wanglab/gogpt-training-data huggingface dataset:
Protein: ABC transporter G family member 30 (ABC transporter ABCG.30) (AtABCG30) (Pleiotropic drug resistance protein 2) (AtPDR2) (Q8GZ52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with ABCG40, import into the embryo the abscisic acid (ABA) delivered from the endosperm via ABCG25 and ABCG31-mediated export to suppress radicle extension and subsequent embryonic growth. Involved in root secretion of phytochemicals (phenolics and sugars) which regulate soil microbiota, influencing both fungal and bacterial communities. May be a general defense protein (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26334616}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein DETOXIFICATION 50
- Probable protein S-acyltransferase 19
- Protein NRT1/ PTR FAMILY 4.6
- Cytochrome P450, family 702, subfamily A, polypeptide 6
Sequence:
MIQTGEEDEEKATSLEVEFASGNGVDDEEELRLQWATVERLPTFKRVTTALLARDEVSGKGRVIDVTRLEGAERRLLIEMLVKQIEDDNLRLLRKIRKRIDKVGIELPTVEVRFNNLSVEAECQVIHGKPIPTLWNTIKGLLSEFICSKKETKIGILKGVSGIVRPGRMTLLLGPPGCGKTTLLQALSGKFSDSVKVGGEVCYNGCSLSEFIPEKTSSYISQNDLHIPELSVRETLDFSACCQGIGSRMEIMKEISRMEKLQEIIPDPAVDAYMKATSVEGLKNNLQTDYILKILGLDICADTRVGDATRPGISGGEKRRLTTGELVVGPATTLFMDEISNGLDSSTTFQIVSCLQQLAHIAEATILISLLQPAPETFELFDDVILMGEGKIIYHAPRADICRFFEEFGFKCPERKGVADFLQEIMSKKDQEQYWCHRDKPYSYISVDSFINKFKESNLGLLLKEELSKPFNKSQTRKDGLCYKKYSLGKWEMLKACSRREFLLMKRNSFIYLFKSALLVFNALVTMTVFLQVGATTDSLHGNYLMGSLFTALFRLLADGLPELTLTISRLGVFCKQKDLYFYPAWAYAIPSIILKIPLSVLDSFIWTLLTYYVIGYSPEVKRFFLQFLILSTFNLSCVSMFRAIAAIFRTIIASTITGAISILVLSLFGGFVIPKSSMPAWLGWGFWLSPLSYAEIGLTANEFFSPRWSKVISSKTTAGEQMLDIRGLNFGRHSYWTAFGALVGFVLFFNALYVLALTYQNNPQRSRAIISHEKYSRPIEEDFKPCPKITSRAKTGKIILPFKPLTVTFQNVQYYIETPQGKTRQLLSDITGALKPGVLTSLMGVSGAGKTTLLDVLSGRKTRGIIKGEIKVGGYPKVQETFARVSGYCEQFDIHSPNITVEESLKYSAWLRLPYNIDSKTKNELVKEVLETVELDDIKDSVVGLPGISGLSIEQRKRLTIAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTVVCTIHQPSIDIFETFDELILMKNGGQLVYYGPPGQNSSKVIEYFESFSGLPKIQKNCNPATWILDITSKSAEEKLGIDFSQSYKDSTLYKQNKMVVEQLSSASLGSEALRFPSQFSQTAWVQLKACLWKQHYSYWRNPSHNITRIVFILLDSTLCGLLFWQKAEDINNQQDLISIFGSMYTLVVFPGMNNCAAVINFIAAERNVFYRERFARMYSSWAYSFSQVLIEVPYSLLQSLLCTIIVYPTIGYHMSVYKMFWSLYSIFCSLLIFNYSGMLMVALTPNIHMAVTLRSSFFSMLNLFAGFVIPKQKIPKWWIWMYYLSPTSWVLEGLLSSQYGDVDKEILVFGEKKRVSAFLEDYFGYKHESLAVVAFVLIAYPIIVATLFAFFMSKLSFQKK
Protein: Sestrin homolog (dSesn) (Q9W1K5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions as a negative feedback regulator of TOR function.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y6P5}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6P5}.
Interaction partners:
- FI11917p
- GATOR complex protein Iml1
- GATOR2 complex protein Wdr24
- Gigas, isoform A
- GATOR complex protein NPRL3
- Peroxiredoxin 2
- Ribosomal protein S6 kinase
- GATOR complex protein NPRL2
- Forkhead box protein O
Sequence:
MYYAVDYYADMGQISQDCFAATQTGASDFDMDELDDLDQVTQVIGYHPQFHDHFLATQNFIMKGDGPLPNDYRYYLAIIAAARHQCPYLVKRYEKEFINQGGDSAWLGGLDFIPAKLRAIYDINKILAHRPWLLRKEHIERLTKGKNSWSLSEVVHAMVLLSHFHSLSSFVFSCGLTQKLDGLSSPKLKSPPAAVAALAPTILITPTSPTEPQKGKPVLAEISLNNANPDYDSQTAASSNGGAPPDSANAVADGPDATTLNGYLATAQQLPQQHGISVETLMERMKVLSQKQDECSEAELSSRFQKVEQQTAELAAVTPEAAVGVPTNLSHYVDDANFIYQDFARRGTESINTFRIQDYSWEDHGYSLVDGLYNDVGIFLDAKFRAAYNLTYCTMGGIKNVDTSKFRRAIWNYIQCIYGIRHDDYDYGEVNQLLVRPLKMFIKTACCFPERITTKDYDSVLVELQDSEKVHVNLMIMEARNQAELLYALREIMRYMT
Protein: Nonsense-mediated mRNA decay factor SMG9 (Suppressor with morphogenetic effect on genitalia protein 9) (Q9XWJ1)
Organism: Caenorhabditis elegans
Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing smg-1 and recruited to stalled ribosomes.
Interaction partners:
- Nonsense-mediated mRNA decay factor SMG8
- Serine/threonine-protein kinase smg-1
- Nonsense-mediated mRNA decay protein
- PIN domain-containing protein
- DNA/RNA-binding domain-containing protein
- Eukaryotic peptide chain release factor subunit 1
- MIF4G domain-containing protein
- UPF3 domain-containing protein
- Regulator of nonsense transcripts 1
- 5'-3' exoribonuclease 1
Sequence:
MKKVEILKTSRPSSAGGAARPSTASPTHGAPKIAIKTRPVADDVAPTAATVIEPSQKAMKESVRFLTDFGEISDAISDLLTSSPNFNVISAIGPQGAGKSTLLSMLAGNNSRQMYREYVFRPVSREANEQSRHQTIQIDIYIVNHQIFLDCQPMYSFSIMEGLPKVRGGRFDDSTAMSDTLRLTAFLLYVSHTVLVVSETHYDKVIIDTLRVAEQIRPYLAIFRPKLAIDRKTNLVFIKTKASSIDLAPTVIREREELLRLSFQDSRWLKVSQEPFKTLIVLEEIRVRREHLFEEGDEPDEAASLNEFDEQIAELREELQKNREDFTVETAAMDEKKWLDMCREVIRDKTLHKTLKEYQRAMTDGVRTHFDNGFHAERDANKFFS
Protein: G-protein coupled receptor 22 (Q99680)
Organism: Homo sapiens (Human)
Function: Orphan G-protein coupled receptor. Seems to act through a G(i)/G(o) mediated pathway. May be involved in ciliogenesis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:D4A3U0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- G-protein coupled receptor 20
- Lysophosphatidic acid receptor 4
- Chemerin-like receptor 2
- tRNA-dihydrouridine
Sequence:
MCFSPILEINMQSESNITVRDDIDDINTNMYQPLSYPLSFQVSLTGFLMLEIVLGLGSNLTVLVLYCMKSNLINSVSNIITMNLHVLDVIICVGCIPLTIVILLLSLESNTALICCFHEACVSFASVSTAINVFAITLDRYDISVKPANRILTMGRAVMLMISIWIFSFFSFLIPFIEVNFFSLQSGNTWENKTLLCVSTNEYYTELGMYYHLLVQIPIFFFTVVVMLITYTKILQALNIRIGTRFSTGQKKKARKKKTISLTTQHEATDMSQSSGGRNVVFGVRTSVSVIIALRRAVKRHRERRERQKRVFRMSLLIISTFLLCWTPISVLNTTILCLGPSDLLVKLRLCFLVMAYGTTIFHPLLYAFTRQKFQKVLKSKMKKRVVSIVEADPLPNNAVIHNSWIDPKRNKKITFEDSEIREKCLVPQVVTD
Protein: Hap5p (A0A1D8PN26)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcriptional activator HAP2
- Hap31p
- Hap3p
- Hap43p
- Suppressor of ferric uptake 1
Sequence:
MNEDPQSEIMERYNESTYLRDDQLPQFDQNNDVIKEEQTHTQDHHHQHPSVSGSHSDELQDQDIHNVIEEHEDHVSTQNIVDEDELLAAQAAAEAAAAAQQQQPGDVFNNVAQGLSGKHRDMMMQYWQETINSIEHDEHDFKNHQLPLARIKKVMKTDEDVRMISAEAPILFAKGCDVFITELTMRAWIHAEENKRRTLQKSDIAAALTKSDMFDFLIDVVPREEEKPKKSNNNSSRSDSYVNNQQSPPIPETEEEVPHMLTQDVKHSHQDVLQQQMLQEQLLQQQLHQEVQQQLQQEVQRQLQEDVPQSDHQQASQREEDITNGAENANGHNDEATYENFNGYQNNY
Protein: Cysteine/Histidine-rich C1 domain family protein (Q9ZW73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerase subunit
- RNApolymerase 14 kDa subunit
- DNA-directed RNA polymerase II subunit 4
- SIN-like family protein
- DNA-directed RNA polymerase I subunit 2
- DNA-directed RNA polymerase III subunit 2
- DNA binding / DNA-directed RNA polymerase
- DNA-directed RNA polymerase III subunit RPC9
Sequence:
MAKTLDLFWHEHPLYEKYRMFTCQECHRSAIPFFEVFYGCFRCNIKWHPYCVPRSTKNINHPCHPNHPLEVLLQGPPSYSDEKCSLCQRKLSNFVYHCKLCNFSIDMECGNRPPPHKVDHPKCHEHALTLMGREVSFTCNACGTHGERNPYVCLPCSVMFHYDCIDLPHVININRHDHRISHSYPLKRGNWVCEICRQDINTTYGGYSCNKCPDFFVHSKCATRKDVWDGTELEGIPEEVVDVAPFEVIEEGVIYHFSHEKHNLFLIEDVFIDGAEDMHCEACARPVSSEKHYKCVECKFILHEECANLPLTKRHGLSTGIFYLRFGKDFSEQNFSCDACNRDGRGFSYKDEEGVVLDVLCASLSFFKHPKLHPHTLFLTTIDRGTCLACGENKLNVLRCVDCDYSLDYKCATLPLVIKHRCDTHYLVLRSGEEAPEGKYWCEICEAETNPERWFYTCDDCGVVCHIECVTGDFLNIKPGIIMKNRENKFEVGFNDHDSRPKCTDCGSRCRFPRFFKVTRKNIEYYYCSKACFQNAKF
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q4V9B9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MCDNGDVEDKPPAPPVRMSSTIFSGAKDHALTANHSSKPLPSVPEERKRNKIYSIFSGAEKGGRRKDRDKERPEISPPSDFEHTIHVGFDAVTGEFTGTPEQWARLLQTSNITKSEQKKNPQAVLDVLKFYDSTGNGRQKYLSFSSEKDSFPSGEQSPAKKTPEPSSPVKAVDDEDNGEDEDDDDDDDEETPPPVVAPRPEHTKSVYTRPSVIDPLPPPVTSPESDAASKATDRQRPKKGKMTDEEIMDKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGEELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQSPEKLSPIFRDFLGRCLEMDVEKRGGSKELLQHPFLKLAKPLSSLTPLILAAKDAMKNNR
Protein: Peptide tarsal-less 3A (Peptide polished rice 3) (A3RLR0)
Organism: Drosophila melanogaster (Fruit fly)
Function: One of four peptides (tal-1A, tal-2A, tal-3A and tal-AA) produced from a polycistronic gene that function redundantly in several developmental processes. Required in early stages of leg development for the intercalation of the tarsal segments during the mid-third instar stage and later for tarsal joint formation. Promotes the post-translational modification of ovo isoform B (svb) into its active form which in turn initiates trichome development and promotes tarsal joint development. This is likely due to recruitment of the E3 ubiquitin-protein ligase Ubr3 to svb for ubiquitination of its N-terminus, converting svb into a transcriptional activator. Also enhances interaction of Ubr3 with Diap1. Required for correct wing and leg formation through its regulation of several genes including those in the Notch signaling pathway. Essential for denticle formation and may have a role in the developmental timing of trichome differentiation. Essential for the development of taenidial folds in the trachea.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26383956}. Nucleus {ECO:0000269|PubMed:26383956}.
Interaction partners:
Sequence:
MSHDLDPTGTY
Protein: Laminin subunit beta-3 (Epiligrin subunit bata) (Kalinin B1 chain) (Kalinin subunit beta) (Laminin B1k chain) (Laminin-5 subunit beta) (Nicein subunit beta) (Q13751)
Organism: Homo sapiens (Human)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane.
Interaction partners:
- Laminin subunit gamma-2
- Laminin subunit alpha-3
- Laminin subunit alpha-4
- Integrin beta-4
- Collagen alpha-1
- CD44 antigen
- Collagen alpha-1
- Integrin alpha-6
- Integrin beta-6
- Integrin alpha-3
Sequence:
MRPFFLLCFALPGLLHAQQACSRGACYPPVGDLLVGRTRFLRASSTCGLTKPETYCTQYGEWQMKCCKCDSRQPHNYYSHRVENVASSSGPMRWWQSQNDVNPVSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERSSDFGKTWRVYQYLAADCTSTFPRVRQGRPQSWQDVRCQSLPQRPNARLNGGKVQLNLMDLVSGIPATQSQKIQEVGEITNLRVNFTRLAPVPQRGYHPPSAYYAVSQLRLQGSCFCHGHADRCAPKPGASAGPSTAVQVHDVCVCQHNTAGPNCERCAPFYNNRPWRPAEGQDAHECQRCDCNGHSETCHFDPAVFAASQGAYGGVCDNCRDHTEGKNCERCQLHYFRNRRPGASIQETCISCECDPDGAVPGAPCDPVTGQCVCKEHVQGERCDLCKPGFTGLTYANPQGCHRCDCNILGSRRDMPCDEESGRCLCLPNVVGPKCDQCAPYHWKLASGQGCEPCACDPHNSLSPQCNQFTGQCPCREGFGGLMCSAAAIRQCPDRTYGDVATGCRACDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYPVCVACHPCFQTYDADLREQALRFGRLRNATASLWSGPGLEDRGLASRILDAKSKIEQIRAVLSSPAVTEQEVAQVASAILSLRRTLQGLQLDLPLEEETLSLPRDLESLDRSFNGLLTMYQRKREQFEKISSADPSGAFRMLSTAYEQSAQAAQQVSDSSRLLDQLRDSRREAERLVRQAGGGGGTGSPKLVALRLEMSSLPDLTPTFNKLCGNSRQMACTPISCPGELCPQDNGTACGSRCRGVLPRAGGAFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLALWLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATCK
Protein: RNA-binding Fox protein 1, isoform M (M9PF74)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYYPSTVLIANEAAESQQSSAMQNAGGGGNTGGGGGGGGGGTPSSPLSNSPSSATASQAGGCGLTLNGSATEGSMSGDTSPVASGEPLLQTPPAHQQQQQQQQPLLCSSPTSMQSSGTSVTGSSIASGTLAATSSSGVGLLPTTGLDSIANGGAPTGCAVVPASTSQVIAHLNAAAAAASGIVSPSANVATSLSSALVPAQSVAAVAAASLDAKSQPKRLHVSNIPFRFRDPDLRAMFGQFGTILDVEIIFNERGSKGFGFVTFANSNDAERARERLHGTVVEGRKIEVNNATARVQTKKVTAVPNVVLTKDGAIPAPALVCVQWPEGYRLPVAAWPFLGAPVGAGAPTLTHLQLPVSMQMAQAPSAVAGGTAATSPATAAAAAAHAAAAAAATPIMLAPRPPHTAVQAATPTAATPRRSVYYDPFLAAAASADPNLRFQAAKPVTEVPAAQPAAILNATAPLLKTPLSQAQQQAYATAATTYTAVAARAAYGAAAAAAAQPALAGYATVAGYAREYADPYLGHGIGPVPGYGATMYRGGFNRFTPY
Protein: Serum paraoxonase/arylesterase 1 (PON 1) (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) (Aromatic esterase 1) (A-esterase 1) (Serum aryldialkylphosphatase 1) (P52430)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Apolipoprotein A-I
- Clusterin
- Apolipoprotein A-II
- Apolipoprotein E
- Apolipoprotein B-100
- Phosphatidylcholine-sterol acyltransferase
- Haptoglobin
- Phospholipid transfer protein
- Apolipoprotein A-IV
- Apolipoprotein C-III
Sequence:
MAKLLALTLVGLVLALYKNHRSSYQTRLNAFREVTPVELPNCNLVKGIETGAEDLEILPNGLTFFSTGLKYPGIKSFDPSKPGKILLMDLNKKEPAVSELEIIGNTLDISSFNPHGISTFTDEDNTVYLLVVNHPDSSSTVEVFKFQEEERSLLHLKTITHELLPSINDIAAIGPESFYATNDHYFADPYLRSWEMYLGLSWSNVVYYSPDKVQVVAEGFDFANGIGISLDGKYVYIAELLAHKIHVYEKHANWTLTPLKVLNFDTLVDNISVDPVTGDLWVGCHPNGMRIFFYDAENPPGSEVLRIQNILSEDPKITVVYAENGTVLQGTTVASVYKGKLLIGTVFHKALYCDL
Protein: Alkaline phosphatase PafA (AP PafA) (EC 3.1.3.1) (Q9KJX5)
Organism: Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Function: Alkaline phosphatase with broad substrate specificity. Has phosphatase activity towards nucleotide phosphates with a preference for ATP. Active towards a great variety of phosphomonoesters with the exception of 2',3'-cyclic AMP and myo-inositol hexakisphosphate.
Subcellular location: Periplasm {ECO:0000269|PubMed:11577161}.
Interaction partners:
- Dicarboxylate/amino acid:cation symporter
Sequence:
MLTPKKWLLGVLVVSGMLGAQKTNAVPRPKLVVGLVVDQMRWDYLYRYYSKYGEGGFKRMLNTGYSLNNVHIDYVPTVTAIGHTSIFTGSVPSIHGIAGNDWYDKELGKSVYCTSDETVQPVGTTSNSVGQHSPRNLWSTTVTDQLGLATNFTSKVVGVSLKDRASILPAGHNPTGAFWFDDTTGKFITSTYYTKELPKWVNDFNNKNVPAQLVANGWNTLLPINQYTESSEDNVEWEGLLGSKKTPTFPYTDLAKDYEAKKGLIRTTPFGNTLTLQMADAAIDGNQMGVDDITDFLTVNLASTDYVGHNFGPNSIEVEDTYLRLDRDLADFFNNLDKKVGKGNYLVFLSADHGAAHSVGFMQAHKMPTGFFVEDMKKEMNAKLKQKFGADNIIAAAMNYQVYFDRKVLADSKLELDDVRDYVMTELKKEPSVLYVLSTDEIWESSIPEPIKSRVINGYNWKRSGDIQIISKDGYLSAYSKKGTTHSVWNSYDSHIPLLFMGWGIKQGESNQPYHMTDIAPTVSSLLKIQFPSGAVGKPITEVIGR
Protein: Alpha-L-arabinofuranosidase C (ABF C) (Arabinosidase C) (EC 3.2.1.55) (Q5BDV3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Alpha-L-arabinofuranosidase B
- Probable alpha-L-arabinofuranosidase A
- Probable exopolygalacturonase Bgalacturonohydrolase B)
- Exopolygalacturonase X-1
- Probable endopolygalacturonase D
- Exopolygalacturonase X-2
- Endopolygalacturonase AN8327
- alcohol dehydrogenase
- Beta-glucuronidase
- NAD binding Rossmann fold oxidoreductase, putative
Sequence:
MTTFTKLSEQEAPGISIHPDRRISKINPNIYAGFAEHMGRCIYGGIYDPGNPLSDENGFRKDVLEALKELKVPVIRYPGGNFTATYHWIDGVGPRDQRPARPELAWLGTETNQFGTDEFLKWCEVLGTEPYLCLNMGTGTLDEALAWVDYCNGTRDTYYANLRRKNGREEPYNVKYWALGNEVWGPWQVEQSTKEEYAHKAYQWAKALKLLDPSIELILCGKEGPTSWDYYTLKQTMLPVHSPLSTSAVPLIDMHSIHLYTAHSSHLPNVTAPLAAERAIEITSSLIDLARVENGVPPEQRRPTICFDEWNVWDPIRAEGSKGAEESYNLSDALAVGVWLNVFVRKSKDVGMACIAQSVNVISPLMTTKDGIVKQTTWWPLYLFSNYMRGWTISAHISVSAYEGETHPKWVRGVKDTPWLDVSATLGEDGYVNVVVINIHEEKGIEAKLDGPSGEVTVFTVTGDNPAVTNMKGKEEVGLVETKWDAQGPYVFPKHSLTLLRWKA
Protein: Cholesterol 25-hydroxylase (EC 1.14.99.38) (Cholesterol 25-monooxygenase) (m25OH) (Q9Z0F5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes. Plays a key role in cell positioning and movement in lymphoid tissues: 25-hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC), an oxysterol that acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells. May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing. In testis, production of 25-hydroxycholesterol by macrophages may play a role in Leydig cell differentiation. Interferon-stimulated gene which has broad antiviral activities against a wide range of enveloped viruses (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9852097}; Multi-pass membrane protein {ECO:0000269|PubMed:9852097}.
Interaction partners:
- Cytochrome P450 7B1
- Cytochrome P450 7A1
- Cholesterol 24-hydroxylase
- Sterol 26-hydroxylase, mitochondrial
- Lanosterol 14-alpha demethylase
- Lathosterol oxidase
- Squalene monooxygenase
- 7-dehydrocholesterol reductase
- Delta
- Squalene synthase
Sequence:
MGCYNGSELQDLGCSSQLLLQPLWDTIRTREAFTRSPIFPVTFSIITYVGFCLPFVVLDVLYPWVPILRRYKIHPDFSPSVKQLLPCLGLTLYQHLVFVFPVTLLHWVRSPALLPQEAPELVQLLSHVLICLLLFDTEIFAWHLLHHKVPWLYRTFHKVHHQNSSSFALATQYMSFWELLSLTFFDVLNVAVLRCHPLTIFTFHVINIWLSVEDHSGYDFPWSTHRLVPFGWYGGVAHHDMHHSQFNCNFAPYFTHWDKMLGTLRSAPLPESLCACGERCVNSRERCAVHLIQKKKQT
Protein: AtbZIP transcription factor (Basic leucine-zipper 52) (Similar to bZIP transcription factors) (Q8VWG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Choline transporter-like protein
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''epsilon
- Serine/threonine protein phosphatase 2A regulatory subunit B''alpha
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Basic leucine zipper 8
Sequence:
MEKSDPPPVPKPGATIIPSSDPIPNADPIPSSSFHRRSRSDDMSMFMFMDPLSSAAPPSSDDLPSDDDLFSSFIDVDSLTSNPNPFQNPSLSSNSVSGAANPPPPPSSRPRHRHSNSVDAGCAMYAGDIMDAKKAMPPEKLSELWNIDPKRAKRILANRQSAARSKERKARYIQELERKVQSLQTEATTLSAQLTLYQRDTNGLANENTELKLRLQAMEQQAQLRNALNEALRKEVERMKMETGEISGNSDSFDMGMQQIQYSSSTFMAIPPYHGSMNLHDMQMHSSFNPMEMSNSQSVSDFLQNGRMQGLEISSNSSSLVKSEGPSLSASESSSAY
Protein: Cilia- and flagella-associated protein 45 (Q57UZ3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}.
Interaction partners:
- Tubulin alpha chain
- CFA20 domain-containing protein
- Uncharacterized protein
- ODAD1 central coiled coil region domain-containing protein
- Uncharacterized protein
- WW domain-containing protein
- WW domain-containing protein
- Ankyrin repeat protein
- Enkurin domain-containing protein
- Enkurin domain-containing protein
Sequence:
MIGMMARSGAGVFPPRRPGQTDGDLRKELNDRNAPRDSTILTRTELDIIREMISGKNIMTTLTRSAVRTRSVEAEEHKRRMQQYDEEQRLCGGNDKPLEQIEEEQQRRLNLERAKTLLDEQYDEVKAMNQIVDEARCIAVRNAQIRERELRKEEEMEYERKMEEMMTAEAEKAAKLYNEREEQQVVARKKTLAVIKAQLEQHDVERVRKLELLQHEREAMTRHLELLREEAQAEKLQQQEKERRIMEAVALANAQQISLKKRQQELDEEEDRRIAEFIKRKQERDRLYAEEQQRIRDEKEREVARLRAEQQRAQNTQALLDDIRAQRAQEEYARDMRRKEKERKEREAAVLQDLAQMREKQIEERKRMKAEERRLEEEEVERINAVQKVALEQERERKMWARKQHEENSLAVLKQIMDVEERRRRERQEYVAEGNSIMMQIREREAAIEAIRQRKLKELEELGVPEEYCQALQKKMKVKVARR
Protein: Sodium-dependent phosphate transport protein 2C (Sodium-phosphate transport protein 2C) (Na(+)-dependent phosphate cotransporter 2C) (Sodium/phosphate cotransporter 2C) (Na(+)/Pi cotransporter 2C) (NaPi-2c) (Solute carrier family 34 member 3) (Q80SU6)
Organism: Mus musculus (Mouse)
Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. The cotransport has a Na(+):Pi stoichiometry of 2:1 and is electroneutral.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12690469}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at the brush border membrane in the kidney. {ECO:0000269|PubMed:12690469}.
Interaction partners:
- Na
- Sodium-dependent phosphate transport protein 2A
- Sodium-dependent phosphate transport protein 2B
- Fibroblast growth factor 23
- Sodium-dependent phosphate transporter 2
- Klotho
- Phosphate-regulating neutral endopeptidase PHEX
- 1,25-dihydroxyvitamin D
- Parathyroid hormone
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
Sequence:
MPNSLAGGQVPNPTLDAFDLVDRSLRNAGISGSIPGLEEGGTDPWTFSPLKNADQLKEVGMASRLRRVVSSFLKACGLLGSLYFFICSLDILSSAFQLLGSKMAGDIFKDNVVLSNPVAGLVIGVLVTVLVQSSSTSSSIVVSMVASKLLTVQVSVPIIMGVNVGTSITSTLVSMAQSGDRDEFQRAFSGSAVHGIFNWLTVLVLLPLESATAALERLSELALGAASLQPGQQAPDILKALTRPFTHLIIQLDSSVITSGITSNTTNSSLIKHWCGFRGETPQGSSEGCGLFSSCTERNSSASPEEDRLLCHHLFAGSKLTDLAVGFILLAGSLLVLCVCLVLIVKLLNSVLKGRIAQAVKTVINADFPFPFGWLSGYLAILVGAGLTFLLQSSSVFTAAIVPLMGVGVIDLERAYPLFLGSNIGTTTTALLAALASPADMLIFAVQVALIHFFFNLAGILLWYLVPVLRLPIPLAKRFGNLTAQYRWVAIVYLLLTFLLLPLAAFGLSLAGGTVLAAVGGPLVGLVLLIILVNVLQQHRPSWLPRCLQSWAWLPLWLHSLEPWDRLVTACCPCRACSNSPMTSKVAHCYENPQVIASQQL
Protein: N-lysine methyltransferase SMYD2-B (EC 2.1.1.-) (Histone methyltransferase SMYD2-B) (EC 2.1.1.354) (SET and MYND domain-containing protein 2B) (Q5RGL7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Kelch-like protein 41a
- DBIRD complex subunit ZNF326
- Cellular tumor antigen p53
- Lysine
- Chemokine
Sequence:
MMKAEGIPGIEQFASPGKGRGLRVSRAYGVGELLFSCPAYSYVLSVGERGLICEQCFTRKKGLAKCGKCKKAFYCNANCQKKNWPMHKLECQAMCAFGENWRPSETVRLVARIIARLKAQKERSPSEILLLLGEMEAHLEDMDNEKREMTEAHIAGLHQFYSKHLDFPDHQALLTLFSQVHCNGFTVEDEELSNLGLAIFPDIALLNHSCSPNVIVTYRGINAEVRAVKDISPGQEIYTSYIDLLYPTADRLERLRDMYYFSCDCKECTTKSMDVVKMSVRKRSDEIGEKEIKDMVRYARNSMENFRRAKQDKSPTELLEMCELSIDKMSTVFDDSNVYILHMMYQAMGICLFTEDYEGAVRYGEKVIKPFTVLYPAYSMNVASMFLKLGRLYIALDRKLAGIDAFQKALTIMEVVHGKDHTYVTELKQEMRDF
Protein: Matrin-type domain-containing protein (Q9CUW6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PLREFVEHVKSQGHKDKAQELKTLEKETGSPDEDHFITVDAVGCFESGQEEDEDDDEEEEEEGEIEAEEEFCKQVKPRETSSEQGKGSETYNPNTAYGEDFLVPVMGYVCQICHKFYDSNSELRFSHCKSLAHFENLQKYKAKNPTPPPTRPVSRKCAINARNALTALFTSSHQPSPQDTVKMPSKVKPGSPGLPPPFRRSTRLKT
Protein: Phosphatidylinositol 4-kinase gamma 7 (AtPI4Kgamma7) (PI-4Kgamma7) (PI4K gamma 7) (EC 2.7.1.67) (Ubiquitin-like domain kinase gamma 7) (UbDK gamma 7) (Q9SI52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3) (By similarity). Undergoes autophosphorylation and phosphorylates serine/threonine residues of protein substrates.
Interaction partners:
- AT2G21270 protein
- Phosphatidylinositol 4-kinase alpha 1
- Protein OXIDATIVE STRESS 3 LIKE 4
- Ternary complex factor MIP1 leucine-zipper protein
- CASP-like protein 5A2
- LIMR family protein At5g01460
- Protein OXIDATIVE STRESS 3 LIKE 3
- Nuclear polyadenylated RNA-binding protein
- Protein RALF-like 31
- Putative RRM-containing protein family protein)
Sequence:
MSRNLDSPVQTQMAVAVFKTPLTGASKMEGKQHHKHQHLQRQSSGRRVFVQTETGCVLGMELDRSDNVHTVKRRLQIALNFPTEESSLTYGDMVLTNDLSAVRNDSPLLLKRNFMHRSSSTPCLSPTGRDLQQKDRSGPIEILGHSDCFSIVKHMVKDIVKAMKMGVEPLPVHSGLGGAYYFRNKRGESVAIVKPTDEEPFAPNNPKGFVGKALGQPGLKSSVRVGETGFREVAAYLLDYGRFANVPPTALVKITHSVFNVNDGVKGNKPREKKLVSKIASFQKFVAHDFDASDHGTSSFPVTSVHRIGILDIRIFNTDRHGGNLLVKKLDGVGMFGQVELIPIDHGLCLPETLEDPYFEWIHWPQASLPFSDEEVDYIQSLDPVKDCDMLRRELPMIREACLRVLVLCTIFLKEASAYGLCLAEIGEMMTREFRPGEEEPSELEVVCIEAKRSVTERDVFSPRSDVVGEAEFQFDLDCDDLESVYSSKIQLTDDYFTKNPFSNGRSSLGKLEESIKEEEEDEEEEEDKTENTVPMIIMKDSFFSSAAFHDKAPSLSKLSTSMKNTHLSDTTRKNPKPLTRGKSENTSSGHKSANEQLPVSASFVKVADMKEDEWVLFLERFQELLGPAFAKRKTATLSKRQRLGTSCQF