wanglab/gogpt-training-data huggingface dataset:
Protein: cAMP-dependent protein kinase inhibitor gamma (PKI-gamma) (O70139)
Organism: Mus musculus (Mouse)
Function: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
Interaction partners:
- cAMP-dependent protein kinase inhibitor alpha
- cAMP-dependent protein kinase inhibitor beta
Sequence:
MMEVESSYSDFISCDRTGRRNAVPDIQGDSEAVSVRKLAGDMGELALEGAEGQAEGSTPDKEASSQPESSDANTSS
Protein: Probable esterase/lipase LipP (O53190)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MNQPDIKGSCASEFTKVRDAFERNFVLRNEVGAAVAVWVDGDLVVNLWGGSADAGGTRPWQHDTLATVLSGTKALTATCVHQLVDRGELDLHAPVARYWPEFGQAGKQAITLAMVMSHRSGAIGPRGRLGWEQVADWDFVCEQLAAAEPWWQPGAAQGYHMTTFGFILGEVFRRVTGRTVGQYLRTEIAEPLGADVHIGLHPGEQLRCADLVDKPHIRQLLADVQAPGYPTSLNEHPKAALSVSMGFAPDDELGSNDLQLWRQIEFPGTNGQVSALGLATFYNGLAQEKLLSREHMELVRVSQGGFDTDLVLGPRVADHGWGLGYMLNQRGVNGPNPRIFGHGGLGGSFGFVDLEHRIGYAYVMNRFDATKANADPRSVVLSNEVYAALGVNRS
Protein: ATP binding cassette subfamily G member 1 (A0A0G2JXH0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MACLMAAFSVGTAMNASNYSAAMTEPKSVCVSVDEVVSSNVDELETDLLNGHLKKVDNNFTEAQRFSSLPRRAAVNIEFKDLSYSVPEGPWWRKKGSPLTCFPI
Protein: Extracellular exo-inulinase inuE (EC 3.2.1.80) (A2R0E0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Exo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. Splits off terminal fructose units successively from the non-reducing end of the inulin molecule, and also hydrolyze sucrose and raffinose (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MARLLKAVTVCALAGIAHAFNYDQPYRGQYHFSPQKNWMNDPNGLLYHNGTYHLFFQYNPGGIEWGNISWGHATSEDLTHWEEQPVALLARGYGSDVTEMYFSGSAVADVNNTSGFGKDGKTPLVAMYTSYYPVAQTLPSGQTVQEDQQSQSIAYSLDDGLTWTTYDAANPVIPNPPQPYQAQYQNFRDPFVFWHDESQKWVVVTSIAELHKLAIYTSDNLKDWKLVSEFGPYNAQGGVWECPGLFKLPLDGGSSTKWVITSGLNPGGPPGTVGSGTQYFVGEFDGTTFTPDADTVYPGNSTANWMDWGPDFYAAAGYNGLSIKDHVHIGWMNNWQYGANIPTYPWRSAMAIPRHLALKTINNKTTLVQQPQEAWSSISSKHPLYSRTYSTFSEGSTNASTTGETFRVDLSFSATSKASTFAIALRASANFTEQTLAGYDFAKQQIFLDRTKSGDVSFDNTFASVYHGPLVPDSTSMVRLSIFVDRSSVEVFGGQGETSLTAQIFPSNDAVHARLVSTGGATEDVRVDVHNITSTWN
Protein: PDZ domain-containing protein GIPC3 (Q8TF64)
Organism: Homo sapiens (Human)
Function: Required for postnatal maturation of the hair bundle and long-term survival of hair cells and spiral ganglion.
Interaction partners:
- E3 ubiquitin-protein ligase ZNRF4
Sequence:
MEGAAAREARGTETPRASAPPPAPSEPPAAPRARPRLVFRTQLAHGSPTGKIEGFTNVRELYAKIAEAFGIAPTEILFCTLNSHKVDMQKLLGGQIGLEDFIFAHVRGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPFTLRLVQPKRAFDMIGQRSRSSKCPVEAKVTSGRETLRLRSGGAATVEEAPSEFEEEASRKVDDLLESYMGIRDPELASTMVETSKKTASAQEFARCLDSVLGEFAFPDEFVVEVWAAIGEAREACG
Protein: Lysozyme g-like protein 2 (EC 3.2.1.-) (Q86SG7)
Organism: Homo sapiens (Human)
Function: May act as a potent antibacterial protein that may play a role in the innate immunity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MLSSVVFWGLIALIGTSRGSYPFSHSMKPHLHPRLYHGCYGDIMTMKTSGATCDANSVMNCGIRGSEMFAEMDLRAIKPYQTLIKEVGQRHCVDPAVIAAIISRESHGGSVLQDGWDHRGLKFGLMQLDKQTYHPVGAWDSKEHLSQATGILTERIKAIQKKFPTWSVAQHLKGGLSAFKSGIEAIATPSDIDNDFVNDIIARAKFYKRQSF
Protein: SfgA (C8V6P1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein fluG
- C2H2-type domain-containing protein
- MYB family conidiophore development protein FlbD
Sequence:
MEARTMVCDRAQPPQPLPHEPPHPDKKKRVRRWHHRGFTGCSTCRRRHVRCDEASPTCRNCTRLGLECDGSQGRMTFKVYGPPPPPPGQSNPPTKRDKSRPRASQKAVKKEDTEVEGVVISPTTVTESKPLVFHFENPAVHSVTSIPEDDKKVKKEQEDEDLVLIPTAGESRPTEVRFHSHTLPVSSLDCLQGRYYTHFVDEVATLLLIYDTSTNINPFRRCFPDVSQSSLSMASAMEALGALHLANTSTGPERIVHFQHAMGKYGEVVKSFRTRYEIGQRSRLPDFATCLLLALFEMMDSQHHNWAIHLKGAREIYRWLFYPNSDPVLEAQRVAEMNHPLRQFLVSLLSYLDVAGACATSDGTVVEGSYWQTLGGGWEYNLGIPSLSQPAANNGPLLELRQCWSIMMEIQAAISSFGKAKQSGWLTPDQQDIMYRDLLQRLVQWRLDAPQCLQKLRDLDDASLSQYPHPDVLEYAGCIEAYEKATNIYLHKVGRAGRPDIQPQQELIAAFCTRILSLIRKLAKDVGRLAVPWPLFVAGRETRDEREQKFVRDTMLDMQRYGFKNVEKALEELEKAWFKRRAFPEGWVETMDDVRSSILLP
Protein: Polypeptide N-acetylgalactosaminyltransferase 1 (EC 2.4.1.41) (Polypeptide GalNAc transferase 1) (GalNAc-T1) (pp-GaNTase 1) (Protein-UDP acetylgalactosaminyltransferase 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form] (Q10472)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates such as apomucin-, MUC5AC-, MUC1- and MUC2-derived peptides.
Subcellular location: [Polypeptide N-acetylgalactosaminyltransferase 1]: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]: Secreted.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- C1GALT1-specific chaperone 1
- Mucin-3A
Sequence:
MRKFAYCKVVLATSLIWVLLDMFLLLYFSECNKCDEKKERGLPAGDVLEPVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSVVIVFHNEAWSTLLRTVHSVINRSPRHMIEEIVLVDDASERDFLKRPLESYVKKLKVPVHVIRMEQRSGLIRARLKGAAVSKGQVITFLDAHCECTVGWLEPLLARIKHDRRTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRDYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQIINKNNRRLAEVWMDEFKNFFYIISPGVTKVDYGDISSRVGLRHKLQCKPFSWYLENIYPDSQIPRHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATEEDSQVPSIRDCNGSRSQQWLLRNVTLPEIF
Protein: L-methionine sulfoximine/L-methionine sulfone acetyltransferase (EC 2.3.1.-) (L-amino acid N-acyltransferase) (EC 2.3.1.-) (Methionine derivative detoxifier A) (MDDA) (Q8ZPD3)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Plays a role in the resistance against the toxic effects of L-methionine sulfoximine (MSX), a rare amino acid which inhibits glutamine synthetase (GlnA). Catalyzes the acetylation of MSX. It can also use L-methionine sulfone (MSO). Also catalyzes the acylation of free L-amino acids using an acyl-CoA as acyl donor (By similarity).
Interaction partners:
- Inner membrane protein
- Protein ElaA
- Leucyl/phenylalanyl-tRNA--protein transferase
- Uncharacterized N-acetyltransferase YjgM
- [Ribosomal protein uS5]-alanine N-acetyltransferase
- Probable acyltransferase FabY
Sequence:
MTIRFADKADCAAITEIYNHAVLHTAAIWNDRTVDTDNRLAWYEARQLLGYPVLVSEENGVVTGYASFGDWRSFDGFRYTVEHSVYVHPAHQGKGLGRKLLSRLIDEARRCGKHVMVAGIESQNAASIRLHHSLGFTVTAQMPQVGVKFGRWLDLTFMQLQLDEHAAPDAC
Protein: Zinc finger protein ZFPM2 (Friend of GATA protein 2) (FOG-2) (Friend of GATA 2) (hFOG-2) (Zinc finger protein 89B) (Zinc finger protein multitype 2) (Q8WW38)
Organism: Homo sapiens (Human)
Function: Transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA4, GATA5 and GATA6. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. Also required in gonadal differentiation, possibly be regulating expression of SRY. Probably acts a corepressor of NR2F2 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23226341}.
Interaction partners:
- Transcription factor GATA-4
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Transcription factor GATA-6
- Erythroid transcription factor
- C-terminal-binding protein 2
- Transcription factor GATA-5
- COUP transcription factor 2
- Steroidogenic factor 1
- Wilms tumor protein
- Sex-determining region Y protein
Sequence:
MSRRKQSKPRQIKRPLEDAIEDEEEECPSEETDIISKGDFPLEESFSTEFGPENLSCEEVEYFCNKGDDEGIQETAESDGDTQSEKPGQPGVETDDWDGPGELEVFQKDGERKIQSRQQLPVGTTWGPFPGKMDLNNNSLKTKAQVPMVLTAGPKWLLDVTWQGVEDNKNNCIVYSKGGQLWCTTTKAISEGEELIAFVVDFDSRLQAASQMTLTEGMYPARLLDSIQLLPQQAAMASILPTAIVNKDIFPCKSCGIWYRSERNLQAHLMYYCSGRQREAAPVSEENEDSAHQISSLCPFPQCTKSFSNARALEMHLNSHSGVKMEEFLPPGASLKCTVCSYTADSVINFHQHLFSHLTQAAFRCNHCHFGFQTQRELLQHQELHVPSGKLPRESDMEHSPSATEDSLQPATDLLTRSELPQSQKAMQTKDASSDTELDKCEKKTQLFLTNQRPEIQPTTNKQSFSYTKIKSEPSSPRLASSPVQPNIGPSFPVGPFLSQFSFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIYSPLMPKGATCFECNITFNNLDNYLVHKKHYCSSRWQQMAKSPEFPSVSEKMPEALSPNTGQTSINLLNPAAHSADPENPLLQTSCINSSTVLDLIGPNGKGHDKDFSTQTKKLSTSSNNDDKINGKPVDVKNPSVPLVDGESDPNKTTCEACNITFSRHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEMCLPEQEQRPPLVQQRFLDVANLNNPCTSTQEPTEGLGECYHPRCDIFPGIVSKHLETSLTINKCVPVSKCDTTHSSVSCLEMDVPIDLSKKCLSQSERTTTSPKRLLDYHECTVCKISFNKVENYLAHKQNFCPVTAHQRNDLGQLDGKVFPNPESERNSPDVSYERSIIKCEKNGNLKQPSPNGNLFSSHLATLQGLKVFSEAAQLIATKEENRHLFLPQCLYPGAIKKAKGADQLSPYYGIKPSDYISGSLVIHNTDIEQSRNAENESPKGQASSNGCAALKKDSLPLLPKNRGMVIVNGGLKQDERPAANPQQENISQNPQHEDDHKSPSWISENPLAANENVSPGIPSAEEQLSSIAKGVNGSSQAPTSGKYCRLCDIQFNNLSNFITHKKFYCSSHAAEHVK
Protein: Chromodomain-helicase-DNA-binding protein 1-like (EC 3.6.4.-) (Amplified in liver cancer protein 1) (Q86WJ1)
Organism: Homo sapiens (Human)
Function: ATP-dependent chromatin remodeler that mediates chromatin-remodeling following DNA damage. Recruited to DNA damage sites through interaction with poly-ADP-ribose: specifically recognizes and binds histones that are poly-ADP-ribosylated on serine residues in response to DNA damage. Poly-ADP-ribose-binding activates the ATP-dependent chromatin remodeler activity, thereby regulating chromatin during DNA repair. Catalyzes nucleosome sliding away from DNA breaks in an ATP-dependent manner. Chromatin remodeling activity promotes PARP2 removal from chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:19661379}. Chromosome {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:29220652, ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}. Note=Localizes at sites of DNA damage; recruited by histones H2B and H3 poly-ADP-ribosylated on 'Ser-6' and 'Ser-10', respectively (H2BS6ADPr and H3S10ADPr) by PARP1 or PARP2. {ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}.
Interaction partners:
- Poly [ADP-ribose] polymerase 1
- Histone H4
- Histone H2B type 1-K
- Histone H3.2
- Histone H2B type 1-J
- Histone H2A type 1-B/E
- Histone H2A type 1
- Histone H2A type 1-C
- Poly [ADP-ribose] polymerase 2
- X-ray repair cross-complementing protein 6
Sequence:
MERAGATSRGGQAPGFLLRLHTEGRAEAARVQEQDLRQWGLTGIHLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFENETAKKVKLQNILSQLRKCVDHPYLFDGVEPEPFEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFTLGAQKPAADADLQLSEILKFGLDKLLASEGSTMDEIDLESILGETKDGQWVSDALPAAEGGSRDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRKRVLSPEELEDRQKKRQEAAAKRRRLIEEKKRQKEEAEHKKKMAWWESNNYQSFCLPSEESEPEDLENGEESSAELDYQDPDATSLKYVSGDVTHPQAGAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKGQDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAARGIPTYIYYFPRSKSAVLHSQSSSSSSRQLVP
Protein: Uridine/cytidine kinase UKL1, chloroplastic (EC 2.7.1.48) (Uridine kinase-like protein 2) (Uridine/cytidine kinase 2) (Q9LK34)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the pyrimidine salvage pathway. Phosphorylates uridine to uridine monophosphate (UMP). Phosphorylates cytidine to cytidine monophosphate (CMP). Does not possess uracil phosphoribosyltransferase (UPRTase) activity that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21828290}.
Interaction partners:
- Uridine nucleosidase 1
- Uridine 5'-monophosphate synthase
- UMP kinase
- Uracil phosphoribosyltransferase, chloroplastic
- dCMP deaminase
- Alkaline-phosphatase-like family protein
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase
- Dihydroorotase, mitochondrial
- Cytidine deaminase 7
Sequence:
MPEDSTAIDYVMEKASGPHFSGLRLDGLLSSPSKSSVSSPSHFRLSNSSFSATDDPAAPHQPFVIGVTGGTASGKTTVCDMIIQQLHDHRIVLVNQDSFYRGLTSEELEHVQEYNFDHPDAFDTEQLLHCVDILKSGQPYQIPIYDFKTHQRKVDAFRQVNACDVIILEGILVFHDSRVRDLMNMKIFVDTDADVRLARRIRRDTVERGRDVDSVLEQYAKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAVDLIVQHIHTKLGQHDLCKIYPNVFVIETTFQIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFCKKLCGVSVIRSGESMENALRACCKGIKIGKILIHRDGDNGMQLIYEKLPSDISERHVLLLDPVLGTGNSANQAIELLIQKGVPEAHIIFLNLISAPEGIHCVCKRFPKLKIVTSEIDQCLNEEFRVIPGLGEFGDRYFGTDE
Protein: Aldose 1-epimerase (Q2U576)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Galactokinase
- Galactose-1-phosphate uridylyltransferase
- beta-galactosidase
- Aldose 1-epimerase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
- Probable alpha-galactosidase D
- Probable alpha-galactosidase A
Sequence:
MADEPSVKFTSLGAIIQELNVGGQNIVLGFTKKELYEKYNTPWFGATIGRVANRIKDAKIQSLNNQEYELEKNNDPNALHGGSRGWGRRHFEGPTLLQRNGKDTLLYTYTSPHLDGGYPGTVEIKVFYTASKEDNRSVLSIEYEVELVGDECNETIVNVTNHSYFNLTGGETIEGTSAKLFTQHYLPLDKTGIPFGRIDVHPSKVTEPFTIGPNKEAFDDAFVMDRDVAVIPLDTRERPLQLLAEFHHPESRINLQVHSTEPAFQFYTGQGTNVGAVDGNPSRGPFSGFCIEPSRFVNAINEPDWRHMVVLKKGDKYGSKIVYKTWKDPQ
Protein: Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) (P07895)
Organism: Rattus norvegicus (Rat)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Superoxide dismutase
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL17m
- Aconitate hydratase, mitochondrial
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein mL43
Sequence:
MLCRAACSAGRRLGPAASTAGSRHKHSLPDLPYDYGALEPHINAQIMQLHHSKHHATYVNNLNVTEEKYHEALAKGDVTTQVALQPALKFNGGGHINHSIFWTNLSPKGGGEPKGELLEAIKRDFGSFEKFKEKLTAVSVGVQGSGWGWLGFNKEQGRLQIAACSNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVSQRYIVCKK
Protein: Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (AtB alpha) (PP2A, subunit B, alpha isoform) (Q38821)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment.
Interaction partners:
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''epsilon
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Serine/threonine protein phosphatase 2A regulatory subunit B''alpha
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase PP2A-4 catalytic subunit
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' alpha isoform
Sequence:
MNGGDEVVAASADPSLPLEWRFSQVFGERSAGEEVQEVDIISAIEFDNSGNHLATGDRGGRVVLFERTDTNNSSGTRRELEEADYPLRHPEFRYKTEFQSHDPEFDYLKSLEIEEKINKIRWCQTANGALFLLSTNDKTIKFWKVQDKKIKKICDMNSDPSRTVGNGTVASSSNSNITNSCLVNGGVSEVNNSLCNDFSLPAGGISSLRLPVVVTSHESSPVARCRRVYAHAHDYHINSISNNSDGETFISADDLRINLWNLEISNQSFNIVDVKPAKMEDLSEVITSAEFHPTHCNMLAYSSSKGSIRLIDLRQSALCDSHSKLFEEPEQAGPKSFFTEIIASVSDIKFAKEGRYLLSRDYMTLKLWDINMDAGPVATFQVHEYLKPKLCDLYENDSIFDKFECCISGNGLRAATGSYSNLFRVFGVAPGSTETATLEASRNPMRRHVPIPSRPSRALSSITRVVSRGSESPGVDGNTNALDYTTKLLHLAWHPNENSIACAAANSLYMYYA
Protein: Caveolin-1 (P79132)
Organism: Bos taurus (Bovine)
Function: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P49817}; Peripheral membrane protein {ECO:0000250}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}.
Interaction partners:
- Caveolin-2
- Tyrosine-protein kinase
- Tyrosine-protein kinase Fyn
- Integrin beta-1
- Receptor protein-tyrosine kinase
- Caveolae associated protein 1
- Caveolin-3
- Estrogen receptor
- Calmodulin-like protein 4
- Dynamin-2
Sequence:
MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMAEEMNEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNIRINTQKEI
Protein: BTB/POZ domain-containing protein POB1 (POZ/BTB CONTAINING-PROTEIN 1) (AtPOB1) (Q9FPW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Cullin-3A
- U-box domain-containing protein 17
- Protein NBR1 homolog
- E3 ubiquitin-protein ligase PRT1
- Cullin-3B
Sequence:
MRGTTENTDLFDPKTQMDPDFTRHGSSSDGDFGFAFNDSNFSDRLLRIEIMGGPSDSRSEVEGCTSIADWARHRKRRREDIKKESGVTISDIVACPEEQILTDEQPDMDGCPGGENPDDEGGEAMVEEALSGDEEETSSEPNWGMDCSTVVRVKELHISSPILAAKSPFFYKLFSNGMRESEQRHVTLRINASEEAALMELLNFMYSNAVSVTTAPALLDVLMAADKFEVASCMRYCSRLLRNMPMTPESALLYLELPSSVLMAKAVQPLTDAAKQFLAARYKDITKFHEEVMSLPLAGIEAILSSDELQIASEDAVYDFILKWARAQYPCLEERREILGSRLALSIRFPFMTCRKLKKVLTCSDFEHEIASKLVLEALFFKAEAPHRQRSLASEESASLNRRLIERAYKYRPVKVVEFELPRPQCVVYLDLKREECGGLFPSGRVYSQAFHLGGQGFFLSAHCNMDQQSSFHCFGLFLGMQEKGSVSFGVDYEFSARSKPAEDFISKYKGNYTFTGGKAVGYRNLFGVPWTSFIAEDSQYFINGILHLRAELTIKRSTDP
Protein: NAC domain-containing protein 20 (ONAC020) (OsNAC20) (A2WJP3)
Organism: Oryza sativa subsp. indica (Rice)
Function: Transcription factor that acts redundantly with NAC26 to regulate the expression of genes involved in the biosynthesis of starch and storage proteins in grain. Directly binds to the promoters of starch synthase 1 (SS1), pullulanase (PUL), glutelin A1 (GLUA1), glutelins B4 and B5 (GLUB4 and GLUB5), alpha-globulin and 16 kDa prolamin, and activates their expression (By similarity). Possesses transactivation activity in yeast.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:32989010}. Endoplasmic reticulum {ECO:0000269|PubMed:27872632}.
Interaction partners:
Sequence:
MGEQQQQVERQPDLPPGFRFHPTDEEIITFYLAPKVVDSRGFCVAAIGEVDLNKCEPWDLPGKAKMNGEKEWYFYCQKDRKYPTGMRTNRATEAGYWKATGKDKEIFRNHHMLIGMKKTLVFYKGRAPKGDKTNWVMHEYRLADASPPPPPSSAEPPRQDDWAVCRIFHKSSGIKKPVPVAPHQVPAAANYQQQQQMAMASAGIIQVPMQMQMPSMSDQLQMLDDFSTTASLSLMAPPSYSTLPAGFPLQINSGAHPQQFVGNPSMYYHQQQQMDMAGGGFVVSEPSSLVVSPQDAADQNNNAADISSMACTMDAAIWKY
Protein: Protein cereblon (Protein ohgata) (Q9VH36)
Organism: Drosophila melanogaster (Fruit fly)
Function: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins (Probable). Has an essential role in mediating growth by negatively regulating insulin signaling. It also has a role in maintaining presynaptic function in the neuromuscular junction synapses of third-instar larvae.
Subcellular location: Nucleus {ECO:0000269|PubMed:27702999}.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- RING-box protein 1A
- RING-box protein 1B
- Eukaryotic translation release factor 3, isoform A
- BET1 homolog
- GH11935p
Sequence:
MDEEENSEINSVQARDEDVQLEDQQSQGLQDRQVDVIEQAWNNAMPDEPSPPAEDAFQDPLATDGEGGDALEAMVENVLQDDTASEGSHPSSDMSLESPGSEDDSDLESLPHWMIPQNRLRSAVDMMVSQARNRDGGIAALLSGDNFLQRVRSMVFSQERRRSRTSEETSQEAAEQPVDPPPQQPPRPPIDIGFDTNLPAEHSYFGNHLSRVPGVDYLEVGSVHHMLIFLHQHILFPGEVLPFMIDGRMFDEDMPGLDGLIFGVSFPRLQPPEDNPHKLYGVTCQIYERGESGRGLVFYKSRALQRIVINCDDIKGSPQYIARNPTSKCFSKVKILPEYFLPEPLQTVDMGSMARFRDIPSMRDKYRRFQLSTTTWPSDACQEYSFSSIVERARQRLESQKIDTMPKCPIQLSFWLVRNLHLTEKMMRLTFLTDSVNTRLQLIKSTFKDETLFFCRYCNSSLALCSDLFAMSKHGVQTQYCNPEGYIHETNTVYRVISHAIGYSGEPSTKFSWFPGYQWHIILCKFCAQHVGWEFKAVHPNLTPKVFFGLAGSSVRIGKASEYSPFNGTTYVVRNMMRMISSDME
Protein: Protein LBH (Limb bud and heart-expressed protein) (Q9CX60)
Organism: Mus musculus (Mouse)
Function: Modulates the activity of key transcription factors involved in cardiogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11336496}. Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSVYFPIHCSDYLRSAEMTEVMMNAPSMEEIGLSPRKDGLSYQIFPDPSDFDRCCKLKDRLPSIVVEPTEGEVESGELRWPPEEFLVQEDEQDNCEETTNEKKDQ
Protein: type I protein arginine methyltransferase (EC 2.1.1.319) (F1R3J9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Forkhead box protein O1-A
- Forkhead box protein O1-B
- Forkhead box O4
- Forkhead box O3b.
- Forkhead box O3A
- Forkhead box O6 a
- Runt-related transcription factor
- Core-binding factor subunit beta
- rRNA 2'-O-methyltransferase fibrillarin
Sequence:
MAETADRMEVSQGESSAKPAAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNKHLFKDKVVLDVGSGTGILCMFAAKAGAKKVIGIECSSISDYAVKIVKANKLDHIVTIIKGKVEEVELPVENVDIIISEWMGYCLFYESMLNTVIYARDKWLKPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKEVAITEPLVDVVDPKQLVSTACLIKEVDIYTVKIEDLSFTSPFCLQVKRNDYIHALVTYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYLDDYLTVKTGEEIFGTISMKPNVKNNRDLDFTVDIDFKGQLCEVSKTSEYRMR
Protein: Cytohesin 1a (Cytohesin-3 isoform X1) (A0A2R8QK04)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- ADP-ribosylation factor 6
- FERM domain-containing protein 4A
- ADP-ribosylation factor-like 4, like.
- ADP-ribosylation factor-like protein 4A
- Large ribosomal subunit protein mL45
- Si:rp71-17i16.5
Sequence:
MPHKEQADVPEDLSLEERDELSNIRRRKKELLDDIERLKFEIAEVMTEIEQLTCVGESKTTQRNKQIAMGRKKFNMDPKKGIQFLLENDLLQQTPEDIAQFLYKGEGLNKTVIGDYLGERDEFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCQCNPGVFQSTDTCYVLSFAIIMLNTSLHNPNVRDKPAVERFISMNRGINDGGDLPEELLRNLYESIKSEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEEPRKPNCFELYNPNHKGQVIKACKTEADGRVVEGNHVVYRISAPTPEEKEEWIKSIKASISRDPFYDMLATRKRRIANKK