wanglab/gogpt-training-data huggingface dataset:
Protein: Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa) (p20-ARC) (P33204)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, actin patch.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 1
- Proline-rich protein LAS17
- Structure-specific endonuclease subunit SLX1
- Protein LDB17
- Actin
Sequence:
MSQSLRPYLTAVRYSLEAALTLSNFSSQEVERHNRPEVEVPNTSAELLLQPMHISRNENEQVLIEPSVNSVRMSLMVKQADEIEQILVHKFTRFLEQRAEAFYILRRVPIPGYSISFLITNKHTESMKTGKLVDFIIEFMEDVDKEISEIKLFLNARARFVAEAYLDEFVY
Protein: 3-hydroxypropionyl-coenzyme A synthetase (3-hydroxypropionyl-CoA synthetase) (EC 6.2.1.36) (Q973W5)
Organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
Function: Plays a role in the autotrophic CO(2) fixation pathway. Activates 3-hydroxypropionate to its CoA ester. Can also activate propionate, and to a lesser extent acrylate, acetate and butyrate.
Interaction partners:
- 3-hydroxypropionyl-CoA dehydratase
- L-gulonate 3-dehydrogenase
- Enoyl-CoA hydratase
- Enoyl-CoA hydratase
- Enoyl-CoA hydratase
- Acryloyl-coenzyme A reductase
Sequence:
MTEKLSEQLQQLGEQNLEEKADYNMRYYKYLYKKSIEEPDKFWGELAEELITWYEPWKQAFVQEEGLLTKWFVGGKLNASYNAVDRHLNSHRKYKAAIFWESEKGEKKVVTYQDLFYEVNKWANALRELGVKKGDRVTIYMPLTPEGVIAKLAVARLGAIHSVVFAGFGAQALADRIADAGAKVVITADAYYRRGKLVELKKTVDEALNILGDKSPVQKVLVYKRTGTEIPFKEGRDVYFDEVGKYKYIEPVPVEATEPLFILYTSGTTGKPKGIVHSTGGYLVGTAVMLLWSYGLSQENDVLFNTSDIGWIVGHSYITYSPLVMGRSIVIYESAPDYPYPDKWAEMIEKYRATTFGTSATAIRTLMKYGEDYVKQHDLSSLRIIVTNGEPLNYAPWKWGLEVVGGGKVFMSHQWWQTETGGPNIGYIPGVVYLPMKSGPAVGFALPGNKVTVVNEEGKETKPRERGYLVMLPPFPPMMMIGMWNDPDNERLKKTYFSKFPGIYYPGDYAMIDEDGYIWVMGRADETIKVAAHRIGAGEVESIVTSHPAVAEAAAVGIPDPVKGEAVHLFVVLKVGYKPSPQLAREIQEHVRKYMGAIVTPEVHFVDKLPKTRSGKIMRRVIKAVMMGQSAGDITTLEDEASMDEIKKAVEEFKKSLSQ
Protein: Uncharacterized protein C582.04c (Q10338)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MAENKKFSIRKKRECSYPTFRTLYEFNKFFLRYKTEISKIQRRTSSLIQYEEHSSAIFIYYETPQMFDLATKALQTLYNSHTREGETKAASKWYRNPRKDFPSQEAALVRKKKRDALILKKYLLNVDPSLSFRAEGLFTLPSDDLDVYEFFGGENLTLFNQVRVDCQCYIHYLPKLAAFYVRCDSVKNLKVALKRVKHIFYEQVSLIRLERTQPILHLMNFDDYSTSYELFYDRNFPLAKKYKPNSIYLHRLPESIPTPVDSVKINLIRERSFNLLKNFVSASLFNVFLFSGTVFMRVKVGIPLFERLKVGTNKVKNNSVNIAQSFLEPQTRSTFLRYLFSDEVSVKVCHVLKELRSPTGEKLFESFSDDPITAVHFEVMNCKGVQDTLTAIWNTNSGKPSGWYLESTMYKALDVTYYNLNTLSWNLYIEYGHPTQNSTFYKEFISNISMSDDGRIYFMNTRDIKVRSLVVKLKHKYWHLSSGFHLHITRFEAHDMGKVKDIDTDFEPGLQCYQVGSDTSVLRYGLSFWDPKWDYLLADNQHKQQWQAPSYKPLISEFFPMGIEHFIETAQSIVMAVNRSTID
Protein: C6 transcription factor GliZ-like, putative (Q4WYF9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTSTLPYLTSPPATHPSNSDHKKLRSACDSCHQCKVKCSGGSPCFRCTSKGLNCRYGYQNRAGKPKGSKNRKTLEREHQLRMEWLTSQLRDANGGLGNLNIDLSDPTTLLPSPFFQSTRWKQGHMLPQSSVQPTPANQCIKSTEHESECLPTPQGLDTWTMDLGPIAQTPRESTSESLEAFTTPISFTGGGETYLRQLSDPTTPISFGFPSPHARLDGTGDPCACVQTQAVNISTLHQLTCRDRSDRFDLAMKSITSTLETCEKFVVCEACDKSVASILLTLSAIELIFTLFEQLTMNNRRLSPPEEEQRLIPCSLGDYKVTKEESQAIRNVLVKMTLSKGKQALNALQNLVNGSVDFLDESGPCEASQHDSNNANEPMLSGLSVTDRNYMTQCISRKNAALEVLMAAVAV
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (M0RB22)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Interleukin-1 receptor accessory protein
- SLIT and NTRK-like family, member 2
- Neuroligin-3
- Interleukin-1 receptor accessory protein-like 1
- SLIT and NTRK-like family, member 1
- Liprin-alpha-3
- SLIT and NTRK-like family, member 3
- X-linked interleukin-1 receptor accessory protein-like 2
- PTPRF interacting protein alpha 1
- SLIT and NTRK-like family, member 5
Sequence:
VLFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEFDDGSGSVLRIQPLRTPRDEAIYECVASNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRSGGTPIRGALQIEQSEESDQGKYECVATNSAGTRYSAPANLYVRGRNVRRVPPRFSIPPTNHEIMPGGSVNITCVAVGSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAVAQITVKALPKPPGTPVVTESTATSITLTWDSGNPEPVSYYIIQHKPKNSEEPYKEIDGIATTRYSVAGLSPYSDYEFRVVAVNNIGRGPASEPVLTQTSEQAPSSAPRDVQARMLSSTTILVQWKEPEEPNGQIQGYRVYYTMDPTQHVNNWMKHNVADSQITTIGNLVPQKTYSVKVLAFTSIGDGPLSSDIQVITQTGVPGQPLNFKAEPESETSILLSWTPPRSDTIASYELVYRDGDQGEEQRITIEPGTSYRLQGLKPNSLYYFRLSARSPQGLGASTAEISARTMQSKPSAPPQDISCTSPSSTSILVSWQPPPVEKQNGIITEYSLKYAAVDGEDYRPHEILGIPSDTTKYLLEQLEKWTEYRITVTAHTDVGPGPESLSVLIRTDEDVPSGPPRKVEVEAVNATAVKVSWRSPVPNKQHGQIRGYQVHYVKMENGEPKGQPMLKDVMLADAQWEFDDATEHDMIISGLQPETSYSLTVTAYTTKGDGARSKPKLVSTTGAVPGRPRLVINHTQMNTALIQWHPPVDTFGPLQGYRLKFGRKDMEPLTTLEFSEKEDHFTATDIHKGASYIFRLSARNKVGFGEEMVKEISVPEEVPTGFPQNLHSEGTTSTSVQISWQPPVLAERNGVITKYTLLYRDINVPLLPMEHLIVPADTSMTLTGLKSDTTYDVKVRAHTSKGPGPYSPSVQFRTLPVDQVFAKNFHVKAVMKTSVLLSWEIPENYNSAMPFKILYDDGKMVEEVDGRATQKLIVNLKPEKSYSFVLTNRGNSAGGLQHRVTAKTAPDVLRTKPAFIGKTNLDGMITVQLPDVPANENIKGYYIIIVPLKKSRGKFIKPWESPDEMELDELLKEISRKRRSIRYGREVELKPYIAAHFDVLPTEFTLGDDKHYGGFTNKQLQSGQEYVFFVLAVMDHAESKMYATSPYSDPVVSMDLDPQPITDEEEGLIWVVGPVLAVVFIICIVIAILLYKRKRAESESRKSSLPNSKEVPSHHPTDPVELRRLNFQTPGSDDSGYPGNLHFSSMASHPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYVNANYIDGYRKQNAYIATQGSLPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETHGLVQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGNTEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFLDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFDHYAT
Protein: Aminopeptidase P2 (AtAPP2) (EC 3.4.11.9) (Q8RY11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Pentatricopeptide repeat
- Alpha/beta-Hydrolases superfamily protein
- Serine carboxypeptidase-like 26
- Serine carboxypeptidase-like 42
- Glycine--tRNA ligase, mitochondrial 1
- Serine carboxypeptidase-like 34
- Prolyl carboxypeptidase like protein
- Subtilisin-like protease SBT1.9
- Proteasome subunit alpha type-5-B
- Alpha/beta-Hydrolases superfamily protein
Sequence:
MIPLTLSSPSLNRLVLSTSRYSHSLFLSNFNSLSLIHRKLPYKPLFGARCHASSSSSSSSSFTAKSSKEIRKAQTKVVVDEKLSSIRRLFSEPGVGIDAYIIPSQDAHQSEFIAECYARRAYISGFTGSAGTAVVTKDKAALWTDGRYFLQAEKQLNSSWILMRAGNPGVPTASEWIADVLAPGGRVGIDPFLFSADAAEELKEVIAKKNHELVYLYNVNLVDEIWKDSRPKPPSRQIRIHDLKYAGLDVASKLLSLRNQIMDAGTSAIVISMLDEIAWVLNLRGSDVPHSPVMYAYLIVEVDQAQLFVDNSKVTVEVKDHLKNAGIELRPYDSILQGIDSLAARGAQLLMDPSTLNVAIISTYKSACERYSRNFESEAKVKTKFTDSSSGYTANPSGIYMQSPISWAKAIKNDAELKGMKNSHLRDAAALAHFWAWLEEEVHKNANLTEVDVADRLLEFRSMQDGFMDTSFDTISGSGANGAIIHYKPEPESCSRVDPQKLFLLDSGAQYVDGTTDITRTVHFSEPSAREKECFTRVLQGHIALDQAVFPEGTPGFVLDGFARSSLWKIGLDYRHGTGHGVGAALNVHEGPQSISFRYGNMTPLQNGMIVSNEPGYYEDHAFGIRIENLLHVRDAETPNRFGGATYLGFEKLTFFPIQTKMVDVSLLSDTEVDWLNSYHAEVWEKVSPLLEGSTTQQWLWNNTRPLAKP
Protein: E3 ubiquitin-protein ligase TRIM56 (EC 2.3.2.27) (Tripartite motif-containing protein 56) (Q80VI1)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity by mediating ubiquitination of CGAS and STING1. In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta. Also mediates monoubiquitination of CGAS, thereby promoting CGAS oligomerization and subsequent activation. Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling (By similarity). Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21074459}.
Interaction partners:
- Stimulator of interferon genes protein
- E3 ubiquitin-protein ligase TRIM32
- E3 ubiquitin-protein ligase TRIM38
Sequence:
MNSKVSSPTLLEALSSDFLACKICLEQLHTPKTLPCLHTYCQDCLAQLDIGGQVRCPECREIVPVPAEGVAAFKTNFFVNGLLDLVKARAPGDVHSGKPTCALCPLVGGKSSGGPATARCLDCADDLCQACADGHRCSRQTHKHRVVDLVGYRAGWYDEEARERQASQCPQHPGEALCFLCQPCSQLLCKDCRLGPHIDHPCLPLAEAVRSRKPGLEELLAGVDSNLVELEATRVAEKEALALLREQAASVGTQVEEAAERILKSLLAQKQEVLGQLRALVEAAEEATRERLTKIERQEQVAKAAAAFARRVLSLGLEAEILSLEGAITQRLRQLQDAPWTSGPTRCVLPQLELHPGLEDKNCHLLRLIFEEPKQSPKDSGKGGAGTQGGDEAQGQGDDRTKIGKQGGAQPLTPKEGKDQNPQEDDGVFIERGNRPNKKKKCKGRGKSVSREPSPILRPNLEGSGLLPRPVFSWSFPTRMPGDKRSPRITGLCPYGPQEILVADEQNRVLKRFSLNGDYKGTVQVPEGCSPCSVAALQNAVAFSANAKLYLVSPDGEIQWRRSLSLTQSSHAVAAMPCGDRVAVSVAGHVEVYKKDGSLATRFIPGGKASRGQRALVFLTTSPQGNFVGSDWQQNSVVFCDGLGQVIWEYKGPGLHGCQPGSVSVDKKGYIFLTLREVNKVVILDPKGSLLGDFLTAYHGLEKPRVTTMVDGKYLVVSLSNGTIHVFRVRFPDS
Protein: Phosphoglycerate kinase 1 (EC 2.7.11.1) (EC 2.7.2.3) (P00559)
Organism: Equus caballus (Horse)
Function: Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P00558}. Mitochondrion matrix {ECO:0000250|UniProtKB:P00558}. Note=Hypoxic conditions promote mitochondrial targeting. Targeted to the mitochondrion following phosphorylation by MAPK1/ERK2, cis-trans isomerization by PIN1, and binding to mitochondrial circRNA mcPGK1. {ECO:0000250|UniProtKB:P00558}.
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphoglycerate mutase
- Glyceraldehyde-3-phosphate dehydrogenase.
- Phosphoglycerate mutase
- Phosphoglycerate mutase
- phosphopyruvate hydratase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Cleavage stimulation factor subunit 3
Sequence:
MSLSNKLTLDKLNVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDVGPMPDKYSLQPVAVELKSLLGKDVLFLKDCVGPEVEKACADPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIETFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKNLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGTESSKKYAEAVARAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNV
Protein: Eukaryotic peptide chain release factor subunit 1-1 (Eukaryotic release factor 1-1) (eRF1-1) (Omnipotent suppressor protein 1 homolog 1) (SUP1 homolog 1) (Q39097)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Modulates plant growth and development.
Subcellular location: Cytoplasm.
Interaction partners:
- T10F20.8 protein
- Eukaryotic peptide chain release factor subunit 1-3
- Eukaryotic peptide chain release factor subunit 1-2
- ABC transporter E family member 2
- AT5g45350/MFC19_1
- ABC transporter E family member 1
- ABC transporter E family member 3
- Regulator of nonsense transcripts UPF3
- Nonsense-mediated mRNA decay factor SMG7
- Regulator of nonsense transcripts 1 homolog
Sequence:
MGDKNDDDKNIEIWKIKKLIKSLEAARGNGTSMISLIMPPRDQVSRVTKMLGDEYGTASNIKSRVNRQSVLGAITSAQQRLKLYNRVPPNGLVLYTGTIVNEDGKEKKVTIDFEPFRPINASLYLCDNKFHTEALNELLESDDKFGFIVMDGNGTLFGTLSGNTREVLHKFSVDLPKKHGRGGQSALRFARLRMEKRHNYVRKTAELATQYYINPATSQPNVSGLILAGSADFKTELSQSDMFDPRLAAKILNVVDVSYGGENGFNQAIELSAEILANVKFIQEKRLIGKYFEEISQDTGKYVFGVEDTLNALESGAIETLIVWENLDINRYVMKNSATGETVIKHLNKEQEANTENFKVADSDLALDVEEKLSLLEWLANEYRRFGCALEFVTNKSQEGSQFCRGFGGIGGILRYQLDMTAFDSEDGEALDDDSE
Protein: Ribosomal protein bS6--L-glutamate ligase (EC 6.3.2.-) (Polyglutamate synthase) (Ribosomal protein bS6 modification protein) (P0C0U4)
Organism: Escherichia coli (strain K12)
Function: Is an L-glutamate ligase that catalyzes the ATP-dependent post-translational addition of glutamate residues to the C-terminus of ribosomal protein S6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH.
Interaction partners:
- Uncharacterized protein YbjN
- Uncharacterized protein YbjC
- Oxygen-insensitive NADPH nitroreductase
- Small ribosomal subunit protein bS6
Sequence:
MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG
Protein: Claudin 30 (Claudin-4) (B1H3P7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Zona occludens protein 1
- Zona occludens protein 1
- Zona occludens protein 1
- Tight junction protein ZO-1-like
- Claudin
- Tight junction protein ZO-3-like isoform X2
- Tight junction protein ZO-3-like isoform X4
- Claudin
- Claudin-8-like
- Claudin
Sequence:
MASAGFQMLGTALGIIGWIGAIVVCALPQWKVTAFIGENIITAQTTWQGIWMNCVVQSTGQMQCKVYDSMLALPQDLQAARALIIISIMMGLVGILLSVAGGKCTNCVEDERTKSRIGVGSGVVFIIAGVLCLIPVCWSANTIIRDFYNPMLNSSQKMELGAALYIGWGAAALMIIGGGFLCANCPPKEDNYPTKYSAARSTAPRDYV
Protein: L-ascorbate peroxidase (EC 1.11.1.11) (Q39780)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MAFPVVDTEYLKEIDKARRDLRALIALKNCAPIMLRLAWHDAGTYDVSTKTGGPNGSIRNEEEFTHGANSGLKIAIDFCEEVKAKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNICPREGRLPDAKRGAPHLRDIFYRMGLSDKDIVALSGGHTLGRAHPERSGFDGPWTNEPLKFDNSYFLELLKGESEGLLKLPTDKALLDDPEFRKYVELYAKDEDAFFRDYAESHKKLSELGFTPTSARSKVMVKDSTVLAQGAVGVAVAAAVVILSYFYEVRKRMK
Protein: Dynein regulatory complex protein 12 (Q57YJ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
Sequence:
MPPKDNRKVTKTENDFAEEDQQINDEIVRAKLRLAALEAVHADRLEEIAMLKRSRDDLLSTFEKCEGDANAATEDRLDILTDFTRQYKNDEKFKIEIATRMDATLNRLAEEKLKLVEELKKTKTEFEEAIAQVKAECETLYSRIADMEREFDTIMMETKSGDSTQ
Protein: 3-hydroxy-D-aspartate aldolase (EC 4.1.3.41) (beta-hydroxyaspartate aldolase) (A1B8Z1)
Organism: Paracoccus denitrificans (strain Pd 1222)
Function: Catalyzes the condensation of glyoxylate and glycine into (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate). Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Is also able to catalyze the reverse reaction in vitro, i.e. the cleavage of (3S)-3-hydroxy-D-aspartate, and that of D-threonine to a lesser extent.
Interaction partners:
- Iminosuccinate reductase
- beta-hydroxyaspartate dehydratase
- L-aspartate--glyoxylate aminotransferase
- HTH-type transcriptional regulator BhcR
Sequence:
MNAKTDFSGYEVGYDIPALPGMDESEIQTPCLILDLDALERNIRKMGDYAKAHGMRHRSHGKMHKSVDVQKLQESLGGSVGVCCQKVSEAEAFARGGIKDVLVTNEVREPAKIDRLARLPKTGATVTVCVDDVQNIADLSAAAQKHGTELGIFVEIDCGAGRCGVTTKEAVVEIAKAAAAAPNLTFKGIQAYQGAMQHMDSFEDRKAKLDAAIAQVKEAVDALEAEGLAPEFVSGGGTGSYYFESNSGIYNELQCGSYAFMDADYGRIHDAEGKRIDQGEWENALFILTSVMSHAKPHLAVVDAGLKAQSVDSGLPFVYGRDDVKYIKCSDEHGVVEDKDGVLKVNDKLRLVPGHCDPTCNVHDWYVGVRNGKVETVWPVSARGKGY
Protein: Repetin (Q6XPR3)
Organism: Homo sapiens (Human)
Function: Involved in the cornified cell envelope formation. Multifunctional epidermal matrix protein. Reversibly binds calcium.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Protein DEPP1
- Loricrin
- Late cornified envelope protein 3C
- Trichohyalin
- Filaggrin
- Late cornified envelope protein 3B
- Involucrin
- Late cornified envelope protein 3D
- Small proline-rich protein 2A
- Late cornified envelope protein 5A
Sequence:
MAQLLNSILSVIDVFHKYAKGNGDCALLCKEELKQLLLAEFGDILQRPNDPETVETILNLLDQDRDGHIDFHEYLLLVFQLVQACYHKLDNKSHGGRTSQQERGQEGAQDCKFPGNTGRQHRQRHEEERQNSHHSQPERQDGDSHHGQPERQDRDSHHGQSEKQDRDSHHSQPERQDRDSHHNQSERQDKDFSFDQSERQSQDSSSGKKVSHKSTSGQAKWQGHIFALNRCEKPIQDSHYGQSERHTQQSETLGQASHFNQTNQQKSGSYCGQSERLGQELGCGQTDRQGQSSHYGQTDRQDQSYHYGQTDRQGQSSHYSQTDRQGQSSHYSQPDRQGQSSHYGQMDRKGQCYHYDQTNRQGQGSHYSQPNRQGQSSHYGQPDTQDQSSHYGQTDRQDQSSHYGQTERQGQSSHYSQMDRQGQGSHYGQTDRQGQSSHYGQPDRQGQNSHYGQTDRQGQSSHYGQTDRQGQSSHYSQPDKQGQSSHYGKIDRQDQSYHYGQPDGQGQSSHYGQTDRQGQSFHYGQPDRQGQSSHYSQMDRQGQSSHYGQTDRQGQSSHYGQTDRQGQSYHYGQTDRQGQSSHYIQSQTGEIQGQNKYFQGTEGTRKASYVEQSGRSGRLSQQTPGQEGYQNQGQGFQSRDSQQNGHQVWEPEEDSQHHQHKLLAQIQQERPLCHKGRDWQSCSSEQGHRQAQTRQSHGEGLSHWAEEEQGHQTWDRHSHESQEGPCGTQDRRTHKDEQNHQRRDRQTHEHEQSHQRRDRQTHEDKQNRQRRDRQTHEDEQNHQR
Protein: YY1-associated factor 2 (Q5SP48)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADWLFYQPKVPKRQAKPSSDDGYWDCSVCTFKNTAEAFKCMMCDVRKGTSTRKPRPVSQLVSQQVTQQFASATLPKKEKKEKTEKDKNEREPTLKKNNHKKMRPRLKNVDRSSAQHLEVTVGDLTVIITDYKEKTKPSSSSSSSATSADHHSQSGSNSDNTEKGISRSSSPRGEVSSLNGESH
Protein: Emerin (P50402)
Organism: Homo sapiens (Human)
Function: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:19167377}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus.
Interaction partners:
- Barrier-to-autointegration factor
- Prelamin-A/C
- SUN domain-containing protein 1
- Nesprin-1
- Barrier-to-autointegration factor-like protein
- Nesprin-2
- Lamin-B1
- SUN domain-containing protein 2
- LIM domain only protein 7
- Inner nuclear membrane protein Man1
Sequence:
MDNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRLSPPSSSAASSYSFSDLNSTRGDADMYDLPKKEDALLYQSKGYNDDYYEESYFTTRTYGEPESAGPSRAVRQSVTSFPDADAFHHQVHDDDLLSSSEEECKDRERPMYGRDSAYQSITHYRPVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIRPENRAPGAGLGQDRQVPLWGQLLLFLVFVIVLFFIYHFMQAEEGNPF
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (Q8T3L0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLPYKVICRSPHLTDMLVKLLASLSTELPKEEELLPLSDQMPPLVPIGPVQRAGAAAAAAHPPPPQPPAENTATATEIGDGLAANIEEQAAPASGNPASGDSNAGAKRTQLPTLSVALPVTPSKPRRKIYSKNFSQLQLVIEVLTHQCGTTEGLDNVAKLIVNLTQCSQASSAIFIQYLTAAILGLAEEVRQAIQMLLNEIRMYNIHQGGAGTTSQAASTSGAAAATASYVPTVSGASLLPNLAVHEGIMQDRFTAEHVIISAPKNAKPTCELQLPSMKKLMSNSSAQPYFLRTLKIFMQVRDMYEAQNGLSTGGGVACGAGDNDDDIIDIEGDGGASGGSSSDMAPGSASTISPPPPMETNQIAQDGDDDEEDDDEARSFPGVGNHAVASASKSTKPTLSQILCLDVLWNTLSECLVALEESKDEFAVLVLQPTVEAFFLIHASHRGASKKSGRSFMPNAAGFGLRAAAGAGAIGGLGAAAPSAQEYSPFMDDISSANTPSSASFDDEPRMQDASTNTPLVTNPSTSTAMSAHEAQLRQDRQKFLQFAEKHRTVLNQILRQSPTHLSDGPFAVLVDHTRILDFDVKRKYFQTELERLDEGIRREEHTVSVRRVTVFEDSFRVLYRLGPEEWKNRFYIVFEDEEGQDAGGLLREWYVIISREIFNPMYALFCVSPGDRVTYMINPSSHANPNHLSYFKFVGRVIAKAVHDNKLLECYFTRSFYKHILGKQVKHTDMESQDYEFYKGLDYLMKNDISTLGYELTFSTEVQEFGVTQIRDLKPNGRDTAVTEENKFEYVQLVCQLKMSGSIRQQLDAFLEGFYDIIPKHLISIFNEQELELLISGLPDIDIEDLKANTEYHKYTSKSAQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFGSLEGMNGIQKFQIHRDDRSTDRLPCAHTCFNQLDLPMYKSYDKLRSCLLKAIHECSEGFGFA
Protein: tRNA threonylcarbamoyladenosine biosynthesis protein TsaE (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE) (O05515)
Organism: Bacillus subtilis (strain 168)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB; this reaction does not require ATP in vitro. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. Displays ATPase activity in vitro, which is modulated by the oligomeric status of the protein.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19246765}. Note=Localized predominantly at the cell poles and at the periphery of the bacterium.
Interaction partners:
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
- tRNA N6-adenosine threonylcarbamoyltransferase
- Threonylcarbamoyl-AMP synthase
- Thiamine-monophosphate kinase
- Putative [ribosomal protein bS18]-alanine N-acetyltransferase
- tRNA
- tRNA-specific 2-thiouridylase MnmA
- tRNA
- tRNA dimethylallyltransferase
Sequence:
MKQLKWRTVNPEETKAIAKLTAAFAKPGDVLTLEGDLGAGKTTFTKGFAEGLGITRIVNSPTFTIIKEYNDGVLPLYHMDVYRMEDESEDLGLDEYFHGQGVCLVEWAHLIEEQLPQERLQIVIKRAGDDEREITFTAVGNRYEMLCEELSRHDNISN
Protein: C2H2-type domain-containing protein (Q9GYG1)
Organism: Caenorhabditis elegans
Interaction partners:
- Checkpoint protein
- C2H2-type domain-containing protein
- Proliferating cell nuclear antigen
- SAP domain-containing protein
Sequence:
MNQLVCPLCCETLKEEGAHFYKHFKYKRYACGESTCDMGFYTQQELNAHCSKHGHKRSFQKTVNPYIDKMISVVVEDAYALATDDMETVLEKRWGRDPRSVSPTSPVKKTPTDSAKNKRSSVVTPTSPPVPKKAKSGTSTTSPFAFLNRRTNNSESSLCPNASSTSAQPASSSSAQAIVDSTTSEHNISIDKTKKPRKKRNESMTAAQNQEKAGKNANYDEMSAIDKLIGWFDPNVPERRDAAKVKCAVCNEEIVYDFILRKGHVTRSHMAADVAPEDYDDLLKTAMDRSYPDLPNSDLACQLCMTGAEVRKNMRREHIEKLHTTSLPPLTCPVGECEKGFRRQCDLSSHMKDTHKASMAVYKNATFQQVRRRRNAMINEMINKCFPWSRLEAIENKTVVGEKSDSVNRAPVDRSFDTDVRVRDVNKTRRAPQYNANRSSSSDSDSEHEEAASVATGEVSETGGTDDFPQDVIYICHQFNTEVAQKLSQIVRIKPEIIDVEDVLMNDVTMEINEIPVKEETEEEQPKEENNSTLPSIPIPSIFSPYEPIVPPPATSPDPMNPPIASLLPTRILSATNVLENKYNENVSSRRSTSRERSSNRNYDERWSRNDYSNPRNYSNRSFHQRNQRGHSSSNRFNSPFVSRNNYNNNSETTEGSSRRSEYNSSSSNHHSRSSYRGNRDDRGSRW
Protein: Triosephosphate isomerase (TIM) (TPI) (EC 5.3.1.1) (Triose-phosphate isomerase) (P9WG43)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
Interaction partners:
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Enolase
- Transketolase
- Transaldolase
- Pyruvate kinase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- ATP-dependent 6-phosphofructokinase
Sequence:
MSRKPLIAGNWKMNLNHYEAIALVQKIAFSLPDKYYDRVDVAVIPPFTDLRSVQTLVDGDKLRLTYGAQDLSPHDSGAYTGDVSGAFLAKLGCSYVVVGHSERRTYHNEDDALVAAKAATALKHGLTPIVCIGEHLDVREAGNHVAHNIEQLRGSLAGLLAEQIGSVVIAYEPVWAIGTGRVASAADAQEVCAAIRKELASLASPRIADTVRVLYGGSVNAKNVGDIVAQDDVDGGLVGGASLDGEHFATLAAIAAGGPLP