETTQLMILSASEATVKRVNILSDMHLRSIRTKLMLMSRNEEATKHLECTKQLAAAFHEEFVVREDLMGLAIGTHGSNIQQARKVPGVTAIELDEDTGTFRIYGESADAVKKARGFLEFVEDFIQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNENKLPREDGMVPFVFVGTKESIGNVQVLLEYHIAYLKEVEQLRMERLQIDEQLRQIGSRSYSGRGRGRRGPNYTSGYGTNSELSNPSETESERKDELSDWSLAGEDDRDSRHQRDSRRRPGGRGRSVSGGRGRGGPRGGKSSISSVLKDPDSNPYSLLDNTESDQTADTDASESHHSTNRRRRSRRRRTDEDAVLMDGMTESDTASVNENGLVTVADYISRAESQSRQRNLPRETLAKNKKEMAKDVIEEHGPSEKAINGPTSASGDDISKLQRTPGEEKINTLKEENTQEAAVLNGVS
Protein: Cytochrome c oxidase assembly protein COX18, mitochondrial (Cytochrome c oxidase assembly protein 18) (P53239)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome c oxidase. Plays a central role in the translocation and export of the C-terminal part of the COX2 protein into the mitochondrial intermembrane space.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10809734}; Multi-pass membrane protein {ECO:0000269|PubMed:10809734}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Protein MSS2
- Pentamidine resistance factor
- Mitochondrial inner membrane protein OXA1
- Cytochrome c oxidase assembly factor 6
- Inner membrane mitoribosome receptor MBA1, mitochondrial
- Protein SCO2
- Protein transport protein SEC61
- Sec sixty-one protein homolog
- Cytochrome c oxidase assembly protein COX11
Sequence:
MLKRLANRQNGFASFSCSSVGLRYGRTNPSTKRSFSLFQSVADTFLTVHEASHIPWIVLVPLTTMTLRTLVTLPFSIWQRRRILKQQELRKLVQPITPIIKLRLAAVTNKKSRNAARISSNGSFMPLQLQNAGVLTPEQITLLAVKETRKRQKKLFKKYNVPLWKNALLPMVQIPLWVTVSMGIRTLTETQLIESFYPSWFSALGFSSFDLSSPLVAMPLLAPILVGTLAVLNVELNGRLMFSSSLSSQGIKTISRNSTRVQEAMTSILNVSRLGCVVMLAMSSQAPFLLSLYWISSQLFSLVQNIILNWIYPYQR
Protein: Histone-lysine N-methyltransferase met-2 (EC 2.1.1.-) (EC 2.1.1.367) (P34544)
Organism: Caenorhabditis elegans
Function: Histone methyltransferase which is required for the mono- and dimethylation of 'Lys-9' of histone H3. This increases the efficiency of set-25-mediated trimethylation of histone H3 'Lys-9'. Involved in the transcriptional repression of lin-3 which is required for the negative regulation of vulval cell fate specification during postembryonic development. Has a role in blocking checkpoint signaling and mediating the transcriptional silencing of meiotic sex chromosome inactivation; a mechanism which enables checkpoint proteins to distinguish between the partnerless male X chromosome and asynapsed chromosomes thereby shielding the lone X from inappropriate activation of an apoptotic program. Operates redundantly with set-25 to position chromatin at the nuclear periphery. Required for small-RNA-induced H3K9 methylation. Together with set-25, protects and stabilizes repeat-rich genomic regions by suppressing transcription-induced replication stress through methylation of H3K9. Together with spr-5, required for transgenerational fertility.
Subcellular location: Nucleus {ECO:0000269|PubMed:22939621}. Chromosome {ECO:0000305|PubMed:22939621}. Cytoplasm {ECO:0000269|PubMed:22939621}.
Interaction partners:
- ARF7 effector protein C-terminal domain-containing protein
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase
Sequence:
MDQQEPSNNVDTSSILSDDGMETQEQSSFVTATIDLTVDDYDETEIQEILDNGKAEEGTDEDSDLVEGILNANSDVQALLDAPSEQVAQALNSFFGNESEQEAVAAQRRVDAEKTAKDEAELKQQEEAEDLIIEDSIVKTDEEKQAVRRLKINEFLSWFTRLLPEQFKNFEFTNPNYLTESISDSPVVNVDKCKEIVKSFKESESLEGLSQKYELIDEDVLVAAICIGVLDTNNEEDVDFNVLCDDRIDDWSIEKCVTFLDYPNTGLNSKNGPLRFMQFTVTSPASAILMLTLIRLREEGHPCRLDFDSNPTDDLLLNFDQVEFSNNIIDTAVKYWDDQKENGAQDKIGRELNDFFHEIESTSAEFKQHFENAVGSRNEIIQLVNEKIPDFDGTEAAVNESFTSDQRTEIINSRAIMETLKAEMKLAIAEAQKVYDTKTDFEKFFVLTVGDFCLARANPSDDAELTYAIVQDRVDAMTYKVKFIDTSQIRECNIRDLAMTTQGMYDPSLNTFGDVGLRVACRQVISSSQFGKKTIWLTGTAAGRRRAHRSDFLIFFDNGTDAYVSAPTMPGEPGYEVASEKKSVFSLKEMIAKMNAAQIAIMVGQPVGKEGNLDYFLTFHWIRQSHRSAYIRDFMKEFPEWPLLKMPVGMRICLYNSLVDRRKKMVTVIGTDRAFAIVRHEAPNPLAPGNRCTDFPCNDRNHQHIDEKIYRGSHRLEGAAHKKHMISTNNNLSQRRKDQLQSQFEPTDMIRSMPERNHQQVVKKKTTGTNQNVASTNDAKSKREIEIRKKNQFLFNKIIVPIPVLTPLENLKAHAQCGPDCLQKMDADPYEARFHRNSPIHTPLLCGWRRIMYTMSTGKKRGAVKKNIIYFSPCGAALHQISDVSEYIHVTRSLLTIDCFSFDARIDTATYITVDDKYLKVADFSLGTEGIPIPLVNSVDNDEPPSLEYSKRRFQYNDQVDISSVSRDFCSGCSCDGDCSDASKCECQQLSIEAMKRLPHNLQFDGHDELVPHYQNRLLSSKVISGLYECNDQCSCHRKSCYNRVVQNNIKYPMHIFKTAQSGWGVRALTDIPQSTFICTYVGAILTDDLADELRNADQYFADLDLKDTVELEKGREDHETDFGYGGDESDYDDEEGSDGDSGDDVMNKMVKRQDSSESGEETKRLTRQKRKQSKKSGKGGSVEKDDTTPRDSMEKDNIESKDEPVFNWDKYFEPFPLYVIDAKQRGNLGRFLNHSCDPNVHVQHVMYDTHDLRLPWVAFFTRKYVKAGDELTWDYQYTQDQTATTQLTCHCGAENCTGRLLKS
Protein: Mitochondrial import receptor subunit TOM22 homolog (hTom22) (1C9-2) (Translocase of outer membrane 22 kDa subunit homolog) (Q9NS69)
Organism: Homo sapiens (Human)
Function: Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore. Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:10982837}; Single-pass membrane protein {ECO:0000269|PubMed:10982837}.
Interaction partners:
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM7 homolog
- Mitochondrial import receptor subunit TOM5 homolog
- Mitochondrial import receptor subunit TOM20 homolog
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import receptor subunit TOM6 homolog
- Sorting and assembly machinery component 50 homolog
- Mitochondrial import receptor subunit TOM40B
- Mitochondrial import inner membrane translocase subunit Tim21
- Mitochondrial import inner membrane translocase subunit Tim23
Sequence:
MAAAVAAAGAGEPQSPDELLPKGDAEKPEEELEEDDDEELDETLSERLWGLTEMFPERVRSAAGATFDLSLFVAQKMYRFSRAALWIGTTSFMILVLPVVFETEKLQMEQQQQLQQRQILLGPNTGLSGGMPGALPSLPGKI
Protein: Importin subunit alpha-5 (Importin alpha-5) (Karyopherin subunit alpha-1) (P83953)
Organism: Rattus norvegicus (Rat)
Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P52294}. Nucleus {ECO:0000250|UniProtKB:P52294}.
Interaction partners:
- Importin subunit beta-1
- Signal transducer and activator of transcription 1
- Exportin-2
- Importin subunit alpha
- Importin subunit alpha
- Transcription factor p65
- Nuclear factor NF-kappa-B p105 subunit
- GTP-binding nuclear protein Ran
- Importin-13
- Nuclear pore complex protein Nup50
Sequence:
MSTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQINNMEMAPGGVITSDMTEMIFSNSPEQQLSATQKFRKLLSKEPNPPIDEVINTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLDCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSPPPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNITAGNRAQIQTVIDANMFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCIKPLCDLLTVMDAKIVQVALNGLENILRLGEQEAKRNGSGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGTEDEDSSIAPQVDLSQQQYIFQQCEAPMEGSQL