wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase III PolC-type (PolIII) (EC 2.7.7.7) (P75080)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00356}.
Interaction partners:
- DNA polymerase III subunit alpha
- Beta sliding clamp
- DNA polymerase III subunit gamma/tau
- Probable DNA polymerase III subunit delta
- Uncharacterized protein MG007 homolog
- DNA primase
- Uncharacterized protein MPN_049
- DNA topoisomerase 1
- Probable cell division protein WhiA
Sequence:
MVFDTETEKGKRIWALSQFLVKKNILDHNELHQLNNRIELVYLENDRENALFLVALTLKKPLTIDIWNALYEGFQDAEGAELRITFQEDATFFKDGSTKSSVTLAIIKDYFKSFFGKDKKYRILLEQELTHPNFLSYSNHELKANCQSQELDQWLIEQRQAFIKWMHQAGFTHFGFVSLFNPPAEKQLKVKSMKVSKYDKQFETEVFSTEFVPIHKINQQMDEIKLMGQIFELKDFPGYNNLRNTLNIYVTDFQLGGSLILKWFYKDPKTIEGIKIGTWVKATVKVERDAKTQLLQGIIKEISPIETPAYYRRPDQDKQKRVELVFHTKMSAFDGINSVQEYAQFAKERDWKTIAVTDKDNIHIYPTLYEVAKKYGLKAIYGLECNLIDDHIKIVSNPDKTKLKDATFVIFDIETTGLHGRYDSVIEFAGIKVKHNREVERMQFFLKIDGPLPAAVTEITKITQAQLEDGMEQQAGLEKLRAWLDGCVMVAHNGLSFDLPFLQTQFEKYNIAPLTNPLIDTLALSWALNPGFASHTLSNICAKLKFDFDDERLHRADYDTQALKKVFDYFKEQVELMGITNLEQLDQELNQQCHFELLKRTFTNTGIIYIKSQSGFAKLYELLSIALTDNNATRPLVLTSTLQKFAKSFVITDNPVQGDIFKAALTKPLKELEAAIKRVDFVLIAPPGAYAGYTIREGLKKEAIPNAIKLVVDTAQRLNKLVAVASDAYFIHPWENEYYKAIVCAKGLGGRWHRHFNYKEREQRVPNVFVRTTGEMLNEMSFLGEQLAYELVVENTNKLAKQLTADDLVPVQTKLQPPVIEGSNENLAAKTWSQAKAIYGDPLPKLIEQRIQEELKAIIDNGFGIIYWISHLLVKQSVQDGYFVGPRGSIGSSLVANLIGISEINPLVPHYLCESCQYFEVNEEVDDGYDLMVRDCPKCGAKAAFKGDGHNIPFATFMGFAGDKIPDIDLNFSSEYQAKAHAYVRELFGEQYTFRAGTIATVAEKTAYGYARNYFEIIKQTELATAPEIERFKQKLVGIKRTTGQHPGGIMIFPNHKSVYEFTPCGYPADDTSSDWKTTHFEYDALGNTILKLDILGQDDPTMLKHLGDLTHVNPQNIPRFDKKLTEMFWSVNPLKLKPHYLDEPTGAIGIPEFGTKFVRKILEQTKPKGFGDLIRVSGLSHGKNVWADNAQKILKDQNLSLKDVIACRDDIMLYLIHKGMQAKDAFEIMEKVRKGIALNAKEVQLMQSNGVEQHWINSCLKISYLFPKAHAAAYVLMAWRIAWFKLYHPLSYYACLLSFKLKEHDVSGFKSGVSFVKQKLEELNTLYRIKRIKPKEAELLTSYEVYLEMMARGIKLEQISLTHSHATRFVEHNGMLIAPFITIPGMGEAVANSIIEARNEKPFSSLDDFKKRTKITKKHIEAFTQMQLLDEFREQDNQKKLF
Protein: SKP1-like protein 8 (AtSK8) (Q9LSY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- Cullin-2
- Cullin-like protein 3
- Putative cullin-like protein 2
- Putative cullin-like protein 1
- RING-box protein 1a
- RING-box protein 1b
- F-box protein 7
- Elongin-C
- Cullin-3A
Sequence:
MSTKKIMLKSSEGKTFEIEEETARQCQTIAHMIEAECTDNVILVLKMTSEILEMVIEYCNKHHVDAANPCSDDDLEKWDKEFMEKDKSTIFALTNAANFLNNKSLLHLAGQTVADMIKGNTPKQMREFFNIENDLTPEEEAAIRRENKWAFE
Protein: B-box zinc finger protein 21 (AtBBX21) (Protein LONG HYPOCOTYL UNDER SHADE) (Protein SALT TOLERANCE HOMOLOG 2) (Q9LQZ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that acts as positive regulator of seedling photomorphogenesis. Acts downstream of COP1 and play an important role in early and long-term adjustment of the shade avoidance syndrome (SAS) responses in natural environments.
Subcellular location: Nucleus {ECO:0000269|PubMed:17965270}.
Interaction partners:
- Transcription factor HY5
- E3 ubiquitin-protein ligase COP1
- B-box zinc finger protein 32
- B-box type zinc finger family protein
- Transcription factor HY5-like
- B-box domain protein 30
- B-box domain protein 31
- Transcription factor HFR1
- At5g54470
- Protein ABSCISIC ACID-INSENSITIVE 5
Sequence:
MKIRCDVCDKEEASVFCTADEASLCGGCDHQVHHANKLASKHLRFSLLYPSSSNTSSPLCDICQDKKALLFCQQDRAILCKDCDSSIHAANEHTKKHDRFLLTGVKLSATSSVYKPTSKSSSSSSSNQDFSVPGSSISNPPPLKKPLSAPPQSNKIQPFSKINGGDASVNQWGSTSTISEYLMDTLPGWHVEDFLDSSLPTYGFSKSGDDDGVLPYMEPEDDNNTKRNNNNNNNNNNNTVSLPSKNLGIWVPQIPQTLPSSYPNQYFSQDNNIQFGMYNKETSPEVVSFAPIQNMKQQGQNNKRWYDDGGFTVPQITPPPLSSNKKFRSFW
Protein: Signal transducer and activator of transcription 1 (Q9NAD6)
Organism: Caenorhabditis elegans
Function: Carries out a dual function: signal transduction and activation of transcription. Activated STAT proteins play a role in repression of dauer formation. Neuronal expression is held in check by negative signals through the TGF-beta pathway that target the daf-3 transcription factor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16401427}. Nucleus {ECO:0000269|PubMed:16401427}. Note=Translocated into the nucleus in response to phosphorylation.
Interaction partners:
- Receptor tyrosine-protein kinase let-23
- E3 SUMO-protein ligase gei-17
- Probable RNA-binding protein EIF1AD
Sequence:
MMGSSSQELQTALTDVSKTCHHLWEENKDLQGRFVNELGELQRLQMVIAQLEQQQRLENVFTVKQQMTELQKRAATLYEHLTQKRNDIVIKLNDGTNFATMLQTQLIGEKLFSWKNAQKLAQIGMPFDNREQLLDEIQIEFEFLADQNWQLNMFSCWMLDLLRRAPQLNDGLAQATIGKLTAITEQLNKLLFMLVSQSFIVSVQPEPVLKTQHKFVTEVRLLIGDKLGIRQHLVNTNVSVKIIAEDEAKQLSVDYDAHKEIRNNKTVGTISNDFEKLTMNERGHLAAKFNNSKLTRIAHRKPPPKGASDLKCAASMQAATDQKYALLFFITPFQMGNLSKEEQFDVWTLSLPIMVTVHGSQDCDAQVAILWHRAFASISRNPNTTDVTAVTWDNLAIMLRNKFSLFTGARRPLSDSDLAYLSEKMLMPNVADQKPITFHRFAKQAMRDDLPFSFWEWFFSIMQLIKQKLLKFWDEGWCIGFISKNDASQSMMMCQHSSFLLRFSDSQTGAVSIGFVCEEADGQKIPFHLAPFTIKDLDQLSLASRIASCPQLKDIRYMYPAIDKEEMLRFFESEERHRVGGGDSPTGYIQSEIVMVAKTNGNFRRMSNAPSMFGADSPSPLSVQSKLDWSPGEVHQNHMMEMSDELGQILTVSDMSGDVETLLGPAFKNNITNYNPHDGNHQHNLHFVDMSQQGMMQQHHNQFYPS
Protein: Ninein-like protein (G9G127)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2I6}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y2I6}.
Interaction partners:
Sequence:
MDEDEQNRYVAQLKDEFDSCDTTGTGYLDKEELTALCHKLSLDAHLPLLLDTLLGPQHYARVNFEEFKEGFVAVLSRSLDFSTSEEESSYLEPAVPEEVKPKYVKGTKRYGRRSRPDKTDLELTADSDSLPFGTDKVEANGVRRAKLRRSTSLESVESLKSDEDTGSNKESTHHYFVAQGQLKLWNQDGTGNCQRSSDNQQEVTDGQVRAVWEELGVGAAGSLNREELSLVCDHIGLKHLEAEELDALFRKLDKDQDGKVSLIEFQSGLFKPHDHASPLSTSTPARPKPLRTISKALEERVVRSTSPSLLSATVGQRLLTRLDDGSGCTSPEKVMALWTEEGIHNSRDILQTQTLDFSLEERLCLAELTLALDNELLVSGNGIHQAALVSYKNEINYLQVLADQACQERDKAKADLEQADRRNLQLVREVDDRHATMESLNESKIKDLEQEFRDKLTALRSESEYESEVLLEQVEKERERLRDELQLLRSQDISLQEDMCTTVNENRRLEEEVSALKEKLTEAESAISKLQNDLDRLLQDKYDGLDANGTGLLNQEEQFTEIFKEYEQQCRELQDRNDELCSELELLKSQGSGKRTRLSRSSLPANDWSNRRALTTESDSDDPEMKKGTSPQVRKKLQVTDKNVLGSLESLAPPVSIETELAMEKMKERYEQEVQDLKIQLETKVNFYERSMDLMRQNMEVERKDISQSFKMEISELEDLKARAEERAEQMRQTTERLEAELRGKTSGGAWGQEQERRIQRERAELEQNYAREISNLVLRLTSEKDQLEAELKLRMDREVLLVRAQLDEVTSENCALKDRLAVLQQDVKSLEEDVNNKRKKLEEMEKGYMKNREDEERLRKENSKCREEVLDLSARNLQLSSENAELSSRLCTDQRAVQTLTDRLAQVCQERDAAAVSSKQLQENLQQQENHGLRLQEQWRKEKELLERELQTAKEALQHLTVVESALTSQTLKNKSLEQDKESLLKETAENDQKLKKLQEALRNSETQIEQLNAQILTMWQEKDVHVQEAAAHIKMLQQSQDKVQELEERISQLRKEKEQVQHTHRLQEETAVSVLQNECKSLRVQNKELQNKVAQLQSRELELQRLTHECLTLRNKQAELETAKQEANQQAMRAESTRSMVQAQHTREIQELKEQMGSGTQEHASHLQTQLAEQQRRTQDFEDLLRSQAKQASVQMGLQQEQYEKLMASMQERMDEVEAKLKNTRVMLQEKVNQLKEQLAKNSKSDVLLKDLYVENSQLMKALQVTEQRQKSAEKKSFLLEEKVIALNKLLRKIAPASLTA
Protein: Protein giant (P39572)
Organism: Drosophila melanogaster (Fruit fly)
Function: Represses the expression of both the krueppel and knirps segmentation gap genes. Binds, in vitro, to the krueppel regulatory elements CD1 and CD2. It is required in the early embryo for the development of portions of the head and abdomen.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MLMHEKLMAGQFFDLKTDRKPLMHHHQYQHHQQQPLHHLPHSQLPVQGSLGLPKMDLYTAYAYQQQLLGAALSQQQQQQQQQQQHQQLQQQHTSSAEVLDLSRRCDSVETPRKTPSPYQTSYSYGSGSPSASPTSNLLYAAQMQQQQHQQQQQQQQQQQQLASLYPAFYYSNIKQEQATPTAAPPKVTPTANLLQTFAAASAAAAAAAAASSTNSPRPASNASTMQIDVLENPLSPAVEATTPTTSSSGEAGKNTRPFKAFPRDPLVIAANFAATDVLLDNPRVERYTEYRKRVLEQIRSSNGGSRTVTNPKMRRTNSRSGSVNEGSSSNNNSESEDRAAAEESSDCDSQAGNFESKSATSSSSNLANATAANSGISSGSQVKDAAYYERRRKNNAAAKKSRDRRRIKEDEIAIRAAYLERQNIELLCQIDALKVQLAAFTSAKVTTA
Protein: Vacuolar aminopeptidase 1 (EC 3.4.11.22) (Aminopeptidase yscI) (Leucine aminopeptidase IV) (LAPIV) (Lysosomal aminopeptidase III) (Polypeptidase) (Vacuolar aminopeptidase I) (P14904)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1).
Subcellular location: Vacuole {ECO:0000269|PubMed:24493041, ECO:0000269|PubMed:363165, ECO:0000269|PubMed:8601598}. Note=Transported to the vacuole by the cytosol-to-vacuole targeting (Cvt) pathway. {ECO:0000269|PubMed:9151668, ECO:0000269|PubMed:9214379, ECO:0000269|PubMed:9412464}.
Interaction partners:
- Alpha-mannosidase
- Autophagy-related protein 19
- Autophagy-related protein 11
- Autophagy-related protein 8
- Autophagy-related protein 34
- Autophagy-related protein 9
- Serine/threonine-protein kinase ATG1
- Autophagy-related protein 13
- Saccharopepsin
- Intermediate cleaving peptidase 55
Sequence:
MEEQREILEQLKKTLQMLTVEPSKNNQIANEEKEKKENENSWCILEHNYEDIAQEFIDFIYKNPTTYHVVSFFAELLDKHNFKYLSEKSNWQDSIGEDGGKFYTIRNGTNLSAFILGKNWRAEKGVGVIGSHVDALTVKLKPVSFKDTAEGYGRIAVAPYGGTLNELWLDRDLGIGGRLLYKKKGTNEIKSALVDSTPLPVCRIPSLAPHFGKPAEGPFDKEDQTIPVIGFPTPDEEGNEPPTDDEKKSPLFGKHCIHLLRYVAKLAGVEVSELIQMDLDLFDVQKGTIGGIGKHFLFAPRLDDRLCSFAAMIALICYAKDVNTEESDLFSTVTLYDNEEIGSLTRQGAKGGLLESVVERSSSAFTKKPVDLHTVWANSIILSADVNHLYNPNFPEVYLKNHFPVPNVGITLSLDPNGHMATDVVGTALVEELARRNGDKVQYFQIKNNSRSGGTIGPSLASQTGARTIDLGIAQLSMHSIRAATGSKDVGLGVKFFNGFFKHWRSVYDEFGEL
Protein: Eyes absent homolog (EC 3.1.3.48) (A0A2R8YET7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEDPRGINGQSVQTSQASSDVAVSSSCRSMEMQDLTSPHSRLSGSSESPSGPKLGNSHINSNSMTPNGTEVKTEPMSSSETASTTADGSLNNFSGSAIGSSSFSPRPTHQFSPPQIYPSNRPYPHILPTPSSQTMAAYGQTQFTTGMQQATAYATYPQPGQPYGISSYGIKTEGGLSQSQSPGQTGFLSYGTSFSTPQPGQAPYSYQMQGSSFTTSSGIYTGNNSLTNSSGFNSSQQDYPSYPSFGQGQYAQYYNSSPYPAHYMTSSNTSPTTPSTNATYQLQEPPSGITSQAVTDPTAEYSTIHSPSTPIKDSDSDRLRRGSDGKSRGRGRRNNNPSPPPDSDLERVFIWDLDETIIVFHSLLTGSYANRYGRECDQVHIDDVSSDDNGQDLSTYNFGTDGFPAAATSANLCLATGVRGGVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEEEQGAKKHAMPFWRISSHSDLMALHHALELEYL
Protein: Protein phosphatase 2C 3 (AtPP2C03) (EC 3.1.3.16) (Protein AKT1-INTERACTING 1) (Protein HIGHLY ABA-INDUCED PP2C 2) (Protein HONSU) (Protein phosphatase 2C AIP1) (PP2C AIP1) (Q9LNW3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the negative regulation of the K(+) potassium channel AKT1 by its dephosphorylation, antagonistically to CIPK proteins (e.g. CIPK23). Functions as positive regulator of abscisic acid-mediated cell signaling during seedling growth. Involved in the regulation of seed dormancy. Acts as negative regulator of seed dormancy by inhibiting abscisic signaling and subsequently activating gibberellic acid signaling.
Subcellular location: Cell membrane {ECO:0000305|PubMed:17898163}. Cytoplasm {ECO:0000269|PubMed:22404835}. Nucleus {ECO:0000269|PubMed:22404835}. Note=Probably associated to the plasma membrane when interacting with AKT1 and CIPK23 (Probable). Localizes to nucleus when interacting with PYL8/RCAR3 (PubMed:22404835). {ECO:0000269|PubMed:22404835, ECO:0000305|PubMed:17898163}.
Interaction partners:
- Abscisic acid receptor PYR1
- Abscisic acid receptor PYL8
- Abscisic acid receptor PYL9
- Serine/threonine-protein kinase SRK2D
- Serine/threonine-protein kinase SRK2E
- Serine/threonine-protein kinase SRK2J
- Serine/threonine-protein kinase SRK2I
- Serine/threonine-protein kinase SRK2H
- Serine/threonine-protein kinase SRK2F
- Serine/threonine-protein kinase SRK2B
Sequence:
MADICYEDETSACESRPLWSSRKWRIGVQRFRMSPSEMNPTASTTEEEDKSEGIYNKRNKQEEYDFMNCASSSPSQSSPEEESVSLEDSDVSISDGNSSVNDVAVIPSKKTVKETDLRPRYGVASVCGRRRDMEDAVALHPSFVRKQTEFSRTRWHYFGVYDGHGCSHVAARCKERLHELVQEEALSDKKEEWKKMMERSFTRMDKEVVRWGETVMSANCRCELQTPDCDAVGSTAVVSVITPEKIIVANCGDSRAVLCRNGKAVPLSTDHKPDRPDELDRIQEAGGRVIYWDGARVLGVLAMSRAIGDNYLKPYVTSEPEVTVTDRTEEDEFLILATDGLWDVVTNEAACTMVRMCLNRKSGRGRRRGETQTPGRRSEEEGKEEEEKVVGSRKNGKRGEITDKACTEASVLLTKLALAKHSSDNVSVVVIDLRRRRKRHVA
Protein: Protein HLR1 (LRE1 homolog) (Q04429)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cell wall composition and integrity and response to osmotic stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MENLCPPPPSQMKDFSTPPRNRHRHKRSFAISGDFEFLKQPASAPVLPSAYDSPTFENTPRRVSGMSVTMPDESQNESALLNSPSPRFFISEASTYSSPIKGVPDAIINLDDVLINKPKMCRSHRKTKSVPVKLDEFYSSHKCSSVPELTINEEIDEDDTNPQLLEPVKPLSSTSLSTDMNEDKKMTLKNARSHNSLKIQAQKQRYYNSARYLPLNSEDRATDPQILTKQSSVTSLFSSRSITPVSCNINNAGRINAISGNYLDDVLYDLDTPATTLIQDIDNLQTSINERVRLSPQSSSIKKYFSKDGKSVSSFNFQSQECDMVSFTEDFAHVTSLSSSILDSEKQTDDEEEESIPEEILRGEPLHVYNETSGSDKSVILPTKQKSAPINKDSKHSSTQYEEKSFKKNRKFKIFAKLFCTRK
Protein: Delta-selinene-like synthase, chloroplastic (PsTPS-Sell) (EC 4.2.3.76) (Q20HU6)
Organism: Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Function: Sesquiterpene synthase (sesqui-TPS) involved in the biosynthesis of sesquiterpene natural products. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into delta-selinene (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MAQISESAAIPRRTANHHGNVWDDDLILSLDSPYGAPAYYERVANLIEEMKHLLLREMEDSNHDLIRRLQIVDTLECLGIDRHFQHEIKTAALDYVYRCWNEKGIGMGSSDSGSKDLDATALGLRALRLHRYNVSSGVLENFKDENGKFFCNLTGDKRVRSMLSLLRASEISFPGEKVMQEAKAFTREYLTQVLAGRGDVTDVDQSLLREVKYALEFPWHWSVPRWEARSFIEIYGQNHSWLKSNINQKVLELAKLDFNILQCIHQKEIQFIVRWWRESEIAQLNFYRKRHVEFYFWVVICIFEPEFSQSRIAFAKICTVATVLDDLYDTHGMLDELKTVTEGVSRWDLPLIDDLPDNIKIAFQFFFNTANELAVEVVKKQGRDMIALLKANWQRYVESYLQEAEWIATRHVPSFDEYIKNARASSGMCIGNLIPLLLLGQLLANNIVEQIHSPSKIQELSELTIRLIDDIRDFEDEKERGEIASAIECYMKDNPDSTVENALNHLEGILHLSLEELNWEFIKQDTVPLCCKKFTFNIVRGLQFVYKYGDGLSISNKEVKDQIFKILIDQVPIEE
Protein: Glucose-6-phosphate 1-epimerase (EC 5.1.3.15) (Q6FN26)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Glucose-6-phosphate isomerase
- phosphoglucomutase
- phosphoglucomutase
- phosphopentomutase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
- Transketolase
Sequence:
MSIEETDSQVVITHPSNSNTSVTILKYGATVTSWKLNGEEQLWLSTAAKLDGSKPVRGGIPLVFPVFGKNQSDELLSKLPQHGFARNSTWEFLGQVKSNPPTVQFGLNPKIANQELVKLWPLDFNLILTIELGEDFLKTAIEVENASEENMKFNWLFHTYLHIEDIEDTMVSNLVGMKVYDQLLKESFIDKHPVVTFHQETDSIYQNVDSDRLIQVVGKGKPLHTVKRENLPDAVVWNPWVDKSAGMGDFEPKDGFKNMVCVEPGHVSDFVVLPPGQKWSAAQILSKQELNYQAIEP
Protein: DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-alkyladenine DNA glycosylase) (3-methyladenine DNA glycosidase) (ADPG) (N-methylpurine-DNA glycosylase) (P29372)
Organism: Homo sapiens (Human)
Function: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23290262}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:23290262}. Nucleus {ECO:0000269|PubMed:23290262}.
Interaction partners:
- DNA repair nuclease/redox regulator APEX1
- Methylated-DNA--protein-cysteine methyltransferase
- N-glycosylase/DNA lyase
- Vacuolar protein sorting-associated protein 18 homolog
- Endonuclease III-like protein 1
- Hemoglobin subunit zeta
- DNA repair protein XRCC1
- Elongator complex protein 1
- Uracil-DNA glycosylase
- Endonuclease 8-like 2 lyase Neil2)
Sequence:
MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA
Protein: Coenzyme Q-binding protein COQ10, mitochondrial (Q08058)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16230336, ECO:0000269|PubMed:16823961}; Peripheral membrane protein {ECO:0000269|PubMed:16230336, ECO:0000269|PubMed:16823961}; Matrix side {ECO:0000269|PubMed:16230336, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Atypical kinase COQ8, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
Sequence:
MVLIIRPSQTLILFRKAMLKPIGRYPLKRNFFGLSGTNHTIREQRYVLRKAINAPPSTVYAAVSEVAQYKEFIPYCVDSFVDKRNPVDNKPLIAGLRVGFKQYDEEFICNVTCKDTDHTYTVVAETISHNLFHLLISKWTIMPHPNRPNAAMVELLLRFKFKSRIYNSVSLIFAKTVTELVMNAFAKRAYHLVRLAMLKPSSKEGSP
Protein: Prolyl endopeptidase-like (EC 3.4.21.-) (Prolylendopeptidase-like) (Q4J6C6)
Organism: Homo sapiens (Human)
Function: Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16385448, ECO:0000269|PubMed:23485813}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q8C167}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8C167}. Golgi apparatus {ECO:0000250|UniProtKB:Q8C167}. Nucleus {ECO:0000269|PubMed:23485813}. Note=Co-localizes with AP-1 in the trans-Golgi network (By similarity). Co-localizes with MAP2 and ACTB on the cytoskeleton (By similarity). Co-localizes with STX6 and GOSR2 at the Golgi apparatus (By similarity). {ECO:0000250|UniProtKB:Q8C167}.
Interaction partners:
- Calmodulin-lysine N-methyltransferase
- Amino acid transporter heavy chain SLC3A1
- Protein phosphatase 1B
Sequence:
MQQKTKLFLQALKYSIPHLGKCMQKQHLNHYNFADHCYNRIKLKKYHLTKCLQNKPKISELARNIPSRSFSCKDLQPVKQENEKPLPENMDAFEKVRTKLETQPQEEYEIINVEVKHGGFVYYQEGCCLVRSKDEEADNDNYEVLFNLEELKLDQPFIDCIRVAPDEKYVAAKIRTEDSEASTCVIIKLSDQPVMEASFPNVSSFEWVKDEEDEDVLFYTFQRNLRCHDVYRATFGDNKRNERFYTEKDPSYFVFLYLTKDSRFLTINIMNKTTSEVWLIDGLSPWDPPVLIQKRIHGVLYYVEHRDDELYILTNVGEPTEFKLMRTAADTPAIMNWDLFFTMKRNTKVIDLDMFKDHCVLFLKHSNLLYVNVIGLADDSVRSLKLPPWACGFIMDTNSDPKNCPFQLCSPIRPPKYYTYKFAEGKLFEETGHEDPITKTSRVLRLEAKSKDGKLVPMTVFHKTDSEDLQKKPLLVHVYGAYGMDLKMNFRPERRVLVDDGWILAYCHVRGGGELGLQWHADGRLTKKLNGLADLEACIKTLHGQGFSQPSLTTLTAFSAGGVLAGALCNSNPELVRAVTLEAPFLDVLNTMMDTTLPLTLEELEEWGNPSSDEKHKNYIKRYCPYQNIKPQHYPSIHITAYENDERVPLKGIVSYTEKLKEAIAEHAKDTGEGYQTPNIILDIQPGGNHVIEDSHKKITAQIKFLYEELGLDSTSVFEDLKKYLKF
Protein: Stress-70 protein, mitochondrial (EC 3.6.4.10) (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (mtHSP70) (P48721)
Organism: Rattus norvegicus (Rat)
Function: Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:7811387}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P38646}. Cytoplasm {ECO:0000269|PubMed:17178908}. Mitochondrion matrix {ECO:0000269|PubMed:17178908}. Note=Found in a complex with HSPA9 and VDAC1 at the endoplasmic reticulum-mitochondria contact sites. {ECO:0000269|PubMed:17178908}.
Interaction partners:
- 60 kDa heat shock protein, mitochondrial
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Non-selective voltage-gated ion channel VDAC1
- Mitochondrial import inner membrane translocase subunit TIM44
- Cellular tumor antigen p53
- Parkinson disease protein 7 homolog
- GrpE protein homolog 1, mitochondrial
- DnaJ homolog subfamily A member 3, mitochondrial
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Mitochondrial import inner membrane translocase subunit Tim17-A
Sequence:
MISASRAAAARLVGTTASRSPAAARHQDGWNGLSHEAFRFVSRRDYASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTPDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSSTGEQKEDQKEEKQ
Protein: Corneodesmosin (A0A1U9X8X8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGSSRAPWMGRVGGHGMLALLLAGLLLPGTLAKSIGTFSDPCKDPTRITSPNDPCLTGKGDSSGFSSYSGSSSSGSSISSARSSGGGSSGSSSGSSIAQGGSAGSFKPGTGYSQVSYSSGSGSSLQGASGSSQLGSSSSHSGSSGSHSGSSSHSSSSSSFQFSSSSFQVGNGSALPTNDNSYRGILNPSQPGQSSSSSQTFGVSSSGQSVSSNQRPCSSDIPDSPCSGGPIVSHSGPYIPSSHSVSGGQRPVVVVVDQHGSGAPGVVQGPPCSNGGLPGKPCPPITSVDKSYGGYEVVGGSSDSYLVPGMTYSKGKIYPVGYFTKENPVKGSPGVPSFAAGPPISEGKYFSSNPIIPSQSAASSAIAFQPVGTGGVQLCGGGSTGSKGPCSPSSSRVPSSSSISSSSGLPYHPCGSASQSPCSPPGTGSFSSSSSSQSSGKIILQPCGSKSSSSGHPCMSVSSLTLTGGPDGSPHPDPSAGAKPCGSSSAGKIPCRSIRDILAQVKPLGPQLADPEVFLPQGELLDSP