wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger and BTB domain-containing protein 7B (Krueppel-related zinc finger protein cKrox) (hcKrox) (T-helper-inducing POZ/Krueppel-like factor) (Zinc finger and BTB domain-containing protein 15) (Zinc finger protein 67 homolog) (Zfp-67) (Zinc finger protein 857B) (Zinc finger protein Th-POK) (O15156)
Organism: Homo sapiens (Human)
Function: Transcription regulator that acts as a key regulator of lineage commitment of immature T-cell precursors. Exerts distinct biological functions in the mammary epithelial cells and T cells in a tissue-specific manner. Necessary and sufficient for commitment of CD4 lineage, while its absence causes CD8 commitment. Development of immature T-cell precursors (thymocytes) to either the CD4 helper or CD8 killer T-cell lineages correlates precisely with their T-cell receptor specificity for major histocompatibility complex class II or class I molecules, respectively. Cross-antagonism between ZBTB7B and CBF complexes are determinative to CD4 versus CD8 cell fate decision. Suppresses RUNX3 expression and imposes CD4+ lineage fate by inducing the SOCS suppressors of cytokine signaling. induces, as a transcriptional activator, SOCS genes expression which represses RUNX3 expression and promotes the CD4+ lineage fate. During CD4 lineage commitment, associates with multiple sites at the CD8 locus, acting as a negative regulator of the CD8 promoter and enhancers by epigenetic silencing through the recruitment of class II histone deacetylases, such as HDAC4 and HDAC5, to these loci. Regulates the development of IL17-producing CD1d-restricted naural killer (NK) T cells. Also functions as an important metabolic regulator in the lactating mammary glands. Critical feed-forward regulator of insulin signaling in mammary gland lactation, directly regulates expression of insulin receptor substrate-1 (IRS-1) and insulin-induced Akt-mTOR-SREBP signaling (By similarity). Transcriptional repressor of the collagen COL1A1 and COL1A2 genes. May also function as a repressor of fibronectin and possibly other extracellular matrix genes. Potent driver of brown fat development, thermogenesis and cold-induced beige fat formation. Recruits the brown fat lncRNA 1 (Blnc1):HNRNPU ribonucleoprotein complex to activate thermogenic gene expression in brown and beige adipocytes (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q64321}.
Interaction partners:
- CUB domain-containing protein 1
- Heterogeneous nuclear ribonucleoprotein U
- Runt-related transcription factor 3
Sequence:
MGSPEDDLIGIPFPDHSSELLSCLNEQRQLGHLCDLTIRTQGLEYRTHRAVLAACSHYFKKLFTEGGGGAVMGAGGSGTATGGAGAGVCELDFVGPEALGALLEFAYTATLTTSSANMPAVLQAARLLEIPCVIAACMEILQGSGLEAPSPDEDDCERARQYLEAFATATASGVPNGEDSPPQVPLPPPPPPPPRPVARRSRKPRKAFLQTKGARANHLVPEVPTVPAHPLTYEEEEVAGRVGSSGGSGPGDSYSPPTGTASPPEGPQSYEPYEGEEEEEELVYPPAYGLAQGGGPPLSPEELGSDEDAIDPDLMAYLSSLHQDNLAPGLDSQDKLVRKRRSQMPQECPVCHKIIHGAGKLPRHMRTHTGEKPFACEVCGVRFTRNDKLKIHMRKHTGERPYSCPHCPARFLHSYDLKNHMHLHTGDRPYECHLCHKAFAKEDHLQRHLKGQNCLEVRTRRRRKDDAPPHYPPPSTAAASPAGLDLSNGHLDTFRLSLARFWEQSAPTGPPVSTPGPPDDDEEEGAPTTPQAEGAMESS
Protein: Nicolin-1 (NPCEDRG) (Tubulin polyglutamylase complex subunit 5) (PGs5) (Q9BSH3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:12392556}.
Interaction partners:
- Leucine-rich repeat-containing protein 49
- Polyglutamylase complex subunit TTLL1
- Tubulin polyglutamylase complex subunit 2
- Tubulin polyglutamylase complex subunit 1
- SANT and BTB domain regulator of class switch recombination
- TBC1 domain family member 19
- Centriolar satellite-associated tubulin polyglutamylase complex regulator 1
- Aminomethyltransferase, mitochondrial
Sequence:
MSRVLVPCHVKGSVALQVGDVRTSQGRPGVLVIDVTFPSVAPFELQEITFKNYYTAFLSIRVRQYTSAHTPAKWVTCLRDYCLMPDPHSEEGAQEYVSLFKHQMLCDMARISELRLILRQPSPLWLSFTVEELQIYQQGPKSPSVTFPKWLSHPVPCEQPALLREGLPDPSRVSSEVQQMWALTEMIRASHTSARIGRFDVDGCYDLNLLSYT
Protein: phosphoglycerate mutase (2,3-diphosphoglycerate-independent) (EC 5.4.2.12) (Q9NG18)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MALTLAAHKTLPRRKLVLVVLDGVGIGPRDEYDAVHVAKTPLMDALFNDPKHFRSICAHGTAVGLPTDADMGNSEVGHNALGAGRVVLQGASLVDDALESGEIFTSEGYRYLHGAFSQPGRTLHLIGLLSDGGVHSRDNQVYQILKHAGANGAKRIRVHALYDGRDVPDKTSFKFTDELEEVLAKLREGGCDARIASGGGRMFVTMDRYEADWSIVERGWRAQVLGEGRAFKSAREALTKFREEDANISDQYYPPFVIAGDDGRPIGTIEDGDAVLCFNFRGDRVIEMSRAFEEEEFDKFNRVRLPKVRYAGMMRYDGDLGIPNNFLVPPPKLTRTSEEYLIGSGCNIFALSETQKFGHVTYFWNGNRSGKLSEERETFCEIPSDRVQFNQKPLMKSKEITDAAVDAIKSGKYDMIRINYPNGDMVGHTGDLKATITSLEAVDQSLQRLKEAVDSVNGVFLITADHGNSDDMVQRDKKGKPVRDAEGNLMPLTSHTLAPVLFLSEALVLIPVCKCGQTFRVRPCNVTATFINLMGFEAPSDYEPSLIEVA
Protein: Pro-cathepsin H [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain] (Q3T0I2)
Organism: Bos taurus (Bovine)
Function: Important for the overall degradation of proteins in lysosomes.
Subcellular location: Lysosome {ECO:0000250}.
Interaction partners:
- BH3-interacting domain death agonist
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- Cystatin-A
- Cathepsin D
- Pulmonary surfactant-associated protein B
Sequence:
MWAVLPLLCAGAWLLGAPACGAAELAANSLEKFHFQSWMVQHQKKYSSEEYYHRLQAFASNLREINAHNARNHTFKMGLNQFSDMSFDELKRKYLWSEPQNCSATKSNYLRGTGPYPPSMDWRKKGNFVTPVKNQGSCGSCWTFSTTGALESAVAIATGKLPFLAEQQLVDCAQNFNNHGCQGGLPSQAFEYIRYNKGIMGEDTYPYRGQDGDCKYQPSKAIAFVKDVANITLNDEEAMVEAVALHNPVSFAFEVTADFMMYRKGIYSSTSCHKTPDKVNHAVLAVGYGEEKGIPYWIVKNSWGPNWGMKGYFLIERGKNMCGLAACASFPIPLV
Protein: Pseudooxynicotine dehydrogenase (EC 1.4.2.3) (Pseudooxynicotine amine oxidase) (PNAO) (H8ZPX1)
Organism: Pseudomonas sp
Function: Catalyzes the deamination of pseudooxynicotine to 3-succinoylsemialdehyde-pyridine in the nicotine degradation pathway.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MANDKGDISKDGVSRRKFLGGAVIGAAAAAGVGSQILSLSATAQGADKERVGPLQSNVDYDAVVIGGGFAGVTAARELSRSGLKTLVLEGRSRLGGRTFTSKLDGEKVELGGTWVHWTQPNVWTEVMHYGLEIEETVGLASPETVIWVTDNQVKRAPAAEAFEIFGAACTEYYKEAHNIYPRPFDPFFAKKALQEMDGLSASEYLNKLSLTREQKDMMDSWLSGNGHNYPETIAYSEIMRWFALSNFNMPTMFDSIARYKIKSGTVSLLEAMVAESDMEVQLSTPVLKVKQDSHRVLITTEEGTIAASAVVMAVPLNTMGDVEYSPRLSDAKSEIASQGHAGKGVKGYIRIKQDVGNVMTYAPARNDVTPFTSVFTDHVGENGTLLIAFSADPKLVDINDSKAVEKALHPLLPGVEVTSSYGYDWNLDPFSKGTWCTYRPGQTTRYLTELQKREGRLFFAGSDMANGWRGFIDGAIESGREVGYQVASYLKGKNSNA
Protein: Galectin-9C (Gal-9C) (Galectin-9-like protein B) (Q6DKI2)
Organism: Homo sapiens (Human)
Function: Binds galactosides.
Interaction partners:
- Hepatitis A virus cellular receptor 2
- Lymphocyte activation gene 3 protein
- C-type lectin domain family 7 member A
- Cytotoxic T-lymphocyte protein 4
- T-cell immunoreceptor with Ig and ITIM domains
- Programmed cell death protein 1
- CD44 antigen
- Programmed cell death 1 ligand 1
- Tumor necrosis factor receptor superfamily member 9
- B- and T-lymphocyte attenuator
Sequence:
MAFSGCQAPYLSPAVPFSGTIQGGLQDGFQITVNGAVLSCSGTRFAVDFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQKGTWGPEERKMHMPFQKGMPFDLCFLVQSSDFKVMVNGSLFVQYFHRVPFHRVDTISVNGSVQLSYISFQNPRAVPVQPAFSTVPFSQPVCFPPRPRGRRQKPPSVRPANPAPITQTVIHTVQSASGQMFSQTPAIPPMMYPHPAYPMPFITTIPGGLYPSKSIILSGTVLPSAQRFHINLCSGSHIAFHMNPRFDENAVVRNTQINNSWGSEERSLPRKMPFVRGQSFSVWILCEAHCLKVAVDGQHVFEYYHRLRNLPTINKLEVGGDIQLTHVQT
Protein: PLAGL2 (Pleiomorphic adenoma gene-like 2) (Q925T4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTFFTSVPPWIQDAKQEEEVGWKLVPRPRGREAESQVKCQCEISGTPFSNGEKLRPHSLPHPEQRPYSCPQLHCGKAFASKYKLYRHMATHSAQKPHQCMYCDKMFHRKDHLRNHLQTHDPNKEALHCSECGKNYNTKLGYRRHLAMHAASSGDLSCKVCLQTFESTQALLEHLKAHSRRVAGGAKEKKHPCDHCDRRFYTRKDVRRHLVVHTGRKDFLCQYCAQRFGRKDHLTRHVKKSHSQELLKIKTEPVDMLGLLSCSSTVSVKEELSPVLCMASRDVMGAKAFPGMLPMGMYGAHIPTMPSAGMPHSLVHNTLPMGMSYPLESSPISSSAQLPPKYQLGSTSYLPDKLPKVEVDSFLAELPGSLSLSSAEPQPASPQPAAAAALLDEALLAKSPANLSEALCAANVDFSHLLGFLPLNLPPCNPPGATGGLVMGYSQAEAQPLLTTLQAQPQDSAGAGGPLNFGPLHSLPPVFTSGLSTTTLPRFHQAFQ
Protein: Rfx, isoform G (A0A0B4K621)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHSRYGFDCQTRHYQQHQQTHHQHHHHHHPNPPCSIPLESPPTPPVISPSAAAAVAYSNLLEKCRCKQSVAANPVPAPPAQLQLQLHHHHHHHHHQTFVASASATSYSNCSALGLGSRTGSGSGSGSGTGSTPSTSSLANSSCAAATNISGGSSNATMYHHHHRRHNNLSYCGVSGQEQNYQVQYVDSELYHSNSSQTQMTYPFCPVGDYQGNGQTAYYSTTGQYGTTSSAGGSSNGAHSTTLPYLVPVEEGILLNGSAHSLSQSQSQSHGRDSPHSLTEVAYIQEAQSTPQTPTSTTTTHSASGGSLGTGGGGASPDSDQSALGSSNKIASATIKWLSRNYETADGVSLPRSTLYNHYMQHCSEHKLEPVNAASFGKLIRSVFSGLRTRRLGTRGNSKYHYYGIRIKPGSLLNSQAMDDKQMLAAGYGPSSDGTGGPGSGPMVSVTSSTAGQLTGSNGLGGGHGQRHSNGTKKHTFKPETYEACIQYIGDGTSALPSFPPIELNHSFNSELTLEDVDTFRGLYREHCESFLDAVLNLEFNTVEFLLRDFWRASDNNNLDECEEEKYLSKTKLYLLCHCAEVQKFVREVDYQFYQNTVDVIIPDVLRSIPNALTQAIRNFAKNLEIWLCESMLGVPEQLAQIKTSAVSAFCQTLRRYTSLNHLAQAARAVLQNGAQISQMLSDLNRVDFHNVQEQAAWVSQCAPAVVQRLESDFKAALQQQSSLEQWASWLQLVVESAMEEYNGKPTYARAARQFLLKWSFYSSMIIRDLTLRSASSFGSFHLIRLLFDEYMFYLVEHKIAEAQDKTAIAVICERMKKDMDFEFECQFAYITSDTEHQTTPSSASSGGDVGNEAKRLKQE
Protein: Serine/threonine protein phosphatase 2A regulatory subunit (Q5BIJ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDNEALDPTIKSSTSAATPTAAASETTTTAASSVVETTTTIAAATASAAESKNETTATNNNSNTSGSISSSSSNNIVIPASATNGIKESNSNLSTTTTAAAVAAATTVEGVAPAITSTIVVTGGTPPLSSLANKLKDNTPPYDAPPPTPISKVLNITGTPIVRKEKRQTSARYNASKNCELTALIPLNEKTAASEREELFIQKIQQCCTLFDFSEPLSDLKFKEVKRAALHEMVDFLTNQNGVITEVIYPEAINMFAVNLFRTLPPSSNPNGAEFDPEEDEPTLESSWPHLQLVYELFLRFLESPDFQPSMAKRFIDHQFVLQLLDLFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNVFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKQFLLKVLLPLHKAKSLSVYHPQLTYCVVQFLEKDPSLSEAVIKSLLKFWPKTHSPKEVMFLNELEELLDVIEPAEFQKVMVPLFRQIAKCVSSPHFQVAERALYYWNNEYIMSLITDNSAVILPIMFPALNRNSKTHWNKTIHGLIYNALKLFMEIDQRLFDECSKNYKQEKQMEREKLSQREELWQQVESLAKTNPEWTKARRFNDCLPVSDSRALCDQYSENSDSAYDQSEQRARQPPPPLPPQKQAHQEPRE
Protein: 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta (OFOR2) (EC 1.2.7.11) (Q9YBX8)
Organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Function: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as pyruvate, 2-oxobutyrate, glyoxylate and 2-oxoglutarate to form their CoA derivatives.
Interaction partners:
- 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha
- 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha
- Succinate--CoA ligase subunit alpha
- Succinate--CoA ligase subunit beta
- Pyruvate kinase
- Citrate synthase
- 2-oxoacid oxidoreductase
- Pyruvate dehydrogenase complex, E2 component
- isocitrate dehydrogenase
- Acetate--CoA ligase
Sequence:
MARSWLDYKTQAWVQWCPGCGDFGILNSIYRAVSELGIDPENLAVVGGIGCSGRTTYYVKGSNFHALHGRAIPVATGVKLANPHLNVIVAGGDGDLMGIGGGHFVALGRRNLNITVLLFDNAVYGLTKGQAAPTLPAWVKTKALSMPNIHDNINPVLLAFAAGYTFIARGYAYHTQQLKELIKTAVRHRGAALVDILQPCPTYNNIMTNKWYEERIYYVDQEEGYDPIIRTPEEFQKKAPAIAAKLMEFGDRIPLGILYWNQTRESFEERLEKIMPGYMSAPPATRRIELEGKPFLHPFDIFKDRLVTP
Protein: Neuronal pentraxin chromo domain (H3BLN6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MELSAVGERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSRLIAAFEQKERERELYGPKKRGPKPKTFLLKQELPARGNISSAPAPAMPTALHSKMDELEGQLLAKVLALEKERAALSHGSHQQRQEVEKELNALQGRVAELEHGSSAYSPPDAFKVSIPIRNNYMYARVRKALPELYAFTACMWLRSRSGGSGQGTPFSYSVPGQANEIVLLEAGLEPMELLINDKVAQLPLSLKDSNWHHICISWTTRDGLWSAYQDGELRGSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWDHALTPAQVLGMANCTGPLMGNVLPWEDKLVEAFGGAKKAAFDVCKGRAKA
Protein: Fructose-bisphosphate aldolase (EC 4.1.2.13) (J3KPS3)
Organism: Homo sapiens (Human)
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate kinase 1
- Glyceraldehyde-3-phosphate dehydrogenase
- ATP-dependent 6-phosphofructokinase, liver type
- Alpha-enolase
- Phosphoglycerate kinase 2
- ATP-dependent 6-phosphofructokinase, platelet type
- ATP-dependent 6-phosphofructokinase, muscle type
- Glucose-6-phosphate isomerase
- Probable phosphoglycerate mutase 4
Sequence:
MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQVGLQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSNHAY
Protein: Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Suppressor of actin mutations 1-like protein) (Q9ES21)
Organism: Rattus norvegicus (Rat)
Function: Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 3-phosphate (PtdIns(3)P) and has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2). Shows a very robust PtdIns(4)P phosphatase activity when it binds PtdIns(4)P in a 'cis' configuration in the cellular environment, with much less activity seen when it binds PtdIns(4)P in 'trans' configuration (By similarity). PtdIns(4)P phosphatase activity (when it binds PtdIns(4)P in 'trans' configuration) is enhanced in the presence of PLEKHA3 (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10887188}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NTJ5}; Multi-pass membrane protein {ECO:0000255}. Note=Trafficking between the ER and Golgi is regulated by nutrient status and by TMEM39A (By similarity). Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS) in the presence of phosphatidylinositol-4,5-bisphosphate (PubMed:27044890). {ECO:0000250|UniProtKB:Q9NTJ5, ECO:0000269|PubMed:27044890}.
Interaction partners:
- Phosphatidylinositol 4-kinase alpha
- Inositol polyphosphate 5-phosphatase OCRL
- Phosphatidylinositol 4-kinase beta
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Myotubularin
- Phosphatidylinositol 4-kinase type 2-alpha
- Phosphatidylinositol 4-kinase type 2-beta
Sequence:
MAATAYEHLKLHITPEKFYVEACDDGADDVLIIDRVSTEVTLAVKKDVPPSAVTRPIYGIMGTIHLVAGNYLVVITKKMKVGEFFNHVIWKATDFDVLSYKKTMLHLTDIQLQDNKTFLAMLNHVLSTDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYSGNRASFVQTRGSIPVFWSQRPNLKYKPDPQINKVANHMDGFQRHFDSQVIIYGKQVIINLVNHKGSEKPLEQTFAKMVSSLGSGMIRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGKVVTNQEGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKIYKNAWADNANACAKQYAGTGALKTDFTRTGKRTQLGLVMDGFNSLLRYYKNNFSDGFRQDSIDLFLGNYSVDELDSHSPLSVPRDWKFLALPIIMVVAFSMCIICLLMAGDTWTETLAYVLFWGVASIGTFFIILYNGKDFVDAPRLVQKEKID
Protein: Tesmin (Metallothionein-like 5, testis-specific) (Testis-specific metallothionein-like protein) (Q9Y4I5)
Organism: Homo sapiens (Human)
Function: Essential for normal spermatogenesis and male fertility (By similarity). Required for the completion of meiosis in male germ cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9WTJ6}. Nucleus {ECO:0000250|UniProtKB:Q9WTJ6}. Note=Predominantly localized to the cytoplasm. Translocates from the cytoplasm to the nucleus in the G2/M transition upon treatment with cadmium, cobalt or zinc. {ECO:0000250|UniProtKB:Q9WTJ6}.
Interaction partners:
- Metallothionein
- Protein lin-9 homolog
Sequence:
MEEGPLPGGLPSPEDAMVTELLSPEGPFASENIGLKAPVKYEEDEFHVFKEAYLGPADPKEPVLHAFNPALGADCKGQVKAKLAGGDSDGGELLGEYPGIPELSALEDVALLQAPQPPACNVHFLSSLLPAHRSPAVLPLGAWVLEGASHPGVRMIPVEIKEAGGTTTSNNPEEATLQNLLAQESCCKFPSSQELEDASCCSLKKDSNPMVICQLKGGTQMLCIDNSRTRELKALHLVPQYQDQNNYLQSDVPKPMTALVGRFLPASTKLNLITQQLEGALPSVVNGSAFPSGSTLPGPPKITLAGYCDCFASGDFCNNCNCNNCCNNLHHDIERFKAIKACLGRNPEAFQPKIGKGQLGNVKPQHNKGCNCRRSGCLKNYCECYEAQIMCSSICKCIGCKNYEESPERKTLMSMPNYMQTGGLEGSHYLPPTKFSGLPRFSHDRRPSSCISWEVVEATCACLLAQGEEAEKEHCSKCLAEQMILEEFGRCLSQILHTEFKSKGLKME
Protein: Forkhead box K, isoform G (Forkhead box K, isoform H) (Forkhead box K, isoform I) (Forkhead box K, isoform J) (LD11294p) (Q8IQE9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MAATTTTTTTTLATTTGNSSSTNNSSSNNNNSIASSHNNNNNIVTVHTVLNNPPTNTAGGGVADAATVAIAKDMLQLHHGAAAAATAALNNYNNSSNNNNNSADQLTGNSNNSANHPPATSSTTNSSSSSTTSANTNNPSANAASTLTSSSPPYGELRFNQEVLPITDAVTVIGRNSSTSLVHFNVAENNLVSRKHFQVLYDVELRAFFVQCLSKNGIFVDDFLQRRNVDPLRLPQRCYFRFPSTEIRIEFESYVPATSSDAIDGHSPSLVVGGGGGVAGGGAHVIITPLPRDELHQQQLHHHQQQPHLQQQQHPHHPPAHHLPLQQQQQQQQPAHHPLPHTPHHPLHHTALHQQQQRSGSIVVAPPAGAAAHLIAGDGPGIYSPLKISIPKKEQKSPYLSPTGTISAANSCPASPRQGFIQNQPNNYNNYGNNNTQDLFQTPSTASYNHNEKPPYSYAQLIVQAISAAPDKQLTLSGIYSFIVKHYPYYRKETNKGWQNSIRHNLSLNRYFIKVARSQDEPGKGSFWRIDPDSGAKLIDHSYKKRRQRSSQGFRPPYGMPRSAPVSPSHMDNSRESSPLQDIVLQSAPGSPGMSLEQRAADPEIIYNSQNAHQQQQQQQQQQQQQTLSNNSNQYSSGSPYYVTNQSSGVATPQTHVEGSAASGGGGGGGVGALLALKRNHVMGGGASQHTLHQQQAVAQQQHSEIIYEELPTDYSGHIEASEEECVTTATDATVAKRPKYVSEVL
Protein: Putative glutamine amidotransferase GAT1_2.1 (EC 2.4.2.-) (Class I glutamine amidotransferase) (GAT1_2 domain-containing protein 1) (Q8H0Z4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative glutamine amidotransferase that represses shoot branching. May act as a factor that links nitrogen stress response and branching control. May activate strigolactones by amidation, or represent a new pathway for repression of shoot branching.
Interaction partners:
- Protein DUF642 L-GALACTONO-1,4-LACTONE-RESPONSIVE GENE 1
- Protein PELOTA 1
- Protein DJ-1 homolog A
- 3-phosphoinositide-dependent protein kinase 2
- Endoglucanase 5
Sequence:
MVVANDLSSKILPRVLIVSRRTLRKNKYVDFVGEYHLDLIVSSGAVPVIVPRVNGIHSMLQSFEPIHGVLLCEGEDVDPSLYADDELSDLSPEDMEEIKKAHAEDMTIDREKDSIELTLARLCLERNIPFLGICRGSQILNVAAGGTLYQDIDKELGTTMTTTNHIDYDNYDGHRHEARIVEETPLHKLFEEMEIMVNSYHHQGVKRLAQRFVPMAYAPDGLIEGFYDPNRYDPKEGQFLMGLQFHPERMRLPGSDEFDYPGCALVYQEFVKAVIAFQKKQVNATQVEMKRKTTTLVKSFSQAEFLEANTVLSKQQENRLKQMGATVRNSCVYMKRMKMKEEQERAMDKLSAERLSDMLSFHHMMARLCSNAIKRKLLEPEHTDRTIESSFFLNY
Protein: 5'-AMP-activated protein kinase subunit beta-1 (AMPK subunit beta-1) (AMPKb) (Q9Y478)
Organism: Homo sapiens (Human)
Function: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
Interaction partners:
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase subunit gamma-2
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit gamma-3
- 5'-AMP-activated protein kinase subunit gamma-1
- 5'-AMP-activated protein kinase subunit beta-2
- Serine/threonine-protein kinase STK11
- Calcium/calmodulin-dependent protein kinase kinase 2
- Serine/threonine-protein kinase mTOR
- Tuberin
Sequence:
MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI
Protein: Possible membrane protein (O05444)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MQAANRRSADTICGVTAPAPLPIPRTRSWPAIVVAAIAAVVAVAALIVALTNARPAATPATTSVPTYTAAQTAAAQRQLCDTYKLVAHAVPVDTNGSDKALARITLTNAAAILDNAAADPALDAKHRDAARASDRLPHNDRNGEWWHSS
Protein: RE40914p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Uncharacterized protein, isoform C) (Q8SXS0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- V-type proton ATPase subunit E
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit G
- GEO12035p1
- ATPase H
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 16 kDa proteolipid subunit c
- Uncharacterized protein
Sequence:
MLKSTIVDPRVRLVPSKKLLDFLDAQKKHLKELPENVAKIMKQRGHTLPTSIRIIKDAGLEYKRPKLNYELLTKLTENLADKPEEPAKDKSEPDSGVKDSDDAKSTREVKHFLYLTDLHWLSKTLAELRRQDHCQVFLHQLIESCDLLLPENEMKPRNPELEARCQRLRAEQQNRDYLKMTKNVDAGLKHYPEDTISYQIKSLNKQIIAVVQFIFSVAAGFTFGFFGVNLMVGPLPFGFRILLGVIVALIIALAEMYFLAKKLHEYDEVLDAPKRKPQPSTPAKRTPPAEGSQVQTLKPHVD
Protein: Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase 1b) (SAPK1b) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3) (P53779)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the amyloid-beta precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-BMAL1 heterodimer and plays a role in the photic regulation of the circadian clock. Phosphorylates JUND and this phosphorylation is inhibited in the presence of MEN1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16737965}. Membrane {ECO:0000269|PubMed:16737965}; Lipid-anchor {ECO:0000269|PubMed:16737965}. Nucleus {ECO:0000269|PubMed:16737965}. Mitochondrion {ECO:0000269|PubMed:16737965}. Note=Palmitoylation regulates MAPK10 trafficking to cytoskeleton. Recruited to the mitochondria in the presence of SARM1 (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR
Protein: Chromatin remodeling factor17 (F4JY25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MARASKREVSSDEAYSSEEEEQVNDQANVEEDDDELEAVARSAGSDEEDVAPDEAPVSDDEVVPVEDDAEEDEEDEEKAEISKREKARLKEMQKMKKQKIQQILDSQNASIDADMNNKGKGRIKYLLQQTELFAHFAKSDPSPSQKKGKGRGRHSSKLTEEEEDEECLKEEEGGIVGSGGTRLLTQPACIQGKLRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLGNPEERRHIREELLVAGKFDICVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLEVVNGGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGDHLVTNAGKMVLLDKLLPKLKDRDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGDERDASIEAYNKPGSEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTENAIEAKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIQFKMDDSADFYDFDDDNKDESKVDFKKIVSENWNDPPKRERKRNYSEVEYFKQTLRQGAPAKPKEPRIPRMPQLHDFQFFNIQRLTELYEKEVRYLMQAHQKTQMKDTIEVDEPEEVGDPLTAEEVEEKELLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAQVFQVRYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYRNPWLELKIQYGQNKGKLYNEECDRFMICMVHKLGYGNWDELKAAFRTSPLFRFDWFVKSRTTQELARRCDTLIRLIEKENQEFDERERQARKEKKLSKSATPSKRPSGRQANESPSSLLKKRKQLSMDDYVSSGKRRK