wanglab/gogpt-training-data huggingface dataset:
Protein: DNA repair and recombination protein RAD52 (Q59NG2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- DNA repair protein RAD51 homolog
- Replication protein A subunit
- DNA 3'-5' helicase
- Crossover junction endonuclease MUS81
- DNA-dependent ATPase
- Rfa2p
- DNA-dependent ATPase
- DNA ligase 4
- Serine/threonine-protein kinase MEC1
- DNA repair and recombination protein RAD52
Sequence:
MNSRPAPPQPRPPQQQPQQPQQPQPNQQRLPFRPDESRARRLNQPLEQHANPINPSNFAAREYTEQEHKDIQTKLNKSLGPEFISYRDGPGGTRVQYIEGWKILNLANEIFGFNGWNSQIVSCQVDFLDTHGGSGKFSVGISMVVRITIRDGTFHEDVGYGSIENCRSKILALERCKKEALTDGLKRCLRCFGNVLGNCLYDKTIVAQMKKLKKFPIEFDPNDYYRDPLLVERERKKNIIEKQHEEQKRQQEDASRLDNSGQQVQHQQQNNSNVVSNGSIPVNGQQNHQNKGSDIVEPLEANQGNTRAGQVPQLSHHAAAFVTPKSPTKVVSYVPTSKEAEELDDSFMFSDDIFDGESQSIYYPPEVREHEQNQQQQKEENQGVARNGATKETTNNGRSENRPQNESMAVDQNPPVLMNAFVTAKSAEVLQQSPTVEAAAKNIVQFDPKFVSPNMRRTVDPTKSVPIKRSDIKNSVATTPSPLGVNTSSNRINKPMITSNNNNNINNMGKRIGMPPQPRTNKLVNSGNNPSSGIPHTVSTSVNGASGNENVENNSTIANTTVNQ
Protein: 3-ketoacyl-CoA thiolase A, peroxisomal (EC 2.3.1.16) (Acetyl-CoA C-myristoyltransferase) (EC 2.3.1.155) (Acetyl-CoA acyltransferase A) (EC 2.3.1.9) (Beta-ketothiolase A) (Peroxisomal 3-oxoacyl-CoA thiolase A) (Thiolase A) (P21775)
Organism: Rattus norvegicus (Rat)
Function: Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs). Plays an important role in fatty acid peroxisomal beta-oxidation. Catalyzes the cleavage of short, medium, long, and very long straight chain 3-oxoacyl-CoAs. Medium chain straight 3-oxoacyl-CoAs are preferred substrates.
Subcellular location: Peroxisome {ECO:0000269|PubMed:1680677, ECO:0000269|PubMed:2210380, ECO:0000269|PubMed:9325339}. Note=Transported into peroxisomes following association with PEX7. {ECO:0000250|UniProtKB:P09110}.
Interaction partners:
- Peroxisomal targeting signal 2 receptor
- Enoyl-CoA delta isomerase 2
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal acyl-coenzyme A oxidase 2
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
Sequence:
MSESVGRTSAMHRLQVVLGHLAGRPESSSALQAAPCSATFPQASASDVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSNRGNPGNISSRLLESDKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQALYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN
Protein: Sin3A-associated protein 130, isoform B (Sin3A-associated protein 130, isoform E) (Q8IQH9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSAPSEGGAGGGPVGGGSTATAPSATGSLSASASLVSHSHPPLQLRGVINKYSLPSHLPSSAAHPAVAAKITHVKSDGGGGISIAGTPILSGGTIKVASANQVQQTSLGGTPIALNAGQATTAASIRAIGAGGQSTQVRVVMPMIKQLENVTATGRTQITAIPAAPARSGANASITVTRPVTQATYLPRASVTATQMGGVGVGVGQRLVTPLRATSSATVTPTAPTVLSSTGGFVRGATASVSRSGVALTSQPSSAVISSSNSGAWMQSQGQVQLIRTIHQPRQRIITTSAGVSNASVVTTTPVQAPTALSVSAGQPLATQQATGPGGGPQAYVATVLPQRQHQATLVYSSNVSAPNASQNPGQQFNPRFAVATPTGGVTTTTPGGTTVTPRQVRPIPLGKSFPTAKLNTTSISIRAPSIPQLNTSVTASPTAVSVSGGATVAPGRGPGAGGTALTATNLPTTRIIQLQQPATGTTQQIIGSGARLAGNVMLQPFLMSTTAAAKMGIRPPVTMTAKVQPSLTITQLNPIGKLSAGGGSGGQTMGPQGVASIQAVPVPNVSASVVNSSSVTGATSAAGGATVLPLTISGRGAGVGPGGNILTGTLTPIKNASGITLGKMMMAPASSAPGADGSSTSGATVTGFQRTWNPVVASQSQLMKIDEKGSAATIYYESMPASASTGVLSLTTTTVTQSTQAQAQLVSSAGGSLSVSSLPFASHATAGAGSGGGGSQATFTVLPSGAGGTATRTIGHQQLIIPAGPNSAPPQHMVIPLHTSVKVTTGAGNPQQATASGALVSSFMRKRDAEGSPIRAAKNLGPTLLSMASNNSGQNMPPAPGTTFNIQPVSVTVPQSVGSGLTVEALAKKERERVTHGVASSAASVPATVGPVNSTRNSRADSPASSDGSTTVSANSSPGVDQQLQDRIGDQPATGGAGGRDNSTHFNPINEMYSSHQSIQQNLGHSSLGARSGSSAFVDVQAPTPQQQQPQQVPHLVGSTQMQQGTRMNGTGNSSSSSYDCSSRKKPRRSTNDSQHSTQSQASLSLPPPSSEPTPPAGASYMQKHNNGGLLVTAATPGVAPNSAPGDANHRNSTPAVAGNKENANPVDFVIRRPRNCALLNTYKPTHKLANNHFHRYTDVKPREERRATVIDLANQPNVQGKINGWKIYHLRSQMEDLNESEVFSLGRLETMLQDLEKDKEKHSEIERVTELLKGNIQRSKIITDGINEAQNQLMKIFEHKPHVSNIITRCASKRNFKKREKI
Protein: Integral membrane protein 2 (A0A3B3IUC0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}. Endosome membrane {ECO:0000256|ARBA:ARBA00004639}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004639}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}. Membrane {ECO:0000256|RuleBase:RU367061}; Single-pass type II membrane protein {ECO:0000256|RuleBase:RU367061}.
Interaction partners:
Sequence:
MCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGIKYIKDDVILNEPSADAPAALYQTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKLQRRETIKGIQKREASNCFAIRHFENKFAVETLICS
Protein: Zinc finger and BTB domain-containing protein 2 (Q8N680)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Required for meiotic nuclear division protein 1 homolog
- Zinc finger protein 639
- Zinc finger protein 219
Sequence:
MDLANHGLILLQQLNAQREFGFLCDCTVAIGDVYFKAHKSVLASFSNYFKMLFVHQTSECVRLKPTDIQPDIFSYLLHLMYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASQGAFSHPDQVFPLASSLYGIQIADHQLRQATKIASAPEKLGRDPRPQTSRISQEQVPEASQLSQLTSNLAQVNRTNMTPSDPLQTSLSPELVSTPVPPPPPGEETNLEASSSDEQPASLTIAHVKPSIMKRNGSFPKYYACHLCGRRFTLRSSLREHLQIHTGVPFTSSQQGESRVPLTLCSNAADLGKDAMEVPEAGMISDSELQHISDSPIIDGQQQSETPPPSDIADIDNLEQADQEREVKRRKYECTICGRKFIQKSHWREHMYIHTGKPFKCSTCDKSFCRANQAARHVCLNQSIDTYTMVDKQTLELCTFEEGSQMDNMLVQTNKPYKCNLCDKTFSTPNEVVKHSCQNQNSDVFALDEGRSILLGSGDSEVTEPDHPVLASIKKEQETVLLD
Protein: Outer mitochondrial transmembrane helix translocase (EC 7.4.2.-) (ATPase family AAA domain-containing protein 1) (Thorase) (Q9D5T0)
Organism: Mus musculus (Mouse)
Function: Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria (By similarity). Specifically recognizes and binds tail-anchored transmembrane proteins: acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane (By similarity). Also plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8NBU5}; Single-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:17768142}; Single-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000269|PubMed:21496646}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UBX domain-containing protein 7
- Phosphoacetylglucosamine mutase
- Peroxisomal membrane protein 11B
- Peroxisomal membrane protein PMP34
- Acyl-CoA-binding domain-containing protein 5
- Peroxisomal membrane protein 2
- Peroxisomal membrane protein PEX14
- Peroxisomal biogenesis factor 19
- Peroxisomal membrane protein PEX16
- ATP-binding cassette sub-family D member 3
Sequence:
MVHAEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDPLNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEESHDEDEIRPVQQQDLHRAIEKMKKSKDAAFQNVLTHVCLD
Protein: FGGY family of carbohydrate kinase (F4JQ90)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome regulatory subunit RPN13
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- 26S proteasome non-ATPase regulatory subunit 12 homolog A
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome non-ATPase regulatory subunit 3 homolog A
Sequence:
MTTAELNPFPSRSVFLGVDVGTGSARAGLFDDNGKLLGSATSPIQIWKDGDCIEQSSTDIWHAVCAAVKSACSLANVSDVEVKGIGFAATCSLVAVDAEGSPVTVSWSGDSRRNIIVWMDHRAVKQAERINSFNSPVLQYCGGGVSPEMEPPKLLWVKENLKESWSMVYKWMDLSDWLSYRATGDDTRSLCTTVCKWTYLGHAHMHQMTEKASRDMEACGWDDEFWEEIGLGDLVDGHHAKIGRSVAFPGHPLGNGLTATAAKELGLLAGTPVGTSLIDAHAGGVGVMESKLESDSLTKESDVDTLCSRMVLVCGTSTCHMAVSREKLFIPGVWGPFWSAMVPEYWLTEGGQSATGALLDHIIENHVASPRLANRAASQKVSVFELLNNILKTMAEDTSSPFISALTSDMHILPDFHGNRSPVADPNSKGVIFGMSLDTSEKQLALLYLATIQGIAYGTRHIVEHCNTHGHKIDTLLACGGLSKNPLFIQEHADIVGCPIILPRESESVLLGAAILGAVAGKNYPSLHDAMKALNAAGQVVHPSSDPKIKKYHDAKYRIFRNLYEQQLSHRSIIAEALA
Protein: NAD-dependent protein deacetylase hst4 (EC 2.3.1.286) (Homologous to SIR2 protein 4) (Regulatory protein SIR2 homolog 4) (Q9UR39)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: NAD-dependent histone deacetylase, which contributes to both telomeric and centromeric silencing, proper cell cycle progression, DNA damage control, recombination, and genomic maintenance.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10512858}.
Interaction partners:
- NAD-dependent protein deacetylase hst2
- NAD-dependent histone deacetylase sir2
- Putative glutamine-dependent NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- Uncharacterized kinase C24B10.02c
- Uncharacterized kinase C3H5.11
- Putative purine nucleoside phosphorylase
- NAD-capped RNA hydrolase
- Putative nicotinamide mononucleotide adenylyltransferase
- Histone deacetylase clr6
Sequence:
MKVEEHVPLIQESRKRKCQSSENASKRQQLLSKLPLRLHTGNENVDLSPLVSAIRKAKRIVVVTGAGISCDAGIPDFRSSEGLFSSLRAEYKLNCSGKELFDGSVYRDLKSVNIFHAMIRKLHMLSNNARPTDFHLFLSQLAQESKLLRLYTQNIDFLETRLEGLQTCIPLPQSAPWPTTIPLHGTLEVVSCTRCSFLKKFNPDIFDRNGVTVCPDCKTENEVRRIAGKRSVIEGCLRPRIVLYNEIHPDSESIGSVCSQDLKSRPDCLIVAGTSCKIPGVKRIIKEMSNCVHKQKGNVIWLNYDEPTKDFLNLCDLVVQGDLQIAIRRLKPLLDAPSWKLKSHSAKRTSKQKSSEQTKITSSTKITKAIGLNTKSNDSSKKDNTSFQLHQVLNSIEIPKVEIKQEVEYATPSPL
Protein: Uncharacterized protein (Q584U7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGLCNSKSFERDQLAPPPGNRLSDESQRQGGGYKNHSNPAAYEHQTGAEQYLKTFLRSVESVLSERFTFHSQEERDAVSLSFMNSCAEITRTKFRLKMETVVEIISKIAEREKLKTISETLPSVKEFYVDAGFFRLLNTWMSSGGSPANQCTTSSEKYVTEGKDVKRDSRAPTNFASVLIDHLNSASLIPTMDLFPRFAEGGEVMTLEQFGKFVTVTQGNERADAQIVEKYNHRFGGIVHRYNFNTYLMGLMTNNALDPSRTTSVWQDMTQPLTRYLIKTIRIESESDLQRALSDNSRAFVLKIKRNSEGVLCSGSCPLTCIIEGIKTSGFSTIPYPIILCLSPPNTLPVQLKDELAEILSKGLGTMLAKGLMFEGAIISDPKFSPAAQRKKVLVLGYQSPLKPFVGSLMADMNRDGLGVRVTDVVTGTPAAKAGVSKDDWFTHINGEAIINKQHLREQLEKLELGEEFTLKRENLDELKIVVGGAVDREDKSESAALSDLLFLKYAKKKTNLKPWEVVVLTADVLPSLKPNQDSLDDHFAFFSDVDEHSSEQCIGIATQMGVQLIDHGNSREGGLWAQGRFVDNGRSGYLIKNNTNGKLTTSVSVDILAGPQEIKGLPLSSSTARVYGAGKASVKGSKIVFEGCNETTVAVIDCKFVQDSSSFDFTTAFPPLLLRSGYRVLRLEQTGGLTRFDECALGAHCLVSWNKAA
Protein: Lysosomal amino acid transporter 1 (Q95XZ6)
Organism: Caenorhabditis elegans
Function: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes. May play a role in the degradation of autophagic substrates in autolysosomes by regulating lysosome function.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:22822152}; Multi-pass membrane protein {ECO:0000269|PubMed:22822152}.
Interaction partners:
- Cystinosin homolog
- Ribonuclease T2 protein rnst-2
- Inositol polyphosphate-4-phosphatase
- Amino acid transporter transmembrane domain-containing protein
- DRBM domain-containing protein
- RING-type domain-containing protein
Sequence:
MKTGGLSDFADFGEEDANCTQGIQWIKDVFTDCVDTDLKLLGFIIGLISLALWLIPLFPQLWQNYKTKKCEGLSLAFLFFWLVGDTCNMLGAILTNQQPIQKIIGVYYIIQDLVLWTQYGYYLKIYNRPTTSSARSNTIVVPVLALASVGSFFVFESALPPVGDHRVKRSFLESLNHQEGLPLEGILKMWPIFTSYTDMLGYIIGSMAAVCYFGGRIPQIIKNYRHSSCEGLSLTMFYIIVAANFTYGISVLLATTSWLYLLRHLPWLAGSLGCCCFDAVIISQYYLYRPKTPLAEDTERAGLLNSQDDSD
Protein: SRR1-like protein BER1 (Benomyl resistant protein 1) (Q06688)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in microtubule stability and kinetochore function. May be involved in protein N-terminus acetylation and/or proteasome biogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MDFKASGTKFKKTGKKVVPAKAFEEIVQTNRDVLKKSAFLSDLLENLQPHLNNIKKIRCVAIGNFKEDFPATYQFALLLEITDYIKSEDERDVVVSLYDPIFTKEEIQYLKSLGSKWLIEEEFSENDAIDYESVLYFLPHAPLDLTENILSSQRPHLWLANNMISHTDRYTKAKLCENYPNLSKLVHYLQTNAPPEVKKAHDVDGFATFIPKRKRKNRNNSSKLKVTPSDIDYDSIAPKFKSCQILTDFDEGKYLKEKPWINSFSDLTLHAIEY
Protein: Rhodanese domain-containing protein (Q585K9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- FAD/NAD
Sequence:
MVSEAGRANGSRFKPVLLEVAGALVDNRCADVTRRLRQYRNRYAPILRLVTTLIAPVMEESQLFGDDDSCVESAAVADDGRLKEGVTEMAGATAVVGGDGALRGRNGGVKRGRGEPLITAPRCAVVAEKRIIVVHRLHDKEVPDAVEKLERFMSYHFLPLALLHNCQPNISPDDVPFVLRHYVHEATRTASFLVADLSKRAAAIIDPQVDVSCYEEDLAFLQVQLVGIVLTHCFVDIAMGHAALLEHHPTAKLLSGTPFVSTGYGCSDGLSLHLSSRLHLRCISVPSFSPECLVVELHLDAQLLALFTGTVMGTDAVPRYEFFGDFPLPLEPQGDLQHTSAMPAPEVARRFLRERVWDAYFFPDPAAGHVQPWDHVVVFPSHGGYSNVTHQLDLYWAVHIGDMKRMKHSRTVMDKILDPEKYAQHMLDRPRLPKPLLVSHVREWNLLSVPSAFGGSGEGLLRRRLLPPPACALTSPCPGPVVVDIRSAADHVTMHLKGSVNVPMTFPAAAYGVKKAELWLQCMLKPLQPVVVVCANERQCHLARQRLELISPGASVETFTLQELCPPCGVHAVDGQEKEVFNRVDVTTSLPATVDSRHLPRHLTWVFDSTASAQSRLDCYQKLQFIEPAEDTLVLDCRTPYEFRNGSHTRSVFLSLGDLCHITALDLVAQQLTPEADVHCGGWPSPELGRIILDRMYEAALASGLKCRPGCRGIRKIVVYCATGYRSLIAASLMRRAFEAASLDIVVYDVAGGALQVMQQRPDLWTVKDRSIICIS
Protein: Doxorubicin resistance ATP-binding protein DrrA (EC 7.6.2.-) (P9WQL9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ABC transporter complex DrrABC involved in doxorubicin resistance. Responsible for energy coupling to the transport system. Binds ATP.
Subcellular location: Cell membrane {ECO:0000305|PubMed:12057006}; Peripheral membrane protein {ECO:0000305|PubMed:12057006}; Cytoplasmic side {ECO:0000305|PubMed:12057006}.
Interaction partners:
- Doxorubicin resistance ABC transporter permease protein DrrB
- Probable doxorubicin resistance ABC transporter permease protein DrrC
- Phenolphthiocerol/phthiocerol polyketide synthase subunit E
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Phthiocerol/phthiodiolone dimycocerosyl transferase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit D
- Phenolphthiocerol/phthiocerol polyketide synthase subunit A
- Long-chain-fatty-acid--AMP ligase FadD26
- Phenolphthiocerol/phthiocerol polyketide synthase subunit B
- Phthiocerol dimycocerosate exporter MmpL7
Sequence:
MRNDDMAVVVNGVRKTYGKGKIVALDDVSFKVRRGEVIGLLGPNGAGKTTMVDILSTLTRPDAGSAIIAGYDVVSEPAGVRRSIMVTGQQVAVDDALSGEQNLVLFGRLWGLSKSAARKRAAELLEQFSLVHAGKRRVGTYSGGMRRRIDIACGLVVQPQVAFLDEPTTGLDPRSRQAIWDLVASFKKLGIATLLTTQYLEEADALSDRIILIDHGIIIAEGTANELKHRAGDTFCEIVPRDLKDLDAIVAALGSLLPEHHRAMLTPDSDRITMPAPDGIRMLVEAARRIDEARIELADIALRRPSLDHVFLAMTTDPTESLTHLVSGSAR
Protein: Endoplasmic reticulum aminopeptidase 2 (EC 3.4.11.-) (Leukocyte-derived arginine aminopeptidase) (L-RAP) (Q6P179)
Organism: Homo sapiens (Human)
Function: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12799365}; Single-pass type II membrane protein {ECO:0000269|PubMed:12799365}.
Interaction partners:
- Tripeptidyl-peptidase 2
- HLA class I histocompatibility antigen, C alpha chain
Sequence:
MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT
Protein: Beta-methylmalyl-CoA dehydratase (EC 4.2.1.148) (2-methylfumaryl-CoA hydratase) (Mesaconyl-CoA hydratase) (A9WC34)
Organism: Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Function: Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. Catalyzes the reversible dehydration of beta-methylmalyl-CoA ((2R,3S)-beta-methylmalyl-CoA) to yield mesaconyl-CoA (2-methylfumaryl-CoA).
Interaction partners:
- Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase
- 2-methylfumaryl-CoA isomerase
- acetate--CoA ligase
- Succinyl-CoA--L-malate CoA-transferase beta subunit
Sequence:
MSAKTNPGNFFEDFRLGQTIVHATPRTITEGDVALYTSLYGSRFALTSSTPFAQSLGLERAPIDSLLVFHIVFGKTVPDISLNAIANLGYAGGRFGAVVYPGDTLSTTSKVIGLRQNKDGKTGVVYVHSVGVNQWDEVVLEYIRWVMVRKRDPNAPAPETVVPDLPDSVPVTDLTVPYTVSAANYNLAHAGSNYLWDDYEVGEKIDHVDGVTIEEAEHMQATRLYQNTARVHFNLHVEREGRFGRRIVYGGHIISLARSLSFNGLANALSIAAINSGRHTNPSFAGDTIYAWSEILAKMAIPGRTDIGALRVRTVATKDRPCHDFPYRDAEGNYDPAVVLDFDYTVLMPRRG
Protein: Smooth, isoform L (A0A0B4K7W3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYNGASNGSGASGAGGGGATIVVTEGPQNKKIRTGVQQPGENDVHMHARSTPQQNQQQALMNKSNDDLRRKRPETTRPNHILLFTIINPFYPITVDVLHKICHPHGQVLRIVIFKKNGVQAMVEFDNLDAATRARENLNGADIYAGCCTLKIDYAKPEKLNVYKNEPDTSWDYTLSTVKEIGNGRSPLLQEPLYEPPLLGPGAAFPPFGAPEYHTTTPENWKGAAIHPTGLMKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPPGLTEDQLIGIFNIKDVPATSVRLFPLKTERSSSGLIEFSNISQAVLAIMKCNHLPIEGKGTKFPFIMKLCFSSSKSMNGAWNNAASEGMIEKENEVDTKVDIYN
Protein: Corticotropin-releasing factor-binding protein (CRF-BP) (CRF-binding protein) (Corticotropin-releasing hormone-binding protein) (CRH-BP) (P24388)
Organism: Rattus norvegicus (Rat)
Function: Binds CRF and inactivates it. May prevent inappropriate pituitary-adrenal stimulation in pregnancy.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Corticoliberin
- Urocortin
- Corticotropin-releasing factor receptor 1
- Corticotropin-releasing factor receptor 2
- Urocortin-2
- Pro-opiomelanocortin
Sequence:
MSPNFKLQCHFTLILLTALRGESRYLEVQEAAVYDPFLLFSANLKRNLAEEQPYRRALRCLDMLSLPGQFTFTADQPQLHCAAFFIGEPEEFITIHFDLVSIDCQGGDFLKVFDGWILKGEKFPSSQDHPLPTRERYTDFCESGLTRRSVTSSQNVAMVFFRVHEPGNGFTITIKTDPNLFPCNIISQTPSGRFALVVPYQHQNCSFSIIYPVTIKISDLALGHLHGLQLKKPAAGCGGTGDFVELLGGTGLDTSKMMLLVDLCYPFHGPAQMKISCDNAVVRMVSSGKHMNRVTFEYRQLEPLELETSTRNSIPEYCLSSL
Protein: Probable purine nucleoside permease C285.05 (O74493)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable nucleoside permease that transports adenosine and guanosine.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome b
- Cytochrome c oxidase polypeptide 5, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome b-c1 complex subunit 10
Sequence:
MLFLKLVASVLALMTIVPAQAGLIGKRSVFKPKVMIINMFSLEANAWLSQMDDLYANNITVVGLNRLYPQVHCNTQQTICQMTTGEGKSNAASSIMALTLSPKFDLTETFFLISGIAGINPYAASLGSVGVARFAVDIDLINSVDLRELPSYFQSSGWEIDTDPYENGSSNEIVYPESMPYQTNLYELNNTLITAAMEIIKDVVLEDNEKAASYRKLYNESAARRPPFITQCDTATGDNYWAGTYMGDFVSNITNVLTNSTGHYCTTQQEDNASLTALTRASFDGLVNINRVVIMRSGSDFDRGAGNITALANLLNSTGHVSSLACDNLYHAGAPLIDHIVNHWSYWT
Protein: G2/mitotic-specific cyclin-B3 (Q9I7I0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cyclins are positive regulatory subunits of the cyclin-dependent kinases (CDKs), and thereby play an essential role in the control of the cell cycle, notably via their destruction during cell division. Probably functions redundantly with other cyclins in regulation of cell cycle. Its presence may be required to delay a deadline for completing cytokinesis that is ordinary imposed by nuclear envelope reformation. Degradation of CycB and CycB3 promote cytokinesis furrow initiation and ingression. Required with CycB for female fertility.
Subcellular location: Nucleus {ECO:0000269|PubMed:9851980}.
Interaction partners:
- Cyclin-dependent kinase 1
- G2/mitotic-specific cyclin-B
- Serine/threonine-protein kinase polo
- Cell division cycle protein 20 homolog
- G2/mitotic-specific cyclin-A
- Cyclin-dependent kinases regulatory subunit
- Cell division control protein
- separase
- Cyclin-dependent kinase 2
- Cyclin-dependent kinases regulatory subunit
Sequence:
MAPTKATTRAAITSGHHQLQQAVNPILGALGAATRKGLTRRAAATGNIDPNVENMQTRAKRKADHSPIKNDKIKRSALGNLTNNVKIMTLHPAQDEEQSGVGKKPTAQQLQALMDAKKQENLSVNVFGASKMTTRASSKVEDSVENCHKVLDKLEEALARPKPRPKAVPAAKKTVLGEVQLPAMPNPMQIPVLLPPTHNLAAPQVAAVKPVRRISNDFNKTEDSLYMSALEDVSSCDSMRLSGNFEAARRRSAKLQQKTEQQPQPLLLTLPETAPSQVVPIPPVPEEVEDFDRKNWDDPFQVSHYAMDIFNYLKVREAEFPIADYMPRQIHLTTWMRTLLVDWMVEVQETFELNHETLYLAVKIVDLYLCREVINKEKLQLLGAAAFFIACKYDERQPPLIEDFLYICDGAYNHDELVRMERETLRVIKYDLGIPLSYRFLRRYARCAKVPMPTLTLARYILELSLMDYANISFSDSQMASAALFMALRMHGGPGQLDKQTWTSTLIYYTGYQLADFAEIVTALNAGLHRKPRATIKTIRNKYSHKIFHEVAKVPLLTNQELFQGNLDLNESNLS
Protein: Protein salt-induced and EIN3/EIL1-dependent 1 (Q9FMS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ethylene-dependent salt stress responses by reducing reactive oxygen species (ROS) accumulation.
Interaction partners:
- Ethylene-responsive transcription factor ERF095
- Serine/threonine-protein kinase Nek5
- Serine/threonine-protein kinase Nek6
Sequence:
MNQEAASNLGLDLKLNISPSLDSSLLTESSSSSLCSEEAEGGGGEAKSMVVVGCPNCIMYIITSLENDPRCPRCNSHVLLDFLTGNHSKKSTS
Protein: Actin protein 2/3 complex subunit-like protein (At2g28130) (Q0V7S1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDLDGPLDFENEDPLVNPPTIIEKRKKVIGLDDLLSDFYKEKSKVIDKVNKKRKVSKVYHSDDDEQGQVDKLSQCVVECQNQMNEIADEEENQEWGLSMFGDQKTPIPSLLVDLDSCCLLKEFMNNQLNLVVGLTVDEGTTFIEGLLVNGWLTRLIMTCGRVEKFICKWTLNILLYSSKEDLRSSACDFWCSILLSQNKVNGASVEIYWLPNYQELKEALESYGFRISLSHSQDVELAEADSECQGPPQNIRAWLTLVTTCCQFRCKKPIFTTSQVEQIAEILVSLLLDRSLLGLSILLQECLISVIGSFKEEEWISSCKKIANSLASRVPQDINCLRVVESVSGVDARSKHLRSSIAHQMLVVLLDHKDSDENLLSSLMSINVKERSCNLFKMYIFLVLAENWLFSSTLVEAKPVLRDMWAVFLRNCSCQINSTDLRSYASKVRTRAAYLLQGCSSN
Protein: 3',5'-nucleoside bisphosphate phosphatase (EC 3.1.3.97) (Q7NXD4)
Organism: Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK)
Function: Hydrolyzes 3',5'-bisphosphonucleosides (pGp, pCp, pUp, and pIp) to nucleoside 5'-phosphate and orthophosphate. Has similar catalytic efficiencies with all the bases. Also shows activity with ribonucleoside 2'-deoxyribonucleoside 3',5'-bisphosphates. Does not show activity with nucleoside 2',5'-bisphosphates.
Interaction partners:
- YrdC-like domain-containing protein
- Ribonuclease 3
- Oxidoreductase-like domain-containing protein
- Uncharacterized protein
- Phosphoglycolate phosphatase
Sequence:
MANIDLHFHSRTSDGALTPTEVIDRAAARAPALLALTDHDCTGGLAEAAAAAARRGIPFLNGVEVSVSWGRHTVHIVGLGIDPAEPALAAGLKSIREGRLERARQMGASLEAAGIAGCFDGAMRWCDNPEMISRTHFARHLVDSGAVKDMRTVFRKYLTPGKPGYVSHQWASLEDAVGWIVGAGGMAVIAHPGRYDMGRTLIERLILDFQAAGGQGIEVASGSHSLDDMHKFALHADRHGLYASSGSDFHAPGEGGRDVGHTEDLPPICRPIWRELEARILRPAD