wanglab/gogpt-training-data huggingface dataset:
Protein: Methylthioalkylmalate synthase 3, chloroplastic (EC 2.3.3.17) (2-isopropylmalate synthase 2) (Methylthioalkylmalate synthase-like) (Q9FN52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17369439}.
Interaction partners:
- 3-isopropylmalate dehydratase small subunit 2
- 3-isopropylmalate dehydratase small subunit 3
- Methionine aminotransferase BCAT4
- 3-isopropylmalate dehydrogenase 1, chloroplastic
- 3-isopropylmalate dehydratase large subunit, chloroplastic
- 3-isopropylmalate dehydratase small subunit 1
- 3-isopropylmalate dehydrogenase 3, chloroplastic
- Cytochrome P450 83A1
- Branched-chain-amino-acid aminotransferase 3, chloroplastic
- Dihydroxy-acid dehydratase, chloroplastic
Sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
Protein: Centrin 2 (B6EUB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MANYMSEAAQLRRGLKPKGKTYGLTNQKRREIREIFDLFDIDGSGSIDASELNVAMRSLGFEMNNQQINELMAEVDKNQSGAIDFDEFVHMMTTKFGERDSIDELSKAFKIIDHDNNGKISPRDIKMIAKELGENFTDNDIEEMIEEADRDKDGEVNLEEFMKMMKRTSYG
Protein: Universal stress protein A family protein C25B2.10 (O74782)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Barrier septum {ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSESAPAGSKEGVSFGNLPRPEPRTSKDQQKLSISTDVKKPSHSAPVTPVRSARSSMEQPTFRPVAKNSVTVAPARAAGFCPPQFEEYHHGRSHSLVSPPPSPHFLKRISFDTFNNKAATDFSLTLKTQHQAYKWTRTSRTFLCGMDGNSYSEVAVDWLFETLLADNDEAVVLRVIDPSSKLAEDLSDEQSYRSLAEHIMAGILKKVDDDKAVSIIVELVVGKPQDMILRTIHVYSPDSLIVGTRGKALNSFQSLLSSGSVSKFCLQKSPIPVIVVRPDRKRVRSKNKRLKDKTRKSYMEILEKSGR
Protein: Mitochondrial carrier homolog 2 (Met-induced mitochondrial protein) (Q791V5)
Organism: Mus musculus (Mouse)
Function: Protein insertase that mediates insertion of transmembrane proteins into the mitochondrial outer membrane. Catalyzes insertion of proteins with alpha-helical transmembrane regions, such as signal-anchored, tail-anchored and multi-pass membrane proteins. Does not mediate insertion of beta-barrel transmembrane proteins (By similarity). Also acts as a receptor for the truncated form of pro-apoptotic BH3-interacting domain death agonist (p15 BID) and has therefore a critical function in apoptosis. Regulates the quiescence/cycling of hematopoietic stem cells (HSCs). Acts as a regulator of mitochondrial fusion, essential for the naive-to-primed interconversion of embryonic stem cells (ESCs). Acts as a regulator of lipid homeostasis and has a regulatory role in adipocyte differentiation and biology.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:15899861, ECO:0000269|PubMed:20436477}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Glucosamine-6-phosphate deaminase 2
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Neuronal growth regulator 1
- BTB/POZ domain-containing protein KCTD15
- Non-selective voltage-gated ion channel VDAC2
Sequence:
MADAASQVLLGSGLTILSQPLMYVKVLIQVGYEPLPPTIGRNIFGRQVCQLPGLFCYAQHIASIDGRRGLFTGLTPRLCSGVLGTVVHGKVLQYYQESEKPEELGSVTVQKEYSSSFDRVIKETTREMIARSAATLITHPFHVITLRSMVQFIGRESKYCGLCDSIVTIYREEGIVGFFAGLIPRLLGDIISLWLCNSLAYLINTYALDSGVSTMNEMKSYSQAVTGFFASMLTYPFVLVSNLMAVNNCGLAGGSPPYSPIYTSWIDCWCMLQKAGNMSRGNSLFFRKVPCGKTYCYDLRMLI
Protein: Phosphodiesterase (EC 3.1.4.-) (Q76KC5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Adenine phosphoribosyltransferase
- GTP:AMP phosphotransferase AK3, mitochondrial
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Adenosine kinase
- Phosphodiesterase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Deoxycytidine kinase
- Adenylosuccinate lyase
- Adenylate kinase 9
- Adenylate cyclase type 9
Sequence:
MRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQTRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKKLCCTTDSSKQIHRIHRDSGDNSQTEPHSFRHKSRRKESIDVKSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLEILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHHSHSHLSMPITINDVPPSIAQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCTETTLRAWLQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPLAAESEGSDCECNPTGKNFPENQILIKRMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSNS
Protein: UPF0390 protein C24B10.18 (Q9P7I8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MAQGEFKKKKNSSANKGGRVTKHSKNPKKGARYCAPRRAAAIKDHTINANITKTLNVRNEKLIAGIASQQVGKLTITKALGEAGAKELKEGKH
Protein: Thyroid hormone receptor beta (Nuclear receptor subfamily 1 group A member 2) (c-erbA-2) (c-erbA-beta) (P18113)
Organism: Rattus norvegicus (Rat)
Function: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.
Subcellular location: Nucleus.
Interaction partners:
- Nuclear receptor corepressor 1
- Nuclear receptor corepressor 2
- Nuclear receptor coactivator 2
- Retinoic acid receptor RXR-alpha
- Retinoic acid receptor RXR-gamma
- Nuclear receptor coactivator
- Mediator of RNA polymerase II transcription subunit 1
Sequence:
MTPNSMTENRLPAWDKQKPHPDRGQDWKLVGMSEACLHRKSHVERRGALKNEQTSSHLIQATWASSIFHLDPDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKSLHPSYSCKYEGKCIIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGQVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPDSETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED
Protein: Chaperonin containing TCP1 subunit 6B (Chaperonin containing Tcp1, subunit 6B (Zeta 2)) (Q6AYJ7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- Chaperonin containing TCP1 subunit 8 like 2
- Bardet-Biedl syndrome 10
- McKusick-Kaufman syndrome protein, isoform CRA_b.
Sequence:
MAAIKIANPGAEVTRSQAALAVNICAARGLQDVLRPSLGPKGALKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASIIAKVAAAQDHITGDGTTSNVLIIGELLKQADLYISEGLHPRIIAEGFDVAKTKALEVLDKIKVQKEMKREMLLDVARTSLRTKVHTELADILTEAVVDSVLAIRRPGIPIDLFMVEIVEMRHKSETDTQLVRGLVLDHGARHPRMKKQVQDAYILICNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKVCAESNKGFVVINQKGIDPVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSLEDLSEECLGHAGLVFEYTLGEEKFTFIEDCVNPLSVTLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHCVQGRARLGIQAFADALLIIPKVLAQNSGYDLQETLIKIQTKHAESKELVGIDLNTGEPMVAAEAGIWDNYCVKKHILHSCTVIATNVLLVDEIMRAGMSSLRE
Protein: COMM domain containing 9 variant (COMM domain containing 9, isoform CRA_b) (cDNA FLJ31106 fis, clone IMR322000144, highly similar to COMM domain-containing protein 9) (cDNA FLJ78335, highly similar to Homo sapiens COMM domain containing 9, mRNA) (cDNA, FLJ95283, highly similar to Homo sapiens COMM domain containing 9 (COMMD9), mRNA) (Q53FR9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAALTAEHFAALQSLLKASSKDVVRQLCQESFSSSALGLKKLLDVTCSSLSVTQEEAEELLQALHRLTRLVAFRDLSSAEAILALFPENFHQNLKNLLTKIILEHVSTWRTEAQANQISLPRLVDLDWRVDIKTSSDSISRMAVPTCLLQMKIQEDPSLCGDKPSISAVTVELSKETLDTMLDGLGRIRDQLSAVASK
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (F4HVJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSVTAAFIDSDQTQHNILMDSQSTVSGVKTVKISNVSLIVSKKDVKEFFSFSGDIQYVEMRSETQESQVAYVTFKDSQGAETAMLLTGAVIADLRVSITPAVNYQLPPEALALDSQEHSFNGFSVKKAEDVVNIMVGRGYALGKDAMEKAKAFDDRHNLISNASATIASLDDKMGLSEKLSIGTTVVNEKLRDIDERYQVREITKSALAAAEETAISARTALMANPYVSSGASWFSNAFGAVTKAVKEKVENGGEGRKEIITLDPSSPKVPAVVPVKLG
Protein: argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate ligase) (Q5T6L4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKDGTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYILGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK
Protein: Interferon induced transmembrane protein 5 (G3V7W9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Cartilage associated protein
- Cartilage associated protein
Sequence:
MDTSYPREDPRAPSSRKADAAAHTALSVGTPGPTPRDHMLWSVFSTLYLNLCCLGFLALVHSVKARDKKVAGDLEAAKQYGSKAKCYNILAAMWTLVPPLLLLGLVVTGALHLSRLAKDSAAFFSTKFDEEDYN
Protein: Serine/threonine-protein kinase PAK 5 (EC 2.7.11.1) (p21-activated kinase 5) (PAK-5) (p21-activated kinase 7) (PAK-7) (Q8C015)
Organism: Mus musculus (Mouse)
Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the mitochondria, and mitochondrial localization is essential for the role in cell survival. {ECO:0000250}.
Interaction partners:
- Cell division control protein 42 homolog
- SH2/SH3 adapter protein Nck1
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 3
- Rho guanine nucleotide exchange factor 7
- Roundabout homolog 2
- Rho guanine nucleotide exchange factor 6
- Cytoplasmic protein NCK2
- Roundabout homolog 1
- LIM domain kinase 1
Sequence:
MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCITPIQLAPMKTIVRGNKSCKETSINGLLEDFDNISVTRSNSLRKESPPTPDQGAASRIQGHSEENGFITFSQYSSESDTTADYTTEKYRDRSLYGDDLDLYYKSSHAAKQNGHAMKMKHGDAYYPEMKSLKTDLAGFPVDYHTHLDSLRKSSEYGDLRWDYQRASSSSPLDYSFQLTPSRTAGTSRCSKESLAYSESDWGPSLDDYDRRPKSSYLHQTSPQPAMRQRSKSGSGLQEPMMPFGASAFKTHPQGHSYNSYTYPRLSEPTMCIPKVDYDRAQMVFSPPLSGSDTYPRGPTKLPQSQSKAGYSSGSHQYPSGYHKASLYHHPSLQTSSQYISTASYLSSLSISSSTYPPPSWGSSSDQQPSRVSHEQFRAALQLVVSPGDPREYLDNFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHDNVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLKALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDSLPPRVKDLHKVSSMLRGFLDLMLVREPSQRATAQELLGHPFLKLAGPPSCIVPLMRQYRHH
Protein: Coupling of ubiquitin conjugation to ER degradation protein 1 (Kinetochore-defect suppressor 4) (P38428)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum membrane where it functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme UBC7 to the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and to the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has also a role in cold adaptation, perhaps through effects on sterol biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Single-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 7
- ERAD-associated E3 ubiquitin-protein ligase DOA10
- U1 SNP1-associating protein 1
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- Degradation in the endoplasmic reticulum protein 1
- UBX domain-containing protein 2
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- Cell division control protein 48
- Nuclear protein localization protein 4
- Protein OS-9 homolog
Sequence:
MEDSRLLITLILVFGVIFLKKFFQSNQHPSAQRLSATGVNAHGRPQGSTQNALRRTGRVNGGHPVTTQMVETVQNLAPNLHPEQIRYSLENTGSVEETVERYLRGDEFSFPPGFEPSRAPMGANAAVDNNAAGGGEFNDPRKKNMICAENLLDKFHVDLNEDMSNLSFKDLDIEERKRLLVWQARKNLETKLQSDKDLQSLLT
Protein: AP-3 complex subunit sigma-2 (AP-3 complex subunit sigma-3B) (Adaptor-related protein complex 3 subunit sigma-2) (Sigma-3B-adaptin) (Sigma3B-adaptin) (Sigma-adaptin 3b) (P59780)
Organism: Homo sapiens (Human)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit delta-1
- AP-3 complex subunit mu-1
- AP-3 complex subunit mu-2
- AP-3 complex subunit beta-1
- AP-2 complex subunit alpha-1
- AP-3 complex subunit beta-2
- AP-4 complex subunit epsilon-1
- AP-4 complex subunit mu-1
- AP-5 complex subunit sigma-1
- AP-5 complex subunit mu-1
Sequence:
MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLEKSEGGLSAAPARAVSAVKNINLPEIPRNINIGDLNIKVPNLSQFV
Protein: Acetyl-CoA:oxalate CoA-transferase (ACOCT) (EC 2.8.3.19) (Acetyl-coenzyme A transferase) (CoA:oxalate CoA-transferase) (P76518)
Organism: Escherichia coli (strain K12)
Function: Involved in the catabolism of oxalate and in the adapatation to low pH. ACOCT serves to prime the oxalate-induced acid tolerance response (ATR) cycle by producing substrate for oxalyl-CoA decarboxylase (OXC) and formyl-coenzyme A transferase (FCOCT). Catalyzes the reversible conversion of acetyl-CoA and oxalate to oxalyl-CoA and acetate. It can also use formyl-CoA and oxalate to produce oxalyl-CoA and formate with significantly reduced specific activity.
Interaction partners:
- Uncharacterized transporter YfdV
- Oxalyl-CoA decarboxylase
- Formyl-CoA:oxalate CoA-transferase
- Protein YfdX
- Citrate lyase subunit beta
- Probable multidrug resistance protein EmrY
- Uncharacterized protein YhiJ
- Probable multidrug resistance protein EmrK
- HTH-type transcriptional regulator YdeO
- Protein YdeP
Sequence:
MTNNESKGPFEGLLVIDMTHVLNGPFGTQLLCNMGARVIKVEPPGHGDDTRTFGPYVDGQSLYYSFINHGKESVVLDLKNDHDKSIFINMLKQADVLAENFRPGTMEKLGFSWETLQEINPRLIYASSSGFGHTGPLKDAPAYDTIIQAMSGIMMETGYPDAPPVRVGTSLADLCGGVYLFSGIVSALYGREKSQRGAHVDIAMFDATLSFLEHGLMAYIATGKSPQRLGNRHPYMAPFDVFNTQDKPITICCGNDKLFSALCQALELTELVNDPRFSSNILRVQNQAILKQYIERTLKTQAAEVWLARIHEVGVPVAPLLSVAEAIKLPQTQARNMLIEAGGIMMPGNPIKISGCADPHVMPGAATLDQHGEQIRQEFSS
Protein: DNA-directed RNA polymerase subunit Rpo6 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit K) (P39463)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00192}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo2
- DNA-directed RNA polymerase subunit Rpo11
- DNA-directed RNA polymerase subunit Rpo12
- DNA-directed RNA polymerase subunit Rpo10
- DNA-directed RNA polymerase subunit Rpo7
- DNA-directed RNA polymerase subunit Rpo5
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo1C
- DNA-directed RNA polymerase subunit Rpo1N
- DNA-directed RNA polymerase subunit Rpo4
Sequence:
MTIDKINEIFKENWKNKLTKYEIARIISARALQLSMGALPLIDTSNLKSDDVISIAEEELKRGVLPITIRRIYPNGQVELISVRKIENR
Protein: Nicotinamide-nucleotide amidohydrolase PncC (NMN amidohydrolase PncC) (EC 3.5.1.42) (NMN deamidase) (Nicotinamide-nucleotide amidase) (P0A6G3)
Organism: Escherichia coli (strain K12)
Function: Has nicotinamidemononucleotide (NMN) aminohydrolase activity, not active on other substrates.
Interaction partners:
- Nicotinate-nucleotide adenylyltransferase
- Trifunctional NAD biosynthesis/regulator protein NadR
- Nicotinate phosphoribosyltransferase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- NH
- NMN amidohydrolase-like protein YfaY
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Nucleoside triphosphate pyrophosphohydrolase
- Protein UshA
- 5'/3'-nucleotidase SurE
Sequence:
MTDSELMQLSEQVGQALKARGATVTTAESCTGGWVAKVITDIAGSSAWFERGFVTYSNEAKAQMIGVREETLAQHGAVSEPVVVEMAIGALKAARADYAVSISGIAGPDGGSEEKPVGTVWFAFATARGEGITRRECFSGDRDAVRRQATAYALQTLWQQFLQNT
Protein: Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1) (C8VRK6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component subunit alpha
- 2-oxoisovalerate dehydrogenase subunit alpha
- Probable mitochondrial E3-binding protein of the pyruvate dehydrogenase complex
- Glucose-6-phosphate isomerase
- Pyruvate kinase
- dihydrolipoyllysine-residue succinyltransferase
- Malic enzyme
- Malic enzyme
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MASLRLFRPAARLLSSRLSATRPTFPQTACTPSILRFRGYATENGTKEVTVRDALNEALAEELERNQKTFILGEEVAQYNGAYKVTRGLLDRFGPKRVIDTPITEAGFCGLAVGAALAGLHPICEFMTFNFAMQAIDQIINSAAKTHYMSGGIQPCNITFRGPNGFAAGVAAQHSQDYSAWYGSIPGLKVVAPWSAEDAKGLMKAAIRDPNPVVVLENELLYGQAFPMSEAAQKDDFVLPIGKAKIERPGKDLTIVSLSRCVGQSLNAAAELKQKYGVEAEVINLRSVKPLDVETIIQSLKKTGRLMCVESGFPMFGVSSEILALSMEYGFDYLTAPAVRVTGAEVPTPYAVGLETMSFPQEDTIVGQAAKLLRL
Protein: Cysteine-rich secretory protein (Q9D259)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAVKFILLLFVAAFVPVVTIRPLKLDRALYNKLITESQTEPQEEIVNTHNAFRRKVSPPARNMLKVSWSSAAAENARILARYCDKSDSDSLERRLPNTFCGENMLMEHYPSSWSKVIEIWFNESKYFKYGEWPSTDDDIETDHYTQMVWASTYLVGCDVAACRRQKAATYLYVCHYCHEGNHQDTLNMPYKEGSPCDDCPNNCEDGLCTNPCIYYDEYNNCDTQVKLYGCSHPAVQPFCKASCLCTTEIK
Protein: SH3 domain-binding glutamic acid-rich-like protein 2 (Q8BG73)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MVVRVFVASCSGFVAIKKKQQDVVRFLEANKIEFEEVDITMSEEQRQWMYKNIPPEKKPAQGNPLPPQIFNGDRYCGDYDSFFESKESNTVFSFLGLKPRPASTAEP
Protein: Copper transport protein ATOX1 (Metal transport protein ATX1) (O00244)
Organism: Homo sapiens (Human)
Function: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
Interaction partners:
- Copper-transporting ATPase 1
- Copper-transporting ATPase 2
- Copper chaperone for superoxide dismutase
- Cytochrome c oxidase copper chaperone
- Superoxide dismutase
- Extracellular superoxide dismutase
- High affinity copper uptake protein 1
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- COMM domain-containing protein 1
- Protein SCO2 homolog
Sequence:
MPKHEFSVDMTCGGCAEAVSRVLNKLGGVKYDIDLPNKKVCIESEHSMDTLLATLKKTGKTVSYLGLE
Protein: ELMO domain-containing protein 3 (RNA-binding motif and ELMO domain-containing protein 1) (RNA-binding motif protein 29) (RNA-binding protein 29) (Q96FG2)
Organism: Homo sapiens (Human)
Function: Acts as a GTPase-activating protein (GAP) for ARL2 with low specific activity.
Subcellular location: Cell projection, stereocilium {ECO:0000269|PubMed:24039609}. Cell projection, kinocilium {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24039609, ECO:0000269|PubMed:29713870}. Note=Also present in the cuticular plate of auditory hair cells. Expressed along the length of the stereocilia, but excluded from the very tip (By similarity). Colocalizes with F-actin cytoskeleton. {ECO:0000269|PubMed:29713870}.
Interaction partners:
- ELMO domain-containing protein 1
Sequence:
MNEKSCSFHSKEELRDGQGERLSAGYSPSYDKDKSVLAFRGIPISELKNHGILQALTTEAYEWEPRVVSTEVVRAQEEWEAVDTIQPETGSQASSEQPGQLISFSEALQHFQTVDLSPFKKRIQPTIRRTGLAALRHYLFGPPKLHQRLREERDLVLTIAQCGLDSQDPVHGRVLQTIYKKLTGSKFDCALHGNHWEDLGFQGANPATDLRGAGFLALLHLLYLVMDSKTLPMAQEIFRLSRHHIQQFPFCLMSVNITHIAIQALREECLSRECNRQQKVIPVVNSFYAATFLHLAHVWRTQRKTISDSGFVLKELEVLAKKSPRRLLKTLELYLARVSKGQASLLGAQKCYGPEAPPFKDLTFTGESDLQSHSSEGVWLI
Protein: 26S proteasome regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4) (Proteasome 26S subunit ATPase 6) (Proteasome subunit p42) (P62333)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC6 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-1
- Proteasomal ubiquitin receptor ADRM1
- Proteasome subunit beta type-6
- 26S proteasome non-ATPase regulatory subunit 6
- Proteasome subunit beta type-5
- Proteasome subunit beta type-4
- Proteasome subunit beta type-7
- Proteasome subunit alpha type-7
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 4
Sequence:
MADPRDKALQDYRKKLLEHKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADSKKLESKLDYKPV