wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc-type alcohol dehydrogenase-like protein C1773.06c (EC 1.-.-.-) (O94564)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 2-hydroxyacid dehydrogenase homolog 2
- Probable L-lactate dehydrogenase
- Putative glutathione S-transferase C1183.02
- Uncharacterized oxidoreductase C663.06c
- UPF0591 membrane protein C15E1.02c
- Uncharacterized sulfatase PB10D8.02c
- UPF0300 protein C737.04
- Uncharacterized oxidoreductase C4H3.08
Sequence:
MALRYVVHDEISGFDQLKPEEYEVPQKLNPGEVLVKLKAASLNYRDLIITKGLYPLPLQLPVVPGSDGAGIIEKVGEDVEGFEKGDSVVCNFFTNYLDGTPTDFATHSALGGTRDGCFQKYAVLPAHALVHAPKNLSFEEIATLPCAAVTAWNGLFGSKEHQVKPGNNVLVLGTGGVSTFALQFALAAGANVTVTSSSDEKLEFAKKLGATHTINYKKTPQWASPALKMTNGVGYHHVIEVGGEKTLPQSIACLAKDGMISMIGFVASEGTTPNLTSIIGQILNRNANIRGIFVGSVSMFRDMVACIEAKDIHPVVDKVFPFDQLKEAYEYQWSQAHIGKVVLKID
Protein: Thioredoxin-like 4, chloroplastic (Lilium-type thioredoxin 3) (Q9C5C5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Transcription regulator
- Transcription regulator NOT2/NOT3/NOT5 family protein
- AT5g35440/MOK9_2
- Cell differentiation, Rcd1-like protein
- Cell differentiation, Rcd1-like protein
- Cell differentiation, Rcd1-like protein
- CCR4-NOT transcription complex subunit 11
- Glutaminyl-peptide cyclotransferase
- Ribosomal RNA-processing protein 42
- Transmembrane protein
Sequence:
MSSLLNISHCSYHGYSGLTSRGGINTVENHRWVWHNNGVRLSFPRAESSINITMGCTLQRGIAKSLSQENLVELSDENDDLCPVECVTEFKTDDELLSVLEKSKETNSLVVVDFYRTACGSCKYIEQGFSKLCKQSGDQEAPVIFLKHNVVDEYDEQSEVAERLRIKAVPLFHFYKNGVLLESFATRDKERIDAAILKYTSSES
Protein: Uncharacterized protein (Q582Y2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MILSEGVPMTNGEVFSLLRRRRDERNGKHQPSFGLQFLGNSSIAQQQSQRITAPKAGSQSMATATQSNFFYPPDAVLKSSEASYSGFMSTPPVGLLNPPKNSALLASPAASHLVVLLTEVRVLRYLSRYSTISGNDGVRAIYGPSSIYNRQPCRLRTACASRLEAHADEQAENQQLAPAAACENEEGRNEDSVDKSIGAFDDSVQAEALRLLEKHRPGTVGHVRGMESLLSLWEQQGRDAERESAARLNVVLRELQRRVGVANQNGDESPASGKDEGKWHERRPVEDRARKLFAQPTVPLAMFLSDQHPVASGASAGRLSRGGVTFIDAATPEPRRRQWTEQDVMQLVIARPKNSLDVYRVVEDLEQYTGDNEELSAFLEKGILEAFA
Protein: Gamma-secretase subunit PEN-2 (Presenilin enhancer protein 2) (Q9CQR7)
Organism: Mus musculus (Mouse)
Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (Probable). PSENEN modulates both endoproteolysis of presenilin and gamma-secretase activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12522139}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12522139}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Cell membrane {ECO:0000250|UniProtKB:Q9NZ42}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Membrane {ECO:0000250|UniProtKB:Q9NZ42}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Note=Predominantly located in the endoplasmic reticulum and in the cis-Golgi. {ECO:0000269|PubMed:12522139}.
Interaction partners:
- Putative gamma-secretase subunit APH-1C
- Gamma-secretase subunit APH-1B
- Presenilin-1
- Gamma-secretase subunit APH-1A
- Presenilin-2
- Nicastrin
- Transmembrane emp24 domain-containing protein 10
- Neurogenic locus notch homolog protein 1
- Amyloid-beta precursor protein
- Tumor necrosis factor
Sequence:
MNLERVSNEEKLNLCRKYYLGGFAFLPFLWLVNIFWFFREAFLAPAYTEQSQIKGYVWRSAVGFLFWVIILATWITIFQIYRPRWGALGDYLSFTIPLGTP
Protein: Spermidine N(1)-acetyltransferase (SAT) (EC 2.3.1.57) (Spermidine/spermine N(1)-acetyltransferase) (SSAT) (P0A951)
Organism: Escherichia coli (strain K12)
Function: Involved in the protection against polyamine toxicity by regulating their concentration. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine. It can also use spermine, but not putrescine.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- UPF0482 protein YnfB
- Polyamine aminopropyltransferase
- Gamma-glutamylputrescine synthetase PuuA
- Constitutive ornithine decarboxylase
- Putrescine aminotransferase
- Agmatinase
- Inducible ornithine decarboxylase
- Putrescine importer PuuP
Sequence:
MPSAHSVKLRPLEREDLRYVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQYRNAIRMCIFQHQYLAEHKTPGQTLLKPTAQ
Protein: Exosome-associated protein 4 (Q383H5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ribosomal RNA processing protein 4
- Ribosomal RNA-processing protein 43
- Ribosomal RNA processing protein 45
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Exosome complex exonuclease RRP40
- Exosome component CSL4
- Ribosomal RNA processing protein 6
- ATP-dependent DEAD/H RNA helicase, putative
- Ribosomal RNA-processing protein 44
- Mitochondrial exoribonuclease DSS-1
Sequence:
MERSHGRRSPDEVRYPHIVLNVLGQSYSSACIEVGSTRVVCAVHHPQQLIDEYRGSRGRVACTVRRSSRAQKHELAFRADVTPEKDLALALEGVVEQAVVLEKIPQLLVEVAVEILAEDGGLWDAIATGVCAALASGGFEMYDTFSACGAALLPDGSIVTDPSATEWNTAKATAVTCAMLNSGNMCFTAQRGSCEPTTALDLVMAALKGTLARKNVISSQLCEQFAF
Protein: LPG5B protein (UDP-galactose transporter) (Q5QHQ6)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Lipophosphoglycan biosynthetic protein
- Beta galactofuranosyl transferase
Sequence:
MALIVHVFSMAMVSLVVLVVQNSLLVVMTRFSRKSVDAAHNYHTSTLVMNQEIAKMIMCLVLYGLDDVYRQYRRDAASSNCANNAVHKMVGLEVDVLLLREDSVNDVERKACQAGDKEAQPLADEEPLEVHIHSSPVSLPQTMTVSNASGEGVRRVADEFGASHDAPGVPQVTSTHDSSKILGIAALFDRQPRQPPYLTSSDRPNNASANAKTRAAGHDEWSCSVDVPEKMRKRSFFMYRRMKTLCSLYCSMLSASVYKRDTLKLFVPAFLFNIQNFLIFIGLSNLDAVSFQIWSQTKLLSTAIFSVWLLGRKLSPMQWLSLVTLTAGVLGAQLGAPRASTEMLATAAPHLLHGTTTVPGLDRVGELRAGDDDESRGSALIGIAACVLSGLSSSYASVYFEKVVKTTSPTLSIRNIQLSLFGIPIAFVSMLILAVFPNWYSSVQCGQRVHWNIFSPPAAEARTLGTAKAYCPVRPFFFWQRYDHFLTWALVFIHALGGLLVAIVVKYADNILKGFATGIAVIVSGMMCSAIDRYELSLAFVLGAVFVIGSSIAFHTFEPKR
Protein: DNA mismatch repair protein Mlh3 (MutL protein homolog 3) (Q9UHC1)
Organism: Homo sapiens (Human)
Function: Probably involved in the repair of mismatches in DNA.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA mismatch repair protein Msh6
- DNA mismatch repair protein Mlh1
- DNA mismatch repair protein Msh3
- DNA mismatch repair protein Msh2
- Exonuclease 1
- MutS protein homolog 4
- Mismatch repair endonuclease PMS2
- PMS1 protein homolog 1
- MutS protein homolog 5
- DNA polymerase delta catalytic subunit
Sequence:
MIKCLSVEVQAKLRSGLAISSLGQCVEELALNSIDAEAKCVAVRVNMETFQVQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENPRFYGFRGEALANIADMASAVEISSKKNRTMKTFVKLFQSGKALKACEADVTRASAGTTVTVYNLFYQLPVRRKCMDPRLEFEKVRQRIEALSLMHPSISFSLRNDVSGSMVLQLPKTKDVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISSEAHYNKNMQFLFVNKRLVLRTKLHKLIDFLLRKESIICKPKNGPTSRQMNSSLRHRSTPELYGIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEGVKMFLKQEKLFVELSGEDIKEFSEDNGFSLFDATLQKRVTSDERSNFQEACNNILDSYEMFNLQSKAVKRKTTAENVNTQSSRDSEATRKNTNDAFLYIYESGGPGHSKMTEPSLQNKDSSCSESKMLEQETIVASEAGENEKHKKSFLEHSSLENPCGTSLEMFLSPFQTPCHFEESGQDLEIWKESTTVNGMAANILKNNRIQNQPKRFKDATEVGCQPLPFATTLWGVHSAQTEKEKKKESSNCGRRNVFSYGRVKLCSTGFITHVVQNEKTKSTETEHSFKNYVRPGPTRAQETFGNRTRHSVETPDIKDLASTLSKESGQLPNKKNCRTNISYGLENEPTATYTMFSAFQEGSKKSQTDCILSDTSPSFPWYRHVSNDSRKTDKLIGFSKPIVRKKLSLSSQLGSLEKFKRQYGKVENPLDTEVEESNGVTTNLSLQVEPDILLKDKNRLENSDVCKITTMEHSDSDSSCQPASHILNSEKFPFSKDEDCLEQQMPSLRESPMTLKELSLFNRKPLDLEKSSESLASKLSRLKGSERETQTMGMMSRFNELPNSDSSRKDSKLCSVLTQDFCMLFNNKHEKTENGVIPTSDSATQDNSFNKNSKTHSNSNTTENCVISETPLVLPYNNSKVTGKDSDVLIRASEQQIGSLDSPSGMLMNPVEDATGDQNGICFQSEESKARACSETEESNTCCSDWQRHFDVALGRMVYVNKMTGLSTFIAPTEDIQAACTKDLTTVAVDVVLENGSQYRCQPFRSDLVLPFLPRARAERTVMRQDNRDTVDDTVSSESLQSLFSEWDNPVFARYPEVAVDVSSGQAESLAVKIHNILYPYRFTKGMIHSMQVLQQVDNKFIACLMSTKTEENGEAGGNLLVLVDQHAAHERIRLEQLIIDSYEKQQAQGSGRKKLLSSTLIPPLEITVTEEQRRLLWCYHKNLEDLGLEFVFPDTSDSLVLVGKVPLCFVEREANELRRGRSTVTKSIVEEFIREQLELLQTTGGIQGTLPLTVQKVLASQACHGAIKFNDGLSLQESCRLIEALSSCQLPFQCAHGRPSMLPLADIDHLEQEKQIKPNLTKLRKMAQAWRLFGKAECDTRQSLQQSMPPCEPP
Protein: phosphoenolpyruvate carboxylase (EC 4.1.1.31) (A9QED9)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MASFNNNNNGKFEKLASIDAQLRQLVPAKVSEDDKLVEYDALLLDRFLDILQDLHGEDLKETVQECYELSAEYEGKSTPKKLEELGNVLTSLDPGDSIVIAKAFSHMLNLADLAEEVQIAYRRRIKLKKGDFADENSATTESDIEETLKRLVVDLKKSPEEVFDALKNQTVDLVFTAHPTQSVRRSLLQKHGRIRNCLAQLYAKDITPDDKQELDEALQREIQAAFRTDEIRRTPPTPQDEMRAGMSYFHETVWKGVPKFLRRVDTALKNIGINERVPYNAPLIQFSSWMGGDRDGNPRVAPEVTRDVCLLARMMAANLYYSQIEDLMFELSMWRCSDELRVRADELHRSSRRDAKHYIEFWKKVPPNEPYRVILGDVRDKLYQTRERSRQMLSHGISDIPEEETFTNIEQFLEPLELCYRSLCSCGDRPIADGSLLDFLRQVSTFGLSLVRLDIRQESDRHTDVLDAITKHLEIGSCREWSEEQKQEWLLSELGGRRPLFGPDLPKTEEIADVLDTFSVLAELPADNFGAYIISMATAPSDVLAVELLQRECHVKQPLRVVPLFEKLADLEAAPAALARLFSIDWYRNRINGKQEVMIGYSDSGKDAGRLSAAWQLYKAQEELINVAKEFGVKLTMFHGRGGTVGRGGGPTHLAILSQPPETIHGSLRVTVQGEVIEQSFGEEHLCFRTLQRFTAATLEHGMHPPVSPKPEWRALMDEMAVVATEEYRSIVFKEPRFVEYFRLATPELEYGRMNIGSRPSKRKPSGGIESLRAIPWIFAWTQTRFHLPVWLGFGAAFKHVIQKDIKNLLMLQEMYNEWPFFRVTIDLVEMVLAKGDPGIAALYDKLLVSEELWSFGERLRTNFEETKSLLLQIAGHKDLLEGDPYLKQRLRLRDSYITTLNVCQAYTLKRIRDPNYSVKLRPHISREIMESSKPADELVKLNPTSEYAPGLEDTLILTMKGIAAGMQNTG
Protein: Probable prefoldin subunit 2 (Q9VTE5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity).
Interaction partners:
- Probable prefoldin subunit 5
- Prefoldin subunit 3
- Probable prefoldin subunit 6
- Probable prefoldin subunit 4
- GEO07746p1
- IP05962p
- GEO12025p1
- Prefoldin subunit 3
- IP21091p
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
Sequence:
MSTESAKPALSQEAIVAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDFIAKTIQMVTNDLSKKGSELNKFKEEHNIKIRGEHLVAEGAKGDDAEDKAENRNVLVFN
Protein: L-malyl-CoA/beta-methylmalyl-CoA lyase (EC 4.1.3.24) ((3S)-malyl-CoA/beta-methylmalyl-CoA lyase) ((S)-citramalyl-CoA lyase) (EC 4.1.3.25) (Q3J5L6)
Organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides)
Function: Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to yield beta-methylmalyl-CoA. It is also able to catalyze the cleavage of (S)-citramalyl-CoA to yield acetyl-CoA and pyruvate, although this reaction is not involved in the ethylmalonyl-CoA pathway.
Interaction partners:
- Mesaconyl-CoA hydratase
- (3S)-malyl-CoA thioesterase ((3S)-malyl-CoA thiolesterase)
- Phosphate acetyltransferase
- propionyl-CoA carboxylase
- 2-hydroxyacid dehydrogenase
- Propionyl-CoA carboxylase beta chain
- Malate synthase G
- Acetyl-coenzyme A synthetase
- Serine-pyruvate aminotransferase/aspartate aminotransferase
- D-isomer specific 2-hydroxyacid dehydrogenase
Sequence:
MSFRLQPAPPARPNRCQLFGPGSRPALFEKMAASAADVINLDLEDSVAPDDKAQARANIIEAINGLDWGRKYLSVRINGLDTPFWYRDVVDLLEQAGDRLDQIMIPKVGCAADVYAVDALVTAIERAKGRTKPLSFEVIIESAAGIAHVEEIAASSPRLQAMSLGAADFAASMGMQTTGIGGTQENYYMLHDGQKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDEGFRAQARRSATLGMVGKWAIHPKQVALANEVFTPSETAVTEAREILAAMDAAKARGEGATVYKGRLVDIASIKQAEVIVRQAEMISA
Protein: Calponin-2 (Calponin H2, smooth muscle) (Neutral calponin) (Q08093)
Organism: Mus musculus (Mouse)
Function: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
Interaction partners:
- WD repeat-containing protein 90
- Filamin-A
Sequence:
MSSTQFNKGPSYGLSAEVKNRLLSKYDPQKEAELRSWIEGLTGLSIGPDFQKGLKDGVILCTLMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMNPVDLFEANDLFESGNMTQVQVSLLALAGKAKTKGLQSGVDIGVKYSEKQERNFDDATMKAGQCVIGLQMGTNKCASQSGMTAYGTRRHLYDPKNHILPPMDHCTISLQMGTNKCASQVGMTAPGTRRHIYDTKLGTDKCDNSSMSLQMGYTQGANQSGQVFGLGRQIYDPKYCPQGSAADGAPAGDGQGEAPEYLAYCQEEAGY
Protein: Short transmembrane mitochondrial protein 1 (B3DFW5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Microprotein involved in mitochondrial respiratory chain complex III (ubiquinol-cytochrome c oxidoreductase) and complex IV (mitochondrial cytochrome c oxidase complex) assembly (By similarity). Required for the formation of mitochondrial supercomplexes (SCs) (By similarity). Also required for the activation of the NLRP3 inflammasome (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:E0CX11}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0DP99}; Single-pass membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P0DP99}.
Interaction partners:
- Ras and Rab interactor 3
- Dihydropyrimidinase
Sequence:
MMQFILGFTLGNVVGMYLAQNYEVPNISKKIEAFKKDVEAKKKPPE
Protein: Heterogeneous nuclear ribonucleoprotein H/F, putative (Q586X0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- RNA-binding protein, putative
- Nuclear cap-binding protein subunit 2
- Splicing factor TSR1
Sequence:
MEQSPEQQQQQQQRSQSPRPEGAAVLRLYGLPYSIKEEKIREFFGSFSLADEEPIVFFVEGLHRGTGFVRLRNAEDAALAINRLHRQNIDETRYVEISTSSEEERQRIMEQQEQSNKACVLRLRGLPFAATEDDVRTFIESMEGVLSIDICRDMDGRNTGDAFIELASEEDVKRVKLLHSKAMGNRYIEVLPSTVYDRDAIMRASSQRSRRGRRSGRGYEISVTDGDVSHHQGHESMMVQRIIDPFVPTTYEGYMQPLGFGGQRPFHHQYHNNHHHAQHHSAQMQNYYHNHQHHRQAQQFHHYSPHNNSFMNPRGGGDGRDVRYSMNNQPYRRFSDERGIVGGGGIVAEGPSAPYPPGAGGAPPPPFLPVFPGQSSLVVARQPSPFVVRIRGVPYSASEEAIAEFFAGVKIPPQGVHMVYDERNRLTGEAFVEVEDRNDVLLALDRNGAMMGTRYIEVFESSPAAMQRLGTAQMGMMSYPMVPQMFC
Protein: Parathyroid hormone-related protein (PTH-rP) (PTHrP) (Parathyroid hormone-like protein) (PLP) [Cleaved into: Osteostatin] (P22858)
Organism: Mus musculus (Mouse)
Function: Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport. Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth. Required for skeletal homeostasis. Promotes mammary mesenchyme differentiation and bud outgrowth by modulating mesenchymal cell responsiveness to BMPs. Up-regulates BMPR1A expression in the mammary mesenchyme and this increases the sensitivity of these cells to BMPs and allows them to respond to BMP4 in a paracrine and/or autocrine fashion. BMP4 signaling in the mesenchyme, in turn, triggers epithelial outgrowth and augments MSX2 expression, which causes the mammary mesenchyme to inhibit hair follicle formation within the nipple sheath.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}.
Interaction partners:
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Parathyroid hormone
- Parathyroid hormone 2 receptor
- Indian hedgehog protein
- Importin subunit beta-1
- Tumor necrosis factor ligand superfamily member 11
- Guanine nucleotide-binding protein G
- Runt-related transcription factor 2
- Tuberoinfundibular peptide of 39 residues
- Protein patched homolog 1
Sequence:
MLRRLVQQWSVLVFLLSYSVPSRGRSVEGLGRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPAPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRREQEKKKRRTRSAWPSTAASGLLEDPLPHTSRTSLEPSLRTH
Protein: Annexin (Q7JMT5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNSGGGYPNQQPSYGGYGQPPQQPGYGNGSYDPYGQPQQQPYPGGGGQPPYPGSNSNQGGGGYPGQGGAPYPGGSGGYPQAPQYGFSGGQGSAPQPNQGGYPPQQQQYPPQQGYQQGGQQQGGGGFFPNQGYGQPVMIGTPSVFPVQGFNSNADAEVLRKAMKGLGCNNSKVISILCQRTNWQRQEISKAFKVMYGKDLIKELKGELHGDFEDLILALMDAPAIYDAKQLHRAMEGLGTKESVLIEIMTSRTNAQIQQVRDAYKMLFKKDLERDLIGETSGHFKRLLVSLCAGGRDESSQTDGLRANQDARRLLQAGEKRLGTDESTFNAILASQNFSQLRLVFEEYQKASNHSIEKAIEFEFSGDIRDGLLAVIAVIRNRPAYFAKLLHDSMKGLGTRDNDLIRLCVTRAEYDMGDIRNMFQSLYRTSLENMIKGDCSGAYKEGLIALVNGNRG
Protein: Cytochrome P450 (Q2UT04)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MIGTVLDTVLGNPQGAVGGLFVGSFVIFWVVPFLYNLFFSPLRNVPGPFWARFTILWEFSQLMKGRSHEEYIKLHKKYGPVVRVSPKRYSVIDPQDVKKIYGFGADFPKSEFYDSLGDPKNIFTVRDNEDHKDRRRKVASLYTMSSMVAYEDAVDRMTTLCIKKMTDLAASRKLISIPKFMQFYAFDVIGEITFDQNFGMMENMGDTQGIIKEIHAMNNTIGIMGLLPELQSTWRAAQKVLFSGTAMGKLTEYIWSQYWKHRNTNSGAKQKSQYDTFLRKVLELEAAHKVGRMNVLDSCGSNIGAGSDTTGITLSAALWYIYRNPDKLAKLRHEIDTMTAEGRISDPVTYKQAQEMPYLNAVIKETLRVHPGVGTILARVVPKGGITLTGGYYVPEGTHIGTNAWPLHYSETVYGPDADQYRPERWLEDKPQPDYRDSMMFAFGSGSRTCIGRNISLLEITKVLPQIVRKFDLKFEEKKDPWDAWCAWFVYPKYKCWIEPRKPVENVA
Protein: RNA-binding region RNP-1 domain-containing protein (Q55CI7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Splicing factor 3A subunit 2
- PSP proline-rich domain-containing protein
- Probable splicing factor 3A subunit 1
- Splicing factor 3B subunit 5
- PHD finger-like domain-containing protein 5A
- C2H2-type zinc finger-containing protein
- RNA-binding region RNP-1 domain-containing protein
- 116 kDa U5 small nuclear ribonucleoprotein component
- Activating signal cointegrator 1 complex subunit 3-like
- RNA recognition motif-containing protein RRM
Sequence:
MNNENIESMDIEPPPPPPSPPLTTITSSSSSLSLSSSSSNFNKEELKLWVGSLPDEVTELELREFFSKYSINEIKLTENSSIQKQNAFVTFFDKESANRAREELSQQLFKNQRLKINWASVKPQKYSDMPVITTTTTPTPTTPPLTATAIAIPTTTFESLWYGYSSSLYSSTTTTNIFNWLSFSLLCLPPPPPPPPPQMTTTSTTTVVSTPPPPHTHPHTHTHPHPHPHPHSYPYTHQHHPPPPIPMPIPIPLHHHPHHPHHPHHPSPPPPPPPPHSSLHHHSSHHSNHHPKIISDNDPYVNKKLFLGSLGDEPEEEVRYRFSRFGEIDCFDLTSKGVAFVRYLKTESAIIAKRELGYRYKIQYDKREPRDHYHFDPNGPSSFISGGASQYYGPDYYSKQQQQPQQQPQQPPLSSSTSSSLSSSSSHPTPPQPLPLPLPPLPPTSSSSLSTFYNEPLSTEEYNQFLLFLEKLQPTRSLIKESKDWFILHLKSGKPIIQLMSKYINNQLTLTTVQNKIEIIYLINDILYFGASRRGSEQSDQISDLFEPFLPIIITSFSKEPIQVQQKLFHVLDIWDSRYFYPYKVIQHFKNLLNK
Protein: U4/U6 small nuclear ribonucleoprotein Prp3 (Pre-mRNA-splicing factor 3) (D3ZI99)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MALSKRELDELKPWIEKTVKRVLGFSEPTVVTAALNCVGKGMDKKKAADHLKPFLDDSTLRFVDKLFEAVEEGRSSRHSKSSSDRSRKRELKEVFGDDSEISKESSGVKKRRIPRFEEVEEEPEVIPGPPSESPGMLTKLQIKQMMEAATRQIEERKKQLSFISPPAPQPKTPSSSQPERLPIGNTIQPSQAATFMNDAIEKARKAAELQARIQAQLALKPGLIGNANMVGLANLHAMGIAPPKVELKDQTKPTPLILDEQGRTVDATGKEVELTHRMPTLKANIRAVKREQFKQQLKEKPSEDMESNTFFDPRVSIAPSQRQRRTFKFHDKGKFEKIAQRLRTKAQLEKLQAEISQAARKTGIHTSTRLALIAPKKELKEGDIPEIEWWDSYIIPNGFDLTEENPKREDYFGITNLVEHPAQLNPPVDNDTPVTLGVYLTKKEQKKLRRQTRREAQKELQEKVRLGLTPPPEPKVRISNLMRVLGTEAVQDPTKVEAHVRAQMAKRQKAHEEANAARKLTAEQRKVKKVKKLKEDISQGVHISVYRVRNLSNPAKKFKIEANAGQLYLTGVVVLHKDVNVVVVEGGPKAQKKFKRLMLHRIKWDEQTSNTKGDGHSQRPELWRDEVQTVPYREHGA
Protein: GEO07727p1 (Hoka) (RE40159p) (Q8SXS4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- AT03047p
- Tetraspanin
Sequence:
MKLAKKCSTYLVICLVLLACCLQESEATRRVNRGRRTLTRRYFTGLAIPGWALIVCVAVGELLIGGALYFILKKVILDKEPDQTAASYTPAQTHATATPYTPAQTHDPATATTYTPAQTHETANVTPTPTHATAIV
Protein: Endonuclease V (EndoV) (EC 3.1.21.7) (Deoxyinosine 3'endonuclease) (Deoxyribonuclease V) (DNase V) (P68739)
Organism: Escherichia coli (strain K12)
Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Has a wide substrate spectrum. In addition to deoxyinosine-containing DNA, the enzyme cleaves DNA containing urea residues, AP sites, base mismatches, insertion/deletion mismatches, flaps, and pseudo-Y structures. Participates in the excision repair of hypoxanthine and xanthine (deaminated adenine and guanine) in DNA. It thereby reduces the mutagenic effects of nitrous acid by attacking lesions caused by nitrosative deamination. Also active on inosines in single- and double-stranded RNA. May cleave tRNA(Arg2), which contains inosine at the wobble position.
Subcellular location: Cytoplasm.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Endonuclease 4
- dITP/XTP pyrophosphatase
- Exodeoxyribonuclease III
- Formamidopyrimidine-DNA glycosylase
- Uncharacterized protein YjaG
- DNA-3-methyladenine glycosylase 2
- UvrABC system protein A
Sequence:
MDLASLRAQQIELASSVIREDRLDKDPPDLIAGADVGFEQGGEVTRAAMVLLKYPSLELVEYKVARIATTMPYIPGFLSFREYPALLAAWEMLSQKPDLVFVDGHGISHPRRLGVASHFGLLVDVPTIGVAKKRLCGKFEPLSSEPGALAPLMDKGEQLAWVWRSKARCNPLFIATGHRVSVDSALAWVQRCMKGYRLPEPTRWADAVASERPAFVRYTANQP
Protein: Ribosomal protein S6 kinase (EC 2.7.11.1) (A0A0R4ID09)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPLAQCADPWQKLPMGHLENEDDSMIEDDSLVHDEGSVKEISITHHVKEGSEKADPRQFELRKVLGQGSFGKVFLVKKISGPDAGQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHGLGIIYRDLKPENILLDDDGHIKLTDFGLSKESIDHENKAYSFCGTVEYMAPEVVNRRGHTQSADWWSYGVLMFEMLTGALPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRNLFKRNPGNRLGAGPDGVEGIKRHSFFTRIDWNKLFRKEVPPPFKPAIKKPDDTFYFDSEFTAKTPRDSPGVPPSANAHQLFRGFSFVATGVEEESQSPIQSNINMSSILQQSHRSTLQFTDAYEVKEDIGVGSYSVCKRCVQKSTGMDYAVKIIKKERRDPTEEVEILLRYGQHPNIITLKDVFDDGRSVYLVTELMKGGELLDKILRQKFFSEREASAVLYTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLTGFTPFANGPEDTPEEILARIGSGKFSLTGGYWNSVSHDAKDLVSKMLHVDPHKRLTAAQVLRHPWIINKDQLPKYQLNRQDAPHLVKGAMAATYSALNRNVSPVLDPVGCSTLAQRRGLKKLTSTAL
Protein: Glutathione S-transferase LANCL1 (EC 2.5.1.18) (40 kDa erythrocyte membrane protein) (p40) (LanC-like protein 1) (O43813)
Organism: Homo sapiens (Human)
Function: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15811525}. Cell membrane {ECO:0000269|PubMed:10944443, ECO:0000269|PubMed:16979580}; Peripheral membrane protein {ECO:0000269|PubMed:10944443}.
Interaction partners:
- Epidermal growth factor receptor kinase substrate 8
- Aldehyde dehydrogenase family 16 member A1
- Stomatin
Sequence:
MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYGLCHGSAGNAYAFLTLYNLTQDMKYLYRACKFAEWCLEYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKARFPAFEL